|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-536 |
0e+00 |
|
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: 744.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLAPADGSVKLLGMDLFRRTPD 91
Cdd:COG4172 5 PLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPDPPRIFRSYPHQLSGGQRQR 171
Cdd:COG4172 85 ELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 172 IVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSV 251
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 252 LQHPKEPYTQKLINAVPELKPrhRPPVDGNPTLLEAKNVVKTYTL-GGFFTGRVK-VRALKGVSARLRRGETIGIVGESG 329
Cdd:COG4172 245 FAAPQHPYTRKLLAAEPRGDP--RPVPPDAPPLLEARDLKVWFPIkRGLFRRTVGhVKAVDGVSLTLRRGETLGLVGESG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 330 SGKSTFARSIARLIdPTSGEVWVNGENVAAAPKRKLHGLRRRLQVVFQDPYRSLDPRMTVGESIVEG-----PvnfGVPK 404
Cdd:COG4172 323 SGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGlrvhgP---GLSA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 405 EEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIG 484
Cdd:COG4172 399 AERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLA 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 485 ILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLIAAAP 536
Cdd:COG4172 479 YLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-537 |
0e+00 |
|
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: 664.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLAPAdGSVKLLGMDLFRRTPd 91
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRIS-GEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 eirRLRGAKMAMVFQEPMTALNPVmTCGDQMDELLRAHVpMGPYERRIRILDLFEEVRLPdppRIFRSYPHQLSGGQRQR 171
Cdd:COG1123 79 ---ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENLG-LSRAEARARVLELLEAVGLE---RRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 172 IVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSV 251
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 252 LQHPKEpytqklINAVPELKPRH---RPPVDGNPTLLEAKNVVKTYTLGGfftgRVKVRALKGVSARLRRGETIGIVGES 328
Cdd:COG1123 231 LAAPQA------LAAVPRLGAARgraAPAAAAAEPLLEVRNLSKRYPVRG----KGGVRAVDDVSLTLRRGETLGLVGES 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 329 GSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHGLRRRLQVVFQDPYRSLDPRMTVGESIVEGPVNFGV-PKEEA 407
Cdd:COG1123 301 GSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLlSRAER 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 408 WKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILF 487
Cdd:COG1123 381 RERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLF 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2486247945 488 VTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLIAAAPG 537
Cdd:COG1123 461 ISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPS 510
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
12-535 |
2.13e-163 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 474.96 E-value: 2.13e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglAPA----DGSVKLLGMDLFR 87
Cdd:PRK15134 4 PLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLP---SPPvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 88 RTPDEIRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPDPPRIFRSYPHQLSGG 167
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGP 247
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 248 AKSVLQHPKEPYTQKLINAVPELKPrhrPPVDGN-PTLLEAKNVVKTYTL-GGFFTGRV-KVRALKGVSARLRRGETIGI 324
Cdd:PRK15134 241 AATLFSAPTHPYTQKLLNSEPSGDP---VPLPEPaSPLLDVEQLQVAFPIrKGILKRTVdHNVVVKNISFTLRPGETLGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 325 VGESGSGKSTFARSIARLIdPTSGEVWVNGENVAAAPKRKLHGLRRRLQVVFQDPYRSLDPRMTVGESIVEGpVNFGVPK 404
Cdd:PRK15134 318 VGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEG-LRVHQPT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 405 EEAWKRAQ---EFMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKL 481
Cdd:PRK15134 396 LSAAQREQqviAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKH 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 482 GIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLIAAA 535
Cdd:PRK15134 476 QLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
13-536 |
3.70e-155 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 457.39 E-value: 3.70e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapADGSVKLLGMDLFRR---- 88
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQ----AGGLVQCDKMLLRRRsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 89 ------TPDEIRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPDPPRIFRSYPH 162
Cdd:PRK10261 88 ielseqSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQ 242
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 243 IETGPAKSVLQHPKEPYTQKLINAVPELK-------PRHRP------------------PVDGNPtLLEAKNVVKTYTLG 297
Cdd:PRK10261 248 VETGSVEQIFHAPQHPYTRALLAAVPQLGamkgldyPRRFPlislehpakqeppieqdtVVDGEP-ILQVRNLVTRFPLR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 298 GFFTGRVK--VRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHGLRRRLQVV 375
Cdd:PRK10261 327 SGLLNRVTreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFI 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 376 FQDPYRSLDPRMTVGESIVEGPVNFGV-PKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILI 454
Cdd:PRK10261 407 FQDPYASLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVII 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 455 CDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLIAA 534
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
..
gi 2486247945 535 AP 536
Cdd:PRK10261 567 VP 568
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-282 |
1.71e-131 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 385.56 E-value: 1.71e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGlAPADGSVKLLGMDLFRRTPDE 92
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPP-GITSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPDPPRIFRSYPHQLSGGQRQRI 172
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVL 252
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250 260 270
....*....|....*....|....*....|..
gi 2486247945 253 QHPKEPYTQKLINAVPELKPRHR--PPVDGNP 282
Cdd:COG0444 240 ENPRHPYTRALLSSIPRLDPDGRrlIPIPGEP 271
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
284-536 |
1.64e-120 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 357.89 E-value: 1.64e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTL-GGFFTGRVK-VRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAP 361
Cdd:COG4608 7 LLEVRDLKKHFPVrGGLFGRTVGvVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 362 KRKLHGLRRRLQVVFQDPYRSLDPRMTVGESIVEGPVNFGV-PKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRI 440
Cdd:COG4608 87 GRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 441 SIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:COG4608 167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246
|
250
....*....|....*.
gi 2486247945 521 FHPQHEYTKSLIAAAP 536
Cdd:COG4608 247 ARPLHPYTQALLSAVP 262
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
284-536 |
3.43e-115 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 343.96 E-value: 3.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTytlggFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDP---TSGEVWVNGENVAAA 360
Cdd:COG0444 1 LLEVRNLKVY-----FPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 PKRKLHGLR-RRLQVVFQDPYRSLDPRMTVGESIVEGP-VNFGVPKEEAWKRAQEFMKIVRLSP--DALNRYPNQFSGGQ 436
Cdd:COG0444 76 SEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLrIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 437 RQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHV 516
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
250 260
....*....|....*....|
gi 2486247945 517 QDVFFHPQHEYTKSLIAAAP 536
Cdd:COG0444 236 EELFENPRHPYTRALLSSIP 255
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
284-514 |
1.78e-106 |
|
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: 318.30 E-value: 1.78e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTlggffTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR 363
Cdd:cd03257 1 LLEVKNLSVSFP-----TGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGLRRRLQVVFQDPYRSLDPRMTVGESIVEGPVNFGVP--KEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRIS 441
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLskKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 442 IARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-246 |
3.92e-106 |
|
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: 317.53 E-value: 3.92e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLfRRTPDE 92
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL----KPTSGSIIFDGKDL-LKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLfEEVRLPDPPRIFRSYPHQLSGGQRQRI 172
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLL-LLVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
12-273 |
6.07e-100 |
|
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: 311.84 E-value: 6.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLP-PGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTP 90
Cdd:COG1123 259 PLLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR----PTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLRGaKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPdpPRIFRSYPHQLSGGQRQ 170
Cdd:COG1123 335 RSLRELRR-RVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 171 RIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKS 250
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
250 260
....*....|....*....|...
gi 2486247945 251 VLQHPKEPYTQKLINAVPELKPR 273
Cdd:COG1123 492 VFANPQHPYTRALLAAVPSLDPA 514
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
284-537 |
8.41e-100 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 302.11 E-value: 8.41e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTlggffTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR 363
Cdd:COG1124 1 MLEVRNLSVSYG-----QGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLhglRRRLQVVFQDPYRSLDPRMTVGESIVEGPVNFGVPKEEAwkRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIA 443
Cdd:COG1124 76 AF---RRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 444 RALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHP 523
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
250
....*....|....
gi 2486247945 524 QHEYTKSLIAAAPG 537
Cdd:COG1124 231 KHPYTRELLAASLA 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
281-539 |
1.19e-88 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 276.08 E-value: 1.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVVKTYTL-GGFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAA 359
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVkRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 360 APKRKLHGLRRRLQVVFQDPYRSLDPRMTVGeSIVEGP--VNFGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQR 437
Cdd:PRK11308 82 ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVG-QILEEPllINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 438 QRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQ 517
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKE 240
|
250 260
....*....|....*....|..
gi 2486247945 518 DVFFHPQHEYTKSLIAAAPGTN 539
Cdd:PRK11308 241 QIFNNPRHPYTQALLSATPRLN 262
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-270 |
8.90e-87 |
|
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: 278.11 E-value: 8.90e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLP-PGG------DRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglapADGSVKLLGMD 84
Cdd:COG4172 274 PLLEARDLKVWFPiKRGlfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-----SEGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 85 LFRRTPDEIRRLRgAKMAMVFQEPMTALNPVMTCGDQMDELLRAH-VPMGPYERRIRILDLFEEVRLpDPPRIFRsYPHQ 163
Cdd:COG4172 349 LDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHgPGLSAAERRARVAEALEEVGL-DPAARHR-YPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQI 243
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
250 260
....*....|....*....|....*..
gi 2486247945 244 ETGPAKSVLQHPKEPYTQKLINAVPEL 270
Cdd:COG4172 506 EQGPTEQVFDAPQHPYTRALLAAAPLL 532
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
12-275 |
1.91e-85 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 267.75 E-value: 1.91e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGD---RPN----AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMD 84
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGlfgRTVgvvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEE----PTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 85 LFRRTPDEIRRLRgAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPdpPRIFRSYPHQL 164
Cdd:COG4608 82 ITGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR--PEHADRYPHEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 165 SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIE 244
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVE 238
|
250 260 270
....*....|....*....|....*....|.
gi 2486247945 245 TGPAKSVLQHPKEPYTQKLINAVPELKPRHR 275
Cdd:COG4608 239 IAPRDELYARPLHPYTQALLSAVPVPDPERR 269
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
14-270 |
3.03e-85 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 264.36 E-value: 3.03e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER----PWSGEVTFDGRPVTRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPMTALNPVMTCGDQMDELLRAHvpmGPYERRIRILDLFEEVRLPdpPRIFRSYPHQLSGGQRQRIV 173
Cdd:COG1124 78 RR----RVQMVFQDPYASLHPRHTVDRILAEPLRIH---GLPDREERIAELLEQVGLP--PSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQ 253
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
250
....*....|....*..
gi 2486247945 254 HPKEPYTQKLINAVPEL 270
Cdd:COG1124 229 GPKHPYTRELLAASLAF 245
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
284-536 |
2.98e-83 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 262.33 E-value: 2.98e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTLGG----FFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAA 359
Cdd:PRK15079 8 LLEVADLKVHFDIKDgkqwFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 360 APKRKLHGLRRRLQVVFQDPYRSLDPRMTVGESIVEGPVNF--GVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQR 437
Cdd:PRK15079 88 MKDDEWRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 438 QRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQ 517
Cdd:PRK15079 168 QRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYD 247
|
250
....*....|....*....
gi 2486247945 518 DVFFHPQHEYTKSLIAAAP 536
Cdd:PRK15079 248 EVYHNPLHPYTKALMSAVP 266
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
12-282 |
1.10e-81 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 258.12 E-value: 1.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSL-PPGGDrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGlAPADGSVKLLGMDLFRRTP 90
Cdd:PRK09473 11 ALLDVKDLRVTFsTPDGD-VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAN-GRIGGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMG---PYERRIRILDlfeEVRLPDPPRIFRSYPHQLSGG 167
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSkaeAFEESVRMLD---AVKMPEARKRMKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGP 247
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
250 260 270
....*....|....*....|....*....|....*..
gi 2486247945 248 AKSVLQHPKEPYTQKLINAVPEL--KPRHRPPVDGNP 282
Cdd:PRK09473 246 ARDVFYQPSHPYSIGLLNAVPRLdaEGESLLTIPGNP 282
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
288-548 |
2.22e-79 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 252.69 E-value: 2.22e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 288 KNVVKTYTlggffTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHG 367
Cdd:COG1135 5 ENLSKTFP-----TKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 368 LRRRLQVVFQDPyrSLDPRMTVGESI-----VEgpvnfGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISI 442
Cdd:COG1135 80 ARRKIGMIFQHF--NLLSSRTVAENValpleIA-----GVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 443 ARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFH 522
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAN 231
|
250 260
....*....|....*....|....*.
gi 2486247945 523 PQHEYTKSLIAAAPGTNYPFGRTAHL 548
Cdd:COG1135 232 PQSELTRRFLPTVLNDELPEELLARL 257
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
283-534 |
3.46e-78 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 246.67 E-value: 3.46e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 283 TLLEAKNVVKTYTLGGFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGEnvaaapk 362
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 363 rKLH----GLR-RRLQVVFQDPYRSLDPRMTVGEsIVEGPV--NFGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGG 435
Cdd:COG4167 76 -KLEygdyKYRcKHIRMIFQDPNTSLNPRLNIGQ-ILEEPLrlNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 436 QRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGH 515
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGK 233
|
250
....*....|....*....
gi 2486247945 516 VQDVFFHPQHEYTKSLIAA 534
Cdd:COG4167 234 TAEVFANPQHEVTKRLIES 252
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
32-266 |
1.07e-77 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 244.20 E-value: 1.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLAPADGSVKLLGMDLFRRtpdeirRLRGAKMAMVFQEPMTA 111
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPL------SIRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQMDELLRAHvpMGPYER-RIRILDLFEEVRLPDPPRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEP 190
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSL--GKLSKQaRALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 191 TTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLINA 266
Cdd:TIGR02770 153 TTDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
13-269 |
1.35e-76 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 245.04 E-value: 1.35e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLP-KGLAPADgSVKLLGMDLFRRTPD 91
Cdd:PRK11022 3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAE-KLEFNGQDLQRISEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPDPPRIFRSYPHQLSGGQRQR 171
Cdd:PRK11022 82 ERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 172 IVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSV 251
Cdd:PRK11022 162 VMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
250
....*....|....*...
gi 2486247945 252 LQHPKEPYTQKLINAVPE 269
Cdd:PRK11022 242 FRAPRHPYTQALLRALPE 259
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
11-269 |
1.87e-72 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 234.41 E-value: 1.87e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 11 LPVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLL-PKGLAPADgSVKLLGMDLFRRT 89
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkDNWHVTAD-RFRWNGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 90 PDEIRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPY-----ERRIRILDLFEEVRLPDPPRIFRSYPHQL 164
Cdd:COG4170 80 PRERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEAIPSWTFKGKWwqrfkWRKKRAIELLHRVGIKDHKDIMNSYPHEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 165 SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIE 244
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVE 239
|
250 260
....*....|....*....|....*
gi 2486247945 245 TGPAKSVLQHPKEPYTQKLINAVPE 269
Cdd:COG4170 240 SGPTEQILKSPHHPYTKALLRSMPD 264
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
284-524 |
9.22e-69 |
|
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: 221.30 E-value: 9.22e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTlggffTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR 363
Cdd:cd03258 1 MIELKNVSKVFG-----DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGLRRRLQVVFQDpYRSLDPRmTVGESiVEGPVNF-GVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISI 442
Cdd:cd03258 76 ELRKARRRIGMIFQH-FNLLSSR-TVFEN-VALPLEIaGVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 443 ARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFH 522
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 2486247945 523 PQ 524
Cdd:cd03258 232 PQ 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
8-268 |
3.78e-67 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 220.35 E-value: 3.78e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 8 AQKLPVLEVENLAVSLPPGGDRP---------NAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapADGSV 78
Cdd:PRK15079 3 EGKKVLLEVADLKVHFDIKDGKQwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKA----TDGEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 79 KLLGMDLFRRTPDEIRRLRgAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVP-MGPYERRIRILDLFEEVRLPdpPRIF 157
Cdd:PRK15079 79 AWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPkLSRQEVKDRVKAMMLKVGLL--PNLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 158 RSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVL 237
Cdd:PRK15079 156 NRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVM 235
|
250 260 270
....*....|....*....|....*....|.
gi 2486247945 238 ELGKQIETGPAKSVLQHPKEPYTQKLINAVP 268
Cdd:PRK15079 236 YLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
286-535 |
9.59e-67 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 219.67 E-value: 9.59e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 286 EAKNVVKTYTLGGfftgrVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKL 365
Cdd:PRK11153 3 ELKNISKVFPQGG-----RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 366 HGLRRRLQVVFQDpYRSLDPRMtvgesiVEGPVNF-----GVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRI 440
Cdd:PRK11153 78 RKARRQIGMIFQH-FNLLSSRT------VFDNVALplelaGTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 441 SIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK11153 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVF 229
|
250
....*....|....*
gi 2486247945 521 FHPQHEYTKSLIAAA 535
Cdd:PRK11153 230 SHPKHPLTREFIQST 244
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
283-523 |
2.53e-66 |
|
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: 216.21 E-value: 2.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 283 TLLEAKNVVKTYTLGGFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPK 362
Cdd:TIGR02769 1 SLLEVRDVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 363 RKLHGLRRRLQVVFQDPYRSLDPRMTVGESIVEGPVNFGVPKEEAWK-RAQEFMKIVRLSPDALNRYPNQFSGGQRQRIS 441
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKaRIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 442 IARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDV-- 519
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLls 240
|
....
gi 2486247945 520 FFHP 523
Cdd:TIGR02769 241 FKHP 244
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
282-512 |
1.79e-65 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 212.21 E-value: 1.79e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 282 PTLLEAKNVVKTYTlggffTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAP 361
Cdd:COG1136 2 SPLLELRNLTKSYG-----TGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 362 KRKLHGLRRR-LQVVFQDPYrsLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRI 440
Cdd:COG1136 77 ERELARLRRRhIGFVFQFFN--LLPELTALENVALPLLLAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 441 SIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASqICDDVIVIRRGECVE 512
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIVS 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
284-529 |
3.49e-65 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 212.16 E-value: 3.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAaPKR 363
Cdd:COG1126 1 MIEIENLHKSF-------GDLEV--LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGLRRRLQVVFQDPyrSLDPRMTVGESIVEGPVN-FGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISI 442
Cdd:COG1126 71 DINKLRRKVGMVFQQF--NLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 443 ARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFH 522
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
....*..
gi 2486247945 523 PQHEYTK 529
Cdd:COG1126 227 PQHERTR 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
12-275 |
1.57e-64 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 213.29 E-value: 1.57e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLP------PGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDL 85
Cdd:PRK11308 4 PLLQAIDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIET----PTGGELYYQGQDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 86 FRRTPDEIRRLRgAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPdpPRIFRSYPHQLS 165
Cdd:PRK11308 80 LKADPEAQKLLR-QKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLR--PEHYDRYPHMFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIET 245
Cdd:PRK11308 157 GGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEK 236
|
250 260 270
....*....|....*....|....*....|
gi 2486247945 246 GPAKSVLQHPKEPYTQKLINAVPELKPRHR 275
Cdd:PRK11308 237 GTKEQIFNNPRHPYTQALLSATPRLNPDDR 266
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
285-520 |
3.49e-64 |
|
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: 209.11 E-value: 3.49e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGgfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapKRK 364
Cdd:COG1122 1 IELENLSFSYPGG--------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDPYRSL-DPrmTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIA 443
Cdd:COG1122 70 LRELRRKVGLVFQNPDDQLfAP--TVEEDVAFGPENLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 444 RALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLN-KEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
284-535 |
3.33e-63 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 207.74 E-value: 3.33e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYtlGGfftGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNG-----ENVA 358
Cdd:COG4107 8 LLSVRGLSKRY--GP---GCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDrdggpRDLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 359 AAPKRKLHGLRR-RLQVVFQDPYRSLDPRMTVGESIVE-----GPVNFGVPKEeawkRAQEFMKIVRLSPDALNRYPNQF 432
Cdd:COG4107 83 ALSEAERRRLRRtDWGMVYQNPRDGLRMDVSAGGNIAErlmaaGERHYGDIRA----RALEWLERVEIPLERIDDLPRTF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 433 SGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVE 512
Cdd:COG4107 159 SGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVE 238
|
250 260
....*....|....*....|...
gi 2486247945 513 SGHVQDVFFHPQHEYTKSLIAAA 535
Cdd:COG4107 239 SGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
285-509 |
3.52e-63 |
|
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: 206.19 E-value: 3.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggffTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03255 1 IELKNLSKTYG-----GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRR-LQVVFQDPYrsLDPRMTVGESiVEGPVNF-GVPKEEAWKRAQEFMKIVRLsPDALNRYPNQFSGGQRQRISI 442
Cdd:cd03255 76 LAAFRRRhIGFVFQSFN--LLPDLTALEN-VELPLLLaGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 443 ARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASqICDDVIVIRRGE 509
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGK 217
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
280-536 |
4.79e-63 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 209.58 E-value: 4.79e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 280 GNPTLLEAKNVVKTytlggFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDP---TSGEVWVNGEN 356
Cdd:PRK09473 8 QADALLDVKDLRVT-----FSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 357 VAAAPKRKLHGLR-RRLQVVFQDPYRSLDPRMTVGESIVEG-PVNFGVPKEEAWKRAQEFMKIVRLsPDALNR---YPNQ 431
Cdd:PRK09473 83 ILNLPEKELNKLRaEQISMIFQDPMTSLNPYMRVGEQLMEVlMLHKGMSKAEAFEESVRMLDAVKM-PEARKRmkmYPHE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 432 FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECV 511
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
250 260
....*....|....*....|....*
gi 2486247945 512 ESGHVQDVFFHPQHEYTKSLIAAAP 536
Cdd:PRK09473 242 EYGNARDVFYQPSHPYSIGLLNAVP 266
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
283-523 |
5.49e-63 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 207.62 E-value: 5.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 283 TLLEAKNVVKTYTLGGFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPK 362
Cdd:PRK10419 2 TLLNVSGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 363 RKLHGLRRRLQVVFQDPYRSLDPRMTVGESIVEgPVN--FGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRI 440
Cdd:PRK10419 82 AQRKAFRRDIQMVFQDSISAVNPRKTVREIIRE-PLRhlLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 441 SIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDV- 519
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKl 240
|
....*
gi 2486247945 520 -FFHP 523
Cdd:PRK10419 241 tFSSP 245
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
285-514 |
4.23e-60 |
|
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: 197.74 E-value: 4.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRk 364
Cdd:cd03259 1 LELKGLSKTYG---------SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhglRRRLQVVFQDPyrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDaLNRYPNQFSGGQRQRISIAR 444
Cdd:cd03259 71 ----RRNIGMVFQDY--ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGL-LNRYPHELSGGQQQRVALAR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
13-266 |
6.63e-60 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 198.77 E-value: 6.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSlppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLAPADGSVKLLGMdlfrrtPDE 92
Cdd:PRK10418 4 QIELRNIALQ----AAQP-LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRVLLDGK------PVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAhvpMGPYERRIRILDLFEEVRLPDPPRIFRSYPHQLSGGQRQRI 172
Cdd:PRK10418 73 PCALRGRKIATIMQNPRSAFNPLHTMHTHARETCLA---LGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVL 252
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLF 229
|
250
....*....|....
gi 2486247945 253 QHPKEPYTQKLINA 266
Cdd:PRK10418 230 NAPKHAVTRSLVSA 243
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
285-522 |
1.76e-59 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 197.21 E-value: 1.76e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRk 364
Cdd:COG1131 1 IEVRGLTKRYG---------DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhgLRRRLQVVFQDPyrSLDPRMTVGEsivegpvN-------FGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQR 437
Cdd:COG1131 71 ---VRRRIGYVPQEP--ALYPDLTVRE-------NlrffarlYGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 438 QRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG--- 514
Cdd:COG1131 138 QRLGLALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGtpd 216
|
250
....*....|...
gi 2486247945 515 -----HVQDVFFH 522
Cdd:COG1131 217 elkarLLEDVFLE 229
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
11-269 |
1.15e-58 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 198.10 E-value: 1.15e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 11 LPVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLAPADGSVKLLGMDLFRRTP 90
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRI-----RILDLFEEVRLPDPPRIFRSYPHQLS 165
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRFgwrkrRAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIET 245
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260
....*....|....*....|....
gi 2486247945 246 GPAKSVLQHPKEPYTQKLINAVPE 269
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAIPD 264
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
286-509 |
2.03e-58 |
|
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: 193.45 E-value: 2.03e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 286 EAKNVVKTYtlggfftGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapKRKL 365
Cdd:cd03225 1 ELKNLSFSY-------PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLT---KLSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 366 HGLRRRLQVVFQDPYRSLdPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARA 445
Cdd:cd03225 71 KELRRKVGLVFQNPDDQF-FGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 446 LACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKLK-AEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
12-511 |
2.76e-58 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 201.79 E-value: 2.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPpgGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLpKGLAPAD-GSVKLLGMDLFRRTP 90
Cdd:COG1129 3 PLLEMRGISKSFG--GVK--ALDGVSLELRPGEVHALLGENGAGKS----TLMKIL-SGVYQPDsGEILLDGEPVRFRSP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLRgakMAMVFQEPmtALNPVMTCGDQM---DELLRAHVpMGPYERRIRILDLFEEVRLP-DPPRIFRSyphqLSG 166
Cdd:COG1129 74 RDAQAAG---IAIIHQEL--NLVPNLSVAENIflgREPRRGGL-IDWRAMRRRARELLARLGLDiDPDTPVGD----LSV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 167 GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 247 PAKSVLQHpkepytqKLINA-----VPELKPRHRPPVDgnPTLLEAKNVvktyTLGGFFtgrvkvralKGVSARLRRGET 321
Cdd:COG1129 223 PVAELTED-------ELVRLmvgreLEDLFPKRAAAPG--EVVLEVEGL----SVGGVV---------RDVSFSVRAGEI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 322 IGIVGESGSGKSTFARSIARLIDPTSGEVWVNGE-----NVAAAPK---------RKLHGLrrrlqvvFQDpyrsldprM 387
Cdd:COG1129 281 LGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirSPRDAIRagiayvpedRKGEGL-------VLD--------L 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGESIV----EGPVNFGV--PKEEAwKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSA 461
Cdd:COG1129 346 SIRENITlaslDRLSRGGLldRRRER-ALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRG 424
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2486247945 462 LDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECV 511
Cdd:COG1129 425 IDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
283-534 |
4.36e-58 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 194.62 E-value: 4.36e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 283 TLLEAKNVVKTYTL-GGFFTgRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAP 361
Cdd:PRK15112 3 TLLEVRNLSKTFRYrTGWFR-RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 362 krklHGLR-RRLQVVFQDPYRSLDPRMTVGEsIVEGPV--NFGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQ 438
Cdd:PRK15112 82 ----YSYRsQRIRMIFQDPSTSLNPRQRISQ-ILDFPLrlNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 439 RISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQD 518
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTAD 236
|
250
....*....|....*.
gi 2486247945 519 VFFHPQHEYTKSLIAA 534
Cdd:PRK15112 237 VLASPLHELTKRLIAG 252
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
12-266 |
7.42e-57 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 191.20 E-value: 7.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLP-----PGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDL- 85
Cdd:COG4167 3 ALLEVRNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIE----PTSGEILINGHKLe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 86 FRRTPDEIRRLRgakmaMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRL-PDPPRIfrsYPHQL 164
Cdd:COG4167 79 YGDYKYRCKHIR-----MIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPEHANF---YPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 165 SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIE 244
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|..
gi 2486247945 245 TGPAKSVLQHPKEPYTQKLINA 266
Cdd:COG4167 231 YGKTAEVFANPQHEVTKRLIES 252
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
281-532 |
7.65e-57 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 193.78 E-value: 7.65e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVVKTYtlGGFftgrvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAA 360
Cdd:COG3842 2 AMPALELENVSKRY--GDV-------TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 PKRKlhglrRRLQVVFQDpYrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRI 440
Cdd:COG3842 73 PPEK-----RNVGMVFQD-Y-ALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLA-DRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 441 SIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY 224
|
250
....*....|..
gi 2486247945 521 FHPQHEYTKSLI 532
Cdd:COG3842 225 ERPATRFVADFI 236
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
280-508 |
2.32e-56 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 189.53 E-value: 2.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 280 GNPTLLEAKNVVKTYTlggffTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVaa 359
Cdd:COG1116 3 AAAPALELRGVSKRFP-----TGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 360 apkrklHGLRRRLQVVFQDPyrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQR 439
Cdd:COG1116 76 ------TGPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 440 ISIARALACEPEILICDEAVSALDV----SVQADILKLLEEiqvkLGIGILFVTHDLRVASQICDDVIVIRRG 508
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDAltreRLQDELLRLWQE----TGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-519 |
4.99e-56 |
|
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: 196.56 E-value: 4.99e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLlpKGLAPADGSV--------------- 78
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGM--DQYEPTSGRIiyhvalcekcgyver 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 79 ---------------KLLGMDLFRRTPDEIRRLRgAKMAMVFQEPMtALNpvmtcGDQ--MDELLRAHVPMGpYERRI-- 139
Cdd:TIGR03269 75 pskvgepcpvcggtlEPEEVDFWNLSDKLRRRIR-KRIAIMLQRTF-ALY-----GDDtvLDNVLEALEEIG-YEGKEav 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 140 -RILDLFEEVRLPDppRIFRsYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVL 218
Cdd:TIGR03269 147 gRAVDLIEMVQLSH--RITH-IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 219 FITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQhpkepytqKLINAVPELKpRHRPPVDGNPtLLEAKNVVKTYtlgg 298
Cdd:TIGR03269 224 LTSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVA--------VFMEGVSEVE-KECEVEVGEP-IIKVRNVSKRY---- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 299 FFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVN-GENVAAAPKRKLHG---LRRRLQV 374
Cdd:TIGR03269 290 ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGrgrAKRYIGI 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 375 VFQDpyRSLDPRMTVGESIVEGpVNFGVPKEEAWKRAQEFMKIVRLSPDA----LNRYPNQFSGGQRQRISIARALACEP 450
Cdd:TIGR03269 370 LHQE--YDLYPHRTVLDNLTEA-IGLELPDELARMKAVITLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEP 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 451 EILICDEAVSALD----VSVQADILKLLEEiqvkLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDV 519
Cdd:TIGR03269 447 RIVILDEPTGTMDpitkVDVTHSILKAREE----MEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
281-532 |
9.28e-56 |
|
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: 187.49 E-value: 9.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAA 360
Cdd:COG1127 2 SEPMIEVRNLTKSF-------GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 PKRKLHGLRRRLQVVFQDP--YRSldprMTVGESI----VEgpvNFGVPKEEAWKRAQEFMKIVRLsPDALNRYPNQFSG 434
Cdd:COG1127 73 SEKELYELRRRIGMLFQGGalFDS----LTVFENVafplRE---HTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 435 GQRQRISIARALACEPEILICDEAVSALD-VSVqADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVES 513
Cdd:COG1127 145 GMRKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAE 223
|
250
....*....|....*....
gi 2486247945 514 GHVQDVfFHPQHEYTKSLI 532
Cdd:COG1127 224 GTPEEL-LASDDPWVRQFL 241
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
283-519 |
9.23e-55 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 184.88 E-value: 9.23e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 283 TLLEAKNVVKTYTlGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPK 362
Cdd:COG3638 1 PMLELRNLSKRYP-GG-------TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 363 RKLHGLRRRLQVVFQDPYrsLDPRMTVGESIVEGPVN--------FGVPKEEAWKRAQEFMKIVRLSPDALNRyPNQFSG 434
Cdd:COG3638 73 RALRRLRRRIGMIFQQFN--LVPRLSVLTNVLAGRLGrtstwrslLGLFPPEDRERALEALERVGLADKAYQR-ADQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 435 GQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDG 229
|
....*
gi 2486247945 515 HVQDV 519
Cdd:COG3638 230 PPAEL 234
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
285-523 |
1.09e-54 |
|
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: 183.83 E-value: 1.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlggfFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGEnvaaapkrK 364
Cdd:cd03293 1 LEVRNVSKTY-----GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE--------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDPyrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIAR 444
Cdd:cd03293 68 VTGPGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 445 ALACEPEILICDEAVSALDV----SVQADILKLLEEiqvkLGIGILFVTHDLRVASQICDDVIVIRRgecvESGHVQDVF 520
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRE----TGKTVLLVTHDIDEAVFLADRVVVLSA----RPGRIVAEV 216
|
...
gi 2486247945 521 FHP 523
Cdd:cd03293 217 EVD 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
285-532 |
2.12e-54 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 187.28 E-value: 2.12e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlGGFftgrvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAApkrk 364
Cdd:COG1118 3 IEVRNISKRF--GSF-------TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTN---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDPyrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISIAR 444
Cdd:COG1118 70 LPPRERRVGFVFQHY--ALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLA-DRYPSQLSGGQRQRVALAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQ 524
Cdd:COG1118 147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
....*...
gi 2486247945 525 HEYTKSLI 532
Cdd:COG1118 227 TPFVARFL 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
32-509 |
2.63e-54 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 191.39 E-value: 2.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIRRLrgaKMAMVFQEPMta 111
Cdd:COG3845 20 ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQ----PDSGEILIDGKPVRIRSPRDAIAL---GIGMVHQHFM-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTC------GdqMDELLRAHVPMGPYERRIRilDLFEEVRLP-DPprifRSYPHQLSGGQRQRIVIAMALLLKPDL 184
Cdd:COG3845 91 LVPNLTVaenivlG--LEPTKGGRLDRKAARARIR--ELSERYGLDvDP----DAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 185 LICDEPTTALnvTTQ-ASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPaksvlqhPKEPYTQKL 263
Cdd:COG3845 163 LILDEPTAVL--TPQeADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVD-------TAETSEEEL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 264 IN-----AVPElkPRHRPPVDGNPTLLEAKNVVktytlggfFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARS 338
Cdd:COG3845 234 AElmvgrEVLL--RVEKAPAEPGEVVLEVENLS--------VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 339 IARLIDPTSGEVWVNGENVAAAPKRKlhglRRRLQVVF--QDPYRS-LDPRMTVGESIV------EGPVNFGVPKEEAWK 409
Cdd:COG3845 304 LAGLRPPASGSIRLDGEDITGLSPRE----RRRLGVAYipEDRLGRgLVPDMSVAENLIlgryrrPPFSRGGFLDRKAIR 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 410 R-AQEFMKI--VRL-SPDALNRypnQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLeeiqVKL---G 482
Cdd:COG3845 380 AfAEELIEEfdVRTpGPDTPAR---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL----LELrdaG 452
|
490 500
....*....|....*....|....*..
gi 2486247945 483 IGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:COG3845 453 AAVLLISEDLDEILALSDRIAVMYEGR 479
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
6-264 |
3.64e-54 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 191.46 E-value: 3.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 6 LRAQKLPVLEVENLAVSLPPGG-------DRPNAVEHVSFTVNEGEVTCLIGESGSGKSviaSTVMGLLPkgLAPADGSV 78
Cdd:PRK15134 268 LPEPASPLLDVEQLQVAFPIRKgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKS---TTGLALLR--LINSQGEI 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 79 KLLGMDLFRRTPDEIRRLRgAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVP-MGPYERRIRILDLFEEVRLpDPPRIF 157
Cdd:PRK15134 343 WFDGQPLHNLNRRQLLPVR-HRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMEEVGL-DPETRH 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 158 RsYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVL 237
Cdd:PRK15134 421 R-YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVL 499
|
250 260
....*....|....*....|....*..
gi 2486247945 238 ELGKQIETGPAKSVLQHPKEPYTQKLI 264
Cdd:PRK15134 500 RQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
285-509 |
8.26e-54 |
|
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: 181.19 E-value: 8.26e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlGGFftgrvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAaPKRK 364
Cdd:cd03262 1 IEIKNLHKSF--GDF-------HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDpyRSLDPRMTVGESIVEGPVN-FGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISIA 443
Cdd:cd03262 71 INELRQKVGMVFQQ--FNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKA-DAYPAQLSGGQQQRVAIA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 444 RALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd03262 148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
308-532 |
7.24e-53 |
|
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: 180.92 E-value: 7.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHGLRR-RLQVVFQDpyRSLDPR 386
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS--FALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 MTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSV 466
Cdd:cd03294 117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWE-HKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 467 QADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLI 532
Cdd:cd03294 196 RREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
285-534 |
8.50e-53 |
|
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: 179.80 E-value: 8.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlGGFFtgrvkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03295 1 IEFENVTKRYG-GGKK-------AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LhglRRRLQVVFQDPyrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDAL-NRYPNQFSGGQRQRISIA 443
Cdd:cd03295 73 L---RRKIGYVIQQI--GLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFaDRYPHELSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 444 RALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHP 523
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
250
....*....|.
gi 2486247945 524 QHEYTKSLIAA 534
Cdd:cd03295 228 ANDFVAEFVGA 238
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
298-536 |
1.12e-52 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 187.61 E-value: 1.12e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 298 GFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIdPT------SGEVWVNGENVAAAPKRKLHGLR-R 370
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGVRgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 371 RLQVVFQDPYRSLDPRMTVGESIVEG-PVNFGVPKEEAWKRAQEFMKIV--RLSPDALNRYPNQFSGGQRQRISIARALA 447
Cdd:PRK15134 93 KIAMIFQEPMVSLNPLHTLEKQLYEVlSLHRGMRREAARGEILNCLDRVgiRQAAKRLTDYPHQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 448 CEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEY 527
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPY 252
|
....*....
gi 2486247945 528 TKSLIAAAP 536
Cdd:PRK15134 253 TQKLLNSEP 261
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
285-509 |
2.32e-52 |
|
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: 176.22 E-value: 2.32e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03229 1 LELKNVSKRYG---------QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHgLRRRLQVVFQDPyrSLDPRMTVGESIVEGpvnfgvpkeeawkraqefmkivrlspdalnrypnqFSGGQRQRISIAR 444
Cdd:cd03229 72 PP-LRRRIGMVFQDF--ALFPHLTVLENIALG-----------------------------------LSGGQQQRVALAR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd03229 114 ALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
285-515 |
5.77e-52 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 176.78 E-value: 5.77e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGgfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:COG2884 2 IRFENVSKRYPGG--------REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDpYRSLdPRMTVGESivegpVNF-----GVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQR 439
Cdd:COG2884 74 IPYLRRRIGVVFQD-FRLL-PDRTVYEN-----VALplrvtGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 440 ISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGH 515
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
284-520 |
7.18e-52 |
|
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: 177.54 E-value: 7.18e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVvkTYTLGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR 363
Cdd:COG1120 1 MLEAENL--SVGYGG-------RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLhglRRRLQVVFQDPyrSLDPRMTVGEsIVE-------GPvnFGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQ 436
Cdd:COG1120 72 EL---ARRIAYVPQEP--PAPFGLTVRE-LVAlgryphlGL--FGRPSAEDREAVEEALERTGLEHLA-DRPVDELSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 437 RQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHV 516
Cdd:COG1120 143 RQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
....
gi 2486247945 517 QDVF 520
Cdd:COG1120 223 EEVL 226
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
12-267 |
9.72e-52 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 177.70 E-value: 9.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSV-----KLLGMDLF 86
Cdd:COG4107 7 PLLSVRGLSKRYGPGCGTVVACRDVSFDLYPGEVLGIVGESGSGKS----TLLKCLYFDLAPTSGSVyyrdrDGGPRDLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 87 RRTPDEIRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRA----HvpmgpYER-RIRILDLFEEVRLPdPPRIFrSYP 161
Cdd:COG4107 83 ALSEAERRRLRRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAagerH-----YGDiRARALEWLERVEIP-LERID-DLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 162 HQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:COG4107 156 RTFSGGMQQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGR 235
|
250 260
....*....|....*....|....*.
gi 2486247945 242 QIETGPAKSVLQHPKEPYTQKLINAV 267
Cdd:COG4107 236 VVESGLTDQVLEDPQHPYTQLLVSSV 261
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
285-511 |
2.49e-51 |
|
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: 175.83 E-value: 2.49e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGgfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03256 1 IEVENLSKTYPNG--------KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDPyrSLDPRMTVGESIVEGPVN--------FGVPKEEAWKRAQEFMKIVRLSPDALNRyPNQFSGGQ 436
Cdd:cd03256 73 LRQLRRQIGMIFQQF--NLIERLSVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQR-ADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 437 RQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECV 511
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-256 |
7.79e-51 |
|
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: 174.31 E-value: 7.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDE 92
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLE----RPTSGSVLVDGTDLTLLSGKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRgAKMAMVFQ-----EPMTALNPVMTcgdqmdELLRAHVPMGpyERRIRILDLFEEVRLPDPPRifrSYPHQLSGG 167
Cdd:cd03258 77 LRKAR-RRIGMIFQhfnllSSRTVFENVAL------PLEIAGVPKA--EIEERVLELLELVGLEDKAD---AYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGP 247
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
....*....
gi 2486247945 248 AKSVLQHPK 256
Cdd:cd03258 225 VEEVFANPQ 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-264 |
1.40e-50 |
|
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: 173.63 E-value: 1.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPD 91
Cdd:COG1127 4 PMIEVRNLTKSF---GDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLR----PDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRgAKMAMVFQEPmtALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQR 171
Cdd:COG1127 76 ELYELR-RRIGMLFQGG--ALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPG---AADKMPSELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 172 IVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSV 251
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEEL 229
|
250
....*....|...
gi 2486247945 252 LQHPkEPYTQKLI 264
Cdd:COG1127 230 LASD-DPWVRQFL 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
14-303 |
2.02e-50 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 176.42 E-value: 2.02e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLER----PTSGSVLVDGVDLTALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRgAKMAMVFQ-----EPMTAL-N---PvmtcgdqmdeLLRAHVPMGpyERRIRILDLFEEVRLPDppRIfRSYPHQL 164
Cdd:COG1135 78 RAAR-RKIGMIFQhfnllSSRTVAeNvalP----------LEIAGVPKA--EIRKRVAELLELVGLSD--KA-DAYPSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 165 SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIE 244
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVE 221
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 245 TGPAKSVLQHPKEPYTQKLINAVpelkPRHRPPVDGNPTLLEAKNVVKTYTLggFFTGR 303
Cdd:COG1135 222 QGPVLDVFANPQSELTRRFLPTV----LNDELPEELLARLREAAGGGRLVRL--TFVGE 274
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
285-520 |
2.05e-50 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 174.16 E-value: 2.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGgfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAapKRK 364
Cdd:TIGR04520 1 IEVENVSFSYPES-------EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EEN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDPyrslDP---RMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRIS 441
Cdd:TIGR04520 72 LWEIRKKVGMVFQNP----DNqfvGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 442 IARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQiCDDVIVIRRGECVESGHVQDVF 520
Cdd:TIGR04520 147 IAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
285-530 |
3.68e-49 |
|
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: 169.60 E-value: 3.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03261 1 IELRGLTKSF-------GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDPyrSLDPRMTVGESiVEGPV--NFGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISI 442
Cdd:cd03261 72 LYRLRRRMGMLFQSG--ALFDSLTVFEN-VAFPLreHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 443 ARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDvFFH 522
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEE-LRA 226
|
....*...
gi 2486247945 523 PQHEYTKS 530
Cdd:cd03261 227 SDDPLVRQ 234
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
285-524 |
6.36e-49 |
|
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: 168.95 E-value: 6.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlGGFftgrvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03300 1 IELENVSKFY--GGF-------VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhglrRRLQVVFQDpYrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIAR 444
Cdd:cd03300 72 -----RPVNTVFQN-Y-ALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQ 524
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
36-276 |
6.51e-49 |
|
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: 169.99 E-value: 6.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDEIRRLRgAKMAMVFQEPMTALNPV 115
Cdd:TIGR02769 30 VSLSIEEGETVGLLGRSGCGKSTLARLLLGLE----KPAQGTVSFRGQDLYQLDRKQRRAFR-RDVQLVFQDSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 116 MTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPdpPRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALN 195
Cdd:TIGR02769 105 MTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLR--SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 196 VTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHpKEPYTQKLINAVPELKPRHR 275
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSAVLPEHPVRR 261
|
.
gi 2486247945 276 P 276
Cdd:TIGR02769 262 S 262
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
285-534 |
1.05e-48 |
|
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: 168.67 E-value: 1.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlGGFftgrvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03296 3 IEVRNVSKRF--GDF-------VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhglrRRLQVVFQdpYRSLDPRMTVGESIVEG----PVNFGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRI 440
Cdd:cd03296 74 -----RNVGFVFQ--HYALFRHMTVFDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLA-DRYPAQLSGGQRQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 441 SIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVY 225
|
250
....*....|....
gi 2486247945 521 FHPQHEYTKSLIAA 534
Cdd:cd03296 226 DHPASPFVYSFLGE 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
12-244 |
1.24e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 167.91 E-value: 1.24e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasT---VMGLLpkgLAPADGSVKLLGMDLFRR 88
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKS----TllnILGGL---DRPTSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 89 TPDEIRRLRGAKMAMVFQEP-----MTALNPVMTCgdqmdeLLRAHVPmgPYERRIRILDLFEEVRLPDppRIfRSYPHQ 163
Cdd:COG1136 76 SERELARLRRRHIGFVFQFFnllpeLTALENVALP------LLLAGVS--RKERRERARELLERVGLGD--RL-DHRPSQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFgVVSEIADQVVVLELGKQI 243
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
.
gi 2486247945 244 E 244
Cdd:COG1136 224 S 224
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
12-277 |
2.41e-48 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 177.35 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPN-------AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapADGSVKLLGMD 84
Cdd:PRK10261 312 PILQVRNLVTRFPLRSGLLNrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVES----QGGEIIFNGQR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 85 LFRRTPDEIRRLRgAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLpDPPRIFRsYPHQL 164
Cdd:PRK10261 388 IDTLSPGKLQALR-RDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGL-LPEHAWR-YPHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 165 SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIE 244
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
250 260 270
....*....|....*....|....*....|...
gi 2486247945 245 TGPAKSVLQHPKEPYTQKLINAVPELKPRHRPP 277
Cdd:PRK10261 545 IGPRRAVFENPQHPYTRKLMAAVPVADPSRQRP 577
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
284-519 |
3.35e-48 |
|
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: 167.34 E-value: 3.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR 363
Cdd:COG4555 1 MIEVENLSKKYG---------KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 klhgLRRRLQVVFQDPYrsLDPRMTVGESI-VEGPVNfGVPKEEAWKRAQEFMKIVRLSPDaLNRYPNQFSGGQRQRISI 442
Cdd:COG4555 72 ----ARRQIGVLPDERG--LYDRLTVRENIrYFAELY-GLFDEELKKRIEELIELLGLEEF-LDRRVGELSTGMKKKVAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 443 ARALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDV 519
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALK-KEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
14-241 |
3.88e-48 |
|
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: 166.51 E-value: 3.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS----TLLNILGGLDRPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRGAKMAMVFQEP-----MTALNPVMtcgdqmdellrahVPM-----GPYERRIRILDLFEEVRLPDpprIFRSYPHQ 163
Cdd:cd03255 77 AAFRRRHIGFVFQSFnllpdLTALENVE-------------LPLllagvPKKERRERAEELLERVGLGD---RLNHYPSE 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVsEIADQVVVLELGK 241
Cdd:cd03255 141 LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGK 217
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
307-536 |
6.50e-48 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 169.54 E-value: 6.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLID-P---TSGEVWVNGENVAAAP---KRKLHGlrRRLQVVFQDP 379
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISekeRRNLVG--AEVAMIFQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 380 YRSLDPRMTVGESIVEG-PVNFGVPKEEAWKRAQEFMKIVRLsPDALNR---YPNQFSGGQRQRISIARALACEPEILIC 455
Cdd:PRK11022 99 MTSLNPCYTVGFQIMEAiKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 456 DEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLIAAA 535
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRAL 257
|
.
gi 2486247945 536 P 536
Cdd:PRK11022 258 P 258
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
14-255 |
4.96e-47 |
|
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: 164.21 E-value: 4.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03261 1 IELRGLTKSF---GGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLR----PDSGEVLIDGEDISGLSEAEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRgAKMAMVFQEPmtALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIV 173
Cdd:cd03261 73 YRLR-RRMGMLFQSG--ALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRG---AEDLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQ 253
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
..
gi 2486247945 254 HP 255
Cdd:cd03261 227 SD 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
288-524 |
1.09e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 164.81 E-value: 1.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 288 KNVVKTYTLGGFFTGRvkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVnGENVAAAPKR--KL 365
Cdd:PRK13634 6 QKVEHRYQYKTPFERR----ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKnkKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 366 HGLRRRLQVVFQDPYRSLDPRmTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARA 445
Cdd:PRK13634 81 KPLRKKVGIVFQFPEHQLFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 446 LACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQ 524
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
309-458 |
3.85e-46 |
|
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: 158.58 E-value: 3.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVaaaPKRKLHGLRRRLQVVFQDPyrSLDPRMT 388
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL---TDDERKSLRKEIGYVFQDP--QLFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 389 VGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDA---LNRYPNQFSGGQRQRISIARALACEPEILICDEA 458
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-257 |
6.30e-46 |
|
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: 160.96 E-value: 6.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGgdrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK----PTSGEVLVDGKDITKKNLREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPmtalnpvmtcGDQM------DE----LLRAHVPmgPYERRIRILDLFEEVRLPDpprIFRSYPHQ 163
Cdd:COG1122 74 RR----KVGLVFQNP----------DDQLfaptveEDvafgPENLGLP--REEIRERVEEALELVGLEH---LADRPPHE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQI 243
Cdd:COG1122 135 LSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
250
....*....|....
gi 2486247945 244 ETGPAKSVLQHPKE 257
Cdd:COG1122 214 ADGTPREVFSDYEL 227
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
285-514 |
6.99e-46 |
|
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: 160.81 E-value: 6.99e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLID-----PTSGEVWVNGENVAA 359
Cdd:cd03260 1 IELRDLNVYYG---------DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 360 APKRKLHgLRRRLQVVFQDPYrsldP-RMTVGESIVEGPVNFGV-PKEEAWKRAQEFMKIVRLSPDALNR-YPNQFSGGQ 436
Cdd:cd03260 72 LDVDVLE-LRRRVGMVFQKPN----PfPGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 437 RQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKlgIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
285-532 |
7.39e-46 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 164.48 E-value: 7.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:COG3839 4 LELENVSKSY--GG-------VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhglrRRLQVVFQDPyrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIAR 444
Cdd:COG3839 75 -----RNIAMVFQSY--ALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 445 ALACEPEILICDEAVSALD----VSVQADILKLLEEiqvkLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRR----LGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELY 222
|
250
....*....|..
gi 2486247945 521 FHPQHEYTKSLI 532
Cdd:COG3839 223 DRPANLFVAGFI 234
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
305-548 |
7.49e-46 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 163.92 E-value: 7.49e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDP----TSGEVWVNGENV---AAAPKRKLhgLRRRLQVVFQ 377
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLlklSPRERRKI--IGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 378 DPYRSLDPRMTVGESIVEGpvnfgVPKEEA----WKRAQEFMKI---------VRLSPDALNRYPNQFSGGQRQRISIAR 444
Cdd:COG4170 97 EPSSCLDPSAKIGDQLIEA-----IPSWTFkgkwWQRFKWRKKRaiellhrvgIKDHKDIMNSYPHELTEGECQKVMIAM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQ 524
Cdd:COG4170 172 AIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPH 251
|
250 260
....*....|....*....|....
gi 2486247945 525 HEYTKSLIAAAPGTNYPFGRTAHL 548
Cdd:COG4170 252 HPYTKALLRSMPDFRQPLPHKSRL 275
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
285-509 |
7.59e-46 |
|
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: 158.71 E-value: 7.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRk 364
Cdd:cd03230 1 IEVRNLSKRYG---------KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhgLRRRLQVVFQDPyrSLDPRMTVGESIvegpvnfgvpkeeawkraqefmkivrlspdalnrypnQFSGGQRQRISIAR 444
Cdd:cd03230 71 ---VKRRIGYLPEEP--SLYENLTVRENL-------------------------------------KLSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
309-526 |
4.98e-45 |
|
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: 158.65 E-value: 4.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKlhglrRRLQVVFQDpyRSLDPRMT 388
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK-----RDISYVPQN--YALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 VGESIVEGPVNFGVPKEEAWKRAQE---FMKIVRLspdaLNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVS 465
Cdd:cd03299 88 VYKNIAYGLKKRKVDKKEIERKVLEiaeMLGIDHL----LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 466 VQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHE 526
Cdd:cd03299 164 TKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNE 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
15-241 |
7.73e-45 |
|
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: 157.24 E-value: 7.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 15 EVENLAVSlPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIR 94
Cdd:cd03225 1 ELKNLSFS-YPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG----PTSGEVLVDGKDLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 95 RlrgaKMAMVFQEPmtalnpvmtcgDQM-------DE----LLRAHVPmgPYERRIRILDLFEEVRLPDppriFRSY-PH 162
Cdd:cd03225 75 R----KVGLVFQNP-----------DDQffgptveEEvafgLENLGLP--EEEIEERVEEALELVGLEG----LRDRsPF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:cd03225 134 TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
309-524 |
9.08e-45 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 158.98 E-value: 9.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENV----------AAAPKRKLHGLRRRLQVVFQd 378
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlKVADKNQLRLLRTRLTMVFQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 379 pYRSLDPRMTVGESIVEGPVN-FGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDE 457
Cdd:PRK10619 100 -HFNLWSHMTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 458 AVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQ 524
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
14-253 |
1.37e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 157.53 E-value: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfRRTPDEI 93
Cdd:COG1131 1 IEVRGLTKRY---GDKT-ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLR----PTSGEVRVLGEDV-ARDPAEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPmtALNPVMTCGDQMDELLRAHvPMGPYERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIV 173
Cdd:COG1131 72 RR----RIGYVPQEP--ALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTD---AADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQ 253
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
281-520 |
1.40e-44 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 157.94 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVvkTYTLGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAA 360
Cdd:COG1121 3 MMPAIELENL--TVSYGG-------RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 pkrklhglRRRLQVVFQdpYRSLDPR--MTVGEsIVE----GPVN-FGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFS 433
Cdd:COG1121 74 --------RRRIGYVPQ--RAEVDWDfpITVRD-VVLmgryGRRGlFRRPSRADREAVDEALERVGLE-DLADRPIGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 434 GGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGeCVES 513
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYFDRVLLLNRG-LVAH 219
|
....*..
gi 2486247945 514 GHVQDVF 520
Cdd:COG1121 220 GPPEEVL 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
309-509 |
1.89e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 156.13 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPkrkLHGLRRRLQVVFQDPYRsldPRMT 388
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQVAYVPQEPAL---WGGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 VGEsivegpvNFGVP-----KEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALD 463
Cdd:COG4619 90 VRD-------NLPFPfqlreRKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2486247945 464 VSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:COG4619 163 PENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-237 |
3.64e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 157.17 E-value: 3.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPD 91
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEK----PTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 eirrlrgakMAMVFQEP-----MTALNPVMTcGdqmdeLLRAHVPMGpyERRIRILDLFEEVRLPDppriFR-SYPHQLS 165
Cdd:COG1116 82 ---------RGVVFQEPallpwLTVLDNVAL-G-----LELRGVPKA--ERRERARELLELVGLAG----FEdAYPHQLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfgvVSE---IADQVVVL 237
Cdd:COG1116 141 GGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDEavfLADRVVVL 212
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
285-514 |
4.39e-44 |
|
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: 155.61 E-value: 4.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlGGFftgrvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKrk 364
Cdd:cd03265 1 IEVENLVKKY--GDF-------EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPR-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhGLRRRLQVVFQDPyrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIAR 444
Cdd:cd03265 70 --EVRRRIGIVFQDL--SVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03265 145 SLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
284-534 |
6.80e-44 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 156.24 E-value: 6.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYtlggfftGRVKvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVwvnGENVAAAPKR 363
Cdd:PRK11701 6 LLSVRGLTKLY-------GPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV---HYRMRDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGL----RRRLQ-----VVFQDPYRSLDPRMTVGESIVE-----GPVNFGVPKEEAwkraQEFMKIVRLSPDALNRYP 429
Cdd:PRK11701 74 DLYALseaeRRRLLrtewgFVHQHPRDGLRMQVSAGGNIGErlmavGARHYGDIRATA----GDWLERVEIDAARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 430 NQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250 260
....*....|....*....|....*
gi 2486247945 510 CVESGHVQDVFFHPQHEYTKSLIAA 534
Cdd:PRK11701 230 VVESGLTDQVLDDPQHPYTQLLVSS 254
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-255 |
1.18e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 155.25 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfrrtpd 91
Cdd:COG1121 5 PAIELENLTVSY---GGRP-VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP----PTSGTVRLFGKPP------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 eirRLRGAKMAMVFQE-------PMTALNPVMTCgdqmdeLLRAHVPMGPY--ERRIRILDLFEEVRLPDppriFRSYP- 161
Cdd:COG1121 71 ---RRARRRIGYVPQRaevdwdfPITVRDVVLMG------RYGRRGLFRRPsrADREAVDEALERVGLED----LADRPi 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 162 HQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLElGK 241
Cdd:COG1121 138 GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVREYFDRVLLLN-RG 215
|
250
....*....|....
gi 2486247945 242 QIETGPAKSVLQHP 255
Cdd:COG1121 216 LVAHGPPEEVLTPE 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
285-519 |
2.31e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 156.40 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGGfftgRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEV-------------- 350
Cdd:PRK13651 3 IKVKNIVKIFNKKL----PTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 351 ---WVNGENVAAAPKRK----LHGLRRRLQVVFQ-DPYRSLDPrmTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSP 422
Cdd:PRK13651 79 ekeKVLEKLVIQKTRFKkikkIKEIRRRVGVVFQfAEYQLFEQ--TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 423 DALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDV 502
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLN-KQGKTIILVTHDLDNVLEWTKRT 235
|
250
....*....|....*..
gi 2486247945 503 IVIRRGECVESGHVQDV 519
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDI 252
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
307-520 |
2.42e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 155.98 E-value: 2.42e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAApKRKLHGLRRRLQVVFQDPYRSLDPR 386
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDK-KVKLSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 mTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDAL-NRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVS 465
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 466 VQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
286-514 |
3.70e-43 |
|
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: 151.82 E-value: 3.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 286 EAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKL 365
Cdd:cd03214 1 EVENLSVGYG---------GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 366 hglRRRLQVVFQdpyrsldprmtvgesivegpvnfgvpkeeawkrAQEFMKIVRLSpdalNRYPNQFSGGQRQRISIARA 445
Cdd:cd03214 72 ---ARKIAYVPQ---------------------------------ALELLGLAHLA----DRPFNELSGGERQRVLLARA 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 446 LACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03214 112 LAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-267 |
1.16e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 152.46 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRtPDE 92
Cdd:COG1126 1 MIEIENLHKSF---GDLE-VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEE----PDSGTITVDGEDLTDS-KKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRgAKMAMVFQE----P-MTALNPVMtcgdqmdELLRAHVPMGPYERRIRILDLFEEVRLPDppRIfRSYPHQLSGG 167
Cdd:COG1126 72 INKLR-RKVGMVFQQfnlfPhLTVLENVT-------LAPIKVKKMSKAEAEERAMELLERVGLAD--KA-DAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTAL---NVttqASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIE 244
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALdpeLV---GEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVE 216
|
250 260
....*....|....*....|...
gi 2486247945 245 TGPAKSVLQHPKEPYTQKLINAV 267
Cdd:COG1126 217 EGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
14-237 |
2.32e-42 |
|
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: 151.09 E-value: 2.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDei 93
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER----PTSGEVLVDGEPVTGPGPD-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 rrlrgakMAMVFQEP-----MTALNPVMTcGDQMDELLRAhvpmgpyERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQ 168
Cdd:cd03293 75 -------RGYVFQQDallpwLTVLDNVAL-GLELQGVPKA-------EARERAEELLELVGLSG---FENAYPHQLSGGM 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 169 RQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfgvVSE---IADQVVVL 237
Cdd:cd03293 137 RQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD---IDEavfLADRVVVL 205
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
281-512 |
2.92e-42 |
|
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: 151.05 E-value: 2.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVVKTYTLGGfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAA 360
Cdd:COG4181 5 SAPIIELRGLTKTVGTGA---GELTI--LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 PKRKLHGLRRR-LQVVFQdpyrS--LDPRMTVGEsivegpvNFGVPKE-----EAWKRAQEFMKIVRLSpDALNRYPNQF 432
Cdd:COG4181 80 DEDARARLRARhVGFVFQ----SfqLLPTLTALE-------NVMLPLElagrrDARARARALLERVGLG-HRLDHYPAQL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 433 SGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQiCDDVIVIRRGECVE 512
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
251-514 |
3.13e-42 |
|
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: 161.16 E-value: 3.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 251 VLQHPKEPytqklinaVPELKPRHRPPVDGNptlLEAKNVVKTYtlggfftGRVKVRALKGVSARLRRGETIGIVGESGS 330
Cdd:COG2274 451 ILDLPPER--------EEGRSKLSLPRLKGD---IELENVSFRY-------PGDSPPVLDNISLTIKPGERVAIVGRSGS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 331 GKSTFARSIARLIDPTSGEVWVNGENVAAAPkrkLHGLRRRLQVVFQDPYrsLDPRmTVGESIVEGpvNFGVPKEEAWKR 410
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQIGVVLQDVF--LFSG-TIRENITLG--DPDATDEEIIEA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 411 AQ-----EFmkIVRLsPDALNRY----PNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqvKL 481
Cdd:COG2274 585 ARlaglhDF--IEAL-PMGYDTVvgegGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LK 659
|
250 260 270
....*....|....*....|....*....|...
gi 2486247945 482 GIGILFVTHDLRVAsQICDDVIVIRRGECVESG 514
Cdd:COG2274 660 GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDG 691
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
31-266 |
1.14e-41 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 150.71 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 31 NAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTpdeiRRLRGAKMAMVFQEPMT 110
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMI----EPTSGELLIDDHPLHFGD----YSYRSQRIRMIFQDPST 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRL-PDPPRIfrsYPHQLSGGQRQRIVIAMALLLKPDLLICDE 189
Cdd:PRK15112 99 SLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASY---YPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 190 PTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLINA 266
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
285-509 |
1.42e-41 |
|
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: 148.71 E-value: 1.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGgfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03292 1 IEFINVTKTYPNG--------TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDpYRSLdPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIAR 444
Cdd:cd03292 73 IPYLRRKIGVVFQD-FRLL-PDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVAIAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
285-509 |
1.66e-41 |
|
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: 147.14 E-value: 1.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPkrk 364
Cdd:cd03228 1 IEFKNVSFSYPGRP-------KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDPYRsldPRMTVGESIvegpvnfgvpkeeawkraqefmkivrlspdalnrypnqFSGGQRQRISIAR 444
Cdd:cd03228 71 LESLRKNIAYVPQDPFL---FSGTIRENI--------------------------------------LSGGQRQRIAIAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIqvKLGIGILFVTHDLRVAsQICDDVIVIRRGE 509
Cdd:cd03228 110 ALLRDPPILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
283-529 |
1.97e-41 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 149.52 E-value: 1.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 283 TLLEAKNVVKTytlggfFTGRvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSG-----EVWVNGENV 357
Cdd:PRK11264 2 SAIEVKNLVKK------FHGQ---TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 358 AAAPKRKLHGLRRRLQVVFQDpyRSLDPRMTVGESIVEGPVNF-GVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQ 436
Cdd:PRK11264 73 LSQQKGLIRQLRQHVGFVFQN--FNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKE-TSYPRRLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 437 RQRISIARALACEPEILICDEAVSALDV----SVQADILKLLEEIQVklgigILFVTHDLRVASQICDDVIVIRRGECVE 512
Cdd:PRK11264 150 QQRVAIARALAMRPEVILFDEPTSALDPelvgEVLNTIRQLAQEKRT-----MVIVTHEMSFARDVADRAIFMDQGRIVE 224
|
250
....*....|....*..
gi 2486247945 513 SGHVQDVFFHPQHEYTK 529
Cdd:PRK11264 225 QGPAKALFADPQQPRTR 241
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
285-514 |
2.11e-41 |
|
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: 148.17 E-value: 2.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03301 1 VELENVTKRFG---------NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhglrRRLQVVFQDpYrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIAR 444
Cdd:cd03301 72 -----RDIAMVFQN-Y-ALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIE-HLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
11-276 |
4.83e-41 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 149.07 E-value: 4.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 11 LPVLEVENLA-----VSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDL 85
Cdd:PRK10419 1 MTLLNVSGLShhyahGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLE----SPSQGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 86 FRRTPDEIRRLRGAkMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPdpPRIFRSYPHQLS 165
Cdd:PRK10419 77 AKLNRAQRKAFRRD-IQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLD--DSVLDKRPPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIET 245
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
250 260 270
....*....|....*....|....*....|.
gi 2486247945 246 GPAkSVLQHPKEPYTQKLINAVPELKPRHRP 276
Cdd:PRK10419 234 QPV-GDKLTFSSPAGRVLQNAVLPAFPVRRR 263
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
284-523 |
5.06e-41 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 147.93 E-value: 5.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAaPKR 363
Cdd:PRK09493 1 MIEFKNVSKHF-------GPTQV--LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGLRRRLQVVFQDPYrsLDPRMTVGESIVEGPVNF-GVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISI 442
Cdd:PRK09493 71 DERLIRQEAGMVFQQFY--LFPHLTALENVMFGPLRVrGASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 443 ARALACEPEILICDEAVSALDVSVQADILK----LLEEiqvklGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQD 518
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKvmqdLAEE-----GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
....*
gi 2486247945 519 VFFHP 523
Cdd:PRK09493 223 LIKNP 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
308-522 |
1.39e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 148.24 E-value: 1.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNG-----ENVaaapkrklHGLRRRLQVVFQDPyrs 382
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGmvlseETV--------WDVRRQVGMVFQNP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 383 lDPRM---TVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAV 459
Cdd:PRK13635 91 -DNQFvgaTVQDDVAFGLENIGVPREEMVERVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 460 SALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQiCDDVIVIRRGECVESGHVQDVFFH 522
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
261-514 |
1.58e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 154.55 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 261 QKLINAVPELK----PRHRPPVDGNptlLEAKNVVktytlggfFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFA 336
Cdd:COG1132 315 FELLDEPPEIPdppgAVPLPPVRGE---IEFENVS--------FSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLV 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 337 RSIARLIDPTSGEVWVNGENVAAAPkrkLHGLRRRLQVVFQDPYRsLDprMTVGESIVegpvnFGVPK------EEAWKR 410
Cdd:COG1132 384 NLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQIGVVPQDTFL-FS--GTIRENIR-----YGRPDatdeevEEAAKA 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 411 AQ--EFmkIVRLsPDALNrYP-----NQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVklGI 483
Cdd:COG1132 453 AQahEF--IEAL-PDGYD-TVvgergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GR 526
|
250 260 270
....*....|....*....|....*....|..
gi 2486247945 484 GILFVTHdlRVAS-QICDDVIVIRRGECVESG 514
Cdd:COG1132 527 TTIVIAH--RLSTiRNADRILVLDDGRIVEQG 556
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
319-526 |
1.59e-40 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 146.70 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 319 GETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGE--NVAAAPKRK-LHGLRRRLQVVFQDpYrSLDPRMTVGESIVE 395
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKaIRELRRNVGMVFQQ-Y-NLWPHLTVQQNLIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 396 GPVN-FGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLL 474
Cdd:PRK11124 106 APCRvLGLSKDQALARAEKLLERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSII 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 475 EEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHvQDVFFHPQHE 526
Cdd:PRK11124 185 RELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTE 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
12-509 |
1.98e-40 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 153.40 E-value: 1.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPggdrPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPD 91
Cdd:PRK09700 4 PYISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKS----TLMKVLSGIHEPTKGTITINNINYNKLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLrgaKMAMVFQE-----PMTALNPVM--------TCGdqmdellrahVPMGPY-ERRIRILDLFEEVRLPDPPRIF 157
Cdd:PRK09700 76 LAAQL---GIGIIYQElsvidELTVLENLYigrhltkkVCG----------VNIIDWrEMRVRAAMMLLRVGLKVDLDEK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 158 RSyphQLSGGQRQRIVIAMALLLKPDLLICDEPTTALnvtTQASI--LKLILELQKKNGTAVLFITHDFGVVSEIADQVV 235
Cdd:PRK09700 143 VA---NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 236 VLELGKQIETGPAKSVLQHP--KEPYTQKLINAVPELKPRHRPPvdGNPTLLEAKNVvktytlggffTGRVKVRAlKGVS 313
Cdd:PRK09700 217 VMKDGSSVCSGMVSDVSNDDivRLMVGRELQNRFNAMKENVSNL--AHETVFEVRNV----------TSRDRKKV-RDIS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 314 ARLRRGETIGIVGESGSGKSTFARSIARlIDP-TSGEVWVNGENVAaaPKRKLHGLRRRLQVVFQD-------PYRSLDP 385
Cdd:PRK09700 284 FSVCRGEILGFAGLVGSGRTELMNCLFG-VDKrAGGEIRLNGKDIS--PRSPLDAVKKGMAYITESrrdngffPNFSIAQ 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 386 RMTVGESI----VEGPVNFGVPKEEAwKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSA 461
Cdd:PRK09700 361 NMAISRSLkdggYKGAMGLFHEVDEQ-RTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2486247945 462 LDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
323-523 |
6.38e-40 |
|
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: 148.33 E-value: 6.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 323 GIVGESGSGKSTFARSIARLIDPTSGEVWVNGE---NVAAAPKRKLHglRRRLQVVFQDPyrSLDPRMTVgesivEGPVN 399
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARGIFLPPH--RRRIGYVFQEA--RLFPHLSV-----RGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 400 FGVPKEEAWKRAQEFMKIVRL---SPdALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEE 476
Cdd:COG4148 100 YGRKRAPRAERRISFDEVVELlgiGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLER 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2486247945 477 IQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHP 523
Cdd:COG4148 179 LRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
13-285 |
6.62e-40 |
|
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: 145.57 E-value: 6.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDE 92
Cdd:COG1120 1 MLEAENLSVGY---GGRP-VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK----PSSGEVLLDGRDLASLSRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRlrgaKMAMVFQEPMTALNpvMTCGDQmdellrahVPMG--PYERRIR---------ILDLFEEVRLPDppriF--RS 159
Cdd:COG1120 73 LAR----RIAYVPQEPPAPFG--LTVREL--------VALGryPHLGLFGrpsaedreaVEEALERTGLEH----LadRP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 160 YpHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLEL 239
Cdd:COG1120 135 V-DELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKD 213
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2486247945 240 GKQIETGPAKSVLqhpkepyTQKLINAVPELKPR-HRPPVDGNPTLL 285
Cdd:COG1120 214 GRIVAQGPPEEVL-------TPELLEEVYGVEARvIEDPVTGRPLVL 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
308-526 |
1.09e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 144.39 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGE--NVAAAPK-RKLHGLRRRLQVVFQDpYrSLD 384
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSeKAIRLLRQKVGMVFQQ-Y-NLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 385 PRMTVGESIVEGPVN-FGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALD 463
Cdd:COG4161 95 PHLTVMENLIEAPCKvLGLSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 464 VSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHvQDVFFHPQHE 526
Cdd:COG4161 174 PEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTE 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-237 |
1.59e-39 |
|
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: 143.06 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 15 EVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfrrtpdeir 94
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK----PTSGSIRVFGKPL--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 95 RLRGAKMAMVFQE-------PMTALNPVMTcGdqmdelLRAHVPMGPY---ERRIRILDLFEEVRLPDppriFRSYP-HQ 163
Cdd:cd03235 64 EKERKRIGYVPQRrsidrdfPISVRDVVLM-G------LYGHKGLFRRlskADKAKVDEALERVGLSE----LADRQiGE 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVL 237
Cdd:cd03235 133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
282-535 |
2.02e-39 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 144.20 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 282 PTLLEAKNVVKTYTLGgfftgrvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGEN----- 356
Cdd:TIGR02323 1 KPLLQVSGLSKSYGGG---------KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaele 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 357 ---VAAAPKRKLhgLRRRLQVVFQDPYRSLDPRMTVGESIVEGPVNFGVPKEEAWKR-AQEFMKIVRLSPDALNRYPNQF 432
Cdd:TIGR02323 72 lyqLSEAERRRL--MRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHYGNIRAtAQDWLEEVEIDPTRIDDLPRAF 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 433 SGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVE 512
Cdd:TIGR02323 150 SGGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVE 229
|
250 260
....*....|....*....|...
gi 2486247945 513 SGHVQDVFFHPQHEYTKSLIAAA 535
Cdd:TIGR02323 230 SGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-267 |
2.50e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 146.48 E-value: 2.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 15 EVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDEIR 94
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLE----RPTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 95 RLRgAKMAMVFQE---------------PMtalnpvmtcgdqmdELlrAHVPMGpyERRIRILDLFEEVRLPDPPRifrS 159
Cdd:PRK11153 79 KAR-RQIGMIFQHfnllssrtvfdnvalPL--------------EL--AGTPKA--EIKARVTELLELVGLSDKAD---R 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 160 YPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLEL 239
Cdd:PRK11153 137 YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDA 216
|
250 260
....*....|....*....|....*...
gi 2486247945 240 GKQIETGPAKSVLQHPKEPYTQKLINAV 267
Cdd:PRK11153 217 GRLVEQGTVSEVFSHPKHPLTREFIQST 244
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
284-549 |
3.60e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 144.06 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTLGgfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAApKR 363
Cdd:PRK13639 1 ILETRDLKYSYPDG--------TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYD-KK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGLRRRLQVVFQDPYRSL-DPrmTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISI 442
Cdd:PRK13639 72 SLLEVRKTVGIVFQNPDDQLfAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGME-GFENKPPHHLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 443 ARALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFfh 522
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLN-KEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVF-- 225
|
250 260
....*....|....*....|....*..
gi 2486247945 523 pqheytkSLIAAAPGTNYPFGRTAHLF 549
Cdd:PRK13639 226 -------SDIETIRKANLRLPRVAHLI 245
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
14-241 |
3.78e-39 |
|
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: 140.61 E-value: 3.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRtPDEI 93
Cdd:cd03230 1 IEVRNLSKRY---GKKT-ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK----PDSGEIKVLGKDIKKE-PEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPMtaLNPVMTCGDQMDellrahvpmgpyerririldlfeevrlpdpprifrsyphqLSGGQRQRIV 173
Cdd:cd03230 72 KR----RIGYLPEEPS--LYENLTVRENLK----------------------------------------LSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGR 172
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
286-508 |
4.29e-39 |
|
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: 141.90 E-value: 4.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 286 EAKNVvkTYTLGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGenvaaapkRKL 365
Cdd:cd03235 1 EVEDL--TVSYGG-------HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG--------KPL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 366 HGLRRRLQVVFQdpYRSLDPRM--TVGESIVEGPVN----FGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQR 439
Cdd:cd03235 64 EKERKRIGYVPQ--RRSIDRDFpiSVRDVVLMGLYGhkglFRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 440 ISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRG 508
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELR-REGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-267 |
5.41e-39 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 143.14 E-value: 5.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGgdrpNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLG-----MDLF 86
Cdd:PRK11701 5 PLLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKT----TLLNALSARLAPDAGEVHYRMrdgqlRDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 87 RRTPDEIRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLrahvpMGPYER---RIR--ILDLFEEV-----RLPDPPRI 156
Cdd:PRK11701 77 ALSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERL-----MAVGARhygDIRatAGDWLERVeidaaRIDDLPTT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 157 FrsyphqlSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVV 236
Cdd:PRK11701 152 F-------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLV 224
|
250 260 270
....*....|....*....|....*....|.
gi 2486247945 237 LELGKQIETGPAKSVLQHPKEPYTQKLINAV 267
Cdd:PRK11701 225 MKQGRVVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
14-256 |
5.89e-39 |
|
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: 142.19 E-value: 5.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppGGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03219 1 LEVRGLTKRF--GGLV--ALDDVSFSVRPGEIHGLIGPNGAGKT----TLFNLISGFLRPTSGSVLFDGEDITGLPPHEI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlRGakMAMVFQEP-----MTALNPVMTCG--DQMDELLRAHVPMGPYERRIRILDLFEEVRLPDppriFRSYP-HQLS 165
Cdd:cd03219 73 AR-LG--IGRTFQIPrlfpeLTVLENVMVAAqaRTGSGLLLARARREEREARERAEELLERVGLAD----LADRPaGELS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIET 245
Cdd:cd03219 146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
250
....*....|.
gi 2486247945 246 GPAKSVLQHPK 256
Cdd:cd03219 225 GTPDEVRNNPR 235
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
281-538 |
6.04e-39 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 145.63 E-value: 6.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaa 360
Cdd:PRK11432 3 QKNFVVLKNITKRFG---------SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 pKRKLHglRRRLQVVFQDpYrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRI 440
Cdd:PRK11432 72 -HRSIQ--QRDICMVFQS-Y-ALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFE-DRYVDQISGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 441 SIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK11432 146 ALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY 225
|
250 260
....*....|....*....|.
gi 2486247945 521 FHPQHEYTKSLIAAA---PGT 538
Cdd:PRK11432 226 RQPASRFMASFMGDAnifPAT 246
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
310-534 |
8.97e-39 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 142.53 E-value: 8.97e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 310 KGVSARLRRGETIGIVGESGSGKS-TFARSIARL---IDPTSGEVWVNGENVAAApkrKLHGlrRRLQVVFQDPYRSLDP 385
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPC---ALRG--RKIATIMQNPRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 386 RMTVGESIVEGPVNFGVPKEEAwkRAQEFMKIVRLSPDA--LNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALD 463
Cdd:PRK10418 95 LHTMHTHARETCLALGKPADDA--TLTAALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 464 VSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLIAA 534
Cdd:PRK10418 173 VVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
319-514 |
1.10e-38 |
|
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: 140.89 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 319 GETIGIVGESGSGKSTFARSIARLIDPTSGE------VWVNGENVAAAPKRklhglRRRLQVVFQDpyRSLDPRMTVGES 392
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTivlngtVLFDSRKKINLPPQ-----QRKIGLVFQQ--YALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 393 IVegpvnFGVPKEEAWKRAQEFMKIV-RLSPDAL-NRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADI 470
Cdd:cd03297 96 LA-----FGLKRKRNREDRISVDELLdLLGLDHLlNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2486247945 471 LKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
12-259 |
1.67e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 144.47 E-value: 1.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPD 91
Cdd:COG3842 4 PALELENVSKRY---GDVT-ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFET----PDSGRILLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EirrlRGakMAMVFQEPmtALNPVMTCGD------QMDELLRAhvpmgpyERRIRILDLFEEVRLPDppriF-RSYPHQL 164
Cdd:COG3842 76 K----RN--VGMVFQDY--ALFPHLTVAEnvafglRMRGVPKA-------EIRARVAELLELVGLEG----LaDRYPHQL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 165 SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFgvvSE---IADQVVVLELGK 241
Cdd:COG3842 137 SGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQ---EEalaLADRIAVMNDGR 213
|
250
....*....|....*...
gi 2486247945 242 QIETGPAKSVLQHPKEPY 259
Cdd:COG3842 214 IEQVGTPEEIYERPATRF 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-248 |
1.98e-38 |
|
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: 140.65 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKsviaSTVMGLLpKGL-APADGSVKLLGMDLFRRTP 90
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGK----STLLGLL-AGLdRPTSGTVRLAGQDLFALDE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLRGAKMAMVFQE----P-MTALNPVMtcgdqmdellrahVPM---GPYERRIRILDLFEEVRLPDppRIfRSYPH 162
Cdd:COG4181 82 DARARLRARHVGFVFQSfqllPtLTALENVM-------------LPLelaGRRDARARARALLERVGLGH--RL-DHYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfgvvSEIA---DQVVVLEL 239
Cdd:COG4181 146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHD----PALAarcDRVLRLRA 221
|
....*....
gi 2486247945 240 GKQIETGPA 248
Cdd:COG4181 222 GRLVEDTAA 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
14-246 |
2.33e-38 |
|
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: 139.96 E-value: 2.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppGGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEi 93
Cdd:cd03259 1 LELKGLSKTY--GSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER----PDSGEILIDGRDVTGVPPER- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLrgakmAMVFQEPmtALNPVMTCGDQMDELLRAHVPMGPyERRIRILDLFEEVRLPDPpriFRSYPHQLSGGQRQRIV 173
Cdd:cd03259 72 RNI-----GMVFQDY--ALFPHLTVAENIAFGLKLRGVPKA-EIRARVRELLELVGLEGL---LNRYPHELSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
12-256 |
2.78e-38 |
|
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: 140.94 E-value: 2.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppGGDRpnAVEHVSFTVNEGEVTCLIGESGSGKsviaSTVMGLLPKGLAPADGSVKLLGMDLFRRTPD 91
Cdd:COG0411 3 PLLEVRGLTKRF--GGLV--AVDDVSLEVERGEIVGLIGPNGAGK----TTLFNLITGFYRPTSGRILFDGRDITGLPPH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRlRGakMAMVFQEP-----MTALNPVMT-CGDQMDELLRAHVPMGPY----ERRIR--ILDLFEEVRLPDpprIFRS 159
Cdd:COG0411 75 RIAR-LG--IARTFQNPrlfpeLTVLENVLVaAHARLGRGLLAALLRLPRarreEREARerAEELLERVGLAD---RADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 160 YPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLEL 239
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
250
....*....|....*..
gi 2486247945 240 GKQIETGPAKSVLQHPK 256
Cdd:COG0411 229 GRVIAEGTPAEVRADPR 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
16-512 |
3.36e-38 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 147.13 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 16 VENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGsvkllgmdlfrrtpdEIRR 95
Cdd:COG0488 1 LENLSKSF---GGRP-LLDDVSLSINPGDRIGLVGRNGAGKS----TLLKILAGELEPDSG---------------EVSI 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 96 LRGAKMAMVFQEP------------MTALNPVMTCGDQMDELLRAhvpMGPYERRI-RILDLFEEVRLPD----PPRI-- 156
Cdd:COG0488 58 PKGLRIGYLPQEPpldddltvldtvLDGDAELRALEAELEELEAK---LAEPDEDLeRLAELQEEFEALGgweaEARAee 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 157 ------FRSYPHQ-----LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVttqASILKLILELQKKNGTaVLFITHD-- 223
Cdd:COG0488 135 ilsglgFPEEDLDrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDL---ESIEWLEEFLKNYPGT-VLVVSHDry 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 224 F--GVVSEIADqvvvLELGK--------------------------------------QIETGPAKSvlQHPKEPytQKL 263
Cdd:COG0488 211 FldRVATRILE----LDRGKltlypgnysayleqraerleqeaaayakqqkkiakeeeFIRRFRAKA--RKAKQA--QSR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 264 INAVPELKPRHRPPVDGNP------------TLLEAKNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSG 331
Cdd:COG0488 283 IKALEKLEREEPPRRDKTVeirfppperlgkKVLELEGLSKSY-------GDKTL--LDDLSLRIDRGDRIGLIGPNGAG 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 332 KSTFARSIARLIDPTSGEVWVnGENVaaapkrklhglrrrlQVVF--QDpYRSLDPRMTVGESIVEGpvNFGVPKEEAWK 409
Cdd:COG0488 354 KSTLLKLLAGELEPDSGTVKL-GETV---------------KIGYfdQH-QEELDPDKTVLDELRDG--APGGTEQEVRG 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 410 RAQEFMkivrLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDV-SVQAdILKLLEEIQvklgiG-ILF 487
Cdd:COG0488 415 YLGRFL----FSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA-LEEALDDFP-----GtVLL 484
|
570 580
....*....|....*....|....*
gi 2486247945 488 VTHDLRVASQICDDVIVIRRGECVE 512
Cdd:COG0488 485 VSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-246 |
3.83e-38 |
|
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: 138.34 E-value: 3.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 15 EVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIR 94
Cdd:cd03214 1 EVENLSVGY---GGRT-VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLK----PSSGEILLDGKDLASLSPKELA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 95 RlrgaKMAMVFQepmtALnpvmtcgdqmdellrahvpmgpyeRRIRILDLfeevrlpdpprIFRSYpHQLSGGQRQRIVI 174
Cdd:cd03214 73 R----KIAYVPQ----AL------------------------ELLGLAHL-----------ADRPF-NELSGGERQRVLL 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 175 AMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
285-520 |
4.79e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 141.51 E-value: 4.79e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGGFFtgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:PRK13641 3 IKFENVDYIYSPGTPM----EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 -LHGLRRRLQVVFQDPYRSLDPRmTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIA 443
Cdd:PRK13641 79 nLKKLRKKVSLVFQFPEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 444 RALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13641 158 GVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQ-KAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIF 233
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
286-509 |
5.63e-38 |
|
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: 136.99 E-value: 5.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 286 EAKNVVKTYtlggfftgrVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapKRKL 365
Cdd:cd00267 1 EIENLSFRY---------GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIA---KLPL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 366 HGLRRRLQVVFQdpyrsldprmtvgesivegpvnfgvpkeeawkraqefmkivrlspdalnrypnqFSGGQRQRISIARA 445
Cdd:cd00267 69 EELRRRIGYVPQ------------------------------------------------------LSGGQRQRVALARA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 446 LACEPEILICDEAVSALDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd00267 95 LLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-241 |
7.91e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 138.65 E-value: 7.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENlaVSLPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDE 92
Cdd:COG2884 1 MIRFEN--VSKRYPGGRE-ALSDVSLEIEKGEFVFLTGPSGAGKS----TLLKLLYGEERPTSGQVLVNGQDLSRLKRRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRgAKMAMVFQEP-----MTALNPVMtcgdqmdeL-LRAHvPMGPYERRIRILDLFEEVRLPDppRIfRSYPHQLSG 166
Cdd:COG2884 74 IPYLR-RRIGVVFQDFrllpdRTVYENVA--------LpLRVT-GKSRKEIRRRVREVLDLVGLSD--KA-KALPHELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 167 GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQkKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:COG2884 141 GEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGR 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
285-519 |
1.12e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 140.63 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlGGFftgrvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:COG4152 2 LELKGLTKRF--GDK-------TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LhGlrrrlqvvfqdpY----RSLDPRMTVGESIVegpvnF-----GVPKEEAWKRAQEFMKIVRLsPDALNRYPNQFSGG 435
Cdd:COG4152 73 I-G------------YlpeeRGLYPKMKVGEQLV-----YlarlkGLSKAEAKRRADEWLERLGL-GDRANKKVEELSKG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 436 QRQRISIARALACEPEILICDEAVSALDvSVQADILK-LLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLD-PVNVELLKdVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
....*
gi 2486247945 515 HVQDV 519
Cdd:COG4152 212 SVDEI 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
281-519 |
1.20e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.16 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVVKTYtlGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVA-A 359
Cdd:COG1129 1 AEPLLEMRGISKSF--GG-------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 360 APKrklHGLRRRLQVVFQDPyrSLDPRMTVGESIVEG--PVNFG-VPKEEAWKRAQEFMKIV--RLSPDALNRypnQFSG 434
Cdd:COG1129 72 SPR---DAQAAGIAIIHQEL--NLVPNLSVAENIFLGrePRRGGlIDWRAMRRRARELLARLglDIDPDTPVG---DLSV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 435 GQRQRISIARALACEPEILICDEAVSALDVSvQADIL-KLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVES 513
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTER-EVERLfRIIRRLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGT 221
|
....*.
gi 2486247945 514 GHVQDV 519
Cdd:COG1129 222 GPVAEL 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
266-518 |
1.97e-37 |
|
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: 145.67 E-value: 1.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 266 AVPELKPRHRPPVDGNPTLLEAKNVVKTYTLGGFftgrvkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDP 345
Cdd:COG4988 318 PEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRP--------ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 346 TSGEVWVNGENVAAAPkrkLHGLRRRLQVVFQDPYrsLdPRMTVGESIVegpvnFGVPK------EEAWKRAQ--EFmki 417
Cdd:COG4988 390 YSGSILINGVDLSDLD---PASWRRQIAWVPQNPY--L-FAGTIRENLR-----LGRPDasdeelEAALEAAGldEF--- 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 418 VRLSPDALN-------RypnQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEiqvkLGIG--ILFV 488
Cdd:COG4988 456 VAALPDGLDtplgeggR---GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRR----LAKGrtVILI 528
|
250 260 270
....*....|....*....|....*....|
gi 2486247945 489 THDLRVASQiCDDVIVIRRGECVESGHVQD 518
Cdd:COG4988 529 THRLALLAQ-ADRILVLDDGRIVEQGTHEE 557
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
14-241 |
2.76e-37 |
|
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: 135.78 E-value: 2.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfRRTPDEI 93
Cdd:cd03229 1 LELKNVSKRY---GQKT-VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEE----PDSGSILIDGEDL-TDLEDEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRgAKMAMVFQEPmtALNPVMTcgdqmdellrahvpmgpyerririldLFEEVRLPdpprifrsyphqLSGGQRQRIV 173
Cdd:cd03229 72 PPLR-RRIGMVFQDF--ALFPHLT--------------------------VLENIALG------------LSGGQQQRVA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:cd03229 111 LARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
324-532 |
3.34e-37 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 140.32 E-value: 3.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 324 IVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRklhglRRRLQVVFQDpyRSLDPRMTVGESIVEGPVNFGVP 403
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-----LRHINMVFQS--YALFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 404 KEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGI 483
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFA-DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2486247945 484 GILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLI 532
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
14-241 |
3.62e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.48 E-value: 3.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:COG4619 1 LELEGLSFRV----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP----PTSGEIYLDGKPLSAMPPPEW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPmtalnpvmtcgDQMDELLRAHVPMgPYERRI------RILDLFEEVRLPdpPRIFRSYPHQLSGG 167
Cdd:COG4619 73 RR----QVAYVPQEP-----------ALWGGTVRDNLPF-PFQLRErkfdreRALELLERLGLP--PDILDKPVERLSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:COG4619 135 ERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
282-508 |
3.63e-37 |
|
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: 137.18 E-value: 3.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 282 PTLLEAKNVVKTYTL---GGfftgrVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGE--- 355
Cdd:COG4778 2 TTLLEVENLSKTFTLhlqGG-----KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggw 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 356 -NVAAAPKRKLHGLRRR--------LQVVfqdpyrsldPRMT----VGESIVEGpvnfGVPKEEAWKRAQEFMKIVRLsP 422
Cdd:COG4778 77 vDLAQASPREILALRRRtigyvsqfLRVI---------PRVSaldvVAEPLLER----GVDREEARARARELLARLNL-P 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 423 DAL-NRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDD 501
Cdd:COG4778 143 ERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADR 221
|
....*..
gi 2486247945 502 VIVIRRG 508
Cdd:COG4778 222 VVDVTPF 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
32-272 |
6.54e-37 |
|
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: 137.77 E-value: 6.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIRRLRGAKMAMVFQEpmTA 111
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIE----PTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQS--FA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQMD---ELlrAHVPmgPYERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICD 188
Cdd:cd03294 113 LLPHRTVLENVAfglEV--QGVP--RAEREERAAEALELVGLEG---WEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 189 EPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLINAVP 268
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
....
gi 2486247945 269 ELKP 272
Cdd:cd03294 266 RAKV 269
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
285-524 |
8.29e-37 |
|
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: 136.41 E-value: 8.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlGGFftgrvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAP--K 362
Cdd:cd03219 1 LEVRGLTKRF--GGL-------VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPphE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 363 RKLHGLRRrlqvVFQDPyrSLDPRMTVGESIV--------EGPVNFGVPKEE--AWKRAQEFMKIVRLSPDAlNRYPNQF 432
Cdd:cd03219 72 IARLGIGR----TFQIP--RLFPELTVLENVMvaaqartgSGLLLARARREEreARERAEELLERVGLADLA-DRPAGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 433 SGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECVE 512
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIA 223
|
250
....*....|..
gi 2486247945 513 SGHVQDVFFHPQ 524
Cdd:cd03219 224 EGTPDEVRNNPR 235
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
27-266 |
8.35e-37 |
|
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: 136.66 E-value: 8.35e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 27 GDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRRlrgaKMAMVFQ 106
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKT----TTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR----KIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 107 EpmTALNPVMTCGDQMdellrAHVPM----GPYERRIRILDLFEEVRLPdPPRIFRSYPHQLSGGQRQRIVIAMALLLKP 182
Cdd:cd03295 83 Q--IGLFPHMTVEENI-----ALVPKllkwPKEKIRERADELLALVGLD-PAEFADRYPHELSGGQQQRVGVARALAADP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 183 DLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQK 262
Cdd:cd03295 155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....
gi 2486247945 263 LINA 266
Cdd:cd03295 235 FVGA 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-509 |
8.78e-37 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 142.76 E-value: 8.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGlaPADGSVKLLGMDLFRRTpdeIRRLRGAKMAMVFQEPMta 111
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHG--TYEGEIIFEGEELQASN---IRDTERAGIAIIHQELA-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQM---DELLRAHVpMGPYERRIRILDLFEEVRLPDPPRIFRSyphQLSGGQRQRIVIAMALLLKPDLLICD 188
Cdd:PRK13549 93 LVKELSVLENIflgNEITPGGI-MDYDAMYLRAQKLLAQLKLDINPATPVG---NLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 189 EPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQhpKEPYTQKLINAVP 268
Cdd:PRK13549 169 EPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTE--DDIITMMVGRELT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 269 ELKPRHrpPVDGNPTLLEAKNVVKTYTLGgffTGRVKVralKGVSARLRRGETIGIVGESGSGKSTFARSI-----ARli 343
Cdd:PRK13549 246 ALYPRE--PHTIGEVILEVRNLTAWDPVN---PHIKRV---DDVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGR-- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 344 dpTSGEVWVNGENVAAapKRKLHGLRRRLQVVFQDPYR-SLDPRMTVGESI----VEGPVNFGVPKEEA-WKRAQEFMKI 417
Cdd:PRK13549 316 --WEGEIFIDGKPVKI--RNPQQAIAQGIAMVPEDRKRdGIVPVMGVGKNItlaaLDRFTGGSRIDDAAeLKTILESIQR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 418 VRL---SPD-ALNRypnqFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLR 493
Cdd:PRK13549 392 LKVktaSPElAIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL-VQQGVAIIVISSELP 466
|
490
....*....|....*.
gi 2486247945 494 VASQICDDVIVIRRGE 509
Cdd:PRK13549 467 EVLGLSDRVLVMHEGK 482
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
276-532 |
9.69e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 137.09 E-value: 9.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 276 PPVDGNPTLLEAKNVvktytlgGFFTGrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLID--P---TSGEV 350
Cdd:COG1117 3 APASTLEPKIEVRNL-------NVYYG--DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 351 WVNGENVAAaPKRKLHGLRRRLQVVFQDPyrslDP-RMTVGESIVegpvnFGvPKEEAWKRAQEFMKIVRLS-------- 421
Cdd:COG1117 74 LLDGEDIYD-PDVDVVELRRRVGMVFQKP----NPfPKSIYDNVA-----YG-LRLHGIKSKSELDEIVEESlrkaalwd 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 422 --PDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALD-VSVQAdILKLLEEIQVKLGIGIlfVTHDLRVASQI 498
Cdd:COG1117 143 evKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDYTIVI--VTHNMQQAARV 219
|
250 260 270
....*....|....*....|....*....|....
gi 2486247945 499 CDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLI 532
Cdd:COG1117 220 SDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
12-241 |
1.60e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.95 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPpgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPD 91
Cdd:COG3638 1 PMLELRNLSKRYP--GGTP-ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE----PTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRgAKMAMVFQEP-----MTALNPVMTcG--DQMDeLLRAHVPMGPYERRIRILDLFEEVRLPDppRIFRSyPHQL 164
Cdd:COG3638 74 ALRRLR-RRIGMIFQQFnlvprLSVLTNVLA-GrlGRTS-TWRSLLGLFPPEDRERALEALERVGLAD--KAYQR-ADQL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 165 SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGR 224
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
31-286 |
1.67e-36 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 136.81 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 31 NAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDEIRRLRgAKMAMVFQEP-- 108
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLL----KPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQFPeh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 109 ----MTALNPVMtcgdqmdellrahvpMGP-------YERRIRILDLFEEVRLPDPprIF-RSyPHQLSGGQRQRIVIAM 176
Cdd:TIGR04521 94 qlfeETVYKDIA---------------FGPknlglseEEAEERVKEALELVGLDEE--YLeRS-PFELSGGQMRRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 177 ALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPK 256
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 2486247945 257 EPYTQKLinAVPE-------LKPRHrPPVDGNPTLLE 286
Cdd:TIGR04521 236 ELEKIGL--DVPEitelarkLKEKG-LPVPKDPLTVE 269
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
12-267 |
1.96e-36 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 136.11 E-value: 1.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGgdrpNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKL-----LGMDLF 86
Cdd:TIGR02323 2 PLLQVSGLSKSYGGG----KGCRDVSFDLYPGEVLGIVGESGSGKS----TLLGCLAGRLAPDHGTATYimrsgAELELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 87 RRTPDEIRRLRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAhVPMGPYER-RIRILDLFEEVRLpDPPRIfRSYPHQLS 165
Cdd:TIGR02323 74 QLSEAERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGERLMA-IGARHYGNiRATAQDWLEEVEI-DPTRI-DDLPRAFS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIET 245
Cdd:TIGR02323 151 GGMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVES 230
|
250 260
....*....|....*....|..
gi 2486247945 246 GPAKSVLQHPKEPYTQKLINAV 267
Cdd:TIGR02323 231 GLTDQVLDDPQHPYTQLLVSSI 252
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-263 |
2.07e-36 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 136.68 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPpGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPD 91
Cdd:PRK13635 4 EIIRVEHISFRYP-DAATY-ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLL----LPEAGTITVGGMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRlrgaKMAMVFQEP------MTALNPVM----TCGDQMDELLRahvpmgpyerriRILDLFEEVRLPDppriFRSY- 160
Cdd:PRK13635 78 DVRR----QVGMVFQNPdnqfvgATVQDDVAfgleNIGVPREEMVE------------RVDQALRQVGMED----FLNRe 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 161 PHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEiADQVVVLELG 240
Cdd:PRK13635 138 PHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKG 216
|
250 260 270
....*....|....*....|....*....|.
gi 2486247945 241 KQIETGPAKSVLQHPKE--------PYTQKL 263
Cdd:PRK13635 217 EILEEGTPEEIFKSGHMlqeigldvPFSVKL 247
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-253 |
2.07e-36 |
|
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: 135.76 E-value: 2.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLfRRTPDE 92
Cdd:COG4555 1 MIEVENLSKKY---GKVP-ALKDVSFTAKDGEITGLLGPNGAGKT----TLLRMLAGLLKPDSGSILIDGEDV-RKEPRE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRlrgaKMAMVFQEPMtaLNPVMTCGDQMDELLRAHvPMGPYERRIRILDLFEEVRLPDPPRifRSYpHQLSGGQRQRI 172
Cdd:COG4555 72 ARR----QIGVLPDERG--LYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLD--RRV-GELSTGMKKKV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVL 252
Cdd:COG4555 142 ALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
.
gi 2486247945 253 Q 253
Cdd:COG4555 221 E 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-509 |
2.15e-36 |
|
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: 141.89 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGlaPADGSVKLLGMDLFRRTpdeIRRLRGAKMAMVFQEPMta 111
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG--TWDGEIYWSGSPLKASN---IRDTERAGIVIIHQELT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQM---DELLRAHVPMGPYERRIRILDLFEEVRLPDPPRifrSYP-HQLSGGQRQRIVIAMALLLKPDLLIC 187
Cdd:TIGR02633 89 LVPELSVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQLDADNV---TRPvGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 188 DEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQhpKEPYTQKLINAV 267
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSE--DDIITMMVGREI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 268 PELKPRHrpPVDGNPTLLEAKNVVKTYTLggfftgRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSI-ARLIDPT 346
Cdd:TIGR02633 243 TSLYPHE--PHEIGDVILEARNLTCWDVI------NPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 347 SGEVWVNGENVAAapKRKLHGLRRRLQVVFQDPYR-SLDPRMTVGESIVEGPVNF--------GVPKEEAWKRAQEFMKI 417
Cdd:TIGR02633 315 EGNVFINGKPVDI--RNPAQAIRAGIAMVPEDRKRhGIVPILGVGKNITLSVLKSfcfkmridAAAELQIIGSAIQRLKV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 418 VRLSPD-ALNRypnqFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVAS 496
Cdd:TIGR02633 393 KTASPFlPIGR----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL-AQEGVAIIVVSSELAEVL 467
|
490
....*....|...
gi 2486247945 497 QICDDVIVIRRGE 509
Cdd:TIGR02633 468 GLSDRVLVIGEGK 480
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
281-532 |
3.31e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 138.54 E-value: 3.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVVKTYtlGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAA 360
Cdd:PRK09452 11 LSPLVELRGISKSF--DG-------KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 PKRKlhglrRRLQVVFQDpYrSLDPRMTVGESivegpVNFG-----VPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGG 435
Cdd:PRK09452 82 PAEN-----RHVNTVFQS-Y-ALFPHMTVFEN-----VAFGlrmqkTPAAEITPRVMEALRMVQLEEFA-QRKPHQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 436 QRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGH 515
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
250
....*....|....*..
gi 2486247945 516 VQDVFFHPQHEYTKSLI 532
Cdd:PRK09452 229 PREIYEEPKNLFVARFI 245
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
288-520 |
4.00e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 136.03 E-value: 4.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 288 KNVVKTYTLGGFFTGRvkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK-LH 366
Cdd:PRK13649 6 QNVSYTYQAGTPFEGR----ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 367 GLRRRLQVVFQDPYRSLDPRmTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARAL 446
Cdd:PRK13649 82 QIRKKVGLVFQFPESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 447 ACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
14-251 |
7.40e-36 |
|
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: 133.46 E-value: 7.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSlpPGGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPK-GLAPADGSVKLLGMDLF--RRTP 90
Cdd:cd03260 1 IELRDLNVY--YGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLiPGAPDEGEVLLDGKDIYdlDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRlrgaKMAMVFQEPmtalNPV-MTCGDQMDELLRAH--VPMGPYERRI----RILDLFEEVRLpdpprifRSYPHQ 163
Cdd:cd03260 77 LELRR----RVGMVFQKP----NPFpGSIYDNVAYGLRLHgiKLKEELDERVeealRKAALWDEVKD-------RLHALG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKngTAVLFITHDFGVVSEIADQVVVLELGKQI 243
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
|
....*...
gi 2486247945 244 ETGPAKSV 251
Cdd:cd03260 220 EFGPTEQI 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
285-511 |
7.62e-36 |
|
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: 131.40 E-value: 7.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVA-AAPKr 363
Cdd:cd03216 1 LELRGITKRF--GG-------VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPR- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 klHGLRRRLQVVFQdpyrsldprmtvgesivegpvnfgvpkeeawkraqefmkivrlspdalnrypnqFSGGQRQRISIA 443
Cdd:cd03216 71 --DARRAGIAMVYQ------------------------------------------------------LSVGERQMVEIA 94
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 444 RALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECV 511
Cdd:cd03216 95 RALARNARLLILDEPTAALTPAEVERLFKVIRRLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-254 |
7.98e-36 |
|
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: 142.28 E-value: 7.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENlaVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:COG2274 474 IELEN--VSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE----PTSGRILIDGIDLRQIDPASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPM----------TALNPVMTcgdqMDELLRAhvpmgpyerrIRILDLFEEV-RLPDpprifrSYPH 162
Cdd:COG2274 548 RR----QIGVVLQDVFlfsgtireniTLGDPDAT----DEEIIEA----------ARLAGLHDFIeALPM------GYDT 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 Q-------LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqkKNGTAVLFITHDFGVVsEIADQVV 235
Cdd:COG2274 604 VvgeggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTI-RLADRII 680
|
250
....*....|....*....
gi 2486247945 236 VLELGKQIETGPAKSVLQH 254
Cdd:COG2274 681 VLDKGRIVEDGTHEELLAR 699
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
284-520 |
9.57e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 134.84 E-value: 9.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTlggfftGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAapkR 363
Cdd:PRK13642 4 ILEVENLVFKYE------KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---E 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGLRRRLQVVFQDPYRSLdPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIA 443
Cdd:PRK13642 75 NVWNLRRKIGMVFQNPDNQF-VGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 444 RALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQiCDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-241 |
1.19e-35 |
|
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: 130.97 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGdrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03228 1 IEFKNVSFSYPGRP--KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD----PTSGEILIDGVDLRDLDLESL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPMtalnpvmtcgdqmdellrahvpmgpyerririldLF-----EEVrlpdpprifrsyphqLSGGQ 168
Cdd:cd03228 75 RK----NIAYVPQDPF----------------------------------LFsgtirENI---------------LSGGQ 101
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 169 RQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVsEIADQVVVLELGK 241
Cdd:cd03228 102 RQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTI-RDADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
33-192 |
1.57e-35 |
|
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: 130.08 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 33 VEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfrrtPDEIRRLRGAKMAMVFQEPmtAL 112
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS----PTEGTILLDGQDL----TDDERKSLRKEIGYVFQDP--QL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 113 NPVMTCGDQMDELLRAHVPMGPYERRiRILDLFEEVRLPD-PPRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPT 191
Cdd:pfam00005 71 FPRLTVRENLRLGLLLKGLSKREKDA-RAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
.
gi 2486247945 192 T 192
Cdd:pfam00005 150 A 150
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
309-517 |
2.02e-35 |
|
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: 132.74 E-value: 2.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapKRKLHGLRRRLQVVFQDPYRSLDprmT 388
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIR---EVTLDSLRRAIGVVPQDTVLFND---T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 VGESIVEGpvNFGVPKEE---AWKRAQEFMKIVRLsPDAlnrYPNQ-------FSGGQRQRISIARALACEPEILICDEA 458
Cdd:cd03253 91 IGYNIRYG--RPDATDEEvieAAKAAQIHDKIMRF-PDG---YDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 459 VSALDVSVQADILKLLEEIQVklGIGILFVTHDLRVASQiCDDVIVIRRGECVESG-HVQ 517
Cdd:cd03253 165 TSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGtHEE 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
14-251 |
2.35e-35 |
|
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: 132.69 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGdrpNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE----PTSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRgAKMAMVFQ-----EPMTALNPVMtCG--DQMDeLLRAHVPMGPYERRIRILDLFEEVRLPDPPRIFRSyphQLSG 166
Cdd:cd03256 74 RQLR-RQIGMIFQqfnliERLSVLENVL-SGrlGRRS-TWRSLFGLFPKEEKQRALAALERVGLLDKAYQRAD---QLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 167 GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDG 227
|
....*
gi 2486247945 247 PAKSV 251
Cdd:cd03256 228 PPAEL 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-241 |
2.42e-35 |
|
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: 129.67 E-value: 2.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 15 EVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIR 94
Cdd:cd00267 1 EIENLSFRY---GGRT-ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK----PTSGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 95 RlrgaKMAMVFQepmtalnpvmtcgdqmdellrahvpmgpyerririldlfeevrlpdpprifrsyphqLSGGQRQRIVI 174
Cdd:cd00267 73 R----RIGYVPQ---------------------------------------------------------LSGGQRQRVAL 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 175 AMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:cd00267 92 ARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
300-523 |
2.90e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 135.60 E-value: 2.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 300 FTGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapkrKLHGLRRRLQVVFQdp 379
Cdd:PRK10851 11 SFGRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS-----RLHARDRKVGFVFQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 380 YRSLDPRMTVGESIVegpvnFGV---PKEE------AWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISIARALACEP 450
Cdd:PRK10851 82 HYALFRHMTVFDNIA-----FGLtvlPRRErpnaaaIKAKVTQLLEMVQLAHLA-DRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 451 EILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHP 523
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
282-536 |
3.63e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 134.59 E-value: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 282 PTLLEAKNVVKTYTLGGFFTGRV--KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWV----NGE 355
Cdd:PRK13631 13 PNPLSDDIILRVKNLYCVFDEKQenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 356 NVAAAPKRKLHG---------LRRRLQVVFQDPYRSLDpRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALN 426
Cdd:PRK13631 93 KKNNHELITNPYskkiknfkeLRRRVSMVFQFPEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 427 RYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIR 506
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMD 250
|
250 260 270
....*....|....*....|....*....|
gi 2486247945 507 RGECVESGHVQDVFFHpQHEYTKSLIAAAP 536
Cdd:PRK13631 251 KGKILKTGTPYEIFTD-QHIINSTSIQVPR 279
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
288-520 |
3.95e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 133.37 E-value: 3.95e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 288 KNVVKTYTLGGFFtgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK-LH 366
Cdd:PRK13646 6 DNVSYTYQKGTPY----EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 367 GLRRRLQVVFQDPYRSL--DprmTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIAR 444
Cdd:PRK13646 82 PVRKRIGMVFQFPESQLfeD---TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
283-520 |
4.24e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 133.43 E-value: 4.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 283 TLLEAKNVVKTYTLGgfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPK 362
Cdd:PRK13636 4 YILKVEELNYNYSDG--------THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 363 rKLHGLRRRLQVVFQDPYRSLDpRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPdaLNRYPNQ-FSGGQRQRIS 441
Cdd:PRK13636 76 -GLMKLRESVGMVFQDPDNQLF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH--LKDKPTHcLSFGQKKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 442 IARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
284-531 |
6.33e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 132.52 E-value: 6.33e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTLGGFFTGRVkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVngENVAAAPKR 363
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEKL---ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYV--DGLDTSDEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGLRRRLQVVFQDPYRSLDPRMtVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpdALNRY-PNQFSGGQRQRISI 442
Cdd:PRK13633 79 NLWDIRNKAGMVFQNPDNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMY--EYRRHaPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 443 ARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQiCDDVIVIRRGECVESGHVQDVFfh 522
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF-- 232
|
....*....
gi 2486247945 523 PQHEYTKSL 531
Cdd:PRK13633 233 KEVEMMKKI 241
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
316-520 |
8.27e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 131.03 E-value: 8.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 316 LRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKlhglrRRLQVVFQDpyRSLDPRMTVGESIve 395
Cdd:COG3840 22 IAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-----RPVSMLFQE--NNLFPHLTVAQNI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 396 gpvNFGV-PK----EEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADI 470
Cdd:COG3840 93 ---GLGLrPGlkltAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2486247945 471 LKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:COG3840 169 LDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALL 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
308-531 |
1.51e-34 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 134.78 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHGLRRR-LQVVFQDpyRSLDPR 386
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 MTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSV 466
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYA-HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 467 QADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSL 531
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
36-241 |
1.83e-34 |
|
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: 129.19 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDeIRRLRgAKMAMVFQ-----EPMT 110
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEE----PDSGTIIIDGLKLTDDKKN-INELR-QKVGMVFQqfnlfPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALNPVMtcgdqmdELLRAHVPMGPYERRIRILDLFEEVRLPDppRIfRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEP 190
Cdd:cd03262 93 VLENIT-------LAPIKVKGMSKAEAEERALELLEKVGLAD--KA-DAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 191 TTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:cd03262 163 TSALDPELVGEVLDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
307-526 |
1.85e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 131.78 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK-LHGLRRRLQVVFQDPYRSLDP 385
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIKPVRKKVGVVFQFPESQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 386 RmTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVS 465
Cdd:PRK13643 100 E-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 466 VQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF----FHPQHE 526
Cdd:PRK13643 179 ARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFqevdFLKAHE 242
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
14-253 |
2.28e-34 |
|
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: 129.48 E-value: 2.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVslppGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03224 1 LEVENLNA----GYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRDITGLPPHER 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlRGakMAMVFQEPMtaLNPVMTCGD--QMDELLRAHvpmGPYERRI-RILDLFeevrlpdpPRI--FRSYP-HQLSGG 167
Cdd:cd03224 73 AR-AG--IGYVPEGRR--IFPELTVEEnlLLGAYARRR---AKRKARLeRVYELF--------PRLkeRRKQLaGTLSGG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQIETGP 247
Cdd:cd03224 137 EQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
|
....*.
gi 2486247945 248 AKSVLQ 253
Cdd:cd03224 216 AAELLA 221
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
284-523 |
3.54e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 130.69 E-value: 3.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYtlggfftgRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapKR 363
Cdd:PRK13652 3 LIETRDLCYSY--------SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGLRRRLQVVFQDPyrslDPRM---TVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRI 440
Cdd:PRK13652 72 NIREVRKFVGLVFQNP----DDQIfspTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 441 SIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13652 147 AIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIF 226
|
...
gi 2486247945 521 FHP 523
Cdd:PRK13652 227 LQP 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
263-514 |
4.43e-34 |
|
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: 136.05 E-value: 4.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 263 LINAVPELKPRHRPPVDGNPTLLEAKNVVKTYTLGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARL 342
Cdd:COG4987 312 LLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAG-------RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 343 IDPTSGEVWVNGENVAAAPKRklhGLRRRLQVVFQDPYrsL-DprMTVGEsivegpvN--FGVPK---EEAWkraqEFMK 416
Cdd:COG4987 385 LDPQSGSITLGGVDLRDLDED---DLRRRIAVVPQRPH--LfD--TTLRE-------NlrLARPDatdEELW----AALE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 417 IVRLSpDALNRYPN-----------QFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVklGIGI 485
Cdd:COG4987 447 RVGLG-DWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTV 523
|
250 260
....*....|....*....|....*....
gi 2486247945 486 LFVTHDLRVASQiCDDVIVIRRGECVESG 514
Cdd:COG4987 524 LLITHRLAGLER-MDRILVLEDGRIVEQG 551
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
32-256 |
6.90e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 128.59 E-value: 6.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIAStVMGLLPkglAPADGSVKLLGMDL-FRRTPDE--IRRLRGaKMAMVFQEp 108
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLE---TPDSGQLNIAGHQFdFSQKPSEkaIRLLRQ-KVGMVFQQ- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 109 mTALNPVMTCgdqMDELLRAHVP---MGPYERRIRILDLFEEVRLPDppriFR-SYPHQLSGGQRQRIVIAMALLLKPDL 184
Cdd:COG4161 91 -YNLWPHLTV---MENLIEAPCKvlgLSKEQAREKAMKLLARLRLTD----KAdRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 185 LICDEPTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVSEIADQVVVLELGKQIETGPAkSVLQHPK 256
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQ 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
15-243 |
7.47e-34 |
|
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: 127.37 E-value: 7.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 15 EVENLAVSLPPGgdrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRtpdeiR 94
Cdd:cd03226 1 RIENISFSYKKG---TEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLI----KESSGSILLNGKPIKAK-----E 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 95 RLRgaKMAMVFQEPmtalnpvmtcGDQM------DELLRAHVPMGPYERRIR-ILDLFEEVRLPDpprifrSYPHQLSGG 167
Cdd:cd03226 69 RRK--SIGYVMQDV----------DYQLftdsvrEELLLGLKELDAGNEQAEtVLKDLDLYALKE------RHPLSLSGG 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQI 243
Cdd:cd03226 131 QKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
279-524 |
2.35e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.95 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 279 DGNPTLLEAKNVVKTYTLGGFFTgrvkvraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVA 358
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSDASFT-------LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 359 AAPKRKLhglRRRLQVVFQDPYRSLdprmtVGeSIVEGPVNFG-----VPKEEAWKRAQEFMKIVRLSpDALNRYPNQFS 433
Cdd:PRK13648 75 DDNFEKL---RKHIGIVFQNPDNQF-----VG-SIVKYDVAFGlenhaVPYDEMHRRVSEALKQVDML-ERADYEPNALS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 434 GGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQiCDDVIVIRRGECVES 513
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKE 223
|
250
....*....|.
gi 2486247945 514 GHVQDVFFHPQ 524
Cdd:PRK13648 224 GTPTEIFDHAE 234
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-257 |
4.77e-33 |
|
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: 126.30 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppggdRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEi 93
Cdd:cd03299 1 LKVENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIK----PDSGKILLNGKDITNLPPEK- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 rrlRGakMAMVFQEpmTALNPVMTCGDQMDELLRAHVPMGPyERRIRILDLFEEVRLPdppRIFRSYPHQLSGGQRQRIV 173
Cdd:cd03299 71 ---RD--ISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKK-EIERKVLEIAEMLGID---HLLNRKPETLSGGEQQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQ 253
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
....
gi 2486247945 254 HPKE 257
Cdd:cd03299 220 KPKN 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
300-509 |
5.09e-33 |
|
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: 125.06 E-value: 5.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 300 FTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHGLrrrlqvVFQDP 379
Cdd:cd03226 7 FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGY------VMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 380 YRSLDpRMTVGESIVEGPVNFGVPKEeawkRAQEFMKivRLSPDAL-NRYPNQFSGGQRQRISIARALACEPEILICDEA 458
Cdd:cd03226 81 DYQLF-TDSVREELLLGLKELDAGNE----QAETVLK--DLDLYALkERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 459 VSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd03226 154 TSGLDYKNMERVGELIRELA-AQGKAVIVITHDYEFLAKVCDRVLLLANGA 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
303-514 |
5.34e-33 |
|
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: 126.11 E-value: 5.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 303 RVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVaaapkRKL--HGLRRRLQVVFQDPy 380
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-----RDLnlRWLRSQIGLVSQEP- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 381 rSLDPrMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALN----RYPNQFSGGQRQRISIARALACEPEILICD 456
Cdd:cd03249 87 -VLFD-GTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 457 EAVSALDVSVQADILKLLEeiQVKLGIGILFVTHDLrvaSQI--CDDVIVIRRGECVESG 514
Cdd:cd03249 165 EATSALDAESEKLVQEALD--RAMKGRTTIVIAHRL---STIrnADLIAVLQNGQVVEQG 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
309-513 |
5.43e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 127.16 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAapkRKLHGLRRRLQVVFQDPyrslDPRM- 387
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE---ENVWDIRHKIGMVFQNP----DNQFv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 --TVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVS 465
Cdd:PRK13650 96 gaTVEDDVAFGLENKGIPHEEMKERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2486247945 466 VQADILKLLEEIQVKLGIGILFVTHDL-RVAsqICDDVIVIRRGEcVES 513
Cdd:PRK13650 175 GRLELIKTIKGIRDDYQMTVISITHDLdEVA--LSDRVLVMKNGQ-VES 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
10-272 |
5.47e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.03 E-value: 5.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 10 KLPVLEVENLAVSLPPggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRT 89
Cdd:PRK13632 4 KSVMIKVENVSFSYPN--SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLL----KPQSGEIKIDGITISKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 90 PDEIRRlrgaKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPmgPYERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQR 169
Cdd:PRK13632 78 LKEIRK----KIGIIFQNPDNQFIGATVEDDIAFGLENKKVP--PKKMKDIIDDLAKKVGMED---YLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 170 QRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfgvVSEI--ADQVVVLELGKQIETGP 247
Cdd:PRK13632 149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHD---MDEAilADKVIVFSEGKLIAQGK 225
|
250 260 270
....*....|....*....|....*....|...
gi 2486247945 248 AKSVLQHPKE--------PYTQKLINAVPELKP 272
Cdd:PRK13632 226 PKEILNNKEIlekakidsPFIYKLSKKLKGIDP 258
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
13-254 |
5.49e-33 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 126.26 E-value: 5.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGgdrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDE 92
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLV----EPSSGSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRgAKMAMVFQE-----PMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPDpprifrsYPH----Q 163
Cdd:TIGR02315 74 LRKLR-RRIGMIFQHynlieRLTVLENVLHGRLGYKPTWRSLLGRFSEEDKERALSALERVGLAD-------KAYqradQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQI 243
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIV 225
|
250
....*....|.
gi 2486247945 244 ETGPAKSVLQH 254
Cdd:TIGR02315 226 FDGAPSELDDE 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
285-514 |
6.32e-33 |
|
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: 125.24 E-value: 6.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03224 1 LEVENLNAGYG---------KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LhgLRRRLQVVFQDpyRSLDPRMTVGESIVEGpVNFGVPKEEAWKRAqefmKIVRLSP---DALNRYPNQFSGGQRQRIS 441
Cdd:cd03224 72 R--ARAGIGYVPEG--RRIFPELTVEENLLLG-AYARRRAKRKARLE----RVYELFPrlkERRKQLAGTLSGGEQQMLA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 442 IARALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03224 143 IARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELR-DEGVTILLVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
14-264 |
7.38e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.73 E-value: 7.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKS----VIAstvmgllpkGLAPAD-GSVKLLGMDLFRR 88
Cdd:COG1118 3 IEVRNISKRF---GSFT-LLDDVSLEIASGELVALLGPSGSGKTtllrIIA---------GLETPDsGRIVLNGRDLFTN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 89 TPdeIRRLRgakMAMVFQEPmtALNPVMT------CGdqmdelLRaHVPMGPYERRIRILDLFEEVRLPDpprIFRSYPH 162
Cdd:COG1118 70 LP--PRERR---VGFVFQHY--ALFPHMTvaeniaFG------LR-VRPPSKAEIRARVEELLELVQLEG---LADRYPS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQ 242
Cdd:COG1118 133 QLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
250 260
....*....|....*....|..
gi 2486247945 243 IETGPAKSVLQHPKEPYTQKLI 264
Cdd:COG1118 213 EQVGTPDEVYDRPATPFVARFL 234
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
282-519 |
8.14e-33 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 125.58 E-value: 8.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 282 PTLLEAKNVVKTYTLGGFFTGRVK-------------VRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSG 348
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSRSLKelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 349 EVWVNGEnVAAapkrkLHGlrrrLQVVFqdpyrslDPRMTVGESIVegpVN---FGVPKEEAWKRAQEfmkIVRLSpdAL 425
Cdd:COG1134 82 RVEVNGR-VSA-----LLE----LGAGF-------HPELTGRENIY---LNgrlLGLSRKEIDEKFDE---IVEFA--EL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 426 NRYPNQ----FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDD 501
Cdd:COG1134 137 GDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDR 215
|
250
....*....|....*...
gi 2486247945 502 VIVIRRGECVESGHVQDV 519
Cdd:COG1134 216 AIWLEKGRLVMDGDPEEV 233
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
281-498 |
8.69e-33 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 125.31 E-value: 8.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVVKTYTlggffTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGE---NV 357
Cdd:PRK11629 2 NKILLQCDNLCKRYQ-----EGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 358 AAAPKRKLHGlrRRLQVVFQdpYRSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALNRyPNQFSGGQR 437
Cdd:PRK11629 77 SSAAKAELRN--QKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGER 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 438 QRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQI 498
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
285-514 |
1.18e-32 |
|
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: 124.32 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlggfftGRVkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03269 1 LEVENVTKRF-------GRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRlqvvfqdpyRSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIAR 444
Cdd:cd03269 72 IGYLPEE---------RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 445 ALACEPEILICDEAVSALDVsVQADILK-LLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDP-VNVELLKdVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
27-287 |
1.55e-32 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 126.74 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 27 GDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRRlrgaKMAMVFQ 106
Cdd:COG1125 12 PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKT----TTLRMINRLIEPTSGRILIDGEDIRDLDPVELRR----RIGYVIQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 107 EpmTALNPVMTCGDQMdellrAHVP--MGPYERRI--RILDLFEEVRLPdpPRIFRS-YPHQLSGGQRQRIVIAMALLLK 181
Cdd:COG1125 84 Q--IGLFPHMTVAENI-----ATVPrlLGWDKERIraRVDELLELVGLD--PEEYRDrYPHELSGGQQQRVGVARALAAD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 182 PDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfgvVSE---IADQVVVLELGKQIETGPAKSVLQHPKEP 258
Cdd:COG1125 155 PPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHD---IDEalkLGDRIAVMREGRIVQYDTPEEILANPAND 231
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2486247945 259 YTQKLINA-----------VPELKPRHRPPVDGNPTLLEA 287
Cdd:COG1125 232 FVADFVGAdrglrrlsllrVEDLMLPEPPTVSPDASLREA 271
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-265 |
1.63e-32 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 125.15 E-value: 1.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVM-------GLLPKglAPADGSVKLLGMD 84
Cdd:COG1117 10 PKIEVRNLNVYY---GDKQ-ALKDINLDIPENKVTALIGPSGCGKS----TLLrclnrmnDLIPG--ARVEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 85 LFRRT--PDEIRRlrgaKMAMVFQEPmtalNP--------V--------MTCGDQMDELLrahvpmgpyERRIRILDLFE 146
Cdd:COG1117 80 IYDPDvdVVELRR----RVGMVFQKP----NPfpksiydnVayglrlhgIKSKSELDEIV---------EESLRKAALWD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 147 EV--RLPDPPrifrsypHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTaVLFITHDF 224
Cdd:COG1117 143 EVkdRLKKSA-------LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYT-IVIVTHNM 213
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2486247945 225 GVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLIN 265
Cdd:COG1117 214 QQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
13-241 |
1.86e-32 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 123.98 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIAsTVMGLLPKglaPADGSVKLLGMDLFRRTPDE 92
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLL-TLIGGLRS---VQEGSLKVLGQELHGASKKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRgAKMAMVFQ-----EPMTALNPVmtcgdQMDELLRAHvpMGPYERRIRILDLFEEVRLPDppRIfRSYPHQLSGG 167
Cdd:TIGR02982 77 LVQLR-RRIGYIFQahnllGFLTARQNV-----QMALELQPN--LSYQEARERARAMLEAVGLGD--HL-NYYPHNLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfGVVSEIADQVVVLELGK 241
Cdd:TIGR02982 146 QKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGK 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
308-520 |
1.92e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 125.49 E-value: 1.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhglRRRLQVVFQDPyrslDPRM 387
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI---RKKIGIIFQNP----DNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 ---TVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDV 464
Cdd:PRK13632 97 igaTVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 465 SVQADILKLLEEIQVKLGIGILFVTHDLRVASQiCDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13632 176 KGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEIL 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
280-519 |
1.93e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 130.53 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 280 GNPTLLEAKNVVKTYtlGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVA- 358
Cdd:COG3845 1 MMPPALELRGITKRF--GG-------VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRi 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 359 AAPKrklHGLRRRLQVVFQDPyrSLDPRMTVGESIV---EGPVNFGVPKEEAWKRAQEFMKIVRLSPDaLNRYPNQFSGG 435
Cdd:COG3845 72 RSPR---DAIALGIGMVHQHF--MLVPNLTVAENIVlglEPTKGGRLDRKAARARIRELSERYGLDVD-PDAKVEDLSVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 436 QRQRISIARALACEPEILICDEAVSALdvSVQA-----DILKLLeeiqVKLGIGILFVTHDLRVASQICDDVIVIRRGEC 510
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVL--TPQEadelfEILRRL----AAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
....*....
gi 2486247945 511 VESGHVQDV 519
Cdd:COG3845 220 VGTVDTAET 228
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-254 |
2.60e-32 |
|
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: 130.65 E-value: 2.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 3 ESSLRAQKLPVLEVENLAVSLPpggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLG 82
Cdd:COG4988 326 TAPLPAAGPPSIELEDVSFSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP----PYSGSILING 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 83 MDLFRRTPDEIRRLrgakMAMVFQEP----------MTALNPVMTcgdqMDELLRAhvpmgpyerrIRILDLFEEVRlpd 152
Cdd:COG4988 399 VDLSDLDPASWRRQ----IAWVPQNPylfagtirenLRLGRPDAS----DEELEAA----------LEAAGLDEFVA--- 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 153 pprifrSYPH-----------QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFIT 221
Cdd:COG4988 458 ------ALPDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILIT 529
|
250 260 270
....*....|....*....|....*....|...
gi 2486247945 222 HDFGVVsEIADQVVVLELGKQIETGPAKSVLQH 254
Cdd:COG4988 530 HRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
3-255 |
2.69e-32 |
|
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: 130.66 E-value: 2.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 3 ESSLRAQKLPVLEVENLAVSLPpgGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLG 82
Cdd:COG4987 323 AEPAPAPGGPSLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD----PQSGSITLGG 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 83 MDLFRRTPDEIRRLrgakMAMVFQEP----MTAL------NPvmTCGDqmDELLRAhvpmgpyerririldlFEEVRLPD 152
Cdd:COG4987 397 VDLRDLDEDDLRRR----IAVVPQRPhlfdTTLRenlrlaRP--DATD--EELWAA----------------LERVGLGD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 153 pprIFRSYPH-----------QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFIT 221
Cdd:COG4987 453 ---WLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLIT 527
|
250 260 270
....*....|....*....|....*....|....
gi 2486247945 222 HDFGVVsEIADQVVVLELGKQIETGPAKSVLQHP 255
Cdd:COG4987 528 HRLAGL-ERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
265-535 |
3.60e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 127.26 E-value: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 265 NAVPelKPRHRPPVDGNPtLLEAKNVVKTytlggfFTGRvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLID 344
Cdd:PRK11607 3 DAIP--RPQAKTRKALTP-LLEIRNLTKS------FDGQ---HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 345 PTSGEVWVNGENVAAAPKrklhgLRRRLQVVFQDpyRSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDA 424
Cdd:PRK11607 71 PTAGQIMLDGVDLSHVPP-----YQRPINMMFQS--YALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 425 lNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSV----QADILKLLEeiqvKLGIGILFVTHDLRVASQICD 500
Cdd:PRK11607 144 -KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLrdrmQLEVVDILE----RVGVTCVMVTHDQEEAMTMAG 218
|
250 260 270
....*....|....*....|....*....|....*
gi 2486247945 501 DVIVIRRGECVESGHVQDVFFHPQHEYTKSLIAAA 535
Cdd:PRK11607 219 RIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
305-514 |
4.06e-32 |
|
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: 123.49 E-value: 4.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapKRKLHGLRRRLQVVFQDPYrsLD 384
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIR---DISRKSLRSMIGVVLQDTF--LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 385 PRmTVGESIVEGPVNfgvPKEEAWKRAQEFMKI---VRLSPDALNRYPNQ----FSGGQRQRISIARALACEPEILICDE 457
Cdd:cd03254 90 SG-TIMENIRLGRPN---ATDEEVIEAAKEAGAhdfIMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 458 AVSALDVS----VQADILKLLEeiqvklGIGILFVTHDLrvaSQI--CDDVIVIRRGECVESG 514
Cdd:cd03254 166 ATSNIDTEteklIQEALEKLMK------GRTSIIIAHRL---STIknADKILVLDDGKIIEEG 219
|
|
| ABC_MetN |
TIGR02314 |
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ... |
13-266 |
5.74e-32 |
|
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.
Pssm-ID: 131367 [Multi-domain] Cd Length: 343 Bit Score: 126.15 E-value: 5.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVmGLLPKglaPADGSVKLLGMDLFRRTPDE 92
Cdd:TIGR02314 1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLER---PTSGSVIVDGQDLTTLSNSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRgAKMAMVFQEpMTALNPVMTCGDQMDELLRAHVPMGPYERRIRilDLFEEVRLPDPPRifrSYPHQLSGGQRQRI 172
Cdd:TIGR02314 77 LTKAR-RQIGMIFQH-FNLLSSRTVFGNVALPLELDNTPKDEIKRKVT--ELLALVGLGDKHD---SYPSNLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVL 252
Cdd:TIGR02314 150 AIARALASNPKVLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIF 229
|
250
....*....|....
gi 2486247945 253 QHPKEPYTQKLINA 266
Cdd:TIGR02314 230 SHPKTPLAQKFIRS 243
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
302-532 |
6.33e-32 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 123.48 E-value: 6.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 302 GRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLID-----PTSGEVWVNGENVAaapKRKLHGLRRRLQVVF 376
Cdd:PRK14247 14 GQVEV--LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIF---KMDVIELRRRVQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 377 QDPyrSLDPRMTVGESIVEGP-VNFGV-PKEEAWKRAQEFMKIVRLSPDALNRY---PNQFSGGQRQRISIARALACEPE 451
Cdd:PRK14247 89 QIP--NPIPNLSIFENVALGLkLNRLVkSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 452 ILICDEAVSALDVSVQADILKLLEEIqvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSL 531
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKY 244
|
.
gi 2486247945 532 I 532
Cdd:PRK14247 245 V 245
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-245 |
7.62e-32 |
|
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: 120.23 E-value: 7.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGgdrpNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03216 1 LELRGITKRFGGV----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYK----PDSGEILVDGKEVSFASPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgAKMAMVfqepmtalnpvmtcgdqmdellrahvpmgpyerririldlfeevrlpdpprifrsypHQLSGGQRQRIV 173
Cdd:cd03216 73 RR---AGIAMV---------------------------------------------------------YQLSVGERQMVE 92
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIET 245
Cdd:cd03216 93 IARALARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
25-269 |
7.87e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 124.14 E-value: 7.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 25 PGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLAPaDGSVKLLGMDLFRRTPDEIRRlrgaKMAMV 104
Cdd:PRK13640 16 PDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNP-NSKITVDGITLTAKTVWDIRE----KVGIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 105 FQEPMTALNPVmTCGDQmdellrahVPMG------PYERRIRIL-DLFEEVRLPDpprIFRSYPHQLSGGQRQRIVIAMA 177
Cdd:PRK13640 90 FQNPDNQFVGA-TVGDD--------VAFGlenravPRPEMIKIVrDVLADVGMLD---YIDSEPANLSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 178 LLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGvVSEIADQVVVLELGKQIETGPAKSVLQHP-- 255
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKVem 236
|
250 260
....*....|....*....|
gi 2486247945 256 -KE-----PYTQKLINAVPE 269
Cdd:PRK13640 237 lKEigldiPFVYKLKNKLKE 256
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
12-256 |
8.51e-32 |
|
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: 122.78 E-value: 8.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPD 91
Cdd:COG0410 2 PMLEVENLHAGY---GGIH-VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP----PRSGSIRFDGEDITGLPPH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRlRGakMAMVFQE-----PMTalnpVMtcgdqmdELLRahvpMGPYERRIRildlfEEVRlPDPPRIFRSYP----- 161
Cdd:COG0410 74 RIAR-LG--IGYVPEGrrifpSLT----VE-------ENLL----LGAYARRDR-----AEVR-ADLERVYELFPrlker 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 162 -HQ----LSGGQRQRIVIAMALLLKPDLLICDEPTTAL--NVTTQasILKLILELqKKNGTAVLFITHDFGVVSEIADQV 234
Cdd:COG0410 130 rRQragtLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLapLIVEE--IFEIIRRL-NREGVTILLVEQNARFALEIADRA 206
|
250 260
....*....|....*....|..
gi 2486247945 235 VVLELGKQIETGPAKSVLQHPK 256
Cdd:COG0410 207 YVLERGRIVLEGTAAELLADPE 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
289-520 |
8.98e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 124.35 E-value: 8.98e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 289 NVVKTYTLGGFFtgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR--KLH 366
Cdd:PRK13645 11 NVSYTYAKKTPF----EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 367 GLRRRLQVVFQDPYRSLDpRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARAL 446
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQLF-QETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 447 ACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
36-256 |
1.20e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 122.43 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIAStVMGLLPkglAPADGSVKLLGMDL-FRRTPDE--IRRLRgAKMAMVFQEpmTAL 112
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLE---MPRSGTLNIAGNHFdFSKTPSDkaIRELR-RNVGMVFQQ--YNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 113 NPVMTCgdqMDELLRAHVP---MGPYERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDE 189
Cdd:PRK11124 94 WPHLTV---QQNLIEAPCRvlgLSKDQALARAEKLLERLRLKP---YADRFPLHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 190 PTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVSEIADQVVVLELGKQIETGPAkSVLQHPK 256
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQ 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
300-519 |
1.21e-31 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 125.22 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 300 FTGRVKVRALKgVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR-KLHGLRRRLQVVFQD 378
Cdd:TIGR02142 5 FSKRLGDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 379 PyrSLDPRMTVGESIvegpvNFGVPKEEAWKRAQEFMKIVRL---SPdALNRYPNQFSGGQRQRISIARALACEPEILIC 455
Cdd:TIGR02142 84 A--RLFPHLSVRGNL-----RYGMKRARPSERRISFERVIELlgiGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 456 DEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDV 519
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
13-241 |
1.60e-31 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 121.30 E-value: 1.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLpKGL-APADGSVKLLGMDLFRRTPD 91
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKS----TLLHLL-GGLdNPTSGEVLFNGQSLSKLSSN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRGAKMAMVFQ-----EPMTALNPVMtcgdqMDELLRAhvpMGPYERRIRILDLFEEVRLPDppRIfRSYPHQLSG 166
Cdd:TIGR02211 76 ERAKLRNKKLGFIYQfhhllPDFTALENVA-----MPLLIGK---KSVKEAKERAYEMLEKVGLEH--RI-NHRPSELSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 167 GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIaDQVVVLELGK 241
Cdd:TIGR02211 145 GERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQ 218
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
285-509 |
1.97e-31 |
|
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: 121.07 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlggfftGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRk 364
Cdd:cd03263 1 LQIRNLTKTY-------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhgLRRRLQVVFQDpyRSLDPRMTVGESIVegpvnF-----GVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQR 439
Cdd:cd03263 73 ---ARQSLGYCPQF--DALFDELTVREHLR-----FyarlkGLPKSEIKEEVELLLRVLGLTDKA-NKRARTLSGGMKRK 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 440 ISIARALACEPEILICDEAVSALDVSVQADILKLLEEiqVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILE--VRKGRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
305-520 |
2.38e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.60 E-value: 2.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGE---VWVNGENVAAapkRKLHGLRRRLQVVFQDPyr 381
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTA---KTVWDIREKVGIVFQNP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 382 slDPRM---TVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEA 458
Cdd:PRK13640 94 --DNQFvgaTVGDDVAFGLENRAVPRPEMIKIVRDVLADVGML-DYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 459 VSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQiCDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIF 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
308-514 |
2.60e-31 |
|
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: 121.18 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAApkrKLHGLRRRLQVVFQDPYRSLDprm 387
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY---TLASLRRQIGLVSQDVFLFND--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGESIVEGpvNFGVPKEEAWKRAQ-----EFmkivrlspdaLNRYPNQF-----------SGGQRQRISIARALACEPE 451
Cdd:cd03251 91 TVAENIAYG--RPGATREEVEEAARaanahEF----------IMELPEGYdtvigergvklSGGQRQRIAIARALLKDPP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 452 ILICDEAVSALDVSVQADILKLLEEIQVklGIGILFVTHDLrvaSQI--CDDVIVIRRGECVESG 514
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRL---STIenADRIVVLEDGKIVERG 218
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
299-545 |
3.81e-31 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 123.37 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 299 FFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLidptSGEVW-----------VNGENVAAAPKRKLHG 367
Cdd:PRK15093 13 FKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV----TKDNWrvtadrmrfddIDLLRLSPRERRKLVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 368 lrRRLQVVFQDPYRSLDPRMTVGESIVEGpvnfgVP----KEEAW-------KRAQEFMKIVRLS--PDALNRYPNQFSG 434
Cdd:PRK15093 89 --HNVSMIFQEPQSCLDPSERVGRQLMQN-----IPgwtyKGRWWqrfgwrkRRAIELLHRVGIKdhKDAMRSFPYELTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 435 GQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETA 241
|
250 260 270
....*....|....*....|....*....|.
gi 2486247945 515 HVQDVFFHPQHEYTKSLIAAAPGtnypFGRT 545
Cdd:PRK15093 242 PSKELVTTPHHPYTQALIRAIPD----FGSA 268
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
302-491 |
3.91e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 121.51 E-value: 3.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 302 GRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAaPkrklhGLRRrlQVVFQDpyR 381
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-P-----GADR--GVVFQK--D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 382 SLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSA 461
Cdd:COG4525 86 ALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180 190
....*....|....*....|....*....|
gi 2486247945 462 LDVSVQADILKLLEEIQVKLGIGILFVTHD 491
Cdd:COG4525 165 LDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
12-223 |
1.61e-30 |
|
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: 117.97 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKS----VIAstvmGLLPkglaPADGSVKLLGMDLfR 87
Cdd:COG4133 1 MMLEAENLSCRR---GERL-LFSGLSFTLAAGEALALTGPNGSGKTtllrILA----GLLP----PSAGEVLWNGEPI-R 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 88 RTPDEIRRlrgaKMAMVFQEPmtALNPVMTCGDQMDELLRAHvpmGPYERRIRILDLFEEVRLPDppriFRSYP-HQLSG 166
Cdd:COG4133 68 DAREDYRR----RLAYLGHAD--GLKPELTVRENLRFWAALY---GLRADREAIDEALEAVGLAG----LADLPvRQLSA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 167 GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILElQKKNGTAVLFITHD 223
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
299-514 |
1.90e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 119.84 E-value: 1.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 299 FFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhglRRRLQVVFQD 378
Cdd:PRK13647 11 HFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 379 PYRSLDPrMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEA 458
Cdd:PRK13647 88 PDDQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMW-DFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 459 VSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLH-NQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
32-259 |
2.27e-30 |
|
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: 118.98 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDEirrlRGakMAMVFQEpmTA 111
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLE----RPDSGTILFGGEDATDVPVQE----RN--VGFVFQH--YA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQMDELLRA-HVPMGPYERRI--RILDLFEEVRLPdppRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICD 188
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVkPRSERPPEAEIraKVHELLKLVQLD---WLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 189 EPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPY 259
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
32-270 |
2.42e-30 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 118.75 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPdeirrlRGAKMAMVFQEpmTA 111
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLE----QPDSGRIRLNGQDATRVHA------RDRKIGFVFQH--YA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQMDELLRAHVPmGPYERRIRILDLFEEVRLPdppRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPT 191
Cdd:TIGR00968 83 LFKHLTVRDNIAFGLEIRKH-PKAKIKARVEELLELVQLE---GLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 192 TALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLINAVPEL 270
Cdd:TIGR00968 159 GALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
284-511 |
2.63e-30 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 125.61 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTlggffTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR 363
Cdd:PRK10535 4 LLELKDIRRSYP-----SGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGLRRR-LQVVFQDpYRSLdPRMTVGESiVEGP-VNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRIS 441
Cdd:PRK10535 79 ALAQLRREhFGFIFQR-YHLL-SHLTAAQN-VEVPaVYAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 442 IARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQiCDDVIVIRRGECV 511
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
284-514 |
3.57e-30 |
|
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: 117.47 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTLGgfftgRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR 363
Cdd:cd03266 1 MITADALTKRFRDV-----KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 klhgLRRRLQVVFQDpyRSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIA 443
Cdd:cd03266 76 ----ARRRLGFVSDS--TGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGME-ELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 444 RALACEPEILICDEAVSALDVSVQADILKLLEEiQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
308-527 |
3.81e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 119.32 E-value: 3.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGenVAAAPKRKLHGLRRRLQVVFQDPYRSLDPRm 387
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGIRKLVGIVFQNPETQFVGR- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQ 467
Cdd:PRK13644 94 TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 468 ADILKLLEEIQVKlGIGILFVTHDLRvASQICDDVIVIRRGECVESGHVQDVFFHPQHEY 527
Cdd:PRK13644 173 IAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
308-515 |
5.15e-30 |
|
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: 117.21 E-value: 5.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPkrkLHGLRRRLQVVFQDPY------R 381
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSRISIIPQDPVlfsgtiR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 382 S-LDPrmtvgesivegpvnFGV-PKEEAW---KRAQeFMKIVRLSPDALNRY----PNQFSGGQRQRISIARALACEPEI 452
Cdd:cd03244 96 SnLDP--------------FGEySDEELWqalERVG-LKEFVESLPGGLDTVveegGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 453 LICDEAVSALDVSVQADILKLLEEiQVKlGIGILFVTHdlRVASQI-CDDVIVIRRGECVESGH 515
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIRE-AFK-DCTVLTIAH--RLDTIIdSDRILVLDKGRVVEFDS 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
307-515 |
5.38e-30 |
|
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: 116.74 E-value: 5.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPkrkLHGLRRRLQVVFQDP------Y 380
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSSLTIIPQDPtlfsgtI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 381 RS-LDPrmtvgesivegpvnFGVPKEEawkraqEFMKIVRLSPDALNrypnqFSGGQRQRISIARALACEPEILICDEAV 459
Cdd:cd03369 99 RSnLDP--------------FDEYSDE------EIYGALRVSEGGLN-----LSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 460 SALDVSVQADILKLL-EEIQvklGIGILFVTHDLRVASQiCDDVIVIRRGECVESGH 515
Cdd:cd03369 154 ASIDYATDALIQKTIrEEFT---NSTILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
309-537 |
6.76e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 118.02 E-value: 6.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLID-----PTSGEVWVNGENVAAaPKRKLHGLRRRLQVVFQdpYRSL 383
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYS-PDVDPIEVRREVGMVFQ--YPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 384 DPRMTVGESIVEGPVNFGV--PKEEAWKRAQEFMKIVRL---SPDALNRYPNQFSGGQRQRISIARALACEPEILICDEA 458
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 459 VSALDVSVQADILKLLEEIqvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLIAAAPG 537
Cdd:PRK14267 177 TANIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGALG 253
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
285-508 |
7.09e-30 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 120.33 E-value: 7.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlGGfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENV-AAAPKr 363
Cdd:PRK11650 4 LKLQAVRKSY--DG------KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnELEPA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 klhglRRRLQVVFQDpYrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPdALNRYPNQFSGGQRQRISIA 443
Cdd:PRK11650 75 -----DRDIAMVFQN-Y-ALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAMG 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 444 RALACEPEILICDEAVSALD----VSVQADILKLleeiQVKLGIGILFVTHDLRVASQICDDVIVIRRG 508
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDaklrVQMRLEIQRL----HRRLKTTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
283-520 |
1.13e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.18 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 283 TLLEAKNVvkTYTLGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPK 362
Cdd:PRK13548 1 AMLEARNL--SVRLGG-------RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 363 RKLhglRRRLQVVFQDPyrSLDPRMTVGEsIVE-GPVNFGVPKEEAWKRAQEFMKIVRLSPDALNRYPnQFSGGQRQRIS 441
Cdd:PRK13548 72 AEL---ARRRAVLPQHS--SLSFPFTVEE-VVAmGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYP-QLSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 442 IARALA------CEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGH 515
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
....*
gi 2486247945 516 VQDVF 520
Cdd:PRK13548 225 PAEVL 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
27-251 |
1.50e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 117.50 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 27 GDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDlfrrTPDE-----IRRlrgaKM 101
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALL----IPSEGKVYVDGLD----TSDEenlwdIRN----KA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 102 AMVFQEPMTALnpVMTcgdqmdeLLRAHVPMGP-------YERRIRILDLFEEVRLPDppriFRSY-PHQLSGGQRQRIV 173
Cdd:PRK13633 88 GMVFQNPDNQI--VAT-------IVEEDVAFGPenlgippEEIRERVDESLKKVGMYE----YRRHaPHLLSGGQKQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEiADQVVVLELGKQIETGPAKSV 251
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
26-247 |
1.61e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 122.58 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 26 GGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRRlrgaKMAMVF 105
Cdd:COG1132 350 PGDRP-VLKDISLTIPPGETVALVGPSGSGKS----TLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR----QIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 106 QEP----MTALNPVmTCGDQ---MDELLRAhvpmgpyerrIRILDLFEEV-RLPDpprifrSYPHQ-------LSGGQRQ 170
Cdd:COG1132 421 QDTflfsGTIRENI-RYGRPdatDEEVEEA----------AKAAQAHEFIeALPD------GYDTVvgergvnLSGGQRQ 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 171 RIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVSEiADQVVVLELGKQIETGP 247
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
286-519 |
1.94e-29 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 116.34 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 286 EAKNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKL 365
Cdd:COG4604 3 EIKNVSKRY-------GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 366 hglRRRLQVVFQDPyrSLDPRMTVGESivegpVNFG-------VPKEEAWK---RAQEFMKIVRLSpdalNRYPNQFSGG 435
Cdd:COG4604 74 ---AKRLAILRQEN--HINSRLTVREL-----VAFGrfpyskgRLTAEDREiidEAIAYLDLEDLA----DRYLDELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 436 QRQRISIARALACEPEILICDEAVSALDV--SVQadILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVES 513
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMkhSVQ--MMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
....*.
gi 2486247945 514 GHVQDV 519
Cdd:COG4604 218 GTPEEI 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
291-514 |
3.77e-29 |
|
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: 114.24 E-value: 3.77e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 291 VKTYTLGGFFTGRvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapkrKLHGLRR 370
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-----KNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 371 RLQVVFQDPyrSLDPRMTVGESIVEGPVNFGVPKeeawKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEP 450
Cdd:cd03268 73 RIGALIEAP--GFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNP 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 451 EILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03268 146 DLLILDEPTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
305-532 |
5.54e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 115.26 E-value: 5.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLID-----PTSGEVWVNGENVAAaPKRKLHGLRRRLQVVFQDP 379
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYS-PRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 380 yrslDP-RMTVGESIVEGPVNFGVPK----EEAWKRAQEFMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILI 454
Cdd:PRK14239 96 ----NPfPMSIYENVVYGLRLKGIKDkqvlDEAVEKSLKGASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 455 CDEAVSALDVSVQADILKLLEEIQVKLgiGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLI 532
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
285-514 |
5.80e-29 |
|
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: 113.83 E-value: 5.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGeTIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVaaapKRK 364
Cdd:cd03264 1 LQLENLTKRYG---------KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDPyrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIAR 444
Cdd:cd03264 67 PQKLRRRIGYLPQEF--GVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 445 ALACEPEILICDEAVSALDVSVQADILKLLeeiqVKLGIG--ILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLL----SELGEDriVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
315-514 |
6.37e-29 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 114.68 E-value: 6.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 315 RLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRklhglRRRLQVVFQDpyRSLDPRMTVGESIV 394
Cdd:PRK10771 21 TVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-----RRPVSMLFQE--NNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 395 EGpVNFGVPKEEAWKRA-QEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKL 473
Cdd:PRK10771 94 LG-LNPGLKLNAAQREKlHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2486247945 474 LEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDG 212
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
12-237 |
6.90e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 115.34 E-value: 6.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfrRTPd 91
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLA----PSSGEITLDGVPV--TGP- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 eirrlrGAKMAMVFQEpmTALNPVMTCGDQMDELLR-AHVPmgPYERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQ 170
Cdd:COG4525 75 ------GADRGVVFQK--DALLPWLNVLDNVAFGLRlRGVP--KAERRARAEELLALVGLAD---FARRRIWQLSGGMRQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 171 RIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfgvVSE---IADQVVVL 237
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEalfLATRLVVM 208
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
36-255 |
7.75e-29 |
|
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: 117.51 E-value: 7.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLF---RRT--PDEIRRLrgakmAMVFQEPmt 110
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLER----PDSGRIRLGGEVLQdsaRGIflPPHRRRI-----GYVFQEA-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALNPVMTCGDQmdeLLRAHVPMGPYERRIRildlFEEV-----------RlpdpprifrsYPHQLSGGQRQRIVIAMALL 179
Cdd:COG4148 87 RLFPHLSVRGN---LLYGRKRAPRAERRIS----FDEVvellgighlldR----------RPATLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 180 LKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHP 255
Cdd:COG4148 150 SSPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
32-267 |
1.03e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.83 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRRLRGAKMAMVFQEpmTA 111
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKS----TMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQMDELLR-AHVPMGpyERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEP 190
Cdd:PRK10070 117 LMPHMTVLDNTAFGMElAGINAE--ERREKALDALRQVGLEN---YAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 191 TTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLINAV 267
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-267 |
1.24e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 114.17 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLP-KGLAPADGSVKLLGMDLFRRTPDE 92
Cdd:PRK14267 5 IETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElNEEARVEGEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRgaKMAMVFQEP-----MT---------ALNPVMTCGDQMDELLrahvpmgpyERRIRILDLFEEV--RLPDppri 156
Cdd:PRK14267 81 IEVRR--EVGMVFQYPnpfphLTiydnvaigvKLNGLVKSKKELDERV---------EWALKKAALWDEVkdRLND---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 157 frsYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLfITHDFGVVSEIADQVVV 236
Cdd:PRK14267 146 ---YPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFEL-KKEYTIVL-VTHSPAQAARVSDYVAF 220
|
250 260 270
....*....|....*....|....*....|.
gi 2486247945 237 LELGKQIETGPAKSVLQHPKEPYTQKLINAV 267
Cdd:PRK14267 221 LYLGKLIEVGPTRKVFENPEHELTEKYVTGA 251
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
282-519 |
1.41e-28 |
|
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: 113.54 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 282 PTLLEAKNVVKTYtlggfftGrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAP 361
Cdd:COG0410 1 MPMLEVENLHAGY-------G--GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 362 --KRKLHGL------RRrlqvVFqdpyrsldPRMTVGESIVEGPVNFGVPKEEAWKRAqefmKIVRLSP---DALNRYPN 430
Cdd:COG0410 72 phRIARLGIgyvpegRR----IF--------PSLTVEENLLLGAYARRDRAEVRADLE----RVYELFPrlkERRRQRAG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 431 QFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGEC 510
Cdd:COG0410 136 TLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLN-REGVTILLVEQNARFALEIADRAYVLERGRI 214
|
....*....
gi 2486247945 511 VESGHVQDV 519
Cdd:COG0410 215 VLEGTAAEL 223
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
309-521 |
1.47e-28 |
|
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: 113.33 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAA-APKRklhglrrrlQVVFQDpyRSLDPRM 387
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpGPDR---------MVVFQN--YSLLPWL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGESIVEG--PVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVS 465
Cdd:TIGR01184 70 TVRENIALAvdRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 466 VQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFF 521
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVPF 204
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
32-259 |
1.77e-28 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 116.29 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDeiRRLRGakmaMVFQEpmTA 111
Cdd:TIGR03265 19 ALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLE----RQTAGTIYQGGRDITRLPPQ--KRDYG----IVFQS--YA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQMDELLRAHvPMGPYERRIRILDLFEEVRLPDPPRifrSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPT 191
Cdd:TIGR03265 87 LFPNLTVADNIAYGLKNR-GMGRAEVAERVAELLDLVGLPGSER---KYPGQLSGGQQQRVALARALATSPGLLLLDEPL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 192 TALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPY 259
Cdd:TIGR03265 163 SALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPF 230
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
307-492 |
3.35e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 112.28 E-value: 3.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHGLRRRLQVVFQDPYRSLDpr 386
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 MTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALNrYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSV 466
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180
....*....|....*....|....*.
gi 2486247945 467 QADILKLLEEIQvKLGIGILFVTHDL 492
Cdd:PRK10908 173 SEGILRLFEEFN-RVGVTVLMATHDI 197
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
14-246 |
3.38e-28 |
|
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: 112.08 E-value: 3.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppGGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRtPDEI 93
Cdd:cd03265 1 IEVENLVKKY--GDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK----PTSGRATVAGHDVVRE-PREV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPmtALNPVMTCGDQMDELLRAH-VPMGpyERRIRILDLFEEVRLPD-PPRIFRSYphqlSGGQRQR 171
Cdd:cd03265 72 RR----RIGIVFQDL--SVDDELTGWENLYIHARLYgVPGA--ERRERIDELLDFVGLLEaADRLVKTY----SGGMRRR 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 172 IVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03265 140 LEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
285-523 |
4.03e-28 |
|
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: 112.25 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRK 364
Cdd:cd03218 1 LRAENLSKRY-------GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhglRRRLQVVF--QDPyrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISI 442
Cdd:cd03218 72 ----RARLGIGYlpQEA--SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLR-KSKASSLSGGERRRVEI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 443 ARALACEPEILICDEAVSALD-VSVQaDILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFF 521
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
..
gi 2486247945 522 HP 523
Cdd:cd03218 223 NE 224
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
12-509 |
4.40e-28 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 117.70 E-value: 4.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPpgGDRpnAVEHVSFTVNEGEVTCLIGESGSGKsviaSTVMGLLPKGLAPADGSVKLLGMDL-FRRTP 90
Cdd:PRK11288 3 PYLSFDGIGKTFP--GVK--ALDDISFDCRAGQVHALMGENGAGK----STLLKILSGNYQPDAGSILIDGQEMrFASTT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIrrlrGAKMAMVFQEpmTALNPVMTCgdqMDELLRAHVP--MGPYERRirilDLFEEVRLP--------DPPRIFRSy 160
Cdd:PRK11288 75 AAL----AAGVAIIYQE--LHLVPEMTV---AENLYLGQLPhkGGIVNRR----LLNYEAREQlehlgvdiDPDTPLKY- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 161 phqLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELG 240
Cdd:PRK11288 141 ---LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 241 KQIETGPAKSVLQHpkepytQKLINA--------VPELKPRHRPPVdgnptLLEAKNvvktytlggfftgrVKVRALKG- 311
Cdd:PRK11288 217 RYVATFDDMAQVDR------DQLVQAmvgreigdIYGYRPRPLGEV-----RLRLDG--------------LKGPGLREp 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 312 VSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRklHGLRRRLQVVFQDpyRSLD---PRMT 388
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPR--DAIRAGIMLCPED--RKAEgiiPVHS 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 VGESIvegpvN---------FGVPKEEAWKR--AQEF---MKIVRLSPDALNRYpnqFSGGQRQRISIARALACEPEILI 454
Cdd:PRK11288 348 VADNI-----NisarrhhlrAGCLINNRWEAenADRFirsLNIKTPSREQLIMN---LSGGNQQKAILGRWLSEDMKVIL 419
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 455 CDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:PRK11288 420 LDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
308-514 |
5.05e-28 |
|
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: 112.19 E-value: 5.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKrklHGLRRRLQVVFQDpyrSLDPRM 387
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP---AWLRRQVGVVLQE---NVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGESIVEGpvNFGVPKE---EAWKR--AQEFMKIVRLSPDA-LNRYPNQFSGGQRQRISIARALACEPEILICDEAVSA 461
Cdd:cd03252 91 SIRDNIALA--DPGMSMErviEAAKLagAHDFISELPEGYDTiVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 462 LDVSVQADILKLLEEIQVklGIGILFVTHDLRvASQICDDVIVIRRGECVESG 514
Cdd:cd03252 169 LDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQG 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
285-514 |
6.15e-28 |
|
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: 111.47 E-value: 6.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGGFFTGRVK-------------VRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVW 351
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 352 VNGeNVAAAPkrklhglrrRLQVVFqdpyrslDPRMTVGESIVEGPVNFGVPKEEAWKRAQEfmkIVRLS--PDALNRYP 429
Cdd:cd03220 81 VRG-RVSSLL---------GLGGGF-------NPELTGRENIYLNGRLLGLSRKEIDEKIDE---IIEFSelGDFIDLPV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 430 NQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEiQVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd03220 141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE-LLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
....*
gi 2486247945 510 CVESG 514
Cdd:cd03220 220 IRFDG 224
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
284-491 |
7.27e-28 |
|
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: 110.65 E-value: 7.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR 363
Cdd:COG4133 2 MLEAENLSCRR-------GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 klhgLRRRLQVVFQDPyrSLDPRMTVGESIvegpvNF-----GVPKEEAwkRAQEFMKIVRLSPdALNRYPNQFSGGQRQ 438
Cdd:COG4133 73 ----YRRRLAYLGHAD--GLKPELTVRENL-----RFwaalyGLRADRE--AIDEALEAVGLAG-LADLPVRQLSAGQKR 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 439 RISIARALACEPEILICDEAVSALDVSVQADILKLLEEiQVKLGIGILFVTHD 491
Cdd:COG4133 139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
318-514 |
1.38e-27 |
|
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: 110.28 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 318 RGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRklhglRRRLQVVFQDpyRSLDPRMTVGESIVEGP 397
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA-----DRPVSMLFQE--NNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 398 V---NFGVPKEEAWKRAQEFMKIVRLspdaLNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLL 474
Cdd:cd03298 96 SpglKLTAEDRQAIEVALARVGLAGL----EKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2486247945 475 EEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
12-238 |
2.28e-27 |
|
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: 109.83 E-value: 2.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLP---PGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLL----GMD 84
Cdd:COG4778 3 TLLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKS----TLLKCIYGNYLPDSGSILVRhdggWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 85 LFRRTPDEIRRLRGAKMAMVFQ----EP-MTALNPVMtcgdqmdELLRAHvPMGPYERRIRILDLFEEVRLPdpPRIFRS 159
Cdd:COG4778 79 LAQASPREILALRRRTIGYVSQflrvIPrVSALDVVA-------EPLLER-GVDREEARARARELLARLNLP--ERLWDL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 160 YPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLE 238
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
305-518 |
2.44e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 116.21 E-value: 2.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapKRKLHGLRRRLQVVFQDPyrsld 384
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIR---TVTRASLRRNIAVVFQDA----- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 385 prMTVGESIVEgpvNFGVPKE--------EAWKRAQEFMKIVRlSPDALN----RYPNQFSGGQRQRISIARALACEPEI 452
Cdd:PRK13657 419 --GLFNRSIED---NIRVGRPdatdeemrAAAERAQAHDFIER-KPDGYDtvvgERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 453 LICDEAVSALDVSVQADILKLLEEiqVKLGIGILFVTHDL---RVAsqicDDVIVIRRGECVESGHVQD 518
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDE--LMKGRTTFIIAHRLstvRNA----DRILVFDNGRVVESGSFDE 555
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
263-520 |
2.93e-27 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 115.95 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 263 LINAVPELKPRHRP---PVDGnPTLLEAKNVVKTYTlggfftGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSI 339
Cdd:TIGR02204 314 LLQAEPDIKAPAHPktlPVPL-RGEIEFEQVNFAYP------ARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 340 ARLIDPTSGEVWVNGENVAAAPKRKLhglRRRLQVVFQDPyrsldprmTVGESIVEGPVNFGVPK------EEAWKRAQE 413
Cdd:TIGR02204 387 LRFYDPQSGRILLDGVDLRQLDPAEL---RARMALVPQDP--------VLFAASVMENIRYGRPDatdeevEAAARAAHA 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 414 FMKIVRLsPDALNRYPNQ----FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVklGIGILFVT 489
Cdd:TIGR02204 456 HEFISAL-PEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIA 532
|
250 260 270
....*....|....*....|....*....|.
gi 2486247945 490 HDLrVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:TIGR02204 533 HRL-ATVLKADRIVVMDQGRIVAQGTHAELI 562
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
12-237 |
4.77e-27 |
|
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: 107.52 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVslppggdrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPD 91
Cdd:cd03215 3 PVLEVRGLSV--------KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP----PASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRlrgAKMAMVfqepmtalnPvmtcGDQMDELLrahvpmgpyerrIRILDLFEEVRLPdpprifrsypHQLSGGQRQR 171
Cdd:cd03215 71 DAIR---AGIAYV---------P----EDRKREGL------------VLDLSVAENIALS----------SLLSGGNQQK 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 172 IVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVL 237
Cdd:cd03215 113 VVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVM 177
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
12-257 |
5.19e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.23 E-value: 5.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENlaVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVkllgmdLFRR--- 88
Cdd:PRK13648 6 SIIVFKN--VSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIE----KVKSGEI------FYNNqai 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 89 TPDEIRRLRgAKMAMVFQEPMtalNPVMTCGDQMDELLRAHVPMGPYERRIRIL-DLFEEVRLPDppriFRSY-PHQLSG 166
Cdd:PRK13648 74 TDDNFEKLR-KHIGIVFQNPD---NQFVGSIVKYDVAFGLENHAVPYDEMHRRVsEALKQVDMLE----RADYePNALSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 167 GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEiADQVVVLELGKQIETG 246
Cdd:PRK13648 146 GQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEG 224
|
250
....*....|.
gi 2486247945 247 PAKSVLQHPKE 257
Cdd:PRK13648 225 TPTEIFDHAEE 235
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
285-514 |
5.40e-27 |
|
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: 109.34 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTY-----------TLGGFFTGRVK-VRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWV 352
Cdd:cd03267 1 IEVSNLSKSYrvyskepgligSLKSLFKRKYReVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 353 NGEnvaaAPKRKLHGLRRRLQVVF-QDPYRSLDprMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPdALNRYPNQ 431
Cdd:cd03267 81 AGL----VPWKRRKKFLRRIGVVFgQKTQLWWD--LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEE-LLDTPVRQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 432 FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECV 511
Cdd:cd03267 154 LSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
...
gi 2486247945 512 ESG 514
Cdd:cd03267 234 YDG 236
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
288-540 |
6.78e-27 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 112.05 E-value: 6.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 288 KNVVKTYtlggfftGRVKVRalKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKlhg 367
Cdd:PRK11000 7 RNVTKAY-------GDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 368 lrRRLQVVFQDpYrSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALA 447
Cdd:PRK11000 75 --RGVGMVFQS-Y-ALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLA-HLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 448 CEPEILICDEAVSALD----VSVQADILKLleeiQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHP 523
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDaalrVQMRIEISRL----HKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
250
....*....|....*..
gi 2486247945 524 QHEYTKSLIaAAPGTNY 540
Cdd:PRK11000 226 ANRFVAGFI-GSPKMNF 241
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
308-517 |
8.19e-27 |
|
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: 115.22 E-value: 8.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKrklHGLRRRLQVVFQDPYrsldprM 387
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDR---HTLRQFINYLPQEPY------I 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGeSIVEGPV---NFGVPKEEAWkRAQEFMKI------------VRLSPDALNrypnqFSGGQRQRISIARALACEPEI 452
Cdd:TIGR01193 560 FSG-SILENLLlgaKENVSQDEIW-AACEIAEIkddienmplgyqTELSEEGSS-----ISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 453 LICDEAVSALDVSVQADILKLLEEIQVKLgigILFVTHDLRVASQIcDDVIVIRRGECVESG-HVQ 517
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDKT---IIFVAHRLSVAKQS-DKIIVLDHGKIIEQGsHDE 694
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
36-265 |
8.43e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 109.29 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTVmGLLPKglaPADGSVKLLGMD--LFRRTPDEIR-------RLRGAKMAMVFQ 106
Cdd:PRK10619 24 VSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEK---PSEGSIVVNGQTinLVRDKDGQLKvadknqlRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 107 E-----PMTALNPVMTCGDQMDELLRAHVpmgpYERRIRILDlfeEVRLPDPPRIfrSYPHQLSGGQRQRIVIAMALLLK 181
Cdd:PRK10619 100 HfnlwsHMTVLENVMEAPIQVLGLSKQEA----RERAVKYLA---KVGIDERAQG--KYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 182 PDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQ 261
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....
gi 2486247945 262 KLIN 265
Cdd:PRK10619 250 QFLK 253
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
286-514 |
8.68e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 110.95 E-value: 8.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 286 EAKNVVKTYT-------LGGFFTGRVK-----VRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVN 353
Cdd:COG4586 3 EVENLSKTYRvyekepgLKGALKGLFRreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 354 GENvaaaPKRKLHGLRRRLQVVF-QdpyRS-LDPRMTVGES------IvegpvnFGVPKEEAWKRAQEFMKIVRLSpDAL 425
Cdd:COG4586 83 GYV----PFKRRKEFARRIGVVFgQ---RSqLWWDLPAIDSfrllkaI------YRIPDAEYKKRLDELVELLDLG-ELL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 426 NRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVI 505
Cdd:COG4586 149 DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVI 228
|
....*....
gi 2486247945 506 RRGECVESG 514
Cdd:COG4586 229 DHGRIIYDG 237
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
31-246 |
9.52e-27 |
|
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: 107.69 E-value: 9.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 31 NAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLlpkgLAPADGSVKLLGMDLFRRTPDEIRrlrgakMAMVFQEPmt 110
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGL----IKPDSGEITFDGKSYQKNIEALRR------IGALIEAP-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALNPVMTCGDQMdeLLRAHVPMGPYERRIRILDlfeEVRLPD-PPRIFRSYphqlSGGQRQRIVIAMALLLKPDLLICDE 189
Cdd:cd03268 82 GFYPNLTARENL--RLLARLLGIRKKRIDEVLD---VVGLKDsAKKKVKGF----SLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 190 PTTALNVTTQASILKLILELQKKNGTaVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGIT-VLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
309-532 |
9.61e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 108.98 E-value: 9.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLID------PTSGEVWVNGENVAAAPKRKLhglRRRLQVVFQDPyrS 382
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKL---RKEVGMVFQQP--N 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 383 LDPRMTVGESIVEGPVNFGVP-KEEAWKRAQEFMKIVRLSP---DALNRYPNQFSGGQRQRISIARALACEPEILICDEA 458
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWKevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 459 VSALDVSVQADILKLLEEIqvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLI 532
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-264 |
9.85e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 108.85 E-value: 9.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLppgGDrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIA---STVMGLLPKglAPADGSVKLLGMDLFRRT 89
Cdd:PRK14247 3 KIEIRDLKVSF---GQ-VEVLDGVNLEIPDNTITALMGPSGSGKSTLLrvfNRLIELYPE--ARVSGEVYLDGQDIFKMD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 90 PDEIRRlrgaKMAMVFQEPmtalNPV--------MTCGDQMDELLRAHVPMgpyERRIR----ILDLFEEV--RLPDPPr 155
Cdd:PRK14247 77 VIELRR----RVQMVFQIP----NPIpnlsifenVALGLKLNRLVKSKKEL---QERVRwaleKAQLWDEVkdRLDAPA- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 156 ifrsypHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKngTAVLFITHDFGVVSEIADQVV 235
Cdd:PRK14247 145 ------GKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVA 216
|
250 260
....*....|....*....|....*....
gi 2486247945 236 VLELGKQIETGPAKSVLQHPKEPYTQKLI 264
Cdd:PRK14247 217 FLYKGQIVEWGPTREVFTNPRHELTEKYV 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
163-515 |
9.94e-27 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 114.14 E-value: 9.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNgtAVLFITHDFGVVSEIADQVVVLeLGKq 242
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIA-YGE- 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 243 ietgP-AKSVLQHPKEpyTQKLINA-----VPELKPRHRP-----------PVDGNPTLLEAKNVVKTYtlGGFftgRVK 305
Cdd:PRK13409 288 ----PgAYGVVSKPKG--VRVGINEylkgyLPEENMRIRPepiefeerpprDESERETLVEYPDLTKKL--GDF---SLE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 306 VRAlkgvsARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNgenvaaapkrklhglrrrLQVVFQDPYRSLDP 385
Cdd:PRK13409 357 VEG-----GEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------------LKISYKPQYIKPDY 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 386 RMTVGESIVEGPVNFGvpkEEAWKraQEFMKIVRLsPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVS 465
Cdd:PRK13409 414 DGTVEDLLRSITDDLG---SSYYK--SEIIKPLQL-ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2486247945 466 VQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIrRGECVESGH 515
Cdd:PRK13409 488 QRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVF-EGEPGKHGH 536
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-511 |
1.03e-26 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 113.35 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLpKGLAPA---DGSVKLLGmdlfrrtpdEIRRLRGAK------MA 102
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKS----TLMKVL-SGVYPHgsyEGEILFDG---------EVCRFKDIRdsealgIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 103 MVFQEpmTALNPVMTCGDQM---DELLRAHVpMGPYERRIRILDLFEEVRLPDPP--RIfrsypHQLSGGQRQRIVIAMA 177
Cdd:NF040905 82 IIHQE--LALIPYLSIAENIflgNERAKRGV-IDWNETNRRARELLAKVGLDESPdtLV-----TDIGVGKQQLVEIAKA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 178 LLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVSEIADQVVVLELGKQIETgpaksvLQHPKE 257
Cdd:NF040905 154 LSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVLRDGRTIET------LDCRAD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 258 PYTQKLI----------NAVPElkprhRPPVDGNpTLLEAKNVVKTYTLggfFTGRvKVraLKGVSARLRRGETIGIVGE 327
Cdd:NF040905 227 EVTEDRIirgmvgrdleDRYPE-----RTPKIGE-VVFEVKNWTVYHPL---HPER-KV--VDDVSLNVRRGEIVGIAGL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 328 SGSGK-----STFARSIARLIdptSGEVWVNGE-----NVAAAPKrklHGL------RRRLQVVFQDPYRsldpRMTVGE 391
Cdd:NF040905 295 MGAGRtelamSVFGRSYGRNI---SGTVFKDGKevdvsTVSDAID---AGLayvtedRKGYGLNLIDDIK----RNITLA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 392 SIvEGPVNFGVPKE-EAWKRAQEFMKIVRL-SPDALNRYPNqFSGGQRQRISIARALACEPEILICDEAVSALDVSVQAD 469
Cdd:NF040905 365 NL-GKVSRRGVIDEnEEIKVAEEYRKKMNIkTPSVFQKVGN-LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYE 442
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2486247945 470 ILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECV 511
Cdd:NF040905 443 IYTIINEL-AAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
285-514 |
1.71e-26 |
|
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: 106.48 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVvkTYTLGGFfTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIA-RLIDP-TSGEVWVNGENvaaapk 362
Cdd:cd03213 4 LSFRNL--TVTVKSS-PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgRRTGLgVSGEVLINGRP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 363 RKLHGLRRRLQVVFQDPYrsLDPRMTVGESivegpvnfgvpkeeawkraqeFMKIVRLSpdalnrypnQFSGGQRQRISI 442
Cdd:cd03213 75 LDKRSFRKIIGYVPQDDI--LHPTLTVRET---------------------LMFAAKLR---------GLSGGERKRVSI 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 443 ARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRvaSQI---CDDVIVIRRGECVESG 514
Cdd:cd03213 123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHQPS--SEIfelFDKLLLLSQGRVIYFG 194
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
251-514 |
1.85e-26 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 114.07 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 251 VLQHPKEPYTQKLInAVPELKPRhrppvdgnptlLEAKNVVKTYTlggfftgRVKVRALKGVSARLRRGETIGIVGESGS 330
Cdd:TIGR01846 434 ILNSPTEPRSAGLA-ALPELRGA-----------ITFENIRFRYA-------PDSPEVLSNLNLDIKPGEFIGIVGPSGS 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 331 GKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhglRRRLQVVFQDpyrSLDPRMTVGESIVEGpvNFGVPKEEAWKR 410
Cdd:TIGR01846 495 GKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL---RRQMGVVLQE---NVLFSRSIRDNIALC--NPGAPFEHVIHA 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 411 AQ-----EFmkIVRLsPDALNRYPNQ----FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVkl 481
Cdd:TIGR01846 567 AKlagahDF--ISEL-PQGYNTEVGEkganLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR-- 641
|
250 260 270
....*....|....*....|....*....|...
gi 2486247945 482 GIGILFVTHDLRVASQiCDDVIVIRRGECVESG 514
Cdd:TIGR01846 642 GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESG 673
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
33-289 |
1.85e-26 |
|
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: 107.55 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 33 VEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDEIrrlrgakmaMVFQEpmTAL 112
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLA----QPTSGGVILEGKQITEPGPDRM---------VVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 113 NPVMTCGDQMDELLRAHVPMGPYERRIRILDlfEEVRLPDPPRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTT 192
Cdd:TIGR01184 66 LPWLTVRENIALAVDRVLPDLSKSERRAIVE--EHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 193 ALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLelgkqiETGPAKSVLQhpkepytqklINAVPELKP 272
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVML------TNGPAANIGQ----------ILEVPFPRP 207
|
250
....*....|....*..
gi 2486247945 273 RHRPPVDGNPTLLEAKN 289
Cdd:TIGR01184 208 RDRLEVVEDPSYYDLRN 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
12-285 |
2.06e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 108.32 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPD 91
Cdd:PRK13548 1 AMLEARNLSVRL---GGRT-LLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALSGELSPDSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRGA---KMAMVFqePMTALNPVmtcgdqmdELLRAHVPMGPYERRIRILDLFEEVRLPDppriF--RSYPhQLSG 166
Cdd:PRK13548 73 ELARRRAVlpqHSSLSF--PFTVEEVV--------AMGRAPHGLSRAEDDALVAAALAQVDLAH----LagRDYP-QLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 167 GQRQRIVIAMAL--LLKPD----LLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELG 240
Cdd:PRK13548 138 GEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2486247945 241 KQIETGPAKSVLqhpkepyTQKLINAVPELKPR-HRPPVDGNPTLL 285
Cdd:PRK13548 218 RLVADGTPAEVL-------TPETLRRVYGADVLvQPHPETGAPLVL 256
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
271-517 |
2.18e-26 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 113.66 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 271 KPRHRPPVDGNPT----LLEAKNVVKTYTlggfftGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPT 346
Cdd:TIGR00958 461 KPNIPLTGTLAPLnlegLIEFQDVSFSYP------NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 347 SGEVWVNGENVaaaPKRKLHGLRRRLQVVFQDPyrsLDPRMTVGESIVEGPVNfgVPKEEAWKRAQE------FMKIVRL 420
Cdd:TIGR00958 535 GGQVLLDGVPL---VQYDHHYLHRQVALVGQEP---VLFSGSVRENIAYGLTD--TPDEEIMAAAKAanahdfIMEFPNG 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 421 SPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQAdilkLLEEIQVKLGIGILFVTHDLRVASQiCD 500
Cdd:TIGR00958 607 YDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-AD 681
|
250
....*....|....*...
gi 2486247945 501 DVIVIRRGECVESG-HVQ 517
Cdd:TIGR00958 682 QILVLKKGSVVEMGtHKQ 699
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
32-262 |
2.26e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 108.71 E-value: 2.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPD-EIRRLRgAKMAMVFQEPMT 110
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL----KPTTGTVTVDDITITHKTKDkYIRPVR-KRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALnpvmtcgdqMDELLRAHVPMGPY-------ERRIRILDLFEEvrLPDPPRIFRSYPHQLSGGQRQRIVIAMALLLKPD 183
Cdd:PRK13646 97 QL---------FEDTVEREIIFGPKnfkmnldEVKNYAHRLLMD--LGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 184 LLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGpaksvlqHPKEPYTQK 262
Cdd:PRK13646 166 IIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT-------SPKELFKDK 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
12-267 |
2.61e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 110.70 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLfRRTPD 91
Cdd:PRK11607 18 PLLEIRNLTKSF----DGQHAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGFEQPTAGQIMLDGVDL-SHVPP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRgakmaMVFQEpmTALNPVMTC------GDQMDELLRAhvpmgpyERRIRILDLFEEVRLPDpprIFRSYPHQLS 165
Cdd:PRK11607 89 YQRPIN-----MMFQS--YALFPHMTVeqniafGLKQDKLPKA-------EIASRVNEMLGLVHMQE---FAKRKPHQLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIET 245
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQI 231
|
250 260
....*....|....*....|..
gi 2486247945 246 GPAKSVLQHPKEPYTQKLINAV 267
Cdd:PRK11607 232 GEPEEIYEHPTTRYSAEFIGSV 253
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-509 |
3.20e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 112.07 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 35 HVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIRRLrgaKMAMVFQEPMtaLNP 114
Cdd:PRK15439 29 GIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP----PDSGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPL--LFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 115 VMTCgdQMDELLRAHVPMGPYERRIRILDLFEEVRLPDPPrifrsyPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTAL 194
Cdd:PRK15439 100 NLSV--KENILFGLPKRQASMQKMKQLLAALGCQLDLDSS------AGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 195 NVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKS------------VLQHPKEPYTQK 262
Cdd:PRK15439 172 TPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADlstddiiqaitpAAREKSLSASQK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 263 LINAVPELKPRHRPpvdGNPTLleaknVVKTYTLGGFftgrvkvralKGVSARLRRGETIGIVGESGSGKSTFARSIARL 342
Cdd:PRK15439 251 LWLELPGNRRQQAA---GAPVL-----TVEDLTGEGF----------RNISLEVRAGEILGLAGVVGAGRTELAETLYGL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 343 IDPTSGEVWVNGENVAA-APKRKLH-GL-----RRRLQVVFQD-PYRSLDPRMTVGEsivegPVNFGVPKEEAwKRAQEF 414
Cdd:PRK15439 313 RPARGGRIMLNGKEINAlSTAQRLArGLvylpeDRQSSGLYLDaPLAWNVCALTHNR-----RGFWIKPAREN-AVLERY 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 415 MKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRV 494
Cdd:PRK15439 387 RRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSI-AAQNVAVLFISSDLEE 465
|
490
....*....|....*
gi 2486247945 495 ASQICDDVIVIRRGE 509
Cdd:PRK15439 466 IEQMADRVLVMHQGE 480
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
14-242 |
6.40e-26 |
|
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: 104.22 E-value: 6.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSlPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03246 1 LEVENVSFR-YPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLR----PTSGRVRLDGADISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRGAKMamvfqepmtalnpvmtcgdQMDELLRahvpmGPYERRIrildlfeevrlpdpprifrsyphqLSGGQRQRIV 173
Cdd:cd03246 75 GDHVGYLP-------------------QDDELFS-----GSIAENI------------------------LSGGQRQRLG 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVsEIADQVVVLELGKQ 242
Cdd:cd03246 107 LARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIV-IAHRPETL-ASADRILVLEDGRV 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-240 |
6.45e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.26 E-value: 6.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLApADGSVKLLGMDLfRRTPDEI 93
Cdd:COG4136 2 LSLENLTITL---GGRP-LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFS-ASGEVLLNGRRL-TALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLrgakmAMVFQEPMtaLNPVMTCGDQMDELLRAHVPMGpyERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIV 173
Cdd:COG4136 76 RRI-----GILFQDDL--LFPHLSVGENLAFALPPTIGRA--QRRARVEQALEEAGLAG---FADRDPATLSGGQRARVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfgvVSEIADQVVVLELG 240
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD---EEDAPAAGRVLDLG 207
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
282-524 |
7.89e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 105.88 E-value: 7.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 282 PTLLEAKNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAP 361
Cdd:COG1137 1 MMTLEAENLVKSY-------GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 362 krkLHgLRRRLQVVF--QDPyrSLDPRMTVGE---SIVEgpvNFGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQ 436
Cdd:COG1137 72 ---MH-KRARLGIGYlpQEA--SIFRKLTVEDnilAVLE---LRKLSKKEREERLEELLEEFGITHLR-KSKAYSLSGGE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 437 RQRISIARALACEPEILICDEAVSALD-VSVqADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGH 515
Cdd:COG1137 142 RRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLK-ERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGT 219
|
....*....
gi 2486247945 516 VQDVFFHPQ 524
Cdd:COG1137 220 PEEILNNPL 228
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
318-509 |
1.06e-25 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 104.94 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 318 RGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRklhglRRRLQVVFQDpyRSLDPRMTVGESIVEGp 397
Cdd:TIGR01277 23 DGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY-----QRPVSMLFQE--NNLFAHLTVRQNIGLG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 398 VNFG-----VPKEEAWKRAQEfMKIvrlsPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILK 472
Cdd:TIGR01277 95 LHPGlklnaEQQEKVVDAAQQ-VGI----ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 2486247945 473 LLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
285-495 |
1.10e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.32 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTytlggFFTGRV-KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKR 363
Cdd:COG1101 2 LELKNLSKT-----FNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KlhglR-RRLQVVFQDPYRSLDPRMTVGE--SIVEG-----PVNFGVPKEEAwKRAQEFMKIVRLS-PDALNRYPNQFSG 434
Cdd:COG1101 77 K----RaKYIGRVFQDPMMGTAPSMTIEEnlALAYRrgkrrGLRRGLTKKRR-ELFRELLATLGLGlENRLDTKVGLLSG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 435 GQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVA 495
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQA 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-237 |
2.02e-25 |
|
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: 110.07 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 3 ESSLRAQKLPVLEVENLAVSLPpggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLG 82
Cdd:TIGR02857 311 KAPVTAAPASSLEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD----PTEGSIAVNG 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 83 MDLFRRTPDEIRRlrgaKMAMVFQEPM-----TALNPVMTCGDQMDELLRAHVpmgpyeRRIRILDLFEEVRLPDPPRIF 157
Cdd:TIGR02857 384 VPLADADADSWRD----QIAWVPQHPFlfagtIAENIRLARPDASDAEIREAL------ERAGLDEFVAALPQGLDTPIG 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 158 RSyPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqkKNGTAVLFITHDFGVVsEIADQVVVL 237
Cdd:TIGR02857 454 EG-GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL--AQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
163-515 |
2.18e-25 |
|
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: 110.26 E-value: 2.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVL--ELG 240
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEE-GKYVLVVEHDLAILDYLADYVHILygEPG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 241 kqietgpAKSVLQHPKEpyTQKLINA-----VPELKPRHRP-----------PVDGNPTLLEAKNVVKTYtlGGFftgRV 304
Cdd:COG1245 291 -------VYGVVSKPKS--VRVGINQyldgyLPEENVRIRDepiefevhaprREKEEETLVEYPDLTKSY--GGF---SL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRAlkgvsARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVwvngenvaaapkrklhglRRRLQVVFQDPYRSLD 384
Cdd:COG1245 357 EVEG-----GEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------------------DEDLKISYKPQYISPD 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 385 PRMTVgESIVEG--PVNFGVPKEEAwkraqEFMKIVRLSPdALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSAL 462
Cdd:COG1245 414 YDGTV-EEFLRSanTDDFGSSYYKT-----EIIKPLGLEK-LLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHL 486
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 463 DVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIrRGECVESGH 515
Cdd:COG1245 487 DVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVF-EGEPGVHGH 538
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-252 |
2.19e-25 |
|
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: 105.17 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADG-SVKLLGMDLFRRTP 90
Cdd:COG1119 2 PLLELRNVTVRR---GGKT-ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP----PTYGnDVRLFGERRGGEDV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLRG---AKMAMVFQEPMTALNPVMT-----------CGDQMDEllRAHvpmgpyerriRILDLFEEVRLPDppri 156
Cdd:COG1119 74 WELRKRIGlvsPALQLRFPRDETVLDVVLSgffdsiglyrePTDEQRE--RAR----------ELLELLGLAHLAD---- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 157 fRSYpHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfgvVSEIAD---Q 233
Cdd:COG1119 138 -RPF-GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIPPgitH 212
|
250
....*....|....*....
gi 2486247945 234 VVVLELGKQIETGPAKSVL 252
Cdd:COG1119 213 VLLLKDGRVVAAGPKEEVL 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
282-520 |
2.24e-25 |
|
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: 104.78 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 282 PTLLEAKNVvkTYTLGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSG-EVWV-----NGE 355
Cdd:COG1119 1 DPLLELRNV--TVRRGG-------KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 356 NVAAapkrklhgLRRRLQVVFQDPYRSLDPRMTVGESIVEGPvnFGV------PKEEAWKRAQEFMKIVRLSPDAlNRYP 429
Cdd:COG1119 72 DVWE--------LRKRIGLVSPALQLRFPRDETVLDVVLSGF--FDSiglyrePTDEQRERARELLELLGLAHLA-DRPF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 430 NQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:COG1119 141 GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
250
....*....|.
gi 2486247945 510 CVESGHVQDVF 520
Cdd:COG1119 221 VVAAGPKEEVL 231
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
26-246 |
2.67e-25 |
|
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: 104.23 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 26 GGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRRlrgaKMAMVF 105
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRR----QIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 106 QEPM----TALNPVM--TCGDQMDELLRAhvpmgpyeRRIRILDLFEEvRLPDpprifrSYPH-------QLSGGQRQRI 172
Cdd:cd03251 83 QDVFlfndTVAENIAygRPGATREEVEEA--------ARAANAHEFIM-ELPE------GYDTvigergvKLSGGQRQRI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVsEIADQVVVLELGKQIETG 246
Cdd:cd03251 148 AIARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTI-ENADRIVVLEDGKIVERG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-271 |
2.92e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 105.96 E-value: 2.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLfrrTPDE 92
Cdd:COG4152 1 MLELKGLTKRF---GDKT-AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGIL----APDSGEVLWDGEPL---DPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRL------RGakmamvfqepmtaLNPVMTCGDQMDELLRAHvPMGPYERRIRILDLFEEVRLPDpprifrsYPH---- 162
Cdd:COG4152 70 RRRIgylpeeRG-------------LYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGD-------RANkkve 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTAL---NVTTqasILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLEL 239
Cdd:COG4152 129 ELSKGNQQKVQLIAALLHDPELLILDEPFSGLdpvNVEL---LKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINK 204
|
250 260 270
....*....|....*....|....*....|...
gi 2486247945 240 GKQIETGPAKSVL-QHPKEPYTQKLINAVPELK 271
Cdd:COG4152 205 GRKVLSGSVDEIRrQFGRNTLRLEADGDAGWLR 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
37-258 |
3.62e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 103.68 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 37 SFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEirrlRgaKMAMVFQEpmTALNPVM 116
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLP----PDSGRILWNGQDLTALPPAE----R--PVSMLFQE--NNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 117 TCGDQMDELLRAHVPMGPYERRiRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNV 196
Cdd:COG3840 87 TVAQNIGLGLRPGLKLTAEQRA-QVEQALERVGLAG---LLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 197 TTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEP 258
Cdd:COG3840 163 ALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPP 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
306-519 |
4.37e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 107.62 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 306 VRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKlhgLRRRLQVVFQDPYRSLDP 385
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA---ASRRVASVPQDTSLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 386 RmtvGESIVE---GP--VNFGvPKEEAWKRAQEfMKIVRLSPDAL-NRYPNQFSGGQRQRISIARALACEPEILICDEAV 459
Cdd:PRK09536 93 D---VRQVVEmgrTPhrSRFD-TWTETDRAAVE-RAMERTGVAQFaDRPVTSLSGGERQRVLLARALAQATPVLLLDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 460 SALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDV 519
Cdd:PRK09536 168 ASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-254 |
5.02e-25 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 109.07 E-value: 5.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSlPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDE- 92
Cdd:COG4618 331 LSVENLTVV-PPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP----PTAGSVRLDGADLSQWDREEl 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 ---------------------IRRLRGAKMAMVFQEPMTAlnpvmtcgdQMDELlrahvpmgpyerrirILdlfeevRLP 151
Cdd:COG4618 405 grhigylpqdvelfdgtiaenIARFGDADPEKVVAAAKLA---------GVHEM---------------IL------RLP 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 152 DpprifrSY-------PHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDF 224
Cdd:COG4618 455 D------GYdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRP 527
|
250 260 270
....*....|....*....|....*....|
gi 2486247945 225 GVVSeIADQVVVLELGKQIETGPAKSVLQH 254
Cdd:COG4618 528 SLLA-AVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
26-241 |
6.63e-25 |
|
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: 102.97 E-value: 6.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 26 GGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfRRTPDEIRRlrgaKMAMVF 105
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELR----PTSGTAYINGYSI-RTDRKAARQ----SLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 106 QEpmTALNPVMTCgdqmDELLRAHVPM-GPYERRIR--ILDLFEEVRLPDppriFR-SYPHQLSGGQRQRIVIAMALLLK 181
Cdd:cd03263 82 QF--DALFDELTV----REHLRFYARLkGLPKSEIKeeVELLLRVLGLTD----KAnKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 182 PDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGK 209
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
309-520 |
6.89e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 104.32 E-value: 6.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAApKRKLHGLRRRLQVVFQDP-----YRSL 383
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYS-KRGLLALRQQVATVFQDPeqqifYTDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 384 DprmtvgESIVEGPVNFGVPKEEAWKRAQEFMKIVrlspDA--LNRYPNQ-FSGGQRQRISIARALACEPEILICDEAVS 460
Cdd:PRK13638 96 D------SDIAFSLRNLGVPEAEITRRVDEALTLV----DAqhFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 461 ALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRI-VAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
14-282 |
7.35e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.56 E-value: 7.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRpNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEI 93
Cdd:PRK11231 3 LRTENLTVGY---GTK-RILNDLSLSLPTGKITALIGPNGCGKS----TLLKCFARLLTPQSGTVFLGDKPISMLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPMT------------ALNPVMTCGDQMDELLRAHVPMGPYERRIrilDLFEEVRLPDpprifrsyp 161
Cdd:PRK11231 75 AR----RLALLPQHHLTpegitvrelvayGRSPWLSLWGRLSAEDNARVNQAMEQTRI---NHLADRRLTD--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 162 hqLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQkKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:PRK11231 139 --LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2486247945 242 QIETGPaksvlqhPKEPYTQKLINAVPELKPR-HRPPVDGNP 282
Cdd:PRK11231 216 VMAQGT-------PEEVMTPGLLRTVFDVEAEiHPEPVSGTP 250
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
48-264 |
8.20e-25 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 105.27 E-value: 8.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 48 LIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDeirrLRGakMAMVFQEpmTALNPVMTC------GDQ 121
Cdd:TIGR01187 1 LLGPSGCGKT----TLLRLLAGFEQPDSGSIMLDGEDVTNVPPH----LRH--INMVFQS--YALFPHMTVeenvafGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 122 MDELLRAhvpmgpyERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQAS 201
Cdd:TIGR01187 69 MRKVPRA-------EIKPRVLEALRLVQLEE---FADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQ 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 202 ILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLI 264
Cdd:TIGR01187 139 MQLELKTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
14-246 |
8.67e-25 |
|
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: 102.45 E-value: 8.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLfRRTPDEI 93
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL----EPDAGFATVDGFDV-VKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEpmTALNPVMTCGDQMDELLRAHvPMGPYERRIRILDLFEEVRLPDppriFRSYP-HQLSGGQRQRI 172
Cdd:cd03266 77 RR----RLGFVSDS--TGLYDRLTARENLEYFAGLY-GLKGDELTARLEELADRLGMEE----LLDRRvGGFSTGMRQKV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
32-246 |
8.78e-25 |
|
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: 102.80 E-value: 8.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRRlrgakMAMVF-QEPMT 110
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKT----TTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-----IGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALN-PVMtcgDQMdELLRA--HVPMGPYERRI-RILDLFEEVRLPDPPrifrsyPHQLSGGQRQRIVIAMALLLKPDLLI 186
Cdd:cd03267 107 WWDlPVI---DSF-YLLAAiyDLPPARFKKRLdELSELLDLEELLDTP------VRQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 187 CDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
308-514 |
9.14e-25 |
|
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: 102.28 E-value: 9.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVaaapkRKLH--GLRRRLQVVFQDP---YRS 382
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-----RQLDpaDLRRNIGYVPQDVtlfYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 383 LDPRMTVGESIVEgpvnfgvpkeeawkrAQEFMKIVRLS--PDALNRYPNQF-----------SGGQRQRISIARALACE 449
Cdd:cd03245 94 LRDNITLGAPLAD---------------DERILRAAELAgvTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 450 PEILICDEAVSALDVSVQADILKLLEeiQVKLGIGILFVTHDLRVAsQICDDVIVIRRGECVESG 514
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLR--QLLGDKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
309-514 |
1.01e-24 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 108.37 E-value: 1.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPkrkLHGLRRRLQVVFQDPyrSL--Dpr 386
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT---QASLRAAIGIVPQDT--VLfnD-- 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 mTVGESIVEGpvNFGVPKEE---AWKRAQ--EFmkIVRLspdalnryPNQF-----------SGGQRQRISIARALACEP 450
Cdd:COG5265 447 -TIAYNIAYG--RPDASEEEveaAARAAQihDF--IESL--------PDGYdtrvgerglklSGGEKQRVAIARTLLKNP 513
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 451 EILICDEAVSALDVSVQADILKLLEEiqVKLGIGILFVTHDLrvaSQI--CDDVIVIRRGECVESG 514
Cdd:COG5265 514 PILIFDEATSALDSRTERAIQAALRE--VARGRTTLVIAHRL---STIvdADEILVLEAGRIVERG 574
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-247 |
1.17e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.78 E-value: 1.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 31 NAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRtpdEIRRLRgaKMAMVF-QEpm 109
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKS----TTIKMLTGILVPTSGEVRVLGYVPFKR---RKEFAR--RIGVVFgQR-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 110 TALN---PVMtcgdqmD--ELLRA--HVPMGPYERRIR----ILDLfEE-----VRlpdpprifrsyphQLSGGQRQRIV 173
Cdd:COG4586 105 SQLWwdlPAI------DsfRLLKAiyRIPDAEYKKRLDelveLLDL-GElldtpVR-------------QLSLGQRMRCE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGP 247
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
14-271 |
1.63e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.59 E-value: 1.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGD-RPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPD- 91
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL----KPTSGKIIIDGVDITDKKVKl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 -EIRRlrgaKMAMVFQEPMTALnpvmtcgdqMDELLRAHVPMGPY-------ERRIRILDLFEEVRLPDPPRIFRSyPHQ 163
Cdd:PRK13637 79 sDIRK----KVGLVFQYPEYQL---------FEETIEKDIAFGPInlglseeEIENRVKRAMNIVGLDYEDYKDKS-PFE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQI 243
Cdd:PRK13637 145 LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCE 224
|
250 260
....*....|....*....|....*....
gi 2486247945 244 ETGPAKSVLqhpKEPYTQKLIN-AVPELK 271
Cdd:PRK13637 225 LQGTPREVF---KEVETLESIGlAVPQVT 250
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
32-246 |
1.69e-24 |
|
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: 101.56 E-value: 1.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEirrlRGakMAMVFQEpmTA 111
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEE----PTSGRIYIGGRDVTDLPPKD----RD--IAMVFQN--YA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQMDELLR-AHVPMGPYERRIRildlfEEVRLPDPPRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEP 190
Cdd:cd03301 83 LYPHMTVYDNIAFGLKlRKVPKDEIDERVR-----EVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 191 TTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
36-241 |
1.72e-24 |
|
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: 101.60 E-value: 1.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEgEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRR-----TPDEIRRLrgakmAMVFQEpmT 110
Cdd:cd03297 17 IDFDLNE-EVTGIFGASGAGKSTLLRCIAGLE----KPDGGTIVLNGTVLFDSrkkinLPPQQRKI-----GLVFQQ--Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALNPVMTCGDQMDELLRAHVPMgpyERRIR---ILDLFeevrlpDPPRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLIC 187
Cdd:cd03297 85 ALFPHLNVRENLAFGLKRKRNR---EDRISvdeLLDLL------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 188 DEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
12-237 |
1.87e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVslpPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPD 91
Cdd:COG3845 256 VVLEVENLSV---RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP----PASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRlrgAKMAMVFQEPM-TALNPVMTCGDQMdeLLRAHVPmGPYERRIRI---------LDLFEE--VRLPDPPRIFRS 159
Cdd:COG3845 329 ERRR---LGVAYIPEDRLgRGLVPDMSVAENL--ILGRYRR-PPFSRGGFLdrkairafaEELIEEfdVRTPGPDTPARS 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 160 yphqLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVL 237
Cdd:COG3845 403 ----LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVM 475
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
285-514 |
2.05e-24 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 107.03 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggfftGRvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapKRK 364
Cdd:PRK11176 342 IEFRNVTFTYP------GK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR---DYT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDPYRSLDprmTVGESIVegpvnfgVPKEEAWKRAqEFMKIVRLS--PDALNRYPNQF---------- 432
Cdd:PRK11176 412 LASLRNQVALVSQNVHLFND---TIANNIA-------YARTEQYSRE-QIEEAARMAyaMDFINKMDNGLdtvigengvl 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 433 -SGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLgiGILFVTHDLrvaSQI--CDDVIVIRRGE 509
Cdd:PRK11176 481 lSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRL---STIekADEILVVEDGE 555
|
....*
gi 2486247945 510 CVESG 514
Cdd:PRK11176 556 IVERG 560
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
263-517 |
2.30e-24 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 107.11 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 263 LINAVPELKP--RHRPPVDGnptLLEAKNVVKTYTLGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIA 340
Cdd:TIGR02203 310 LLDSPPEKDTgtRAIERARG---DVEFRNVTFRYPGRD-------RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIP 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 341 RLIDPTSGEVWVNGENVAaapKRKLHGLRRRLQVVFQDPYRSLDprmTVGESIVEGPVNfGVPKE--EAWKRAQEFMKIV 418
Cdd:TIGR02203 380 RFYEPDSGQILLDGHDLA---DYTLASLRRQVALVSQDVVLFND---TIANNIAYGRTE-QADRAeiERALAAAYAQDFV 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 419 RLSPDALNRYPNQ----FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVklGIGILFVTHDLrv 494
Cdd:TIGR02203 453 DKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRL-- 528
|
250 260
....*....|....*....|....*.
gi 2486247945 495 aSQI--CDDVIVIRRGECVESG-HVQ 517
Cdd:TIGR02203 529 -STIekADRIVVMDDGRIVERGtHNE 553
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
12-258 |
2.46e-24 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 102.19 E-value: 2.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDrpNAVEH-VSFTVNEGEVTCLIGESGSGKSviasTV---MGLLPKglaPADGSVKLLGMDL-F 86
Cdd:COG4598 7 PALEVRDLHKSF---GD--LEVLKgVSLTARKGDVISIIGSSGSGKS----TFlrcINLLET---PDSGEIRVGGEEIrL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 87 RRTPD---------EIRRLRgAKMAMVFQE-----PMTALNPVMTCGDQMDELLRAhvpmgpyERRIRILDLFEEVRLPD 152
Cdd:COG4598 75 KPDRDgelvpadrrQLQRIR-TRLGMVFQSfnlwsHMTVLENVIEAPVHVLGRPKA-------EAIERAEALLAKVGLAD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 153 ppriFR-SYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVSEIA 231
Cdd:COG4598 147 ----KRdAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLV-VTHEMGFARDVS 221
|
250 260
....*....|....*....|....*..
gi 2486247945 232 DQVVVLELGKQIETGPAKSVLQHPKEP 258
Cdd:COG4598 222 SHVVFLHQGRIEEQGPPAEVFGNPKSE 248
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
310-524 |
2.51e-24 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 104.19 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 310 KGVSArlrrgetigIVGESGSGKSTFARSIARLIDPTSGEVWVNG-------ENVAAAPKRklhglrRRLQVVFQDPyrS 382
Cdd:PRK11144 24 QGITA---------IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPPEK------RRIGYVFQDA--R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 383 LDPRMTVgesivEGPVNFGVPKeeawKRAQEFMKIVRL--SPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVS 460
Cdd:PRK11144 87 LFPHYKV-----RGNLRYGMAK----SMVAQFDKIVALlgIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 461 ALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQ 524
Cdd:PRK11144 158 SLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
309-509 |
2.58e-24 |
|
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: 99.60 E-value: 2.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAApkrKLHGLRRRLQVVFQDpyrsldprmt 388
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELGDHVGYLPQD---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 vgesivegpvnfgvpkeeawkraqefmkiVRLSPDALNRypNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQA 468
Cdd:cd03246 85 -----------------------------DELFSGSIAE--NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2486247945 469 DILKLLEEIQVKlGIGILFVTHDLRVASQiCDDVIVIRRGE 509
Cdd:cd03246 134 ALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
13-294 |
2.61e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.46 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDrpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLG--MDLFRRTP 90
Cdd:PRK13639 1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGIL----KPTSGEVLIKGepIKYDKKSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRlrgaKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRilDLFEEVRLPDpprIFRSYPHQLSGGQRQ 170
Cdd:PRK13639 74 LEVRK----TVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVK--EALKAVGMEG---FENKPPHHLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 171 RIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKS 250
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 251 VLQHPKE--------PYTQKLINavpELKPRHRPPVDGNPTLLEAKNVVKTY 294
Cdd:PRK13639 224 VFSDIETirkanlrlPRVAHLIE---ILNKEDNLPIKMGYTIGEARRNIKEL 272
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
9-252 |
4.27e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 105.65 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 9 QKLPVLEVENLA---VSLPPGGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVK-LLG-- 82
Cdd:TIGR03269 275 VGEPIIKVRNVSkryISVDRGVVK--AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE----PTSGEVNvRVGde 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 83 -MDLFRRTPDEirRLRGAK-MAMVFQEpmTALNPVMTCGDQMDELLRAHVPmGPYERRIRILDL----FEEVRLPDpprI 156
Cdd:TIGR03269 349 wVDMTKPGPDG--RGRAKRyIGILHQE--YDLYPHRTVLDNLTEAIGLELP-DELARMKAVITLkmvgFDEEKAEE---I 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 157 FRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVV 236
Cdd:TIGR03269 421 LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAAL 500
|
250
....*....|....*.
gi 2486247945 237 LELGKQIETGPAKSVL 252
Cdd:TIGR03269 501 MRDGKIVKIGDPEEIV 516
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-264 |
4.41e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 101.66 E-value: 4.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 33 VEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLP--KGLAPADGSVKLLGMDLFRRTPDEIRRlrgaKMAMVFQEPMT 110
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiyDSKIKVDGKVLYFGKDIFQIDAIKLRK----EVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 AlnPVMTCGDQMDELLRAHvpmGPYERR---------IRILDLFEEV--RLPDPPRifrsyphQLSGGQRQRIVIAMALL 179
Cdd:PRK14246 102 F--PHLSIYDNIAYPLKSH---GIKEKReikkiveecLRKVGLWKEVydRLNSPAS-------QLSGGQQQRLTIARALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 180 LKPDLLICDEPTTALNVTTQASILKLILELqkKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPY 259
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNEL 247
|
....*
gi 2486247945 260 TQKLI 264
Cdd:PRK14246 248 TEKYV 252
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-276 |
5.16e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.74 E-value: 5.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPpggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDE 92
Cdd:PRK13647 4 IIEVEDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY----LPQRGRVKVMGREVNAENEKW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRrlrgAKMAMVFQEP------MTALNPVmTCGDQMDELLRAHVpmgpyERRIRilDLFEEVRLPDppriFRSY-PHQLS 165
Cdd:PRK13647 77 VR----SKVGLVFQDPddqvfsSTVWDDV-AFGPVNMGLDKDEV-----ERRVE--EALKAVRMWD----FRDKpPYHLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKlILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIET 245
Cdd:PRK13647 141 YGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME-ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAE 219
|
250 260 270
....*....|....*....|....*....|....*....
gi 2486247945 246 GpAKSVLQHP--------KEPYTQKLINAVPELKPRHRP 276
Cdd:PRK13647 220 G-DKSLLTDEdiveqaglRLPLVAQIFEDLPELGQSKLP 257
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
35-258 |
5.24e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 100.94 E-value: 5.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 35 HVSFTVNEGEVTCLIGESGSGKSVIA------STVMG--LLPKGLAPADGSVKLlgmdlfrrtpDEIRRLRGakmaMVFQ 106
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLrcinklEEITSgdLIVDGLKVNDPKVDE----------RLIRQEAG----MVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 107 E----P-MTALNPVMTCGDQMDELLRAhvpmgpyERRIRILDLFEEVRLPDpprifRS--YPHQLSGGQRQRIVIAMALL 179
Cdd:PRK09493 85 QfylfPhLTALENVMFGPLRVRGASKE-------EAEKQARELLAKVGLAE-----RAhhYPSELSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 180 LKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEP 258
Cdd:PRK09493 153 VKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQ 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
36-265 |
5.41e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.98 E-value: 5.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTvMGLLPKglaPADGSVKLLGMDL-----FRRTPDEIRRLRgAKMAMVFQEpmT 110
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRC-INLLEQ---PEAGTIRVGDITIdtarsLSQQKGLIRQLR-QHVGFVFQN--F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALNPVMTCGDQMDE--LLRAHVPMGPYERRIRilDLFEEVRLPDPPRifrSYPHQLSGGQRQRIVIAMALLLKPDLLICD 188
Cdd:PRK11264 95 NLFPHRTVLENIIEgpVIVKGEPKEEATARAR--ELLAKVGLAGKET---SYPRRLSGGQQQRVAIARALAMRPEVILFD 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 189 EPTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLIN 265
Cdd:PRK11264 170 EPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
36-272 |
6.48e-24 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 103.15 E-value: 6.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTVMGLL-PKGLApadGSVKLLGMDLFRRTPDEirrlRGakMAMVFQEpmTALNP 114
Cdd:TIGR03258 24 LSLEIEAGELLALIGKSGCGKTTLLRAIAGFVkAAGLT---GRIAIADRDLTHAPPHK----RG--LALLFQN--YALFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 115 VMTCGDQMDELLRAHvPMGPYERRIRILDLFEEVRLPDPPRifrSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTAL 194
Cdd:TIGR03258 93 HLKVEDNVAFGLRAQ-KMPKADIAERVADALKLVGLGDAAA---HLPAQLSGGMQQRIAIARAIAIEPDVLLLDEPLSAL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 195 NVTTQASILKLILELQKK-NGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLINAVPELKP 272
Cdd:TIGR03258 169 DANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANILPA 247
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
33-256 |
7.36e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.88 E-value: 7.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 33 VEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTpdeirrLRGAKMAMVFQEpmTAL 112
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLE----KPTEGQIFIDGEDVTHRS------IQQRDICMVFQS--YAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 113 NPVMTCGDQMDELLRAH-VPMGpyERRIRILDLFEEVRLPDppriFRS-YPHQLSGGQRQRIVIAMALLLKPDLLICDEP 190
Cdd:PRK11432 90 FPHMSLGENVGYGLKMLgVPKE--ERKQRVKEALELVDLAG----FEDrYVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 191 TTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPK 256
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
32-293 |
7.54e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 7.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKL----------LGMDLFRRTPDEIR---RLRg 98
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLI----KSKYGTIQVgdiyigdkknNHELITNPYSKKIKnfkELR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 99 AKMAMVFQEPMTALNPVMTCGDQMdellRAHVPMGPYERRIRILDLFEEVRLP-DPPRIFRSyPHQLSGGQRQRIVIAMA 177
Cdd:PRK13631 116 RRVSMVFQFPEYQLFKDTIEKDIM----FGPVALGVKKSEAKKLAKFYLNKMGlDDSYLERS-PFGLSGGQKRRVAIAGI 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 178 LLLKPDLLICDEPTTALNVTTQASILKLILElQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPA------KSV 251
Cdd:PRK13631 191 LAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPyeiftdQHI 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2486247945 252 LQHPK--EPYTQKLINAVPELKPRHRPPVDGNPTLLE--AKNVVKT 293
Cdd:PRK13631 270 INSTSiqVPRVIQVINDLIKKDPKYKKLYQKQPRTIEqlADAINEF 315
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
307-509 |
7.77e-24 |
|
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: 98.66 E-value: 7.77e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhgLRRRLQVVFQDPYRS-LDP 385
Cdd:cd03215 14 GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA--IRAGIAYVPEDRKREgLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 386 RMTVGESIVegpvnfgvpkeeawkraqefmkivrlspdalnrYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVS 465
Cdd:cd03215 92 DLSVAENIA---------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2486247945 466 VQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd03215 139 AKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGR 181
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
319-519 |
8.37e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.83 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 319 GETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhglRRRLQVVFQDPYRSLDprMTVGESIVEG-- 396
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV---ARRIGLLAQNATTPGD--ITVQELVARGry 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 397 ---PV--NFGVPKEEAWKRAQEFMKIVRLSPDALNrypnQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADIL 471
Cdd:PRK10253 108 phqPLftRWRKEDEEAVTKAMQATGITHLADQSVD----TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2486247945 472 KLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDV 519
Cdd:PRK10253 184 ELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
307-520 |
9.44e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 9.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhglRRRLQVVFQDPyrsLDPR 386
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL---ARRLALLPQHH---LTPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 -MTVGESIVEG--PVN--FGVPKEEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISIARALACEPEILICDEAVSA 461
Cdd:PRK11231 90 gITVRELVAYGrsPWLslWGRLSAEDNARVNQAMEQTRINHLA-DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 462 LDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVF 520
Cdd:PRK11231 169 LDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
309-514 |
1.64e-23 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 104.64 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhglRRRLQVVFQDPyrsldprmt 388
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVL---ANSVAMVDQDI--------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 vgeSIVEGPV--NFGVpkeeaWKRAQEFMKIVRLSPDA-----LNRYPNQ-----------FSGGQRQRISIARALACEP 450
Cdd:TIGR03796 563 ---FLFEGTVrdNLTL-----WDPTIPDADLVRACKDAaihdvITSRPGGydaelaegganLSGGQRQRLEIARALVRNP 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 451 EILICDEAVSALDVSVQADILKLLEeiqvKLGIGILFVTHDLrvaSQI--CDDVIVIRRGECVESG 514
Cdd:TIGR03796 635 SILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRL---STIrdCDEIIVLERGKVVQRG 693
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-241 |
1.97e-23 |
|
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: 98.63 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGgdrPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKS----TLLKLIYKEELPTSGTIRVNGQDVSDLRGRAI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRgAKMAMVFQEpmTALNPVMTCGDQMDELLRAhVPMGPYERRIRILDLFEEVRLPDPPRifrSYPHQLSGGQRQRIV 173
Cdd:cd03292 74 PYLR-RKIGVVFQD--FRLLPDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGLSHKHR---ALPAELSGGEQQRVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLiLELQKKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNL-LKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
308-514 |
2.07e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 98.75 E-value: 2.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhgLRRRLQVVFQDpyRSLDPRM 387
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHER--ARAGIAYVPQG--REIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRlspDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQ 467
Cdd:TIGR03410 91 TVEENLLTGLAALPRRSRKIPDEIYELFPVLK---EMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSII 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2486247945 468 ADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:TIGR03410 168 KDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
32-264 |
2.36e-23 |
|
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: 98.85 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDEirrlRGakMAMVFQEpmTA 111
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFE----TPTSGEILLDGKDITNLPPHK----RP--VNTVFQN--YA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQMDELLRAHvPMGPYERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPT 191
Cdd:cd03300 83 LFPHLTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLEG---YANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 192 TALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLI 264
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
7-254 |
2.85e-23 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 103.58 E-value: 2.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 7 RAQKLP----VLEVENLAVsLPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLG 82
Cdd:TIGR01842 306 PAMPLPepegHLSVENVTI-VPPGGKKP-TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWP----PTSGSVRLDG 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 83 MDLFRRTPDEIRRLRGAKMAMVFQEPMTALNPVMTCGDQMD--ELLRAHVPMGPYERRIRILDLFEEVRLPDPPrifrsy 160
Cdd:TIGR01842 380 ADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADpeKIIEAAKLAGVHELILRLPDGYDTVIGPGGA------ 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 161 phQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTaVLFITHDFGVVsEIADQVVVLELG 240
Cdd:TIGR01842 454 --TLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGIT-VVVITHRPSLL-GCVDKILVLQDG 529
|
250
....*....|....
gi 2486247945 241 KQIETGPAKSVLQH 254
Cdd:TIGR01842 530 RIARFGERDEVLAK 543
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
13-223 |
3.64e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 97.93 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDE 92
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKS----TLLAILAGLDDGSSGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRGAKMAMVFQEPMtaLNPVMTCGD--QMDELLRAhvpMGPYERRIRILDLFEEVRLPdppRIFRSYPHQLSGGQRQ 170
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFM--LIPTLNALEnvELPALLRG---ESSRQSRNGAKALLEQLGLG---KRLDHLPAQLSGGEQQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 171 RIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHD 223
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
278-537 |
3.95e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.40 E-value: 3.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 278 VDGNPTLLEAKNVvktyTLGgfFTGRVkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSG-----EVWV 352
Cdd:PRK14271 15 VDAAAPAMAAVNL----TLG--FAGKT---VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 353 NGENVAAApkRKLHGLRRRLQVVFQDPyrslDP-RMTVGESIVEG-PVNFGVPKEEAWKRAQEFMKIVRL---SPDALNR 427
Cdd:PRK14271 86 GGRSIFNY--RDVLEFRRRVGMLFQRP----NPfPMSIMDNVLAGvRAHKLVPRKEFRGVAQARLTEVGLwdaVKDRLSD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 428 YPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLgiGILFVTHDLRVASQICDDVIVIRR 507
Cdd:PRK14271 160 SPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFD 237
|
250 260 270
....*....|....*....|....*....|
gi 2486247945 508 GECVESGHVQDVFFHPQHEYTKSLIAAAPG 537
Cdd:PRK14271 238 GRLVEEGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
280-509 |
4.11e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.60 E-value: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 280 GNPTLLEakNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVngenvAA 359
Cdd:PRK11247 10 GTPLLLN--AVSKRY-------GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLA-----GT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 360 APkrkLHGLRRRLQVVFQDPyrsldpRMTVGESIVEgpvNFGVPKEEAWK-RAQEFMKIVRLSPDAlNRYPNQFSGGQRQ 438
Cdd:PRK11247 74 AP---LAEAREDTRLMFQDA------RLLPWKKVID---NVGLGLKGQWRdAALQALAAVGLADRA-NEWPAALSGGQKQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 439 RISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:PRK11247 141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
305-514 |
4.33e-23 |
|
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: 97.73 E-value: 4.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDP---TSGEVWVNGEnvaaapKRKLHGLRRRLQVVFQDPYr 381
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQ------PRKPDQFQKCVAYVRQDDI- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 382 sLDPRMTVGESIVEGpVNFGVPKEEAWKRAQEFMKIVRLSPDAL----NRYPNQFSGGQRQRISIARALACEPEILICDE 457
Cdd:cd03234 92 -LLPGLTVRETLTYT-AILRLPRKSSDAIRKKRVEDVLLRDLALtrigGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 458 AVSALDVSVQADILKLLEEIQVKlGIGILFVTHDLRV-ASQICDDVIVIRRGECVESG 514
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQPRSdLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
281-509 |
5.30e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 102.31 E-value: 5.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVVKTYtlGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARsIARLIDPT---SGEVWVNGENV 357
Cdd:PRK13549 2 MEYLLEMKNITKTF--GG-------VKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEIIFEGEEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 358 AAAPKRKLHglRRRLQVVFQDpyRSLDPRMTVGESIVEG--PVNFGVPKEEA-WKRAQEFMKIVRLSPDALNRYPNqFSG 434
Cdd:PRK13549 72 QASNIRDTE--RAGIAIIHQE--LALVKELSVLENIFLGneITPGGIMDYDAmYLRAQKLLAQLKLDINPATPVGN-LGL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 435 GQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
307-495 |
5.49e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.23 E-value: 5.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAApkrklhGLRRrlQVVFQDpyRSLDPR 386
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP------GAER--GVVFQN--EGLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 MTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSV 466
Cdd:PRK11248 85 RNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFT 163
|
170 180
....*....|....*....|....*....
gi 2486247945 467 QADILKLLEEIQVKLGIGILFVTHDLRVA 495
Cdd:PRK11248 164 REQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
12-264 |
6.48e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.92 E-value: 6.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTV--MG-LLPKglAPADGSVKLLGMDLFRR 88
Cdd:PRK14239 4 PILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNdLNPE--VTITGSIVYNGHNIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 89 TPD--EIRRlrgaKMAMVFQEPmtalNPV-MTCGDQMDELLR------AHVPMGPYERRIRILDLFEEV--RLPDPPRif 157
Cdd:PRK14239 78 RTDtvDLRK----EIGMVFQQP----NPFpMSIYENVVYGLRlkgikdKQVLDEAVEKSLKGASIWDEVkdRLHDSAL-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 158 rsyphQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKngTAVLFITHDFGVVSEIADQVVVL 237
Cdd:PRK14239 148 -----GLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFF 220
|
250 260
....*....|....*....|....*..
gi 2486247945 238 ELGKQIETGPAKSVLQHPKEPYTQKLI 264
Cdd:PRK14239 221 LDGDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
12-234 |
8.51e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 97.19 E-value: 8.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPD 91
Cdd:PRK11629 4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKS----TLLHLLGGLDTPTSGDVIFNGQPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRGAKMAMVFQ-----EPMTALNPVMTcgdqmdELLRAHVPmgPYERRIRILDLFEEVRLPDpprifRSY--PHQL 164
Cdd:PRK11629 80 AKAELRNQKLGFIYQfhhllPDFTALENVAM------PLLIGKKK--PAEINSRALEMLAAVGLEH-----RANhrPSEL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 165 SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQV 234
Cdd:PRK11629 147 SGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL 216
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
13-249 |
9.27e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 98.24 E-value: 9.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapADGSVKLLGMdlfRRTPDE 92
Cdd:PRK13642 4 ILEVENLVFKYEKESD-VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE----FEGKVKIDGE---LLTAEN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRgAKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIrildlfEEVRLPDPPRIFRSY-PHQLSGGQRQR 171
Cdd:PRK13642 76 VWNLR-RKIGMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRV------DEALLAVNMLDFKTRePARLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 172 IVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEiADQVVVLELGKQI-ETGPAK 249
Cdd:PRK13642 149 VAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIkEAAPSE 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-263 |
9.31e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 98.36 E-value: 9.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 33 VEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDE-IRRLRgAKMAMVFQEPMTA 111
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALL----KPSSGTITIAGYHITPETGNKnLKKLR-KKVSLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LnpvmtcgdqMDELLRAHVPMGPY-------ERRIRILDLFEEVRLPDppRIFRSYPHQLSGGQRQRIVIAMALLLKPDL 184
Cdd:PRK13641 98 L---------FENTVLKDVEFGPKnfgfsedEAKEKALKWLKKVGLSE--DLISKSPFELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 185 LICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPK-------- 256
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwlkkhyld 245
|
....*..
gi 2486247945 257 EPYTQKL 263
Cdd:PRK13641 246 EPATSRF 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
284-511 |
9.80e-23 |
|
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: 101.44 E-value: 9.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYtlGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARsIARLIDPT---SGEVWVNGENVAAA 360
Cdd:TIGR02633 1 LLEMKGIVKTF--GG-------VKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwDGEIYWSGSPLKAS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 PKRKLHglRRRLQVVFQDpyRSLDPRMTVGESIVEG---PVNFGVPKEEA-WKRAQEFMKIVRLSPDALNRYPNQFSGGQ 436
Cdd:TIGR02633 71 NIRDTE--RAGIVIIHQE--LTLVPELSVAENIFLGneiTLPGGRMAYNAmYLRAKNLLRELQLDADNVTRPVGDYGGGQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 437 RQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECV 511
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
307-534 |
1.22e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.41 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLiDPTSGEVWVNGE----NVAAAPKR-KLHGLRRRLQVVFQDPyr 381
Cdd:PRK14258 21 KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGRveffNQNIYERRvNLNRLRRQVSMVHPKP-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 382 SLDPrMTVGESIVEGPVNFG-VPK-------EEAWKRAQEFMKIvrlsPDALNRYPNQFSGGQRQRISIARALACEPEIL 453
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIVGwRPKleiddivESALKDADLWDEI----KHKIHKSALDLSGGQQQRLCIARALAVKPKVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 454 ICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVI-----RRGECVESGHVQDVFFHPQHEYT 528
Cdd:PRK14258 173 LMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKKIFNSPHDSRT 252
|
....*.
gi 2486247945 529 KSLIAA 534
Cdd:PRK14258 253 REYVLS 258
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
32-508 |
1.35e-22 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 100.96 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGlapaDGSVKLLGMDLFRRTPDEIRRlrgAKMAMVFQEpmta 111
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD----SGSILFQGKEIDFKSSKEALE---NGISMVHQE---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCgDQMDELLRAHVPM-GPYERRIRILD----LFEEVRLPDPPRIFRSyphQLSGGQRQRIVIAMALLLKPDLLI 186
Cdd:PRK10982 82 LNLVLQR-SVMDNMWLGRYPTkGMFVDQDKMYRdtkaIFDELDIDIDPRAKVA---TLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 187 CDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVlqhpkepyTQKLINA 266
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL--------TMDKIIA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 267 V---PELKPRHrPPVDGNP--TLLEAKNVVKtytlggfftgrVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIAR 341
Cdd:PRK10982 229 MmvgRSLTQRF-PDKENKPgeVILEVRNLTS-----------LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 342 LIDPTSGEVWVNGENVA--------------AAPKRKLHGLRRRLQVVFQDPYRSLDPRMTvgesivegpvNFGVPKEEA 407
Cdd:PRK10982 297 IREKSAGTITLHGKKINnhnaneainhgfalVTEERRSTGIYAYLDIGFNSLISNIRNYKN----------KVGLLDNSR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 408 WKRAQEFMKivrlspDALN-RYPNQ------FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVK 480
Cdd:PRK10982 367 MKSDTQWVI------DSMRvKTPGHrtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAEL-AK 439
|
490 500
....*....|....*....|....*...
gi 2486247945 481 LGIGILFVTHDLRVASQICDDVIVIRRG 508
Cdd:PRK10982 440 KDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
14-251 |
1.36e-22 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 96.44 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEi 93
Cdd:TIGR03410 1 LEVSNLNVYY----GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLP----VKSGSIRLDGEDITKLPPHE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 rRLRgAKMAMVFQEPMtaLNPVMTCgdqMDELLRAHVPMGPYERRI--RILDLFeevrlpdpPrIFRSYPHQ----LSGG 167
Cdd:TIGR03410 72 -RAR-AGIAYVPQGRE--IFPRLTV---EENLLTGLAALPRRSRKIpdEIYELF--------P-VLKEMLGRrggdLSGG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALnvttQASILKLI----LELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQI 243
Cdd:TIGR03410 136 QQQQLAIARALVTRPKLLLLDEPTEGI----QPSIIKDIgrviRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVV 211
|
....*...
gi 2486247945 244 ETGPAKSV 251
Cdd:TIGR03410 212 ASGAGDEL 219
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
264-514 |
1.40e-22 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 101.96 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 264 INAVPELKPRHRPPVDGNPTLLEAKnvvktyTLGGFFTGRVKVR------------ALKGVSARLRRGETIGIVGESGSG 331
Cdd:TIGR03797 418 ILAVIPLWERAKPILEALPEVDEAK------TDPGKLSGAIEVDrvtfryrpdgplILDDVSLQIEPGEFVAIVGPSGSG 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 332 KSTFARSIARLIDPTSGEVWVNGENVAAAPKRklhGLRRRLQVVFQDPyrsldpRMTVG---ESIVEGPVnfgVPKEEAW 408
Cdd:TIGR03797 492 KSTLLRLLLGFETPESGSVFYDGQDLAGLDVQ---AVRRQLGVVLQNG------RLMSGsifENIAGGAP---LTLDEAW 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 409 KRAQE--FMKIVRLSPDALNRYPNQ----FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLg 482
Cdd:TIGR03797 560 EAARMagLAEDIRAMPMGMHTVISEgggtLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR- 638
|
250 260 270
....*....|....*....|....*....|....
gi 2486247945 483 igiLFVTHDLrvaSQI--CDDVIVIRRGECVESG 514
Cdd:TIGR03797 639 ---IVIAHRL---STIrnADRIYVLDAGRVVQQG 666
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
32-254 |
1.63e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 97.51 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPD-EIRRLRgAKMAMVFQEPMT 110
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKS----TIMQLLNGLHVPTQGSVRVDDTLITSTSKNkDIKQIR-KKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALnpvmtcgdqMDELLRAHVPMGPY-------------ERRIRILDLFEEvrlpdpprIFRSYPHQLSGGQRQRIVIAMA 177
Cdd:PRK13649 97 QL---------FEETVLKDVAFGPQnfgvsqeeaealaREKLALVGISES--------LFEKNPFELSGGQMRRVAIAGI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 178 LLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQH 254
Cdd:PRK13649 160 LAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVL-VTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
14-256 |
1.66e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 98.99 E-value: 1.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKS----VIAstvmGLLPkglaPADGSVKLLGMDLFRRT 89
Cdd:COG3839 4 LELENVSKSY---GGVE-ALKDIDLDIEDGEFLVLLGPSGCGKStllrMIA----GLED----PTSGEILIGGRDVTDLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 90 PDEirrlRGakMAMVFQEPmtALNPVMTCGDQMDELLR-AHVPMGPYERRIR----ILDLfEEV--RlpdpprifrsYPH 162
Cdd:COG3839 72 PKD----RN--IAMVFQSY--ALYPHMTVYENIAFPLKlRKVPKAEIDRRVReaaeLLGL-EDLldR----------KPK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFgvvSE---IADQVVVLEL 239
Cdd:COG3839 133 QLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ---VEamtLADRIAVMND 209
|
250
....*....|....*....
gi 2486247945 240 GK--QIetGPAKSVLQHPK 256
Cdd:COG3839 210 GRiqQV--GTPEELYDRPA 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
13-255 |
1.84e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 97.37 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDrpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDL--FRRTP 90
Cdd:PRK13644 1 MIRLENVSYSYPDGTP---ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLL----RPQKGKVLVSGIDTgdFSKLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 dEIRRLRGakmaMVFQEPMTALnpvmtCGDQMDELLR---AHVPMGPYERRIRILDLFEEVRLPDppriFRSY-PHQLSG 166
Cdd:PRK13644 74 -GIRKLVG----IVFQNPETQF-----VGRTVEEDLAfgpENLCLPPIEIRKRVDRALAEIGLEK----YRHRsPKTLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 167 GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVsEIADQVVVLELGKQIETG 246
Cdd:PRK13644 140 GQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEG 217
|
....*....
gi 2486247945 247 PAKSVLQHP 255
Cdd:PRK13644 218 EPENVLSDV 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-246 |
2.14e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.81 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 15 EVENLAVSLPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIR 94
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQ-GVEDVSFEAKPGQTVAIVGPTGAGKS----TLINLLQRVFDPQSGRILIDGTDIRTVTRASLR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 95 RlrgaKMAMVFQEPM-----TALNPVMTCGDQMDELLR-------AHVPMgpyERRIRILDLF--EEVRlpdpprifrsy 160
Cdd:PRK13657 409 R----NIAVVFQDAGlfnrsIEDNIRVGRPDATDEEMRaaaeraqAHDFI---ERKPDGYDTVvgERGR----------- 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 161 phQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVlfITHDFGVVSEiADQVVVLELG 240
Cdd:PRK13657 471 --QLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVFDNG 545
|
....*.
gi 2486247945 241 KQIETG 246
Cdd:PRK13657 546 RVVESG 551
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
307-492 |
2.21e-22 |
|
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: 100.51 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKlhgLRRRLQVVFQDPYrSLDpr 386
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE---VRRRVSVCAQDAH-LFD-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 MTVGESIVEGpvNFGVPKEEAWK--RAQEFMKIVRLSPDALNRYPNQ----FSGGQRQRISIARALACEPEILICDEAVS 460
Cdd:TIGR02868 423 TTVRENLRLA--RPDATDEELWAalERVGLADWLRALPDGLDTVLGEggarLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|..
gi 2486247945 461 ALDVSVQADILKLLeeIQVKLGIGILFVTHDL 492
Cdd:TIGR02868 501 HLDAETADELLEDL--LAALSGRTVVLITHHL 530
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
14-246 |
2.56e-22 |
|
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: 95.04 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLG--MDLFRRT-- 89
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII----LPDSGEVLFDGkpLDIAARNri 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 90 ---PDEirrlRGakmamvfqepmtaLNPVMTCGDQMDELLRAHvPMGPYERRIRILDLFEEVRLPDppriFRSYP-HQLS 165
Cdd:cd03269 73 gylPEE----RG-------------LYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSE----YANKRvEELS 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIET 245
Cdd:cd03269 131 KGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
.
gi 2486247945 246 G 246
Cdd:cd03269 210 G 210
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
308-514 |
2.68e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 94.30 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRklhgLRRRLQVVFQDPYRSLDprm 387
Cdd:cd03247 17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSLISVLNQRPYLFDT--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGEsivegpvNFGVpkeeawkraqefmkivrlspdalnrypnQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQ 467
Cdd:cd03247 90 TLRN-------NLGR----------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2486247945 468 ADILKLLeeIQVKLGIGILFVTHDLRVASQIcDDVIVIRRGECVESG 514
Cdd:cd03247 135 RQLLSLI--FEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
303-509 |
3.15e-22 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 95.23 E-value: 3.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 303 RVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHglrRRLQVVFQDPyrS 382
Cdd:cd03248 24 RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH---SKVSLVGQEP--V 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 383 LDPRmTVGESIVEG--PVNFGVPKEEAWK-RAQEFMKIVRLSPDA-LNRYPNQFSGGQRQRISIARALACEPEILICDEA 458
Cdd:cd03248 99 LFAR-SLQDNIAYGlqSCSFECVKEAAQKaHAHSFISELASGYDTeVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 459 VSALDVSVQADILKLLEEIQVKLgiGILFVTHDLRVASQiCDDVIVIRRGE 509
Cdd:cd03248 178 TSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGR 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
14-223 |
5.16e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 95.54 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGDRPN-AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRtPDE 92
Cdd:COG1101 2 LELKNLSKTFNPGTVNEKrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP----PDSGSILIDGKDVTKL-PEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRrlrgAKM-AMVFQEPM--TAlnPVMTCGDQM----------------DELLRAHvpmgpYERRIRILDLFEEVRLPDP 153
Cdd:COG1101 77 KR----AKYiGRVFQDPMmgTA--PSMTIEENLalayrrgkrrglrrglTKKRREL-----FRELLATLGLGLENRLDTK 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 154 PRifrsyphQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHD 223
Cdd:COG1101 146 VG-------LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-223 |
5.35e-22 |
|
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: 99.36 E-value: 5.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 10 KLPVLEVENLAVSLPPGgdrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRT 89
Cdd:TIGR02868 331 GKPTLELRDLSAGYPGA---PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD----PLQGEVTLDGVPVSSLD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 90 PDEIRRLRG--AKMAMVFQEpmTALNPVM-TCGDQMDEllrahvpmgpyerriRILDLFEEVRLPDPPRifrSYPH---- 162
Cdd:TIGR02868 404 QDEVRRRVSvcAQDAHLFDT--TVRENLRlARPDATDE---------------ELWAALERVGLADWLR---ALPDgldt 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 163 -------QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLIleLQKKNGTAVLFITHD 223
Cdd:TIGR02868 464 vlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVLITHH 529
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
281-503 |
6.58e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 94.40 E-value: 6.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTLLEAKNVvktytlgGFFTGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAA 360
Cdd:PRK10247 4 NSPLLQLQNV-------GYLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 PKRklhglRRRLQV--VFQDPyrsldprMTVGESIVEgpvNFGVP-----KEEAWKRAQEFMKIVRLSPDALNRYPNQFS 433
Cdd:PRK10247 75 KPE-----IYRQQVsyCAQTP-------TLFGDTVYD---NLIFPwqirnQQPDPAIFLDDLERFALPDTILTKNIAELS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 434 GGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQiCDDVI 503
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVI 208
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
261-505 |
6.59e-22 |
|
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: 99.28 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 261 QKLINAVPELKPRHRPPVDGNPTLLEAKNVVKTYtlggfftgRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIA 340
Cdd:TIGR02857 298 FAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAY--------PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 341 RLIDPTSGEVWVNGENVAAAPkrkLHGLRRRLQVVFQDPYrsldprMTVGeSIVEGpVNFGVP--KEEAWKRAQE---FM 415
Cdd:TIGR02857 370 GFVDPTEGSIAVNGVPLADAD---ADSWRDQIAWVPQHPF------LFAG-TIAEN-IRLARPdaSDAEIREALEragLD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 416 KIVRLSPDALN----RYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVklGIGILFVTHD 491
Cdd:TIGR02857 439 EFVAALPQGLDtpigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHR 516
|
250
....*....|....
gi 2486247945 492 LRVASQiCDDVIVI 505
Cdd:TIGR02857 517 LALAAL-ADRIVVL 529
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
302-512 |
7.26e-22 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 94.46 E-value: 7.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 302 GRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHGLR-RRLQVVFQDpy 380
Cdd:PRK10584 19 GEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRaKHVGFVFQS-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 381 RSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVS 460
Cdd:PRK10584 97 FMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 461 ALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQiCDDVIVIRRGECVE 512
Cdd:PRK10584 176 NLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
32-257 |
1.14e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.47 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLlGMDLF--RRTPDEIRRLRgAKMAMVFQEPM 109
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLL----QPTSGTVTI-GERVItaGKKNKKLKPLR-KKVGIVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 110 TALnpvmtcgdqMDELLRAHVPMGPY-------ERRIRILDLFEEVRLPdpPRIFRSYPHQLSGGQRQRIVIAMALLLKP 182
Cdd:PRK13634 96 HQL---------FEETVEKDICFGPMnfgvseeDAKQKAREMIELVGLP--EELLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 183 DLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKE 257
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
14-253 |
1.20e-21 |
|
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: 93.83 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGgdRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03253 1 IEFENVTFAYDPG--RP-VLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLFRFYDVSSGSILIDGQDIREVTLDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEpmTAL------------NPVMTCGDQMDELLRAHVpmgpyERRIrildlfeeVRLPDpprifrSYP 161
Cdd:cd03253 74 RR----AIGVVPQD--TVLfndtigynirygRPDATDEEVIEAAKAAQI-----HDKI--------MRFPD------GYD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 162 HQ-------LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDfgvVSEI--AD 232
Cdd:cd03253 129 TIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHR---LSTIvnAD 203
|
250 260
....*....|....*....|.
gi 2486247945 233 QVVVLELGKQIETGPAKSVLQ 253
Cdd:cd03253 204 KIIVLKDGRIVERGTHEELLA 224
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
32-246 |
1.25e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.07 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSViastvMGLLPKGLAPADGSVKLLG---MDLFRRTPDEIRRLRgAKMAMVFQEP 108
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKST-----MIQLTNGLIISETGQTIVGdyaIPANLKKIKEVKRLR-KEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 109 MTALnpvmtcgdqMDELLRAHVPMGPY-------ERRIRILDLFEEVRLPDppRIFRSYPHQLSGGQRQRIVIAMALLLK 181
Cdd:PRK13645 100 EYQL---------FQETIEKDIAFGPVnlgenkqEAYKKVPELLKLVQLPE--DYVKRSPFELSGGQKRRVALAGIIAMD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 182 PDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
36-259 |
1.58e-21 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 95.95 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRR-----TPDEIRRLrgakmAMVFQEpmT 110
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLT----RPDEGEIVLNGRTLFDSrkgifLPPEKRRI-----GYVFQE--A 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALNPVMTcgdqmdelLRAHVPMG-----PYERRIRildlFEEV-RLPDPPRIFRSYPHQLSGGQRQRIVIAMALLLKPDL 184
Cdd:TIGR02142 85 RLFPHLS--------VRGNLRYGmkrarPSERRIS----FERViELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 185 LICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPY 259
Cdd:TIGR02142 153 LLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
14-254 |
1.80e-21 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 97.86 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPpGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIAStvmgLLPKGLAPADGSVKLLGMDLFRRTPDEI 93
Cdd:TIGR02203 331 VEFRNVTFRYP-GRDRP-ALDSISLVIEPGETVALVGRSGSGKSTLVN----LIPRFYEPDSGQILLDGHDLADYTLASL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEpmtalnpVMTCGDQMDELLR----AHVPMGPYERRIRILDLFEEV-RLP---DPPriFRSYPHQLS 165
Cdd:TIGR02203 405 RR----QVALVSQD-------VVLFNDTIANNIAygrtEQADRAEIERALAAAYAQDFVdKLPlglDTP--IGENGVLLS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVsEIADQVVVLELGKQIET 245
Cdd:TIGR02203 472 GGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTI-EKADRIVVMDDGRIVER 548
|
....*....
gi 2486247945 246 GPAKSVLQH 254
Cdd:TIGR02203 549 GTHNELLAR 557
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-252 |
1.97e-21 |
|
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: 93.32 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 26 GGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIRRlrgaKMAMVF 105
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYV----PENGRVLVDGHDLALADPAWLRR----QVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 106 QEPmtalnpVMTCGDQMDELLRAHvPMGPYERRIrildlfEEVRLPDPPRIFRSYPH-----------QLSGGQRQRIVI 174
Cdd:cd03252 83 QEN------VLFNRSIRDNIALAD-PGMSMERVI------EAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 175 AMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVSEiADQVVVLELGKQIETGPAKSVL 252
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
276-517 |
2.12e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 97.86 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 276 PPV--DGNPTLLEAKNVVkTYTLGGFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVN 353
Cdd:PRK10789 297 APVvkDGSEPVPEGRGEL-DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFH 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 354 GENVaaaPKRKLHGLRRRLQVVFQDPYRSLDprmTVGESIVEG-PVNFGVPKEEAWKRAQEFMKIVRLsPDAlnrYPNQ- 431
Cdd:PRK10789 376 DIPL---TKLQLDSWRSRLAVVSQTPFLFSD---TVANNIALGrPDATQQEIEHVARLASVHDDILRL-PQG---YDTEv 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 432 ------FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEeiQVKLGIGILFVTHDLRvASQICDDVIVI 505
Cdd:PRK10789 446 gergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLS-ALTEASEILVM 522
|
250
....*....|..
gi 2486247945 506 RRGECVESGHVQ 517
Cdd:PRK10789 523 QHGHIAQRGNHD 534
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-264 |
2.14e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.95 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 11 LPVLEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTV--MGLLpKGLAPADGSVKLLGMDLFRR 88
Cdd:PRK14258 5 IPAIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNEL-ESEVRVEGRVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 89 TPDeIRRLRgAKMAMVFQEPmtALNPvMTCGDQMD---ELLRAHVPM---GPYERRIRILDLFEEVRlpdpPRIFRSyPH 162
Cdd:PRK14258 80 RVN-LNRLR-RQVSMVHPKP--NLFP-MSVYDNVAygvKIVGWRPKLeidDIVESALKDADLWDEIK----HKIHKS-AL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLE---- 238
Cdd:PRK14258 150 DLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKgnen 229
|
250 260
....*....|....*....|....*..
gi 2486247945 239 -LGKQIETGPAKSVLQHPKEPYTQKLI 264
Cdd:PRK14258 230 rIGQLVEFGLTKKIFNSPHDSRTREYV 256
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
13-252 |
3.38e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGgdrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLG--MDLFRRTP 90
Cdd:PRK13636 5 ILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGIL----KPSSGRILFDGkpIDYSRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLRGakmaMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRI-RILDLFEEVRLPDPPrifrsyPHQLSGGQR 169
Cdd:PRK13636 78 MKLRESVG----MVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVdNALKRTGIEHLKDKP------THCLSFGQK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 170 QRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAK 249
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
...
gi 2486247945 250 SVL 252
Cdd:PRK13636 228 EVF 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
277-533 |
3.92e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 93.31 E-value: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 277 PVDGNPTLLEAKNVVKTYtlGGFFtgrvkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLID--PT---SGEVW 351
Cdd:PRK14243 3 TLNGTETVLRTENLNVYY--GSFL-------AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 352 VNGENVAAaPKRKLHGLRRRLQVVFQDPY---RSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIvrlsPDALNRY 428
Cdd:PRK14243 74 FHGKNLYA-PDVDPVEVRRRIGMVFQKPNpfpKSIYDNIAYGARINGYKGDMDELVERSLRQAALWDEV----KDKLKQS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 429 PNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGIlfVTHDLRVASQICD-------- 500
Cdd:PRK14243 149 GLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIII--VTHNMQQAARVSDmtaffnve 226
|
250 260 270
....*....|....*....|....*....|....
gi 2486247945 501 -DVIVIRRGECVESGHVQDVFFHPQHEYTKSLIA 533
Cdd:PRK14243 227 lTEGGGRYGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
275-519 |
3.97e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.90 E-value: 3.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 275 RPPVDGNPTLLEAKNVVKTYTlggfftGRVKVralKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNG 354
Cdd:PRK13536 32 SIPGSMSTVAIDLAGVSKSYG------DKAVV---NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 355 ENVAAapkrKLHGLRRRLQVVFQdpYRSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALNRYpNQFSG 434
Cdd:PRK13536 103 VPVPA----RARLARARIGVVPQ--FDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARV-SDLSG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 435 GQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
....*
gi 2486247945 515 HVQDV 519
Cdd:PRK13536 255 RPHAL 259
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
29-246 |
6.67e-21 |
|
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: 91.83 E-value: 6.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 29 RPN--AVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRRlrgaKMAMVFQ 106
Cdd:cd03249 13 RPDvpILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRS----QIGLVSQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 107 EPMTALNPVMtcgdqmdELLRahvpmgpYERRIRILDLFEEV-RLPDPPRIFRSYPH-----------QLSGGQRQRIVI 174
Cdd:cd03249 85 EPVLFDGTIA-------ENIR-------YGKPDATDEEVEEAaKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 175 AMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVSEiADQVVVLELGKQIETG 246
Cdd:cd03249 151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQG 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
12-540 |
7.05e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 95.84 E-value: 7.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPpgGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLpKGLAPAD-GSVKLLGMDLFRRTP 90
Cdd:PRK10762 3 ALLQLKGIDKAFP--GVK--ALSGAALNVYPGRVMALVGENGAGKS----TMMKVL-TGIYTRDaGSILYLGKEVTFNGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 deiRRLRGAKMAMVFQEpmtaLN--PVMTCGDQMdELLRAHV-PMGpyerRIRILDLFEEV-----RLPdppriFRSYPH 162
Cdd:PRK10762 74 ---KSSQEAGIGIIHQE----LNliPQLTIAENI-FLGREFVnRFG----RIDWKKMYAEAdkllaRLN-----LRFSSD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSG----GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLE 238
Cdd:PRK10762 137 KLVGelsiGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 239 LGKQIetgpAKSVLQHPKEpytQKLIN-----AVPELKPR-HRPPvdgNPTLLEAKNVvktytlggffTGrvkvRALKGV 312
Cdd:PRK10762 216 DGQFI----AEREVADLTE---DSLIEmmvgrKLEDQYPRlDKAP---GEVRLKVDNL----------SG----PGVNDV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 313 SARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVaaAPKRKLHGLRRRLQVVFQDPYRS-LDPRMTVGE 391
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV--VTRSPQDGLANGIVYISEDRKRDgLVLGMSVKE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 392 SIVEGPVNFGVPKEEAWKRAQE------FMKIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVS 465
Cdd:PRK10762 350 NMSLTALRYFSRAGGSLKHADEqqavsdFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVG 429
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 466 VQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRgecvesGHVQDVFFHPQHEYTKsLIAAAPGTNY 540
Cdd:PRK10762 430 AKKEIYQLINQFK-AEGLSIILVSSEMPEVLGMSDRILVMHE------GRISGEFTREQATQEK-LMAAAVGKLN 496
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-253 |
8.23e-21 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 96.47 E-value: 8.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPpgGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:TIGR03375 464 IEFRNVSFAYP--GQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQ----PTEGSVLLDGVDIRQIDPADL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQepmtalNPVMTCGDqmdelLRAHVPMG-PY---ERRIRILDLF---EEVRL-PDpprifrSYPHQ-- 163
Cdd:TIGR03375 538 RR----NIGYVPQ------DPRLFYGT-----LRDNIALGaPYaddEEILRAAELAgvtEFVRRhPD------GLDMQig 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 -----LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILK-LILELQKKngTAVLfITHDFGVVsEIADQVVVL 237
Cdd:TIGR03375 597 ergrsLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDrLKRWLAGK--TLVL-VTHRTSLL-DLVDRIIVM 672
|
250
....*....|....*.
gi 2486247945 238 ELGKQIETGPAKSVLQ 253
Cdd:TIGR03375 673 DNGRIVADGPKDQVLE 688
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
282-535 |
1.03e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.50 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 282 PTLLEAKNVVKTYTlggfftgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAP 361
Cdd:PRK15439 9 PPLLCARSISKQYS---------GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 362 KRKLHGLrrRLQVVFQDPYrsLDPRMTVGESIVegpvnFGVPK-EEAWKRAQEFMKI--VRLSPDALnryPNQFSGGQRQ 438
Cdd:PRK15439 80 PAKAHQL--GIYLVPQEPL--LFPNLSVKENIL-----FGLPKrQASMQKMKQLLAAlgCQLDLDSS---AGSLEVADRQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 439 RISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECVESGhvqd 518
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSG---- 222
|
250
....*....|....*..
gi 2486247945 519 vffhPQHEYTKSLIAAA 535
Cdd:PRK15439 223 ----KTADLSTDDIIQA 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-237 |
1.13e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.99 E-value: 1.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 27 GDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVkllgmdlfrrtpdeiRRLRGAKMAMVFQ 106
Cdd:NF040873 3 GGRP-VLHGVDLTIPAGSLTAVVGPNGSGKS----TLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 107 E-------PMTALNpVMTCGdqmdeLLRAHVPMGPYER--RIRILDLFEEVRLPD-PPRIFRSyphqLSGGQRQRIVIAM 176
Cdd:NF040873 63 RsevpdslPLTVRD-LVAMG-----RWARRGLWRRLTRddRAAVDDALERVGLADlAGRQLGE----LSGGQRQRALLAQ 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 177 ALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEiADQVVVL 237
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
308-509 |
1.19e-20 |
|
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: 90.22 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGeNVAAAPkrklhglrrrlqvvfQDPYRsldPRM 387
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-SIAYVS---------------QEPWI---QNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGESIVegpvnFGVPKEEAWKRaqefmKIVR---LSPDaLNRYPNQ-----------FSGGQRQRISIARALACEPEIL 453
Cdd:cd03250 81 TIRENIL-----FGKPFDEERYE-----KVIKacaLEPD-LEILPDGdlteigekginLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 454 ICDEAVSALDVSVQADILKlleeiQVKLGIG-----ILFVTHDLRVASQiCDDVIVIRRGE 509
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFE-----NCILGLLlnnktRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
319-514 |
1.20e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.77 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 319 GETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAA----APKRKLHGLRRRLQVVfqdpyrsldPRMTVGESIV 394
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwsskAFARKVAYLPQQLPAA---------EGMTVRELVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 395 EGPV-------NFGVPKEEawkRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQ 467
Cdd:PRK10575 108 IGRYpwhgalgRFGAADRE---KVEEAISLVGLKPLA-HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2486247945 468 ADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:PRK10575 184 VDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
311-514 |
1.25e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 311 GVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVaaaPKRKLHGlRRRLQVVFQdpYRSLDPRMTVG 390
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV---PSRARHA-RQRVGVVPQ--FDNLDPDFTVR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 391 ESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALNRYpNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADI 470
Cdd:PRK13537 99 ENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2486247945 471 LKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:PRK13537 178 WERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEG 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
318-543 |
1.26e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.75 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 318 RGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHGLRRRLQVVFQDPyrSLDPRMTVGESiVEGP 397
Cdd:PRK11831 32 RGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSG--ALFTDMNVFDN-VAYP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 398 VNFGVPKEEAWKRAQEFMKI--VRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLE 475
Cdd:PRK11831 109 LREHTQLPAPLLHSTVMMKLeaVGLR-GAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLIS 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 476 EIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLIAAAPGT---NYPFG 543
Cdd:PRK11831 188 ELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFLDGIADGPvpfRYPAG 258
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
15-253 |
1.37e-20 |
|
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: 90.75 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 15 EVENlaVSLPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIR 94
Cdd:cd03254 4 EFEN--VNFSYDEKKP-VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD----PQKGQILIDGIDIRDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 95 RlrgaKMAMVFQEPmtalnpVMTCGDQMDELLRAHvpmgPYERRIRILDLFEEVRLPDpprIFRSYP-----------HQ 163
Cdd:cd03254 77 S----MIGVVLQDT------FLFSGTIMENIRLGR----PNATDEEVIEAAKEAGAHD---FIMKLPngydtvlgengGN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVSEiADQVVVLELGKQI 243
Cdd:cd03254 140 LSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
|
250
....*....|
gi 2486247945 244 ETGPAKSVLQ 253
Cdd:cd03254 217 EEGTHDELLA 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-269 |
1.87e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 91.33 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNaVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDE 92
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLL----EAESGQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRlrgaKMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGpyERRIRILDLFEEVRLPDppriFRSY-PHQLSGGQRQR 171
Cdd:PRK13650 79 IRH----KIGMVFQNPDNQFVGATVEDDVAFGLENKGIPHE--EMKERVNEALELVGMQD----FKERePARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 172 IVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSeIADQVVVLELGKQIETGPAKSV 251
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPREL 227
|
250 260
....*....|....*....|....*.
gi 2486247945 252 LQHPKE--------PYTQKLINAVPE 269
Cdd:PRK13650 228 FSRGNDllqlgldiPFTTSLVQSLRQ 253
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-264 |
2.23e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.31 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 20 AVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLA-PADGSVKLLGMDLFR-RTPDEIRRlr 97
Cdd:PRK14271 24 AVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyRYSGDVLLGGRSIFNyRDVLEFRR-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 98 gaKMAMVFQEPmtalNPV-MTCGDQMDELLRAH--VPM----GPYERRIRILDLFEEV--RLPDPPriFRsyphqLSGGQ 168
Cdd:PRK14271 102 --RVGMLFQRP----NPFpMSIMDNVLAGVRAHklVPRkefrGVAQARLTEVGLWDAVkdRLSDSP--FR-----LSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 169 RQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKngTAVLFITHDFGVVSEIADQVVVLELGKQIETGPA 248
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPT 246
|
250
....*....|....*.
gi 2486247945 249 KSVLQHPKEPYTQKLI 264
Cdd:PRK14271 247 EQLFSSPKHAETARYV 262
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-246 |
3.64e-20 |
|
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: 89.09 E-value: 3.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 35 HVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEirrlrgAKMAMVFQEpmTALNP 114
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKS----TLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQE--NNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 115 VMTCGDQMDELLRAHVPMGPYER--------RIRILDLfeEVRLPDpprifrsyphQLSGGQRQRIVIAMALLLKPDLLI 186
Cdd:cd03298 84 HLTVEQNVGLGLSPGLKLTAEDRqaievalaRVGLAGL--EKRLPG----------ELSGGERQRVALARVLVRDKPVLL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 187 CDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03298 152 LDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-259 |
3.91e-20 |
|
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: 88.74 E-value: 3.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLlpKGLAPADGSVKLLGMDLFRRTPDEi 93
Cdd:cd03217 1 LEIKDLHVSV---GGKE-ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH--PKYEVTEGEILFKGEDITDLPPEE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRGakMAMVFQEPMTalnpvmtcgdqmdellrahVPMgpyerrIRILDLFEEVRLpdpprifrsyphQLSGGQRQRIV 173
Cdd:cd03217 74 RARLG--IFLAFQYPPE-------------------IPG------VKNADFLRYVNE------------GFSGGEKKRNE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEI-ADQVVVLELGKQIETGPAKSVL 252
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELAL 193
|
....*..
gi 2486247945 253 QHPKEPY 259
Cdd:cd03217 194 EIEKKGY 200
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
12-262 |
4.75e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 4.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIAStVMGLLPKglaPADGSVKLLGMDLFRRTPD 91
Cdd:PRK10535 3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDK---PTSGTYRVAGQDVATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRGAKMAMVFQE-----PMTALNPVmtcgdqmdELLRAHVPMGPYERRIRILDLFEEVRLPDppRIfrSY-PHQLS 165
Cdd:PRK10535 79 ALAQLRREHFGFIFQRyhllsHLTAAQNV--------EVPAVYAGLERKQRLLRAQELLQRLGLED--RV--EYqPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEiADQVVVLELGKQIET 245
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN 224
|
250
....*....|....*....
gi 2486247945 246 GPAK--SVLQHPKEPYTQK 262
Cdd:PRK10535 225 PPAQekVNVAGGTEPVVNT 243
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
136-463 |
6.13e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 94.04 E-value: 6.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 136 ERRIRILDLFEEVRLpDPpriFRSYPH-QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKN- 213
Cdd:NF033858 112 ERRRRIDELLRATGL-AP---FADRPAgKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERp 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 214 GTAVLFIT------HDFgvvseiaDQVVVLELGKQIETGPAKSVLQHPKepyTQKL----INAVPELKPRH--------R 275
Cdd:NF033858 188 GMSVLVATaymeeaERF-------DWLVAMDAGRVLATGTPAELLARTG---ADTLeaafIALLPEEKRRGhqpvvippR 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 276 PPVDGNPTLLEAKNVVKTYtlgGFFTgrvkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGE 355
Cdd:NF033858 258 PADDDDEPAIEARGLTMRF---GDFT------AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 356 NVAAapkrklHGLRRRLQVVFQDPYRSLDPRMTVGEsivegpvN-------FGVPKEEAWKRAQEFMKIVRLSpDALNRY 428
Cdd:NF033858 329 PVDA------GDIATRRRVGYMSQAFSLYGELTVRQ-------NlelharlFHLPAAEIAARVAEMLERFDLA-DVADAL 394
|
330 340 350
....*....|....*....|....*....|....*
gi 2486247945 429 PNQFSGGQRQRISIARALACEPEILICDEAVSALD 463
Cdd:NF033858 395 PDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
13-246 |
8.79e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.25 E-value: 8.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIAStvmgLLPKGLAPADGSVKLLGMDLFRRTPDE 92
Cdd:TIGR00958 478 LIEFQDVSFSYPNRPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAA----LLQNLYQPTGGQVLLDGVPLVQYDHHY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRlrgaKMAMVFQEPM-----TALNPVMTCGDQMDELLRAHVPMGPYERRIRIL--DLFEEVRlpdpprifrsyPH--Q 163
Cdd:TIGR00958 553 LHR----QVALVGQEPVlfsgsVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFpnGYDTEVG-----------EKgsQ 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQAsilkLILELQKKNGTAVLFITHDFGVVsEIADQVVVLELGKQI 243
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVV 692
|
...
gi 2486247945 244 ETG 246
Cdd:TIGR00958 693 EMG 695
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
37-241 |
1.06e-19 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 87.61 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 37 SFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDEirrlrgAKMAMVFQEpmTALNPVM 116
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFI----EPASGSIKVNDQSHTGLAPYQ------RPVSMLFQE--NNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 117 TCGDQMDELLRAHVPMGPYERRiRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNV 196
Cdd:TIGR01277 86 TVRQNIGLGLHPGLKLNAEQQE-KVVDAAQQVGIAD---YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2486247945 197 TTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:TIGR01277 162 LLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGK 206
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
32-241 |
1.20e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.62 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDEIRRLRgAKMAMVFQEPMTA 111
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIE----RPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LN---------PVMTCGDQMDELLRahvpmgpyerriRILDLFEEVRLPDPPRifrSYPHQLSGGQRQRIVIAMALLLKP 182
Cdd:PRK10908 92 MDrtvydnvaiPLIIAGASGDDIRR------------RVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 183 DLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
12-252 |
1.68e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPD 91
Cdd:PRK09536 2 PMIDVSDLSVEF---GDTT-VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTL----TPTAGTVLVAGDDVEALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLrgakMAMVFQEPMTALNpvmTCGDQMDELLRA-HV----PMGPYERRI--RILDLFEEVRLPDppRIFRSyphqL 164
Cdd:PRK09536 74 AASRR----VASVPQDTSLSFE---FDVRQVVEMGRTpHRsrfdTWTETDRAAveRAMERTGVAQFAD--RPVTS----L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 165 SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFItHDFGVVSEIADQVVVLELGKQIE 244
Cdd:PRK09536 141 SGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRA 219
|
....*...
gi 2486247945 245 TGPAKSVL 252
Cdd:PRK09536 220 AGPPADVL 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
31-252 |
1.69e-19 |
|
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: 92.11 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 31 NAVEHVSFTVNEGEVTCLIGESGSGKSVIAStvmgLLPKGLAPADGSVKLLGMDLFRRTPDEIRRLrgakMAMVFQEPmt 110
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAK----LLVGFFQARSGEILLNGFSLKDIDRHTLRQF----INYLPQEP-- 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 alnpVMTCGDQMDELLRAHVPMGPYERRIRILDLFE-EVRLPDPPRIFR----SYPHQLSGGQRQRIVIAMALLLKPDLL 185
Cdd:TIGR01193 558 ----YIFSGSILENLLLGAKENVSQDEIWAACEIAEiKDDIENMPLGYQtelsEEGSSISGGQKQRIALARALLTDSKVL 633
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 186 ICDEPTTALNVTTQASILKLILELQKKngtAVLFITHDFGvVSEIADQVVVLELGKQIETGPAKSVL 252
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
38-261 |
1.99e-19 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 87.21 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 38 FTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGmdlfrRTPDEIRRLRG---AKMAMVFQEPMTALNP 114
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIP----PAKGTVKVAG-----ASPGKGWRHIGyvpQRHEFAWDFPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 115 VMTCGDQMdellrahvpMGPYERR-----IRILDLFEEVRLPDppriFRSYP-HQLSGGQRQRIVIAMALLLKPDLLICD 188
Cdd:TIGR03771 72 VMSGRTGH---------IGWLRRPcvadfAAVRDALRRVGLTE----LADRPvGELSGGQRQRVLVARALATRPSVLLLD 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 189 EPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLElGKQIETGpAKSVLQHPkEPYTQ 261
Cdd:TIGR03771 139 EPFTGLDMPTQELLTELFIEL-AGAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADG-TPQQLQDP-APWMT 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
8-264 |
2.50e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.01 E-value: 2.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 8 AQKLPVLEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLfR 87
Cdd:PRK09452 9 SSLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIAGFETPDSGRIMLDGQDI-T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 88 RTPDEIRRLRgakmaMVFQEpmTALNPVMTCGDQMDELLR-AHVPMGpyERRIRILDLFEEVRLPDpprIFRSYPHQLSG 166
Cdd:PRK09452 80 HVPAENRHVN-----TVFQS--YALFPHMTVFENVAFGLRmQKTPAA--EITPRVMEALRMVQLEE---FAQRKPHQLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 167 GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:PRK09452 148 GQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
250
....*....|....*...
gi 2486247945 247 PAKSVLQHPKEPYTQKLI 264
Cdd:PRK09452 228 TPREIYEEPKNLFVARFI 245
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
14-246 |
3.15e-19 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 86.09 E-value: 3.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGgdrpNAVEHVSFTVNEGeVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLfRRTPDEI 93
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRILATLTPPSSGTIRIDGQDV-LKQPQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRGakmaMVFQEPMTalNPVMTCGDQMDELLRAHvPMGPYERRIRILDLFEEVRLPDppriFRS-YPHQLSGGQRQRI 172
Cdd:cd03264 71 RRRIG----YLPQEFGV--YPNFTVREFLDYIAWLK-GIPSKEVKARVDEVLELVNLGD----RAKkKIGSLSGGMRRRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03264 140 GIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
36-247 |
3.30e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.26 E-value: 3.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLApADGSVKLLGMdlfRRTPDEIRRLrgakMAMVFQEPMtaLNPV 115
Cdd:TIGR00955 44 VSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVK-GSGSVLLNGM---PIDAKEMRAI----SAYVQQDDL--FIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 116 MTCGDQMdeLLRAHVPMGPY----ERRIRILDLFEEVRLPD--------PPRIfrsypHQLSGGQRQRIVIAMALLLKPD 183
Cdd:TIGR00955 114 LTVREHL--MFQAHLRMPRRvtkkEKRERVDEVLQALGLRKcantrigvPGRV-----KGLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 184 LLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGP 247
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGS 250
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-253 |
3.78e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.04 E-value: 3.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLlpKGLAPADGSVKLLGMDLFRRTPDEi 93
Cdd:COG0396 1 LEIKNLHVSV---EGKE-ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH--PKYEVTSGSILLDGEDILELSPDE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRGakMAMVFQepmtalNPVMTCGDQMDELLRAHV------PMGPYERRIRILDLFEEVRLpDPPRIFRSYPHQLSGG 167
Cdd:COG0396 74 RARAG--IFLAFQ------YPVEIPGVSVSNFLRTALnarrgeELSAREFLKLLKEKMKELGL-DEDFLDRYVNEGFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNgTAVLFITHDFGVVSEI-ADQVVVLELGKQIETG 246
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPD-RGILIITHYQRILDYIkPDFVHVLVDGRIVKSG 223
|
....*..
gi 2486247945 247 PAKSVLQ 253
Cdd:COG0396 224 GKELALE 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
14-246 |
4.29e-19 |
|
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: 85.06 E-value: 4.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMdlfrrtpdei 93
Cdd:cd03247 1 LSINNVSFSYPE--QEQQVLKNLSLELKQGEKIALLGRSGSGKS----TLLQLLTGDLKPQQGEITLDGV---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 rrlrgakmamvfqepmtalnPVMTCGDQMDELLrAHVPMGPYerririldLFEEVrlpdpprIFRSYPHQLSGGQRQRIV 173
Cdd:cd03247 65 --------------------PVSDLEKALSSLI-SVLNQRPY--------LFDTT-------LRNNLGRRFSGGERQRLA 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVsEIADQVVVLELGKQIETG 246
Cdd:cd03247 109 LARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
9-246 |
4.91e-19 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 90.53 E-value: 4.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 9 QKLPV-----LEVENLAVSLPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGM 83
Cdd:TIGR02204 328 KTLPVplrgeIEFEQVNFAYPARPDQP-ALDGLNLTVRPGETVALVGPSGAGKS----TLFQLLLRFYDPQSGRILLDGV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 84 DLFRRTPDEIRrlrgAKMAMVFQEPMTALNPVMtcgdqmdELLRAHVPMGPYERRIRILDLFEE----VRLPDPpriFRS 159
Cdd:TIGR02204 403 DLRQLDPAELR----ARMALVPQDPVLFAASVM-------ENIRYGRPDATDEEVEAAARAAHAhefiSALPEG---YDT 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 160 YPHQ----LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVSEiADQVV 235
Cdd:TIGR02204 469 YLGErgvtLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIV 545
|
250
....*....|.
gi 2486247945 236 VLELGKQIETG 246
Cdd:TIGR02204 546 VMDQGRIVAQG 556
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-491 |
6.38e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 90.39 E-value: 6.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 27 GDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGmDLF--RRTPDEIRRLRG------ 98
Cdd:PRK11147 14 SDAP-LLDNAELHIEDNERVCLVGRNGAGKS----TLMKILNGEVLLDDGRIIYEQ-DLIvaRLQQDPPRNVEGtvydfv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 99 ----AKMAMVFQEPMTALNPVMTcgDQMDELLR--AHVP-----MGPYERRIRILDLFEEVRL-PDPPRifrsypHQLSG 166
Cdd:PRK11147 88 aegiEEQAEYLKRYHDISHLVET--DPSEKNLNelAKLQeqldhHNLWQLENRINEVLAQLGLdPDAAL------SSLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 167 GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKkngtAVLFITHDFGVVSEIADQVVVLELGKQIE-- 244
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SIIFISHDRSFIRNMATRIVDLDRGKLVSyp 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 245 -------TGPAKSV----LQHpkEPYTQKL----------INA--------VPELKP-----RHRPPVDGNPTL------ 284
Cdd:PRK11147 236 gnydqylLEKEEALrveeLQN--AEFDRKLaqeevwirqgIKArrtrnegrVRALKAlrrerSERREVMGTAKMqveeas 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 ------LEAKNVvkTYTLGGfftgrvKVrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNgenva 358
Cdd:PRK11147 314 rsgkivFEMENV--NYQIDG------KQ-LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 359 aapkrklhglrRRLQVVFQDPYRS-LDPRMTVGESIVEGP----VNfGVPKeEAWKRAQEFM---KIVRLSPDALnrypn 430
Cdd:PRK11147 380 -----------TKLEVAYFDQHRAeLDPEKTVMDNLAEGKqevmVN-GRPR-HVLGYLQDFLfhpKRAMTPVKAL----- 441
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 431 qfSGGQRQRISIARALACEPEILICDEAVSALDVsvqaDILKLLEEIQVKLGIGILFVTHD 491
Cdd:PRK11147 442 --SGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
309-522 |
1.00e-18 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 86.12 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPkrkLHGLRRRLQVVFQDPYR------- 381
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILfsgsirf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 382 SLDPRMTVGESIVegpvnfgvpkEEAWKRAQeFMKIVRLSPDALNRYPNQ----FSGGQRQRISIARALACEPEILICDE 457
Cdd:cd03288 114 NLDPECKCTDDRL----------WEALEIAQ-LKNMVKSLPGGLDAVVTEggenFSVGQRQLFCLARAFVRKSSILIMDE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 458 AVSALDVSVQadilKLLEEIQVKLGIGILFVTHDLRVASQI-CDDVIVIRRGECVESGHVQDVFFH 522
Cdd:cd03288 183 ATASIDMATE----NILQKVVMTAFADRTVVTIAHRVSTILdADLVLVLSRGILVECDTPENLLAQ 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
284-519 |
1.02e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYtlGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGEnvaaAPKR 363
Cdd:PRK09700 5 YISMAGIGKSF--GP-------VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNI----NYNK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 KLHGLRRRL--QVVFQDpyRSLDPRMTVGESIVEG--PVN--FGVPK---EEAWKRAQEFMKIVRLSPDaLNRYPNQFSG 434
Cdd:PRK09700 72 LDHKLAAQLgiGIIYQE--LSVIDELTVLENLYIGrhLTKkvCGVNIidwREMRVRAAMMLLRVGLKVD-LDEKVANLSI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 435 GQRQRISIARALACEPEILICDEAVSALdVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:PRK09700 149 SHKQMLEIAKTLMLDAKVIIMDEPTSSL-TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
....*
gi 2486247945 515 HVQDV 519
Cdd:PRK09700 228 MVSDV 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1-271 |
1.20e-18 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.81 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 1 MTESSLRaqklpvLEVENLAVslppGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTvmglLPKGLAPADGSVKL 80
Cdd:PRK10253 1 MTESVAR------LRGEQLTL----GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRT----LSRLMTPAHGHVWL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 81 LGMDLFRRTPDEIRRlrgaKMAMVFQEPMTAlnpvmtcGD-QMDELL-RAHVPMGPYERRIRILD---LFEEVRLPDPPR 155
Cdd:PRK10253 67 DGEHIQHYASKEVAR----RIGLLAQNATTP-------GDiTVQELVaRGRYPHQPLFTRWRKEDeeaVTKAMQATGITH 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 156 IFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVV 235
Cdd:PRK10253 136 LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLI 215
|
250 260 270
....*....|....*....|....*....|....*.
gi 2486247945 236 VLELGKQIETGPaksvlqhPKEPYTQKLINAVPELK 271
Cdd:PRK10253 216 ALREGKIVAQGA-------PKEIVTAELIERIYGLR 244
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
32-253 |
1.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 86.33 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPD-EIRRLRgAKMAMVFQEPMT 110
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLL----QPTEGKVTVGDIVVSSTSKQkEIKPVR-KKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALnpvmtcgdqMDELLRAHVPMGPYERRIR-------ILDLFEEVRLPDppRIFRSYPHQLSGGQRQRIVIAMALLLKPD 183
Cdd:PRK13643 96 QL---------FEETVLKDVAFGPQNFGIPkekaekiAAEKLEMVGLAD--EFWEKSPFELSGGQMRRVAIAGILAMEPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 184 LLICDEPTTALNVTTQASILKLiLELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQ 253
Cdd:PRK13643 165 VLVLDEPTAGLDPKARIEMMQL-FESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-246 |
1.80e-18 |
|
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: 84.18 E-value: 1.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03245 3 IEFRNVSFSYPN--QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY----KPTSGSVLLDGTDIRQLDPADL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPM----------TALNPVMTcgDQM----------DELLRAHvPMGpYERRIRildlfEEVRlpdp 153
Cdd:cd03245 77 RR----NIGYVPQDVTlfygtlrdniTLGAPLAD--DERilraaelagvTDFVNKH-PNG-LDLQIG-----ERGR---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 154 prifrsyphQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQAsilKLILELQK-KNGTAVLFITHDFGVVSeIAD 232
Cdd:cd03245 140 ---------GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE---RLKERLRQlLGDKTLIIITHRPSLLD-LVD 206
|
250
....*....|....
gi 2486247945 233 QVVVLELGKQIETG 246
Cdd:cd03245 207 RIIVMDSGRIVADG 220
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
25-261 |
1.81e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.92 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 25 PGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIAStvmgLLPKGLAPADGSVKLLGMDLFRRTPDEIRRlrgaKMAMV 104
Cdd:PRK11176 352 PGKEVP-ALRNINFKIPAGKTVALVGRSGSGKSTIAN----LLTRFYDIDEGEILLDGHDLRDYTLASLRN----QVALV 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 105 FQE-----PMTALNPVMTCGD-----QMDELLRAHVPMGPYERRIRILD--LFEEVRLpdpprifrsyphqLSGGQRQRI 172
Cdd:PRK11176 423 SQNvhlfnDTIANNIAYARTEqysreQIEEAARMAYAMDFINKMDNGLDtvIGENGVL-------------LSGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQkKNGTaVLFITHDFGVVsEIADQVVVLELGKQIETGPAKSVL 252
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQ-KNRT-SLVIAHRLSTI-EKADEILVVEDGEIVERGTHAELL 566
|
....*....
gi 2486247945 253 QHpKEPYTQ 261
Cdd:PRK11176 567 AQ-NGVYAQ 574
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-246 |
2.11e-18 |
|
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: 83.62 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLfrrTPDEI 93
Cdd:cd03369 7 IEVENLSVRYAP--DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL----EAEEGKIEIDGIDI---STIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRgAKMAMVFQEPMTALNPVMTCGDQMDEllrahvpmgpYERRirilDLFEEVRLpdpprifRSYPHQLSGGQRQRIV 173
Cdd:cd03369 78 EDLR-SSLTIIPQDPTLFSGTIRSNLDPFDE----------YSDE----EIYGALRV-------SEGGLNLSQGQRQLLC 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTTQASILKLILELQkkNGTAVLFITHDFGVVSEIaDQVVVLELGKQIETG 246
Cdd:cd03369 136 LARALLKRPRVLVLDEATASIDYATDALIQKTIREEF--TNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYD 205
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
309-514 |
2.42e-18 |
|
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: 83.35 E-value: 2.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLID--PTSGEVWVNGENVAAAP--KRKLHGLrrrlQVVFQDPYRsld 384
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPpeERARLGI----FLAFQYPPE--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 385 prmtvgesiVEGpvnfgvpkeeawkraqefmkiVRLSpDALnRYPNQ-FSGGQRQRISIARALACEPEILICDEAVSALD 463
Cdd:cd03217 89 ---------IPG---------------------VKNA-DFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 464 VsvqaDILKLLEEIQVKL---GIGILFVTHDLRVASQICDDVI-VIRRGECVESG 514
Cdd:cd03217 137 I----DALRLVAEVINKLreeGKSVLIITHYQRLLDYIKPDRVhVLYDGRIVKSG 187
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
284-524 |
3.30e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.17 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTYTlggfftGRvkvRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPkr 363
Cdd:PRK10895 3 TLTAKNLAKAYK------GR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 364 kLHGLRRR-LQVVFQDPyrSLDPRMTVGESIVEG-PVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRIS 441
Cdd:PRK10895 72 -LHARARRgIGYLPQEA--SIFRRLSVYDNLMAVlQIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 442 IARALACEPEILICDEAVSALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFF 521
Cdd:PRK10895 148 IARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
...
gi 2486247945 522 HPQ 524
Cdd:PRK10895 227 DEH 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
285-513 |
3.93e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 87.27 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTytlggfFTGrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGE-----NVAA 359
Cdd:PRK11288 5 LSFDGIGKT------FPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfaSTTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 360 ApkrklhgLRRRLQVVFQDPYrsLDPRMTVGESIVEG--PVNFG-VPKEEAWKRAQEFMKI--VRLSPDALNRYpnqFSG 434
Cdd:PRK11288 76 A-------LAAGVAIIYQELH--LVPEMTVAENLYLGqlPHKGGiVNRRLLNYEAREQLEHlgVDIDPDTPLKY---LSI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 435 GQRQRISIARALACEPEILICDEAVSALDvSVQADIL-KLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECVES 513
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEPTSSLS-AREIEQLfRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
285-509 |
4.15e-18 |
|
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: 80.96 E-value: 4.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTlggfftGRVkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVngenvaaapkrk 364
Cdd:cd03221 1 IELENLSKTYG------GKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW------------ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 lhglrrrlqvvfqdpyrslDPRMTVGesivegpvnfgvpkeeawkraqefmkivrlspdalnrYPNQFSGGQRQRISIAR 444
Cdd:cd03221 60 -------------------GSTVKIG-------------------------------------YFEQLSGGEKMRLALAK 83
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 445 ALACEPEILICDEAVSALDV-SVQAdilklLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:cd03221 84 LLLENPNLLLLDEPTNHLDLeSIEA-----LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
13-241 |
4.26e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 83.29 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLfrrtPDE 92
Cdd:cd03248 11 IVKFQNVTFAYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKS----TVVALLENFYQPQGGQVLLDGKPI----SQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRGAKMAMVFQEPmtalnpVMTCGDQMDELLR--AHVPMGpyerriRILDLFEEVRLPDPPRIFRSYPH-------- 162
Cdd:cd03248 82 EHKYLHSKVSLVGQEP------VLFARSLQDNIAYglQSCSFE------CVKEAAQKAHAHSFISELASGYDtevgekgs 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKngTAVLFITHDFGVVsEIADQVVVLELGK 241
Cdd:cd03248 150 QLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTV-ERADQILVLDGGR 225
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
12-255 |
4.86e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 83.89 E-value: 4.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppGGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPD 91
Cdd:PRK11300 4 PLLSVSGLMMRF--GGLL--AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFY----KPTGGTILLRGQHIEGLPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIrrlrgAKMAMV--FQ-----EPMTALnpvmtcgdqmDELLRA---HVPMG--------PYERRI------RILDLFEE 147
Cdd:PRK11300 76 QI-----ARMGVVrtFQhvrlfREMTVI----------ENLLVAqhqQLKTGlfsgllktPAFRRAesealdRAATWLER 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 148 VRLPDppriFRSYPH-QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGV 226
Cdd:PRK11300 141 VGLLE----HANRQAgNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
250 260
....*....|....*....|....*....
gi 2486247945 227 VSEIADQVVVLELGKQIETGPAKSVLQHP 255
Cdd:PRK11300 217 VMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-222 |
5.59e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.17 E-value: 5.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGDRpnaVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGlapaDGsvkllgmdlfrrtpdEI 93
Cdd:COG4178 363 LALEDLTLRTPDGRPL---LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG----SG---------------RI 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRGAKMAMVFQEPMtalnpvMTCGDQMDELLRAHVPmGPYERRiRILDLFEEVRLPD-PPRIFRSYP--HQLSGGQRQ 170
Cdd:COG4178 421 ARPAGARVLFLPQRPY------LPLGTLREALLYPATA-EAFSDA-ELREALEAVGLGHlAERLDEEADwdQVLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 171 RIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITH 222
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELP--GTTVISVGH 542
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
261-520 |
5.85e-18 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 87.11 E-value: 5.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 261 QKLINAVPELKPRHRPPVdgnPT-LLEAKNVVktytlggFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSI 339
Cdd:COG4618 309 NELLAAVPAEPERMPLPR---PKgRLSVENLT-------VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 340 ARLIDPTSGEVWVNGENVAAAPKRKLHglrRRL----QVV-------------FQDPyrslDPrmtvgESIVEgpvnfgv 402
Cdd:COG4618 379 VGVWPPTAGSVRLDGADLSQWDREELG---RHIgylpQDVelfdgtiaeniarFGDA----DP-----EKVVA------- 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 403 pkeeAWKRAQ--EFmkIVRLsPDAlnrY-------PNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKL 473
Cdd:COG4618 440 ----AAKLAGvhEM--ILRL-PDG---YdtrigegGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAA 509
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2486247945 474 LEEIQvKLGIGILFVTHDLRVAsQICDDVIVIRRGECVESGHVQDVF 520
Cdd:COG4618 510 IRALK-ARGATVVVITHRPSLL-AAVDKLLVLRDGRVQAFGPRDEVL 554
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
13-264 |
6.19e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.68 E-value: 6.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIA---STVMGLLPKglAPADGSVKLLGMDLF--R 87
Cdd:PRK14243 10 VLRTENLNVYY---GSFL-AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPG--FRVEGKVTFHGKNLYapD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 88 RTPDEIRRlrgaKMAMVFQEPmtalNPVMTC---------------GDqMDELLrahvpmgpyERRIRILDLFEEVRlpD 152
Cdd:PRK14243 84 VDPVEVRR----RIGMVFQKP----NPFPKSiydniaygaringykGD-MDELV---------ERSLRQAALWDEVK--D 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 153 PpriFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqkKNGTAVLFITHDFGVVSEIAD 232
Cdd:PRK14243 144 K---LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL--KEQYTIIIVTHNMQQAARVSD 218
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2486247945 233 -----QVVVLELGKQ----IETGPAKSVLQHPKEPYTQKLI 264
Cdd:PRK14243 219 mtaffNVELTEGGGRygylVEFDRTEKIFNSPQQQATRDYV 259
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
28-255 |
8.75e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 84.75 E-value: 8.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 28 DRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapADGSVKLLGMDLFRRTPdeirrlRGAKMAMVFQE 107
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQ----TSGHIRFHGTDVSRLHA------RDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 108 pmTALNPVMTCGDQ----MDELLRAHVPMGPYERRiRILDLFEEVRLPdppRIFRSYPHQLSGGQRQRIVIAMALLLKPD 183
Cdd:PRK10851 83 --YALFRHMTVFDNiafgLTVLPRRERPNAAAIKA-KVTQLLEMVQLA---HLADRYPAQLSGGQKQRVALARALAVEPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 184 LLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHP 255
Cdd:PRK10851 157 ILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
307-517 |
9.24e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.14 E-value: 9.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLI--DPTSG-EVWVNGENVAAAPK--RKLHGLRRRLQVVFQDpyR 381
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGsHIELLGRTVQREGRlaRDIRKSRANTGYIFQQ--F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 382 SLDPRMTVGESIVEGPVN--------FGVPKEEAWKRAQEFMKIVRLSPDALNRYpNQFSGGQRQRISIARALACEPEIL 453
Cdd:PRK09984 96 NLVNRLSVLENVLIGALGstpfwrtcFSWFTREQKQRALQALTRVGMVHFAHQRV-STLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 454 ICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQ 517
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
35-244 |
9.83e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 82.31 E-value: 9.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 35 HVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglAPADGSVKLLGMDLFRRTP--DEIRRLRGAKMAMvfqepmtal 112
Cdd:COG2401 48 DLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG--TPVAGCVDVPDNQFGREASliDAIGRKGDFKDAV--------- 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 113 npvmtcgdqmdELLRAhvpmgpyerririldlfeeVRLPDPPRIFRSYPHqLSGGQRQRIVIAMALLLKPDLLICDEPTT 192
Cdd:COG2401 117 -----------ELLNA-------------------VGLSDAVLWLRRFKE-LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 193 ALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIA-DQVVVLELGKQIE 244
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
308-496 |
9.91e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.51 E-value: 9.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVN-GENVAAAPKRKlhglrrrlqvvfqdpyrSLDPR 386
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAgGARVAYVPQRS-----------------EVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 MTVgesIVEGPVNFGV-PKEEAWKR-----------AQEFMKIVRLSPDALNrypnQFSGGQRQRISIARALACEPEILI 454
Cdd:NF040873 70 LPL---TVRDLVAMGRwARRGLWRRltrddraavddALERVGLADLAGRQLG----ELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2486247945 455 CDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVAS 496
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEE-HARGATVVVVTHDLELVR 183
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
14-223 |
1.56e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPpggDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfrRTPdei 93
Cdd:PRK11248 2 LQISHLYADYG---GKP-ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVP----YQHGSITLDGKPV--EGP--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 rrlrGAKMAMVFQEpmTALNPVMTCGDQMDELLR-AHVPMGpyERRIRILDLFEEVRLPDPPRifrSYPHQLSGGQRQRI 172
Cdd:PRK11248 69 ----GAERGVVFQN--EGLLPWRNVQDNVAFGLQlAGVEKM--QRLEIAHQMLKKVGLEGAEK---RYIWQLSGGQRQRV 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHD 223
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHD 188
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
14-241 |
1.67e-17 |
|
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: 79.41 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLgmdlfrrtpdei 93
Cdd:cd03221 1 IELENLSKTY---GGKL-LLKDISLTINPGDRIGLVGRNGAGKS----TLLKLIAGELEPDEGIVTWG------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 rrlrgakmamvfqepmtalnpvmtcgdqmdellrahvpmgpyeRRIRIldlfeevrlpdpprifrSYPHQLSGGQRQRIV 173
Cdd:cd03221 61 -------------------------------------------STVKI-----------------GYFEQLSGGEKMRLA 80
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 174 IAMALLLKPDLLICDEPTTALNVTtqaSILKLILELQKKNGTaVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:cd03221 81 LAKLLLENPNLLLLDEPTNHLDLE---SIEALEEALKEYPGT-VILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
36-252 |
1.78e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.90 E-value: 1.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglaPADGSVKLLGMDLFRRTPDEIRRLRGakmAMVFQEPMTALNPV 115
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRA---YLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 116 MtcgdQMdelLRAHVPMG--PYERRIRILDLFEEVRLPDppRIFRSYpHQLSGGQRQRIVIAMALL-----LKPD--LLI 186
Cdd:PRK03695 87 F----QY---LTLHQPDKtrTEAVASALNEVAEALGLDD--KLGRSV-NQLSGGEWQRVRLAAVVLqvwpdINPAgqLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 187 CDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVL 252
Cdd:PRK03695 157 LDEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
308-508 |
2.75e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 2.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKL--HGLRRRLQVV--FQDpyrsl 383
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIarMGVVRTFQHVrlFRE----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 384 dprMTVGESI-------VEGPVNFGVPK--------EEAWKRAQEFMKIVRLSPDAlNRYPNQFSGGQRQRISIARALAC 448
Cdd:PRK11300 95 ---MTVIENLlvaqhqqLKTGLFSGLLKtpafrraeSEALDRAATWLERVGLLEHA-NRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 449 EPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRG 508
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
28-253 |
4.19e-17 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 84.79 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 28 DRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRRlrgaKMAMVFQE 107
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKS----TLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRR----QMGVVLQE 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 108 PmtalnpVMTCGDQMDELLRAHvPMGPYERRIRI------LDLFEEVRlpdpprifRSYPHQ-------LSGGQRQRIVI 174
Cdd:TIGR01846 540 N------VLFSRSIRDNIALCN-PGAPFEHVIHAaklagaHDFISELP--------QGYNTEvgekganLSGGQRQRIAI 604
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 175 AMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVSEiADQVVVLELGKQIETGPAKSVLQ 253
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLA 680
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
292-504 |
4.34e-17 |
|
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: 80.92 E-value: 4.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 292 KTYTLGGFftgRVKVRAlkgvsARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKrklhglrrr 371
Cdd:cd03237 6 MKKTLGEF---TLEVEG-----GSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQ--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 372 lqvvfqdpYRSLDPRMTVGESIVEGPVNFGVPKEeaWKraQEFMKIVRLSPdALNRYPNQFSGGQRQRISIARALACEPE 451
Cdd:cd03237 69 --------YIKADYEGTVRDLLSSITKDFYTHPY--FK--TEIAKPLQIEQ-ILDREVPELSGGELQRVAIAACLSKDAD 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 452 ILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIV 504
Cdd:cd03237 136 IYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
27-267 |
4.97e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 81.35 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 27 GDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMD---LFRRTPDEIRRlrgaKMAM 103
Cdd:PRK11831 18 GNRC-IFDNISLTVPRGKITAIMGPSGIGKT----TLLRLIGGQIAPDHGEILFDGENipaMSRSRLYTVRK----RMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 104 VFQEpmTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPDPPRIFrsyPHQLSGGQRQRIVIAMALLLKPD 183
Cdd:PRK11831 89 LFQS--GALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 184 LLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSvLQHPKEPYTQKL 263
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA-LQANPDPRVRQF 242
|
....
gi 2486247945 264 INAV 267
Cdd:PRK11831 243 LDGI 246
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
309-514 |
6.00e-17 |
|
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: 84.61 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapKRKLHGLRRRLQVVFQDPY-------R 381
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA---KIGLHDLRFKITIIPQDPVlfsgslrM 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 382 SLDPRMTVGEsivegpvnfgvpkEEAWKRAQ--EFMKIVRLSPDALNRYPNQ----FSGGQRQRISIARALACEPEILIC 455
Cdd:TIGR00957 1379 NLDPFSQYSD-------------EEVWWALElaHLKTFVSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 456 DEAVSALDVS----VQADILKLLEEIQVklgigiLFVTHDLrvaSQICD--DVIVIRRGECVESG 514
Cdd:TIGR00957 1446 DEATAAVDLEtdnlIQSTIRTQFEDCTV------LTIAHRL---NTIMDytRVIVLDKGEVAEFG 1501
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
31-273 |
6.55e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 81.67 E-value: 6.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 31 NAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMD--------LFRRTPDEI-------RR 95
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALL----LPDTGTIEWIFKDeknkkktkEKEKVLEKLviqktrfKK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 96 LRGAK-----MAMVFQ-----------EPMTALNPVmtcgdqmdellrahvPMG--PYERRIRILDLFEEVRLPDpprif 157
Cdd:PRK13651 97 IKKIKeirrrVGVVFQfaeyqlfeqtiEKDIIFGPV---------------SMGvsKEEAKKRAAKYIELVGLDE----- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 158 rSY----PHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVSEIADQ 233
Cdd:PRK13651 157 -SYlqrsPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIL-VTHDLDNVLEWTKR 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2486247945 234 VVVLELGKQIETGPAKSVLQHPK---EPYTQ--KLINAVPELKPR 273
Cdd:PRK13651 235 TIFFKDGKIIKDGDTYDILSDNKfliENNMEppKLLNFVNKLEKK 279
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
305-508 |
8.06e-17 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 83.55 E-value: 8.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHglrRRLQVVFQDPyrSLD 384
Cdd:TIGR01842 330 KKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG---KHIGYLPQDV--ELF 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 385 PRmTVGESIVEGPVNFGVPK-EEAWKRAQEFMKIVRLsPDALNRYPNQ----FSGGQRQRISIARALACEPEILICDEAV 459
Cdd:TIGR01842 405 PG-TVAENIARFGENADPEKiIEAAKLAGVHELILRL-PDGYDTVIGPggatLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2486247945 460 SALDVSVQADILKLLEEIQvKLGIGILFVTHDLRVASQIcDDVIVIRRG 508
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALK-ARGITVVVITHRPSLLGCV-DKILVLQDG 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
14-247 |
9.51e-17 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 83.47 E-value: 9.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENlaVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEI 93
Cdd:TIGR03797 452 IEVDR--VTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKS----TLLRLLLGFETPESGSVFYDGQDLAGLDVQAV 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQepmtalNPVMTCGDQMDELLrAHVPMGPYE--RRIRILDLFEEVRlpDPPRIFRSYPHQ----LSGG 167
Cdd:TIGR03797 526 RR----QLGVVLQ------NGRLMSGSIFENIA-GGAPLTLDEawEAARMAGLAEDIR--AMPMGMHTVISEgggtLSGG 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASIlklILELQKKNGTAVLfITHDFGVVSEiADQVVVLELGKQIETGP 247
Cdd:TIGR03797 593 QRQRLLIARALVRKPRILLFDEATSALDNRTQAIV---SESLERLKVTRIV-IAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
32-255 |
9.53e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 80.62 E-value: 9.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRTPDEIRRLRGakmaMVFQEPM-- 109
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIL----KPTSGSVLIRGEPITKENIREVRKFVG----LVFQNPDdq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 110 ---------TALNPvmtCGDQMDELLRAHvpmgPYERRIRILDLfEEVRlpdpprifRSYPHQLSGGQRQRIVIAMALLL 180
Cdd:PRK13652 91 ifsptveqdIAFGP---INLGLDEETVAH----RVSSALHMLGL-EELR--------DRVPHHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 181 KPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHP 255
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
13-243 |
1.14e-16 |
|
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: 78.36 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNA--VEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGlaPADGSVKLLGMDlfrRTP 90
Cdd:cd03213 3 TLSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL--GVSGEVLINGRP---LDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLrgakMAMVFQEPMtaLNPVMTcgdqMDELLRahvpmgpYERRIRildlfeevrlpdpprifrsyphQLSGGQRQ 170
Cdd:cd03213 78 RSFRKI----IGYVPQDDI--LHPTLT----VRETLM-------FAAKLR----------------------GLSGGERK 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 171 RIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITH-----DFGVvseiADQVVVLELGKQI 243
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRL-ADTGRTIICSIHqpsseIFEL----FDKLLLLSQGRVI 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
8-241 |
1.83e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 82.02 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 8 AQKLPVLEVENLAvslppgGDrpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFR 87
Cdd:PRK15439 263 AAGAPVLTVEDLT------GE---GFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRP----ARGGRIMLNGKEINA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 88 RTPdEIRRLRGA-------KMAMVFQEPMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDlfeeVRLPDPPRIFRSy 160
Cdd:PRK15439 330 LST-AQRLARGLvylpedrQSSGLYLDAPLAWNVCALTHNRRGFWIKPARENAVLERYRRALN----IKFNHAEQAART- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 161 phqLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNgTAVLFITHDFGVVSEIADQVVVLELG 240
Cdd:PRK15439 404 ---LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQN-VAVLFISSDLEEIEQMADRVLVMHQG 479
|
.
gi 2486247945 241 K 241
Cdd:PRK15439 480 E 480
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
43-241 |
2.08e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 79.34 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 43 GEVTCLIGESGSGKSviasTVMGLLpKGLAPADGSVKLLGMDLFRRTPDEIRrlrgakmaMVFQEpmTALNPVMTCGDQM 122
Cdd:PRK11247 38 GQFVAVVGRSGCGKS----TLLRLL-AGLETPSAGELLAGTAPLAEAREDTR--------LMFQD--ARLLPWKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 123 DELLRAHvpmgpyeRRIRILDLFEEVRLPDpprifRS--YPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQA 200
Cdd:PRK11247 103 GLGLKGQ-------WRDAALQALAAVGLAD-----RAneWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2486247945 201 SILKLILELQKKNGTAVLFITHDfgvVSE---IADQVVVLELGK 241
Cdd:PRK11247 171 EMQDLIESLWQQHGFTVLLVTHD---VSEavaMADRVLLIEEGK 211
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
307-524 |
2.52e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVwvngenvaaapkRKLHGLRrrLQVVFQDPYrsLDPR 386
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------------KRNGKLR--IGYVPQKLY--LDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 M--TVGESIVEGPvnfGVPKEE---AWKRAQefmkivrlsPDALNRYPNQ-FSGGQRQRISIARALACEPEILICDEAVS 460
Cdd:PRK09544 82 LplTVNRFLRLRP---GTKKEDilpALKRVQ---------AGHLIDAPMQkLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 461 ALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVeSGHVQDVFFHPQ 524
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICC-SGTPEVVSLHPE 212
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
274-512 |
2.62e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 82.86 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 274 HRPPvDGNPT--LLEAKNVVKTYtlggfftgRVKVR-ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEV 350
Cdd:PLN03130 1226 NRPP-PGWPSsgSIKFEDVVLRY--------RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 351 WVNGENVAaapKRKLHGLRRRLQVVFQDPYR-------SLDPrmtvgesivegpvnFGVPKE----EAWKRAQeFMKIVR 419
Cdd:PLN03130 1297 LIDGCDIS---KFGLMDLRKVLGIIPQAPVLfsgtvrfNLDP--------------FNEHNDadlwESLERAH-LKDVIR 1358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 420 LSPDALNRYPNQ----FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLL-EEIQvklGIGILFVTHdlRV 494
Cdd:PLN03130 1359 RNSLGLDAEVSEagenFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIrEEFK---SCTMLIIAH--RL 1433
|
250
....*....|....*....
gi 2486247945 495 ASQI-CDDVIVIRRGECVE 512
Cdd:PLN03130 1434 NTIIdCDRILVLDAGRVVE 1452
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
45-252 |
3.11e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 45 VTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLG--MDLFRRTPDEIRRlrgaKMAMVFQEPMTALNPVMTCGDQM 122
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLL----RPQKGAVLWQGkpLDYSKRGLLALRQ----QVATVFQDPEQQIFYTDIDSDIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 123 DELLRAHVPMGPYERRIRildlfEEVRLPDPPRiFRSYPHQ-LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQAS 201
Cdd:PRK13638 101 FSLRNLGVPEAEITRRVD-----EALTLVDAQH-FRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 202 ILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVL 252
Cdd:PRK13638 175 MIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
312-519 |
3.25e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 78.44 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 312 VSARLRRGETIGIVGESGSGKSTFARSIARLIdPTSGEVWVNGENVAAAPKRKLHGLRRRL--QV-------VFQdpYRS 382
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLsqQQtppfampVFQ--YLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 383 LdprmtvgesivEGPVnfGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARA-LACEPEI------LIC 455
Cdd:PRK03695 92 L-----------HQPD--KTRTEAVASALNEVAEALGLD-DKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 456 DEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDV 519
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEV 220
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
33-264 |
3.46e-16 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 81.91 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 33 VEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLfrrtpDEI-RRLRGAKMAMVFQ----- 106
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLY----QPWSGEILFDGIPR-----EEIpREVLANSVAMVDQdiflf 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 107 -----EPMTALNPVMTcgdqMDELLRAhvpmgpyERRIRILDLFeeVRLPDpprifrSYPHQL-------SGGQRQRIVI 174
Cdd:TIGR03796 566 egtvrDNLTLWDPTIP----DADLVRA-------CKDAAIHDVI--TSRPG------GYDAELaegganlSGGQRQRLEI 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 175 AMALLLKPDLLICDEPTTALNVTTQasilKLILELQKKNGTAVLFITHDFGVVSEiADQVVVLELGKQIETGPAKSVLQH 254
Cdd:TIGR03796 627 ARALVRNPSILILDEATSALDPETE----KIIDDNLRRRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAV 701
|
250
....*....|
gi 2486247945 255 PKePYtQKLI 264
Cdd:TIGR03796 702 GG-AY-ARLI 709
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
164-498 |
6.01e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 80.75 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQAsilklILE--LQKKNGTaVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVA-----WLErhLQEYPGT-VVAVTHDRYFLDNVAGWILELDRGR 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 242 QI----------ETGPAKSVLQHPKEPYTQKLINAvpEL-------KPRHR----------------------------P 276
Cdd:TIGR03719 236 GIpwegnysswlEQKQKRLEQEEKEESARQKTLKR--ELewvrqspKGRQAkskarlaryeellsqefqkrnetaeiyiP 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 277 PvdgNPTL----LEAKNVVKTYtlggffTGRVkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWV 352
Cdd:TIGR03719 314 P---GPRLgdkvIEAENLTKAF------GDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 353 nGENVaaapkrklhglrrrlQVVFQDPYR-SLDPRMTVGESIVEGPVNFGVPKEEAWKRA---------QEFMKIVrlsp 422
Cdd:TIGR03719 382 -GETV---------------KLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKV---- 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 423 dalnrypNQFSGGQRQRISIARALACEPEILICDEAVSALDVsvqaDILKLLEEIQVKLGIGILFVTHDL----RVASQI 498
Cdd:TIGR03719 442 -------GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHDRwfldRIATHI 510
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-247 |
7.31e-16 |
|
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: 76.76 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGdrPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03244 3 IEFKNVSLRYRPNL--PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE----LSSGSILIDGVDISKIGLHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPmtalnpVMTCGDqmdelLRAHV-PMGPY--ERRIRILdlfEEVRLPDpprIFRSYPHQL------ 164
Cdd:cd03244 77 RS----RISIIPQDP------VLFSGT-----IRSNLdPFGEYsdEELWQAL---ERVGLKE---FVESLPGGLdtvvee 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 165 -----SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILElQKKNGTaVLFITH------DFgvvseiaDQ 233
Cdd:cd03244 136 ggenlSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCT-VLTIAHrldtiiDS-------DR 206
|
250
....*....|....
gi 2486247945 234 VVVLELGKQIETGP 247
Cdd:cd03244 207 ILVLDKGRVVEFDS 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
309-490 |
8.86e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 80.24 E-value: 8.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWV-NGENVAAAPKR---KLHGLRRrlQVVFqdPYRSLD 384
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQRpylPLGTLRE--ALLY--PATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 385 prmtvgesivegpvnfgVPKEEAwkraQEFMKIVRLSP-----DALNRYPNQFSGGQRQRISIARALACEPEILICDEAV 459
Cdd:COG4178 455 -----------------FSDAEL----REALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|..
gi 2486247945 460 SALDVSVQADILKLLEEiqvKL-GIGILFVTH 490
Cdd:COG4178 514 SALDEENEAALYQLLRE---ELpGTTVISVGH 542
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
309-536 |
9.76e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.79 E-value: 9.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAaapKRKLHGLRRRLQVVFQDPYrsldprmt 388
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVA---KFGLTDLRRVLSIIPQSPV-------- 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 vgesIVEGPVNFGV-PKEE--------AWKRAQeFMKIVRLSPDALNRYPNQ----FSGGQRQRISIARALACEPEILIC 455
Cdd:PLN03232 1321 ----LFSGTVRFNIdPFSEhndadlweALERAH-IKDVIDRNPFGLDAEVSEggenFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 456 DEAVSALDVSVQADILKLLEEiQVKlGIGILFVTHDLRVASQiCDDVIVIRRGECVESGHVQDVFFHPQHEYTKSLIAAA 535
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIRE-EFK-SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG 1472
|
.
gi 2486247945 536 P 536
Cdd:PLN03232 1473 P 1473
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
36-253 |
1.00e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRRlrgaKMAMVFQEPMTALNpv 115
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKS----TLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----KVAYLPQQLPAAEG-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 116 MTcgdqmdelLRAHVPMGPY-----------ERRIRILDLFEEVRL-PDPPRIFRSyphqLSGGQRQRIVIAMALLLKPD 183
Cdd:PRK10575 100 MT--------VRELVAIGRYpwhgalgrfgaADREKVEEAISLVGLkPLAHRLVDS----LSGGERQRAWIAMLVAQDSR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 184 LLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQ 253
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
12-256 |
1.22e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.69 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRpNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSvkllgmdlfrrtpd 91
Cdd:PRK09544 3 SLVSLENVSVSF---GQR-RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLV----APDEGV-------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 eIRRLRGAKMAMVFQEpmTALNPVMTCGDQMDELLRahvpmgPYERRIRILDLFEEVR---LPDPPRifrsypHQLSGGQ 168
Cdd:PRK09544 61 -IKRNGKLRIGYVPQK--LYLDTTLPLTVNRFLRLR------PGTKKEDILPALKRVQaghLIDAPM------QKLSGGE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 169 RQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQvvVLELGKQI-ETGP 247
Cdd:PRK09544 126 TQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDE--VLCLNHHIcCSGT 203
|
....*....
gi 2486247945 248 AKSVLQHPK 256
Cdd:PRK09544 204 PEVVSLHPE 212
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
308-518 |
1.29e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.87 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRklhGLRRRLQVVFQDPY------- 380
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA---ALRQAISVVSQRVHlfsatlr 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 381 --------RSLDPRMT-----VG-ESIVEGPvnfgvPKEEAWkraqefmkivrlspdaLNRYPNQFSGGQRQRISIARAL 446
Cdd:PRK11160 432 dnlllaapNASDEALIevlqqVGlEKLLEDD-----KGLNAW----------------LGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 447 ACEPEILICDEAVSALDVSVQADILKLLEeiQVKLGIGILFVTHDLRVASQIcDDVIVIRRGECVESGHVQD 518
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLA--EHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQE 559
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
12-256 |
2.99e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.45 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMD-----LF 86
Cdd:COG1137 2 MTLEAENLVKSY---GKRT-VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK----PDSGRIFLDGEDithlpMH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 87 RRtpdeirrlrgAKMAMVF--QEP-----MTALnpvmtcgdqmdELLRA---HVPMGPYERRIRILDLFEEVRLPdppRI 156
Cdd:COG1137 74 KR----------ARLGIGYlpQEAsifrkLTVE-----------DNILAvleLRKLSKKEREERLEELLEEFGIT---HL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 157 FRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLfIT-HDfgvVSE---IAD 232
Cdd:COG1137 130 RKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVL-ITdHN---VREtlgICD 204
|
250 260
....*....|....*....|....
gi 2486247945 233 QVVVLELGKQIETGPAKSVLQHPK 256
Cdd:COG1137 205 RAYIISEGKVLAEGTPEEILNNPL 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
297-508 |
3.96e-15 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 74.67 E-value: 3.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 297 GGFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENvAAAPKRKLHGLRRRLQVVF 376
Cdd:cd03290 5 NGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKN-ESEPSFEATRSRNRYSVAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 377 --QDPYrsldprmtVGESIVEGPVNFGVPKEEawKRAQEFMKIVRLSPDA-LNRYPNQ---------FSGGQRQRISIAR 444
Cdd:cd03290 84 aaQKPW--------LLNATVEENITFGSPFNK--QRYKAVTDACSLQPDIdLLPFGDQteigerginLSGGQRQRICVAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 445 ALACEPEILICDEAVSALDVSV-----QADILKLLEEIQVKLgigiLFVTHDLRVASQiCDDVIVIRRG 508
Cdd:cd03290 154 ALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKRTL----VLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
309-514 |
4.52e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.06 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARliDP----TSGEVWVNGENV-AAAPKRKLHglrRRLQVVFQDPyrsl 383
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPaykiLEGDILFKGESIlDLEPEERAH---LGIFLAFQYP---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 384 dprmtvgesiVEGPvnfGVPKEE----AWKRAQEFM------------------KIVRLSPDALNRYPNQ-FSGGQRQRI 440
Cdd:CHL00131 94 ----------IEIP---GVSNADflrlAYNSKRKFQglpeldplefleiineklKLVGMDPSFLSRNVNEgFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 441 SIARALACEPEILICDEAVSALDVsvqaDILKLLEEIQVKL---GIGILFVTHDLRVASQICDDVI-VIRRGECVESG 514
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDI----DALKIIAEGINKLmtsENSIILITHYQRLLDYIKPDYVhVMQNGKIIKTG 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
284-513 |
6.50e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.14 E-value: 6.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 284 LLEAKNVVKTytlggfFTGrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARlIDPT---SGEVWVNGEnvaaa 360
Cdd:NF040905 1 ILEMRGITKT------FPG---VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGE----- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 pKRKLHGLR--RRLQVVFQDPYRSLDPRMTVGESIVEG--PVNFGVPK-EEAWKRAQEFMKIVRL--SPDALnryPNQFS 433
Cdd:NF040905 66 -VCRFKDIRdsEALGIVIIHQELALIPYLSIAENIFLGneRAKRGVIDwNETNRRARELLAKVGLdeSPDTL---VTDIG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 434 GGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECVES 513
Cdd:NF040905 142 VGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
285-491 |
7.93e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 77.32 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGGFftgrvkvrALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAApkrK 364
Cdd:PRK10522 323 LELRNVTFAYQDNGF--------SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE---Q 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 365 LHGLRRRLQVVFQDPYrsLDPRMTvgesiveGPVNFGVPKE--EAWKRAQEFMKIVRLSPdalNRYPN-QFSGGQRQRIS 441
Cdd:PRK10522 392 PEDYRKLFSAVFTDFH--LFDQLL-------GPEGKPANPAlvEKWLERLKMAHKLELED---GRISNlKLSKGQKKRLA 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 442 IARALACEPEILICDEAvsALDVSVQ------ADILKLLEEiqvkLGIGILFVTHD 491
Cdd:PRK10522 460 LLLALAEERDILLLDEW--AADQDPHfrrefyQVLLPLLQE----MGKTIFAISHD 509
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
15-253 |
8.34e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 74.35 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 15 EVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIR 94
Cdd:COG4604 3 EIKNVSKRY---GGKV-VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLP----PDSGEVLVDGLDVATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 95 RlrgaKMAMVFQEPmtALNPVMTcgdqMDELL----------------RAHVpmgpyERRIRILDLfEEVRlpdpprifR 158
Cdd:COG4604 75 K----RLAILRQEN--HINSRLT----VRELVafgrfpyskgrltaedREII-----DEAIAYLDL-EDLA--------D 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 159 SYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLE 238
Cdd:COG4604 131 RYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMK 210
|
250
....*....|....*
gi 2486247945 239 LGKQIETGPAKSVLQ 253
Cdd:COG4604 211 DGRVVAQGTPEEIIT 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
13-254 |
9.45e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 9.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLP------------------PGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKsviaSTVMGLLPKGLAPA 74
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGK----STLLKLIAGILEPT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 75 DGSVKLLGmdlfrrtpdeirrlrgaKMAMVFqEPMTALNPVMTCGDQMdeLLRAHVpMGpyERRIRILDLFEEVR----- 149
Cdd:COG1134 80 SGRVEVNG-----------------RVSALL-ELGAGFHPELTGRENI--YLNGRL-LG--LSRKEIDEKFDEIVefael 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 150 -----LPdppriFRSYphqlSGGQRQRIVIAMALLLKPDLLICDEpttALNVTT---QASILKLILELqKKNGTAVLFIT 221
Cdd:COG1134 137 gdfidQP-----VKTY----SSGMRARLAFAVATAVDPDILLVDE---VLAVGDaafQKKCLARIREL-RESGRTVIFVS 203
|
250 260 270
....*....|....*....|....*....|...
gi 2486247945 222 HDFGVVSEIADQVVVLELGKQIETGPAKSVLQH 254
Cdd:COG1134 204 HSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
12-241 |
1.00e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKllgmdlfrrtpd 91
Cdd:COG0488 314 KVLELEGLSKSY---GDKT-LLDDLSLRIDRGDRIGLIGPNGAGKS----TLLKLLAGELEPDSGTVK------------ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 eirrlRGAKMAMVF--QEpMTALNPVMTCgdqMDELLRAHVpmGPYERRIR-ILDLFeevrLPDPPRIFRsYPHQLSGGQ 168
Cdd:COG0488 374 -----LGETVKIGYfdQH-QEELDPDKTV---LDELRDGAP--GGTEQEVRgYLGRF----LFSGDDAFK-PVGVLSGGE 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 169 RQRIVIAMALLLKPDLLICDEPTTALNVTTQAsilklILE--LQKKNGTaVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:COG0488 438 KARLALAKLLLSPPNVLLLDEPTNHLDIETLE-----ALEeaLDDFPGT-VLLVSHDRYFLDRVATRILEFEDGG 506
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
303-505 |
1.03e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.45 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 303 RVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLI--DPTSGEVWVngenvaaapkrklhglrrrlqvvfqdPY 380
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV--------------------------PD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 381 RSLDPRMTVGESIvegpvnfgvPKEEAWKRAQEFMKIVRLSpDALN--RYPNQFSGGQRQRISIARALACEPEILICDEA 458
Cdd:COG2401 94 NQFGREASLIDAI---------GRKGDFKDAVELLNAVGLS-DAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2486247945 459 VSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVI 505
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
300-535 |
1.14e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 77.38 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 300 FTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLID----------------------------------- 344
Cdd:PTZ00265 1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmkn 1254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 345 -------------------PTSGEVWVNGENVAaapKRKLHGLRRRLQVVFQDPyrsldprMTVGESIVEGpVNFGvpKE 405
Cdd:PTZ00265 1255 vnefsltkeggsgedstvfKNSGKILLDGVDIC---DYNLKDLRNLFSIVSQEP-------MLFNMSIYEN-IKFG--KE 1321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 406 EAW----KRAQEFMKIVRLSPDALNRYPNQ-------FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLL 474
Cdd:PTZ00265 1322 DATredvKRACKFAAIDEFIESLPNKYDTNvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 475 EEIQVKLGIGILFVTHdlRVASQICDDVIVI-----RRGECVESGHVQDVFFHPQHEYTKSLIAAA 535
Cdd:PTZ00265 1402 VDIKDKADKTIITIAH--RIASIKRSDKIVVfnnpdRTGSFVQAHGTHEELLSVQDGVYKKYVKLA 1465
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-240 |
1.21e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 74.28 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLAPaDGSVKLLGMDLFR--RTP 90
Cdd:PRK09984 4 IIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSA-GSHIELLGRTVQRegRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLRgAKMAMVFQE-----PMTALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLPdpprifrSYPHQ-- 163
Cdd:PRK09984 79 RDIRKSR-ANTGYIFQQfnlvnRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMV-------HFAHQrv 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 164 --LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELG 240
Cdd:PRK09984 151 stLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
27-246 |
1.28e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.25 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 27 GDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfrrtPDEIRRLRgAKMAMVFQ 106
Cdd:PRK13536 52 GDKA-VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTS----PDAGKITVLGVPV----PARARLAR-ARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 107 epMTALNPVMTCGDQMDELLRaHVPMGPYERRIRILDLFEEVRLPDPPRIFRSyphQLSGGQRQRIVIAMALLLKPDLLI 186
Cdd:PRK13536 122 --FDNLDLEFTVRENLLVFGR-YFGMSTREIEAVIPSLLEFARLESKADARVS---DLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 187 CDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
35-253 |
1.96e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 72.69 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 35 HVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDlFRRTPDEIRRLrgakmAMVFQEP-----M 109
Cdd:PRK10771 17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLT----PASGSLTLNGQD-HTTTPPSRRPV-----SMLFQENnlfshL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 110 T-------ALNPVMTCGDQMDELLRAHVpmgpyeRRIRILDLFEevRLPdpprifrsypHQLSGGQRQRIVIAMALLLKP 182
Cdd:PRK10771 87 TvaqniglGLNPGLKLNAAQREKLHAIA------RQMGIEDLLA--RLP----------GQLSGGQRQRVALARCLVREQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 183 DLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQ 253
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
163-334 |
2.05e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 75.82 E-value: 2.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLfITHDFGVVSEIADQVVVLELGKQ 242
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL-VLNRFDEIPDFVQFAGVLADCTL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 243 IETGPAKSVLQH---PKEPYTQKLIN-AVPEL-KPRHRPPVDGNPTLLEAKNVVKTYTlggfftgrvKVRALKGVSARLR 317
Cdd:PRK10938 214 AETGEREEILQQalvAQLAHSEQLEGvQLPEPdEPSARHALPANEPRIVLNNGVVSYN---------DRPILHNLSWQVN 284
|
170
....*....|....*..
gi 2486247945 318 RGETIGIVGESGSGKST 334
Cdd:PRK10938 285 PGEHWQIVGPNGAGKST 301
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-255 |
2.65e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 75.52 E-value: 2.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 25 PGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRrlrgAKMAMV 104
Cdd:PRK10789 324 PQTDHP-ALENVNFTLKPGQMLGICGPTGSGKS----TLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWR----SRLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 105 FQEPM-----TALNPVMTCGDQMDELLrahvpmgpyERRIRILDLFEEV-RLPdpprifRSYPHQ-------LSGGQRQR 171
Cdd:PRK10789 395 SQTPFlfsdtVANNIALGRPDATQQEI---------EHVARLASVHDDIlRLP------QGYDTEvgergvmLSGGQKQR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 172 IVIAMALLLKPDLLICDEPTTALNVTTQASILKLIleLQKKNGTAVLFITHDFGVVSEiADQVVVLELGKQIETGPAKSV 251
Cdd:PRK10789 460 ISIARALLLNAEILILDDALSAVDGRTEHQILHNL--RQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQL 536
|
....
gi 2486247945 252 LQHP 255
Cdd:PRK10789 537 AQQS 540
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-241 |
3.38e-14 |
|
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: 71.35 E-value: 3.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGDRPNAVEH-VSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapADGSVKLLGmdlfrrtpde 92
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKdINLEVPKGELVAIVGPVGSGKSSLLSALLGELEK----LSGSVSVPG---------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 irrlrgaKMAMVFQEP--MTAL---NPVMtcGDQMDELLrahvpmgpYERRIRILDLfeevrLPDppriFRSYPHQ---- 163
Cdd:cd03250 67 -------SIAYVSQEPwiQNGTireNILF--GKPFDEER--------YEKVIKACAL-----EPD----LEILPDGdlte 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 -------LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASIL-KLILELQKKNGTAVLfITHDFGVVSEiADQVV 235
Cdd:cd03250 121 igekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRIL-VTHQLQLLPH-ADQIV 198
|
....*.
gi 2486247945 236 VLELGK 241
Cdd:cd03250 199 VLDNGR 204
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-237 |
3.47e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.05 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 1 MTESSlraqklPVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKL 80
Cdd:PRK10247 1 MQENS------PLLQLQNVGYLA---GDAK-ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLI----SPTSGTLLF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 81 LGMDLFRRTPDEIRRlrgaKMAMVFQEPMTAlnpvmtcGDQM-DELLRahvpmgPYERR------IRILDLFEEVRLPDp 153
Cdd:PRK10247 67 EGEDISTLKPEIYRQ----QVSYCAQTPTLF-------GDTVyDNLIF------PWQIRnqqpdpAIFLDDLERFALPD- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 154 pRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfgvVSEI--A 231
Cdd:PRK10247 129 -TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD---KDEInhA 204
|
....*.
gi 2486247945 232 DQVVVL 237
Cdd:PRK10247 205 DKVITL 210
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-246 |
3.56e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 75.27 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVsLPPGGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglapADGSVKLLGMDLFRRTPDEI 93
Cdd:PRK11174 350 IEAEDLEI-LSPDGKT--LAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-----YQGSLKINGIELRELDPESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQepmtalNPVMTCGDQMDELLRAHVPMGPYE-----RRIRILDLFEevRLPDpprifrSYPHQ----- 163
Cdd:PRK11174 422 RK----HLSWVGQ------NPQLPHGTLRDNVLLGNPDASDEQlqqalENAWVSEFLP--LLPQ------GLDTPigdqa 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 --LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqkKNGTAVLFITHDfgvVSEIA--DQVVVLEL 239
Cdd:PRK11174 484 agLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQ---LEDLAqwDQIWVMQD 558
|
....*..
gi 2486247945 240 GKQIETG 246
Cdd:PRK11174 559 GQIVQQG 565
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
32-250 |
4.34e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRtpdeirrLRGAKMAMVFQ-EPMT 110
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV----RLASGKISILGQPTRQA-------LQKNLVAYVPQsEEVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 111 ALNPVmtcgdqmdeLLRAHVPMGPY-----------ERRIRILDLFEEVRLPDpprifrsYPH----QLSGGQRQRIVIA 175
Cdd:PRK15056 91 WSFPV---------LVEDVVMMGRYghmgwlrrakkRDRQIVTAALARVDMVE-------FRHrqigELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 176 MALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLElGKQIETGPAKS 250
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTET 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
308-520 |
4.76e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 4.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhglrrrlqVVFQDPYRSLDPRM 387
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--------VAYVPQSEEVDWSF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVgesIVEGPVNFG---------VPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEA 458
Cdd:PRK15056 94 PV---LVEDVVMMGryghmgwlrRAKKRDRQIVTAALARVDMV-EFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 459 VSALDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIrRGECVESGHVQDVF 520
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTF 229
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-253 |
4.86e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.75 E-value: 4.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppGGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:PRK10790 341 IDIDNVSFAY--RDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHSVL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRlrgaKMAMVFQEPMTalnpvmtcgdqMDELLRAHVPMGPYERRIRILDLFEEVRLPDpprIFRSYP-----------H 162
Cdd:PRK10790 414 RQ----GVAMVQQDPVV-----------LADTFLANVTLGRDISEEQVWQALETVQLAE---LARSLPdglytplgeqgN 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKngTAVLFITHDFGVVSEiADQVVVLELGKQ 242
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
250
....*....|.
gi 2486247945 243 IETGPAKSVLQ 253
Cdd:PRK10790 553 VEQGTHQQLLA 563
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-264 |
5.32e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 74.48 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 3 ESSLRAQKLPVLEVENLAVSLPPGGDrpNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLG 82
Cdd:PRK11160 328 TTSTAAADQVSLTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKS----TLLQLLTRAWDPQQGEILLNG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 83 MDLFRRTPDEIRRLrgakMAMVFQEP---MTAL--NPVMTCGDQMDELLRAHVpmgpyeRRIRILDLFEEVR-----LPD 152
Cdd:PRK11160 402 QPIADYSEAALRQA----ISVVSQRVhlfSATLrdNLLLAAPNASDEALIEVL------QQVGLEKLLEDDKglnawLGE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 153 PPRifrsyphQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHD-FGVvsEIA 231
Cdd:PRK11160 472 GGR-------QLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRlTGL--EQF 540
|
250 260 270
....*....|....*....|....*....|...
gi 2486247945 232 DQVVVLELGKQIETGPAKSVLQhpKEPYTQKLI 264
Cdd:PRK11160 541 DRICVMDNGQIIEQGTHQELLA--QQGRYYQLK 571
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
322-517 |
8.29e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 322 IGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhglRRRLQVVFQDPY---RSLDPRMTVGESIVEgpv 398
Cdd:PRK10790 370 VALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL---RQGVAMVQQDPVvlaDTFLANVTLGRDISE--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 399 nfgvpkEEAWK--RAQEFMKIVRLSPDALN----RYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILK 472
Cdd:PRK10790 444 ------EQVWQalETVQLAELARSLPDGLYtplgEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQ 517
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2486247945 473 LLEEIQVKlgIGILFVTHDLrvaSQI--CDDVIVIRRGECVESGHVQ 517
Cdd:PRK10790 518 ALAAVREH--TTLVVIAHRL---STIveADTILVLHRGQAVEQGTHQ 559
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-222 |
8.58e-14 |
|
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: 70.08 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfrrtpDEI 93
Cdd:TIGR01189 1 LAARNLACSR---GERM-LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLR----PDSGEVRWNGTPL-----AEQ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRGAKMAMVFQEPmtALNPVMTcgdqMDELLRAHVPMGPYERRiRILDLFEEVRLPDppriFRSYP-HQLSGGQRQRI 172
Cdd:TIGR01189 68 RDEPHENILYLGHLP--GLKPELS----ALENLHFWAAIHGGAQR-TIEDALAAVGLTG----FEDLPaAQLSAGQQRRL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2486247945 173 VIAMALLLKPDLLICDEPTTALNVTTQAsILKLILELQKKNGTAVLFITH 222
Cdd:TIGR01189 137 ALARLWLSRRPLWILDEPTTALDKAGVA-LLAGLLRAHLARGGIVLLTTH 185
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
14-256 |
1.08e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 70.65 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEi 93
Cdd:cd03218 1 LRAENLSKRY---GKRK-VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK----PDSGKILLDGQDITKLPMHK- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRG----AKMAMVFQEpMTALNPVMtCGDQMDELLRAhvpmgpyERRIRILDLFEEVRLPdppRIFRSYPHQLSGGQR 169
Cdd:cd03218 72 RARLGigylPQEASIFRK-LTVEENIL-AVLEIRGLSKK-------EREEKLEELLEEFHIT---HLRKSKASSLSGGER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 170 QRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAK 249
Cdd:cd03218 140 RRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPE 218
|
....*..
gi 2486247945 250 SVLQHPK 256
Cdd:cd03218 219 EIAANEL 225
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
308-526 |
1.26e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.00 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHGlrrrlqvvfqdpyrsldpRM 387
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSG------------------QL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQ 467
Cdd:PRK13546 101 TGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELG-EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 468 ADILKLLEEIQvKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFfhPQHE 526
Cdd:PRK13546 180 QKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL--PKYE 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
32-246 |
1.52e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.87 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGmdlfrrtpdeirrlrgaKMAMVFqEPMTA 111
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYP----PDSGTVTVRG-----------------RVSSLL-GLGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTcGdqMDELLRAHVPMG-----PYERRIRILDLFEevrLPDppriFRSYP-HQLSGGQRQRIVIAMALLLKPDLL 185
Cdd:cd03220 95 FNPELT-G--RENIYLNGRLLGlsrkeIDEKIDEIIEFSE---LGD----FIDLPvKTYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 186 ICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03220 165 LIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
14-222 |
1.80e-13 |
|
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: 68.33 E-value: 1.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGDRpnaVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGlapaDGSvkllgmdlfrrtpdeI 93
Cdd:cd03223 1 IELENLSLATPDGRVL---LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG----SGR---------------I 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRLRGAKMAMVFQEP-MTALNpvmtcgdqmdelLRAHVpmgpyerririldlfeevrlpdpprifrSYP--HQLSGGQRQ 170
Cdd:cd03223 59 GMPEGEDLLFLPQRPyLPLGT------------LREQL----------------------------IYPwdDVLSGGEQQ 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 171 RIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqkknGTAVLFITH 222
Cdd:cd03223 99 RLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL----GITVISVGH 146
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
302-514 |
1.98e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 69.21 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 302 GRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPT---SGEVWVNGENVAAApKRKLHGlrrrlQVVFQD 378
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEF-AEKYPG-----EIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 379 PYRSLDPRMTVGESIvegpvnfgvpkeeawkraqEFmkivrlspdAL----NRYPNQFSGGQRQRISIARALACEPEILI 454
Cdd:cd03233 90 EEDVHFPTLTVRETL-------------------DF---------ALrckgNEFVRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 455 CDEAVSALDVSVQADILKLLEEIQVKLGiGILFVThdLRVASQIC----DDVIVIRRGECVESG 514
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVLK-TTTFVS--LYQASDEIydlfDKVLVLYEGRQIYYG 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
277-538 |
2.30e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.77 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 277 PVDGNPTLLEAKNVVKTYTLGGFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDP---TSGEVWVN 353
Cdd:TIGR00955 9 DVFGRVAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 354 GEnvaaapKRKLHGLRRRLQVVFQDPYrsLDPRMTVGES-IVEGPVNFG--VPKEEAWKRAQEFMKIVRLSPDALNR--Y 428
Cdd:TIGR00955 89 GM------PIDAKEMRAISAYVQQDDL--FIPTLTVREHlMFQAHLRMPrrVTKKEKRERVDEVLQALGLRKCANTRigV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 429 PNQ---FSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKlGIGILFVTHdlRVASQI---CDDV 502
Cdd:TIGR00955 161 PGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIH--QPSSELfelFDKI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2486247945 503 IVIRRGECVESGHVQDV--FF----HPQHEYTK------SLIAAAPGT 538
Cdd:TIGR00955 238 ILMAEGRVAYLGSPDQAvpFFsdlgHPCPENYNpadfyvQVLAVIPGS 285
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
13-241 |
2.42e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.27 E-value: 2.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLP--PGGDRpnaVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglAPADGSVKLLGMDLFRRTP 90
Cdd:PRK13549 259 ILEVRNLTAWDPvnPHIKR---VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP---GRWEGEIFIDGKPVKIRNP 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 -DEIRrlrgAKMAMVFQE-PMTALNPVMTCGDQMdeLLRAhvpMGPYERRIRILDLFEE-----------VRLPDPP-RI 156
Cdd:PRK13549 333 qQAIA----QGIAMVPEDrKRDGIVPVMGVGKNI--TLAA---LDRFTGGSRIDDAAELktilesiqrlkVKTASPElAI 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 157 FRsyphqLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVV 236
Cdd:PRK13549 404 AR-----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLV 477
|
....*
gi 2486247945 237 LELGK 241
Cdd:PRK13549 478 MHEGK 482
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
13-241 |
2.64e-13 |
|
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: 72.16 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPNaVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLApadGSVKLLGMDLFRRTP-D 91
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKR-VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFE---GNVFINGKPVDIRNPaQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRrlrgAKMAMVFQE-PMTALNPVMTCGDQMDelLRAhvpMGPYERRIRILDLFEE-------VRL------PDPPrIF 157
Cdd:TIGR02633 333 AIR----AGIAMVPEDrKRHGIVPILGVGKNIT--LSV---LKSFCFKMRIDAAAELqiigsaiQRLkvktasPFLP-IG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 158 RsyphqLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVL 237
Cdd:TIGR02633 403 R-----LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVI 476
|
....
gi 2486247945 238 ELGK 241
Cdd:TIGR02633 477 GEGK 480
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
301-490 |
2.65e-13 |
|
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: 67.95 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 301 TGRVKVRALkgvSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVwvngenvaaapkrklhGLRRRLQVVF--QD 378
Cdd:cd03223 12 DGRVLLKDL---SFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI----------------GMPEGEDLLFlpQR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 379 PYrsldprMTVG---ESIVegpvnfgvpkeeawkraqefmkivrlspdalnrYP--NQFSGGQRQRISIARALACEPEIL 453
Cdd:cd03223 73 PY------LPLGtlrEQLI---------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190
....*....|....*....|....*....|....*..
gi 2486247945 454 ICDEAVSALDVSVQADILKLLEEiqvkLGIGILFVTH 490
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLKE----LGITVISVGH 146
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
32-245 |
4.46e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 70.64 E-value: 4.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLlpkgLAPADGSVKLLGmdlfRRTPDEIRRLRGakMAMVFQEpmTA 111
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL----ERITSGEIWIGG----RVVNELEPADRD--IAMVFQN--YA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQMDELLR-AHVPMGPYERRI----RILDLfeEVRLPDPPRifrsyphQLSGGQRQRIVIAMALLLKPDLLI 186
Cdd:PRK11650 87 LYPHMSVRENMAYGLKiRGMPKAEIEERVaeaaRILEL--EPLLDRKPR-------ELSGGQRQRVAMGRAIVREPAVFL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 187 CDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGK--QIET 245
Cdd:PRK11650 158 FDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVaeQIGT 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-240 |
6.17e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 67.90 E-value: 6.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEI 93
Cdd:cd03231 1 LEADELTCER----DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSP----PLAGRVLLNGGPLDFQRDSIA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RRL------RGAKMAMVFQEPMTALNPVmtCGDQMDELLRAHVPMGPYERRIrildlfeevrlpdpprifrsyPHQLSGG 167
Cdd:cd03231 73 RGLlylghaPGIKTTLSVLENLRFWHAD--HSDEQVEEALARVGLNGFEDRP---------------------VAQLSAG 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSeiaDQVVVLELG 240
Cdd:cd03231 130 QQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSE---AGARELDLG 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
303-463 |
6.59e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.98 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 303 RVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVN-GENVAAApkrKLHGLRRRLQVVFQDP-- 379
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDI---NLKWWRSKIGVVSQDPll 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 380 ---------------------------------YRSLDPRMTVgESIVEGPVN-----------FGVPKEEAWKRAQEFM 415
Cdd:PTZ00265 472 fsnsiknnikyslyslkdlealsnyynedgndsQENKNKRNSC-RAKCAGDLNdmsnttdsnelIEMRKNYQTIKDSEVV 550
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 416 KIVR--LSPDALNRYPNQF-----------SGGQRQRISIARALACEPEILICDEAVSALD 463
Cdd:PTZ00265 551 DVSKkvLIHDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
45-255 |
6.73e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 45 VTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLFRRT-----PDEIRRlrgakMAMVFQEpmTALNPVMT-- 117
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLT----RPQKGRIVLNGRVLFDAEkgiclPPEKRR-----IGYVFQD--ARLFPHYKvr 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 118 ------CGDQMDELlrahvpmgpYERRIRILDLfeevrlpDPprIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPT 191
Cdd:PRK11144 95 gnlrygMAKSMVAQ---------FDKIVALLGI-------EP--LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 192 TALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHP 255
Cdd:PRK11144 157 ASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
305-516 |
7.36e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 7.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLhgLRRRLQVVFQDpyRSLD 384
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREAVAIVPEG--RRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 385 PRMTVGESIVEGpvNFGVPKEEAWKRAQefmKIVRLSPDALNRYPNQ---FSGGQRQRISIARALACEPEILICDEAVSA 461
Cdd:PRK11614 93 SRMTVEENLAMG--GFFAERDQFQERIK---WVYELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 462 LDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDdvivirRGECVESGHV 516
Cdd:PRK11614 168 LAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLAD------RGYVLENGHV 215
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
307-518 |
7.90e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.03 E-value: 7.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTfarsiarLID------PTSGEVWVNGENVAAAPKRKLhglRRRLQVVFQDPy 380
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTS-------LLNallgflPYQGSLKINGIELRELDPESW---RKHLSWVGQNP- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 381 rSLdPRMTVGESIVEGPVNfgVPKEEAW---KRAQ--EFmkiVRLSPDALNrYPNQ-----FSGGQRQRISIARALACEP 450
Cdd:PRK11174 433 -QL-PHGTLRDNVLLGNPD--ASDEQLQqalENAWvsEF---LPLLPQGLD-TPIGdqaagLSVGQAQRLALARALLQPC 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 451 EILICDEAVSALDVSVQADILKLLEeiQVKLGIGILFVTHDLRVASQiCDDVIVIRRGECVESGHVQD 518
Cdd:PRK11174 505 QLLLLDEPTASLDAHSEQLVMQALN--AASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
35-241 |
9.14e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 35 HVSFTVNEGEVTCLIGESGSGKSVIASTVMGL--LPKGlapadgsvkllgmDLF---RRTPDEIRRLRGakMAMVFQEpm 109
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLedITSG-------------DLFigeKRMNDVPPAERG--VGMVFQS-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 110 TALNPVMTCGDQMDELLR-AHVPMGPYERRI----RILDLfeevrlpdpPRIFRSYPHQLSGGQRQRIVIAMALLLKPDL 184
Cdd:PRK11000 84 YALYPHLSVAENMSFGLKlAGAKKEEINQRVnqvaEVLQL---------AHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 185 LICDEPTT----ALNVTTQASILKlileLQKKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:PRK11000 155 FLLDEPLSnldaALRVQMRIEISR----LHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGR 211
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
308-522 |
1.21e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 70.30 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 308 ALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKLHGlrrrlqvvfqdpyrsldpRM 387
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNG------------------QL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 388 TVGESIVEGPVNFGVPKE---EAWKRAQEFMKIVRLspdaLNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDV 464
Cdd:PRK13545 101 TGIENIELKGLMMGLTKEkikEIIPEIIEFADIGKF----IYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 465 SVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVFFH 522
Cdd:PRK13545 177 TFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
27-246 |
1.29e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 70.23 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 27 GDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIAStvmgLLPKGLAPADGSVKLLGMDLFRRTPDEirrLRGAkMAMVFQ 106
Cdd:COG5265 369 PERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLAR----LLFRFYDVTSGRILIDGQDIRDVTQAS---LRAA-IGIVPQ 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 107 EpmTAL------------NPvmtcGDQMDELLRAhvpmgpyERRIRILDLFEevRLPDpprifrSYPHQ-------LSGG 167
Cdd:COG5265 440 D--TVLfndtiayniaygRP----DASEEEVEAA-------ARAAQIHDFIE--SLPD------GYDTRvgerglkLSGG 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKknGTAVLFITHDFGVVSEiADQVVVLELGKQIETG 246
Cdd:COG5265 499 EKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERG 574
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
309-524 |
1.84e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 70.58 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKRKlhgLRRRLQVVFQDPYrsldprmt 388
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE---LRRQFSMIPQDPV-------- 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 vgesIVEGPVNFGV------PKEEAWkRAQEFMKI------------VRLSPDALNrypnqFSGGQRQRISIARALACEP 450
Cdd:PTZ00243 1395 ----LFDGTVRQNVdpfleaSSAEVW-AALELVGLrervasesegidSRVLEGGSN-----YSVGQRQLMCMARALLKKG 1464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 451 EILIC-DEAVS----ALDVSVQADILKLLEEIQVklgigiLFVTHDLRVASQiCDDVIVIRRGECVESGHVQDVFFHPQ 524
Cdd:PTZ00243 1465 SGFILmDEATAnidpALDRQIQATVMSAFSAYTV------ITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
278-526 |
1.99e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 70.14 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 278 VDGNPTLLEAknVVKTYTLG--GFFTGR--VKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLID----PTSGE 349
Cdd:TIGR00956 44 SDYQPTFPNA--LLKILTRGfrKLKKFRdtKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 350 VWVNGENVAAAPKRKlhglrrRLQVVFQDPYRSLDPRMTVGESIV-----EGPVN--FGVPKEE-AWKRAQEFMKIVRLS 421
Cdd:TIGR00956 122 ITYDGITPEEIKKHY------RGDVVYNAETDVHFPHLTVGETLDfaarcKTPQNrpDGVSREEyAKHIADVYMATYGLS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 422 PDALNRYPNQF----SGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQVKLG----IGILFVTHDlr 493
Cdd:TIGR00956 196 HTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDttplVAIYQCSQD-- 273
|
250 260 270
....*....|....*....|....*....|...
gi 2486247945 494 vASQICDDVIVIRRGecvesghvQDVFFHPQHE 526
Cdd:TIGR00956 274 -AYELFDKVIVLYEG--------YQIYFGPADK 297
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
11-253 |
2.34e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.84 E-value: 2.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 11 LPVLEVENLAVSLPpgGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapaDGSVKLLGMDLFRRTP 90
Cdd:PRK10895 1 MATLTAKNLAKAYK--GRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPR-----DAGNIIIDDEDISLLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLRGakMAMVFQEPmtALNPVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVRLpdpPRIFRSYPHQLSGGQRQ 170
Cdd:PRK10895 72 LHARARRG--IGYLPQEA--SIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI---EHLRDSMGQSLSGGERR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 171 RIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKS 250
Cdd:PRK10895 145 RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
...
gi 2486247945 251 VLQ 253
Cdd:PRK10895 224 ILQ 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
164-476 |
2.50e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 69.38 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTtqaSILKLILELQKKNGTaVLFITHD--FgvvseiADQVV--VLEL 239
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGT-VVAVTHDryF------LDNVAgwILEL 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 240 --------------------------GKQiETGPAKS-------VLQHPK------------------EPYTQKL----- 263
Cdd:PRK11819 234 drgrgipwegnysswleqkakrlaqeEKQ-EAARQKAlkrelewVRQSPKarqakskarlaryeellsEEYQKRNetnei 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 264 -INAVPELkprhrppvdGNpTLLEAKNVVKTYtlGGfftgrvkvRAL-KGVSARLRRGETIGIVGESGSGKSTFARSIAR 341
Cdd:PRK11819 313 fIPPGPRL---------GD-KVIEAENLSKSF--GD--------RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG 372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 342 LIDPTSGEVWVnGENVaaapkrklhglrrrlQVVFQDPYR-SLDPRMTVGESIVEGPVNFGVPKEEAWKRA--------- 411
Cdd:PRK11819 373 QEQPDSGTIKI-GETV---------------KLAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSRAyvgrfnfkg 436
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 412 --QEfmKIVrlspdalnrypNQFSGGQRQRISIARALACEPEILICDEAVSALDVsvqaDILKLLEE 476
Cdd:PRK11819 437 gdQQ--KKV-----------GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV----ETLRALEE 486
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
12-222 |
4.16e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDlfrrtpD 91
Cdd:PRK13539 1 MMLEGEDLACVR---GGRV-LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP----PAAGTIKLDGGD------I 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRGAkmaMVFQEPMTALNPVMTCGDQMD---ELLrahvpmGPYERRI-RILDLFEEVRLPDPPriFRSyphqLSGG 167
Cdd:PRK13539 67 DDPDVAEA---CHYLGHRNAMKPALTVAENLEfwaAFL------GGEELDIaAALEAVGLAPLAHLP--FGY----LSAG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 168 QRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLfITH 222
Cdd:PRK13539 132 QKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIA-ATH 185
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-254 |
6.51e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.75 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRpNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDLfrrtPD 91
Cdd:PRK13537 6 APIDFRNVEKRY---GDK-LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLT----HPDAGSISLCGEPV----PS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 EIRRLRgAKMAMVFQepMTALNPVMTCGDQMDELLRaHVPMGPYERRIRILDLFEEVRLPDPPRifrSYPHQLSGGQRQR 171
Cdd:PRK13537 74 RARHAR-QRVGVVPQ--FDNLDPDFTVRENLLVFGR-YFGLSAAAARALVPPLLEFAKLENKAD---AKVGELSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 172 IVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSV 251
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
...
gi 2486247945 252 LQH 254
Cdd:PRK13537 226 IES 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
10-248 |
7.47e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 10 KLPVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGllpkglAPA----DGSVKLLGMDL 85
Cdd:CHL00131 4 NKPILEIKNLHASV---NENE-ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG------HPAykilEGDILFKGESI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 86 FRRTPDEIRRLrGAKMAmvFQepmtalNPVMTCGDQMDELLRA-----HVPMGPYErrIRILDLFEEV--RLP----DPP 154
Cdd:CHL00131 74 LDLEPEERAHL-GIFLA--FQ------YPIEIPGVSNADFLRLaynskRKFQGLPE--LDPLEFLEIIneKLKlvgmDPS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 155 RIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNgTAVLFITHDFGVVSEIA-DQ 233
Cdd:CHL00131 143 FLSRNVNEGFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSE-NSIILITHYQRLLDYIKpDY 221
|
250
....*....|....*
gi 2486247945 234 VVVLELGKQIETGPA 248
Cdd:CHL00131 222 VHVMQNGKIIKTGDA 236
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
318-509 |
1.92e-11 |
|
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: 62.01 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 318 RGETIGIVGESGSGKSTFARSIARLIDPTSGEV-WVNGENVAAAPkrklhglrrrlqvvfqdpyrsldprmtvgesiveg 396
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEV----------------------------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 397 pvnfgvpkeeawkraqefmkIVRLSPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKL--- 473
Cdd:smart00382 46 --------------------LDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeel 105
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2486247945 474 --LEEIQVKLGIGILFVTHDLRVASQIC-----DDVIVIRRGE 509
Cdd:smart00382 106 rlLLLLKSEKNLTVILTTNDEKDLGPALlrrrfDRRIVLLLIL 148
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
36-246 |
3.45e-11 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 63.06 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGlAPADGSVKLLGMDlfrRTPDEIRRlrgaKMAMVFQEPMTAlnPV 115
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGG-GTTSGQILFNGQP---RKPDQFQK----CVAYVRQDDILL--PG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 116 MTcgdqMDELLRAHVPM-GPY---ERRIRILDLFEEVRLPDPPRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPT 191
Cdd:cd03234 96 LT----VRETLTYTAILrLPRkssDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 192 TALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
309-490 |
3.54e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 3.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVaaapkrklHGLRRRLQVVFQDPYRSLDPRMT 388
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--------DDPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 VGESIvEGPVNFGVPKEEAWKRAQEFMKIvrlsPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQA 468
Cdd:PRK13539 90 VAENL-EFWAAFLGGEELDIAAALEAVGL----APLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|..
gi 2486247945 469 DILKLLEEIQVKLGIgILFVTH 490
Cdd:PRK13539 165 LFAELIRAHLAQGGI-VIAATH 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-258 |
4.31e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.20 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 39 TVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRtPDEIRrlrgAKMAMVFQEPMTALNPVMTC 118
Cdd:cd03237 21 SISESEVIGILGPNGIGKT----TFIKMLAGVLKPDEGDIEIELDTVSYK-PQYIK----ADYEGTVRDLLSSITKDFYT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 119 GDQMD-ELLRahvPMGpyerrirILDLFEEvRLPDpprifrsyphqLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVT 197
Cdd:cd03237 92 HPYFKtEIAK---PLQ-------IEQILDR-EVPE-----------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 198 TQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLElGKqietgPAKSVLQHPKEP 258
Cdd:cd03237 150 QRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GE-----PSVNGVANPPQS 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-241 |
7.37e-11 |
|
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: 65.42 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 11 LPVLEVENLAVSLPPGGdRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLfRRTP 90
Cdd:TIGR01257 926 VPGVCVKNLVKIFEPSG-RP-AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP----PTSGTVLVGGKDI-ETNL 998
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRlrgaKMAMVFQEPMtaLNPVMTCGDQMdeLLRAHVPMGPYER-RIRILDLFEEVRLPDPprifRSYPHQ-LSGGQ 168
Cdd:TIGR01257 999 DAVRQ----SLGMCPQHNI--LFHHLTVAEHI--LFYAQLKGRSWEEaQLEMEAMLEDTGLHHK----RNEEAQdLSGGM 1066
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 169 RQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqkKNGTAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:TIGR01257 1067 QRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY--RSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
309-522 |
7.40e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTS--GEVWVNGENVAaapKRKLhglrRRLQVVFQDPYrsLDPR 386
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT---KQIL----KRTGFVTQDDI--LYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 MTVGESIVEGPVnFGVP----KEEAWKRAQEFMKIVRLSPDALNRYPNQF----SGGQRQRISIARALACEPEILICDEA 458
Cdd:PLN03211 155 LTVRETLVFCSL-LRLPksltKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 459 VSALDVSVQADILKLLEEIQVKlgiGILFVTHDLRVAS---QICDDVIVIRRGECVESGHVQDVFFH 522
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQK---GKTIVTSMHQPSSrvyQMFDSVLVLSEGRCLFFGKGSDAMAY 297
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
287-519 |
8.75e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.60 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 287 AKNVVKTYTLGGFFTgrvKVRALKGVSARLRRGETIGIVGESGSGKSTFARSiARLIDPTSGE------VWVNGENVAaa 360
Cdd:NF000106 10 ARNAVEVRGLVKHFG---EVKAVDGVDLDVREGTVLGVLGP*GAA**RGALP-AHV*GPDAGRrpwrf*TWCANRRAL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 pkRKLHGLRRRLQVVFQDPYRSLDPRMTVGESIvegpvnfGVPKEEAWKRAQEFMKIVRLSpDALNRYPNQFSGGQRQRI 440
Cdd:NF000106 84 --RRTIG*HRPVR*GRRESFSGRENLYMIGR*L-------DLSRKDARARADELLERFSLT-EAAGRAAAKYSGGMRRRL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 441 SIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDV 519
Cdd:NF000106 154 DLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-240 |
1.02e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDlfrrtpde 92
Cdd:PRK13538 1 MLEARNLACER---DERI-LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLAR----PDAGEVLWQGEP-------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRGAkmamvFQEPM------TALNPVMTCgdqmDELLRAHVPMGPYERRIRILDLFEEVRLpdppRIFRSYP-HQLS 165
Cdd:PRK13538 65 IRRQRDE-----YHQDLlylghqPGIKTELTA----LENLRFYQRLHGPGDDEALWEALAQVGL----AGFEDVPvRQLS 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 166 GGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDfgvVSEIADQVVVLELG 240
Cdd:PRK13538 132 AGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD---LPVASDKVRKLRLG 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
269-520 |
1.56e-10 |
|
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: 64.20 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 269 ELKP---RHRPPVDGNPTLLEAKNvvktytlGGFFTGRVKVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDP 345
Cdd:TIGR00957 618 ELEPdsiERRTIKPGEGNSITVHN-------ATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 346 TSGEVWVNGeNVAAAPKrklhglrrrlQVVFQDPyrsldprmTVGESIVegpvnFGVPKEEawKRAQEFMKIVRLSPDaL 425
Cdd:TIGR00957 691 VEGHVHMKG-SVAYVPQ----------QAWIQND--------SLRENIL-----FGKALNE--KYYQQVLEACALLPD-L 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 426 NRYPN-----------QFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADIL-KLLEEIQVKLGIGILFVTHDLR 493
Cdd:TIGR00957 744 EILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGIS 823
|
250 260
....*....|....*....|....*..
gi 2486247945 494 VASQIcDDVIVIRRGECVESGHVQDVF 520
Cdd:TIGR00957 824 YLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-241 |
1.76e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.26 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 1 MTESSLRAQKLPVLEVENLAvslppGGDRpNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapADGSVKL 80
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVT-----SRDR-KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKR----AGGEIRL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 81 LGMDLFRRTP-DEIRRlrgaKMAMVFQEPM-TALNPVMTCGDQMdELLRAhVPMGPYERRIRILDLFEEVRLPDPPRIFR 158
Cdd:PRK09700 323 NGKDISPRSPlDAVKK----GMAYITESRRdNGFFPNFSIAQNM-AISRS-LKDGGYKGAMGLFHEVDEQRTAENQRELL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 159 SYP--------HQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEI 230
Cdd:PRK09700 397 ALKchsvnqniTELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITV 475
|
250
....*....|.
gi 2486247945 231 ADQVVVLELGK 241
Cdd:PRK09700 476 CDRIAVFCEGR 486
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
307-492 |
1.77e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.45 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVA---AAPKRKLHGLRRRlqvvfqdpyRSL 383
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAeqrDEPHENILYLGHL---------PGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 384 DPRMTVGESIVEGPVNFGVPKEEAWkraqEFMKIVRLSpDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALD 463
Cdd:TIGR01189 85 KPELSALENLHFWAAIHGGAQRTIE----DALAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....*....
gi 2486247945 464 VSVQADILKLLEEIQVKLGIGILFVTHDL 492
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHQDL 188
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
312-380 |
1.89e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 63.28 E-value: 1.89e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 312 VSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPkrkLHGLRRRLQVVFQDPY 380
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN---REAYRQLFSAVFSDFH 416
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
32-248 |
3.49e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 60.28 E-value: 3.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLlPKGlapADGSVKLLGMDLFRRTPDEIRRLRGAKMA---MVFQEp 108
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGD-PRA---TSGRIVFDGKDITDWQTAKIMREAVAIVPegrRVFSR- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 109 MTALNPVMTCGDQMDELLrahvpmgpYERRI-RILDLFeevrlpdpPRIFRSYPHQ---LSGGQRQRIVIAMALLLKPDL 184
Cdd:PRK11614 95 MTVEENLAMGGFFAERDQ--------FQERIkWVYELF--------PRLHERRIQRagtMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 185 LICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHDFGVVSEIADQVVVLELGKQI--ETGPA 248
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDA 223
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
307-525 |
4.33e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 307 RALKGVSARLRRGETIGIVGESGSGKSTFARSIA-RLIDPT-------SGEVWVNGENVAAAPKRKLHGLRRRLQVVFQD 378
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 379 PYRsldprMTVGESIVEGPVNFGVPKEEAWKRAQEFM--KIVRLSPDAL-NRYPNQFSGGQRQRISIARALA-------- 447
Cdd:PRK13547 95 AFA-----FSAREIVLLGRYPHARRAGALTHRDGEIAwqALALAGATALvGRDVTTLSGGELARVQFARVLAqlwpphda 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 448 -CEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQDVfFHPQH 525
Cdd:PRK13547 170 aQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV-LTPAH 247
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
13-241 |
4.94e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPggdrpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapADGSVKLLGMDLFRRTPDE 92
Cdd:PRK10982 250 ILEVRNLTSLRQP------SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREK----SAGTITLHGKKINNHNANE 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 I-----------RRLRGakmamVFQEPMTALNPVMTcgdQMDEllrahvpmgpYERRIRILD----------LFEEVRLP 151
Cdd:PRK10982 320 AinhgfalvteeRRSTG-----IYAYLDIGFNSLIS---NIRN----------YKNKVGLLDnsrmksdtqwVIDSMRVK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 152 DPPRifRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEIA 231
Cdd:PRK10982 382 TPGH--RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGIT 458
|
250
....*....|
gi 2486247945 232 DQVVVLELGK 241
Cdd:PRK10982 459 DRILVMSNGL 468
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
288-514 |
8.07e-10 |
|
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: 61.95 E-value: 8.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 288 KNVVKTYTLggffTGRVKVRALkgvSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVaaapKRKLHG 367
Cdd:TIGR01257 932 KNLVKIFEP----SGRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDA 1000
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 368 LRRRLQVVFQdpYRSLDPRMTVGESIvegpVNFGVPKEEAWKRAQEFMKIVrLSPDALNRYPNQ----FSGGQRQRISIA 443
Cdd:TIGR01257 1001 VRQSLGMCPQ--HNILFHHLTVAEHI----LFYAQLKGRSWEEAQLEMEAM-LEDTGLHHKRNEeaqdLSGGMQRKLSVA 1073
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 444 RALACEPEILICDEAVSALDVSVQADILKLLeeIQVKLGIGILFVTHDLRVASQICDDVIVIRRGECVESG 514
Cdd:TIGR01257 1074 IAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
34-506 |
8.16e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 8.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 34 EHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLlgmdlfrrTPDE-IRRLRGAKMAMvfqEPMTAL 112
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKS----TFMKILGGDLEPSAGNVSL--------DPNErLGKLRQDQFAF---EEFTVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 113 ----------------------NPVMTCGDQMD--ELLRAHVPMGPYERRIRILDLFEEVRLPDPPrifrsypH-----Q 163
Cdd:PRK15064 83 dtvimghtelwevkqerdriyaLPEMSEEDGMKvaDLEVKFAEMDGYTAEARAGELLLGVGIPEEQ-------HyglmsE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTqasILKLILELQKKNGTAVLfITHD--F--GVVSEIADqvvvLEL 239
Cdd:PRK15064 156 VAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT---IRWLEDVLNERNSTMII-ISHDrhFlnSVCTHMAD----LDY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 240 GK--------------------QIETGPAK-----SVLQH-----------PKEPYT-QKLINAVP--ELKPRHRPpvdg 280
Cdd:PRK15064 228 GElrvypgnydeymtaatqareRLLADNAKkkaqiAELQSfvsrfsanaskAKQATSrAKQIDKIKleEVKPSSRQ---- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 281 NPTL------------LEAKNVVKTYTLGGFFtgrvkvralKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSG 348
Cdd:PRK15064 304 NPFIrfeqdkklhrnaLEVENLTKGFDNGPLF---------KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 349 EV-WVNGENVAAAPkrklhglrrrlqvvfQDPYRSLDPRMTVGESIVEgpvnfgvpkeeaWKRAQEFMKIVR-------L 420
Cdd:PRK15064 375 TVkWSENANIGYYA---------------QDHAYDFENDLTLFDWMSQ------------WRQEGDDEQAVRgtlgrllF 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 421 SPDALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDV-SVQAdiLKL-LEEIQVKLgigiLFVTHDLRVASQI 498
Cdd:PRK15064 428 SQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIES--LNMaLEKYEGTL----IFVSHDREFVSSL 501
|
....*...
gi 2486247945 499 CDDVIVIR 506
Cdd:PRK15064 502 ATRIIEIT 509
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
43-240 |
8.87e-10 |
|
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: 57.38 E-value: 8.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 43 GEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIRRLRgakmamvfqepmtalnpvmtcgdqm 122
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELG----PPGGGVIYIDGEDILEEVLDQLLLI------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 123 dellrahvpmgpyerririldlfeevrlpdpprIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASI 202
Cdd:smart00382 53 ---------------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALL 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2486247945 203 LKLI-----LELQKKNGTAVLFITHDFGVVSE-----IADQVVVLELG 240
Cdd:smart00382 100 LLLEelrllLLLKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLLI 147
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-223 |
1.05e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 3 ESSLRAQKLpVLEVENLAVSLPpggDRpNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKllg 82
Cdd:PRK11147 310 EEASRSGKI-VFEMENVNYQID---GK-QLVKDFSAQVQRGDKIALIGPNGCGKT----TLLKLMLGQLQADSGRIH--- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 83 mdlfrrtpdeirrlRGAKMAMV-FQEPMTALNPVMTCgdqMDELL--RAHVPMGPYERRI--RILD-LFEEVRLPDPPRi 156
Cdd:PRK11147 378 --------------CGTKLEVAyFDQHRAELDPEKTV---MDNLAegKQEVMVNGRPRHVlgYLQDfLFHPKRAMTPVK- 439
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 157 frsyphQLSGGQRQRIVIAmALLLKP-DLLICDEPTTALNVTTqasiLKLILEL-QKKNGTaVLFITHD 223
Cdd:PRK11147 440 ------ALSGGERNRLLLA-RLFLKPsNLLILDEPTNDLDVET----LELLEELlDSYQGT-VLLVSHD 496
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
309-491 |
1.05e-09 |
|
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: 61.10 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWvngenvaAAPKRKLHGLRrrlqvvfQDPYrsLDPRMT 388
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-------PQPGIKVGYLP-------QEPQ--LDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 VGESIVEG--------------PVNFGVPKEEAWKRAQEFMKI---------------VRLSPDALnRYP------NQFS 433
Cdd:TIGR03719 85 VRENVEEGvaeikdaldrfneiSAKYAEPDADFDKLAAEQAELqeiidaadawdldsqLEIAMDAL-RCPpwdadvTKLS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 434 GGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIQvklgiG-ILFVTHD 491
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP-----GtVVAVTHD 217
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
36-253 |
1.77e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLAP----ADGSVKLLGMDLFRRTPDEIRRLRgakmAMVFQ--EPM 109
Cdd:PRK13547 20 LSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPrgarVTGDVTLNGEPLAAIDAPRLARLR----AVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 110 TALNpvmtcgdqMDELlrahVPMG--PYERR-----IRILDL-FEEVRLPDPPRIFRSYPHQLSGGQRQRIVIAMALL-L 180
Cdd:PRK13547 96 FAFS--------AREI----VLLGryPHARRagaltHRDGEIaWQALALAGATALVGRDVTTLSGGELARVQFARVLAqL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 181 KPD--------LLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVL 252
Cdd:PRK13547 164 WPPhdaaqpprYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
.
gi 2486247945 253 Q 253
Cdd:PRK13547 244 T 244
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
154-238 |
2.30e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 56.81 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 154 PRIFRSYPHQ---LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEI 230
Cdd:cd03222 59 DGITPVYKPQyidLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYL 138
|
....*...
gi 2486247945 231 ADQVVVLE 238
Cdd:cd03222 139 SDRIHVFE 146
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
13-246 |
2.32e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.26 E-value: 2.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLppggDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGllPKGLAPADGSVKLLGMDLFRRTPDE 92
Cdd:PRK09580 1 MLSIKDLHVSV----EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVTGGTVEFKGKDLLELSPED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 iRRLRGAKMAmvFQEPM------------TALNPVmtcgdqmdellRAHVPMGPYErRIRILDLFEE-VRLPDPPR--IF 157
Cdd:PRK09580 75 -RAGEGIFMA--FQYPVeipgvsnqfflqTALNAV-----------RSYRGQEPLD-RFDFQDLMEEkIALLKMPEdlLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 158 RSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNgTAVLFITHDFGVVSEIA-DQVVV 236
Cdd:PRK09580 140 RSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGK-RSFIIVTHYQRILDYIKpDYVHV 218
|
250
....*....|
gi 2486247945 237 LELGKQIETG 246
Cdd:PRK09580 219 LYQGRIVKSG 228
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
160-237 |
2.42e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 2.42e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 160 YPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEiADQVVVL 237
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVF 1431
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
155-250 |
2.68e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.80 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 155 RIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQV 234
Cdd:COG1245 447 KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRL 526
|
90
....*....|....*.
gi 2486247945 235 VVLElGKQIETGPAKS 250
Cdd:COG1245 527 MVFE-GEPGVHGHASG 541
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
309-514 |
4.24e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.49 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLID--PTSGEVWVNGENVaaapkrklhglrrrlqvvfqdpyRSLDPR 386
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDL-----------------------LELSPE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 387 MTVGESI-------VEGP-----------VNfGVPK---EEAWKR------AQEFMKIVRLSPDALNRYPNQ-FSGGQRQ 438
Cdd:PRK09580 74 DRAGEGIfmafqypVEIPgvsnqfflqtaLN-AVRSyrgQEPLDRfdfqdlMEEKIALLKMPEDLLTRSVNVgFSGGEKK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 439 RISIARALACEPEILICDEAVSALDVsvqaDILKLLEEIQVKLGIG---ILFVTHDLRVASQICDD-VIVIRRGECVESG 514
Cdd:PRK09580 153 RNDILQMAVLEPELCILDESDSGLDI----DALKIVADGVNSLRDGkrsFIIVTHYQRILDYIKPDyVHVLYQGRIVKSG 228
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
154-238 |
4.25e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 154 PRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQ 233
Cdd:PRK13409 444 ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDR 523
|
....*
gi 2486247945 234 VVVLE 238
Cdd:PRK13409 524 LMVFE 528
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
268-463 |
4.45e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 268 PELKPRHRPPVDGNPTLLEAKNVVKTYTLGGFFT-----------GRVkvrALKGVSARLRRGETIGIVGESGSGKSTFA 336
Cdd:TIGR01271 1186 PRPSGGGGKYQLSTVLVIENPHAQKCWPSGGQMDvqgltakyteaGRA---VLQDLSFSVEGGQRVGLLGRTGSGKSTLL 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 337 RSIARLIDpTSGEVWVNG---ENVAAAPKRKLHGLRRRLQVVFQDPYR-SLDPRMTVGEsivegpvnfgvpkEEAWKRAQ 412
Cdd:TIGR01271 1263 SALLRLLS-TEGEIQIDGvswNSVTLQTWRKAFGVIPQKVFIFSGTFRkNLDPYEQWSD-------------EEIWKVAE 1328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 413 E--FMKIVRLSPDALNRYPNQ----FSGGQRQRISIARALACEPEILICDEAVSALD 463
Cdd:TIGR01271 1329 EvgLKSVIEQFPDKLDFVLVDggyvLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
309-495 |
1.01e-08 |
|
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: 55.58 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAP---KRKLH------GLRRRLQVV---- 375
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdsiARGLLylghapGIKTTLSVLenlr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 376 FqdpYRSLDPRMTVGESIVEgpVNFGvpkeeawkraqefmkivrlspdALNRYP-NQFSGGQRQRISIARALACEPEILI 454
Cdd:cd03231 96 F---WHADHSDEQVEEALAR--VGLN----------------------GFEDRPvAQLSAGQQRRVALARLLLSGRPLWI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2486247945 455 CDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVA 495
Cdd:cd03231 149 LDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-191 |
1.04e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 58.21 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKsviaSTVM----GLLPkglaPADGSVKLLGmdlfrRTPD----EIRRlRGAKMAM 103
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGK----STTMkmltGLLP----ASEGEAWLFG-----QPVDagdiATRR-RVGYMSQ 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 104 VFqepmtALnpvmtcgdqMDEL-------LRA---HVPmgPYERRIRILDLFEEVRLPDpprIFRSYPHQLSGGQRQRIV 173
Cdd:NF033858 347 AF-----SL---------YGELtvrqnleLHArlfHLP--AAEIAARVAEMLERFDLAD---VADALPDSLPLGIRQRLS 407
|
170
....*....|....*...
gi 2486247945 174 IAMALLLKPDLLICDEPT 191
Cdd:NF033858 408 LAVAVIHKPELLILDEPT 425
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
306-518 |
1.17e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.43 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 306 VRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVA-AAPKRKL-HGL---RRRLQVVFQdpy 380
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALeNGIsmvHQELNLVLQ--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 381 RSLDPRMTVGESIVEGpvnFGVPKEEAWKRAQEFMKIVRLSPDALNRYPNqFSGGQRQRISIARALACEPEILICDEAVS 460
Cdd:PRK10982 88 RSVMDNMWLGRYPTKG---MFVDQDKMYRDTKAIFDELDIDIDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 461 ALDVSVQADILKLLEEIQVKlGIGILFVTHDLRVASQICDDVIVIRRGECVESGHVQD 518
Cdd:PRK10982 164 SLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAG 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
285-463 |
1.87e-08 |
|
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: 55.63 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 285 LEAKNVVKTYTLGGfftgrvkVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDpTSGEVWVNGENVAAAPK-- 362
Cdd:cd03289 3 MTVKDLTAKYTEGG-------NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLqk 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 363 -RKLHGLRRRLQVVFQDPYR-SLDPrmtvgesivegpvnFGVPK-EEAWKRAQEF-MKIVrlspdaLNRYPNQ------- 431
Cdd:cd03289 75 wRKAFGVIPQKVFIFSGTFRkNLDP--------------YGKWSdEEIWKVAEEVgLKSV------IEQFPGQldfvlvd 134
|
170 180 190
....*....|....*....|....*....|....*.
gi 2486247945 432 ----FSGGQRQRISIARALACEPEILICDEAVSALD 463
Cdd:cd03289 135 ggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
309-472 |
2.25e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 57.23 E-value: 2.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGenvaaapkrklhglrrRLQVVFQDPYrsLDPRmT 388
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----------------RISFSPQTSW--IMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 VGESIVegpvnFGVPKEEAwkRAQEFMKIVRLSPDaLNRYPNQ-----------FSGGQRQRISIARALACEPEILICDE 457
Cdd:TIGR01271 503 IKDNII-----FGLSYDEY--RYTSVIKACQLEED-IALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDS 574
|
170
....*....|....*
gi 2486247945 458 AVSALDVSVQADILK 472
Cdd:TIGR01271 575 PFTHLDVVTEKEIFE 589
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
14-253 |
2.47e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.26 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGDRpnAVEHVSFTVNEGEVTCLIGESGSGKSviaSTVMGLLpKGLAPADGSVKLLGMDLFRRTPDEI 93
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDL--VLRHINVTIHGGEKVGIVGRTGAGKS---SLTLGLF-RINESAEGEIIIDGLNIAKIGLHDL 1358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 RrlrgakmamvFQEPMTALNPVMTCGDqmdelLRAHV-PMGPYERRirilDLFEEVRLPDPPRIFRSYP----HQ----- 163
Cdd:TIGR00957 1359 R----------FKITIIPQDPVLFSGS-----LRMNLdPFSQYSDE----EVWWALELAHLKTFVSALPdkldHEcaegg 1419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 --LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQaSILKLILELQKKNGTaVLFITHDFGVVSEIAdQVVVLELGK 241
Cdd:TIGR00957 1420 enLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD-NLIQSTIRTQFEDCT-VLTIAHRLNTIMDYT-RVIVLDKGE 1496
|
250
....*....|..
gi 2486247945 242 QIETGPAKSVLQ 253
Cdd:TIGR00957 1497 VAEFGAPSNLLQ 1508
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
313-464 |
2.64e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.79 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 313 SARLRRGETIGIVGESGSGKSTFARSIA-RLID--PTSGEVW-----VNGENVAA------APKRKLHGLRRRLQVVFQD 378
Cdd:PLN03073 197 SVTLAFGRHYGLVGRNGTGKTTFLRYMAmHAIDgiPKNCQILhveqeVVGDDTTAlqcvlnTDIERTQLLEEEAQLVAQQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 379 pyRSLDPRMTVGESivEGPVNFGVPKEEAWKRAQEFMKIVRL-------------------SPDALNRYPNQFSGGQRQR 439
Cdd:PLN03073 277 --RELEFETETGKG--KGANKDGVDKDAVSQRLEEIYKRLELidaytaearaasilaglsfTPEMQVKATKTFSGGWRMR 352
|
170 180
....*....|....*....|....*
gi 2486247945 440 ISIARALACEPEILICDEAVSALDV 464
Cdd:PLN03073 353 IALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
27-223 |
3.06e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.13 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 27 GDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLlpkgLAPADGSVKLLGMDLFRRTPDEIRRLRGAKMAMV-- 104
Cdd:PRK10522 333 QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGL----YQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFhl 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 105 FQEpmtALNPVmtcGDQMDELLrahvpmgpYERRIRILDLFEEVRLPDppriFRSYPHQLSGGQRQRIVIAMALLLKPDL 184
Cdd:PRK10522 409 FDQ---LLGPE---GKPANPAL--------VEKWLERLKMAHKLELED----GRISNLKLSKGQKKRLALLLALAEERDI 470
|
170 180 190
....*....|....*....|....*....|....*....
gi 2486247945 185 LICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHD 223
Cdd:PRK10522 471 LLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
35-243 |
3.87e-08 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.81 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 35 HVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLAPaDGSVKLLGMDlfrrtPDEIRRLRGAKMAMVFQEPMTalNP 114
Cdd:cd03233 25 DFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV-EGDIHYNGIP-----YKEFAEKYPGEIIYVSEEDVH--FP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 115 VMTCGDQMD--ELLRAHvpmgpyerririldlfEEVRlpdpprifrsyphQLSGGQRQRIVIAMALLLKPDLLICDEPTT 192
Cdd:cd03233 97 TLTVRETLDfaLRCKGN----------------EFVR-------------GISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 193 ALNVTTQASILKLILELQKKNGTAVLF--------ITHDFgvvseiaDQVVVLELGKQI 243
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVslyqasdeIYDLF-------DKVLVLYEGRQI 199
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
243-287 |
4.29e-08 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 50.09 E-value: 4.29e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2486247945 243 IETGPAKSVLQHPKEPYTQKLINAVPELKP--RHRPPVDGNPTLLEA 287
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVPRLDPpkRPLYTIPGNVPSLLE 47
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
156-241 |
6.15e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 6.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 156 IFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVV 235
Cdd:PLN03211 199 IGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVL 278
|
....*.
gi 2486247945 236 VLELGK 241
Cdd:PLN03211 279 VLSEGR 284
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-509 |
6.99e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 33 VEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGmdlfrrtpdeirrlrGAKMAMVFQE----P 108
Cdd:PRK10636 17 LDNATATINPGQKVGLVGKNGCGKS----TLLALLKNEISADGGSYTFPG---------------NWQLAWVNQEtpalP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 109 MTALNPVMTcGD----QMDELLR-----------AHV-----PMGPYERRIRILDL-----FEEVRLPDPPRIFrsyphq 163
Cdd:PRK10636 78 QPALEYVID-GDreyrQLEAQLHdanerndghaiATIhgkldAIDAWTIRSRAASLlhglgFSNEQLERPVSDF------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 lSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTtqaSILKLILELQKKNGTAVLfITHDFGVVSEIADQVVVLELGKQI 243
Cdd:PRK10636 151 -SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQGTLIL-ISHDRDFLDPIVDKIIHIEQQSLF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 244 E-TG--------------PAKSVLQHPKEPYTQ----------------------KLINAVPELKPRH----------RP 276
Cdd:PRK10636 226 EyTGnyssfevqratrlaQQQAMYESQQERVAHlqsyidrfrakatkakqaqsriKMLERMELIAPAHvdnpfhfsfrAP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 277 PVDGNPtLLEAKNVVKTYtlggfftGRVKVraLKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEvwvngen 356
Cdd:PRK10636 306 ESLPNP-LLKMEKVSAGY-------GDRII--LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE------- 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 357 VAAAPKRKLhGLRRRLQVVFqdpyrsldprMTVGESIVEGPVNFGvPKEEAwKRAQEFMKIVRLSPDALNRYPNQFSGGQ 436
Cdd:PRK10636 369 IGLAKGIKL-GYFAQHQLEF----------LRADESPLQHLARLA-PQELE-QKLRDYLGGFGFQGDKVTEETRRFSGGE 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 437 RQRISIARALACEPEILICDEAVSALDVsvqaDILKLLEEIQVKLGIGILFVTHDLRVASQICDDVIVIRRGE 509
Cdd:PRK10636 436 KARLVLALIVWQRPNLLLLDEPTNHLDL----DMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGK 504
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
311-497 |
7.69e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 52.88 E-value: 7.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 311 GVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPkrklhglrrrlqvvfQDPYRSL------- 383
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR---------------DEYHQDLlylghqp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 384 --DPRMTVGESI-----VEGPVNfgvpKEEAWkraqefmkivrlspDALNRY--------P-NQFSGGQRQRISIARALA 447
Cdd:PRK13538 84 giKTELTALENLrfyqrLHGPGD----DEALW--------------EALAQVglagfedvPvRQLSAGQQRRVALARLWL 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2486247945 448 CEPEILICDEAVSALDVSVQADILKLLEEIQVKLGIGILFVTHDLRVASQ 497
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQDLPVASD 195
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
32-254 |
1.11e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.51 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGL-LP-KGLAPADGSVKLLGMDlfrrtpdeirrlrgakmamvfqepm 109
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVtMPnKGTVDIKGSAALIAIS------------------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 110 TALNPVMTcGDQMDELlrAHVPMGPYERRIR-----ILDLFEEVRLPDPPriFRSYphqlSGGQRQRIVIAMALLLKPDL 184
Cdd:PRK13545 94 SGLNGQLT-GIENIEL--KGLMMGLTKEKIKeiipeIIEFADIGKFIYQP--VKTY----SSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2486247945 185 LICDEpttALNVTTQASILKLILELQ--KKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQH 254
Cdd:PRK13545 165 LVIDE---ALSVGDQTFTKKCLDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
316-500 |
1.27e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 316 LRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAapkrklhglrrRLQvvfQDPYRslDPRMTVGESIVE 395
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVA-----------RLQ---QDPPR--NVEGTVYDFVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 396 GPVNFGV---------------PKEE----------------AWK---RAQEFMKIVRLSPDALnryPNQFSGGQRQRIS 441
Cdd:PRK11147 90 GIEEQAEylkryhdishlvetdPSEKnlnelaklqeqldhhnLWQlenRINEVLAQLGLDPDAA---LSSLSGGWLRKAA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 442 IARALACEPEILICDEAVSALDVsvqaDILKLLEEIQVKLGIGILFVTHDL----RVASQICD 500
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHDRsfirNMATRIVD 225
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
163-237 |
1.42e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.75 E-value: 1.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQkKNGTAVLFITHDFGVVSEIADQVVVL 237
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELA-EDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
256-517 |
1.42e-07 |
|
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: 54.63 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 256 KEPYTQKLINAVPElkpRHRPPVDGNPTlleakNVVKTYTLGGFFTGrVKVRALKGVSARLRRGETIGIVGESGSGKSTF 335
Cdd:TIGR01257 1911 KEPIFDEDDDVAEE---RQRIISGGNKT-----DILRLNELTKVYSG-TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTT 1981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 336 ARSIARLIDPTSGEVWVNGENVAAapkrKLHGLRRRLQVVFQdpYRSLDPRMTVGESIVEGPVNFGVPKEEAWKRAQEFM 415
Cdd:TIGR01257 1982 FKMLTGDTTVTSGDATVAGKSILT----NISDVHQNMGYCPQ--FDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSI 2055
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 416 KIVRLSPDAlNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTHDLRVA 495
Cdd:TIGR01257 2056 QSLGLSLYA-DRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSI-IREGRAVVLTSHSMEEC 2133
|
250 260
....*....|....*....|..
gi 2486247945 496 SQICDDVIVIRRGECVESGHVQ 517
Cdd:TIGR01257 2134 EALCTRLAIMVKGAFQCLGTIQ 2155
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
162-235 |
1.43e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.21 E-value: 1.43e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 162 HQLSGGQRQRIVIAMAL---LLKPD-LLICDEPTTALNVTTQASILKLILELQKKNGTaVLFITHDFGVVsEIADQVV 235
Cdd:cd03227 76 LQLSGGEKELSALALILalaSLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQ-VIVITHLPELA-ELADKLI 151
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
304-517 |
1.56e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 304 VKVRALKGVSARLRRGETIGIVGESGSGKSTFARsiarlidptsgevwvngENVAAAPKRKLHGLRR---RLQVVFQDPY 380
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------------EGLYASGKARLISFLPkfsRNKLIFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 381 RSLdprmtvgesivegpVNFGVpkeeawkraqEFMKivrlspdaLNRYPNQFSGGQRQRISIARALACEPE--ILICDEA 458
Cdd:cd03238 69 QFL--------------IDVGL----------GYLT--------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2486247945 459 VSALDvsvQADILKLLEEIQ--VKLGIGILFVTHDLRVASQiCDDVIVIRRGECVESGHVQ 517
Cdd:cd03238 117 STGLH---QQDINQLLEVIKglIDLGNTVILIEHNLDVLSS-ADWIIDFGPGSGKSGGKVV 173
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
309-472 |
2.67e-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: 52.17 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGenvaaapkrklhglrrrlQVVFQDPYRSLDPRmT 388
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------------RISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 VGESIVegpvnFGVPKEEAwkRAQEFMKIVRLSPDaLNRYPNQ-----------FSGGQRQRISIARALACEPEILICDE 457
Cdd:cd03291 114 IKENII-----FGVSYDEY--RYKSVVKACQLEED-ITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170
....*....|....*
gi 2486247945 458 AVSALDVSVQADILK 472
Cdd:cd03291 186 PFGYLDVFTEKEIFE 200
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
32-254 |
3.46e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 51.74 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLP--KGLAPADGSVKLLGMDlfrrtpdeirrlrgakmamvfqepm 109
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSptVGKVDRNGEVSVIAIS------------------------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 110 TALNPVMTcgdQMDELLRAHVPMGPYERRIRIL--DLFEEVRLPDppriFRSYP-HQLSGGQRQRIVIAMALLLKPDLLI 186
Cdd:PRK13546 94 AGLSGQLT---GIENIEFKMLCMGFKRKEIKAMtpKIIEFSELGE----FIYQPvKKYSSGMRAKLGFSINITVNPDILV 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2486247945 187 CDEPTTALNVTTQASILKLILELQKKNGTaVLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQH 254
Cdd:PRK13546 167 IDEALSVGDQTFAQKCLDKIYEFKEQNKT-IFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
309-490 |
5.45e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVaaapKRKLHGLRRrlQVVFQDPYRSLDPRMT 388
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQK--QLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 VGESIVegpvnFGVPKEEAWKRAQEFMKIVRLspDALNRYP-NQFSGGQRQRISIARALACEPEILICDEAVSALDvsvQ 467
Cdd:PRK13540 91 LRENCL-----YDIHFSPGAVGITELCRLFSL--EHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---E 160
|
170 180
....*....|....*....|....*
gi 2486247945 468 ADILKLLEEIQV--KLGIGILFVTH 490
Cdd:PRK13540 161 LSLLTIITKIQEhrAKGGAVLLTSH 185
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
243-285 |
6.02e-07 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 47.36 E-value: 6.02e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2486247945 243 IETGPAKSVLQHPKEPYTQKLINAVPELKPRHRPPV--DGNPTLL 285
Cdd:TIGR01727 3 VETGPAEEIFKNPLHPYTKALLSAIPTIKKRDRKLIsiPGEVPSL 47
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
36-237 |
6.10e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 6.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 36 VSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLlgMDLFRRTPDEIRRLRgAKMAMVFQEPMTALNPV 115
Cdd:PTZ00265 404 LNFTLTEGKTYAFVGESGCGKS----TILKLIERLYDPTEGDIII--NDSHNLKDINLKWWR-SKIGVVSQDPLLFSNSI 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 116 ---------------------------------------MTCGDQMDELLRAHVPMGPYERR--------IRILDLFEEV 148
Cdd:PTZ00265 477 knnikyslyslkdlealsnyynedgndsqenknkrnscrAKCAGDLNDMSNTTDSNELIEMRknyqtikdSEVVDVSKKV 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 149 -------RLPDP-PRIFRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFI 220
Cdd:PTZ00265 557 lihdfvsALPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIII 636
|
250
....*....|....*..
gi 2486247945 221 THDFGVVsEIADQVVVL 237
Cdd:PTZ00265 637 AHRLSTI-RYANTIFVL 652
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-254 |
1.41e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 35 HVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLAPADGSVKLLGMdlfrrTPDEI-RRLRGAkmaMVFQEPMTALN 113
Cdd:TIGR00956 79 PMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGI-----TPEEIkKHYRGD---VVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 114 PVMTCGDQMDELLRAHVPMGPY------ERRIRILDLFEEVRLPDPPR-------IFRSyphqLSGGQRQRIVIAMALLL 180
Cdd:TIGR00956 151 PHLTVGETLDFAARCKTPQNRPdgvsreEYAKHIADVYMATYGLSHTRntkvgndFVRG----VSGGERKRVSIAEASLG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 181 KPDLLICDEPTTALNVTT----------QASILK---LILELQKKNGTAVLFithdfgvvseiaDQVVVLELGKQIETGP 247
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATalefiralktSANILDttpLVAIYQCSQDAYELF------------DKVIVLYEGYQIYFGP 294
|
....*..
gi 2486247945 248 AKSVLQH 254
Cdd:TIGR00956 295 ADKAKQY 301
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
28-253 |
1.76e-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: 51.10 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 28 DRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapADGSVKLLGmdlfrrtpdeirrlrgaKMAMVFQE 107
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK----VEGHVHMKG-----------------SVAYVPQQ 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 108 PMtalnpVMTCGDQMDELLRAHVPMGPYERRIRILDLFEEVR-LPDPPRI-FRSYPHQLSGGQRQRIVIAMALLLKPDLL 185
Cdd:TIGR00957 708 AW-----IQNDSLRENILFGKALNEKYYQQVLEACALLPDLEiLPSGDRTeIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 186 ICDEPTTALNVTTQASILKLIL--ELQKKNGTAVLfITHDFGVVSEIaDQVVVLELGKQIETGPAKSVLQ 253
Cdd:TIGR00957 783 LFDDPLSAVDAHVGKHIFEHVIgpEGVLKNKTRIL-VTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
305-490 |
2.05e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.88 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRALKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDP---TSGEVWVNGenvaaaPKRKLHGLRRRLQVVFQDPYR 381
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNG------RPLDSSFQRSIGYVQQQDLHL 848
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 382 sldPRMTVGESI-----VEGPVNfgVPKEEAWKRAQEFMKIVRLS--PDALNRYPNQ-FSGGQRQRISIARALACEPEIL 453
Cdd:TIGR00956 849 ---PTSTVRESLrfsayLRQPKS--VSKSEKMEYVEEVIKLLEMEsyADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLL 923
|
170 180 190
....*....|....*....|....*....|....*...
gi 2486247945 454 I-CDEAVSALDVSVQADILKLLEEIqVKLGIGILFVTH 490
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIH 960
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
164-339 |
2.43e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.60 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLL---KPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVsEIADQvvVLELG 240
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHNMHVV-KVADY--VLELG 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 241 KQ---------IETGPAKSVLQH-PKEPYTQKLINAVPELKPRHRPPvdGNPTLLEAKNVVKTYTlggfftgrvkvRALK 310
Cdd:PRK00635 886 PEggnlggyllASCSPEELIHLHtPTAKALRPYLSSPQELPYLPDPS--PKPPVPADITIKNAYQ-----------HNLK 952
|
170 180
....*....|....*....|....*....
gi 2486247945 311 GVSARLRRGETIGIVGESGSGKSTFARSI 339
Cdd:PRK00635 953 HIDLSLPRNALTAVTGPSASGKHSLVFDI 981
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
433-518 |
2.60e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 433 SGGQRQRISIARALACEPEILICDEAVSALDVSVQADILK--LLEEIQVKLGIgilFVTHDLRVASQIcDDVIVIRRGEC 510
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGKTRV---LVTNQLHFLSQV-DRIILVHEGMI 817
|
....*...
gi 2486247945 511 VESGHVQD 518
Cdd:PLN03130 818 KEEGTYEE 825
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-269 |
2.63e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 50.36 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 30 PNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLPKGLAPADGSVKLLGMDLFRRTPDEIRRLrgakMAMVFQEPM 109
Cdd:PLN03232 1249 PPVLHGLSFFVSPSEKVGVVGRTGAGKS----SMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPV 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 110 TALNPVMTCGDQMDEllraHVPMGPYE--RRIRILDLFEEVRLPDPPRIFRSyPHQLSGGQRQRIVIAMALLLKPDLLIC 187
Cdd:PLN03232 1321 LFSGTVRFNIDPFSE----HNDADLWEalERAHIKDVIDRNPFGLDAEVSEG-GENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 188 DEPTTALNVTTQASILKLILELQKKngTAVLFITHDFGVVSEiADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLINAV 267
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTG 1472
|
..
gi 2486247945 268 PE 269
Cdd:PLN03232 1473 PA 1474
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
32-246 |
6.20e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.58 E-value: 6.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 32 AVEHVSFTVNEGEVTCLIGESGsgksviASTVMGLLPKGLAPADGSVK-------LLGMDLFRRTPDEIRRLRGAKmamv 104
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*G------AA**RGALPAHV*GPDAGRRpwrf*twCANRRALRRTIG*HRPVR*GR---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 105 fQEPMTALNPVMTCGDQMDellrahvpMGPYERRIRILDLFEEVRLPDPP-RIFRSYphqlSGGQRQRIVIAMALLLKPD 183
Cdd:NF000106 98 -RESFSGRENLYMIGR*LD--------LSRKDARARADELLERFSLTEAAgRAAAKY----SGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 184 LLICDEPTTALNVTTQASILKLILELQkKNGTAVLFITHDFGVVSEIADQVVVLELGKQIETG 246
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMV-RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
14-260 |
7.16e-06 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 47.60 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAV----SLPPggdrpnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKglapADGSVKLLGMDLFRRT 89
Cdd:cd03288 20 IKIHDLCVryenNLKP------VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDI----FDGKIVIDGIDISKLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 90 PDEIRrlrgAKMAMVFQEPMT-------ALNPVMTCGDqmDELLRAhvpmgpyerrIRILDLFEEVR-LPDP-PRIFRSY 160
Cdd:cd03288 90 LHTLR----SRLSIILQDPILfsgsirfNLDPECKCTD--DRLWEA----------LEIAQLKNMVKsLPGGlDAVVTEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 161 PHQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQaSILKLILELQKKNGTaVLFITHdfgVVSEI--ADQVVVLE 238
Cdd:cd03288 154 GENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILQKVVMTAFADRT-VVTIAH---RVSTIldADLVLVLS 228
|
250 260
....*....|....*....|..
gi 2486247945 239 LGKQIETGPAKSVLQHPKEPYT 260
Cdd:cd03288 229 RGILVECDTPENLLAQEDGVFA 250
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
309-491 |
9.05e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 309 LKGVSARLRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWvngenvaAAPKRKLhGLrrrLQvvfQDPYrsLDPRMT 388
Cdd:PRK11819 23 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-------PAPGIKV-GY---LP---QEPQ--LDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 VGESIVEG--------------PVNFGVPKEEAWKRAQEFMKI---------------VRLSPDALnRYP------NQFS 433
Cdd:PRK11819 87 VRENVEEGvaevkaaldrfneiYAAYAEPDADFDALAAEQGELqeiidaadawdldsqLEIAMDAL-RCPpwdakvTKLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 434 GGQRQRISIARALACEPEILICDEAVSALDV-SVQadilkLLEEIQVKLGIGILFVTHD 491
Cdd:PRK11819 166 GGERRRVALCRLLLEKPDMLLLDEPTNHLDAeSVA-----WLEQFLHDYPGTVVAVTHD 219
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
164-334 |
1.10e-05 |
|
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: 48.47 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMAL--LLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFITHDFGVVSEiADQVVVL---- 237
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDL-GNTLIVVEHDEDTIRA-ADYVIDIgpga 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 238 --ELGKQIETGPAKSVLQHPKEPYTQKLIN----AVPelKPRHRPpvdgNPTLLEAKNVvktytlggfftgrvKVRALKG 311
Cdd:TIGR00630 567 geHGGEVVASGTPEEILANPDSLTGQYLSGrkkiEVP--AERRPG----NGKFLTLKGA--------------RENNLKN 626
|
170 180
....*....|....*....|...
gi 2486247945 312 VSARLRRGETIGIVGESGSGKST 334
Cdd:TIGR00630 627 ITVSIPLGLFTCITGVSGSGKST 649
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
433-520 |
1.11e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 433 SGGQRQRISIARALACEPEILICDEAVSALDVSVQADILK--LLEEIQVKLGIgilFVTHDLRVASQIcDDVIVIRRGEC 510
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTRV---LVTNQLHFLPLM-DRIILVSEGMI 817
|
90
....*....|
gi 2486247945 511 VESGHVQDVF 520
Cdd:PLN03232 818 KEEGTFAELS 827
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
164-240 |
1.23e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 46.56 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLICDEPTTALNV-----TTQASILKLileLQKKNGTAVLfITHDFGVVSEiADQVVVLE 238
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDIhlsdhLMQEGILKF---LQDDKRTLVL-VTHKLQYLPH-ADWIIAMK 215
|
..
gi 2486247945 239 LG 240
Cdd:cd03290 216 DG 217
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
13-220 |
1.47e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.48 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLPPGGDRPnAVEHVSFTVNEGEVTCLIGESGSG-------------------------KSVIASTVMGLL 67
Cdd:NF040905 257 VFEVKNWTVYHPLHPERK-VVDDVSLNVRRGEIVGIAGLMGAGrtelamsvfgrsygrnisgtvfkdgKEVDVSTVSDAI 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 68 PKGLAPADGSVKLLGMDLfrrtPDEIRRlrgakmamvfQEPMTALNPVMTCG--DQMDELLRAHvpmgPYERRIRIL--D 143
Cdd:NF040905 336 DAGLAYVTEDRKGYGLNL----IDDIKR----------NITLANLGKVSRRGviDENEEIKVAE----EYRKKMNIKtpS 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2486247945 144 LFEEVRlpdpprifrsyphQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKnGTAVLFI 220
Cdd:NF040905 398 VFQKVG-------------NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVI 460
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
164-222 |
1.55e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLKPDLLI-CDEPTTALNVTTQASILKLILELqKKNGTAVLFITH 222
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIH 960
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
305-472 |
1.76e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 305 KVRALKGVSARLRRGETIGIVGESGSGKSTfarsiarLIDPTSGEV---WVNGE-NVAAAPKRKlHGLRRRLQVVFQDPY 380
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTT-------LMDVLAGRKtggYIEGDiRISGFPKKQ-ETFARISGYCEQNDI 963
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 381 RSldPRMTVGESIVEG-----PVNfgVPKEEAWKRAQEFMKIVRLS--PDALNRYP--NQFSGGQRQRISIARALACEPE 451
Cdd:PLN03140 964 HS--PQVTVRESLIYSaflrlPKE--VSKEEKMMFVDEVMELVELDnlKDAIVGLPgvTGLSTEQRKRLTIAVELVANPS 1039
|
170 180
....*....|....*....|.
gi 2486247945 452 ILICDEAVSALDVSVQADILK 472
Cdd:PLN03140 1040 IIFMDEPTSGLDARAAAIVMR 1060
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
317-509 |
2.26e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.21 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 317 RRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNG---ENVAAAPKRKLHG-----LRRRLQVVFQDPYRSLDPRMt 388
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdEILDEFRGSELQNyftklLEGDVKVIVKPQYVDLIPKA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 389 vgesiVEGPVNFGVPKEEAWKRAQEFMKIVRLSPdALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQA 468
Cdd:cd03236 103 -----VKGKVGELLKKKDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2486247945 469 DILKLLEEIqVKLGIGILFVTHDLRVASQIcDDVIVIRRGE 509
Cdd:cd03236 177 NAARLIREL-AEDDNYVLVVEHDLAVLDYL-SDYIHCLYGE 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
165-253 |
2.57e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 165 SGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILElQKKNGTaVLFITHDFGVVSEiADQVVVLELGKQIE 244
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE-EFKSCT-MLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
....*....
gi 2486247945 245 TGPAKSVLQ 253
Cdd:PLN03130 1453 FDTPENLLS 1461
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
33-267 |
2.59e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.21 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 33 VEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGllpkGLAPADGSVKLLGMDLFRRTPDEIRrlrgakmamvfqePMTAL 112
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG----ELEPSEGKIKHSGRISFSPQTSWIM-------------PGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 113 NPVMTcGDQMDELlrahvpmgPYERRIRILDLFEEV-RLPDPPRI-FRSYPHQLSGGQRQRIVIAMALLLKPDLLICDEP 190
Cdd:TIGR01271 505 DNIIF-GLSYDEY--------RYTSVIKACQLEEDIaLFPEKDKTvLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 191 TTALNVTTQASILKLILELQKKNGTAVLfithdfgVVSEI-----ADQVVVLELGKQIETGpAKSVLQHPKEPYTQKLIN 265
Cdd:TIGR01271 576 FTHLDVVTEKEIFESCLCKLMSNKTRIL-------VTSKLehlkkADKILLLHEGVCYFYG-TFSELQAKRPDFSSLLLG 647
|
..
gi 2486247945 266 AV 267
Cdd:TIGR01271 648 LE 649
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-235 |
3.06e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGllpkGLAPADGSVKLLgmdlfrrtpdei 93
Cdd:PRK15064 320 LEVENLTKGF---DNGP-LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG----ELEPDSGTVKWS------------ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 94 rrlRGAKMAMVFQEPMTALNPVMTCGDQMDELLRAhvpmGPYERRIR-ILD--LFEEVRLPDPPRIfrsyphqLSGGQRQ 170
Cdd:PRK15064 380 ---ENANIGYYAQDHAYDFENDLTLFDWMSQWRQE----GDDEQAVRgTLGrlLFSQDDIKKSVKV-------LSGGEKG 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 171 RIVIAMALLLKPDLLICDEPTTALNVttqASILKLILELQKKNGTaVLFITHDFGVVSEIADQVV 235
Cdd:PRK15064 446 RMLFGKLMMQKPNVLVMDEPTNHMDM---ESIESLNMALEKYEGT-LIFVSHDREFVSSLATRII 506
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
316-505 |
3.61e-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: 44.49 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 316 LRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNGENVAAAPKrklhglrrrlqvvfqdpYRSLdprmtvgesive 395
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQ-----------------YIDL------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 396 gpvnfgvpkeeawkraqefmkivrlspdalnrypnqfSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLE 475
Cdd:cd03222 73 -------------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIR 115
|
170 180 190
....*....|....*....|....*....|
gi 2486247945 476 EIQVKLGIGILFVTHDLRVASQICDDVIVI 505
Cdd:cd03222 116 RLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
24-241 |
3.61e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 46.33 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 24 PPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPkglaPADGSVKLLGMDLFRRTPDEIRRLrgakMAM 103
Cdd:COG4615 339 GEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYR----PESGEILLDGQPVTADNREAYRQL----FSA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 104 V------FQEPMTALNPVMTcgDQMDELLRAhvpmgpyerririLDLFEEVRLPDppRIFRSYphQLSGGQRQRIVIAMA 177
Cdd:COG4615 411 VfsdfhlFDRLLGLDGEADP--ARARELLER-------------LELDHKVSVED--GRFSTT--DLSQGQRKRLALLVA 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 178 LLLKPDLLICDE------PT------TalnvttqasilKLILELqKKNGTAVLFITHD---FGVvseiADQVVVLELGK 241
Cdd:COG4615 472 LLEDRPILVFDEwaadqdPEfrrvfyT-----------ELLPEL-KARGKTVIAISHDdryFDL----ADRVLKMDYGK 534
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
27-240 |
3.67e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 45.68 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 27 GDRPNAVEHVSFTVNEGEVTCLIGESGSGKS-----VIASTVMGLLPKGLAPADGSVKLLGM-----------DLFRRTP 90
Cdd:cd03271 5 GARENNLKNIDVDIPLGVLTCVTGVSGSGKSslindTLYPALARRLHLKKEQPGNHDRIEGLehidkvividqSPIGRTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 -----------DEIR-------------------RLRGAKMAMVFQepmtalnpvMTCGDQMDelLRAHVPmgpyerRI- 139
Cdd:cd03271 85 rsnpatytgvfDEIRelfcevckgkrynretlevRYKGKSIADVLD---------MTVEEALE--FFENIP------KIa 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 140 RILDLFEEVRLpDPPRIFRSYPhQLSGGQRQRIVIAMAlLLKPD----LLICDEPTTALNVttqASILKLILELQK--KN 213
Cdd:cd03271 148 RKLQTLCDVGL-GYIKLGQPAT-TLSGGEAQRIKLAKE-LSKRStgktLYILDEPTTGLHF---HDVKKLLEVLQRlvDK 221
|
250 260
....*....|....*....|....*..
gi 2486247945 214 GTAVLFITHDFGVVsEIADQvvVLELG 240
Cdd:cd03271 222 GNTVVVIEHNLDVI-KCADW--IIDLG 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-223 |
3.95e-05 |
|
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: 46.47 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 13 VLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGS------VKLLGMDLF 86
Cdd:TIGR03719 322 VIEAENLTKAF---GDKL-LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQE----QPDSGTieigetVKLAYVDQS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 87 RRTPDeirrlrGAKMamVFQEpMTALNPVMTCGD-QMDEllRAHVPM-----GPYERRIRildlfeevrlpdpprifrsy 160
Cdd:TIGR03719 394 RDALD------PNKT--VWEE-ISGGLDIIKLGKrEIPS--RAYVGRfnfkgSDQQKKVG-------------------- 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486247945 161 phQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQkknGTAVLfITHD 223
Cdd:TIGR03719 443 --QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA---GCAVV-ISHD 499
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
164-240 |
4.51e-05 |
|
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: 46.54 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 164 LSGGQRQRIVIAMALLLK---PDLLICDEPTTALNVttqASILKLILELQK--KNGTAVLFITHDFGVVsEIADQVVvlE 238
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHF---DDIKKLLEVLQRlvDKGNTVVVIEHNLDVI-KTADYII--D 903
|
..
gi 2486247945 239 LG 240
Cdd:TIGR00630 904 LG 905
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
313-490 |
4.92e-05 |
|
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: 46.28 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 313 SARLRRGETIGIVGESGSGKStfarSIARLIdptsGEVW-VNGENVAAAPKRKLhglrrrlqvvFQDPYRsldPRMTVG- 390
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKS----SLFRIL----GELWpVYGGRLTKPAKGKL----------FYVPQR---PYMTLGt 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 391 --ESIVegpvnFGVPKEEAWKRA---QEFMKI---VRL--------SPDALNRYPNQFSGGQRQRISIARALACEPEILI 454
Cdd:TIGR00954 531 lrDQII-----YPDSSEDMKRRGlsdKDLEQIldnVQLthileregGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180 190
....*....|....*....|....*....|....*.
gi 2486247945 455 CDEAVSALDVSVQADILKLLEEIqvklGIGILFVTH 490
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLCREF----GITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
163-531 |
5.71e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQRIVIAMALLLKPDLLICDEPTTALN-------------------VTTQA-----SILKLILEL--QKKNGTA 216
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDlhavlwletyllkwpktfiVVSHAreflnTVVTDILHLhgQKLVTYK 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 217 VLFITHDFGVVSEIADQVVVLELGKQ----IETGPAKSVLQHPKEPYTQKLINAVPEL--------KPRHR---PPVDGN 281
Cdd:PLN03073 424 GDYDTFERTREEQLKNQQKAFESNERsrshMQAFIDKFRYNAKRASLVQSRIKALDRLghvdavvnDPDYKfefPTPDDR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 282 PtllEAKNVVKTYTLGGFFTGRVKVRALK-GVSARLRrgetIGIVGESGSGKSTFARSIARLIDPTSGEVWvngenvaAA 360
Cdd:PLN03073 504 P---GPPIISFSDASFGYPGGPLLFKNLNfGIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTVF-------RS 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 361 PKrklhglrRRLQVVFQDPYRSLDprMTVGESIVEGPVNFGVPKEEAWKRAQEFMKIVRLSPDALnrypNQFSGGQRQRI 440
Cdd:PLN03073 570 AK-------VRMAVFSQHHVDGLD--LSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPM----YTLSGGQKSRV 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 441 SIARALACEPEILICDEAVSALDV-SVQADILKLleeiqVKLGIGILFVTHDLRVASQICDDVIVIRRGECVEsghvqdv 519
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDLdAVEALIQGL-----VLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTP------- 704
|
410
....*....|...
gi 2486247945 520 fFHPQ-HEYTKSL 531
Cdd:PLN03073 705 -FHGTfHDYKKTL 716
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-309 |
6.18e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 45.99 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 18 NLAVSLPP-------GGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLApaDGSVKLLGmdlFRRTP 90
Cdd:PLN03140 874 NYFVDMPAemkeqgvTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYI--EGDIRISG---FPKKQ 948
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 91 DEIRRLRGakmamvFQEPMTALNPVMTCGDQM--DELLRAHVPMGPYERRIRILDLFEEVRLPDPPRIFRSYP--HQLSG 166
Cdd:PLN03140 949 ETFARISG------YCEQNDIHSPQVTVRESLiySAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLST 1022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 167 GQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIADQVVVLELGKQ-IET 245
Cdd:PLN03140 1023 EQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQvIYS 1102
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 246 GPAKSVlQHPKEPYTQKlINAVPELKPRHRPPVdgnpTLLEAKNVVKTYTLGGFFTGRVKVRAL 309
Cdd:PLN03140 1103 GPLGRN-SHKIIEYFEA-IPGVPKIKEKYNPAT----WMLEVSSLAAEVKLGIDFAEHYKSSSL 1160
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-222 |
7.43e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.39 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLppgGDRPnAVEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLPKGLApadGSVKLLGMdlfRRTPD 91
Cdd:PRK10938 259 PRIVLNNGVVSY---NDRP-ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYS---NDLTLFGR---RRGSG 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 92 E----IRRLRG---AKMAMVFQEPMTALNpVMTCG--DQMdellrahvpmGPYER---RIRI-----LDLFE-EVRLPDP 153
Cdd:PRK10938 329 EtiwdIKKHIGyvsSSLHLDYRVSTSVRN-VILSGffDSI----------GIYQAvsdRQQKlaqqwLDILGiDKRTADA 397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 154 PriFRSyphqLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITH 222
Cdd:PRK10938 398 P--FHS----LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-222 |
1.52e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.01 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 33 VEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglAPADGSVKLLGMDlfrrtpdeIRRLRGA-KMAMVFQEPMTA 111
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLL----NPEKGEILFERQS--------IKKDLCTyQKQLCFVGHRSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 112 LNPVMTCGDQMdeLLRAHVPMGPYERRiRILDLFEEVRLPDpprifrsYP-HQLSGGQRQRIVIAMALLLKPDLLICDEP 190
Cdd:PRK13540 85 INPYLTLRENC--LYDIHFSPGAVGIT-ELCRLFSLEHLID-------YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|....
gi 2486247945 191 TTALNvttQASILKLILELQ--KKNGTAVLFITH 222
Cdd:PRK13540 155 LVALD---ELSLLTIITKIQehRAKGGAVLLTSH 185
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
14-206 |
1.85e-04 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 43.30 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 14 LEVENLAVSLPPGGdrpNAV-EHVSFTVNEGEVTCLIGESGSGKSVIASTVMGLLpkglaPADGSVKLLGMDLFRRTPDE 92
Cdd:cd03289 3 MTVKDLTAKYTEGG---NAVlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-----NTEGDIQIDGVSWNSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 93 IRRLRGAKMAMVFQEPMTALNPVMTCGDQMDEllrahvpmgpyerriRILDLFEEVRLPDpprIFRSYPHQ--------- 163
Cdd:cd03289 75 WRKAFGVIPQKVFIFSGTFRKNLDPYGKWSDE---------------EIWKVAEEVGLKS---VIEQFPGQldfvlvdgg 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2486247945 164 --LSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLI 206
Cdd:cd03289 137 cvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTL 181
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
163-223 |
2.71e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 2.71e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 163 QLSGGQRQ------RIVIAMALLLKPDLLICDEPTTAL---NVTTqaSILKLILELQKKNGTAVLFITHD 223
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLdeeNIEE--SLAEIIEERKSQKNFQLIVITHD 182
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
12-242 |
3.90e-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: 41.85 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 12 PVLEVENLAVSLPPGGDRPNAVEHVSFTVNEGEVTCLIGESGSGKSviasTVMGLLP--KGLAPADGSVKLLGmdlfRRT 89
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKT----TLLDVLAgrKTAGVITGEILING----RPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 90 PDEIRRLRGakmamvFQEPMTALNPVMTcgdqMDELLRahvpmgpyerririldlfeevrlpdppriFRSYPHQLSGGQR 169
Cdd:cd03232 74 DKNFQRSTG------YVEQQDVHSPNLT----VREALR-----------------------------FSALLRGLSVEQR 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 170 QRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELqKKNGTAVLFITHD-FGVVSEIADQVVVLELGKQ 242
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIHQpSASIFEKFDRLLLLKRGGK 187
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
33-264 |
4.62e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 42.15 E-value: 4.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 33 VEHVSFTVNEGEVTCLIGESGSGKSVIASTVMGllpkGLAPADGSVKLLGMDLFRRTPDEIrrlrgakMAMVFQEPMTAl 112
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILG----ELEPSEGKIKHSGRISFSSQFSWI-------MPGTIKENIIF- 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 113 npvmtcGDQMDELlrahvpmgPYERRIRILDLFEEV-RLPDPPRIFRSYPH-QLSGGQRQRIVIAMALLLKPDLLICDEP 190
Cdd:cd03291 121 ------GVSYDEY--------RYKSVVKACQLEEDItKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2486247945 191 TTALNVTTQASILKLILELQKKNGTAVLfithdfgVVSEI-----ADQVVVLELGKQIETGpAKSVLQHPKEPYTQKLI 264
Cdd:cd03291 187 FGYLDVFTEKEIFESCVCKLMANKTRIL-------VTSKMehlkkADKILILHEGSSYFYG-TFSELQSLRPDFSSKLM 257
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
170-245 |
4.85e-04 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 42.34 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 170 QRIV-IAMAL---LLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTAVLFITHDFGVVSEIA-----DQVVVLELG 240
Cdd:COG1106 208 KRLLaLAGALldaLAKGGVLLIDEIEASLHPSLLRKLLKLFLDLANKNNAQLIFTTHSTELLDAFLellrrDQIWFVEKD 287
|
....*
gi 2486247945 241 KQIET 245
Cdd:COG1106 288 KDGAS 292
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
316-509 |
5.62e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 42.87 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 316 LRRGETIGIVGESGSGKSTFARSIARLIDPTSGEVWVNG--ENVaaapkrklhgLRR----RLQVVFQDPYrslDPRMTV 389
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswDEV----------LKRfrgtELQNYFKKLY---NGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 390 GESI---------VEGPVnfgvpkEEAWKRAQE---FMKIV-RLSPDA-LNRYPNQFSGGQRQRISIARALACEPEILIC 455
Cdd:PRK13409 163 VHKPqyvdlipkvFKGKV------RELLKKVDErgkLDEVVeRLGLENiLDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2486247945 456 DEAVSALDVSVQADILKLLEEIQVklGIGILFVTHDLRVASQICdDVIVIRRGE 509
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLA-DNVHIAYGE 287
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
409-509 |
9.59e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 42.08 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 409 KRAQEFMKIVRLSPdALNRYPNQFSGGQRQRISIARALACEPEILICDEAVSALDVSVQADILKLLEEIqVKLGIGILFV 488
Cdd:COG1245 191 GKLDELAEKLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVV 268
|
90 100
....*....|....*....|....
gi 2486247945 489 THDLrvasQICD---DVIVIRRGE 509
Cdd:COG1245 269 EHDL----AILDylaDYVHILYGE 288
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
164-235 |
1.05e-03 |
|
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: 40.00 E-value: 1.05e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2486247945 164 LSGGQRQRIVIA--MALLLKPDLLICDEPTTALNvttQASILKLILELQK--KNGTAVLFITHDFGVVSEiADQVV 235
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLH---QQDINQLLEVIKGliDLGNTVILIEHNLDVLSS-ADWII 159
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
312-384 |
1.49e-03 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 41.04 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 312 VSARLRRGETIGIVGESGSGKSTFARSIARLIdpTSGE------------VWVNGENVAAAPKRKLHGLRRRLQVVFQDP 379
Cdd:COG3598 6 VPGLLPEGGVTLLAGPPGTGKSFLALQLAAAV--AAGGpwlgrrvppgkvLYLAAEDDRGELRRRLKALGADLGLPFADL 83
|
....*
gi 2486247945 380 YRSLD 384
Cdd:COG3598 84 DGRLR 88
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
162-241 |
1.81e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 162 HQLSGGQRQRIVIAMALLLKPDLLICDEPTTALNVTTQASILKLILELQKkngtAVLFITHDFGVVSEIADQVVVLELGK 241
Cdd:PLN03073 626 YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG----GVLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
322-343 |
2.62e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 39.44 E-value: 2.62e-03
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
314-345 |
3.93e-03 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 39.61 E-value: 3.93e-03
10 20 30
....*....|....*....|....*....|..
gi 2486247945 314 ARLRRGETIGIVGESGSGKSTFARSIARLIDP 345
Cdd:PRK07429 3 SMPDRPVLLGVAGDSGCGKTTFLRGLADLLGE 34
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
322-347 |
4.52e-03 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 38.60 E-value: 4.52e-03
10 20
....*....|....*....|....*.
gi 2486247945 322 IGIVGESGSGKSTFARSIARLIDPTS 347
Cdd:PRK05480 9 IGIAGGSGSGKTTVASTIYEELGDES 34
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
511-536 |
5.34e-03 |
|
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.
Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 35.45 E-value: 5.34e-03
|
| NACHT |
COG5635 |
Predicted NTPase, NACHT family domain [Signal transduction mechanisms]; |
137-341 |
5.94e-03 |
|
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.40 E-value: 5.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 137 RRIRILDLFEEVRLPDPPRIFRSYPHQLSGGQRQRIVIAmALLLKPDLLICDEPTTALNVTTQASILKLILELQKKNGTA 216
Cdd:COG5635 2 LLLLALILALLALVLLLDLLVTRLAIALAALLLLALVAL-GLALLALLDLLLADLGALLALVSRSALSAAALLARALSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486247945 217 VLFITHDFGVVSEIADQVVVLELGKQIETGPAKSVLQHPKEPYTQKLINAVPELKPRHRPPVDGNPTLLEAKNVVKTYTL 296
Cdd:COG5635 81 LLVLLLLESLLLLLLLLLLLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2486247945 297 GGFFTGRVKVRALKGVSARLRRgetIGIVGESGSGKSTFARSIAR 341
Cdd:COG5635 161 LNLLERIESLKRLELLEAKKKR---LLILGEPGSGKTTLLRYLAL 202
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
322-342 |
7.07e-03 |
|
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.
Pssm-ID: 238984 [Multi-domain] Cd Length: 273 Bit Score: 38.47 E-value: 7.07e-03
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
163-223 |
8.04e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.95 E-value: 8.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2486247945 163 QLSGGQRQRivIAMALLLKP--DLLICDEPTTALNVTTQASilkliLE--LQKKNGTAVLfITHD 223
Cdd:PRK11819 445 VLSGGERNR--LHLAKTLKQggNVLLLDEPTNDLDVETLRA-----LEeaLLEFPGCAVV-ISHD 501
|
|
| |
