|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-523 |
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: 739.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVESGRLVFRDEDLADRSE 80
Cdd:COG4172 4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 EAMRQLRGRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPFELSGGQRQ 160
Cdd:COG4172 84 RELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 161 RVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPA 240
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 241 VLRVPREDYTRQLLAAvSAQPLVPRTQVAGPVVLKAEALGKVFCSRSGWWGRRTTQ--ALDAVQLQLREGETLGIVGESG 318
Cdd:COG4172 244 LFAAPQHPYTRKLLAA-EPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRRTVGHvkAVDGVSLTLRRGETLGLVGESG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 319 SGKSTLGRCLVRLLRAdSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDPFASLNPRQTVGQIVMTGPLVQGVSKADAER 398
Cdd:COG4172 323 SGKSTLGLALLRLIPS-EGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAER 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 399 RAR--ELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVF 476
Cdd:COG4172 402 RARvaEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLF 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1331382268 477 ITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMA 523
Cdd:COG4172 482 ISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAA 528
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-523 |
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: 636.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALPAGadRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVeSGRLVFRDEDLADRSEe 81
Cdd:COG1123 3 PLLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI-SGEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 amrQLRGRDISMVFQEPMSALNPLmRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLpdpERLRLAYPFELSGGQRQR 161
Cdd:COG1123 79 ---ALRGRRIGMVFQDPMTQLNPV-TVGDQIAEALENLGLSRAE-ARARVLELLEAVGL---ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 162 VVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAV 241
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 242 LRVPredytrQLLAAV----SAQPLVPRTQVAGPVVLKAEALGKVFCSRsgwwGRRTTQALDAVQLQLREGETLGIVGES 317
Cdd:COG1123 231 LAAP------QALAAVprlgAARGRAAPAAAAAEPLLEVRNLSKRYPVR----GKGGVRAVDDVSLTLRRGETLGLVGES 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 318 GSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDPFASLNPRQTVGQIVMTGPLVQGV-SKADA 396
Cdd:COG1123 301 GSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLlSRAER 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 397 ERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVF 476
Cdd:COG1123 381 RERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLF 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1331382268 477 ITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMA 523
Cdd:COG1123 461 ISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAA 507
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-521 |
3.49e-161 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 468.42 E-value: 3.49e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKV-ESGRLVFRDEDLADRS 79
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVyPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 80 EEAMRQLRGRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPFELSGGQR 159
Cdd:PRK15134 83 EQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 160 QRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAP 239
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 240 AVLRVPREDYTRQLLAAVSAQPLVPRTQVAGPvVLKAEALGKVFCSRSGWWGRRTTQ--ALDAVQLQLREGETLGIVGES 317
Cdd:PRK15134 243 TLFSAPTHPYTQKLLNSEPSGDPVPLPEPASP-LLDVEQLQVAFPIRKGILKRTVDHnvVVKNISFTLRPGETLGLVGES 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 318 GSGKSTLGRCLVRLLRAdSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDPFASLNPRQTVGQIVMTGPLVQ--GVSKAD 395
Cdd:PRK15134 322 GSGKSTTGLALLRLINS-QGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHqpTLSAAQ 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 396 AERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIV 475
Cdd:PRK15134 401 REQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYL 480
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1331382268 476 FITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELL 521
Cdd:PRK15134 481 FISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-523 |
1.16e-153 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 452.77 E-value: 1.16e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDP-LKVESGRLVFRDE-----DLA 76
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAgGLVQCDKMLLRRRsrqviELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 77 DRSEEAMRQLRGRDISMVFQEPMSALNPLMRVGEQIDETLRAH---GVAAARVRRQRVVDLlgyVGLPDPERLRLAYPFE 153
Cdd:PRK10261 92 EQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHqgaSREEAMVEAKRMLDQ---VRIPEAQTILSRYPHQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVV 233
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 234 EQGTAPAVLRVPREDYTRQLLAAV------SAQPLVPR-------------------TQVAGPVVLKAEALGKVFCSRSG 288
Cdd:PRK10261 249 ETGSVEQIFHAPQHPYTRALLAAVpqlgamKGLDYPRRfplislehpakqeppieqdTVVDGEPILQVRNLVTRFPLRSG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 289 WWGR--RTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQ 366
Cdd:PRK10261 329 LLNRvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 367 DPFASLNPRQTVGQIVMTGPLVQGVSKAD-AERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIAD 445
Cdd:PRK10261 409 DPYASLDPRQTVGDSIMEPLRVHGLLPGKaAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIAD 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 446 ECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMA 523
Cdd:PRK10261 489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAA 566
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-257 |
5.72e-128 |
|
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: 375.93 E-value: 5.72e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVeSGRLVFRDEDLADRSEEA 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGIT-SGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLRGRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPFELSGGQRQRV 162
Cdd:COG0444 80 LRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVL 242
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
250
....*....|....*
gi 1331382268 243 RVPREDYTRQLLAAV 257
Cdd:COG0444 240 ENPRHPYTRALLSSI 254
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
272-523 |
1.72e-124 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 367.52 E-value: 1.72e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 272 VVLKAEALGKVFCSRSGWWGRRTT--QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGL 349
Cdd:COG4608 6 PLLEVRDLKKHFPVRGGLFGRTVGvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 350 SEGRLRALRSDVQMIFQDPFASLNPRQTVGQIVMTGPLVQGV-SKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQR 428
Cdd:COG4608 86 SGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 429 IGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDEL 245
|
250
....*....|....*
gi 1331382268 509 FADARHPYTRELLMA 523
Cdd:COG4608 246 YARPLHPYTQALLSA 260
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
273-523 |
1.89e-118 |
|
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: 351.66 E-value: 1.89e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSRSGwwgrrTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRA---DSGRIEWLGREVAGL 349
Cdd:COG0444 1 LLEVRNLKVYFPTRRG-----VVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 350 SEGRLRALR-SDVQMIFQDPFASLNPRQTVGQIVMTGPLV-QGVSKADAERRARELLGLVGLPAAA--FERFPHEFSGGQ 425
Cdd:COG0444 76 SEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPErrLDRYPHELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 426 RQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGET 505
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPV 235
|
250
....*....|....*...
gi 1331382268 506 AALFADARHPYTRELLMA 523
Cdd:COG0444 236 EELFENPRHPYTRALLSS 253
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-236 |
2.05e-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: 2.05e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEEa 82
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL----KPTSGSIIFDGKDLLKLSRR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLRGRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLgYVGLPDPERLRLAYPFELSGGQRQRV 162
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLL-LVGVGLPEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
273-503 |
4.10e-104 |
|
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: 311.36 E-value: 4.10e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSRSGWwgrrtTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEG 352
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-----VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 353 RLRALRSDVQMIFQDPFASLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGL--VGLPAAAFERFPHEFSGGQRQRIG 430
Cdd:cd03257 76 LRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLvgVGLPEEVLNRYPHELSGGQRQRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 431 IARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03257 156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
274-523 |
1.32e-99 |
|
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: 300.57 E-value: 1.32e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFcsrsgWWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGlseGR 353
Cdd:COG1124 2 LEVRNLSVSY-----GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR---RR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 LRALRSDVQMIFQDPFASLNPRQTVGQIVMTGPLVQGVskADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIAR 433
Cdd:COG1124 74 RKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 434 ALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADAR 513
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPK 231
|
250
....*....|
gi 1331382268 514 HPYTRELLMA 523
Cdd:COG1124 232 HPYTRELLAA 241
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
2-257 |
1.88e-98 |
|
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: 307.77 E-value: 1.88e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALP-------AGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkveSGRLVFRDED 74
Cdd:COG4172 274 PLLEARDLKVWFPikrglfrRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-----EGEIRFDGQD 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 75 LADRSEEAMRQLRgRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARV-RRQRVVDLLGYVGLPDPERLRlaYPFE 153
Cdd:COG4172 349 LDGLSRRALRPLR-RRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPGLSAAeRRARVAEALEEVGLDPAARHR--YPHE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVV 233
Cdd:COG4172 426 FSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
|
250 260
....*....|....*....|....
gi 1331382268 234 EQGTAPAVLRVPREDYTRQLLAAV 257
Cdd:COG4172 506 EQGPTEQVFDAPQHPYTRALLAAA 529
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-257 |
2.53e-97 |
|
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: 304.13 E-value: 2.53e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALPA-GADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRqLpdpLKVESGRLVFRDEDLADRSE 80
Cdd:COG1123 259 PLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLG-L---LRPTSGSILFDGKDLTKLSR 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 EAMRQLRgRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPdpERLRLAYPFELSGGQRQ 160
Cdd:COG1123 335 RSLRELR-RRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 161 RVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPA 240
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEE 491
|
250
....*....|....*..
gi 1331382268 241 VLRVPREDYTRQLLAAV 257
Cdd:COG1123 492 VFANPQHPYTRALLAAV 508
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
291-524 |
6.28e-95 |
|
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: 298.52 E-value: 6.28e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLL----RADSGRIEWLGREVAGLSEGRLRALR-SDVQMIF 365
Cdd:COG4172 19 GGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLpdpaAHPSGSILFDGQDLLGLSERELRRIRgNRIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 366 QDPFASLNPRQTVG-QIVMTGPLVQGVSKADAERRARELLGLVGLPAAAF--ERFPHEFSGGQRQRIGIARALAVEPKVL 442
Cdd:COG4172 99 QEPMTSLNPLHTIGkQIAEVLRLHRGLSGAAARARALELLERVGIPDPERrlDAYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 443 IADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLM 522
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLLA 258
|
..
gi 1331382268 523 AE 524
Cdd:COG4172 259 AE 260
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
289-526 |
2.50e-93 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 287.76 E-value: 2.50e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 289 WWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDP 368
Cdd:PRK15079 28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 369 FASLNPRQTVGQIVMTgPLVQ---GVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIAD 445
Cdd:PRK15079 108 LASLNPRMTIGEIIAE-PLRTyhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 446 ECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMAEA 525
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
.
gi 1331382268 526 I 526
Cdd:PRK15079 267 I 267
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-257 |
9.94e-89 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 275.84 E-value: 9.94e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALP--AGADRS-----HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRqLPDPlkvESGRLVFRDEDL 75
Cdd:COG4608 7 LLEVRDLKKHFPvrGGLFGRtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLR-LEEP---TSGEILFDGQDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 76 ADRSEEAMRQLRgRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPdPERLRlAYPFELS 155
Cdd:COG4608 83 TGLSGRELRPLR-RRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR-PEHAD-RYPHEFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQ 235
Cdd:COG4608 160 GGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEI 239
|
250 260
....*....|....*....|..
gi 1331382268 236 GTAPAVLRVPREDYTRQLLAAV 257
Cdd:COG4608 240 APRDELYARPLHPYTQALLSAV 261
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-259 |
1.62e-86 |
|
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: 267.05 E-value: 1.62e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVFRDEDLADRSEEA 82
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP----WSGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRqlrgRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAarvRRQRVVDLLGYVGLPdpERLRLAYPFELSGGQRQRV 162
Cdd:COG1124 77 FR----RRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPD---REERIAELLEQVGLP--PSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVL 242
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*..
gi 1331382268 243 RVPREDYTRQLLAAVSA 259
Cdd:COG1124 228 AGPKHPYTRELLAASLA 244
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
269-523 |
1.12e-85 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 267.60 E-value: 1.12e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 269 AGPVVLKAEALGKVFCSRSGWW-GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVA 347
Cdd:PRK11308 1 SQQPLLQAIDLKKHYPVKRGLFkPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 348 GLSEGRLRALRSDVQMIFQDPFASLNPRQTVGQIvMTGPLVQGVSKADAERRAR--ELLGLVGLPAAAFERFPHEFSGGQ 425
Cdd:PRK11308 81 KADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQI-LEEPLLINTSLSAAERREKalAMMAKVGLRPEHYDRYPHMFSGGQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 426 RQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGET 505
Cdd:PRK11308 160 RQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTK 239
|
250
....*....|....*...
gi 1331382268 506 AALFADARHPYTRELLMA 523
Cdd:PRK11308 240 EQIFNNPRHPYTQALLSA 257
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
277-521 |
4.10e-79 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 251.15 E-value: 4.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 277 EALGKVFCSRSGwwgrrTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRA 356
Cdd:COG1135 5 ENLSKTFPTKGG-----PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 357 LRSDVQMIFQDpFASLNPRqTVGQIVMTgPL-VQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARAL 435
Cdd:COG1135 80 ARRKIGMIFQH-FNLLSSR-TVAENVAL-PLeIAGVPKAEIRKRVAELLELVGLSDKA-DAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 436 AVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHP 515
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSE 235
|
....*.
gi 1331382268 516 YTRELL 521
Cdd:COG1135 236 LTRRFL 241
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-257 |
5.73e-78 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 247.73 E-value: 5.73e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVESGRLVFRDEDLADRSE 80
Cdd:PRK11022 1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 EAMRQLRGRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPFELSGGQRQ 160
Cdd:PRK11022 81 KERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 161 RVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPA 240
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
250
....*....|....*..
gi 1331382268 241 VLRVPREDYTRQLLAAV 257
Cdd:PRK11022 241 IFRAPRHPYTQALLRAL 257
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
25-256 |
6.40e-76 |
|
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: 239.19 E-value: 6.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVESGRLVFRDEDLADRSeeamrqLRGRDISMVFQEPMSALNP 104
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNPRTAFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVGEQIDETLRAHGVAAArVRRQRVVDLLGYVGLPDPERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSAL 184
Cdd:TIGR02770 78 LFTMGNHAIETLRSLGKLSK-QARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 185 DVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAA 256
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLSA 228
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-257 |
2.31e-75 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 241.35 E-value: 2.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVESGRLVFRDEDLADRSE 80
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 EAMRQLRGRDISMVFQEPMSALNPLMRVGEQIDE-----TLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPFELS 155
Cdd:COG4170 81 RERRKIIGREIAMIFQEPSSCLDPSAKIGDQLIEaipswTFKGKWWQRFKWRKKRAIELLHRVGIKDHKDIMNSYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQ 235
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250 260
....*....|....*....|..
gi 1331382268 236 GTAPAVLRVPREDYTRQLLAAV 257
Cdd:COG4170 241 GPTEQILKSPHHPYTKALLRSM 262
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
274-523 |
2.34e-72 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 231.26 E-value: 2.34e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFCSRSGWWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREvagLSEGR 353
Cdd:COG4167 5 LEVRNLSKTFKYRTGLFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHK---LEYGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 LRALRSDVQMIFQDPFASLNPRQTVGQIvMTGPLVQGVSKADAERRAR--ELLGLVGLPAAAFERFPHEFSGGQRQRIGI 431
Cdd:COG4167 82 YKYRCKHIRMIFQDPNTSLNPRLNIGQI-LEEPLRLNTDLTAEEREERifATLRLVGLLPEHANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 432 ARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250
....*....|..
gi 1331382268 512 ARHPYTRELLMA 523
Cdd:COG4167 241 PQHEVTKRLIES 252
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
277-510 |
3.97e-71 |
|
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: 226.69 E-value: 3.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 277 EALGKVFCSRsgwwgRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRA 356
Cdd:cd03258 5 KNVSKVFGDT-----GGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 357 LRSDVQMIFQDpFASLNPRQTVGQIVMtgPL-VQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARAL 435
Cdd:cd03258 80 ARRRIGMIFQH-FNLLSSRTVFENVAL--PLeIAGVPKAEIEERVLELLELVGLEDKA-DAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 436 AVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFA 230
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
273-523 |
2.05e-69 |
|
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: 223.53 E-value: 2.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSRSGWWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEG 352
Cdd:TIGR02769 2 LLEVRDVTHTYRTGGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 353 RLRALRSDVQMIFQDPFASLNPRQTVGQIVMTgPL--VQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIG 430
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGE-PLrhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 431 IARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLS 240
|
250
....*....|...
gi 1331382268 511 dARHPYTRELLMA 523
Cdd:TIGR02769 241 -FKHPAGRNLQSA 252
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-257 |
3.53e-69 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 224.99 E-value: 3.53e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVeSGRLVFRDEDLADRSE 80
Cdd:PRK09473 10 DALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRI-GGSATFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 EAMRQLRGRDISMVFQEPMSALNPLMRVGEQIDETLRAH-GVAAARVRRQRVvDLLGYVGLPDP-ERLRLaYPFELSGGQ 158
Cdd:PRK09473 89 KELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHkGMSKAEAFEESV-RMLDAVKMPEArKRMKM-YPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 159 RQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTA 238
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNA 246
|
250
....*....|....*....
gi 1331382268 239 PAVLRVPREDYTRQLLAAV 257
Cdd:PRK09473 247 RDVFYQPSHPYSIGLLNAV 265
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
291-523 |
6.89e-68 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 221.98 E-value: 6.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDpFA 370
Cdd:PRK11153 14 GGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQH-FN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SLNPRQTVGQIVMtgPL-VQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK11153 93 LLSSRTVFDNVAL--PLeLAGTPKAEIKARVTELLELVGLSDKA-DRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 450 ALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMA 523
Cdd:PRK11153 170 ALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQS 243
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
274-523 |
2.24e-67 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 218.40 E-value: 2.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFCSRSGWWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGR 353
Cdd:PRK10419 4 LNVSGLSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 LRALRSDVQMIFQDPFASLNPRQTVGQIVMTgPL--VQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGI 431
Cdd:PRK10419 84 RKAFRRDIQMVFQDSISAVNPRKTVREIIRE-PLrhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 432 ARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAd 511
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT- 241
|
250
....*....|..
gi 1331382268 512 ARHPYTRELLMA 523
Cdd:PRK10419 242 FSSPAGRVLQNA 253
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-257 |
2.86e-67 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 220.35 E-value: 2.86e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGADRS---------HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDE 73
Cdd:PRK15079 8 LLEVADLKVHFDIKDGKQwfwqppktlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV----KATDGEVAWLGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 74 DLADRSEEAMRQLRgRDISMVFQEPMSALNPLMRVGEQIDETLRAH--GVAAARVRrQRVVDLLGYVGL-PDperLRLAY 150
Cdd:PRK15079 84 DLLGMKDDEWRAVR-SDIQMIFQDPLASLNPRMTIGEIIAEPLRTYhpKLSRQEVK-DRVKAMMLKVGLlPN---LINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 151 PFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKG 230
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG 238
|
250 260
....*....|....*....|....*..
gi 1331382268 231 RVVEQGTAPAVLRVPREDYTRQLLAAV 257
Cdd:PRK15079 239 HAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
15-256 |
3.16e-67 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 219.84 E-value: 3.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 15 AGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAkallRQLPDPLKVESGRLVFRDEDLADRSEEAMRQLRgRDISMV 94
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLA----RLLTMIETPTGGELYYQGQDLLKADPEAQKLLR-QKIQIV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 95 FQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLpDPE---RlrlaYPFELSGGQRQRVVIAMALAFD 171
Cdd:PRK11308 98 FQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGL-RPEhydR----YPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTR 251
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQ 252
|
....*
gi 1331382268 252 QLLAA 256
Cdd:PRK11308 253 ALLSA 257
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
297-523 |
4.61e-66 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 216.90 E-value: 4.61e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLrADSGRIE----WLGREVAGLSEGRLRALRSD-VQMIFQDPFAS 371
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGgsatFNGREILNLPEKELNKLRAEqISMIFQDPMTS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 372 LNPRQTVG-QIVMTGPLVQGVSKADAERRARELLGLVGLPAAA--FERFPHEFSGGQRQRIGIARALAVEPKVLIADECV 448
Cdd:PRK09473 110 LNPYMRVGeQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 449 SALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMA 523
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNA 264
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-255 |
9.96e-65 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 219.19 E-value: 9.96e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALPAG-------ADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkvESGRLVFRDED 74
Cdd:PRK15134 274 PLLDVEQLQVAFPIRkgilkrtVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-----SQGEIWFDGQP 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 75 LADRSEEAMRQLRGRdISMVFQEPMSALNPLMRVGEQIDETLRAH-GVAAARVRRQRVVDLLGYVGLpDPErLRLAYPFE 153
Cdd:PRK15134 349 LHNLNRRQLLPVRHR-IQVVFQDPNSSLNPRLNVLQIIEEGLRVHqPTLSAAQREQQVIAVMEEVGL-DPE-TRHRYPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVV 233
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
250 260
....*....|....*....|..
gi 1331382268 234 EQGTAPAVLRVPREDYTRQLLA 255
Cdd:PRK15134 506 EQGDCERVFAAPQQEYTRQLLA 527
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
4-262 |
6.06e-63 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 209.16 E-value: 6.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKAL-LRQLPDplkveSGRLVFRDEDLADRSEEA 82
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInLLERPT-----SGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLRgRDISMVFQEPmsalNPLMR--VGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPDPERlrlAYPFELSGGQRQ 160
Cdd:COG1135 77 LRAAR-RKIGMIFQHF----NLLSSrtVAENVALPLEIAGVPKAE-IRKRVAELLELVGLSDKAD---AYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 161 RVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPA 240
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLD 227
|
250 260
....*....|....*....|..
gi 1331382268 241 VLRVPREDYTRQLLAAVSAQPL 262
Cdd:COG1135 228 VFANPQSELTRRFLPTVLNDEL 249
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
274-499 |
1.31e-62 |
|
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: 203.88 E-value: 1.31e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFCSrsgwwGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGR 353
Cdd:cd03255 1 IELKNLSKTYGG-----GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 LRALRSD-VQMIFQDPfaSLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIA 432
Cdd:cd03255 76 LAAFRRRhIGFVFQSF--NLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRL-NHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 433 RALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVaARLCDRIAVMRKGRV 499
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
271-502 |
1.90e-62 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 203.74 E-value: 1.90e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 271 PVVLKAEALGKVFCSrsgwwGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLS 350
Cdd:COG1136 2 SPLLELRNLTKSYGT-----GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 351 EGRLRALRSD-VQMIFQDPFasLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRI 429
Cdd:COG1136 77 ERELARLRRRhIGFVFQFFN--LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRL-DHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 430 GIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQ 502
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
295-513 |
3.99e-62 |
|
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: 203.33 E-value: 3.99e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglSEGRLRALRSDVQMIFQDP----FA 370
Cdd:COG1122 14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKVGLVFQNPddqlFA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SlnprqTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSA 450
Cdd:COG1122 91 P-----TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLA-DRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAG 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 451 LDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADAR 513
Cdd:COG1122 165 LDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
269-501 |
1.40e-61 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 202.63 E-value: 1.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 269 AGPVVLKAEALGKVFCSRSGwwgrrTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAG 348
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGG-----GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 349 LSegrlralrSDVQMIFQDPfaSLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLpaAAFE-RFPHEFSGGQRQ 427
Cdd:COG1116 78 PG--------PDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGL--AGFEdAYPHQLSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 428 RIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVM--RKGRVVE 501
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRIVE 221
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1-256 |
1.81e-60 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 200.06 E-value: 1.81e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHL------RIALPaGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDED 74
Cdd:COG4167 2 SALLEVRNLsktfkyRTGLF-RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAK-MLAGIIEP---TSGEILINGHK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 75 LADRSeeamRQLRGRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGL-PDPerlRLAYPFE 153
Cdd:COG4167 77 LEYGD----YKYRCKHIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPEH---ANFYPHM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVV 233
Cdd:COG4167 150 LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
250 260
....*....|....*....|...
gi 1331382268 234 EQGTAPAVLRVPREDYTRQLLAA 256
Cdd:COG4167 230 EYGKTAEVFANPQHEVTKRLIES 252
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
298-521 |
2.99e-60 |
|
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: 198.66 E-value: 2.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDP--FASLnpr 375
Cdd:COG1127 21 LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIGMLFQGGalFDSL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 qTVGQIVMTgPLVQ--GVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:COG1127 98 -TVFENVAF-PLREhtDLSEAEIRELVLEKLELVGLPGAA-DKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLDP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGeTAALFADARHPYTRELL 521
Cdd:COG1127 175 ITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG-TPEELLASDDPWVRQFL 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
294-521 |
3.85e-59 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 195.60 E-value: 3.85e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaGLSEGRLRALRSDVQMIFQDpFaSLN 373
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKLRRKVGMVFQQ-F-NLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMTGPL-VQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALD 452
Cdd:COG1126 90 PHLTVLENVTLAPIkVKKMSKAEAEERAMELLERVGLADKA-DAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 453 -ALIQvQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELL 521
Cdd:COG1126 169 pELVG-EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFL 236
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
273-508 |
4.90e-59 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 195.66 E-value: 4.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSRsgwwgrrtTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEG 352
Cdd:COG3638 2 MLELRNLSKRYPGG--------TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 353 RLRALRSDVQMIFQDPfaSLNPRQTVGQIVMTG-----PLVQGV----SKADAERrARELLGLVGLPAAAFERfPHEFSG 423
Cdd:COG3638 74 ALRRLRRRIGMIFQQF--NLVPRLSVLTNVLAGrlgrtSTWRSLlglfPPEDRER-ALEALERVGLADKAYQR-ADQLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 424 GQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:COG3638 150 GQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDG 229
|
....*
gi 1331382268 504 ETAAL 508
Cdd:COG3638 230 PPAEL 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
295-519 |
4.94e-59 |
|
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: 196.33 E-value: 4.94e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRS-DVQMIFQDpFAsLN 373
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQS-FA-LL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWE-HKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRE 519
Cdd:cd03294 194 LIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVRE 259
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-256 |
5.02e-59 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 196.07 E-value: 5.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVESGRLvfrdedLADRSEEAMRQLRGRDISMVFQEPMSALNP 104
Cdd:PRK10418 21 GVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRQTAGRV------LLDGKPVAPCALRGRKIATIMQNPRSAFNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVGEQIDETLRAHGVAAarvRRQRVVDLLGYVGLPDPERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSAL 184
Cdd:PRK10418 95 LHTMHTHARETCLALGKPA---DDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 185 DVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAA 256
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
296-523 |
5.53e-59 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 198.43 E-value: 5.53e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLL----RADSGRIEWLGREVAGLSEGRLRAL-RSDVQMIFQDPFA 370
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLvGAEVAMIFQDPMT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SLNPRQTVG-QIVMTGPLVQGVSKADAERRARELLGLVGLPAAA--FERFPHEFSGGQRQRIGIARALAVEPKVLIADEC 447
Cdd:PRK11022 101 SLNPCYTVGfQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 448 VSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMA 523
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRA 256
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
274-502 |
3.16e-58 |
|
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: 192.69 E-value: 3.16e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFCSRSGwwgrrTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegr 353
Cdd:cd03293 1 LEVRNVSKTYGGGGG-----AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 lralrSDVQMIFQDPfaSLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIAR 433
Cdd:cd03293 73 -----PDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFE-NAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 434 ALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVM--RKGRVVEQ 502
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-257 |
4.96e-58 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 195.79 E-value: 4.96e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVESGRLVFRDEDLADRSE 80
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 EAMRQLRGRDISMVFQEPMSALNPLMRVGEQIDE-----TLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPFELS 155
Cdd:PRK15093 81 RERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQnipgwTYKGRWWQRFGWRKRRAIELLHRVGIKDHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQ 235
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVET 240
|
250 260
....*....|....*....|..
gi 1331382268 236 GTAPAVLRVPREDYTRQLLAAV 257
Cdd:PRK15093 241 APSKELVTTPHHPYTQALIRAI 262
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-511 |
5.95e-58 |
|
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: 201.18 E-value: 5.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLpDPLKVESGRLVFR------------------------------ 71
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGM-DQYEPTSGRIIYHvalcekcgyverpskvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 72 DEDLADRSEEAMRQLRGRdISMVFQEPMsALNPLMRVGEQIDETLRAHGVAAARVRrQRVVDLLGYVGLpdpERLRLAYP 151
Cdd:TIGR03269 93 EVDFWNLSDKLRRRIRKR-IAIMLQRTF-ALYGDDTVLDNVLEALEEIGYEGKEAV-GRAVDLIEMVQL---SHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 152 FELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGR 231
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 232 VVEQGTAPAVLRVpredytrqLLAAVSAQPLVPRTQVAGPvVLKAEALGKVFCSRSgwwgRRTTQALDAVQLQLREGETL 311
Cdd:TIGR03269 247 IKEEGTPDEVVAV--------FMEGVSEVEKECEVEVGEP-IIKVRNVSKRYISVD----RGVVKAVDNVSLEVKEGEIF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 312 GIVGESGSGKSTLGRCLVRLLRADSGRIEW-LGREVAGLSE----GRLRALRSdVQMIFQDpfASLNPRQTVgqivmTGP 386
Cdd:TIGR03269 314 GIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTKpgpdGRGRAKRY-IGILHQE--YDLYPHRTV-----LDN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 387 LVQGVS----KADAERRARELLGLVGL----PAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQ 458
Cdd:TIGR03269 386 LTEAIGlelpDELARMKAVITLKMVGFdeekAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVD 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 459 ILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:TIGR03269 466 VTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-235 |
5.94e-57 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 189.48 E-value: 5.94e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKS----MLAkALLRqlPDplkveSGRLVFRDEDLAD 77
Cdd:COG1136 3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKStllnILG-GLDR--PT-----SGEVLIDGQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 78 RSEEAMRQLRGRDISMVFQEPmsALNPLMRVGEQIDETLRAHGVAAaRVRRQRVVDLLGYVGLPDpeRLRlAYPFELSGG 157
Cdd:COG1136 75 LSERELARLRRRHIGFVFQFF--NLLPELTALENVALPLLLAGVSR-KERRERARELLERVGLGD--RLD-HRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 158 QRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfAVVEAIADRVLVLEKGRVVEQ 235
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
294-518 |
1.29e-56 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 192.62 E-value: 1.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRlralRsDVQMIFQDpFAsLN 373
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK----R-NVGMVFQD-YA-LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:COG3842 90 PHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLA-DRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFadaRHPYTR 518
Cdd:COG3842 169 KLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIY---ERPATR 230
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-246 |
3.51e-56 |
|
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: 187.79 E-value: 3.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKAL-LRQLPDplkveSGRLVFRDEDLADRSEE 81
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCInGLERPT-----SGSVLVDGTDLTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRgRDISMVFQEpmsaLNPLMR--VGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPDPERlrlAYPFELSGGQR 159
Cdd:cd03258 76 ELRKAR-RRIGMIFQH----FNLLSSrtVFENVALPLEIAGVPKAE-IEERVLELLELVGLEDKAD---AYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 160 QRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAP 239
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
....*..
gi 1331382268 240 AVLRVPR 246
Cdd:cd03258 227 EVFANPQ 233
|
|
| PhnK |
COG4107 |
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and ... |
273-520 |
8.21e-56 |
|
ABC-type phosphonate transport system, ATPase component PhnK [Inorganic ion transport and metabolism];
Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 187.71 E-value: 8.21e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSrsgwwGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGRE-----VA 347
Cdd:COG4107 8 LLSVRGLSKRYGP-----GCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYRDRDggprdLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 348 GLSEGRLRAL-RSDVQMIFQDPFASLNPRQTVGQIVMTGPLVQGVSK-ADAERRARELLGLVGLPAAAFERFPHEFSGGQ 425
Cdd:COG4107 83 ALSEAERRRLrRTDWGMVYQNPRDGLRMDVSAGGNIAERLMAAGERHyGDIRARALEWLERVEIPLERIDDLPRTFSGGM 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 426 RQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGET 505
Cdd:COG4107 163 QQRVQIARALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGLT 242
|
250
....*....|....*
gi 1331382268 506 AALFADARHPYTREL 520
Cdd:COG4107 243 DQVLEDPQHPYTQLL 257
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
295-503 |
2.88e-55 |
|
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: 184.65 E-value: 2.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrlrALRSDVQMIFQDPfaSLNP 374
Cdd:cd03259 13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-----PERRNIGMVFQDY--ALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:cd03259 86 HLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLL-NRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 455 IQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03259 165 LREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
291-524 |
6.09e-55 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 193.00 E-value: 6.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRAD-----SGRIEWLGREVAGLSEGRLRALRSD-VQMI 364
Cdd:PRK15134 18 QQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVRGNkIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 365 FQDPFASLNPRQTV-GQIVMTGPLVQGVSKADAERRARELLGLVGLPAAA--FERFPHEFSGGQRQRIGIARALAVEPKV 441
Cdd:PRK15134 98 FQEPMVSLNPLHTLeKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAkrLTDYPHQLSGGERQRVMIAMALLTRPEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 442 LIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELL 521
Cdd:PRK15134 178 LIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
...
gi 1331382268 522 MAE 524
Cdd:PRK15134 258 NSE 260
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
294-518 |
1.15e-54 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 187.66 E-value: 1.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGlsegRLRALRSDVQMIFQDPfaSLN 373
Cdd:COG1118 14 SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLPPRERRVGFVFQHY--ALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:COG1118 88 PHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLA-DRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFadaRHPYTR 518
Cdd:COG1118 167 KVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVY---DRPATP 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
295-514 |
1.23e-54 |
|
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: 183.92 E-value: 1.23e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDPfaSLNP 374
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRRQIGMIFQQF--NLIE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTG---------PLVQGVSKADAERrARELLGLVGLPAAAFERfPHEFSGGQRQRIGIARALAVEPKVLIAD 445
Cdd:cd03256 92 RLSVLENVLSGrlgrrstwrSLFGLFPKEEKQR-ALAALERVGLLDKAYQR-ADQLSGGQQQRVAIARALMQQPKLILAD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 446 ECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARH 514
Cdd:cd03256 170 EPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLD 238
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
297-521 |
2.95e-54 |
|
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: 182.89 E-value: 2.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRalRSDVQMIFQdpfASLNPRQ 376
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR--RKIGYVIQQ---IGLFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAF-ERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALI 455
Cdd:cd03295 91 TVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFaDRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPIT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 456 QVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELL 521
Cdd:cd03295 171 RDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-526 |
4.13e-54 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 189.84 E-value: 4.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKAL---LRqlPDplkveSGRLVFRDEDLADRS-EEAMRQlrGrdISMVFQ 96
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILsgvYQ--PD-----SGEILLDGEPVRFRSpRDAQAA--G--IAIIHQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 97 EPmsALNPLMRVGEQI---DETLRAHGVAAARVRRqRVVDLLGYVGLP-DPERlRLAypfELSGGQRQRVVIAMALAFDP 172
Cdd:COG1129 87 EL--NLVPNLSVAENIflgREPRRGGLIDWRAMRR-RARELLARLGLDiDPDT-PVG---DLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 173 ALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGtapavlrvPREDYTRQ 252
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG--------PVAELTED 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 253 LLAA-----VSAQPLVPRTQVAGPVVLKAEALgkvfcSRSGwwgrrttqALDAVQLQLREGETLGIVGESGSGKSTLGRC 327
Cdd:COG1129 231 ELVRlmvgrELEDLFPKRAAAPGEVVLEVEGL-----SVGG--------VVRDVSFSVRAGEILGIAGLVGAGRTELARA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 328 LVRLLRADSGRIEWLGREV----------AG---LSEGRLRalrsdvQMIFQDpfaslnprQTVGQ-IVMT--GPLVQG- 390
Cdd:COG1129 298 LFGADPADSGEIRLDGKPVrirsprdairAGiayVPEDRKG------EGLVLD--------LSIREnITLAslDRLSRGg 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 391 -VSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADEC-----VSAldaliQVQILELLE 464
Cdd:COG1129 364 lLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPtrgidVGA-----KAEIYRLIR 438
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 465 SLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALfadarhpyTRELLMAEAI 526
Cdd:COG1129 439 ELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA--------TEEAIMAAAT 491
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-267 |
6.70e-54 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 192.38 E-value: 6.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEEAMRQLRgRDISMVFQEPMS 100
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV----ESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDPYA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRlaYPFELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:PRK10261 413 SLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWR--YPHEFSGGQRQRICIARALALNPKVIIADEA 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAAVS-A 259
Cdd:PRK10261 491 VSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPvA 570
|
....*...
gi 1331382268 260 QPLVPRTQ 267
Cdd:PRK10261 571 DPSRQRPQ 578
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-232 |
2.17e-53 |
|
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: 179.99 E-value: 2.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAM 83
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKS----TLLNILGGLDRPTSGEVRVDGTDISKLSEKEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 RQLRGRDISMVFQEPmsALNPLMRVGEQIDETLRAHGVAAaRVRRQRVVDLLGYVGLPDpeRLRlAYPFELSGGQRQRVV 163
Cdd:cd03255 77 AAFRRRHIGFVFQSF--NLLPDLTALENVELPLLLAGVPK-KERRERAEELLERVGLGD--RLN-HYPSELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 164 IAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEaIADRVLVLEKGRV 232
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
298-519 |
4.23e-53 |
|
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: 179.62 E-value: 4.23e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDP--FASLnpr 375
Cdd:cd03261 16 LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSGalFDSL--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 qTVGQIVMTgPLVQ--GVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:cd03261 93 -TVFENVAF-PLREhtRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADArHPYTRE 519
Cdd:cd03261 170 IASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQ 234
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
290-498 |
1.54e-52 |
|
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: 177.27 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 290 WGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPF 369
Cdd:cd03225 9 YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKVGLVFQNPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASL-NPrqTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECV 448
Cdd:cd03225 86 DQFfGP--TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLR-DRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 449 SALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGR 498
Cdd:cd03225 163 AGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
294-521 |
9.14e-52 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 179.33 E-value: 9.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLL------RADsgRIEWLGREVAGLS-EGRLRALRSDVQMIFQ 366
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITkdnwhvTAD--RFRWNGIDLLKLSpRERRKIIGREIAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 367 DPFASLNPRQTVG-QIV-------MTGPLVQgvSKADAERRARELLGLVGL--PAAAFERFPHEFSGGQRQRIGIARALA 436
Cdd:COG4170 97 EPSSCLDPSAKIGdQLIeaipswtFKGKWWQ--RFKWRKKRAIELLHRVGIkdHKDIMNSYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 437 VEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPY 516
Cdd:COG4170 175 NQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPY 254
|
....*
gi 1331382268 517 TRELL 521
Cdd:COG4170 255 TKALL 259
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-523 |
1.27e-51 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 183.30 E-value: 1.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKAL--LRQlPDplkveSGRLVFRDEDLADRS-EEAMRqlRGrdISMVFQE 97
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILygLYQ-PD-----SGEILIDGKPVRIRSpRDAIA--LG--IGMVHQH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 PMsaLNPLMRVGEQI---DETLRAHGVAAARVRRqRVVDLLGYVGLP-DPErlrlAYPFELSGGQRQRVVIAMALAFDPA 173
Cdd:COG3845 89 FM--LVPNLTVAENIvlgLEPTKGGRLDRKAARA-RIRELSERYGLDvDPD----AKVEDLSVGEQQRVEILKALYRGAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 174 LLIADEPTSALdvtTQAQILDLLRKIQQ--DKGMALLFITHDFAVVEAIADRVLVLEKGRVVeqGTapavlrVPREDYTR 251
Cdd:COG3845 162 ILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTVLRRGKVV--GT------VDTAETSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 252 QLLAAV----SAQPLVPRTQVA-GPVVLKAEALGkvfcsrsgWWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGR 326
Cdd:COG3845 231 EELAELmvgrEVLLRVEKAPAEpGEVVLEVENLS--------VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 327 CLVRLLRADSGRIEWLGREVAGLSEGRLRALRsdVQMIFQDPFAS-LNPRQTVGQ-IVMT----GPLVQG--VSKADAER 398
Cdd:COG3845 303 ALAGLRPPASGSIRLDGEDITGLSPRERRRLG--VAYIPEDRLGRgLVPDMSVAEnLILGryrrPPFSRGgfLDRKAIRA 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 399 RARELL-------GLVGLPAAAferfpheFSGGQRQRIGIARALAVEPKVLIADECVSALD----ALIQVQILELleslq 467
Cdd:COG3845 381 FAEELIeefdvrtPGPDTPARS-------LSGGNQQKVILARELSRDPKLLIAAQPTRGLDvgaiEFIHQRLLEL----- 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 468 RRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVeqGETAAlfADArhpyTRE---LLMA 523
Cdd:COG3845 449 RDAGAAVLLISEDLDEILALSDRIAVMYEGRIV--GEVPA--AEA----TREeigLLMA 499
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-270 |
1.57e-51 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 176.80 E-value: 1.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHL-----RIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDL 75
Cdd:PRK10419 1 MTLLNVSGLshhyaHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLAR-LLVGLESP---SQGNVSWRGEPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 76 ADRSEEAMRQLRgRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLayPFELS 155
Cdd:PRK10419 77 AKLNRAQRKAFR-RDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKR--PPQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQ 235
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVET 233
|
250 260 270
....*....|....*....|....*....|....*
gi 1331382268 236 GTAPAVLRVpREDYTRQLLAAVsaQPLVPRTQVAG 270
Cdd:PRK10419 234 QPVGDKLTF-SSPAGRVLQNAV--LPAFPVRRRTT 265
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
296-498 |
7.97e-51 |
|
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: 171.60 E-value: 7.97e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLsEGRLRALRSDVQMIFQDPfaSLNPR 375
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLRRRIGMVFQDF--ALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 QTVGQIVMtgplvqgvskadaerrarelLGLvglpaaaferfphefSGGQRQRIGIARALAVEPKVLIADECVSALDALI 455
Cdd:cd03229 91 LTVLENIA--------------------LGL---------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPIT 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1331382268 456 QVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGR 498
Cdd:cd03229 136 RREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-257 |
8.21e-51 |
|
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: 174.61 E-value: 8.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHL----RIALPAGA-DRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLrQLPDPlkvESGRLVFRDEDLA 76
Cdd:TIGR02769 1 SLLEVRDVthtyRTGGLFGAkQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLL-GLEKP---AQGTVSFRGQDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 77 DRSEEAMRQLRgRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRlaYPFELSG 156
Cdd:TIGR02769 77 QLDRKQRRAFR-RDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADK--LPRQLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 157 GQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQg 236
Cdd:TIGR02769 154 GQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE- 232
|
250 260
....*....|....*....|.
gi 1331382268 237 TAPAVLRVPREDYTRQLLAAV 257
Cdd:TIGR02769 233 CDVAQLLSFKHPAGRNLQSAV 253
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-243 |
1.57e-50 |
|
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: 172.52 E-value: 1.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKAL--LrqlpdpLKVESGRLVFRDEDLadrSEE 81
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngL------LKPTSGEVLVDGKDI---TKK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRgRDISMVFQEPMSAL-NPlmRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLpdpERLRLAYPFELSGGQRQ 160
Cdd:COG1122 69 NLRELR-RKVGLVFQNPDDQLfAP--TVEEDVAFGPENLGLPREEIRE-RVEEALELVGL---EHLADRPPHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 161 RVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPA 240
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
...
gi 1331382268 241 VLR 243
Cdd:COG1122 221 VFS 223
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
295-508 |
1.94e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.56 E-value: 1.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrlRALRSDVQMIFQDPfaSLNP 374
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDP----AEVRRRIGYVPQEP--ALYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIV-MTGPLvQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:COG1131 87 DLTVRENLrFFARL-YGLPRKEARERIDELLELFGLTDAA-DRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 454 LIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:COG1131 165 EARRELWELLRELAAEGK-TVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-243 |
2.10e-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: 172.86 E-value: 2.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEEA 82
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLL----RPDSGEILVDGQDITGLSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLRgRDISMVFQEpmSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLrlaYPFELSGGQRQRV 162
Cdd:COG1127 77 LYELR-RRIGMLFQG--GALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADK---MPSELSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVL 242
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
.
gi 1331382268 243 R 243
Cdd:COG1127 231 A 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
273-521 |
2.18e-50 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 173.82 E-value: 2.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSRSGWWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREvagLSEG 352
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHP---LHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 353 RLRALRSDVQMIFQDPFASLNPRQTVGQIvMTGPLV--QGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIG 430
Cdd:PRK15112 81 DYSYRSQRIRMIFQDPSTSLNPRQRISQI-LDFPLRlnTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 431 IARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250
....*....|.
gi 1331382268 511 DARHPYTRELL 521
Cdd:PRK15112 240 SPLHELTKRLI 250
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
290-509 |
6.57e-50 |
|
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: 171.77 E-value: 6.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 290 WGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSdvqMIFQDPF 369
Cdd:COG1120 9 VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA---YVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASLNprQTVGQIVMTG-----PLVQGVSKADaERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIA 444
Cdd:COG1120 86 APFG--LTVRELVALGryphlGLFGRPSAED-REAVEEALERTGLEHLA-DRPVDELSGGERQRVLIARALAQEPPLLLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 445 DECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALF 509
Cdd:COG1120 162 DEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
14-262 |
1.43e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 173.83 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 14 PAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMRQLRgRDISM 93
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIR-CINLLERP---TSGRVLVDGQDLTALSEKELRKAR-RQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 94 VFQEpmsaLNPLMR--VGEQIDETLRAHGVAAARVRrQRVVDLLGYVGLPDperLRLAYPFELSGGQRQRVVIAMALAFD 171
Cdd:PRK11153 87 IFQH----FNLLSSrtVFDNVALPLELAGTPKAEIK-ARVTELLELVGLSD---KADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTR 251
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTR 238
|
250
....*....|.
gi 1331382268 252 QLLAAVSAQPL 262
Cdd:PRK11153 239 EFIQSTLHLDL 249
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
21-243 |
5.33e-48 |
|
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: 166.14 E-value: 5.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDplkveSGRLVFRDEDLADRSEEAMRQLRgRDISMVFQEpm 99
Cdd:cd03261 14 TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrPD-----SGEVLIDGEDISGLSEAELYRLR-RRMGMLFQS-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 SALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLrlaYPFELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:cd03261 86 GALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDL---YPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLR 243
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-234 |
8.78e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 166.42 E-value: 8.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRse 80
Cdd:COG1116 5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS----TLLRLIAGLEKPTSGEVLVDGKPVTGP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 eamrqlrGRDISMVFQEPmsALNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPDPERlrlAYPFELSGGQRQ 160
Cdd:COG1116 79 -------GPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGLAGFED---AYPHQLSGGMRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 161 RVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfaVVEAI--ADRVLVLEK--GRVVE 234
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD--VDEAVflADRVVVLSArpGRIVE 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-246 |
5.23e-47 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 167.20 E-value: 5.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKAL--LrqlpdpLKVESGRLVFRDEDLADR 78
Cdd:COG3842 3 MPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIagF------ETPDSGRILLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 79 SEEAmrqlrgRDISMVFQEPmsALNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPDperLRLAYPFELSGGQ 158
Cdd:COG3842 73 PPEK------RNVGMVFQDY--ALFPHLTVAENVAFGLRMRGVPKAE-IRARVAELLELVGLEG---LADRYPHQLSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 159 RQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAvvEA--IADRVLVLEKGRVVEQG 236
Cdd:COG3842 141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE--EAlaLADRIAVMNDGRIEQVG 218
|
250
....*....|
gi 1331382268 237 TAPAVLRVPR 246
Cdd:COG3842 219 TPEEIYERPA 228
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
22-240 |
5.37e-47 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 162.91 E-value: 5.37e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEEAMRQLRgRDISMVFQEpmSA 101
Cdd:COG2884 17 ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEE----RPTSGQVLVNGQDLSRLKRREIPYLR-RRIGVVFQD--FR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLIADEPT 181
Cdd:COG2884 90 LLPDRTVYENVALPLRVTGKSRKEIRR-RVREVLDLVGLSDKAK---ALPHELSGGEQQRVAIARALVNRPELLLADEPT 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 182 SALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPA 240
Cdd:COG2884 166 GNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
21-257 |
5.41e-47 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 163.63 E-value: 5.41e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSmlakALLR---QLPDPlkvESGRLVFRDEDLADrSEEAMRQLRgRDISMVFQE 97
Cdd:COG1126 15 EVLKGISLDVEKGEVVVIIGPSGSGKS----TLLRcinLLEEP---DSGTITVDGEDLTD-SKKDINKLR-RKVGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 ----P-MSAL-N---PLMRVgeqidetlraHGVAAARVRrQRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMAL 168
Cdd:COG1126 86 fnlfPhLTVLeNvtlAPIKV----------KKMSKAEAE-ERAMELLERVGLADKAD---AYPAQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 169 AFDPALLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHD--FAvvEAIADRVLVLEKGRVVEQGTAPAVLRVPR 246
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEmgFA--REVADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
250
....*....|.
gi 1331382268 247 EDYTRQLLAAV 257
Cdd:COG1126 229 HERTRAFLSKV 239
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-231 |
6.07e-47 |
|
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: 162.64 E-value: 6.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 5 SVEHLRIALPAGAdrSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSeeaMR 84
Cdd:cd03225 1 ELKNLSFSYPDGA--RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLL----GPTSGEVLVDGKDLTKLS---LK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 85 QLRGRdISMVFQEPMSAL-NPlmRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLPDperLRLAYPFELSGGQRQRVV 163
Cdd:cd03225 72 ELRRK-VGLVFQNPDDQFfGP--TVEEEVAFGLENLGLPEEEIEE-RVEEALELVGLEG---LRDRSPFTLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 164 IAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGR 231
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
297-512 |
6.69e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 165.19 E-value: 6.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwLGREV--AGLSEGRLRALRSDVQMIFQDPFASLNp 374
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT-IGERVitAGKKNKKLKPLRKKVGIVFQFPEHQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:PRK13634 100 EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 455 IQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADA 512
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
296-521 |
4.76e-46 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 161.46 E-value: 4.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRI-----EWLGREVAGLSEGRLRALRSDVQMIFQDpfA 370
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLIRQLRQHVGFVFQN--F 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SLNPRQTVGQIVMTGPL-VQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK11264 95 NLFPHRTVLENIIEGPViVKGEPKEEATARARELLAKVGL-AGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 450 ALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELL 521
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
274-520 |
6.67e-46 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 161.25 E-value: 6.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVfcsrsgwWGRRttQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGR-----EVAG 348
Cdd:PRK11701 7 LSVRGLTKL-------YGPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 349 LSEGRLRAL-RSDVQMIFQDPFASLNPRQTVGQIVMTGPLVQGVSK-ADAERRARELLGLVGLPAAAFERFPHEFSGGQR 426
Cdd:PRK11701 78 LSEAERRRLlRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHyGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 427 QRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETA 506
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTD 237
|
250
....*....|....
gi 1331382268 507 ALFADARHPYTREL 520
Cdd:PRK11701 238 QVLDDPQHPYTQLL 251
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
295-504 |
6.95e-46 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 160.22 E-value: 6.95e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDpFaSLNP 374
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD-F-RLLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTgPL-VQGVSKADAERRARELLGLVGLPAAAFeRFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:COG2884 93 DRTVYENVAL-PLrVTGKSRKEIRRRVREVLDLVGLSDKAK-ALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 454 LIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGE 504
Cdd:COG2884 171 ETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
295-526 |
1.07e-45 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 163.87 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRAL-RSDVQMIFQDpFAsLN 373
Cdd:TIGR01186 6 KKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVrRKKIGMVFQQ-FA-LF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:TIGR01186 84 PHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYE-HRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDP 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMAEAI 526
Cdd:TIGR01186 163 LIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDL 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
296-499 |
1.49e-45 |
|
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: 158.85 E-value: 1.49e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaGLSEGRLRALRSDVQMIFQDpFaSLNPR 375
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELRQKVGMVFQQ-F-NLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 QTVGQIVMTGPL-VQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:cd03262 91 LTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKA-DAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1331382268 455 IQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRV 499
Cdd:cd03262 170 LVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-235 |
2.92e-45 |
|
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: 158.40 E-value: 2.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRseeam 83
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKS----TLLRIIAGLERPTSGEVLVDGEPVTGP----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 rqlrGRDISMVFQEPmsALNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVV 163
Cdd:cd03293 72 ----GPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAE-ARERAEELLELVGLSGFEN---AYPHQLSGGMRQRVA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 164 IAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfaVVEAI--ADRVLVLEK--GRVVEQ 235
Cdd:cd03293 142 LARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD--IDEAVflADRVVVLSArpGRIVAE 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
294-521 |
4.50e-45 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 158.72 E-value: 4.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGlSEGRLRALRSDVQMIFQDpFaSLN 373
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVND-PKVDERLIRQEAGMVFQQ-F-YLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMTGPL-VQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALD 452
Cdd:PRK09493 90 PHLTALENVMFGPLrVRGASKEEAEKQARELLAKVGLAERA-HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 453 ALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELL 521
Cdd:PRK09493 169 PELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-256 |
1.90e-44 |
|
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: 157.08 E-value: 1.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDplkveSGRLVFRDEDLADRSEEAMRqlrgRDISMVFQ 96
Cdd:cd03295 12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIePT-----SGEIFIDGEDIREQDPVELR----RKIGYVIQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 97 EpmSALNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPdPERLRLAYPFELSGGQRQRVVIAMALAFDPALLI 176
Cdd:cd03295 83 Q--IGLFPHMTVEENIALVPKLLKWPKEK-IRERADELLALVGLD-PAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 177 ADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfaVVEAI--ADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLL 254
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHD--IDEAFrlADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
..
gi 1331382268 255 AA 256
Cdd:cd03295 237 GA 238
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
21-243 |
2.56e-44 |
|
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: 157.61 E-value: 2.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLpdpLKVESGRLVFRDEDLADRSEEAMRQLRgRDISMVFQEPMS 100
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQ-HLNGL---LKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQFPEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALnplmrvgeqIDET--------LRAHGVAAARVRrQRVVDLLGYVGLPdpERLRLAYPFELSGGQRQRVVIAMALAFDP 172
Cdd:TIGR04521 94 QL---------FEETvykdiafgPKNLGLSEEEAE-ERVKEALELVGLD--EEYLERSPFELSGGQMRRVAIAGVLAMEP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 173 ALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLR 243
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
295-515 |
4.11e-44 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 159.47 E-value: 4.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRlralRsDVQMIFQDpFAsLNP 374
Cdd:COG3839 16 VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD----R-NIAMVFQS-YA-LYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:COG3839 89 HMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLL-DRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 455 IQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFadaRHP 515
Cdd:COG3839 168 LRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELY---DRP 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
296-508 |
6.78e-44 |
|
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: 155.03 E-value: 6.78e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLL-----RADSGRIEWLGREVAGLSEGRLrALRSDVQMIFQDPfa 370
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVL-ELRRRVGMVFQKP-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 slNP-RQTVGQIVMTGPLVQGV-SKADAERRARELLGLVGLPAAAFER-FPHEFSGGQRQRIGIARALAVEPKVLIADEC 447
Cdd:cd03260 91 --NPfPGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 448 VSALDALIQVQILELLESLQRrfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:cd03260 169 TSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
273-507 |
7.47e-44 |
|
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: 154.90 E-value: 7.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSRSGwwgrrTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSE- 351
Cdd:COG4181 8 IIELRGLTKTVGTGAG-----ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 352 GRLRALRSDVQMIFQDpFaSLNPRQTVGQIVMTgPLvQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGI 431
Cdd:COG4181 83 ARARLRARHVGFVFQS-F-QLLPTLTALENVML-PL-ELAGRRDARARARALLERVGL-GHRLDHYPAQLSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 432 ARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAA 507
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
22-257 |
1.10e-43 |
|
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: 155.88 E-value: 1.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAMRQLRGRDISMVFQEpmSA 101
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKS----TLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQS--FA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQIDETLRAHGVAAArVRRQRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLIADEPT 181
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRA-EREERAAEALELVGLEGWEH---KYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 182 SALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAAV 257
Cdd:cd03294 189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
21-236 |
1.95e-43 |
|
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: 153.44 E-value: 1.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAmrqlrgRDISMVFQEPms 100
Cdd:cd03259 14 RALDDLSLTVEPGEFLALLGPSGCGKT----TLLRLIAGLERPDSGEILIDGRDVTGVPPER------RNIGMVFQDY-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPLMRVGEQIDETLRAHGVAAArVRRQRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:cd03259 82 ALFPHLTVAENIAFGLKLRGVPKA-EIRARVRELLELVGLEGLLN---RYPHELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03259 158 LSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
21-243 |
2.22e-43 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.68 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDplkveSGRLVFRDEDLADRSEEAMRQlrgrdISMVFQEPm 99
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLrPT-----SGEVRVLGEDVARDPAEVRRR-----IGYVPQEP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 sALNPLMRVGEQIDETLRAHGVAAaRVRRQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:COG1131 83 -ALYPDLTVRENLRFFARLYGLPR-KEARERIDELLELFGLTDAADRKVG---TLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 180 PTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLR 243
Cdd:COG1131 158 PTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-257 |
2.93e-43 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 154.31 E-value: 2.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGadrsHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDE-----DLAD 77
Cdd:PRK11701 6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLA----PDAGEVHYRMRdgqlrDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 78 RSEEAMRQLRGRDISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLpDPERLRLAyPFELSGG 157
Cdd:PRK11701 78 LSEAERRRLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEI-DAARIDDL-PTTFSGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 158 QRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGT 237
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGL 235
|
250 260
....*....|....*....|
gi 1331382268 238 APAVLRVPREDYTRQLLAAV 257
Cdd:PRK11701 236 TDQVLDDPQHPYTQLLVSSV 255
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
295-503 |
4.55e-43 |
|
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: 152.78 E-value: 4.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrlrALRSDVQMIFQDpFAsLNP 374
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLP-----PHKRPVNTVFQN-YA-LFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:cd03300 86 HLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYA-NRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 455 IQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03300 165 LRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
294-511 |
4.85e-43 |
|
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: 154.13 E-value: 4.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVagLSEGRLRALRSDVQMIFQDPfasln 373
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEIRKKVGMVFQNP----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMT----GPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:TIGR04520 87 DNQFVGATVEDdvafGLENLGVPREEMRKRVDEALKLVGMEDFR-DREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 450 ALDALIQVQILELLESLQRRFRLSIVFITHDLRVAArLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:TIGR04520 166 MLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-240 |
1.98e-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: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKS---MLAKALLRqlPDplkveSGRLVFRDEDLADR 78
Cdd:COG4181 7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKStllGLLAGLDR--PT-----SGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 79 SEEAMRQLRGRDISMVFQE----P-MSAL-N---PLmrvgeqideTLRAHGVAAARVRRqrvvdLLGYVGLPdpERLRlA 149
Cdd:COG4181 80 DEDARARLRARHVGFVFQSfqllPtLTALeNvmlPL---------ELAGRRDARARARA-----LLERVGLG--HRLD-H 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 150 YPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfavvEAIA---DRVLV 226
Cdd:COG4181 143 YPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHD----PALAarcDRVLR 218
|
250
....*....|....
gi 1331382268 227 LEKGRVVEQGTAPA 240
Cdd:COG4181 219 LRAGRLVEDTAATA 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
290-519 |
6.69e-42 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 150.16 E-value: 6.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 290 WGrrTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREV---AGLSEGRLRALRSDVQMIFQ 366
Cdd:COG4161 12 YG--SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 367 DpfASLNPRQTVGQIVMTGPL-VQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIAD 445
Cdd:COG4161 90 Q--YNLWPHLTVMENLIEAPCkVLGLSKEQAREKAMKLLARLRLTDKA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 446 ECVSALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGeTAALFAdarHPYTRE 519
Cdd:COG4161 167 EPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQG-DASHFT---QPQTEA 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
21-236 |
7.46e-42 |
|
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: 149.64 E-value: 7.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKAL--LRQLPDPLKVEsGRLVFRDEDLADRSEEAMRqLRgRDISMVFQEP 98
Cdd:cd03260 14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrLNDLIPGAPDE-GEVLLDGKDIYDLDVDVLE-LR-RRVGMVFQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 msalNPL-MRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAyPFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:cd03260 91 ----NPFpGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLH-ALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIQQDkgMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
294-519 |
1.14e-41 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 149.39 E-value: 1.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREV---AGLSEGRLRALRSDVQMIFQDpfA 370
Cdd:PRK11124 14 AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIRELRRNVGMVFQQ--Y 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SLNPRQTVGQIVMTGPL-VQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK11124 92 NLWPHLTVQQNLIEAPCrVLGLSKDQALARAEKLLERLRLKPYA-DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 450 ALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGeTAALFAdarHPYTRE 519
Cdd:PRK11124 171 ALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQG-DASCFT---QPQTEA 235
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
17-314 |
1.67e-41 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 151.01 E-value: 1.67e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 17 ADRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLR---QLPDPlkvESGRLVFRDEDLADRSEEAMRqlrgRDISM 93
Cdd:COG1125 12 PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKT----TTLRminRLIEP---TSGRILIDGEDIRDLDPVELR----RRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 94 VFQEpmSALNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLpDPERLRLAYPFELSGGQRQRVVIAMALAFDPA 173
Cdd:COG1125 81 VIQQ--IGLFPHMTVAENIATVPRLLGWDKER-IRARVDELLELVGL-DPEEYRDRYPHELSGGQQQRVGVARALAADPP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 174 LLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAvvEAI--ADRVLVLEKGRVVEQGTAPAVLRVPREDYTR 251
Cdd:COG1125 157 ILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDID--EALklGDRIAVMREGRIVQYDTPEEILANPANDFVA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 252 QLLAAVSAQPLVPRTQVAG-----PVVLKAEALGKVFCSRSGWWGRRTTQALDAvqlqlrEGETLGIV 314
Cdd:COG1125 235 DFVGADRGLRRLSLLRVEDlmlpePPTVSPDASLREALSLMLERGVDWLLVVDE------DGRPLGWL 296
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-232 |
1.76e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.04 E-value: 1.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIAlpagADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDladRSEEAM 83
Cdd:COG4619 1 LELEGLSFR----VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP----PTSGEIYLDGKP---LSAMPP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 RQLRgRDISMVFQEPmsALnPLMRVGEQIDETLRAHGvaaARVRRQRVVDLLGYVGLPDperLRLAYPF-ELSGGQRQRV 162
Cdd:COG4619 70 PEWR-RQVAYVPQEP--AL-WGGTVRDNLPFPFQLRE---RKFDRERALELLERLGLPP---DILDKPVeRLSGGERQRL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRV 232
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
296-502 |
1.98e-41 |
|
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: 148.64 E-value: 1.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrlrALRSDVQMIFQDpfASLNPR 375
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-----VQERNVGFVFQH--YALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 QTVGQIVMTG----PLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSAL 451
Cdd:cd03296 89 MTVFDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLA-DRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 452 DALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRvVEQ 502
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGR-IEQ 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-257 |
5.11e-41 |
|
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: 148.27 E-value: 5.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIalpaGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdPLkveSGRLVFRDEDLADRSeea 82
Cdd:COG1120 1 MLEAENLSV----GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLK-PS---SGEVLLDGRDLASLS--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 mRQLRGRDISMVFQEPMSALNplMRVGEQIDETLRAHGVAAARVR---RQRVVDLLGYVGLpdpERLRLAYPFELSGGQR 159
Cdd:COG1120 70 -RRELARRIAYVPQEPPAPFG--LTVRELVALGRYPHLGLFGRPSaedREAVEEALERTGL---EHLADRPVDELSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 160 QRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAP 239
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
250
....*....|....*...
gi 1331382268 240 AVLrvpredyTRQLLAAV 257
Cdd:COG1120 224 EVL-------TPELLEEV 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
291-502 |
2.64e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 146.55 E-value: 2.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRlralrsdvQMIFQDpfA 370
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--------GVVFQK--D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSA 450
Cdd:COG4525 86 ALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFA-RRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 451 LDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVM--RKGRVVEQ 502
Cdd:COG4525 165 LDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVER 218
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
296-508 |
2.85e-40 |
|
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: 145.77 E-value: 2.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGlsegRLRALRSDVQMIFQDPFasLNPR 375
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK----EPREARRQIGVLPDERG--LYDR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 QTV-GQIVMTGPLvQGVSKADAERRARELLGLVGLPAAAFERFpHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:COG4555 89 LTVrENIRYFAEL-YGLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 455 IQVQILELLESLqRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:COG4555 167 ARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-247 |
3.77e-40 |
|
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: 146.04 E-value: 3.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLpdpLKVESGRLVFRDEDLADrsEEAMRQLRgRDISMVFQEPMSA 101
Cdd:TIGR04520 17 ALKNVSLSIEKGEFVAIIGHNGSGKSTLAK-LLNGL---LLPTSGKVTVDGLDTLD--EENLWEIR-KKVGMVFQNPDNQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LnplmrVGEQIDET----LRAHGVAAARVRRqRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:TIGR04520 90 F-----VGATVEDDvafgLENLGVPREEMRK-RVDEALKLVGM---EDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAvvEAI-ADRVLVLEKGRVVEQGTapavlrvPRE 247
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDME--EAVlADRVIVMNKGKIVAEGT-------PRE 222
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
296-523 |
7.57e-40 |
|
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: 144.97 E-value: 7.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGR-----EVAGLSEG-RLRALRSDVQMIFQDPF 369
Cdd:TIGR02323 17 KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRsgaelELYQLSEAeRRRLMRTEWGFVHQNPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASLNPRQTVGQIVMTGPLVQGVSK-ADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECV 448
Cdd:TIGR02323 97 DGLRMRVSAGANIGERLMAIGARHyGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPT 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 449 SALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMA 523
Cdd:TIGR02323 177 GGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSS 251
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
298-446 |
1.06e-39 |
|
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: 141.25 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREvagLSEGRLRALRSDVQMIFQDPFasLNPRQT 377
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQD---LTDDERKSLRKEIGYVFQDPQ--LFPRLT 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 378 VGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAA---FERFPHEFSGGQRQRIGIARALAVEPKVLIADE 446
Cdd:pfam00005 76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
295-512 |
1.96e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 144.81 E-value: 1.96e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGlSEGRLRALRSDVQMIFQDPFASLNp 374
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQYPEYQLF- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAF-ERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:PRK13637 98 EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADA 512
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEV 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
294-510 |
2.08e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 144.39 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREvagLSEGRLRALRSDVQMIFQDPfasln 373
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDVRRQVGMVFQNP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMT----GPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK13635 91 DNQFVGATVQDdvafGLENIGVPREEMVERVDQALRQVGMEDFL-NREPHRLSGGQKQRVAIAGVLALQPDIIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 450 ALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAALFA 510
Cdd:PRK13635 170 MLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-238 |
3.20e-39 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 142.85 E-value: 3.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 20 SHALYDLSLQLNRGECLCVVGESGSGKSMLAKAL-LRQLPDplkveSGRLVFRDE--DLADR-SEEAMRQLRgRDISMVF 95
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnLLEMPR-----SGTLNIAGNhfDFSKTpSDKAIRELR-RNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 QEpmSALNPLMRVGEQ-IDETLRAHGVAAARVRrQRVVDLLgyvglpdpERLRLA-----YPFELSGGQRQRVVIAMALA 169
Cdd:PRK11124 89 QQ--YNLWPHLTVQQNlIEAPCRVLGLSKDQAL-ARAEKLL--------ERLRLKpyadrFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 170 FDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTA 238
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
274-499 |
3.39e-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: 3.39e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFcsrsgwwgrRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGlsegR 353
Cdd:cd03230 1 IEVRNLSKRY---------GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----E 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 LRALRSDVQMIFQDPfaSLNPRQTVgqivmtgplvqgvskadaerraRELLglvglpaaaferfphEFSGGQRQRIGIAR 433
Cdd:cd03230 68 PEEVKRRIGYLPEEP--SLYENLTV----------------------RENL---------------KLSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 434 ALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRV 499
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-241 |
6.32e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 142.12 E-value: 6.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALPAGAdrsHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEE 81
Cdd:COG3638 1 PMLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE----PTSGEILVDGQDVTALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRgRDISMVFQEP-----MSAL-NPLM-RVGeqidetlRAHGVAAARVR-----RQRVVDLLGYVGLPDpERLRLA 149
Cdd:COG3638 74 ALRRLR-RRIGMIFQQFnlvprLSVLtNVLAgRLG-------RTSTWRSLLGLfppedRERALEALERVGLAD-KAYQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 150 YpfELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEK 229
Cdd:COG3638 145 D--QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRD 222
|
250
....*....|..
gi 1331382268 230 GRVVEQGTAPAV 241
Cdd:COG3638 223 GRVVFDGPPAEL 234
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
25-257 |
7.25e-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: 142.28 E-value: 7.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADR-----SEEAMRQLRGRDISMVFQEPM 99
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLA----PDHGTATYIMRSGAELelyqlSEAERRRLMRTEWGFVHQNPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 SALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLpDPERLRlAYPFELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:TIGR02323 97 DGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEI-DPTRID-DLPRAFSGGMQQRLQIARNLVTRPRLVFMDE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAAV 257
Cdd:TIGR02323 175 PTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSSI 252
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
299-523 |
7.99e-39 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 142.15 E-value: 7.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 299 DAVQLQLREGETLGIVGESGSGKSTlgRCLVRL------LRADSGRIEWLGREVAGLS-EGRLRALrsdvqmIFQDPFAS 371
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSL--TCAAALgilpagVRQTAGRVLLDGKPVAPCAlRGRKIAT------IMQNPRSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 372 LNPRQTVGQIVMTGPLVQGVSKADAerRARELLGLVGL--PAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK10418 92 FNPLHTMHTHARETCLALGKPADDA--TLTAALEAVGLenAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTT 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 450 ALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMA 523
Cdd:PRK10418 170 DLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
298-499 |
8.84e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.72 E-value: 8.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPFAslnPRQT 377
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQVAYVPQEPAL---WGGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 VGQiVMTGPLvQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQV 457
Cdd:COG4619 90 VRD-NLPFPF-QLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1331382268 458 QILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRV 499
Cdd:COG4619 168 RVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-262 |
1.29e-38 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 142.24 E-value: 1.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVFRDEDLA--DRSeeamrqLRGRDISMVFQEPM 99
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEP----TSGELLIDDHPLHfgDYS------YRSQRIRMIFQDPS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 SALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGL-PDPERLrlaYPFELSGGQRQRVVIAMALAFDPALLIAD 178
Cdd:PRK15112 98 TSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASY---YPHMLAPGQKQRLGLARALILRPKVIIAD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 179 EPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAAVS 258
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAGHF 254
|
....
gi 1331382268 259 AQPL 262
Cdd:PRK15112 255 GEAL 258
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
21-254 |
2.48e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 143.36 E-value: 2.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKA---LLRqlPDplkveSGRLVFRDEDLAdrseeAMRQLRGRDISMVFQE 97
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET--PD-----SGRIVLNGRDLF-----TNLPPRERRVGFVFQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 PmsALNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:COG1118 84 Y--ALFPHMTVAENIAFGLRVRPPSKAE-IRARVEELLELVQLEGLAD---RYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfaVVEA--IADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLL 254
Cdd:COG1118 158 DEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHD--QEEAleLADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFL 234
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
290-503 |
2.80e-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: 2.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 290 WGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSeGRLRALRsdvqmifqdpf 369
Cdd:cd03214 7 VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS-PKELARK----------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 aslnpRQTVGQIVmtgplvqgvskadaerrarELLGLVGLPaaafERFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:cd03214 75 -----IAYVPQAL-------------------ELLGLAHLA----DRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 450 ALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03214 127 HLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
294-503 |
3.41e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 143.93 E-value: 3.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrlrALRSDVQMIFQDpFAsLN 373
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-----AENRHVNTVFQS-YA-LF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:PRK09452 99 PHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFA-QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:PRK09452 178 KLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
21-232 |
4.26e-38 |
|
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: 138.82 E-value: 4.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLaDRSEEAMRQLRgRDISMVFQEpmS 100
Cdd:cd03262 14 HVLKGIDLTVKKGEVVVIIGPSGSGKS----TLLRCINLLEEPDSGTIIIDGLKL-TDDKKNINELR-QKVGMVFQQ--F 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPLMRVGEQIDETLR-AHGVAAARVRRqRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:cd03262 86 NLFPHLTVLENITLAPIkVKGMSKAEAEE-RALELLEKVGLADKAD---AYPAQLSGGQQQRVAIARALAMNPKVMLFDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVLEKGRV 232
Cdd:cd03262 162 PTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
293-498 |
6.81e-38 |
|
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: 136.74 E-value: 6.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 293 RTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPFasl 372
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLRKNIAYVPQDPF--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 373 nprqtvgqiVMTGPLvqgvskadaerraRE-LLglvglpaaaferfphefSGGQRQRIGIARALAVEPKVLIADECVSAL 451
Cdd:cd03228 87 ---------LFSGTI-------------REnIL-----------------SGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1331382268 452 DALIQVQILELLESLQRrfRLSIVFITHDLRvAARLCDRIAVMRKGR 498
Cdd:cd03228 128 DPETEALILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
297-503 |
7.52e-38 |
|
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: 138.16 E-value: 7.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLsegrlRALRSDVQMIFQDpFAsLNPRQ 376
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-----PPKDRDIAMVFQN-YA-LYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGPLVQGVSKADAERRAR---ELLGLVGLpaaaFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:cd03301 88 TVYDNIAFGLKLRKVPKDEIDERVRevaELLQIEHL----LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03301 164 KLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
21-231 |
1.03e-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: 136.55 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLR-QLPDplkveSGRLVFRDEDLADrsEEAMRQLRGRDISMVFQEPm 99
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGlEEPD-----SGSILIDGEDLTD--LEDELPPLRRRIGMVFQDF- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 sALNPLMRVGEQIdetlrahgvaaarvrrqrvvdllgyvglpdperlrlAYPfeLSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:cd03229 86 -ALFPHLTVLENI------------------------------------ALG--LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGR 231
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-243 |
1.06e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 138.68 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLAdrse 80
Cdd:COG1121 4 MPAIELENLTVSY----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLP----PTSGTVRLFGKPPR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 eamrqLRGRDISMVFQepMSALNPL--MRVGEQIDETLRAHGVAAARVR---RQRVVDLLGYVGLPDPERLRLAypfELS 155
Cdd:COG1121 72 -----RARRRIGYVPQ--RAEVDWDfpITVRDVVLMGRYGRRGLFRRPSradREAVDEALERVGLEDLADRPIG---ELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLeKGRVVEQ 235
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRR-EGKTILVVTHDLGAVREYFDRVLLL-NRGLVAH 219
|
....*...
gi 1331382268 236 GTAPAVLR 243
Cdd:COG1121 220 GPPEEVLT 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
274-511 |
1.14e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 140.61 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFCSRSGWwgrrTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGR-----EVAG 348
Cdd:PRK13651 3 IKVKNIVKIFNKKLPT----ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKdeknkKKTK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 349 LSEGRL----------------RALRSDVQMIFQdpFASLNP-RQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPA 411
Cdd:PRK13651 79 EKEKVLeklviqktrfkkikkiKEIRRRVGVVFQ--FAEYQLfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 412 AAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRI 491
Cdd:PRK13651 157 SYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRT 235
|
250 260
....*....|....*....|
gi 1331382268 492 AVMRKGRVVEQGETAALFAD 511
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDILSD 255
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-236 |
1.46e-37 |
|
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: 137.43 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNrGECLCVVGESGSGKSMLakalLRQLPDPLKVESGRLVFRDEDLADRSEEAMRQLRGRDISMVFQEpmSALNP 104
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTL----LRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVGEQIDETLRAHgvaAARVRRQRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSAL 184
Cdd:cd03297 89 HLNVRENLAFGLKRK---RNREDRISVDELLDLLGL---DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 185 DVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03297 163 DRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
291-509 |
1.58e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 138.30 E-value: 1.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglseGRLRAL------RSDVQMI 364
Cdd:COG1121 15 SYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRigyvpqRAEVDWD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 365 FqdPFaslnprqTVGQIVMTG-----PLVQGVSKADAERrARELLGLVGLPAAAFERFpHEFSGGQRQRIGIARALAVEP 439
Cdd:COG1121 90 F--PI-------TVRDVVLMGrygrrGLFRRPSRADREA-VDEALERVGLEDLADRPI-GELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 440 KVLIADECVSALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKgRVVEQGETAALF 509
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNR-GLVAHGPPEEVL 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-248 |
1.68e-37 |
|
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: 137.85 E-value: 1.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALpagadRSHALYDLSLQLNRGECLCVVGESGSGKSMLakalLRQLPDPLKVESGRLVFRDEDLADRSEEAm 83
Cdd:cd03299 1 LKVENLSKDW-----KEFKLKNVSLEVERGDYFVILGPTGSGKSVL----LETIAGFIKPDSGKILLNGKDITNLPPEK- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 rqlrgRDISMVFQEpmSALNPLMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVV 163
Cdd:cd03299 71 -----RDISYVPQN--YALFPHMTVYKNIAYGLKKRKVDKKEIER-KVLEIAEMLGI---DHLLNRKPETLSGGEQQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 164 IAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLR 243
Cdd:cd03299 140 IARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
....*
gi 1331382268 244 VPRED 248
Cdd:cd03299 220 KPKNE 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-241 |
2.53e-37 |
|
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: 137.81 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGadrSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRqLPDPlkvESGRLVFRDEDLADRSEEA 82
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINR-LVEP---SSGSILLEGTDITKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLRgRDISMVFQE-----PMSAL-NPLM-RVGEQidETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYpfeLS 155
Cdd:TIGR02315 74 LRKLR-RRIGMIFQHynlieRLTVLeNVLHgRLGYK--PTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQ---LS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQ 235
Cdd:TIGR02315 148 GGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFD 227
|
....*.
gi 1331382268 236 GTAPAV 241
Cdd:TIGR02315 228 GAPSEL 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
296-523 |
4.66e-37 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 139.55 E-value: 4.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRL----LRADSGRIEWLGREVAGLS-EGRLRALRSDVQMIFQDPFA 370
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSpRERRKLVGHNVSMIFQEPQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SLNPRQTVGQIVMT--------GPLVQGVSKAdaERRARELLGLVGL--PAAAFERFPHEFSGGQRQRIGIARALAVEPK 440
Cdd:PRK15093 101 CLDPSERVGRQLMQnipgwtykGRWWQRFGWR--KRRAIELLHRVGIkdHKDAMRSFPYELTEGECQKVMIAIALANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 441 VLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTREL 520
Cdd:PRK15093 179 LLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQAL 258
|
...
gi 1331382268 521 LMA 523
Cdd:PRK15093 259 IRA 261
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
21-242 |
5.61e-37 |
|
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: 136.91 E-value: 5.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEEAMRQlrgrdISMVFQEPMs 100
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLL----KPDSGSILIDGEDVRKEPREARRQ-----IGVLPDERG- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 aLNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:COG4555 85 -LYDRLTVRENIRYFAELYGLFDEE-LKKRIEELIELLGLEEFLDRRVG---ELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVL 242
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
294-519 |
1.24e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 136.32 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRL------LRAdSGRIEWLGREVAGlSEGRLRALRSDVQMIFQD 367
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgARV-EGEILLDGEDIYD-PDVDVVELRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 368 PfaslNPrqtvgqIVMT-------GPLVQGV-SKADAERRARELLGLVGL----------PAAAFerfphefSGGQRQRI 429
Cdd:COG1117 101 P----NP------FPKSiydnvayGLRLHGIkSKSELDEIVEESLRKAALwdevkdrlkkSALGL-------SGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 430 GIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFrlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALF 509
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIF 241
|
250
....*....|
gi 1331382268 510 ADARHPYTRE 519
Cdd:COG1117 242 TNPKDKRTED 251
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
297-511 |
1.38e-36 |
|
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: 139.08 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDaVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwLGREVAgLSEGRLRAL---RSDVQMIFQDpfASLN 373
Cdd:COG4148 15 TLD-VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIR-LGGEVL-QDSARGIFLpphRRRIGYVFQE--ARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGqivmtGPLVQGVSKADAERRAR------ELLGLVGLpaaaFERFPHEFSGGQRQRIGIARALAVEPKVLIADEC 447
Cdd:COG4148 90 PHLSVR-----GNLLYGRKRAPRAERRIsfdevvELLGIGHL----LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 448 VSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
298-509 |
1.45e-36 |
|
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: 135.54 E-value: 1.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLS-EGRlralrsDVQMIFQDpfASLNPRQ 376
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPpEKR------DISYVPQN--YALFPHM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGPLVQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQ 456
Cdd:cd03299 87 TVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 457 VQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALF 509
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-241 |
1.85e-36 |
|
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: 135.39 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGadrSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVFRDEDLADRSEEAM 83
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP----TSGSVLIDGTDINKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 RQLRgRDISMVFQ-----EPMSAL-NPLM-RVGEQidETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAypfELSG 156
Cdd:cd03256 74 RQLR-RQIGMIFQqfnliERLSVLeNVLSgRLGRR--STWRSLFGLFPKEEKQRALAALERVGLLDKAYQRAD---QLSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 157 GQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDG 227
|
....*
gi 1331382268 237 TAPAV 241
Cdd:cd03256 228 PPAEL 232
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-231 |
2.92e-36 |
|
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: 134.48 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVE--------HLRialpaGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQ-LPDplkveSGRLVFRD 72
Cdd:COG4778 3 TLLEVEnlsktftlHLQ-----GGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNyLPD-----SGSILVRH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 73 E----DLADRSEEAMRQLRGRDISMVFQepmsALNPLMRVG--EQIDETLRAHGVAAARVRRqRVVDLLGYVGLPdpERL 146
Cdd:COG4778 73 DggwvDLAQASPREILALRRRTIGYVSQ----FLRVIPRVSalDVVAEPLLERGVDREEARA-RARELLARLNLP--ERL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 147 RLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLV 226
Cdd:COG4778 146 WDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVD 224
|
....*
gi 1331382268 227 LEKGR 231
Cdd:COG4778 225 VTPFS 229
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
21-232 |
4.32e-36 |
|
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: 132.14 E-value: 4.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDplkveSGRLVFRDEDLADRSEEAMRQlrgrdISMVFQEPM 99
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPD-----SGEIKVLGKDIKKEPEEVKRR-----IGYLPEEPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 saLNPLMRVGEQIDetlrahgvaaarvrrqrvvdllgyvglpdperlrlaypfeLSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:cd03230 84 --LYENLTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 180 PTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRV 232
Cdd:cd03230 122 PTSGLDPESRREFWELLREL-KKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
307-503 |
4.40e-36 |
|
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: 133.57 E-value: 4.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 307 EGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREvagLSEGR----LRALRSDVQMIFQDpfASLNPRQTVGQIV 382
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTV---LFDSRkkinLPPQQRKIGLVFQQ--YALFPHLNVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 383 MTGPLVqgvsKADAERR--ARELLGLVGLPAAAFeRFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQIL 460
Cdd:cd03297 97 AFGLKR----KRNREDRisVDELLDLLGLDHLLN-RYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1331382268 461 ELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
22-231 |
4.75e-36 |
|
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: 131.74 E-value: 4.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAMRQLrgrdISMVFQEPMsa 101
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYD----PTSGEILIDGVDLRDLDLESLRKN----IAYVPQDPF-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 lnpLMrvgeqiDETLRahgvaaarvrrqrvvdllgyvglpdpERLrlaypfeLSGGQRQRVVIAMALAFDPALLIADEPT 181
Cdd:cd03228 87 ---LF------SGTIR--------------------------ENI-------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 182 SALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEaIADRVLVLEKGR 231
Cdd:cd03228 125 SALDPETEALILEALRALAKGK--TVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
22-232 |
6.97e-36 |
|
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: 132.92 E-value: 6.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLR-QLPdplkvESGRLVFRDEDLADRSEEAMRQLRgRDISMVFQEpmS 100
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKeELP-----TSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQD--F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPLMRVGEQIDETLRAHGVAAaRVRRQRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:cd03292 88 RLLPDRNVYENVAFALEVTGVPP-REIRKRVPAALELVGLSHKHR---ALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRV 232
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
291-510 |
7.09e-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: 141.90 E-value: 7.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPF- 369
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQIGVVLQDVFl 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 --ASL--NprqtvgqIVMTGPlvqGVSKADAERRARellgLVGLpaAAF-ERFPH-----------EFSGGQRQRIGIAR 433
Cdd:COG2274 561 fsGTIreN-------ITLGDP---DATDEEIIEAAR----LAGL--HDFiEALPMgydtvvgeggsNLSGGQRQRLAIAR 624
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 434 ALAVEPKVLIADECVSALDALIQVQILELLESLQRrfRLSIVFITHDLRVaARLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:COG2274 625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLST-IRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
296-521 |
1.01e-35 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 133.94 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEG----------RLRALRSDVQMIF 365
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 366 QDpfASLNPRQTVGQIVMTGPL-VQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIA 444
Cdd:PRK10619 99 QH--FNLWSHMTVLENVMEAPIqVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 445 DECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELL 521
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFL 252
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-231 |
1.41e-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: 130.06 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEEAMRqlrgRDISMVFQepms 100
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLL----KPTSGEILIDGKDIAKLPLEELR----RRIGYVPQ---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 alnplmrvgeqidetlrahgvaaarvrrqrvvdllgyvglpdperlrlaypfeLSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:cd00267 81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGR 231
Cdd:cd00267 108 TSGLDPASRERLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
294-508 |
1.60e-35 |
|
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: 132.11 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwlgreVAGLSEGR-LRALRSDVQMIFQDPfaSL 372
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRAT-----VAGHDVVRePREVRRRIGIVFQDL--SV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 373 NPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALD 452
Cdd:cd03265 85 DDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAA-DRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 453 ALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-249 |
2.16e-35 |
|
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: 132.36 E-value: 2.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAmrqlrgRDISMVFQE 97
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKT----TLLRLIAGFETPTSGEILLDGKDITNLPPHK------RPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 pmSALNPLMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:cd03300 81 --YALFPHLTVFENIAFGLRLKKLPKAEIKE-RVAEALDLVQL---EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTapavlrvPREDY 249
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT-------PEEIY 219
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
296-498 |
3.26e-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: 129.29 E-value: 3.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglSEGRLRALRSDVQMIFQdpfaslnpr 375
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRRRIGYVPQ--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 qtvgqivmtgplvqgvskadaerrarellglvglpaaaferfpheFSGGQRQRIGIARALAVEPKVLIADECVSALDALI 455
Cdd:cd00267 81 ---------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1331382268 456 QVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGR 498
Cdd:cd00267 116 RERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
313-511 |
3.31e-35 |
|
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: 134.54 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 313 IVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrlrALRSDVQMIFQDpfASLNPRQTVGQIVMTGPLVQGVS 392
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-----PHLRHINMVFQS--YALFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 393 KADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRL 472
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFA-DRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 1331382268 473 SIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEE 191
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
25-243 |
3.56e-35 |
|
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: 135.23 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKA---LLRqlPDplkveSGRLVFRDEDLADRSEEAMRQLRGRDISMVFQEPmsA 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER--PD-----SGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQEA--R 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDperlRlaYPFELSGGQRQRVVIAMALAFDPALLIADEPT 181
Cdd:COG4148 88 LFPHLSVRGNLLYGRKRAPRAERRISFDEVVELLGIGHLLD----R--RPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 182 SALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLR 243
Cdd:COG4148 162 AALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
271-508 |
3.82e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 137.84 E-value: 3.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 271 PVVLKAEALGKVFcsrSGwwgrrtTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLS 350
Cdd:COG1129 2 EPLLEMRGISKSF---GG------VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 351 egRLRALRSDVQMIFQDPfaSLNPRQTVGQ-IVMTGPLVQG--VSKADAERRARELLGLVGL---PAAAFErfphEFSGG 424
Cdd:COG1129 73 --PRDAQAAGIAIIHQEL--NLVPNLSVAEnIFLGREPRRGglIDWRAMRRRARELLARLGLdidPDTPVG----DLSVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 425 QRQRIGIARALAVEPKVLIADECVSALDAlIQVQIL-ELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:COG1129 145 QQQLVEIARALSRDARVLILDEPTASLTE-REVERLfRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
|
....*
gi 1331382268 504 ETAAL 508
Cdd:COG1129 223 PVAEL 227
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
291-498 |
3.85e-35 |
|
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: 131.40 E-value: 3.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRI------EWLgrEVAGLSEGRLRALRSDV--- 361
Cdd:COG4778 20 GGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIlvrhdgGWV--DLAQASPREILALRRRTigy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 362 --QmifqdpFASLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEP 439
Cdd:COG4778 98 vsQ------FLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 440 KVLIADECVSALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGR 498
Cdd:COG4778 172 PLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
22-238 |
4.06e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 131.67 E-value: 4.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKAL-LRQLPDplkveSGRLVFRDE--DLADR-SEEAMRQLRgRDISMVFQE 97
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLnLLETPD-----SGQLNIAGHqfDFSQKpSEKAIRLLR-QKVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 pmSALNPLMRVGEQIDET-LRAHGVAAARVRrQRVVDLLgyvglpdpERLRL-----AYPFELSGGQRQRVVIAMALAFD 171
Cdd:COG4161 91 --YNLWPHLTVMENLIEApCKVLGLSKEQAR-EKAMKLL--------ARLRLtdkadRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTA 238
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA 225
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
7-231 |
4.29e-35 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 130.83 E-value: 4.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 7 EHLRIALPAGAdrsHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAMRQL 86
Cdd:TIGR02673 5 HNVSKAYPGGV---AALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALT----PSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 87 RgRDISMVFQEpmSALNPLMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAM 166
Cdd:TIGR02673 78 R-RRIGVVFQD--FRLLPDRTVYENVALPLEVRGKKEREIQR-RVGAALRQVGLEHKAD---AFPEQLSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 167 ALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGR 231
Cdd:TIGR02673 151 AIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
297-513 |
5.22e-35 |
|
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: 131.41 E-value: 5.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRAL---RSdvqmiFQDPfaSLN 373
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigRT-----FQIP--RLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMTGPLVQGVS----------KADAERRARELLGLVGLPAAAFERfPHEFSGGQRQRIGIARALAVEPKVLI 443
Cdd:cd03219 88 PELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRP-AGELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 444 ADECVSALDALIQVQILELLESLqRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADAR 513
Cdd:cd03219 167 LDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
303-521 |
5.77e-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: 5.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 303 LQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRlralRSdVQMIFQDP--FASLNPRQTVGq 380
Cdd:COG3840 20 LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE----RP-VSMLFQENnlFPHLTVAQNIG- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 381 ivmtgpLvqGVS---KADAERRAR--ELLGLVGLpaAAFE-RFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:COG3840 94 ------L--GLRpglKLTAEQRAQveQALERVGL--AGLLdRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 455 IQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELL 521
Cdd:COG3840 164 LRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
303-518 |
7.35e-35 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 135.16 E-value: 7.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 303 LQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALR-SDVQMIFQDpFAsLNPRQTVGQI 381
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQS-FA-LMPHMTVLDN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 382 VMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILE 461
Cdd:PRK10070 127 TAFGMELAGINAEERREKALDALRQVGLENYA-HSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQD 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 462 LLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTR 518
Cdd:PRK10070 206 ELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-526 |
1.06e-34 |
|
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: 136.49 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplKVESGRLVFRDEDLADRSeeaMRQLRGRDISMVFQEPMsa 101
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPH--GTWDGEIYWSGSPLKASN---IRDTERAGIVIIHQELT-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQI---DETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAypFELSGGQRQRVVIAMALAFDPALLIAD 178
Cdd:TIGR02633 89 LVPELSVAENIflgNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPV--GDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 179 EPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVeqGTAPAvlRVPREDYTRQLLAAVS 258
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV--ATKDM--STMSEDDIITMMVGRE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 259 AQPLVPRT-QVAGPVVLKAEALgkvfcsrSGWW-GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRClvrLLRADS 336
Cdd:TIGR02633 242 ITSLYPHEpHEIGDVILEARNL-------TCWDvINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQA---LFGAYP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 337 GRIE---WL-GREVAglSEGRLRALRSDVQMIFQD-PFASLNPRQTVGQIVMTGPL--VQGVSKADAERRARELL-GLVG 408
Cdd:TIGR02633 312 GKFEgnvFInGKPVD--IRNPAQAIRAGIAMVPEDrKRHGIVPILGVGKNITLSVLksFCFKMRIDAAAELQIIGsAIQR 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 409 LPAAAFERF--PHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRfRLSIVFITHDLRVAAR 486
Cdd:TIGR02633 390 LKVKTASPFlpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLG 468
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1331382268 487 LCDRIAVMRKGRVveQGETaalfadARHPYTRELLMAEAI 526
Cdd:TIGR02633 469 LSDRVLVIGEGKL--KGDF------VNHALTQEQVLAAAL 500
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
295-511 |
1.35e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 131.35 E-value: 1.35e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAgLSEGRLRALRSDVQMIFQDP----FA 370
Cdd:PRK13639 15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEVRKTVGIVFQNPddqlFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SlnprqTVGQIVMTGPLVQGVSKADAERRARELLGLVGLpaAAFE-RFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK13639 94 P-----TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGM--EGFEnKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 450 ALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
22-256 |
1.94e-34 |
|
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: 129.77 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSeeamrqLRGRDISMVFQEpmSA 101
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKT----TLLRLIAGLERPDSGTILFGGEDATDVP------VQERNVGFVFQH--YA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQIDETLRAHGVA----AARVRRqRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:cd03296 85 LFRHMTVFDNVAFGLRVKPRSerppEAEIRA-KVHELLKLVQL---DWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAA 256
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-236 |
2.18e-34 |
|
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: 127.55 E-value: 2.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 5 SVEHLRIalpaGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSeeamR 84
Cdd:cd03214 1 EVENLSV----GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLL----KPSSGEILLDGKDLASLS----P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 85 QLRGRDISMVFQepmsALnplmrvgeqidETLRAHGVAaarvrrQRVVDllgyvglpdperlrlaypfELSGGQRQRVVI 164
Cdd:cd03214 69 KELARKIAYVPQ----AL-----------ELLGLAHLA------DRPFN-------------------ELSGGERQRVLL 108
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 165 AMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03214 109 ARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-236 |
2.77e-34 |
|
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: 128.42 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 5 SVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdPLkveSGRLVFRDEDLADRSEEA-- 82
Cdd:cd03235 1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLK-PT---SGSIRVFGKPLEKERKRIgy 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLRGRDISMvfqePMSALNpLMRVGeqidetLRAHGVAAARVR---RQRVVDLLGYVGLPDPERLRLAypfELSGGQR 159
Cdd:cd03235 73 VPQRRSIDRDF----PISVRD-VVLMG------LYGHKGLFRRLSkadKAKVDEALERVGLSELADRQIG---ELSGGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 160 QRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKgRVVEQG 236
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRR-EGMTILVVTHDLGLVLEYFDRVLLLNR-TVVASG 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-235 |
3.53e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 129.60 E-value: 3.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDL----A 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKT----TLLNLIAGFLAPSSGEITLDGVPVtgpgA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 77 DRSeeamrqlrgrdisMVFQEpmSALNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPDPERlrlAYPFELSG 156
Cdd:COG4525 77 DRG-------------VVFQK--DALLPWLNVLDNVAFGLRLRGVPKAE-RRARAEELLALVGLADFAR---RRIWQLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 157 GQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfaVVEAI--ADRVLVL--EKGRV 232
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS--VEEALflATRLVVMspGPGRI 215
|
...
gi 1331382268 233 VEQ 235
Cdd:COG4525 216 VER 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-237 |
5.51e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.75 E-value: 5.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALPaGADRsHALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLadrSEE 81
Cdd:PRK13635 4 EIIRVEHISFRYP-DAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAK-LLNGLLLP---EAGTITVGGMVL---SEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRgRDISMVFQEPMSALnplmrVGEQIDETLrAHGVAAARVRR----QRVVDLLGYVGLpdpERLRLAYPFELSGG 157
Cdd:PRK13635 75 TVWDVR-RQVGMVFQNPDNQF-----VGATVQDDV-AFGLENIGVPReemvERVDQALRQVGM---EDFLNREPHRLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 158 QRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVeAIADRVLVLEKGRVVEQGT 237
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGT 223
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
295-511 |
6.46e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 129.95 E-value: 6.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREV-AGLSEGRLRALRSDVQMIFQDPFASLN 373
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLRKKVSLVFQFPEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 pRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:PRK13641 100 -ENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 454 LIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
295-500 |
7.30e-34 |
|
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: 125.62 E-value: 7.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegRLRALRSDVQMIFQdpfaslnp 374
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS--PRDARRAGIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 rqtvgqivmtgplvqgvskadaerrarellglvglpaaaferfpheFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:cd03216 83 ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPA 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1331382268 455 IQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVV 500
Cdd:cd03216 117 EVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-246 |
1.02e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.96 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKS----MLAkALLrqlpdplKVESGRLVFRDEDLA 76
Cdd:COG3839 1 MASLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKStllrMIA-GLE-------DPTSGEILIGGRDVT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 77 DRSEEAmrqlrgRDISMVFQEPmsALNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLgyvglpdpERLRLA-----YP 151
Cdd:COG3839 69 DLPPKD------RNIAMVFQSY--ALYPHMTVYENIAFPLKLRKVPKAE-IDRRVREAA--------ELLGLEdlldrKP 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 152 FELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFavVEA--IADRVLVLEK 229
Cdd:COG3839 132 KQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ--VEAmtLADRIAVMND 209
|
250
....*....|....*..
gi 1331382268 230 GRVVEQGTAPAVLRVPR 246
Cdd:COG3839 210 GRIQQVGTPEELYDRPA 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
297-511 |
1.45e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 128.71 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGR-LRALRSDVQMIFQDPFASLNpR 375
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdIKQIRKKVGLVFQFPESQLF-E 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 QTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALI 455
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 456 QVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK13649 181 RKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
4-233 |
1.86e-33 |
|
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: 126.67 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKAL--LRqlpdplKVESGRLVFRDEDLADRSEE 81
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIggLR------SVQEGSLKVLGQELHGASKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRgRDISMVFQEpmSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDpeRLRlAYPFELSGGQRQR 161
Cdd:TIGR02982 76 QLVQLR-RRIGYIFQA--HNLLGFLTARQNVQMALELQPNLSYQEARERARAMLEAVGLGD--HLN-YYPHNLSGGQKQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 162 VVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEaIADRVLVLEKGRVV 233
Cdd:TIGR02982 150 VAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILD-VADRILQMEDGKLL 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
25-182 |
2.02e-33 |
|
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: 123.91 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVFRDEDLADRSEEAMRqlrgRDISMVFQEPmsALNP 104
Cdd:pfam00005 3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSP----TEGTILLDGQDLTDDERKSLR----KEIGYVFQDP--QLFP 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 105 LMRVGEQIDETLRAHGVAAaRVRRQRVVDLLGYVGLPD-PERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTS 182
Cdd:pfam00005 73 RLTVRENLRLGLLLKGLSK-REKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
21-246 |
2.06e-33 |
|
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: 126.78 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDplkveSGRLVFRDEDLADRSEeamRQLRGRDISMVFQEP- 98
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLrPT-----SGSVLFDGEDITGLPP---HEIARLGIGRTFQIPr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 ----MSALNPLMrVGEQIDETLRAHGVAAARVR---RQRVVDLLGYVGLpDPERLRLAYpfELSGGQRQRVVIAMALAFD 171
Cdd:cd03219 86 lfpeLTVLENVM-VAAQARTGSGLLLARARREEreaRERAEELLERVGL-ADLADRPAG--ELSYGQQRRLEIARALATD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPR 246
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
295-511 |
2.69e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 128.04 E-value: 2.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRaLRSDVQMIFQDPFASLNp 374
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMK-LRESVGMVFQDPDNQLF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:PRK13636 97 SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI-EHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 455 IQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK13636 176 GVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
16-242 |
3.23e-33 |
|
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: 134.19 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 16 GADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVFRDEDLADRSEEAMRqlrgRDISMVF 95
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP----TSGRILIDGIDLRQIDPASLR----RQIGVVL 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 QEPM----SALNPLMRVGEQIDEtlrAHGVAAARVrrqrvVDLLGYVglpdpERLRLAYpfE---------LSGGQRQRV 162
Cdd:COG2274 556 QDVFlfsgTIRENITLGDPDATD---EEIIEAARL-----AGLHDFI-----EALPMGY--DtvvgeggsnLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqqDKGMALLFITHDFAVVeAIADRVLVLEKGRVVEQGTAPAVL 242
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
21-236 |
3.25e-33 |
|
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: 125.44 E-value: 3.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAmrqlrgRDISMVFQEpmS 100
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKT----TTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD------RDIAMVFQN--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPLMRVGEQIDETLRAHGVAAARVRRQ--RVVDLLGYVGLPDperlrlAYPFELSGGQRQRVVIAMALAFDPALLIAD 178
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKLRKVPKDEIDERvrEVAELLQIEHLLD------RKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 179 EPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
23-258 |
5.71e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 125.98 E-value: 5.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEaMRQLRgRDISMVFQE----P 98
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKS----TLLRCINKLEEITSGDLIVDGLKVNDPKVD-ERLIR-QEAGMVFQQfylfP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 -MSALNPLMrVGeqideTLRAHGVAAARVRRQrVVDLLGYVGLPdpERLRlAYPFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:PRK09493 91 hLTALENVM-FG-----PLRVRGASKEEAEKQ-ARELLAKVGLA--ERAH-HYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAAV 257
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
.
gi 1331382268 258 S 258
Cdd:PRK09493 240 S 240
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
23-234 |
6.10e-33 |
|
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: 125.16 E-value: 6.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMRQLRGRDISMVFQ-----E 97
Cdd:TIGR02211 21 LKGVSLSIGKGEIVAIVGSSGSGKSTLLH-LLGGLDNP---TSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQfhhllP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 PMSALN----PLMRVGEQIDETlrahgvaaarvrRQRVVDLLGYVGLPDpeRLRlAYPFELSGGQRQRVVIAMALAFDPA 173
Cdd:TIGR02211 97 DFTALEnvamPLLIGKKSVKEA------------KERAYEMLEKVGLEH--RIN-HRPSELSGGERQRVAIARALVNQPS 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 174 LLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIaDRVLVLEKGRVVE 234
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDGQLFN 221
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
22-251 |
6.76e-33 |
|
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: 128.62 E-value: 6.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAmrqlrgRDISMVFQEpmSA 101
Cdd:TIGR03265 19 ALKDISLSVKKGEFVCLLGPSGCGKT----TLLRIIAGLERQTAGTIYQGGRDITRLPPQK------RDYGIVFQS--YA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQIDETLRAHGVAAARVRrQRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLIADEPT 181
Cdd:TIGR03265 87 LFPNLTVADNIAYGLKNRGMGRAEVA-ERVAELLDLVGLPGSER---KYPGQLSGGQQQRVALARALATSPGLLLLDEPL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 182 SALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTapavlrvPREDYTR 251
Cdd:TIGR03265 163 SALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGT-------PQEIYRH 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-237 |
6.91e-33 |
|
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: 132.19 E-value: 6.91e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAM 83
Cdd:COG4988 337 IELEDVSFSYP---GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP----PYSGSILINGVDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 RQLrgrdISMVFQEPmsAL-------NPLMRVGEQIDETLRAhgvAAARVRRQRVVDllgyvGLPDperlRLAYP----- 151
Cdd:COG4988 410 RRQ----IAWVPQNP--YLfagtireNLRLGRPDASDEELEA---ALEAAGLDEFVA-----ALPD----GLDTPlgegg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 152 FELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVeAIADRVLVLEKGR 231
Cdd:COG4988 472 RGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALL-AQADRILVLDDGR 548
|
....*.
gi 1331382268 232 VVEQGT 237
Cdd:COG4988 549 IVEQGT 554
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
298-510 |
8.33e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.38 E-value: 8.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREvagLSEGRLRALRSDVQMIFQDPfaslnPRQT 377
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWDIRHKIGMVFQNP-----DNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 VGQIVMT----GPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:PRK13650 95 VGATVEDdvafGLENKGIPHEEMKERVNEALELVGMQDFK-EREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAArLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:PRK13650 174 EGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
295-503 |
9.45e-33 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 131.83 E-value: 9.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPF---AS 371
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQIGVVPQDTFlfsGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 372 L-------NPRQTVGQIVmtgplvqgvskaDAERRARellglvglpAAAF-ERFPH-----------EFSGGQRQRIGIA 432
Cdd:COG1132 430 IrenirygRPDATDEEVE------------EAAKAAQ---------AHEFiEALPDgydtvvgergvNLSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 433 RALAVEPKVLIADECVSALDALIQVQILELLESLQRRfRLSIVfITHDLRvAARLCDRIAVMRKGRVVEQG 503
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKG-RTTIV-IAHRLS-TIRNADRILVLDDGRIVEQG 556
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
295-508 |
9.98e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 126.00 E-value: 9.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglSEGRLRALRSDVQMIFQDP----FA 370
Cdd:PRK13647 18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSKVGLVFQDPddqvFS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SlnprqTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSA 450
Cdd:PRK13647 95 S-----TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFR-DKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 451 LDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:PRK13647 169 LDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-243 |
1.23e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 126.32 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEaMRQLRGRdISMVFQEPMSA 101
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKS----TLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDIRKK-VGLVFQYPEYQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LnplmrVGEQIDETL----RAHGVAAARVRRqRVVDLLGYVGLpDPERLRLAYPFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:PRK13637 96 L-----FEETIEKDIafgpINLGLSEEEIEN-RVKRAMNIVGL-DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLR 243
Cdd:PRK13637 169 DEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-526 |
1.47e-32 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 130.43 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdpLKVESGRLVFRDEDLADRSeeaMRQLRGRDISMVFQEPMsa 101
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP--HGTYEGEIIFEGEELQASN---IRDTERAGIAIIHQELA-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQI--DETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:PRK13549 93 LVKELSVLENIflGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVG---NLGLGQQQLVEIAKALNKQARLLILDE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVeqGTAPA---------VLRVPREdyT 250
Cdd:PRK13549 170 PTASLTESETAVLLDIIRDLKA-HGIACIYISHKLNEVKAISDTICVIRDGRHI--GTRPAagmteddiiTMMVGRE--L 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 251 RQLLaavsaqPLVPRTqvAGPVVLKAEALgkvfcsrSGW-WGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRClv 329
Cdd:PRK13549 245 TALY------PREPHT--IGEVILEVRNL-------TAWdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQC-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 330 rLLRADSGRIE---WL-GREVAglSEGRLRALRSDVQMIFQDPFA-SLNPRQTVGQIVMTGPLVQ----GVSKADAERRA 400
Cdd:PRK13549 308 -LFGAYPGRWEgeiFIdGKPVK--IRNPQQAIAQGIAMVPEDRKRdGIVPVMGVGKNITLAALDRftggSRIDDAAELKT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 401 --RELLGL---VGLPAAAFERfpheFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRfRLSIV 475
Cdd:PRK13549 385 ilESIQRLkvkTASPELAIAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAII 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 476 FITHDLRVAARLCDRIAVMRKGRvveqgetaaLFAD-ARHPYTRELLMAEAI 526
Cdd:PRK13549 460 VISSELPEVLGLSDRVLVMHEGK---------LKGDlINHNLTQEQVMEAAL 502
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
20-257 |
1.90e-32 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 128.61 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 20 SHALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPLKvesGRLVFRDEDLADRSEEAMRQLRGRDISMVFQEpm 99
Cdd:PRK10070 41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVR-LLNRLIEPTR---GQVLIDGVDIAKISDAELREVRRKKIAMVFQS-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 SALNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:PRK10070 115 FALMPHMTVLDNTAFGMELAGINAEE-RREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAAV 257
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-242 |
2.18e-32 |
|
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: 123.70 E-value: 2.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRialpAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAm 83
Cdd:cd03224 1 LEVENLN----AGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP----PRSGSIRFDGRDITGLPPHE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 RQLRGrdISMVFQEPMsaLNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLgyvglPD-PERL-RLAYpfELSGGQRQR 161
Cdd:cd03224 72 RARAG--IGYVPEGRR--IFPELTVEENLLLGAYARRRAKRKARLERVYELF-----PRlKERRkQLAG--TLSGGEQQM 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 162 VVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAV 241
Cdd:cd03224 141 LAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
.
gi 1331382268 242 L 242
Cdd:cd03224 220 L 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
296-511 |
2.19e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 125.66 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGR-LRALRSDVQMIFQDPFASLNp 374
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyIRPVRKRIGMVFQFPESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 455 IQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
291-516 |
5.21e-32 |
|
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: 125.99 E-value: 5.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDaVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEG-RLRALRSDVQMIFQDpf 369
Cdd:TIGR02142 7 KRLGDFSLD-ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQE-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASLNPRQTVgqivmTGPLVQGVSKADA-ERRAR-----ELLGLVGLpaaaFERFPHEFSGGQRQRIGIARALAVEPKVLI 443
Cdd:TIGR02142 84 ARLFPHLSV-----RGNLRYGMKRARPsERRISferviELLGIGHL----LGRLPGRLSGGEKQRVAIGRALLSSPRLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 444 ADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPY 516
Cdd:TIGR02142 155 MDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
273-508 |
5.50e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 124.84 E-value: 5.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFcsrsgwwGRRTtqALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAG---- 348
Cdd:COG4152 1 MLELKGLTKRF-------GDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 349 ----LSEGRlralrsdvqmifqdpfaSLNPRQTVG-QIVMTGPLvQGVSKADAERRARELLGLVGLPAAAFERFpHEFSG 423
Cdd:COG4152 72 rigyLPEER-----------------GLYPKMKVGeQLVYLARL-KGLSKAEAKRRADEWLERLGLGDRANKKV-EELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 424 GQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
....*
gi 1331382268 504 ETAAL 508
Cdd:COG4152 212 SVDEI 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
25-245 |
1.09e-31 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 125.22 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSeeamrqLRGRDISMVFQEpmSALNP 104
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKT----TVLRLVAGLEKPTEGQIFIDGEDVTHRS------IQQRDICMVFQS--YALFP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVGEQIDETLRAHGVAAARvRRQRV------VDLLGYvglpdPERlrlaYPFELSGGQRQRVVIAMALAFDPALLIAD 178
Cdd:PRK11432 92 HMSLGENVGYGLKMLGVPKEE-RKQRVkealelVDLAGF-----EDR----YVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 179 EPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVP 245
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
298-525 |
1.55e-31 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 124.83 E-value: 1.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLS-EGRlralrsDVQMIFQDpfASLNPRQ 376
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiQQR------DICMVFQS--YALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGPLVQGVSKADAERRARELLGLVGLpaAAFE-RFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALI 455
Cdd:PRK11432 94 SLGENVGYGLKMLGVPKEERKQRVKEALELVDL--AGFEdRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 456 QVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFadaRHPYTREL--LMAEA 525
Cdd:PRK11432 172 RRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELY---RQPASRFMasFMGDA 240
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
297-503 |
1.57e-31 |
|
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: 121.10 E-value: 1.57e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglsegrlRALRSDVQMIFQDPFASLNPRQ 376
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGYVPQRRSIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTG-----PLVQGVSKADaERRARELLGLVGLPAAAFERFpHEFSGGQRQRIGIARALAVEPKVLIADECVSAL 451
Cdd:cd03235 86 SVRDVVLMGlyghkGLFRRLSKAD-KAKVDEALERVGLSELADRQI-GELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 452 DALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMrKGRVVEQG 503
Cdd:cd03235 164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-249 |
1.81e-31 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.07 E-value: 1.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLR--QLPDPLKVEsGRLVFRDEDLADRSEE 81
Cdd:COG1117 12 IEVRNLNVYY----GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGARVE-GEILLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMrQLRgRDISMVFQEPmsalNPL-MRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDpE---RLRlAYPFELSGG 157
Cdd:COG1117 87 VV-ELR-RRVGMVFQKP----NPFpKSIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWD-EvkdRLK-KSALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 158 QRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDkgMALLFITHDFAvvEA--IADRVLVLEKGRVVEQ 235
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQ--QAarVSDYTAFFYLGELVEF 234
|
250
....*....|....*...
gi 1331382268 236 GTAPAVLRVPR----EDY 249
Cdd:COG1117 235 GPTEQIFTNPKdkrtEDY 252
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-255 |
1.85e-31 |
|
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: 127.96 E-value: 1.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGAdrSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAM 83
Cdd:COG4987 334 LELEDVSFRYPGAG--RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLD----PQSGSITLGGVDLRDLDEDDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 RQLrgrdISMVFQEPmsalnPLMrvgeqiDETLRAH-GVAAARVRRQRVVDLLGYVGLPD-----PERL--RL-AYPFEL 154
Cdd:COG4987 408 RRR----IAVVPQRP-----HLF------DTTLRENlRLARPDATDEELWAALERVGLGDwlaalPDGLdtWLgEGGRRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 155 SGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAiADRVLVLEKGRVVE 234
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVE 549
|
250 260
....*....|....*....|.
gi 1331382268 235 QGTAPAVLRvpREDYTRQLLA 255
Cdd:COG4987 550 QGTHEELLA--QNGRYRQLYQ 568
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
274-508 |
2.68e-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: 120.69 E-value: 2.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFcsrsgwwGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAglseGR 353
Cdd:cd03263 1 LQIRNLTKTY-------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 LRALRSDVQMIFQdpFASLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIAR 433
Cdd:cd03263 70 RKAARQSLGYCPQ--FDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKA-NKRARTLSGGMKRKLSLAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 434 ALAVEPKVLIADECVSALDALIQVQILELLESLQRrfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:cd03263 147 ALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
19-258 |
2.80e-31 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 121.06 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 19 RSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSeeamrqLRGRDISMVFQEp 98
Cdd:TIGR00968 12 SFQALDDVNLEVPTGSLVALLGPSGSGKS----TLLRIIAGLEQPDSGRIRLNGQDATRVH------ARDRKIGFVFQH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 mSALNPLMRVGEQIDETLRAHGVAAARVRrQRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIAD 178
Cdd:TIGR00968 81 -YALFKHLTVRDNIAFGLEIRKHPKAKIK-ARVEELLELVQL---EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 179 EPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAAVS 258
Cdd:TIGR00968 156 EPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVN 235
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
295-502 |
3.42e-31 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 123.66 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglseGRLRALRSDVQMIFQDpfASLNP 374
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-----SRLHARDRKVGFVFQH--YALFR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTG----PLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSA 450
Cdd:PRK10851 88 HMTVFDNIAFGltvlPRRERPNAAAIKAKVTQLLEMVQLAHLA-DRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 451 LDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGrVVEQ 502
Cdd:PRK10851 167 LDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQG-NIEQ 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
291-502 |
4.29e-31 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 120.31 E-value: 4.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRS-DVQMIFQdpF 369
Cdd:PRK11629 18 GSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNqKLGFIYQ--F 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERfPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK11629 96 HHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 450 ALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLcDRIAVMRKGRVVEQ 502
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
23-254 |
4.31e-31 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 121.01 E-value: 4.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKAL-LRQLPDPLKVESGRLVFRDEDLADRSEEAMRQLRgRDISMVFQEpmSA 101
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInLLEQPEAGTIRVGDITIDTARSLSQQKGLIRQLR-QHVGFVFQN--FN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQIDE-----TLRAHGVAAARVRRqrvvdLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLI 176
Cdd:PRK11264 96 LFPHRTVLENIIEgpvivKGEPKEEATARARE-----LLAKVGLAGKET---SYPRRLSGGQQQRVAIARALAMRPEVIL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 177 ADEPTSALDVTTQAQILDLLRKIQQDKgMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLL 254
Cdd:PRK11264 168 FDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFL 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
25-501 |
1.02e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.18 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDplkveSGRLVFRdedladrseeamrqlRGRDISMVFQEP----- 98
Cdd:COG0488 16 DVSLSINPGDRIGLVGRNGAGKSTLLKILAGELePD-----SGEVSIP---------------KGLRIGYLPQEPplddd 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 -------MSALNPLMRVGEQIDETLRAHGVAAARVRRQ-----------------RVVDLLGYVGLPDPERLRlayPF-E 153
Cdd:COG0488 76 ltvldtvLDGDAELRALEAELEELEAKLAEPDEDLERLaelqeefealggweaeaRAEEILSGLGFPEEDLDR---PVsE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqqdKGmALLFITHDFAVVEAIADRVLVLEKGRV- 232
Cdd:COG0488 153 LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNY---PG-TVLVVSHDRYFLDRVATRILELDRGKLt 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 233 -------------------------------------VEQGTAPAVL------RVPREDYTRQLLAAVSAQPL---VPRT 266
Cdd:COG0488 229 lypgnysayleqraerleqeaaayakqqkkiakeeefIRRFRAKARKakqaqsRIKALEKLEREEPPRRDKTVeirFPPP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 267 QVAGPVVLKAEALGKVFCSRsgwwgrrttQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWlGrev 346
Cdd:COG0488 309 ERLGKKVLELEGLSKSYGDK---------TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-G--- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 347 aglsegrlralrSDVQMIF--QDpFASLNPRQTVGQIvmtgplVQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGG 424
Cdd:COG0488 376 ------------ETVKIGYfdQH-QEELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGG 436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 425 QRQRIGIARALAVEPKVLIADECVSALDaliqVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVE 501
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLD----IETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
294-513 |
1.05e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 1.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglSEGRLRALRSDVQMIFQDP----- 368
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEIRKKIGIIFQNPdnqfi 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 369 ---------FASLN---PRQTVGQIVMTGPLVQGVSKAdaerrarellglvglpaaaFERFPHEFSGGQRQRIGIARALA 436
Cdd:PRK13632 98 gatveddiaFGLENkkvPPKKMKDIIDDLAKKVGMEDY-------------------LDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 437 VEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRvAARLCDRIAVMRKGRVVEQGETAALFADAR 513
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD-EAILADKVIVFSEGKLIAQGKPKEILNNKE 234
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
22-237 |
1.07e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.48 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLpdpLKVESGRLVFRDEDLadrSEEAMRQLRGRdISMVFQEPMSA 101
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISK-ILTGL---LKPQSGEIKIDGITI---SKENLKEIRKK-IGIIFQNPDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LnplmrVGEQIDETLrAHGVAAARVRRQR----VVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:PRK13632 96 F-----IGATVEDDI-AFGLENKKVPPKKmkdiIDDLAKKVGM---EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAvvEAI-ADRVLVLEKGRVVEQGT 237
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMD--EAIlADKVIVFSEGKLIAQGK 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
298-503 |
1.22e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.88 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRL---RA-LRSDVQMIFqdPFasln 373
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrRAvLPQHSSLSF--PF---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 prqTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALA------VEPKVLIADEC 447
Cdd:PRK13548 92 ---TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLA-GRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 448 VSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:PRK13548 168 TSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADG 223
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
295-525 |
1.30e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 120.61 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGR-LRALRSDVQMIFQDPFASLN 373
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIKPVRKKVGVVFQFPESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 pRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:PRK13643 99 -EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 454 LIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMAEA 525
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLKAHELGVPKA 248
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
294-499 |
1.36e-30 |
|
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: 118.28 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDpfASLN 373
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFErFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:cd03292 91 PDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRA-LPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1331382268 454 LIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRV 499
Cdd:cd03292 170 DTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
274-503 |
2.23e-30 |
|
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: 117.77 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFcsrsgwwgrRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGR 353
Cdd:cd03269 1 LEVENVTKRF---------GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 LRALRSDvqmifqdpfASLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFpHEFSGGQRQRIGIAR 433
Cdd:cd03269 72 IGYLPEE---------RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRV-EELSKGNQQKVQFIA 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 434 ALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
297-523 |
3.76e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 118.26 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRlralrsdvQMIFQDpfASLNPRQ 376
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--------GVVFQN--EGLLPWR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGPLVQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQ 456
Cdd:PRK11248 86 NVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-EGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 457 VQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMR--KGRVVEQ-----------GETA-ALFADARHPYTRELLM 522
Cdd:PRK11248 165 EQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSpgPGRVVERlplnfarrfvaGESSrSIKSDPQFIAMREYVL 244
|
.
gi 1331382268 523 A 523
Cdd:PRK11248 245 S 245
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-254 |
4.20e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 117.55 E-value: 4.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 27 SLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAmrqlrgRDISMVFQEpmSALNPLM 106
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKS----TLLNLIAGFLPPDSGRILWNGQDLTALPPAE------RPVSMLFQE--NNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 107 RVGEQIDETLRAhGVAAARVRRQRVVDLLGYVGLPDPE-RLrlayPFELSGGQRQRVVIAMALAFDPALLIADEPTSALD 185
Cdd:COG3840 87 TVAQNIGLGLRP-GLKLTAEQRAQVEQALERVGLAGLLdRL----PGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 186 VTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLL 254
Cdd:COG3840 162 PALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-526 |
4.27e-30 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 123.36 E-value: 4.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMRQLrgrDISMVFQEpMS 100
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMK-VLSGIHEP---TKGTITINNINYNKLDHKLAAQL---GIGIIYQE-LS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPL-----MRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLP-DPERLRLaypfELSGGQRQRVVIAMALAFDPAL 174
Cdd:PRK09700 91 VIDELtvlenLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKvDLDEKVA----NLSISHKQMLEIAKTLMLDAKV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 175 LIADEPTSALdvtTQAQILDLLRKIQQDK--GMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAV-------LRVP 245
Cdd:PRK09700 167 IIMDEPTSSL---TNKEVDYLFLIMNQLRkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVsnddivrLMVG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 246 REDYTRqllaAVSAQPLVprTQVAGPVVLKAEALgkvfcsrsgwwGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLG 325
Cdd:PRK09700 244 RELQNR----FNAMKENV--SNLAHETVFEVRNV-----------TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 326 RCLVRLLRADSGRIEWLGREVAGLSEgrLRALRSDVQMIFQDP-----FASLNPRQTVG-----QIVMTGPLVQGVSKAD 395
Cdd:PRK09700 307 NCLFGVDKRAGGEIRLNGKDISPRSP--LDAVKKGMAYITESRrdngfFPNFSIAQNMAisrslKDGGYKGAMGLFHEVD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 396 AERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRlSIV 475
Cdd:PRK09700 385 EQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VIL 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 476 FITHDLRVAARLCDRIAVMRKGRVVEqgetaalFADARHPYTRELLMAEAI 526
Cdd:PRK09700 464 MVSSELPEIITVCDRIAVFCEGRLTQ-------ILTNRDDMSEEEIMAWAL 507
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
297-513 |
5.71e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 118.65 E-value: 5.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwlgreVAGLS---EGRLRALRSDVQMIFQDPfasln 373
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVY-----VDGLDtsdEENLWDIRNKAGMVFQNP----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMT----GPLVQGVSKADAERRARELLGLVGLpaAAFERF-PHEFSGGQRQRIGIARALAVEPKVLIADECV 448
Cdd:PRK13633 95 DNQIVATIVEEdvafGPENLGIPPEEIRERVDESLKKVGM--YEYRRHaPHLLSGGQKQRVAIAGILAMRPECIIFDEPT 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 449 SALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAALFADAR 513
Cdd:PRK13633 173 AMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEVE 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-247 |
7.08e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 118.58 E-value: 7.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDL-ADRSEEAMRQLRgRDISMVFQEPMS 100
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKS----TLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLR-KKVGIVFQFPEH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALnplmrvgeqIDETLRAH--------GVAAARVRrQRVVDLLGYVGLPdpERLRLAYPFELSGGQRQRVVIAMALAFDP 172
Cdd:PRK13634 97 QL---------FEETVEKDicfgpmnfGVSEEDAK-QKAREMIELVGLP--EELLARSPFELSGGQMRRVAIAGVLAMEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 173 ALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPRE 247
Cdd:PRK13634 165 EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDE 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
297-518 |
7.28e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 120.71 E-value: 7.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAglsegRLRALRSDVQMIFQDpfASLNPRQ 376
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-----HVPPYQRPINMMFQS--YALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALI- 455
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFA-KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLr 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 456 ---QVQILELLEslqrRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFadaRHPYTR 518
Cdd:PRK11607 186 drmQLEVVDILE----RVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---EHPTTR 244
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
23-251 |
1.50e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.53 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLpdpLKVESGRLVFRDEDLadrSEEAMRQLRgRDISMVFQEPMSAL 102
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVR-LIDGL---LEAESGQIIIDGDLL---TEENVWDIR-HKIGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 nplmrVGEQIDET----LRAHGVAAARVRrQRVVDLLGYVGLPDperLRLAYPFELSGGQRQRVVIAMALAFDPALLIAD 178
Cdd:PRK13650 95 -----VGATVEDDvafgLENKGIPHEEMK-ERVNEALELVGMQD---FKEREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 179 EPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVeAIADRVLVLEKGRVVEQGTapavlrvPREDYTR 251
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTST-------PRELFSR 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-237 |
1.89e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 122.20 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAMRQLrgrdISMVFQEPMsa 101
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYD----PTSGRILIDGVDIRDLTLESLRRQ----IGVVPQDTF-- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 lnpLMR--VGEQI--------DETLRAhgvAAARVRRQRVVDLL--GY---VGlpdpERLRlaypfELSGGQRQRVVIAM 166
Cdd:COG1132 425 ---LFSgtIRENIrygrpdatDEEVEE---AAKAAQAHEFIEALpdGYdtvVG----ERGV-----NLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 167 ALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAiADRVLVLEKGRVVEQGT 237
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
290-521 |
2.14e-29 |
|
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: 121.80 E-value: 2.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 290 WGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALrsdVQMIFQDP- 368
Cdd:COG4987 343 YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR---IAVVPQRPh 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 369 -FASlnprqTVGQIVMTGplvqgvsKADA-ERRARELLGLVGLpAAAFERFPH-----------EFSGGQRQRIGIARAL 435
Cdd:COG4987 420 lFDT-----TLRENLRLA-------RPDAtDEELWAALERVGL-GDWLAALPDgldtwlgeggrRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 436 AVEPKVLIADECVSALDALIQVQILE-LLESLQRRfrlSIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAALFadARH 514
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLAdLLEALAGR---TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELL--AQN 560
|
....*..
gi 1331382268 515 PYTRELL 521
Cdd:COG4987 561 GRYRQLY 567
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
273-506 |
3.42e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 115.56 E-value: 3.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSRSGWWGR-------------RTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRI 339
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSlkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 340 EWLGReVAGLSEgrlralrsdVQMIFqdpfaslNPRQTVGQ-IVMTGpLVQGVSKADAERRARELLGLVGLpaaafERFP 418
Cdd:COG1134 84 EVNGR-VSALLE---------LGAGF-------HPELTGREnIYLNG-RLLGLSRKEIDEKFDEIVEFAEL-----GDFI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 419 HE----FSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVM 494
Cdd:COG1134 141 DQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|..
gi 1331382268 495 RKGRVVEQGETA 506
Cdd:COG1134 220 EKGRLVMDGDPE 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
295-511 |
3.51e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 116.24 E-value: 3.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegRLRALRSDVQMIFQDPFASLNP 374
Cdd:PRK13644 15 TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKLVGIVFQNPETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RqTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFeRFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:PRK13644 93 R-TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRH-RSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 455 IQVQILELLESLQRRFRlSIVFITHDLRvAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK13644 171 SGIAVLERIKKLHEKGK-TIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSD 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-237 |
4.23e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.05 E-value: 4.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAgaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAK---ALLrqLPDPLKvESGRLVfrdeDLADRSE 80
Cdd:PRK13640 6 VEFKHVSFTYPD--SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKlinGLL--LPDDNP-NSKITV----DGITLTA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 EAMRQLRGRdISMVFQEPMSALnplmrVGEQIDETLrAHGVAAARVRRQR----VVDLLGYVGLPDPERlrlAYPFELSG 156
Cdd:PRK13640 77 KTVWDIREK-VGIVFQNPDNQF-----VGATVGDDV-AFGLENRAVPRPEmikiVRDVLADVGMLDYID---SEPANLSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 157 GQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfaVVEA-IADRVLVLEKGRVVEQ 235
Cdd:PRK13640 147 GQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHD--IDEAnMADQVLVLDDGKLLAQ 224
|
..
gi 1331382268 236 GT 237
Cdd:PRK13640 225 GS 226
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
38-249 |
5.01e-29 |
|
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: 117.21 E-value: 5.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 38 VVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAmrqlrgRDISMVFQEpmSALNPLMRVGEQIDETLR 117
Cdd:TIGR01187 1 LLGPSGCGKT----TLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL------RHINMVFQS--YALFPHMTVEENVAFGLK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 118 AHGVAAARvRRQRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLR 197
Cdd:TIGR01187 69 MRKVPRAE-IKPRVLEALRLVQL---EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 198 KIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTapavlrvPREDY 249
Cdd:TIGR01187 145 TIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGT-------PEEIY 189
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-236 |
5.64e-29 |
|
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: 113.74 E-value: 5.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDL--ADRSEeamrqlrgRDISMVFQEp 98
Cdd:cd03298 12 EQPMHFDLTFAQGEITAIVGPSGSGKS----TLLNLIAGFETPQSGRVLINGVDVtaAPPAD--------RPVSMLFQE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 mSALNPLMRVGEQIDETlRAHGVAAARVRRQRVVDLLGYVGLPDPERLRlayPFELSGGQRQRVVIAMALAFDPALLIAD 178
Cdd:cd03298 79 -NNLFAHLTVEQNVGLG-LSPGLKLTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 179 EPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
22-238 |
1.19e-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: 113.23 E-value: 1.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSeeamRQLRgRDISMVFQEPmsA 101
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKT----TTIKMLTTLLKPTSGRATVAGHDVVREP----REVR-RRIGIVFQDL--S 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPDpERLRLAYPFelSGGQRQRVVIAMALAFDPALLIADEPT 181
Cdd:cd03265 84 VDDELTGWENLYIHARLYGVPGAE-RRERIDELLDFVGLLE-AADRLVKTY--SGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 182 SALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTA 238
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-233 |
1.20e-28 |
|
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: 111.37 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKAL--LRQlPDplkveSGRLVFRDEDLADRSEEAMRQLRgrdISMVFQep 98
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILsgLYK-PD-----SGEILVDGKEVSFASPRDARRAG---IAMVYQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 msalnplmrvgeqidetlrahgvaaarvrrqrvvdllgyvglpdperlrlaypfeLSGGQRQRVVIAMALAFDPALLIAD 178
Cdd:cd03216 83 -------------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 179 EPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVV 233
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
292-500 |
1.46e-28 |
|
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: 112.35 E-value: 1.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAglsegrLRALRSDVQMIFQDPfas 371
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK------AKERRKSIGYVMQDV--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 372 lnPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSAL 451
Cdd:cd03226 81 --DYQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 452 DALIQVQILELLESLQRRFRLSIVfITHDLRVAARLCDRIAVMRKGRVV 500
Cdd:cd03226 158 DYKNMERVGELIRELAAQGKAVIV-ITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
17-238 |
2.34e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.69 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 17 ADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLrqlpDPLKVESGRLVFRDEDLADRSEEAMRQlrgrDISMVFQ 96
Cdd:PRK13648 19 SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMI----GIEKVKSGEIFYNNQAITDDNFEKLRK----HIGIVFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 97 EPMSALnplmrVGE--QIDET--LRAHGVAAARVRRqRVVDLLGYVGLPDperlRLAY-PFELSGGQRQRVVIAMALAFD 171
Cdd:PRK13648 91 NPDNQF-----VGSivKYDVAfgLENHAVPYDEMHR-RVSEALKQVDMLE----RADYePNALSGGQKQRVAIAGVLALN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAvvEAI-ADRVLVLEKGRVVEQGTA 238
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLS--EAMeADHVIVMNKGTVYKEGTP 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
297-512 |
2.53e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.69 E-value: 2.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglSEGRLRALRSDVQMIFQDPfaslnPRQ 376
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAI---TDDNFEKLRKHIGIVFQNP-----DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMT----GPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALD 452
Cdd:PRK13648 96 FVGSIVKYdvafGLENHAVPYDEMHRRVSEALKQVDMLERA-DYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 453 ALIQVQILELLESLQRRFRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAALFADA 512
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
296-511 |
4.31e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 113.56 E-value: 4.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREV-AGLSEGR-LRALRSDVQMIFQDPFASLN 373
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKeVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 pRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:PRK13645 105 -QETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK13645 184 KGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
295-511 |
4.57e-28 |
|
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: 111.76 E-value: 4.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGL-SEGRLR---ALRSDVQMIFqdpfa 370
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARagiGYVPEGRRIF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 slnPRQTVGQIVMTGplvqGVSKADAERRARellglvglPAAAFERFP--HEF--------SGGQRQRIGIARALAVEPK 440
Cdd:cd03224 88 ---PELTVEENLLLG----AYARRRAKRKAR--------LERVYELFPrlKERrkqlagtlSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 441 VLIADECVSALDALIQVQILELLESLqRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
297-511 |
4.84e-28 |
|
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: 111.94 E-value: 4.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPFASlnpRQ 376
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQIGLVSQDVFLF---ND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGplVQGVSKADAERRAREllglvglpAAAFE---RFPHEF-----------SGGQRQRIGIARALAVEPKVL 442
Cdd:cd03251 91 TVAENIAYG--RPGATREEVEEAARA--------ANAHEfimELPEGYdtvigergvklSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 443 IADECVSALDALIQVQILELLESLQRRfRLSIVfITHDLRVAARlCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKN-RTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-246 |
4.87e-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: 112.00 E-value: 4.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRialpAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSE 80
Cdd:COG0410 1 MPMLEVENLH----AGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP----PRSGSIRFDGEDITGLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 EAMRQLR------GRDIsmvFqepmsalnPLMRVgeqiDETLRA-----HGVAAARVRRQRVVDL---LGyvglpdpERL 146
Cdd:COG0410 73 HRIARLGigyvpeGRRI---F--------PSLTV----EENLLLgayarRDRAEVRADLERVYELfprLK-------ERR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 147 -RLAYpfELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVL 225
Cdd:COG0410 131 rQRAG--TLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAY 207
|
250 260
....*....|....*....|.
gi 1331382268 226 VLEKGRVVEQGTAPAVLRVPR 246
Cdd:COG0410 208 VLERGRIVLEGTAAELLADPE 228
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
295-502 |
5.66e-28 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 114.56 E-value: 5.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIeWLGREVAGLSEGRLRalrsDVQMIFQDpFAsLNP 374
Cdd:PRK11650 17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI-WIGGRVVNELEPADR----DIAMVFQN-YA-LYP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:PRK11650 90 HMSVRENMAYGLKIRGMPKAEIEERVAEAARILEL-EPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 455 IQVQI-LELLEsLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRvVEQ 502
Cdd:PRK11650 169 LRVQMrLEIQR-LHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV-AEQ 215
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
23-256 |
6.15e-28 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 112.20 E-value: 6.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSmlakALLR-----QLPDplkveSGRLVFRDEDL------------ADRSEeaMRQ 85
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKS----TFLRcinllETPD-----SGEIRVGGEEIrlkpdrdgelvpADRRQ--LQR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 86 LRGRdISMVFQEpmSALNPLMRVGEQIDET-LRAHGVAAARVRrQRVVDLLGYVGLPDperLRLAYPFELSGGQRQRVVI 164
Cdd:COG4598 93 IRTR-LGMVFQS--FNLWSHMTVLENVIEApVHVLGRPKAEAI-ERAEALLAKVGLAD---KRDAYPAHLSGGQQQRAAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 165 AMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRV 244
Cdd:COG4598 166 ARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGN 244
|
250
....*....|..
gi 1331382268 245 PREDYTRQLLAA 256
Cdd:COG4598 245 PKSERLRQFLSS 256
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
292-513 |
6.88e-28 |
|
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: 111.71 E-value: 6.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLgrclVRLLRAD-----SGRIEWLGREVAGLSegrLRALRSDVQMIFQ 366
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTL----LSLITGDlpptyGNDVRLFGERRGGED---VWELRKRIGLVSP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 367 DPFASLNPRQTVGQIVMTGP-----LVQGVSKADaERRARELLGLVGLPAAAFERFpHEFSGGQRQRIGIARALAVEPKV 441
Cdd:COG1119 86 ALQLRFPRDETVLDVVLSGFfdsigLYREPTDEQ-RERARELLELLGLAHLADRPF-GTLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 442 LIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADAR 513
Cdd:COG1119 164 LILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSEN 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
296-500 |
7.26e-28 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 111.12 E-value: 7.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDPFASLNpr 375
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 QTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALI 455
Cdd:PRK10908 94 RTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKA-KNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1331382268 456 QVQILELLESLQrRFRLSIVFITHDLRVAARLCDRIAVMRKGRVV 500
Cdd:PRK10908 173 SEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
22-247 |
9.04e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 112.49 E-value: 9.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAK---ALLrqLPdplkvESGRLVFRDEDLADrsEEAMRQLRGRdISMVFQEP 98
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKhmnALL--IP-----SEGKVYVDGLDTSD--EENLWDIRNK-AGMVFQNP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 MSALNPLMrVGEQI---DETLrahGVAAARVRrQRVVDLLGYVGLPDPERLRlayPFELSGGQRQRVVIAMALAFDPALL 175
Cdd:PRK13633 95 DNQIVATI-VEEDVafgPENL---GIPPEEIR-ERVDESLKKVGMYEYRRHA---PHLLSGGQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 176 IADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHdfAVVEAI-ADRVLVLEKGRVVEQGTapavlrvPRE 247
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITH--YMEEAVeADRIIVMDSGKVVMEGT-------PKE 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
23-255 |
1.04e-27 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 111.60 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKAL--LRQLPDPLKVESGRLV--FRDED--LADRSEEAMRQLRGRdISMVFQ 96
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCInfLEKPSEGSIVVNGQTInlVRDKDgqLKVADKNQLRLLRTR-LTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 97 E-----PMSALNPLMRVGEQIdetlraHGVAAARVRrQRVVDLLGYVGLPdpERLRLAYPFELSGGQRQRVVIAMALAFD 171
Cdd:PRK10619 100 HfnlwsHMTVLENVMEAPIQV------LGLSKQEAR-ERAVKYLAKVGID--ERAQGKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTR 251
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQ 249
|
....
gi 1331382268 252 QLLA 255
Cdd:PRK10619 250 QFLK 253
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
292-509 |
1.06e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 112.20 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglSEGRLRALRSDVQMIFQDPFAS 371
Cdd:PRK13652 14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPI---TKENIREVRKFVGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 372 L-NPrqTVGQIVMTGPLVQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSA 450
Cdd:PRK13652 91 IfSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 451 LDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALF 509
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIF 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
274-503 |
1.10e-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: 110.00 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFCSRsgwwgrrttQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGR 353
Cdd:cd03268 1 LKTNDLTKTYGKK---------RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 LRalrsdVQMIFQDPfaSLNPRQTVGQIVMTGPLVQGVSKADAErrarELLGLVGLPAAAFERFpHEFSGGQRQRIGIAR 433
Cdd:cd03268 72 RR-----IGALIEAP--GFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKV-KGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 434 ALAVEPKVLIADECVSALDALIQVQILELLESLqRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-246 |
1.28e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 112.25 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALPAGadrSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRlVFRDEDLADRSEE 81
Cdd:PRK13636 4 YILKVEELNYNYSDG---THALKGININIKKGEVTAILGGNGAGKS----TLFQNLNGILKPSSGR-ILFDGKPIDYSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRgRDISMVFQEPMSALNPlMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLpdpERLRLAYPFELSGGQRQR 161
Cdd:PRK13636 76 GLMKLR-ESVGMVFQDPDNQLFS-ASVYQDVSFGAVNLKLPEDEVRK-RVDNALKRTGI---EHLKDKPTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 162 VVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAV 241
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
250
....*....|....*.
gi 1331382268 242 -----------LRVPR 246
Cdd:PRK13636 230 faekemlrkvnLRLPR 245
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
295-517 |
1.47e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.16 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLR-----ADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPf 369
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMD---VIELRRRVQMVFQIP- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 aSLNPRQTVGQIVMTGPLVQGV--SKADAERRARELLGLVGLPAAAFERF---PHEFSGGQRQRIGIARALAVEPKVLIA 444
Cdd:PRK14247 92 -NPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 445 DECVSALDALIQVQILELLESLQRrfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYT 517
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
297-511 |
1.53e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.82 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADS---GRIEWLGREvagLSEGRLRALRSDVQMIFQDP---FA 370
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGIT---LTAKTVWDIREKVGIVFQNPdnqFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SlnprQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSA 450
Cdd:PRK13640 99 G----ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 451 LDALIQVQILELLESLQRRFRLSIVFITHDLRVAArLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
298-502 |
1.79e-27 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 110.25 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRS-DVQMIFQDPFasLNPRQ 376
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAkHVGFVFQSFM--LIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGPLVQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQ 456
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1331382268 457 VQILELLESLQRRFRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQ 502
Cdd:PRK10584 183 DKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
295-510 |
2.21e-27 |
|
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: 115.63 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlRALRSDVQMIFQDPFaslnp 374
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDP---ASWRRQIAWVPQNPY----- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 rqtvgqivmtgpLVQG-------VSKADA-ERRARELLGLVGLpaAAF-ERFPHEF-----------SGGQRQRIGIARA 434
Cdd:COG4988 422 ------------LFAGtirenlrLGRPDAsDEELEAALEAAGL--DEFvAALPDGLdtplgeggrglSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 435 LAVEPKVLIADECVSALDALIQVQILELLESLQRrfRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAALFA 510
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLA 560
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
274-503 |
2.75e-27 |
|
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: 109.20 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFcsrsgwwgrRTTQALDAVQLQLREGeTLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGlsegR 353
Cdd:cd03264 1 LQLENLTKRY---------GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK----Q 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 LRALRSDVQMIFQDPfaSLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERfPHEFSGGQRQRIGIAR 433
Cdd:cd03264 67 PQKLRRRIGYLPQEF--GVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKK-IGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 434 ALAVEPKVLIADECVSALDALIQVQILELLESL-QRRfrlSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgEDR---IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
296-513 |
3.27e-27 |
|
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: 109.69 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLS-------------EGRlralrsdvq 362
Cdd:COG0410 17 HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPphriarlgigyvpEGR--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 363 MIFqdpfaslnPRQTVGQIVMTGPLVQGVSKADAERRARellglvglpaaAFERFP--HEF--------SGGQRQRIGIA 432
Cdd:COG0410 88 RIF--------PSLTVEENLLLGAYARRDRAEVRADLER-----------VYELFPrlKERrrqragtlSGGEQQMLAIG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 433 RALAVEPKVLIADECVSALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADA 512
Cdd:COG0410 149 RALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP 227
|
.
gi 1331382268 513 R 513
Cdd:COG0410 228 E 228
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
262-511 |
4.48e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.48 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 262 LVPRTQVAGPVVLKAEALGKVFCSRSgwwgRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIeW 341
Cdd:PRK13631 10 LKVPNPLSDDIILRVKNLYCVFDEKQ----ENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-Q 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 342 LGREVAGLSEG--------------RLRALRSDVQMIFQDPFASLNpRQTVGQIVMTGPLVQGVSKADAERRARELLGLV 407
Cdd:PRK13631 85 VGDIYIGDKKNnhelitnpyskkikNFKELRRRVSMVFQFPEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 408 GLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVfITHDLRVAARL 487
Cdd:PRK13631 164 GLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHVLEV 242
|
250 260
....*....|....*....|....
gi 1331382268 488 CDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK13631 243 ADEVIVMDKGKILKTGTPYEIFTD 266
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-245 |
5.04e-27 |
|
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: 112.13 E-value: 5.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAMRQLRGRDISMVFQEpmSALNP 104
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKT----TLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQE--ARLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYvglpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSAL 184
Cdd:TIGR02142 89 HLSVRGNLRYGMKRARPSERRISFERVIELLGI------GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 185 DVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVP 245
Cdd:TIGR02142 163 DDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
294-523 |
5.76e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 109.74 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADS-----GRIEWLGREVaglSEGR--LRALRSDVQMIFQ 366
Cdd:PRK14258 19 TQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNI---YERRvnLNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 367 DPfaSLNPRQTVG------QIVMTGPLVQGVSKADAERRARELLGLVglpAAAFERFPHEFSGGQRQRIGIARALAVEPK 440
Cdd:PRK14258 96 KP--NLFPMSVYDnvaygvKIVGWRPKLEIDDIVESALKDADLWDEI---KHKIHKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 441 VLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVM-----RKGRVVEQGETAALFADARHP 515
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKKIFNSPHDS 250
|
....*...
gi 1331382268 516 YTRELLMA 523
Cdd:PRK14258 251 RTREYVLS 258
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-237 |
8.35e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 109.87 E-value: 8.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEA-MRQLRGRdISMVFQEPMS 100
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKS----TLIQNINALLKPTTGTVTVDDITITHKTKDKyIRPVRKR-IGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPlMRVGEQIDETLRAHGVAAARVRrQRVVDLLGYVGLPdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:PRK13646 97 QLFE-DTVEREIIFGPKNFKMNLDEVK-NYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGT 237
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTS 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
294-506 |
9.13e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 108.63 E-value: 9.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEG----RLRALRsdvqmifQDPf 369
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRelakRLAILR-------QEN- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 aSLNPRQTVGQIVMTG--PLVQG-VSKADAE--RRARELLGLVGLPaaafERFPHEFSGGQRQRIGIARALAVEPKVLIA 444
Cdd:COG4604 85 -HINSRLTVRELVAFGrfPYSKGrLTAEDREiiDEAIAYLDLEDLA----DRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 445 DECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETA 506
Cdd:COG4604 160 DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-228 |
1.00e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 107.57 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALpagadRSHALY-DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVeSGRLVFRDEDLADRSEEA 82
Cdd:COG4136 2 LSLENLTITL-----GGRPLLaPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSA-SGEVLLNGRRLTALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 mrqlrgRDISMVFQEPMsaLNPLMRVGEQIdetlrAHGVAAA---RVRRQRVVDLLGYVGLPDperLRLAYPFELSGGQR 159
Cdd:COG4136 76 ------RRIGILFQDDL--LFPHLSVGENL-----AFALPPTigrAQRRARVEQALEEAGLAG---FADRDPATLSGGQR 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 160 QRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAiADRVLVLE 228
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPA-AGRVLDLG 207
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
21-227 |
1.38e-26 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 106.93 E-value: 1.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAK--ALLRqlpdplKVESGRLVFRDEDLADRSEEAMRQLRGRDISMVFQep 98
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNiiGLLE------KFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQ-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 msalNPLMRVGEQIDETLR---AHGVAAARVRRQRVVDLLGYVGLpdpeRLRLA-YPFELSGGQRQRVVIAMALAFDPAL 174
Cdd:TIGR03608 84 ----NFALIENETVEENLDlglKYKKLSKKEKREKKKEALEKVGL----NLKLKqKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 175 LIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEaIADRVLVL 227
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDPEVAK-QADRVIEL 206
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-245 |
1.50e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.92 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGECLCVVGESGSGKSMLAkallRQLPDPLKVESGRLVFRDEDLADRSE-EAMRQLRGrdisMVFQ 96
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLA----LHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG----IVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 97 EPMSALnplmrVGEQIDETLrAHG-----VAAARVRRqRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFD 171
Cdd:PRK13644 85 NPETQF-----VGRTVEEDL-AFGpenlcLPPIEIRK-RVDRALAEIGL---EKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAiADRVLVLEKGRVVEQGTAPAVLRVP 245
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
298-504 |
1.54e-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: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLralrsdvqMIFQDpfASLNPRQT 377
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQN--YSLLPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 VGQIVMTG--PLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALI 455
Cdd:TIGR01184 71 VRENIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAA-DKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 456 QVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGE 504
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQ 198
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-245 |
1.62e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 110.56 E-value: 1.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEeamrqlRGRDISMVFQE 97
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKT----TLLRIIAGLEHQTSGHIRFHGTDVSRLHA------RDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 pmSALNPLMRVGEQIDETLRA---HGVAAARVRRQRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPAL 174
Cdd:PRK10851 83 --YALFRHMTVFDNIAFGLTVlprRERPNAAAIKAKVTQLLEMVQL---AHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 175 LIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVP 245
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
22-249 |
2.10e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.42 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAmrqlrgRDISMVFQEpmSA 101
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKT----TVLRLIAGFETPDSGRIMLDGQDITHVPAEN------RHVNTVFQS--YA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLPDPERLRlayPFELSGGQRQRVVIAMALAFDPALLIADEPT 181
Cdd:PRK09452 97 LFPHMTVFENVAFGLRMQKTPAAEITP-RVMEALRMVQLEEFAQRK---PHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 182 SALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTapavlrvPREDY 249
Cdd:PRK09452 173 SALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT-------PREIY 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
273-503 |
2.24e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 108.18 E-value: 2.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFcsrsgwwgrRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADS---GRIEWLGREV--A 347
Cdd:PRK09984 4 IIRVEKLAKTF---------NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVqrE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 348 GLSEGRLRALRSDVQMIFQDpFASLNpRQTVGQIVMTGPL---------VQGVSKADaERRARELLGLVGLPAAAFERFP 418
Cdd:PRK09984 75 GRLARDIRKSRANTGYIFQQ-FNLVN-RLSVLENVLIGALgstpfwrtcFSWFTREQ-KQRALQALTRVGMVHFAHQRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 419 hEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGR 498
Cdd:PRK09984 152 -TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGH 230
|
....*
gi 1331382268 499 VVEQG 503
Cdd:PRK09984 231 VFYDG 235
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-255 |
2.49e-26 |
|
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: 106.84 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRialpAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLaDRSEEAM 83
Cdd:TIGR03410 1 LEVSNLN----VYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLP----VKSGSIRLDGEDI-TKLPPHE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 RQLRGrdISMVFQEPMSAlnPLMRVGEQIdetlrahgvaaarvrrqrvvdLLGYVGLPDPERLRLAYPFE---------- 153
Cdd:TIGR03410 72 RARAG--IAYVPQGREIF--PRLTVEENL---------------------LTGLAALPRRSRKIPDEIYElfpvlkemlg 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 -----LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLE 228
Cdd:TIGR03410 127 rrggdLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVME 206
|
250 260
....*....|....*....|....*..
gi 1331382268 229 KGRVVEQGTAPAVlrvpREDYTRQLLA 255
Cdd:TIGR03410 207 RGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
303-508 |
2.67e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.98 E-value: 2.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 303 LQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIeWLgrevAGLSEGRLRALRSDVQMIFQDP--FASLNPRQTVGQ 380
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL-TL----NGQDHTTTPPSRRPVSMLFQENnlFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 381 IVMTGplvqgvSKADAERRA--RELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQ 458
Cdd:PRK10771 95 GLNPG------LKLNAAQREklHAIARQMGI-EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 459 ILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-512 |
3.16e-26 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 112.07 E-value: 3.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQlnRGECLCVVGESGSGKSMLAKALLR-QLPDplkveSGRLVFRDEDLADRSEEAMRQLrgrDISMVFQEPMsaLN 103
Cdd:PRK15439 31 DFTLH--AGEVHALLGGNGAGKSTLMKIIAGiVPPD-----SGTLEIGGNPCARLTPAKAHQL---GIYLVPQEPL--LF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 104 PLMRVGEQIdetlrAHGVAAARVRRQRVVDLLGYVGLpdpeRLRLAYPF-ELSGGQRQRVVIAMALAFDPALLIADEPTS 182
Cdd:PRK15439 99 PNLSVKENI-----LFGLPKRQASMQKMKQLLAALGC----QLDLDSSAgSLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 183 ALdvtTQAQILDLLRKIQ--QDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTA---------PAVLRVPREDYTR 251
Cdd:PRK15439 170 SL---TPAETERLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTadlstddiiQAITPAAREKSLS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 252 QLLAAVSAQPLVPRTQVAGPVVLKAEALgkvfcsrsgwwgrrTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRL 331
Cdd:PRK15439 247 ASQKLWLELPGNRRQQAAGAPVLTVEDL--------------TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 332 LRADSGRIEWLGREVAGLSEG-RLRA----LRSDVQM--IFQDPFASLNprqTVGQIVMTGPLVQgvskadaeRRAREll 404
Cdd:PRK15439 313 RPARGGRIMLNGKEINALSTAqRLARglvyLPEDRQSsgLYLDAPLAWN---VCALTHNRRGFWI--------KPARE-- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 405 glvglpAAAFERFPHE--------------FSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRf 470
Cdd:PRK15439 380 ------NAVLERYRRAlnikfnhaeqaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ- 452
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1331382268 471 RLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADA 512
Cdd:PRK15439 453 NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINVDT 494
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
23-233 |
3.45e-26 |
|
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: 105.80 E-value: 3.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKAL--LrqlpdpLKVESGRLVFRDEDLADRSeeamrqlRGRDISMVFQEPMS 100
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILagL------IKESSGSILLNGKPIKAKE-------RRKSIGYVMQDVDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNpLMRVGEQIDETLRAHGVAAARVRRqrVVDLLgyvglpDPERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:cd03226 83 QLF-TDSVREELLLGLKELDAGNEQAET--VLKDL------DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 181 TSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVV 233
Cdd:cd03226 154 TSGLDYKNMERVGELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
292-503 |
3.53e-26 |
|
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: 106.54 E-value: 3.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlRALRSDVQMIFQDPFas 371
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISR---KSLRSMIGVVLQDTF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 372 LNPRQTVGQIVMTGPLvqgvSKADAERRARELLGLV--------GLPAAAFERfPHEFSGGQRQRIGIARALAVEPKVLI 443
Cdd:cd03254 88 LFSGTIMENIRLGRPN----ATDEEVIEAAKEAGAHdfimklpnGYDTVLGEN-GGNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 444 ADECVSALD----ALIQVQILELLESlqrrfRLSIVfITHDLRVaARLCDRIAVMRKGRVVEQG 503
Cdd:cd03254 163 LDEATSNIDteteKLIQEALEKLMKG-----RTSII-IAHRLST-IKNADKILVLDDGKIIEEG 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
23-237 |
3.55e-26 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 106.82 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMRQLRGRDISMVFQepMSAL 102
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTP---TSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQ--FHHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPLMRVGEQIDETLRAHGVAAARVRrQRVVDLLGYVGLPDPERLRlayPFELSGGQRQRVVIAMALAFDPALLIADEPTS 182
Cdd:PRK11629 99 LPDFTALENVAMPLLIGKKKPAEIN-SRALEMLAAVGLEHRANHR---PSELSGGERQRVAIARALVNNPRLVLADEPTG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 183 ALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIaDRVLVLEKGRVVEQGT 237
Cdd:PRK11629 175 NLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELS 228
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
297-504 |
4.45e-26 |
|
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: 112.53 E-value: 4.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALrsdVQMIFQDPFaslnprq 376
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF---INYLPQEPY------- 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 tvgqiVMTGP----LVQGVSKADAERRARELLGLVGLpAAAFERFPHEF-----------SGGQRQRIGIARALAVEPKV 441
Cdd:TIGR01193 559 -----IFSGSilenLLLGAKENVSQDEIWAACEIAEI-KDDIENMPLGYqtelseegssiSGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 442 LIADECVSALDALIQVQILELLESLQRRfrlSIVFITHDLRVAARlCDRIAVMRKGRVVEQGE 504
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGS 691
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-526 |
4.90e-26 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 111.25 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKAL--LRQLpdplkvESGRLVFRDEDLA----DRSEEAmrqlrgrDISMVF 95
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLtgIYTR------DAGSILYLGKEVTfngpKSSQEA-------GIGIIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 QEpmsaLN--PLMRVGEQI---DETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAF 170
Cdd:PRK10762 86 QE----LNliPQLTIAENIflgREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVG---ELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 171 DPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVlrvpREDYT 250
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL----TEDSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 251 RQLLAAVSAQPLVPRTQVA-GPVVLKAEALgkvfcSRSGwwgrrttqaLDAVQLQLREGETLGIVGESGSGKSTLGRCLV 329
Cdd:PRK10762 234 IEMMVGRKLEDQYPRLDKApGEVRLKVDNL-----SGPG---------VNDVSFTLRKGEILGVSGLMGAGRTELMKVLY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 330 RLLRADSGRIEWLGREVAGLS--EGrlraLRSDVQMIFQDpfaslnpRQTVGqivmtgpLVQGVS--------------- 392
Cdd:PRK10762 300 GALPRTSGYVTLDGHEVVTRSpqDG----LANGIVYISED-------RKRDG-------LVLGMSvkenmsltalryfsr 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 393 -----KADAERRARE-LLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLEsl 466
Cdd:PRK10762 362 aggslKHADEQQAVSdFIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLIN-- 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 467 qrRFR---LSIVFITHDLRVAARLCDRIAVMRKGRVveQGETAAlfADArhpyTRELLMAEAI 526
Cdd:PRK10762 440 --QFKaegLSIILVSSEMPEVLGMSDRILVMHEGRI--SGEFTR--EQA----TQEKLMAAAV 492
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
296-510 |
5.34e-26 |
|
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: 106.16 E-value: 5.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDP--Fasln 373
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAIGVVPQDTvlF---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 pRQTVGQIVMTGPLvqGVSKADAERRARellglvglpAA----AFERFPHEF-----------SGGQRQRIGIARALAVE 438
Cdd:cd03253 88 -NDTIGYNIRYGRP--DATDEEVIEAAK---------AAqihdKIMRFPDGYdtivgerglklSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 439 PKVLIADECVSALDALIQVQILELLESLQRRfRLSIVfITHDLRVAARlCDRIAVMRKGRVVEQGETAALFA 510
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKG-RTTIV-IAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
281-503 |
5.85e-26 |
|
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: 105.69 E-value: 5.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 281 KVFCSRSGWWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGrlralrsd 360
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 361 vqmifqdpfASLNPRQTVGQ-IVMTGpLVQGVSKADAERRARELLGLVGLPAAAFERFPHeFSGGQRQRIGIARALAVEP 439
Cdd:cd03220 93 ---------GGFNPELTGREnIYLNG-RLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKT-YSSGMKARLAFAIATALEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 440 KVLIADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03220 162 DILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
16-253 |
5.91e-26 |
|
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: 106.03 E-value: 5.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 16 GADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVFRDEDLADRSEEAMRqlrgRDISMVF 95
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVP----ENGRVLVDGHDLALADPAWLR----RQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 QEP----------MSALNPLMRVgEQIDETLRAHGvAAARVRRQRvvdlLGY---VGlpdpERlrlayPFELSGGQRQRV 162
Cdd:cd03252 83 QENvlfnrsirdnIALADPGMSM-ERVIEAAKLAG-AHDFISELP----EGYdtiVG----EQ-----GAGLSGGQRQRI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQqdKGMALLFITHDFAVVEAiADRVLVLEKGRVVEQGTAPAVL 242
Cdd:cd03252 148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELL 224
|
250
....*....|.
gi 1331382268 243 RvpREDYTRQL 253
Cdd:cd03252 225 A--ENGLYAYL 233
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
25-231 |
6.81e-26 |
|
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: 104.87 E-value: 6.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVFRDEDLADRSEEAmrqlrGRDISMVFQEPmsALNP 104
Cdd:COG4133 20 GLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP----SAGEVLWNGEPIRDAREDY-----RRRLAYLGHAD--GLKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVGEQIDETLRAHGVAAARvrrQRVVDLLGYVGLPDPERLRLAYpfeLSGGQRQRVVIAMALAFDPALLIADEPTSAL 184
Cdd:COG4133 89 ELTVRENLRFWAALYGLRADR---EAIDEALEAVGLAGLADLPVRQ---LSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1331382268 185 DVTTQAQILDLLRKIQQDKGMALLfITHDfaVVEAIADRVLVLEKGR 231
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLL-TTHQ--PLELAAARVLDLGDFK 206
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-237 |
7.38e-26 |
|
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: 105.78 E-value: 7.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRqLPDplkVESGRLVFRDEDLADRSEEAMRqlrgRDISMVFQEpmsal 102
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFR-FYD---VSSGSILIDGQDIREVTLDSLR----RAIGVVPQD----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPLMrvgeqiDETLR---AHG---------VAAARVRR--QRVVDL-LGY---VGlpdpER-LRLaypfelSGGQRQRVV 163
Cdd:cd03253 84 TVLF------NDTIGyniRYGrpdatdeevIEAAKAAQihDKIMRFpDGYdtiVG----ERgLKL------SGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 164 IAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQqdKGMALLFITHDFAVVeAIADRVLVLEKGRVVEQGT 237
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGT 218
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
292-503 |
7.40e-26 |
|
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: 105.14 E-value: 7.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRsdvqmIFQDPFAs 371
Cdd:cd03266 15 KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG-----FVSDSTG- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 372 LNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSAL 451
Cdd:cd03266 89 LYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 452 DALIQVQILELLESLqRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03266 168 DVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-252 |
8.11e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 106.28 E-value: 8.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLP---DPLKVEsGRLVFRDEDLADRSEEAMRqlrgRDISMVFQEPm 99
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVD-GKVLYFGKDIFQIDAIKLR----KEVGMVFQQP- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 salNPL--MRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPF-ELSGGQRQRVVIAMALAFDPALLI 176
Cdd:PRK14246 100 ---NPFphLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPAsQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 177 ADEPTSALDVTTQAQILDLLRKIQQDkgMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQ 252
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
22-236 |
8.44e-26 |
|
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: 105.06 E-value: 8.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLR-QLPDplkveSGRLVFRDEDLADRSEEAMRQL---RGrdismvfqe 97
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPD-----SGEVLFDGKPLDIAARNRIGYLpeeRG--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 pmsaLNPLMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:cd03269 81 ----LYPKMKVIDQLVYLAQLKGLKKEEARR-RIDEWLERLELSEYANKRVE---ELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKiQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
290-499 |
9.79e-26 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.92 E-value: 9.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 290 WGRRTTqaLDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIewlgreVAGlsEGRLRALRSDVQMIFQDpf 369
Cdd:PRK11247 22 YGERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAG--TAPLAEAREDTRLMFQD-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASLNPRQTVGQIVMTGplvqgvSKADAERRARELLGLVGLPAAAFErFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK11247 90 ARLLPWKKVIDNVGLG------LKGQWRDAALQALAAVGLADRANE-WPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 450 ALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRV 499
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
297-510 |
1.32e-25 |
|
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: 105.26 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRAlrsDVQMIFQDpfASLNPRQ 376
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRR---QVGVVLQE--NVLFNRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGP------LVQGVSKADAERRAREL-LG---LVGLPAAAferfpheFSGGQRQRIGIARALAVEPKVLIADE 446
Cdd:cd03252 92 IRDNIALADPgmsmerVIEAAKLAGAHDFISELpEGydtIVGEQGAG-------LSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 447 CVSALDALIQVQILELLESLQRrfRLSIVFITHDLRvAARLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-235 |
1.38e-25 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 104.86 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAkALLRQLPDPlkvESGRLVFRDEDLADRSEEA 82
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLL-AILAGLDDG---SSGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLRGRDISMVFQEPM--SALNPLMRVgeQIDETLRAhgvAAARVRRQRVVDLLGYVGLPdpERLRlAYPFELSGGQRQ 160
Cdd:PRK10584 82 RAKLRAKHVGFVFQSFMliPTLNALENV--ELPALLRG---ESSRQSRNGAKALLEQLGLG--KRLD-HLPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 161 RVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfAVVEAIADRVLVLEKGRVVEQ 235
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD-LQLAARCDRRLRLVNGQLQEE 227
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
301-509 |
1.60e-25 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 107.81 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 301 VQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlrALRSdVQMIFQDpfASLNPRQTVGQ 380
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP----AERG-VGMVFQS--YALYPHLSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 381 IVMTGPLVQGVSKADAERR---ARELLGLvglpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQV 457
Cdd:PRK11000 95 NMSFGLKLAGAKKEEINQRvnqVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 458 QILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALF 509
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
16-243 |
2.32e-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: 103.74 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 16 GADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLpdpLKVESGRLVFRDEDLADRSEEAMRqlrgrDISMVF 95
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLK-MLTGE---LRPTSGTAYINGYSIRTDRKAARQ-----SLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 QEpmSALNPLMRVGEQIDETLRAHGVAAARVRRQrVVDLLGYVGLPDPeRLRLAypFELSGGQRQRVVIAMALAFDPALL 175
Cdd:cd03263 82 QF--DALFDELTVREHLRFYARLKGLPKSEIKEE-VELLLRVLGLTDK-ANKRA--RTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 176 IADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAIADRVLVLEKGRVVEQGTaPAVLR 243
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGS-PQELK 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
298-512 |
3.21e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.17 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREvagLSEGRLRALRSDVQMIFQDPFASLnPRQT 377
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGEL---LTAENVWNLRRKIGMVFQNPDNQF-VGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 VGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQV 457
Cdd:PRK13642 99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFK-TREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 458 QILELLESLQRRFRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAALFADA 512
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATS 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
285-500 |
3.74e-25 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 109.43 E-value: 3.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 285 SRSGWWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSD-VQM 363
Cdd:PRK10535 11 RRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 364 IFQDpfASLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLI 443
Cdd:PRK10535 91 IFQR--YHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 444 ADECVSALDALIQVQILELLESLQRRFRLSIVfITHDLRVAARlCDRIAVMRKGRVV 500
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAAQ-AERVIEIRDGEIV 222
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
295-508 |
4.40e-25 |
|
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: 103.37 E-value: 4.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLS-EGRLRALRSDV---QMIFqdpfa 370
Cdd:TIGR03410 13 SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPpHERARAGIAYVpqgREIF----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 slnPRQTVGQIVMTGplvqgvskadAERRARellGLVGLPAAAFERFP--HEF--------SGGQRQRIGIARALAVEPK 440
Cdd:TIGR03410 88 ---PRLTVEENLLTG----------LAALPR---RSRKIPDEIYELFPvlKEMlgrrggdlSGGQQQQLAIARALVTRPK 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 441 VLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
16-237 |
4.53e-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: 103.46 E-value: 4.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 16 GADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRqLPDPlkvESGRLVFRDEDLADRSeeaMRQLRgRDISMVF 95
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPR-FYDV---DSGRILIDGHDVRDYT---LASLR-RQIGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 QEPMsalnplmrvgeQIDETLR------AHGVAAARVRRQ-RVVDLLGYV-GLPD------PERlrlayPFELSGGQRQR 161
Cdd:cd03251 83 QDVF-----------LFNDTVAeniaygRPGATREEVEEAaRAANAHEFImELPEgydtviGER-----GVKLSGGQRQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 162 VVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAiADRVLVLEKGRVVEQGT 237
Cdd:cd03251 147 IAIARALLKDPPILILDEATSALDTESERLVQAALERLMKNR--TTFVIAHRLSTIEN-ADRIVVLEDGKIVERGT 219
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-257 |
6.01e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.94 E-value: 6.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALpaGADRshALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEe 81
Cdd:PRK11231 1 MTLRTENLTVGY--GTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLL----TPQSGTVFLGDKPISMLSS- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 amRQLrGRDISMVFQEPMSAlnplmrvgEQID-ETLRAHGvaaarvrRQRVVDLLGYVGLPDPERLRLAYP--------- 151
Cdd:PRK11231 72 --RQL-ARRLALLPQHHLTP--------EGITvRELVAYG-------RSPWLSLWGRLSAEDNARVNQAMEqtrinhlad 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 152 ---FELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLE 228
Cdd:PRK11231 134 rrlTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRYCDHLVVLA 212
|
250 260
....*....|....*....|....*....
gi 1331382268 229 KGRVVEQGTapavlrvPREDYTRQLLAAV 257
Cdd:PRK11231 213 NGHVMAQGT-------PEEVMTPGLLRTV 234
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
22-261 |
6.16e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.70 E-value: 6.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAkallrQLPDPLKV-ESGRLVFRDEDLAD--RSEEAMRQLRgRDISMVFQEP 98
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMI-----QLTNGLIIsETGQTIVGDYAIPAnlKKIKEVKRLR-KEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 MSALnplmrVGEQIDETLrAHGVAAARVRRQ----RVVDLLGYVGLPDPERLRlaYPFELSGGQRQRVVIAMALAFDPAL 174
Cdd:PRK13645 100 EYQL-----FQETIEKDI-AFGPVNLGENKQeaykKVPELLKLVQLPEDYVKR--SPFELSGGQKRRVALAGIIAMDGNT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 175 LIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTapavlrvPREDYTRQ-L 253
Cdd:PRK13645 172 LVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS-------PFEIFSNQeL 244
|
....*...
gi 1331382268 254 LAAVSAQP 261
Cdd:PRK13645 245 LTKIEIDP 252
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-233 |
7.64e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 103.63 E-value: 7.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAG-ADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEA 82
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLP----PDSGSILIDGKDVTKLPEYK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 mrqlRGRDISMVFQEPMSALNPLMrvgeQIDETL---------RAHGVAAARVRRQRVVDLLGYV--GLPDperlRLAYP 151
Cdd:COG1101 78 ----RAKYIGRVFQDPMMGTAPSM----TIEENLalayrrgkrRGLRRGLTKKRRELFRELLATLglGLEN----RLDTK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 152 FE-LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAvvEAIA--DRVLVLE 228
Cdd:COG1101 146 VGlLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNME--QALDygNRLIMMH 223
|
....*
gi 1331382268 229 KGRVV 233
Cdd:COG1101 224 EGRII 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
292-510 |
1.12e-24 |
|
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: 102.62 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDP--F 369
Cdd:cd03249 13 RPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRSQIGLVSQEPvlF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASlnprqTVGQ-IVMTGPlvqGVSKADAERRAREllglvglpAAAFE---RFPHEF-----------SGGQRQRIGIARA 434
Cdd:cd03249 90 DG-----TIAEnIRYGKP---DATDEEVEEAAKK--------ANIHDfimSLPDGYdtlvgergsqlSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 435 LAVEPKVLIADECVSALDALIQVQILELLESLqRRFRLSIVfITHDLRvAARLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQEALDRA-MKGRTTIV-IAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
289-521 |
1.13e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 103.00 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 289 WWGRrtTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRAD-----SGRIEWLGREVAGLSEGRLRaLRSDVQM 363
Cdd:PRK14267 13 YYGS--NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIE-VRREVGM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 364 IFQ--DPFASLNPRQTVGQIVMTGPLVQgvSKADAERRARELLGLVGLPAAAFER---FPHEFSGGQRQRIGIARALAVE 438
Cdd:PRK14267 90 VFQypNPFPHLTIYDNVAIGVKLNGLVK--SKKELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 439 PKVLIADECVSALDALIQVQILELLESLQRRFrlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTR 518
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245
|
...
gi 1331382268 519 ELL 521
Cdd:PRK14267 246 KYV 248
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-522 |
1.19e-24 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 107.18 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLakallrqlpdpLKVESG---------RLVFRDE-----DLADrSEEamrqlr 87
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTL-----------MKVLSGvyphgsyegEILFDGEvcrfkDIRD-SEA------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 88 gRDISMVFQEpmSALNPLMRVGEQI---DETLRaHGVAAARVRRQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVI 164
Cdd:NF040905 78 -LGIVIIHQE--LALIPYLSIAENIflgNERAK-RGVIDWNETNRRARELLAKVGLDESPDTLVT---DIGVGKQQLVEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 165 AMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEqgtapaVLRV 244
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKA-QGITSIIISHKLNEIRRVADSITVLRDGRTIE------TLDC 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 245 PREDYT----------RQLlaavsAQPLVPRTQVAGPVVLKAEalgkvfcsrsGWW----GRRTTQALDAVQLQLREGET 310
Cdd:NF040905 224 RADEVTedriirgmvgRDL-----EDRYPERTPKIGEVVFEVK----------NWTvyhpLHPERKVVDDVSLNVRRGEI 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 311 LGIVGESGSGK-----STLGRCLVRLLradSGRIEWLGREVaglsegRLR----ALRSDVQMIFQDpfaslnpRQTVGQI 381
Cdd:NF040905 289 VGIAGLMGAGRtelamSVFGRSYGRNI---SGTVFKDGKEV------DVStvsdAIDAGLAYVTED-------RKGYGLN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 382 VM-------TGPLVQGVSKADAERRARELlglvglpaAAFERFPHEF--------------SGGQRQRIGIARALAVEPK 440
Cdd:NF040905 353 LIddikrniTLANLGKVSRRGVIDENEEI--------KVAEEYRKKMniktpsvfqkvgnlSGGNQQKVVLSKWLFTDPD 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 441 VLIADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVeqGETAAlfADArhpyTREL 520
Cdd:NF040905 425 VLILDEPTRGIDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRIT--GELPR--EEA----SQER 495
|
..
gi 1331382268 521 LM 522
Cdd:NF040905 496 IM 497
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-237 |
1.26e-24 |
|
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: 102.23 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRqLPDPLkveSGRLVFRDEDLadrSEEAMRQLRGRdISMVFQEPMSAL 102
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLER-FYDPT---SGEILLDGVDI---RDLNLRWLRSQ-IGLVSQEPVLFD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPLM------RVGEQIDETLRAHGVAAARvrrqrvvDLLgyVGLPDPERLRL-AYPFELSGGQRQRVVIAMALAFDPALL 175
Cdd:cd03249 91 GTIAenirygKPDATDEEVEEAAKKANIH-------DFI--MSLPDGYDTLVgERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 176 IADEPTSALDVTTQAQILDLLRKIQqdKGMALLFITHDFAVVEAiADRVLVLEKGRVVEQGT 237
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAM--KGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-241 |
1.46e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.29 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSE-EAMRQLRgRDISMVFQEPMS 100
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQ-LLNGLHVP---TQGSVRVDDTLITSTSKnKDIKQIR-KKVGLVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALnplmrvgeqIDETL--------RAHGVA---AARVRRQRvvdlLGYVGLPdpERLRLAYPFELSGGQRQRVVIAMALA 169
Cdd:PRK13649 97 QL---------FEETVlkdvafgpQNFGVSqeeAEALAREK----LALVGIS--ESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 170 FDPALLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAV 241
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
253-510 |
1.84e-24 |
|
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: 107.35 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 253 LLAAVSAQPLVPRTQ--------VAGPVVLKAEALGKVFCSR-SGWWGRRTTQALDAVQLQLREGETLGIVGESGSGKST 323
Cdd:TIGR03797 415 LISILAVIPLWERAKpilealpeVDEAKTDPGKLSGAIEVDRvTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKST 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 324 LGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDpfASLNPRQTVGQIVMTGPLVQgvskadaeRRAREL 403
Cdd:TIGR03797 495 LLRLLLGFETPESGSVFYDGQDLAGLD---VQAVRRQLGVVLQN--GRLMSGSIFENIAGGAPLTL--------DEAWEA 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 404 LGLVGLpAAAFERFP---H--------EFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQrrfrL 472
Cdd:TIGR03797 562 ARMAGL-AEDIRAMPmgmHtvisegggTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK----V 636
|
250 260 270
....*....|....*....|....*....|....*...
gi 1331382268 473 SIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAALFA 510
Cdd:TIGR03797 637 TRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMA 673
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
303-503 |
1.90e-24 |
|
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: 101.03 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 303 LQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRlralrSDVQMIFQDP--FASLNPRQTVGQ 380
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQENnlFAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 381 IVMTGPLVQGVSKADAERRARELlGLVGLPAaafeRFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQIL 460
Cdd:cd03298 94 GLSPGLKLTAEDRQAIEVALARV-GLAGLEK----RLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1331382268 461 ELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03298 169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
296-519 |
1.99e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 102.16 E-value: 1.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRL--LRAD---SGRIEWLGREVAGLSEGRLRaLRSDVQMIFQDPfa 370
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSPRTDTVD-LRKEIGMVFQQP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 slNP-RQTVGQIVMTGPLVQGVSKADAERRARELlGLVGlpAAAFERFP---HE----FSGGQRQRIGIARALAVEPKVL 442
Cdd:PRK14239 96 --NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEK-SLKG--ASIWDEVKdrlHDsalgLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 443 IADECVSALDALIQVQILELLESLQRRFrlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRE 519
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETED 245
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
298-523 |
2.09e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 102.43 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRA-DS-----GRIEWLGREVAGLSEGRLRalrSDVQMIFQ--DPF 369
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSkikvdGKVLYFGKDIFQIDAIKLR---KEVGMVFQqpNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASLNPRQTVGQIVMTgplvQGVS-KADAERRARELLGLVGLPAAAFERF---PHEFSGGQRQRIGIARALAVEPKVLIAD 445
Cdd:PRK14246 103 PHLSIYDNIAYPLKS----HGIKeKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 446 ECVSALDALIQVQILELLESLQRrfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYTRELLMA 523
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYVIG 254
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-234 |
2.63e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 102.09 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAgadrSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEa 82
Cdd:PRK11248 1 MLQISHLYADYGG----KPALEDINLTLESGELLVVLGPSGCGKT----TLLNLIAGFVPYQHGSITLDGKPVEGPGAE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 mrqlRGrdisMVFQEpmSALNPLMRVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRV 162
Cdd:PRK11248 72 ----RG----VVFQN--EGLLPWRNVQDNVAFGLQLAGVEKMQ-RLEIAHQMLKKVGLEGAEK---RYIWQLSGGQRQRV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDF--AVVEAIADRVLVLEKGRVVE 234
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIeeAVFMATELVLLSPGPGRVVE 211
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-237 |
2.72e-24 |
|
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: 101.15 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRqLPDPlkvESGRLVFRDEDLADRSEEAMRQLrgrdISMVFQEP-- 98
Cdd:cd03254 17 PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMR-FYDP---QKGQILIDGIDIRDISRKSLRSM----IGVVLQDTfl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 ----------MSALNPLMRVGEQIDETLRAHgvaaaRVRRQRVVDLLGYVGlpdpERLRLaypfeLSGGQRQRVVIAMAL 168
Cdd:cd03254 89 fsgtimenirLGRPNATDEEVIEAAKEAGAH-----DFIMKLPNGYDTVLG----ENGGN-----LSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 169 AFDPALLIADEPTSALDVTTQAQILDLLRKIQqdKGMALLFITHDFAVVEAiADRVLVLEKGRVVEQGT 237
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGT 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
298-510 |
5.58e-24 |
|
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: 105.98 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGrlrALRSDVQMIFQDPFasLNPRQT 377
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPA---WLRRQMGVVLQENV--LFSRSI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 VGQIVMTGPlvqgvskADAERRARELLGLVGlpAAAF-ERFPHEF-----------SGGQRQRIGIARALAVEPKVLIAD 445
Cdd:TIGR01846 548 RDNIALCNP-------GAPFEHVIHAAKLAG--AHDFiSELPQGYntevgekganlSGGQRQRIAIARALVGNPRILIFD 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 446 ECVSALDALIQVQILELLESLQRrfRLSIVFITHDLRvAARLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:TIGR01846 619 EATSALDYESEALIMRNMREICR--GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLA 680
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
297-503 |
6.27e-24 |
|
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: 99.88 E-value: 6.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPFaslnprq 376
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSRISIIPQDPV------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 tvgqiVMTG-------PLVQgvsKADAE-RRARELLGLVGLPAAAFERFPHE-------FSGGQRQRIGIARALAVEPKV 441
Cdd:cd03244 89 -----LFSGtirsnldPFGE---YSDEElWQALERVGLKEFVESLPGGLDTVveeggenLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 442 LIADECVSALD----ALIQvqilellESLQRRFR-LSIVFITHdlrvaaRL-----CDRIAVMRKGRVVEQG 503
Cdd:cd03244 161 LVLDEATASVDpetdALIQ-------KTIREAFKdCTVLTIAH------RLdtiidSDRILVLDKGRVVEFD 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-508 |
6.46e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 105.98 E-value: 6.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGeCLC-VVGESGSGKSMLAkALL---RqlpdplKVESGRLVFRDEDLADRSEEA--------MRQLRG 88
Cdd:NF033858 15 VALDDVSLDIPAG-CMVgLIGPDGVGKSSLL-SLIagaR------KIQQGRVEVLGGDMADARHRRavcpriayMPQGLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 89 RDismvfqepmsaLNPLMRVGEQID--ETLRAHGvaaARVRRQRVVDLLGYVGLpDPERLRLAYpfELSGGQRQRVVIAM 166
Cdd:NF033858 87 KN-----------LYPTLSVFENLDffGRLFGQD---AAERRRRIDELLRATGL-APFADRPAG--KLSGGMKQKLGLCC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 167 ALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDK-GMALLFIThdfAVVEAIA--DRVLVLEKGRVVEQGTAPAVLR 243
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpGMSVLVAT---AYMEEAErfDWLVAMDAGRVLATGTPAELLA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 244 --------------VPREDytRQLLAAVSAQPLVPRTqvAGPVVLKAEALGKVFcsrsgwwGRRTtqALDAVQLQLREGE 309
Cdd:NF033858 227 rtgadtleaafialLPEEK--RRGHQPVVIPPRPADD--DDEPAIEARGLTMRF-------GDFT--AVDHVSFRIRRGE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 310 TLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglsEGRLRALRSDVQMIFQdPFaSLNPRQTVGQ-IVMTGPLV 388
Cdd:NF033858 294 IFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV----DAGDIATRRRVGYMSQ-AF-SLYGELTVRQnLELHARLF 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 389 QgVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQR 468
Cdd:NF033858 368 H-LPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSR 445
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1331382268 469 RFRLSIvFI-THDLRVAARlCDRIAVMRKGRVVEQGETAAL 508
Cdd:NF033858 446 EDGVTI-FIsTHFMNEAER-CDRISLMHAGRVLASDTPAAL 484
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
25-242 |
6.92e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 100.54 E-value: 6.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplKVESGRLVFRDEDladRSEEAMRQLRGR------DISMVFQEP 98
Cdd:COG1119 21 DISWTVKPGEHWAILGPNGAGKSTLLSLITGDLP---PTYGNDVRLFGER---RGGEDVWELRKRiglvspALQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 MSALNPL-------MRVGEQIDETLRahgvaaarvrrQRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFD 171
Cdd:COG1119 95 ETVLDVVlsgffdsIGLYREPTDEQR-----------ERARELLELLGL---AHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfavVEAIAD---RVLVLEKGRVVEQGTAPAVL 242
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIPPgitHVLLLKDGRVVAAGPKEEVL 231
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
303-505 |
7.06e-24 |
|
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: 99.55 E-value: 7.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 303 LQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwlgreVAGLSEGRLRALRSDVQMIFQDP--FASLNPRQTVGQ 380
Cdd:TIGR01277 19 LNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIK-----VNDQSHTGLAPYQRPVSMLFQENnlFAHLTVRQNIGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 381 IVMTGPLVQGVSKADAERRAREllglVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQIL 460
Cdd:TIGR01277 94 GLHPGLKLNAEQQEKVVDAAQQ----VGI-ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEML 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1331382268 461 ELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGET 505
Cdd:TIGR01277 169 ALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVSDC 213
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
19-237 |
7.22e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 105.43 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 19 RSHALYDLSLQLNRGECLCVVGESGSGKSMLAkALLRQLPDPlkvESGRLVFRDEDLADRSEEAMRqlrgRDISMVFQEP 98
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRVFDP---QSGRILIDGTDIRTVTRASLR----RNIAVVFQDA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 M---SALNPLMRVGEQ--IDETLRAHGVAAAR---VRRQrvvdLLGY---VGlpdpERLRlaypfELSGGQRQRVVIAMA 167
Cdd:PRK13657 419 GlfnRSIEDNIRVGRPdaTDEEMRAAAERAQAhdfIERK----PDGYdtvVG----ERGR-----QLSGGERQRLAIARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 168 LAFDPALLIADEPTSALDVTTQAQI---LDLLRkiqqdKGMALLFITHDFAVVEAiADRVLVLEKGRVVEQGT 237
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVkaaLDELM-----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
18-258 |
9.80e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.99 E-value: 9.80e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAmrqlrgRDISMVFQE 97
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKS----TLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ------RPINMMFQS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 pmSALNPLMRVGEQIDETLRAHGVAAARVRrQRVVDLLGYVGLPDPERLRlayPFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:PRK11607 100 --YALFPHMTVEQNIAFGLKQDKLPKAEIA-SRVNEMLGLVHMQEFAKRK---PHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 178 DEPTSALDVT----TQAQILDLLRKIqqdkGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQL 253
Cdd:PRK11607 174 DEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEF 249
|
....*
gi 1331382268 254 LAAVS 258
Cdd:PRK11607 250 IGSVN 254
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
272-519 |
1.05e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.63 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 272 VVLKAEALgkvfcsrSGWWGRRTtqALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRL------LRADsGRIEWLGRE 345
Cdd:PRK14243 9 TVLRTENL-------NVYYGSFL--AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVE-GKVTFHGKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 346 VAGlSEGRLRALRSDVQMIFQDPfaslNP-RQTVGQIVMTGPLVQGVsKAD----AERRAREllglvglpAAAFERFPHE 420
Cdd:PRK14243 79 LYA-PDVDPVEVRRRIGMVFQKP----NPfPKSIYDNIAYGARINGY-KGDmdelVERSLRQ--------AALWDEVKDK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 421 F-------SGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFrlSIVFITHDLRVAARLCDRIAV 493
Cdd:PRK14243 145 LkqsglslSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAF 222
|
250 260 270
....*....|....*....|....*....|....*
gi 1331382268 494 M---------RKGRVVEQGETAALFADARHPYTRE 519
Cdd:PRK14243 223 FnveltegggRYGYLVEFDRTEKIFNSPQQQATRD 257
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
23-241 |
1.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 1.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDL-ADRSEEAMRQLRgRDISMVFQEPMSA 101
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKS----TLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQFPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 L--NPLMrvgEQIDETLRAHGVAAARVRRQrVVDLLGYVGLPdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:PRK13641 98 LfeNTVL---KDVEFGPKNFGFSEDEAKEK-ALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAV 241
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQK-AGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEI 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-500 |
1.32e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 103.84 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALL-RQLPDplkveSGRLVFRdedladrsEEAMRQLRGRD-----ISMVF 95
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSgNYQPD-----AGSILID--------GQEMRFASTTAalaagVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 QEpmSALNPLMRVGEQI--DETLRAHGVAAARVRRQRVVDLLGYVGLP-DPERlRLAYpfeLSGGQRQRVVIAMALAFDp 172
Cdd:PRK11288 86 QE--LHLVPEMTVAENLylGQLPHKGGIVNRRLLNYEAREQLEHLGVDiDPDT-PLKY---LSIGQRQMVEIAKALARN- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 173 ALLIA-DEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEqgTAPAVLRVPREdytr 251
Cdd:PRK11288 159 ARVIAfDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA--TFDDMAQVDRD---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 252 QLLAAVSAQPLV------PRTQvaGPVVLKAEALGkvfcsrsgwwGRRTTQaldAVQLQLREGETLGIVGESGSGKSTLG 325
Cdd:PRK11288 232 QLVQAMVGREIGdiygyrPRPL--GEVRLRLDGLK----------GPGLRE---PISFSVRAGEIVGLFGLVGAGRSELM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 326 RCLVRLLRADSGRIEWLGREVaglsegrlrALRSdvqmifqdpfaslnPRQTVGQIVMTGP-------LVQGVSKAD--- 395
Cdd:PRK11288 297 KLLYGATRRTAGQVYLDGKPI---------DIRS--------------PRDAIRAGIMLCPedrkaegIIPVHSVADnin 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 396 -AERRARELLGLV---GLPAAAFERF--------PH------EFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQV 457
Cdd:PRK11288 354 iSARRHHLRAGCLinnRWEAENADRFirslniktPSreqlimNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKH 433
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1331382268 458 QILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVV 500
Cdd:PRK11288 434 EIYNVIYELAAQGV-AVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-236 |
1.32e-23 |
|
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: 97.77 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 20 SHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADrSEEAMRQLrgrdISMVFQEPM 99
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDL----KPQQGEITLDGVPVSD-LEKALSSL----ISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 salnplmrvgeQIDETLRAHgvaaarvrrqrvvdllgyVGLPdperlrlaypfeLSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:cd03247 86 -----------LFDTTLRNN------------------LGRR------------FSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAiADRVLVLEKGRVVEQG 236
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEH-MDKILFLENGKIIMQG 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
297-503 |
1.52e-23 |
|
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: 98.82 E-value: 1.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDP---FASLn 373
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRRNIGYVPQDVtlfYGTL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 pRQtvgQIVMTGPLvqgvskADAER--RARELLGL---VGLPAAAFERFPHE----FSGGQRQRIGIARALAVEPKVLIA 444
Cdd:cd03245 95 -RD---NITLGAPL------ADDERilRAAELAGVtdfVNKHPNGLDLQIGErgrgLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 445 DECVSALDALIQVQILELLESLQRrfRLSIVFITHDLRVAArLCDRIAVMRKGRVVEQG 503
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
298-517 |
1.67e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 100.17 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRA-----DSGRIEWLGREVAGLSEgrLRALRSDVQMIFQDPfasl 372
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRD--VLEFRRRVGMLFQRP---- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 373 NP-RQTVGQIVMTGPLVQG-VSKADAERRARELLGLVGLPAAAFERF---PHEFSGGQRQRIGIARALAVEPKVLIADEC 447
Cdd:PRK14271 111 NPfPMSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 448 VSALDALIQVQILELLESLQRrfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADARHPYT 517
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-265 |
1.91e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLadrSEEAMRQLRgRDISMVFQEPMS 100
Cdd:PRK13652 18 EALNNINFIAPRNSRIAVIGPNGAGKS----TLFRHFNGILKPTSGSVLIRGEPI---TKENIREVR-KFVGLVFQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 -----------ALNPlmrVGEQIDETLRAHgvaaarvrrqRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALA 169
Cdd:PRK13652 90 qifsptveqdiAFGP---INLGLDEETVAH----------RVSSALHMLGL---EELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 170 FDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTapavlrvPREDY 249
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT-------VEEIF 226
|
250
....*....|....*...
gi 1331382268 250 TR-QLLAAVSAQ-PLVPR 265
Cdd:PRK13652 227 LQpDLLARVHLDlPSLPK 244
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
291-510 |
2.51e-23 |
|
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: 103.63 E-value: 2.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlRALRSDVQMIFQDP-- 368
Cdd:TIGR02204 349 ARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP---AELRARMALVPQDPvl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 369 -FASLNPRQTVGQIVMTGPLVQGVSKAdaeRRARELLGlvGLPAAaFERFPHE----FSGGQRQRIGIARALAVEPKVLI 443
Cdd:TIGR02204 426 fAASVMENIRYGRPDATDEEVEAAARA---AHAHEFIS--ALPEG-YDTYLGErgvtLSGGQRQRIAIARAILKDAPILL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 444 ADECVSALDALIQVQILELLESLQRRfRLSIVfITHdlRVAARL-CDRIAVMRKGRVVEQGETAALFA 510
Cdd:TIGR02204 500 LDEATSALDAESEQLVQQALETLMKG-RTTLI-IAH--RLATVLkADRIVVMDQGRIVAQGTHAELIA 563
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
295-508 |
2.73e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlRALRSDVQMIFQDpfASLNP 374
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA---RAASRRVASVPQD--TSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQIVMTG--PLVQGVSKAD-AERRA-RELLGLVGlpAAAF-ERFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK09536 91 EFDVRQVVEMGrtPHRSRFDTWTeTDRAAvERAMERTG--VAQFaDRPVTSLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 450 ALDALIQVQILELLESLQRRFRLSIVFItHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-257 |
3.88e-23 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 98.65 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDplkveSGRLVFRDEDLADRSEE 81
Cdd:COG4559 1 MLEAENLSVRL----GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELtPS-----SGEVRLNGRPLAAWSPW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRGrdismVF-QEpmSALN-PLmRVGEQIDETLRAHGVAAARVRRQ-----RVVDLLGYVGlpdperlRLaYPfEL 154
Cdd:COG4559 72 ELARRRA-----VLpQH--SSLAfPF-TVEEVVALGRAPHGSSAAQDRQIvrealALVGLAHLAG-------RS-YQ-TL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 155 SGGQRQRVVIAMALA-------FDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVL 227
Cdd:COG4559 135 SGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLNLAAQYADRILLL 213
|
250 260 270
....*....|....*....|....*....|
gi 1331382268 228 EKGRVVEQGTAPAVLrvpredyTRQLLAAV 257
Cdd:COG4559 214 HQGRLVAQGTPEEVL-------TDELLERV 236
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-249 |
4.29e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.31 E-value: 4.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRqLPD--PLKVESGRLVFRDEDLADRSEEAMrQLRgRDISMVFQEPm 99
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINR-MNDlnPEVTITGSIVYNGHNIYSPRTDTV-DLR-KEIGMVFQQP- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 salNPL-MRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRL-AYPFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:PRK14239 96 ---NPFpMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLhDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIQQDKGMALlfITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPR----EDY 249
Cdd:PRK14239 173 DEPTSALDPISAGKIEETLLGLKDDYTMLL--VTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKhketEDY 246
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-243 |
4.45e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.78 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAK---ALLrqLPDPLKVEsgrLVFRDEDL---ADRSEEAM------------ 83
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEhlnALL--LPDTGTIE---WIFKDEKNkkkTKEKEKVLeklviqktrfkk 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 ----RQLRgRDISMVFQEPMSALnplmrVGEQIDETL----RAHGVAAARVRrQRVVDLLGYVGLPDpERLRLAyPFELS 155
Cdd:PRK13651 97 ikkiKEIR-RRVGVVFQFAEYQL-----FEQTIEKDIifgpVSMGVSKEEAK-KRAAKYIELVGLDE-SYLQRS-PFELS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQ 235
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKD 246
|
....*...
gi 1331382268 236 GTAPAVLR 243
Cdd:PRK13651 247 GDTYDILS 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-275 |
5.09e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.92 E-value: 5.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLA---KALLRQLPDPLKVES------GRLVFRDEDLADRSEEAMRQLRgRDIS 92
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVthfNGLIKSKYGTIQVGDiyigdkKNNHELITNPYSKKIKNFKELR-RRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 93 MVFQEPMSALnplmrVGEQIDETLR----AHGVAAARVRrQRVVDLLGYVGLPDP--ERlrlaYPFELSGGQRQRVVIAM 166
Cdd:PRK13631 120 MVFQFPEYQL-----FKDTIEKDIMfgpvALGVKKSEAK-KLAKFYLNKMGLDDSylER----SPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 167 ALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTapavlrvPR 246
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT-------PY 261
|
250 260
....*....|....*....|....*....
gi 1331382268 247 EDYTRQLLAAVSAQPLVPRTQVAGPVVLK 275
Cdd:PRK13631 262 EIFTDQHIINSTSIQVPRVIQVINDLIKK 290
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-233 |
5.66e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.88 E-value: 5.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MT-LLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRS 79
Cdd:PRK10535 1 MTaLLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKP---TSGTYRVAGQDVATLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 80 EEAMRQLRGRDISMVFQE--PMSALNplmrvGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDperlRLAY-PFELSG 156
Cdd:PRK10535 77 ADALAQLRREHFGFIFQRyhLLSHLT-----AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLED----RVEYqPSQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 157 GQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDfAVVEAIADRVLVLEKGRVV 233
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIV 222
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
18-236 |
5.79e-23 |
|
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: 96.88 E-value: 5.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGeCLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEamrqLRGRdISMVFQE 97
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKT----TLMRILATLTPPSSGTIRIDGQDVLKQPQK----LRRR-IGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 PMsaLNPLMRVGEQIDETLRAHGVAAARVRrQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:cd03264 81 FG--VYPNFTVREFLDYIAWLKGIPSKEVK-ARVDEVLELVNLGDRAKKKIG---SLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-236 |
6.14e-23 |
|
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: 96.85 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAmrqlrgRDISMVFQEpmS 100
Cdd:TIGR01277 12 HLPMEFDLNVADGEIVAIMGPSGAGKS----TLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQE--N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPLMRVGEQIDETLRAhGVAAARVRRQRVVDLLGYVGLPD-PERLrlayPFELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:TIGR01277 80 NLFAHLTVRQNIGLGLHP-GLKLNAEQQEKVVDAAQQVGIADyLDRL----PEQLSGGQRQRVALARCLVRPNPILLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:TIGR01277 155 PFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
297-500 |
7.73e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.85 E-value: 7.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRlRAlrSDVQMIFQDPFASLNPRQ 376
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYK-RA--KYIGRVFQDPMMGTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TV----------GQivmTGPLVQGVSKADAErRARELL-----GL-------VGLpaaaferfpheFSGGQRQRIGIARA 434
Cdd:COG1101 98 TIeenlalayrrGK---RRGLRRGLTKKRRE-LFRELLatlglGLenrldtkVGL-----------LSGGQRQALSLLMA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 435 LAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVV 500
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-259 |
8.09e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 98.24 E-value: 8.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 38 VVGESGSGKSMLAKALLRqLPDPLkveSGRLVFRDEDLADRSEEAMRQLRG--RDISMVFQEPmsalNPL-MRVGEQIDE 114
Cdd:PRK14271 52 LMGPTGSGKTTFLRTLNR-MNDKV---SGYRYSGDVLLGGRSIFNYRDVLEfrRRVGMLFQRP----NPFpMSIMDNVLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 115 TLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLA-YPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQIL 193
Cdd:PRK14271 124 GVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSdSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 194 DLLRKIQQDkgMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQLLAAVSA 259
Cdd:PRK14271 204 EFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSG 267
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
3-237 |
1.10e-22 |
|
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: 101.72 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPaGADRShALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSeea 82
Cdd:TIGR02203 330 DVEFRNVTFRYP-GRDRP-ALDSISLVIEPGETVALVGRSGSGKSTLVN-LIPRFYEP---DSGQILLDGHDLADYT--- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLRgRDISMVFQEPMsalnplmrvgeQIDETLrAHGVAAARVR---RQRVVDLLGYVGLPD-PERLRLAYPFE----- 153
Cdd:TIGR02203 401 LASLR-RQVALVSQDVV-----------LFNDTI-ANNIAYGRTEqadRAEIERALAAAYAQDfVDKLPLGLDTPigeng 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 --LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdkGMALLFITHDFAVVEAiADRVLVLEKGR 231
Cdd:TIGR02203 468 vlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGR 544
|
....*.
gi 1331382268 232 VVEQGT 237
Cdd:TIGR02203 545 IVERGT 550
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
273-480 |
1.67e-22 |
|
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: 95.24 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFcsrsgwwGRRTtqALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEg 352
Cdd:COG4133 2 MLEAENLSCRR-------GERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 353 rlrALRSDVQMIFQDPfaSLNPRQTVGQIVMtgpLVQGVSKADAER-RARELLGLVGLPAAAfERFPHEFSGGQRQRIGI 431
Cdd:COG4133 72 ---DYRRRLAYLGHAD--GLKPELTVRENLR---FWAALYGLRADReAIDEALEAVGLAGLA-DLPVRQLSAGQKRRVAL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 432 ARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLsIVFITHD 480
Cdd:COG4133 143 ARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQ 190
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
18-243 |
1.80e-22 |
|
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: 101.36 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMRqlrgRDISMVFQE 97
Cdd:TIGR01846 468 DSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTK-LLQRLYTP---QHGQVLVDGVDLAIADPAWLR----RQMGVVLQE 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 PM----SALNPLMRVGEQIDEtlrAHGVAAARVrrqrvvdllgyVGLPD-PERLRLAYPFE-------LSGGQRQRVVIA 165
Cdd:TIGR01846 540 NVlfsrSIRDNIALCNPGAPF---EHVIHAAKL-----------AGAHDfISELPQGYNTEvgekganLSGGQRQRIAIA 605
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 166 MALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdkGMALLFITHDFAVVEAiADRVLVLEKGRVVEQGTAPAVLR 243
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLA 680
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-249 |
1.84e-22 |
|
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: 95.29 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLrQLPDPlKVESGRLVFRDEDLADRS-EEa 82
Cdd:cd03217 1 LEIKDLHVSV----GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIM-GHPKY-EVTEGEILFKGEDITDLPpEE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 mRQLRGrdISMVFQEPMsalnplmrvgeqidetlRAHGVaaarvrrqRVVDLLGYVGLpdperlrlaypfELSGGQRQRV 162
Cdd:cd03217 74 -RARLG--IFLAFQYPP-----------------EIPGV--------KNADFLRYVNE------------GFSGGEKKRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAI-ADRVLVLEKGRVVEQGTAPAV 241
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELA 192
|
....*...
gi 1331382268 242 LRVPREDY 249
Cdd:cd03217 193 LEIEKKGY 200
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-479 |
1.92e-22 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 100.47 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 27 SLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAMRQLrgrdismVFQEPMSALNPLM 106
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELP----LLSGERQSQFSHITRLSFEQLQKL-------VSDEWQRNNTDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 107 RVGEqiDETlrahGVAAARV------RRQRVVDLLGYVGLPDPERLRLAYpfeLSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:PRK10938 92 SPGE--DDT----GRTTAEIiqdevkDPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLR---VPREDYTRQLL--- 254
Cdd:PRK10938 163 FDGLDVASRQQLAELLASLHQ-SGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQqalVAQLAHSEQLEgvq 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 255 ----AAVSAQPLVPRTQvaGPVVLKAealGKVfcsrsgWWGRRTTqaLDAVQLQLREGETLGIVGESGSGKSTL------ 324
Cdd:PRK10938 242 lpepDEPSARHALPANE--PRIVLNN---GVV------SYNDRPI--LHNLSWQVNPGEHWQIVGPNGAGKSTLlslitg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 325 -------------GRclvrllRADSGRIEWLGREVAGLSEGRL----RALRSDVQMIFQDPFASLNprqtvgqivmtgpL 387
Cdd:PRK10938 309 dhpqgysndltlfGR------RRGSGETIWDIKKHIGYVSSSLhldyRVSTSVRNVILSGFFDSIG-------------I 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 388 VQGVSkaDAERR-ARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESL 466
Cdd:PRK10938 370 YQAVS--DRQQKlAQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVL 447
|
490
....*....|...
gi 1331382268 467 QRRFRLSIVFITH 479
Cdd:PRK10938 448 ISEGETQLLFVSH 460
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-246 |
2.14e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.07 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLaDRSEEAMRQLRgRDISMVFQE 97
Cdd:PRK13639 13 DGTEALKGINFKAEKGEMVALLGPNGAGKS----TLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 PMSAL-NPlmRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLI 176
Cdd:PRK13639 87 PDDQLfAP--TVEEDVAFGPLNLGLSKEEVEK-RVKEALKAVGMEGFEN---KPPHHLSGGQKKRVAIAGILAMKPEIIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 177 ADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAV-----------LRVP 245
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDL-NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVfsdietirkanLRLP 239
|
.
gi 1331382268 246 R 246
Cdd:PRK13639 240 R 240
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-254 |
2.30e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.49 E-value: 2.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDplkveSGRLVFRDEDL--ADRS------EEamrqlRGrdi 91
Cdd:COG4152 15 TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILaPD-----SGEVLWDGEPLdpEDRRrigylpEE-----RG--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 92 smvfqepmsaLNPLMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFD 171
Cdd:COG4152 82 ----------LYPKMKVGEQLVYLARLKGLSKAEAKR-RADEWLERLGLGDRANKKVE---ELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKiQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVlrvpREDYTR 251
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRE-LAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI----RRQFGR 222
|
...
gi 1331382268 252 QLL 254
Cdd:COG4152 223 NTL 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
23-232 |
2.31e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.29 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEeamrqlrgrDISMVFQEpmSAL 102
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKS----TLLRLLAGLETPSAGELLAGTAPLAEARE---------DTRLMFQD--ARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPLMRVGEQIDETLRAHGVAAARvrrqrvvDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLIADEPTS 182
Cdd:PRK11247 93 LPWKKVIDNVGLGLKGQWRDAAL-------QALAAVGLADRAN---EWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 183 ALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRV 232
Cdd:PRK11247 163 ALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-232 |
2.66e-22 |
|
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: 94.04 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIAlpagadrsHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEE 81
Cdd:cd03215 3 PVLEVRGLSVK--------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP----PASGEITLDGKPVTRRSPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRgrdISMVFQEPMS-ALNPLMRVGEQIdeTLRAHgvaaarvrrqrvvdllgyvglpdperlrlaypfeLSGGQRQ 160
Cdd:cd03215 71 DAIRAG---IAYVPEDRKReGLVLDLSVAENI--ALSSL----------------------------------LSGGNQQ 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 161 RVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRV 232
Cdd:cd03215 112 KVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-274 |
2.75e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.99 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEE 81
Cdd:PRK13548 1 AMLEARNLSVRL----GGRTLLDDVSLTLRPGEVVAILGPNGAGKS----TLLRALSGELSPDSGEVRLNGRPLADWSPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRGrdisMVFQEpmSALNPLMRVGEQIDETLRAHGVAAARVRR-----QRVVDLLGYVGLPdperlrlaYPfELSG 156
Cdd:PRK13548 73 ELARRRA----VLPQH--SSLSFPFTVEEVVAMGRAPHGLSRAEDDAlvaaaLAQVDLAHLAGRD--------YP-QLSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 157 GQRQRVVIAMALA------FDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKG 230
Cdd:PRK13548 138 GEQQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQG 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1331382268 231 RVVEQGTAPAVLrvpredyTRQLLAAV-SAQPLVPRTQVAG-PVVL 274
Cdd:PRK13548 218 RLVADGTPAEVL-------TPETLRRVyGADVLVQPHPETGaPLVL 256
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
296-503 |
2.84e-22 |
|
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: 94.79 E-value: 2.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPfaslnpr 375
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDLRSSLTIIPQDP------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 qtvgqIVMTGPLVQGVSKADaERRARELLGLVGLPAAAferfpHEFSGGQRQRIGIARALAVEPKVLIADECVSAL---- 451
Cdd:cd03369 92 -----TLFSGTIRSNLDPFD-EYSDEEIYGALRVSEGG-----LNLSQGQRQLLCLARALLKRPRVLVLDEATASIdyat 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 452 DALIQVQILELLESlqrrfrLSIVFITHDLRVAARlCDRIAVMRKGRVVEQG 503
Cdd:cd03369 161 DALIQKTIREEFTN------STILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-257 |
3.05e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 96.06 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 19 RSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLR--QLPDPLKVEsGRLVFRDEDLADRSEEAMRqLRgRDISMVFQ 96
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEARVE-GEVRLFGRNIYSPDVDPIE-VR-REVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 97 EPmsalNPL--MRVGEQIDETLRAHGVAAARVRRQRVVD-LLGYVGLPDPERLRLA-YPFELSGGQRQRVVIAMALAFDP 172
Cdd:PRK14267 93 YP----NPFphLTIYDNVAIGVKLNGLVKSKKELDERVEwALKKAALWDEVKDRLNdYPSNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 173 ALLIADEPTSALDVTTQAQILDLLRKIQQDkgMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQ 252
Cdd:PRK14267 169 KILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEK 246
|
....*
gi 1331382268 253 LLAAV 257
Cdd:PRK14267 247 YVTGA 251
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-236 |
3.14e-22 |
|
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: 95.48 E-value: 3.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMRQlrgrdISMVFQE---- 97
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLK-ILSGLLQP---TSGEVRVAGLVPWKRRKKFLRR-----IGVVFGQktql 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 -----PMSALNpLMRVGEQIDEtlrahgvAAARVRRQRVVDLLGYVGLPD-PERlrlaypfELSGGQRQRVVIAMALAFD 171
Cdd:cd03267 107 wwdlpVIDSFY-LLAAIYDLPP-------ARFKKRLDELSELLDLEELLDtPVR-------QLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
297-510 |
3.42e-22 |
|
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: 100.18 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLsegRLRALRSDVQMIFQDPFASlnpRQ 376
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY---TLASLRRQVALVSQDVVLF---ND 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGPLVQgVSKADAERRARE--LLGLV-GLPAAAfeRFP-----HEFSGGQRQRIGIARALAVEPKVLIADECV 448
Cdd:TIGR02203 421 TIANNIAYGRTEQ-ADRAEIERALAAayAQDFVdKLPLGL--DTPigengVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 449 SALDALIQVQILELLESLQRRfRLSIVfITHDLRVAARlCDRIAVMRKGRVVEQGETAALFA 510
Cdd:TIGR02203 498 SALDNESERLVQAALERLMQG-RTTLV-IAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
21-236 |
3.64e-22 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 94.59 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLrqlpDPLKVESGRLVFrDEDLADRSEEAMRQlrgrdISMVFQEPms 100
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIL----GLIKPDSGEITF-DGKSYQKNIEALRR-----IGALIEAP-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPLMRVGEQidetLRAHGVAAaRVRRQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:cd03268 82 GFYPNLTAREN----LRLLARLL-GIRKKRIDEVLDVVGLKDSAKKKVK---GFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 181 TSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03268 154 TNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
22-237 |
5.69e-22 |
|
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: 94.48 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLadrSEEAMRQLRGRdISMVFQEPM-- 99
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVE----LSSGSILIDGVDI---SKIGLHDLRSR-ISIIPQDPVlf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 -----SALNPLmrvGEQIDETLRAhgvAAARVR-RQRVVDLLGyvGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPA 173
Cdd:cd03244 91 sgtirSNLDPF---GEYSDEELWQ---ALERVGlKEFVESLPG--GLDTVVEEGGE---NLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 174 LLIADEPTSALDVTTQAQILDLLRkiQQDKGMALLFITHDfavVEAIA--DRVLVLEKGRVVEQGT 237
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIR--EAFKDCTVLTIAHR---LDTIIdsDRILVLDKGRVVEFDS 220
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
27-242 |
5.96e-22 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 94.65 E-value: 5.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 27 SLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAmrqlrgRDISMVFQEpmSALNPLM 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS----TLLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RPVSMLFQE--NNLFSHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 107 RVGEQIdeTLRAH-GVAAARVRRQRVVDLLGYVGLPDP-ERLrlayPFELSGGQRQRVVIAMALAFDPALLIADEPTSAL 184
Cdd:PRK10771 87 TVAQNI--GLGLNpGLKLNAAQREKLHAIARQMGIEDLlARL----PGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 185 DVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVL 242
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-252 |
6.32e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 94.98 E-value: 6.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 38 VVGESGSGKSMLAKALLR--QLPDPLKVESGRLVfrdeDLADRSEEAMRQLRGRdISMVFQEPmsalNPL--MRVGEQID 113
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNRliELYPEARVSGEVYL----DGQDIFKMDVIELRRR-VQMVFQIP----NPIpnLSIFENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 114 ETLRAHGVAAARVR-RQRVVDLLGYVGLPDPERLRLAYPF-ELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQ 191
Cdd:PRK14247 105 LGLKLNRLVKSKKElQERVRWALEKAQLWDEVKDRLDAPAgKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAK 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 192 ILDLLRKIQQDkgMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPREDYTRQ 252
Cdd:PRK14247 185 IESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-243 |
6.84e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.96 E-value: 6.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 20 SHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAMRQLRGRDISMVFQEPM 99
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKS----TLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 SALnplmrVGEQI--DETLRAHGVAAARVRRQRVV-DLLGYVGLPdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLI 176
Cdd:PRK13643 95 SQL-----FEETVlkDVAFGPQNFGIPKEKAEKIAaEKLEMVGLA--DEFWEKSPFELSGGQMRRVAIAGILAMEPEVLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 177 ADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLR 243
Cdd:PRK13643 168 LDEPTAGLDPKARIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-248 |
1.03e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 95.16 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGADRSHaLYDLSLQLNRGECLCVVGESGSGKSMLAK---ALLRQLPDPLKVESGRLvfrdedladrS 79
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQ-LNGVSFSITKGEWVSIIGQNGSGKSTTARlidGLFEEFEGKVKIDGELL----------T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 80 EEAMRQLRgRDISMVFQEPMSALnplmrVGEQIDETLrAHGVAAARVRRQ----RVVDLLGYVGLPDperLRLAYPFELS 155
Cdd:PRK13642 73 AENVWNLR-RKIGMVFQNPDNQF-----VGATVEDDV-AFGMENQGIPREemikRVDEALLAVNMLD---FKTREPARLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVeAIADRVLVLEKGRVVEQ 235
Cdd:PRK13642 143 GGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKE 221
|
250
....*....|...
gi 1331382268 236 GtAPAVLRVPRED 248
Cdd:PRK13642 222 A-APSELFATSED 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
289-510 |
1.21e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 94.69 E-value: 1.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 289 WWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaGLSEGRLRALRSDVQMIFQDP 368
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 369 FASLNPRQTVGQIVMTGPLVqGVSKADAERRARELLGLVGlpAAAFERFPHE-FSGGQRQRIGIARALAVEPKVLIADEC 447
Cdd:PRK13638 87 EQQIFYTDIDSDIAFSLRNL-GVPEAEITRRVDEALTLVD--AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 448 VSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
295-503 |
1.46e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 91.99 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlrALRSDVQMIFQDPF---AS 371
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK----ALSSLISVLNQRPYlfdTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 372 LnpRQTVGqivmtgplvqgvskadaeRRarellglvglpaaaferfpheFSGGQRQRIGIARALAVEPKVLIADECVSAL 451
Cdd:cd03247 91 L--RNNLG------------------RR---------------------FSGGERQRLALARILLQDAPIVLLDEPTVGL 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 452 DALIQVQILELL-ESLQRRfrlSIVFITHDLRVAARLcDRIAVMRKGRVVEQG 503
Cdd:cd03247 130 DPITERQLLSLIfEVLKDK---TLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
23-213 |
1.54e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMRQlrgrDISMVFQEPMsal 102
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLK-IVASLISP---TSGTLLFEGEDISTLKPEIYRQ----QVSYCAQTPT--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 nplmRVGEQI-DETLRAHGVAAARVRRQRVVDLLGYVGLPDPerlRLAYPF-ELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:PRK10247 92 ----LFGDTVyDNLIFPWQIRNQQPDPAIFLDDLERFALPDT---ILTKNIaELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190
....*....|....*....|....*....|...
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQDKGMALLFITHD 213
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-270 |
1.59e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 94.45 E-value: 1.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAMRQLRGRdISMVFQEpmSALNP 104
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKT----TLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQS--GALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRlayPFELSGGQRQRVVIAMALAFDPALLIADEPTSAL 184
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPFVGQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 185 DVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAvLRVPREDYTRQLLAAVSAQPlVP 264
Cdd:PRK11831 175 DPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA-LQANPDPRVRQFLDGIADGP-VP 252
|
....*.
gi 1331382268 265 RTQVAG 270
Cdd:PRK11831 253 FRYPAG 258
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
298-508 |
1.66e-21 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.08 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlRALRSDVQMIFQD-PFASlnpRQ 376
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQQlPAAE---GM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTG--PLVQGVSKADAERRAR--ELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALD 452
Cdd:PRK10575 101 TVRELVAIGryPWHGALGRFGAADREKveEAISLVGLKPLA-HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 453 ALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:PRK10575 180 IAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
298-510 |
2.28e-21 |
|
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: 98.09 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlRALRSDVQMIFQDpfaslnprqt 377
Cdd:TIGR03796 495 IENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPR---EVLANSVAMVDQD---------- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 vgqIVMTGPLVQ--------GVSKADAERRAR------ELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLI 443
Cdd:TIGR03796 562 ---IFLFEGTVRdnltlwdpTIPDADLVRACKdaaihdVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILI 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 444 ADECVSALDALIQVQILELLeslqRRFRLSIVFITHDLRvAARLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:TIGR03796 639 LDEATSALDPETEKIIDDNL----RRRGCTCIIVAHRLS-TIRDCDEIIVLERGKVVQRGTHEELWA 700
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-237 |
2.49e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 94.77 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKS----MLAkALLRqlPDplkveSGRLVFRDEDLADRSEEAMRQlrgrdISMVF- 95
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSttikMLT-GILV--PT-----SGEVRVLGYVPFKRRKEFARR-----IGVVFg 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 QEpmSALN---PLMrvgeqidETLRAHGV------AAARVRRQRVVDLLGYVGLPD-PERlrlaypfELSGGQRQRVVIA 165
Cdd:COG4586 103 QR--SQLWwdlPAI-------DSFRLLKAiyripdAEYKKRLDELVELLDLGELLDtPVR-------QLSLGQRMRCELA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 166 MALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGT 237
Cdd:COG4586 167 AALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
298-499 |
2.98e-21 |
|
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: 90.74 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALrsdVQMIFQDpfaslnprqt 377
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH---VGYLPQD---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 vgQIVMTGPLVQGVskadaerrarellglvglpaaaferfpheFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQV 457
Cdd:cd03246 85 --DELFSGSIAENI-----------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1331382268 458 QILELLESLQRRfRLSIVFITHDLRVAARlCDRIAVMRKGRV 499
Cdd:cd03246 134 ALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-236 |
3.05e-21 |
|
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: 92.05 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEA 82
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKT----TTLRMLAGLLEPDAGFATVDGFDVVKEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLRgrdismvFQEPMSALNPLMRVGEQIDETLRAHGVA--AARVRRQRVVDLLGYVGLPDperLRLAypfELSGGQRQ 160
Cdd:cd03266 77 RRRLG-------FVSDSTGLYDRLTARENLEYFAGLYGLKgdELTARLEELADRLGMEELLD---RRVG---GFSTGMRQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 161 RVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKiQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03266 144 KVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
298-503 |
4.97e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 92.38 E-value: 4.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRL-RALrsdvqmifqdpfaSLNPRQ 376
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLaRRL-------------ALLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 -------TVGQIVMTG-----PLVQGVSKADAER--RARELLGLVGLPaaafERFPHEFSGGQRQRIGIARALAVEPKVL 442
Cdd:PRK11231 85 hltpegiTVRELVAYGrspwlSLWGRLSAEDNARvnQAMEQTRINHLA----DRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 443 IADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-254 |
6.29e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.86 E-value: 6.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALPAGADrshALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEE 81
Cdd:COG3845 256 VVLEVENLSVRDDRGVP---ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP----PASGSIRLDGEDITGLSPR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRgrdISMVFQEPMS-ALNPLMRVGE------QIDETLRAHGV---AAARVRRQRVVDLLGyVGLPDPE-RLRLay 150
Cdd:COG3845 329 ERRRLG---VAYIPEDRLGrGLVPDMSVAEnlilgrYRRPPFSRGGFldrKAIRAFAEELIEEFD-VRTPGPDtPARS-- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 151 pfeLSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKiQQDKGMALLFITHDFAVVEAIADRVLVLEKG 230
Cdd:COG3845 403 ---LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEG 478
|
250 260
....*....|....*....|....
gi 1331382268 231 RVVEQgtapavlrVPREDYTRQLL 254
Cdd:COG3845 479 RIVGE--------VPAAEATREEI 494
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-237 |
6.92e-21 |
|
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: 96.04 E-value: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRqLPDplkVESGRLVFRDEDLADRSEEAMRqlrgRDISMVFQEPmsAL 102
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR-FYD---VTSGRILIDGQDIRDVTQASLR----AAIGIVPQDT--VL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 -NplmrvgeqidETLR---AHG---------VAAARVrrqrvVDLLGYV-GLPDP------ER-LRLaypfelSGGQRQR 161
Cdd:COG5265 444 fN----------DTIAyniAYGrpdaseeevEAAARA-----AQIHDFIeSLPDGydtrvgERgLKL------SGGEKQR 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 162 VVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMalLFITHDFAVVeAIADRVLVLEKGRVVEQGT 237
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTT--LVIAHRLSTI-VDADEILVLEAGRIVERGT 575
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-236 |
8.18e-21 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 91.11 E-value: 8.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLA--DRSEeamrqLRgRDISMVFQEP 98
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLY----KPTSGSVLLDGTDIRqlDPAD-----LR-RNIGYVPQDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 MsaL-------NPLMRVGEQIDETLrahgVAAARVrrQRVVDLLGyvGLPDPERLRLA-YPFELSGGQRQRVVIAMALAF 170
Cdd:cd03245 88 T--LfygtlrdNITLGAPLADDERI----LRAAEL--AGVTDFVN--KHPNGLDLQIGeRGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 171 DPALLIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEaIADRVLVLEKGRVVEQG 236
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
21-242 |
8.39e-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: 96.09 E-value: 8.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLA--DRSEeamrqLRgRDISMVFQEP 98
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQ----PTEGSVLLDGVDIRqiDPAD-----LR-RNIGYVPQDP 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 MsaL-------NPLMRVGEQIDETLRAhgvAAARVRRQRVVDLL--GYvGLPDPERLRlaypfELSGGQRQRVVIAMALA 169
Cdd:TIGR03375 549 R--LfygtlrdNIALGAPYADDEEILR---AAELAGVTEFVRRHpdGL-DMQIGERGR-----SLSGGQRQAVALARALL 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 170 FDPALLIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEaIADRVLVLEKGRVVEQGTAPAVL 242
Cdd:TIGR03375 618 RDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVL 687
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-237 |
1.03e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 95.66 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGADrsHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpDPlkvESGRLVFRDEDLADRSEEA 82
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQ--PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAW-DP---QQGEILLNGQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLrgrdISMVFQEP--MSAlnplmrvgeqideTLRAH-GVAAARVRRQRVVDLLGYVGL----PDPERLRlAYPFE-- 153
Cdd:PRK11160 412 LRQA----ISVVSQRVhlFSA-------------TLRDNlLLAAPNASDEALIEVLQQVGLekllEDDKGLN-AWLGEgg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 --LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAIaDRVLVLEKGR 231
Cdd:PRK11160 474 rqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQ 550
|
....*.
gi 1331382268 232 VVEQGT 237
Cdd:PRK11160 551 IIEQGT 556
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
4-237 |
1.11e-20 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.50 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVESGRLVfrDEDLADRSEeaM 83
Cdd:TIGR00955 22 QLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLL--NGMPIDAKE--M 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 RQLRGrdisMVFQEPMsaLNPLMRVGEQ--IDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPFE---LSGGQ 158
Cdd:TIGR00955 98 RAISA----YVQQDDL--FIPTLTVREHlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIGVPGRvkgLSGGE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 159 RQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGT 237
Cdd:TIGR00955 172 RKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGS 250
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
298-510 |
1.32e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 1.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGlsegRLRALRSDVQMIFQdpFASLNPRQT 377
Cdd:PRK13537 23 VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS----RARHARQRVGVVPQ--FDNLDPDFT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 VGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFpHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQV 457
Cdd:PRK13537 97 VRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 458 QILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:PRK13537 176 LMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
293-510 |
1.53e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 95.09 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 293 RTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREvagLSEGRLRALRSDVQMI------FQ 366
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD---LRDYTLASLRNQVALVsqnvhlFN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 367 DPFASlNPRQTVGQIVmtgplvqgvSKADAERRAREllglvglpAAAFE---RFPHEF-----------SGGQRQRIGIA 432
Cdd:PRK11176 431 DTIAN-NIAYARTEQY---------SREQIEEAARM--------AYAMDfinKMDNGLdtvigengvllSGGQRQRIAIA 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 433 RALAVEPKVLIADECVSALDALIQVQILELLESLQRRfRLSIVfITHDLRVAARlCDRIAVMRKGRVVEQGETAALFA 510
Cdd:PRK11176 493 RALLRDSPILILDEATSALDTESERAIQAALDELQKN-RTSLV-IAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
296-510 |
1.57e-20 |
|
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: 94.89 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDpfaslnpr 375
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT---QASLRAAIGIVPQD-------- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 qTV------------GQIvmtgplvqGVSKADAERRARellglvglpAAAFERF----PHEF-----------SGGQRQR 428
Cdd:COG5265 441 -TVlfndtiayniayGRP--------DASEEEVEAAAR---------AAQIHDFieslPDGYdtrvgerglklSGGEKQR 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 429 IGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRfRLSIVfITHDLRVAARlCDRIAVMRKGRVVEQGETAAL 508
Cdd:COG5265 503 VAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARG-RTTLV-IAHRLSTIVD-ADEILVLEAGRIVERGTHAEL 579
|
..
gi 1331382268 509 FA 510
Cdd:COG5265 580 LA 581
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
270-499 |
1.90e-20 |
|
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: 88.64 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 270 GPVVLKAEALgkvfcsrsgwwgrRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGL 349
Cdd:cd03215 1 GEPVLEVRGL-------------SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 350 SEGRlrALRSDVQMIfqdpfaslnprqtvgqivmtgplvqgvskadAERRARELLgLVGLPAAAFERFPHEFSGGQRQRI 429
Cdd:cd03215 68 SPRD--AIRAGIAYV-------------------------------PEDRKREGL-VLDLSVAENIALSSLLSGGNQQKV 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 430 GIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRV 499
Cdd:cd03215 114 VLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
294-503 |
3.14e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 94.26 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDP--FA- 370
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLRRNIAVVFQDAglFNr 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SLNPRQTVGQIVMTGPLVQGVSKADA-----ERRARELLGLVGlpaaafERfPHEFSGGQRQRIGIARALAVEPKVLIAD 445
Cdd:PRK13657 424 SIEDNIRVGRPDATDEEMRAAAERAQahdfiERKPDGYDTVVG------ER-GRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 446 ECVSALDALIQVQILELLESLqRRFRLSIVfITHDLRvAARLCDRIAVMRKGRVVEQG 503
Cdd:PRK13657 497 EATSALDVETEAKVKAALDEL-MKGRTTFI-IAHRLS-TVRNADRILVFDNGRVVESG 551
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
300-503 |
4.43e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 91.47 E-value: 4.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 300 AVQLQL-REGETlGIVGESGSGKSTLGRCLVRLLRADSGRIEwLGREVAGLSEGR--LRALRSDVQMIFQDpfASLNPRQ 376
Cdd:PRK11144 16 TVNLTLpAQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIV-LNGRVLFDAEKGicLPPEKRRIGYVFQD--ARLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVgqivmTGPLVQGVSKADAERRAR--ELLGLVGLpaaaFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:PRK11144 92 KV-----RGNLRYGMAKSMVAQFDKivALLGIEPL----LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 455 IQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:PRK11144 163 RKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-230 |
4.58e-20 |
|
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: 89.06 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMrqlrgrdisMVFQEpmSAL 102
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLN-LISGLAQP---TSGGVILEGKQITEPGPDRM---------VVFQN--YSL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPLMRVGEQIDETLRAHGVAAARVRRQRVVD-LLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPT 181
Cdd:TIGR01184 66 LPWLTVRENIALAVDRVLPDLSKSERRAIVEeHIALVGL---TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 182 SALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKG 230
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
298-508 |
5.28e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.43 E-value: 5.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGlsegRLRALRSDVQMIFQdpFASLNPRQT 377
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA----RARLARARIGVVPQ--FDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 VGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPhEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQV 457
Cdd:PRK13536 131 VRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVS-DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 458 QILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:PRK13536 210 LIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
23-243 |
5.68e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 89.85 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAMrqlrGRDISMVFQEPMSAL 102
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQP----PSEGEILLDAQPLESWSSKAF----ARKVAYLPQQLPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NplMRVGEqidetLRA------HGvAAARVR---RQRVVDLLGYVGL-PDPERLRLAypfeLSGGQRQRVVIAMALAFDP 172
Cdd:PRK10575 99 G--MTVRE-----LVAigrypwHG-ALGRFGaadREKVEEAISLVGLkPLAHRLVDS----LSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 173 ALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLR 243
Cdd:PRK10575 167 RCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
23-249 |
7.11e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 88.97 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLrQLPDpLKVESGRLVFRDEDLADRS-EEamRQLRGrdISMVFQEP--- 98
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM-GHPK-YEVTSGSILLDGEDILELSpDE--RARAG--IFLAFQYPvei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 --MSALNpLMR--VGEQIDETLRAHGVaaarvrRQRVVDLLGYVGLpDPERLR--LAYPFelSGGQRQRVVIAMALAFDP 172
Cdd:COG0396 90 pgVSVSN-FLRtaLNARRGEELSAREF------LKLLKEKMKELGL-DEDFLDryVNEGF--SGGEKKRNEILQMLLLEP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 173 ALLIADEPTSALDVttqaqilDLLRKI------QQDKGMALLFITHDFAVVEAI-ADRVLVLEKGRVVEQGTAPAVLRVP 245
Cdd:COG0396 160 KLAILDETDSGLDI-------DALRIVaegvnkLRSPDRGILIITHYQRILDYIkPDFVHVLVDGRIVKSGGKELALELE 232
|
....
gi 1331382268 246 REDY 249
Cdd:COG0396 233 EEGY 236
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-227 |
1.12e-19 |
|
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: 91.96 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAM 83
Cdd:TIGR02857 322 LEFSGVSVAYP---GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD----PTEGSIAVNGVPLADADADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 RqlrgRDISMVFQEPM-----SALNPLMRVGEQIDETLRAhgvAAARVRRQRVVDllgyvGLPDPERLRLA-YPFELSGG 157
Cdd:TIGR02857 395 R----DQIAWVPQHPFlfagtIAENIRLARPDASDAEIRE---ALERAGLDEFVA-----ALPQGLDTPIGeGGAGLSGG 462
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 158 QRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdkGMALLFITHDFAVVEAiADRVLVL 227
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-236 |
1.18e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.47 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEamrqlrGRDISMVFQEpmSALNP 104
Cdd:PRK11000 21 DINLDIHEGEFVVFVGPSGCGKS----TLLRMIAGLEDITSGDLFIGEKRMNDVPPA------ERGVGMVFQS--YALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVGEQIDETLRAHGVAAARvRRQRVVDLlgyvglpdPERLRLAY-----PFELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:PRK11000 89 HLSVAENMSFGLKLAGAKKEE-INQRVNQV--------AEVLQLAHlldrkPKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfaVVEA--IADRVLVLEKGRVVEQG 236
Cdd:PRK11000 160 PLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD--QVEAmtLADKIVVLDAGRVAQVG 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
296-504 |
1.24e-19 |
|
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: 91.79 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCL--VRLLRADSGRI----------EWLGR------------------- 344
Cdd:TIGR03269 14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcGYVERpskvgepcpvcggtlepee 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 345 -EVAGLSEGRLRALRSDVQMIFQDPFAsLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPaaafERFPH---E 420
Cdd:TIGR03269 94 vDFWNLSDKLRRRIRKRIAIMLQRTFA-LYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS----HRITHiarD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 421 FSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVV 500
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
....
gi 1331382268 501 EQGE 504
Cdd:TIGR03269 249 EEGT 252
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-232 |
1.35e-19 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 86.12 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIAlPAGADRShALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVfrdedladrseeam 83
Cdd:cd03246 1 LEVENVSFR-YPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP----TSGRVR-------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 rqLRGRDISmvfqepmsalnplmrvgeQIDET-LRAHgvaaarvrrqrvvdlLGYVglpdPERLRLaypFE-------LS 155
Cdd:cd03246 61 --LDGADIS------------------QWDPNeLGDH---------------VGYL----PQDDEL---FSgsiaeniLS 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAiADRVLVLEKGRV 232
Cdd:cd03246 99 GGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKA-AGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
21-233 |
1.54e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.24 E-value: 1.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMRQLRgRDISMVFQEPMS 100
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLK-LICGIERP---SAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNplMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLPDPERlrlAYPFELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:PRK10908 91 LMD--RTVYDNVAIPLIIAGASGDDIRR-RVSAALDKVGLLDKAK---NFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVV 233
Cdd:PRK10908 165 TGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
292-499 |
1.55e-19 |
|
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: 87.53 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREvagLSEGRLRALRSDVQMIFQDP--F 369
Cdd:cd03248 24 RPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP---ISQYEHKYLHSKVSLVGQEPvlF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 A-SLNPRQTVG-QIVMTGPLVQGVSKADAERRARELLglVGLPAAAFERfPHEFSGGQRQRIGIARALAVEPKVLIADEC 447
Cdd:cd03248 101 ArSLQDNIAYGlQSCSFECVKEAAQKAHAHSFISELA--SGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 448 VSALDALIQVQILELL-ESLQRRfrlSIVFITHDLRVAARlCDRIAVMRKGRV 499
Cdd:cd03248 178 TSALDAESEQQVQQALyDWPERR---TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
303-508 |
1.75e-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: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 303 LQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwlgreVAGLSEGRLRALRSDVQMifQDPFA---SLNPRQTV- 378
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVK-----VAGASPGKGWRHIGYVPQ--RHEFAwdfPISVAHTVm 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 379 -GQIVMTGPLVQgvSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQV 457
Cdd:TIGR03771 74 sGRTGHIGWLRR--PCVADFAAVRDALRRVGLTELA-DRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 458 QILELLESLQRRfRLSIVFITHDLRVAARLCDRIaVMRKGRVVEQGETAAL 508
Cdd:TIGR03771 151 LLTELFIELAGA-GTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQL 199
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
28-480 |
2.39e-19 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 91.55 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 28 LQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVF--------------RDED------LADRSEEAMRQLR 87
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVL----LDDGRIIYeqdlivarlqqdppRNVEgtvydfVAEGIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 88 G-RDIS-MVFQEPM-SALNPLMRVGEQIDEtlraHGVAAARVRRQRVVDLLGYvglpDPERlRLAypfELSGGQRQRVVI 164
Cdd:PRK11147 100 RyHDIShLVETDPSeKNLNELAKLQEQLDH----HNLWQLENRINEVLAQLGL----DPDA-ALS---SLSGGWLRKAAL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 165 AMALAFDPALLIADEPTSALDVTTqaqiLDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVE---------Q 235
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSypgnydqylL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 236 GTAPAvLRVPRE---DYTRQLlaavsAQPLV--------PRTQVAGPV-VLKA---------EALGKVF-----CSRSG- 288
Cdd:PRK11147 244 EKEEA-LRVEELqnaEFDRKL-----AQEEVwirqgikaRRTRNEGRVrALKAlrrerserrEVMGTAKmqveeASRSGk 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 289 --WWGRRTTQALDAVQL------QLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwLGR--EVAGLSEGRlralr 358
Cdd:PRK11147 318 ivFEMENVNYQIDGKQLvkdfsaQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTklEVAYFDQHR----- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 359 sdvqmifqdpfASLNPRQTV-------GQIVMtgplVQGvskadaerRARELLG----LVGLPAAAfeRFP-HEFSGGQR 426
Cdd:PRK11147 392 -----------AELDPEKTVmdnlaegKQEVM----VNG--------RPRHVLGylqdFLFHPKRA--MTPvKALSGGER 446
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 427 QRIGIARALAVEPKVLIADECVSALDaliqVQILELLESLQRRFRLSIVFITHD 480
Cdd:PRK11147 447 NRLLLARLFLKPSNLLILDEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
274-511 |
2.54e-19 |
|
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: 86.83 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 274 LKAEALGKVFcsrsgwwgrRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGR 353
Cdd:cd03218 1 LRAENLSKRY---------GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 354 lRAlRSDVQMIFQDpfASLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIAR 433
Cdd:cd03218 72 -RA-RLGIGYLPQE--ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLR-KSKASSLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 434 ALAVEPKVLIADECVSALDALIQVQILELLESLQRRfrlSI-VFIT-HDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDR---GIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
298-499 |
2.85e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.89 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGrevaGLSEGRLRalrsdvqmifQDPFasLNPRQT 377
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----GLRIGYLP----------QEPP--LDDDLT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 VGQIVMTG--PLVQGVSKA------------------------------DAERRARELLGLVGLPAAAFERFPHEFSGGQ 425
Cdd:COG0488 78 VLDTVLDGdaELRALEAELeeleaklaepdedlerlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPVSELSGGW 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 426 RQRIGIARALAVEPKVLIADECVSALDAliqvQILELLESLQRRFRLSIVFITHD---LRvaaRLCDRIAVMRKGRV 499
Cdd:COG0488 158 RRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEFLKNYPGTVLVVSHDryfLD---RVATRILELDRGKL 227
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
279-503 |
3.20e-19 |
|
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: 86.56 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 279 LGKVFCSRSGWWGRRttQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRAD---SGRIEWLGREV-AGLSEGRL 354
Cdd:cd03234 6 WWDVGLKAKNWNKYA--RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRkPDQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 355 RALRSDvqmifqDPFAS-LNPRQTvgqIVMTGPLVQGVSKADAERRAR---ELLGLVGLPAAAFERFPHeFSGGQRQRIG 430
Cdd:cd03234 84 AYVRQD------DILLPgLTVRET---LTYTAILRLPRKSSDAIRKKRvedVLLRDLALTRIGGNLVKG-ISGGERRRVS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 431 IARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFItHDLRVAA-RLCDRIAVMRKGRVVEQG 503
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTI-HQPRSDLfRLFDRILLLSSGEIVYSG 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
294-494 |
5.70e-19 |
|
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: 90.04 E-value: 5.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlRALRSDVQMIFQDPFAsln 373
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA---DSWRDQIAWVPQHPFL--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIVMtgpLVQGVSKADAERRARELLGLVGLPAAAFE-------RFPHEFSGGQRQRIGIARALAVEPKVLIADE 446
Cdd:TIGR02857 408 FAGTIAENIR---LARPDASDAEIREALERAGLDEFVAALPQgldtpigEGGAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1331382268 447 CVSALDALIQVQILELLESLQRrfRLSIVFITHDLRVAARlCDRIAVM 494
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
23-236 |
6.15e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 6.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLaDRSEEAMRQLRgRDISMVFQEPMSAL 102
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKS----TLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALR-QQVATVFQDPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NpLMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVglpDPERLRlAYPFE-LSGGQRQRVVIAMALAFDPALLIADEPT 181
Cdd:PRK13638 91 F-YTDIDSDIAFSLRNLGVPEAEITR-RVDEALTLV---DAQHFR-HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 182 SALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVA-QGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
22-251 |
6.46e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 88.36 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEeamrqlRGRDISMVFQEpmSA 101
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKS----TLLRMVAGLERITSGEIWIGGRVVNELEP------ADRDIAMVFQN--YA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQIDETLRAHGVAAARVRR--QRVVDLLGYVGLPDPErlrlayPFELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:PRK11650 87 LYPHMSVRENMAYGLKIRGMPKAEIEErvAEAARILELEPLLDRK------PRELSGGQRQRVAMGRAIVREPAVFLFDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQDKGMALLFITHDfaVVEA--IADRVLVLEKGRvVEQ-GTapavlrvPREDYTR 251
Cdd:PRK11650 161 PLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD--QVEAmtLADRVVVMNGGV-AEQiGT-------PVEVYEK 225
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-256 |
6.69e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.63 E-value: 6.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLR--QLPDPLKVEsGRLVFRDEDLADRSEEAMRqLRgRDISMVF 95
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRmnELESEVRVE-GRVEFFNQNIYERRVNLNR-LR-RQVSMVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 QEPmsALNPlMRVGEQIdetlrAHGVAAARVRRQRVVDLLGYVGLPDPE-------RLRLAyPFELSGGQRQRVVIAMAL 168
Cdd:PRK14258 95 PKP--NLFP-MSVYDNV-----AYGVKIVGWRPKLEIDDIVESALKDADlwdeikhKIHKS-ALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 169 AFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEK-----GRVVEQGTAPAVLR 243
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFN 245
|
250
....*....|...
gi 1331382268 244 VPREDYTRQLLAA 256
Cdd:PRK14258 246 SPHDSRTREYVLS 258
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
292-503 |
6.91e-19 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 85.85 E-value: 6.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwlgreVAGLSEG-RLRALRSDVQMIF---QD 367
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVR-----VAGLVPWkRRKKFLRRIGVVFgqkTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 368 PFASLNPRQTVGQIVMtgplVQGVSKADAERRARELLGLVGLpaaafERFPH----EFSGGQRQRIGIARALAVEPKVLI 443
Cdd:cd03267 106 LWWDLPVIDSFYLLAA----IYDLPPARFKKRLDELSELLDL-----EELLDtpvrQLSLGQRMRAEIAAALLHEPEILF 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 444 ADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:cd03267 177 LDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
18-236 |
7.11e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 86.71 E-value: 7.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRL-VFRDEdladRSEEAMRQLRGRdISMVFQ 96
Cdd:PRK13647 16 DGTKALKGLSLSIPEGSKTALLGPNGAGKS----TLLLHLNGIYLPQRGRVkVMGRE----VNAENEKWVRSK-VGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 97 EPMSALNPlMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLPDperLRLAYPFELSGGQRQRVVIAMALAFDPALLI 176
Cdd:PRK13647 87 DPDDQVFS-STVWDDVAFGPVNMGLDKDEVER-RVEEALKAVRMWD---FRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 177 ADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-236 |
8.73e-19 |
|
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: 85.28 E-value: 8.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 8 HLRIALPAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLR-QLPDplkveSGRLvfrdedladrseeamrQL 86
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPD-----SGTV----------------TV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 87 RGRDISMVfqEPMSALNPLMRVGEQIDETLRAHGVAAARVrRQRVVDLLGYVGLPDperlRLAYPF-ELSGGQRQRVVIA 165
Cdd:cd03220 82 RGRVSSLL--GLGGGFNPELTGRENIYLNGRLLGLSRKEI-DEKIDEIIEFSELGD----FIDLPVkTYSSGMKARLAFA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 166 MALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03220 155 IATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
296-511 |
1.16e-18 |
|
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: 88.73 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGR--CLVRLLRADSGRIEWLGREV--AGLSEGRlralRSDVQMIFQDpfAS 371
Cdd:TIGR02633 15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLkaSNIRDTE----RAGIVIIHQE--LT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 372 LNPRQTVGQIVMTGPLV--QGVSKADAE--RRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADEC 447
Cdd:TIGR02633 89 LVPELSVAENIFLGNEItlPGGRMAYNAmyLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 448 VSALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSED 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-237 |
1.56e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.01 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAkALLRQLPDPlkvESGRLVFRDEDLADRSEEAMRqlrgRDISMVFQEPMsal 102
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVA-ALLQNLYQP---TGGQVLLDGVPLVQYDHHYLH----RQVALVGQEPV--- 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 npLMR--VGEQI--------DETLRAHGVAAArvrrqrVVDLLGyvGLPDperlrlAYPFE-------LSGGQRQRVVIA 165
Cdd:TIGR00958 566 --LFSgsVRENIaygltdtpDEEIMAAAKAAN------AHDFIM--EFPN------GYDTEvgekgsqLSGGQKQRIAIA 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 166 MALAFDPALLIADEPTSALDvttqAQILDLLRKIQQDKGMALLFITHDFAVVEAiADRVLVLEKGRVVEQGT 237
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGT 696
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
22-237 |
2.22e-18 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 88.15 E-value: 2.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDplkVESGRLVFRDEDLADRSEEAMRqlrgRDISMVFQEpMSA 101
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIAN-LLTRFYD---IDEGEILLDGHDLRDYTLASLR----NQVALVSQN-VHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNplmrvgeqidETLrAHGVAAARVRRQRVVDLLgyvglpdpERLRLAYPFE-------------------LSGGQRQRV 162
Cdd:PRK11176 429 FN----------DTI-ANNIAYARTEQYSREQIE--------EAARMAYAMDfinkmdngldtvigengvlLSGGQRQRI 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAiADRVLVLEKGRVVEQGT 237
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLSTIEK-ADEILVVEDGEIVERGT 561
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
28-245 |
2.26e-18 |
|
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: 84.13 E-value: 2.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 28 LQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVfrdedLADRSEEAMRqlrgRDISMVFQE-------PMS 100
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIP----PAKGTVK-----VAGASPGKGW----RHIGYVPQRhefawdfPIS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPLMRVGEQIDETLRAHGVAAARVrrqrVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:TIGR03771 68 VAHTVMSGRTGHIGWLRRPCVADFAA----VRDALRRVGLTELADRPVG---ELSGGQRQRVLVARALATRPSVLLLDEP 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVLeKGRVVEQGTaPAVLRVP 245
Cdd:TIGR03771 141 FTGLDMPTQELLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLL-NGRVIADGT-PQQLQDP 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-233 |
2.37e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 2.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRialpagadRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKAL--LRqlpdplKVESGRLVFRDEDLADRS 79
Cdd:COG1129 255 VVLEVEGLS--------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALfgAD------PADSGEIRLDGKPVRIRS 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 80 -EEAMRQlrGrdISMVfqeP----MSALNPLMRVGEQI-----DETLRAHGVAAARVRR--QRVVDLLGyVGLPDPERL- 146
Cdd:COG1129 321 pRDAIRA--G--IAYV---PedrkGEGLVLDLSIRENItlaslDRLSRGGLLDRRRERAlaEEYIKRLR-IKTPSPEQPv 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 147 RlaypfELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLV 226
Cdd:COG1129 393 G-----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIREL-AAEGKAVIVISSELPELLGLSDRILV 466
|
....*..
gi 1331382268 227 LEKGRVV 233
Cdd:COG1129 467 MREGRIV 473
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
284-503 |
3.07e-18 |
|
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: 82.98 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 284 CSRSGWWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLgrclvrlLRADSGRIEWLGREVAGLSEGR---LRALRSD 360
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTL-------LNALAGRRTGLGVSGEVLINGRpldKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 361 VQMIFQDPFasLNPRQTVGQIVMTgplvqgvskadaerrARELLGLvglpaaaferfphefSGGQRQRIGIARALAVEPK 440
Cdd:cd03213 84 IGYVPQDDI--LHPTLTVRETLMF---------------AAKLRGL---------------SGGERKRVSIALELVSNPS 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 441 VLIADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAA-RLCDRIAVMRKGRVVEQG 503
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPSSEIfELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
4-236 |
3.19e-18 |
|
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: 82.98 E-value: 3.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGADRSHA--LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKveSGrlvfrdEDLADRSEE 81
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGV--SG------EVLINGRPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 AMRQLRGRdISMVFQEPMsaLNPLMRVgeqiDETLRAhgvaAARVRRqrvvdllgyvglpdperlrlaypfeLSGGQRQR 161
Cdd:cd03213 76 DKRSFRKI-IGYVPQDDI--LHPTLTV----RETLMF----AAKLRG-------------------------LSGGERKR 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 162 VVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHD-FAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
273-511 |
3.36e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 83.93 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFcsrsgwwGRRTtqALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEG 352
Cdd:COG1137 3 TLEAENLVKSY-------GKRT--VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 353 RlRALR---------SdvqmIFQDpfasLnprqTVGQIVMtgpLV---QGVSKADAERRARELLGLVGL------PAAAF 414
Cdd:COG1137 74 K-RARLgigylpqeaS----IFRK----L----TVEDNIL---AVlelRKLSKKEREERLEELLEEFGIthlrksKAYSL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 415 erfphefSGGQRQRIGIARALAVEPKVLIADECVSALD--ALIQVQilELLESLQRRfrlSI-VFIT-HDLRVAARLCDR 490
Cdd:COG1137 138 -------SGGERRRVEIARALATNPKFILLDEPFAGVDpiAVADIQ--KIIRHLKER---GIgVLITdHNVRETLGICDR 205
|
250 260
....*....|....*....|.
gi 1331382268 491 IAVMRKGRVVEQGETAALFAD 511
Cdd:COG1137 206 AYIISEGKVLAEGTPEEILNN 226
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
292-511 |
4.11e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 87.86 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREvagLSEGRLRALRSDVQMIFQDPfas 371
Cdd:TIGR00958 491 RPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP---LVQYDHHYLHRQVALVGQEP--- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 372 lnprqtvgqIVMTGPLVQ----GVSKADAERrarellglvgLPAAAFERFPHEF-------------------SGGQRQR 428
Cdd:TIGR00958 565 ---------VLFSGSVREniayGLTDTPDEE----------IMAAAKAANAHDFimefpngydtevgekgsqlSGGQKQR 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 429 IGIARALAVEPKVLIADECVSALDAliqvQILELLESLQRRFRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAAL 508
Cdd:TIGR00958 626 IAIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
...
gi 1331382268 509 FAD 511
Cdd:TIGR00958 701 MED 703
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
273-510 |
4.44e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 85.14 E-value: 4.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSR---SGWWG---------RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIE 340
Cdd:COG4586 1 IIEVENLSKTYRVYekePGLKGalkglfrreYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 341 wlgreVAGLSEGRLR-ALRSDVQMIF------------QDPFAsLNPRqtvgqivmtgplVQGVSKADAERRARELLGLV 407
Cdd:COG4586 81 -----VLGYVPFKRRkEFARRIGVVFgqrsqlwwdlpaIDSFR-LLKA------------IYRIPDAEYKKRLDELVELL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 408 GLpaAAFERFP-HEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAAR 486
Cdd:COG4586 143 DL--GELLDTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEA 220
|
250 260
....*....|....*....|....
gi 1331382268 487 LCDRIAVMRKGRVVEQGETAALFA 510
Cdd:COG4586 221 LCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
25-237 |
4.81e-18 |
|
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: 87.69 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPLkveSGRLVFRDEDLADRSEEAMRQlrgrDISMVFQEPMsalnp 104
Cdd:TIGR03796 497 NFSLTLQPGQRVALVGGSGSGKSTIAK-LVAGLYQPW---SGEILFDGIPREEIPREVLAN----SVAMVDQDIF----- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMR--VGEQIdeTLRAHGVAAARVRR-------QRVVdllgyVGLPDperlrlAYPFEL-------SGGQRQRVVIAMAL 168
Cdd:TIGR03796 564 LFEgtVRDNL--TLWDPTIPDADLVRackdaaiHDVI-----TSRPG------GYDAELaegganlSGGQRQRLEIARAL 630
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 169 AFDPALLIADEPTSALDVTTQAQILDLLRKiqqdKGMALLFITHDFAVVEAiADRVLVLEKGRVVEQGT 237
Cdd:TIGR03796 631 VRNPSILILDEATSALDPETEKIIDDNLRR----RGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGT 694
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
297-510 |
6.76e-18 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 86.69 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLsegRLRALRSDVQMIFQDPFasLNPRQ 376
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPF--LFSDT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGPlvqGVSKADAERRAR------ELLGL-VGLPAAAFERFPHeFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK10789 405 VANNIALGRP---DATQQEIEHVARlasvhdDILRLpQGYDTEVGERGVM-LSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 450 ALDALIQVQILELLeslqRRFRLSIVFITHDLRVAARL-CDRIAVMRKGRVVEQGETAALFA 510
Cdd:PRK10789 481 AVDGRTEHQILHNL----RQWGEGRTVIISAHRLSALTeASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
20-257 |
1.06e-17 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.58 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 20 SHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkvESGRLVFRDEDLADRSEEAMRQLRGrdisMVFQEPM 99
Cdd:COG4138 9 AGRLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-----GQGEILLNGRPLSDWSAAELARHRA----YLSQQQS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 SAlnPLMRVGEQIdeTLRAHGVAAARVRRQRVVDLLGYVGLPDperlRLAYPFE-LSGGQRQRVVIAMAL-----AFDP- 172
Cdd:COG4138 80 PP--FAMPVFQYL--ALHQPAGASSEAVEQLLAQLAEALGLED----KLSRPLTqLSGGEWQRVRLAAVLlqvwpTINPe 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 173 -ALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLrvpredyTR 251
Cdd:COG4138 152 gQLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVM-------TP 223
|
....*.
gi 1331382268 252 QLLAAV 257
Cdd:COG4138 224 ENLSEV 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
294-480 |
1.08e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.07 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlRALRSDVQMIFQDPfasln 373
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP---EIYRQQVSYCAQTP----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 prqtvgqiVMTGPLV--------QGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIAD 445
Cdd:PRK10247 91 --------TLFGDTVydnlifpwQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*
gi 1331382268 446 ECVSALDALIQVQILELLESLQRRFRLSIVFITHD 480
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-234 |
1.17e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.93 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplKVESGRLVFRDEDLadrseeamrqlrGRDISMvfqepms 100
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKG--TPVAGCVDVPDNQF------------GREASL------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 alnplmrvgeqIDETLRAHGVAAArvrrqrvVDLLGYVGLPDPErLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:COG2401 103 -----------IDAIGRKGDFKDA-------VELLNAVGLSDAV-LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 181 TSALDVTTqAQILDL-LRKIQQDKGMALLFITHDFAVVEAIA-DRVLVLEKGRVVE 234
Cdd:COG2401 164 CSHLDRQT-AKRVARnLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-232 |
1.23e-17 |
|
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: 82.13 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAMRqlrgRDISMVFQEPMsal 102
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQ----PQGGQVLLDGKPISQYEHKYLH----SKVSLVGQEPV--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 nplmRVGEQIDETLrAHGVAAARVrrQRVVDLLGYVGLPD-PERLRLAYPFE-------LSGGQRQRVVIAMALAFDPAL 174
Cdd:cd03248 99 ----LFARSLQDNI-AYGLQSCSF--ECVKEAAQKAHAHSfISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 175 LIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAiADRVLVLEKGRV 232
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-243 |
1.25e-17 |
|
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: 85.96 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLrIALPAGADRsHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdPLkveSGRLVFRDEDLADRSEEAm 83
Cdd:COG4618 331 LSVENL-TVVPPGSKR-PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP-PT---AGSVRLDGADLSQWDREE- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 rqlRGRDISMVFQEP-------------MSALNPlmrvgEQIdetlrahgVAAARvrRQRVVDLLgyVGLPD-------P 143
Cdd:COG4618 404 ---LGRHIGYLPQDVelfdgtiaeniarFGDADP-----EKV--------VAAAK--LAGVHEMI--LRLPDgydtrigE 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 144 ERLRLaypfelSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVeAIADR 223
Cdd:COG4618 464 GGARL------SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDK 535
|
250 260
....*....|....*....|
gi 1331382268 224 VLVLEKGRVVEQGTAPAVLR 243
Cdd:COG4618 536 LLVLRDGRVQAFGPRDEVLA 555
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
293-511 |
1.35e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.65 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 293 RTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRA---------------L 357
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQaisvvsqrvhlfsatL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 358 RSDVQMifQDPFASLNPRQTVGQIVMTGPLVQGVSKADAerrareLLGLVGLPaaaferfpheFSGGQRQRIGIARALAV 437
Cdd:PRK11160 431 RDNLLL--AAPNASDEALIEVLQQVGLEKLLEDDKGLNA------WLGEGGRQ----------LSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 438 EPKVLIADECVSALDALIQVQILELL-ESLQRRfrlSIVFITHDLRVAARLcDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLaEHAQNK---TVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQ 563
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
23-231 |
1.55e-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: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDPLKVESGRlvfrdedladrseeamrqlrgrdismvfqepmsa 101
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELePDEGIVTWGS---------------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 lnplmrvgeqidetlrahgvaaarvrrqrvvdllgyvglpdpeRLRLAYpFE-LSGGQRQRVVIAMALAFDPALLIADEP 180
Cdd:cd03221 62 -------------------------------------------TVKIGY-FEqLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 181 TSALDVTTQAQILDLLRKIQQdkgmALLFITHDFAVVEAIADRVLVLEKGR 231
Cdd:cd03221 98 TNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
298-510 |
2.57e-17 |
|
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: 84.80 E-value: 2.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRA----LRSDVQMI--------- 364
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRhigyLPQDVELFdgtiaenia 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 365 -FQDPfaslNPRQTVgqivmtgplvqgvskaDAERRAR--ELLGlvglpaaafeRFPHEF-----------SGGQRQRIG 430
Cdd:COG4618 428 rFGDA----DPEKVV----------------AAAKLAGvhEMIL----------RLPDGYdtrigeggarlSGGQRQRIG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 431 IARALAVEPKVLIADECVSALDALIQVQILELLESLQRRfRLSIVFITHDLRVAArLCDRIAVMRKGRVVEQGETAALFA 510
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
16-237 |
3.24e-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: 85.01 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 16 GADRSHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAMRqlrgRDISMVF 95
Cdd:TIGR03797 462 RPDGPLILDDVSLQIEPGEFVAIVGPSGSGKS----TLLRLLLGFETPESGSVFYDGQDLAGLDVQAVR----RQLGVVL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 Q--EPMSAlnplmRVGEQIdetlrahgVAAARVRRQRVVDLLGYVGLPDPERlrlAYPF-----------ELSGGQRQRV 162
Cdd:TIGR03797 534 QngRLMSG-----SIFENI--------AGGAPLTLDEAWEAARMAGLAEDIR---AMPMgmhtvisegggTLSGGQRQRL 597
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKgmalLFITHDFAVVeAIADRVLVLEKGRVVEQGT 237
Cdd:TIGR03797 598 LIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR----IVIAHRLSTI-RNADRIYVLDAGRVVQQGT 667
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-270 |
4.33e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 82.16 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLR-QLPDplkveSGRLVFRDEDLADRSeeamRQLRGRdISMVFQepMSALN 103
Cdd:PRK13537 25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPD-----AGSISLCGEPVPSRA----RHARQR-VGVVPQ--FDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 104 PLMRVGEQIDETLRAHGVAAARVRRqRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPALLIADEPTSA 183
Cdd:PRK13537 93 PDFTVRENLLVFGRYFGLSAAAARA-LVPPLLEFAKLENKADAKVG---ELSGGMKRRLTLARALVNDPDVLVLDEPTTG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 184 LDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPA---------VLRV--PREDYTRQ 252
Cdd:PRK13537 169 LDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAlieseigcdVIEIygPDPVALRD 247
|
250
....*....|....*...
gi 1331382268 253 LLAavsaqPLVPRTQVAG 270
Cdd:PRK13537 248 ELA-----PLAERTEISG 260
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
153-493 |
4.91e-17 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 84.09 E-value: 4.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 153 ELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAIADRVLVL--EKG 230
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAygEPG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 231 R--VVeqgTAPAVLRVPREDYTRQLLA---------AVSAQPLVPRTQVAGPVVLKAEALGKVFCSRSgwwgrrttqaLD 299
Cdd:PRK13409 290 AygVV---SKPKGVRVGINEYLKGYLPeenmrirpePIEFEERPPRDESERETLVEYPDLTKKLGDFS----------LE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 300 AVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGR------EVAGLSEGRLRALRSDVQMIFQDPFasLN 373
Cdd:PRK13409 357 VEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKisykpqYIKPDYDGTVEDLLRSITDDLGSSY--YK 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PrqtvgQIVmtgplvqgvskadaerrarELLGLVGLpaaaFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:PRK13409 435 S-----EII-------------------KPLQLERL----LDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1331382268 454 LIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAV 493
Cdd:PRK13409 487 EQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMV 526
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
292-501 |
5.48e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 80.00 E-value: 5.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLL--RADSGRIEwlgrevaglsegrlralrsdvqmIFQDPF 369
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVD-----------------------VPDNQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 aslnPRQTvgqivmtgPLVQGVSKADAERRARELLGLVGL-PAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECV 448
Cdd:COG2401 97 ----GREA--------SLIDAIGRKGDFKDAVELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 449 SALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLC-DRIAVMRKGRVVE 501
Cdd:COG2401 165 SHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPE 218
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
16-237 |
7.52e-17 |
|
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: 79.38 E-value: 7.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 16 GADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEEAMRqlrgRDISMVF 95
Cdd:cd03369 17 APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL----EAEEGKIEIDGIDISTIPLEDLR----SSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 96 QEPM----SALNPLMRVGEQIDETLRAhgvaAARVRRQrvvdllgyvGLpdperlrlaypfELSGGQRQRVVIAMALAFD 171
Cdd:cd03369 89 QDPTlfsgTIRSNLDPFDEYSDEEIYG----ALRVSEG---------GL------------NLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKiqQDKGMALLFITHDFAVVeAIADRVLVLEKGRVVEQGT 237
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDH 206
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
296-501 |
9.49e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 9.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGrlRALRSDVQMIFQDpfASLNPR 375
Cdd:PRK11288 18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTT--AALAAGVAIIYQE--LHLVPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 QTVGQIVMTGPLVQG---VSKADAERRARELLGLVGL---PAAAFERfpheFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:PRK11288 94 MTVAENLYLGQLPHKggiVNRRLLNYEAREQLEHLGVdidPDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 450 ALDALIQVQILELLESLQRRFRLsIVFITHDLRVAARLCDRIAVMRKGRVVE 501
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
290-503 |
1.12e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 290 WGRRTTQalDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIeWLGREVAGLSEGRLRALRsdVQMIFQDpf 369
Cdd:PRK10253 17 YGKYTVA--ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV-WLDGEHIQHYASKEVARR--IGLLAQN-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASLNPRQTVGQIVMTG-----PLVQGVSKADAE--RRARELLGLVGLPAAAFErfphEFSGGQRQRIGIARALAVEPKVL 442
Cdd:PRK10253 90 ATTPGDITVQELVARGryphqPLFTRWRKEDEEavTKAMQATGITHLADQSVD----TLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 443 IADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
4-230 |
1.53e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 82.55 E-value: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGADRSHalyDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVFRDedladrseeam 83
Cdd:COG4178 363 LALEDLTLRTPDGRPLLE---DLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPY----GSGRIARPA----------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 rqlrGRDISMVFQEPMsalnplMRVGeqideTLR---AHGVAAARVRRQRVVDLLGYVGLPD-PERLRLAYPFE--LSGG 157
Cdd:COG4178 425 ----GARVLFLPQRPY------LPLG-----TLRealLYPATAEAFSDAELREALEAVGLGHlAERLDEEADWDqvLSLG 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 158 QRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRkiQQDKGMALLFITHDfAVVEAIADRVLVLEKG 230
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLR--EELPGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
38-236 |
2.01e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 38 VVGESGSGKSMLAKAL--LRQlPDplkveSGRLVFRDEDLADRSEEAMRQLRGRDISMVFQEpmSALNPLMRVgeqiDET 115
Cdd:PRK11144 29 IFGRSGAGKTSLINAIsgLTR-PQ-----KGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQD--ARLFPHYKV----RGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 116 LRaHGVAAA-RVRRQRVVDLLGYvglpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILD 194
Cdd:PRK11144 97 LR-YGMAKSmVAQFDKIVALLGI------EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1331382268 195 LLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:PRK11144 170 YLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
23-236 |
2.24e-16 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 78.47 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDpLKVESGRLVFRdedladrSEEAMRQLRGRDISMVFQEpmSAL 102
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEG-GGTTSGQILFN-------GQPRKPDQFQKCVAYVRQD--DIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPLMRVGEQIDET--LRAHGVAAARVRRQRVVD-LLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:cd03234 93 LPGLTVRETLTYTaiLRLPRKSSDAIRKKRVEDvLLRDLAL---TRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 180 PTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
299-508 |
2.87e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 79.04 E-value: 2.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 299 DAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDVQMIFQDP--FASLNPRQ 376
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGalFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQivmtgPLVQGVSKADAERRARELLGL--VGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDAL 454
Cdd:PRK11831 104 NVAY-----PLREHTQLPAPLLHSTVMMKLeaVGLRGAA-KLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 455 IQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:PRK11831 178 TMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
296-512 |
3.85e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.00 E-value: 3.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLraLRSDVQMIFQDpfaslnpR 375
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKI--MREAVAIVPEG-------R 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 QTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPHE---FSGGQRQRIGIARALAVEPKVLIADECVSALD 452
Cdd:PRK11614 90 RVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 453 ALIQVQILELLESLqRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADA 512
Cdd:PRK11614 170 PIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANE 228
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
297-503 |
7.13e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.34 E-value: 7.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSeGRLRAlRSDVQMIFQDpfASLNPRQ 376
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLP-GHQIA-RMGVVRTFQH--VRLFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TV--------GQIVMTGpLVQGVSKADAERRA-RELLGL-------VGLPAAAfERFPHEFSGGQRQRIGIARALAVEPK 440
Cdd:PRK11300 96 TVienllvaqHQQLKTG-LFSGLLKTPAFRRAeSEALDRaatwlerVGLLEHA-NRQAGNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 441 VLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANG 236
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
21-243 |
8.62e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.04 E-value: 8.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDplkveSGRLvfrdedladrseeamrQLRGRdISMVFqEPM 99
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILePT-----SGRV----------------EVNGR-VSALL-ELG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 SALNPLMRVGEQIDETLRAHGVAAARVRR--QRVVDL--LG-YVGLPdperLRlAYpfelSGGQRQRVVIAMALAFDPAL 174
Cdd:COG1134 97 AGFHPELTGRENIYLNGRLLGLSRKEIDEkfDEIVEFaeLGdFIDQP----VK-TY----SSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 175 LIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLR 243
Cdd:COG1134 168 LLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-506 |
8.96e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.77 E-value: 8.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLrqlpDPLKVESGRLVFRDEDLA-DRSEEAMRQlrgrDISMVFQEpms 100
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLF----GIYQKDSGSILFQGKEIDfKSSKEALEN----GISMVHQE--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 aLNpLMRVGEQIDET------LRAHGVAAARVRR--QRVVDLLGYVglPDPeRLRLAypfELSGGQRQRVVIAMALAFDP 172
Cdd:PRK10982 82 -LN-LVLQRSVMDNMwlgrypTKGMFVDQDKMYRdtKAIFDELDID--IDP-RAKVA---TLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 173 ALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQgtapavlrVPREDYTRQ 252
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT--------QPLAGLTMD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 253 LLAAVS-----AQPLVPRTQVAGPVVLKAEALGKVfcsrsgwwgrrTTQALDAVQLQLREGETLGIVGESGSGKSTLGRC 327
Cdd:PRK10982 225 KIIAMMvgrslTQRFPDKENKPGEVILEVRNLTSL-----------RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVET 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 328 LVRLLRADSGRIEWLGREVAGLS--------------EGRLRALRSDVQMIFQDPFASLNPRQTvgqivMTGPLVQGVSK 393
Cdd:PRK10982 294 LFGIREKSAGTITLHGKKINNHNaneainhgfalvteERRSTGIYAYLDIGFNSLISNIRNYKN-----KVGLLDNSRMK 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 394 ADAERrareLLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRlS 473
Cdd:PRK10982 369 SDTQW----VIDSMRVKTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-G 443
|
490 500 510
....*....|....*....|....*....|...
gi 1331382268 474 IVFITHDLRVAARLCDRIAVMRKGRVVEQGETA 506
Cdd:PRK10982 444 IIIISSEMPELLGITDRILVMSNGLVAGIVDTK 476
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
291-504 |
1.01e-15 |
|
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: 79.70 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTqaLDAVQLQLREGETLGIVGESGSGKSTLGRCLVRL-------LRADSGRIEWLGREVAGLSEGRLRalrSDVQM 363
Cdd:TIGR01842 329 GKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIwpptsgsVRLDGADLKQWDRETFGKHIGYLP---QDVEL 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 364 ifqdpfaslnprqtvgqivMTGPLVQGVSKADAERRARELLGLVGLpAAAFE---RFPHEF-----------SGGQRQRI 429
Cdd:TIGR01842 404 -------------------FPGTVAENIARFGENADPEKIIEAAKL-AGVHElilRLPDGYdtvigpggatlSGGQRQRI 463
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 430 GIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRfRLSIVFITHdlRVAARLC-DRIAVMRKGRVVEQGE 504
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITH--RPSLLGCvDKILVLQDGRIARFGE 536
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-242 |
1.32e-15 |
|
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: 79.31 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGADRShaLYDLSLQLNRGECLCVVGESGSGKSMLAKALL-RQLPDPLKVesgRLvfrdeDLADRSEEA 82
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPT--LRGISFSLQAGEALAIIGPSGSGKSTLARLIVgIWPPTSGSV---RL-----DGADLKQWD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLrGRDISMVFQ--EPMSAlnplmRVGEQI---DETLRAHGVAAARVRRQrVVDLLgyVGLPDPERLRLAYPFE-LSG 156
Cdd:TIGR01842 387 RETF-GKHIGYLPQdvELFPG-----TVAENIarfGENADPEKIIEAAKLAG-VHELI--LRLPDGYDTVIGPGGAtLSG 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 157 GQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAiADRVLVLEKGRVVEQG 236
Cdd:TIGR01842 458 GQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHRPSLLGC-VDKILVLQDGRIARFG 535
|
....*.
gi 1331382268 237 TAPAVL 242
Cdd:TIGR01842 536 ERDEVL 541
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
22-227 |
1.37e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 74.96 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdPLkveSGRLvfrdedladrseeamRQLRGRDISMVFQEpmSA 101
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLR-PT---SGTV---------------RRAGGARVAYVPQR--SE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLM--RVGEQIDETLRAHGVAAARVR---RQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPALLI 176
Cdd:NF040873 66 VPDSLplTVRDLVAMGRWARRGLWRRLTrddRAAVDDALERVGLADLAGRQLG---ELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 177 ADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAiADRVLVL 227
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
296-511 |
1.39e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.28 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREV----------AGLSegrlralrsdvqMIF 365
Cdd:PRK10762 18 KALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpkssqeAGIG------------IIH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 366 QDpfasLN--PRQTVGQIVMTG-PLVQGVSKADAER---RARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEP 439
Cdd:PRK10762 86 QE----LNliPQLTIAENIFLGrEFVNRFGRIDWKKmyaEADKLLARLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 440 KVLIADECVSAL-----DALIQVqILELLEslQRRfrlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK10762 161 KVIIMDEPTDALtdtetESLFRV-IRELKS--QGR---GIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED 231
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-236 |
2.35e-15 |
|
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: 74.61 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVEsGRLVFRDEDladrSEEAMRQLRGrDISMVFQEPMSal 102
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVE-GDIHYNGIP----YKEFAEKYPG-EIIYVSEEDVH-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPLMRVGEQIDETLRAHGVAAARVrrqrvvdllgyvglpdperlrlaypfeLSGGQRQRVVIAMALAFDPALLIADEPTS 182
Cdd:cd03233 95 FPTLTVRETLDFALRCKGNEFVRG---------------------------ISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 183 ALDVTTQAQILDLLRKIQQDKGMALLF--------ITHDFavveaiaDRVLVLEKGRVVEQG 236
Cdd:cd03233 148 GLDSSTALEILKCIRTMADVLKTTTFVslyqasdeIYDLF-------DKVLVLYEGRQIYYG 202
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-231 |
2.94e-15 |
|
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: 74.43 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 14 PAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLvfrdedladrseeamrQLRGRdISM 93
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELE----KLSGSV----------------SVPGS-IAY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 94 VFQEP--MSAL---NPLMrvGEQIDETlrahgvaaarvRRQRVVDL--LgyvgLPDPERLrlayPF-------E----LS 155
Cdd:cd03250 71 VSQEPwiQNGTireNILF--GKPFDEE-----------RYEKVIKAcaL----EPDLEIL----PDgdlteigEkginLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILD-LLRKIQQDKGMALLfITHDFAVVEAiADRVLVLEKGR 231
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRIL-VTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-492 |
2.96e-15 |
|
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: 78.44 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKAL---------------------LRQLP--DPLK-----VESGrlVFRD 72
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMagvdkdfngearpqpgikvgyLPQEPqlDPTKtvrenVEEG--VAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 73 EDLADRSEEamrqlrgrdISMVFQEPMSALNPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGyvgLPDPErlrlAYPF 152
Cdd:TIGR03719 97 KDALDRFNE---------ISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALR---CPPWD----ADVT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 153 ELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQildLLRKIQQDKGmALLFITHDFAVVEAIADRVLVLEKG-- 230
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAW---LERHLQEYPG-TVVAVTHDRYFLDNVAGWILELDRGrg 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 231 ----------------RVVEQGTAPAVLR--VPRE-DYTRQ------------------LLAAVSAQ---------PLVP 264
Cdd:TIGR03719 237 ipwegnysswleqkqkRLEQEEKEESARQktLKRElEWVRQspkgrqakskarlaryeeLLSQEFQKrnetaeiyiPPGP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 265 RTqvaGPVVLKAEALGKVFCSRsgwwgrrttQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwlgr 344
Cdd:TIGR03719 317 RL---GDKVIEAENLTKAFGDK---------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE---- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 345 evaglsegrlraLRSDVQMIFQDPF-ASLNPRQTVGQIVMTGPLVQGVSKADAERRAreLLGLVGLPAAAFERFPHEFSG 423
Cdd:TIGR03719 381 ------------IGETVKLAYVDQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRA--YVGRFNFKGSDQQKKVGQLSG 446
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 424 GQRQRIGIARALAVEPKVLIADECVSALDaliqVQILELLESLQRRFRLSIVFITHDlrvaaR-LCDRIA 492
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLD----VETLRALEEALLNFAGCAVVISHD-----RwFLDRIA 507
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
25-243 |
3.00e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.50 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLAD-RSEEAMRQLrgrdiSMVFQEPmsALN 103
Cdd:COG4604 19 DVSLTIPKGGITALIGPNGAGKSTLLSMISRLLP----PDSGEVLVDGLDVATtPSRELAKRL-----AILRQEN--HIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 104 PLMRVGEqidetLrahgVAAAR---------VRRQRVVD-LLGYVGLPDperLRLAYPFELSGGQRQRVVIAMALAFDPA 173
Cdd:COG4604 88 SRLTVRE-----L----VAFGRfpyskgrltAEDREIIDeAIAYLDLED---LADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 174 LLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHD--FAVveAIADRVLVLEKGRVVEQGTA-----PAVLR 243
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDinFAS--CYADHIVAMKDGRVVAQGTPeeiitPEVLS 230
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
264-508 |
3.79e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 3.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 264 PRTQVAGPVVLKAEALGKVFcsrSGwwgrrtTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLG 343
Cdd:PRK15439 2 QTSDTTAPPLLCARSISKQY---SG------VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 344 REVAGLSEGRLRALrsDVQMIFQDPFasLNPRQTVGQIVmtgpLVQGVSKADAERRARELLGLVG------LPAAAFERf 417
Cdd:PRK15439 73 NPCARLTPAKAHQL--GIYLVPQEPL--LFPNLSVKENI----LFGLPKRQASMQKMKQLLAALGcqldldSSAGSLEV- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 418 phefsgGQRQRIGIARALAVEPKVLIADECVSAL-----DALIQvQILELLESlqrrfRLSIVFITHDLRVAARLCDRIA 492
Cdd:PRK15439 144 ------ADRQIVEILRGLMRDSRILILDEPTASLtpaetERLFS-RIRELLAQ-----GVGIVFISHKLPEIRQLADRIS 211
|
250
....*....|....*.
gi 1331382268 493 VMRKGRVVEQGETAAL 508
Cdd:PRK15439 212 VMRDGTIALSGKTADL 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
153-493 |
4.34e-15 |
|
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: 77.90 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 153 ELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVL--EKG 230
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYLADYVHILygEPG 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 231 R--VVeqgTAPAVLRVPREDYTRQLLA---------AVSAQPLVPRTQVAGPVVLKAEALGKVFCSRSgwwgrrttqaLD 299
Cdd:COG1245 291 VygVV---SKPKSVRVGINQYLDGYLPeenvrirdePIEFEVHAPRREKEEETLVEYPDLTKSYGGFS----------LE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 300 AVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGR------EVAGLSEGRLRA-LRSDVQMIFQDPFAsl 372
Cdd:COG1245 358 VEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpqYISPDYDGTVEEfLRSANTDDFGSSYY-- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 373 nprqtvgQIVMTGPLvqGVSKAdAERRARELlglvglpaaaferfphefSGGQRQRIGIARALAVEPKVLIADECVSALD 452
Cdd:COG1245 436 -------KTEIIKPL--GLEKL-LDKNVKDL------------------SGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1331382268 453 ALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAV 493
Cdd:COG1245 488 VEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
273-511 |
4.55e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.93 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSRsgwwgrrttQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwLGREVAGLSEG 352
Cdd:PRK10895 3 TLTAKNLAKAYKGR---------RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII-IDDEDISLLPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 353 RLRALRSdVQMIFQDpfASLNPRQTVGQIVMTG-PLVQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGI 431
Cdd:PRK10895 73 HARARRG-IGYLPQE--ASIFRRLSVYDNLMAVlQIRDDLSAEQREDRANELMEEFHI-EHLRDSMGQSLSGGERRRVEI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 432 ARALAVEPKVLIADECVSALDALIQVQILELLESLqRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFAD 511
Cdd:PRK10895 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
292-506 |
5.83e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.25 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRAD--------SGRIEWLGREVAGLSEGRLRALRSDVQM 363
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 364 IFQDPFASlnprqTVGQIVMTGPLVQGVSKADAERRAREL----LGLVGlPAAAFERFPHEFSGGQRQRIGIARALA--- 436
Cdd:PRK13547 91 AAQPAFAF-----SAREIVLLGRYPHARRAGALTHRDGEIawqaLALAG-ATALVGRDVTTLSGGELARVQFARVLAqlw 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 437 ------VEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETA 506
Cdd:PRK13547 165 pphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
25-238 |
6.67e-15 |
|
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: 74.12 E-value: 6.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLadrSEEAMRQLRGRDISMVFQEPmSALNP 104
Cdd:cd03218 18 GVSLSVKQGEIVGLLGPNGAGKT----TTFYMIVGLVKPDSGKILLDGQDI---TKLPMHKRARLGIGYLPQEA-SIFRK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMrVGEQIDETLRAHGVAAARvRRQRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSAL 184
Cdd:cd03218 90 LT-VEENILAVLEIRGLSKKE-REEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 185 DVTTqaqILDLLRKIQQ--DKGMALLfIThDFAVVE--AIADRVLVLEKGRVVEQGTA 238
Cdd:cd03218 165 DPIA---VQDIQKIIKIlkDRGIGVL-IT-DHNVREtlSITDRAYIIYEGKVLAEGTP 217
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-236 |
7.50e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.64 E-value: 7.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVFRDEDLADRSEEAMRQlrgrdISMVFQepMSALNP 104
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSP----DAGKITVLGVPVPARARLARAR-----IGVVPQ--FDNLDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVGEQIDETLRAHGVAAaRVRRQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMALAFDPALLIADEPTSAL 184
Cdd:PRK13536 128 EFTVRENLLVFGRYFGMST-REIEAVIPSLLEFARLESKADARVS---DLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 185 DVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQG 236
Cdd:PRK13536 204 DPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
298-510 |
1.38e-14 |
|
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: 76.91 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPfaslnprqt 377
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFKITIIPQDP--------- 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 vgqIVMTGPLVQGV----SKADAE-RRARELLGLVGLPAAAFERFPHE-------FSGGQRQRIGIARALAVEPKVLIAD 445
Cdd:TIGR00957 1370 ---VLFSGSLRMNLdpfsQYSDEEvWWALELAHLKTFVSALPDKLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 446 ECVSALDA----LIQVQILELLESlqrrfrLSIVFITHDLRVAARLCdRIAVMRKGRVVEQGETAALFA 510
Cdd:TIGR00957 1447 EATAAVDLetdnLIQSTIRTQFED------CTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
22-270 |
1.41e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 76.29 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEEAmrqLRGRdISMVFQEPM-- 99
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHF----DVSEGDIRFHDIPLTKLQLDS---WRSR-LAVVSQTPFlf 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 -------SALNPLMRVGEQIDETLRAHGVAAarvrrqrvvDLLgyvglpdpeRLRLAYPFE-------LSGGQRQRVVIA 165
Cdd:PRK10789 402 sdtvannIALGRPDATQQEIEHVARLASVHD---------DIL---------RLPQGYDTEvgergvmLSGGQKQRISIA 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 166 MALAFDPALLIADEPTSALDVTTQAQILDLLRkiQQDKGMALLFITHDF-AVVEaiADRVLVLEKGRVVEQGTAPAVLRV 244
Cdd:PRK10789 464 RALLLNAEILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLsALTE--ASEILVMQHGHIAQRGNHDQLAQQ 539
|
250 260 270
....*....|....*....|....*....|
gi 1331382268 245 P---REDYT-RQLLAAVSAQPLVPRTQVAG 270
Cdd:PRK10789 540 SgwyRDMYRyQQLEAALDDAPEIREEAVDA 569
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-229 |
1.54e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 71.42 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGADRshaLYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFrdedladrseeam 83
Cdd:cd03223 1 IELENLSLATPDGRVL---LKDLSFEIKPGDRLLITGPSGTGKS----SLFRALAGLWPWGSGRIGM------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 rqLRGRDISMVFQEPmsalnpLMRVGeqideTLRAhgvaaarvrrqrvvdllgyvglpdperlRLAYPF--ELSGGQRQR 161
Cdd:cd03223 61 --PEGEDLLFLPQRP------YLPLG-----TLRE----------------------------QLIYPWddVLSGGEQQR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 162 VVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRkiqqDKGMALLFITHDfAVVEAIADRVLVLEK 229
Cdd:cd03223 100 LAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK----ELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
297-481 |
2.10e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 75.86 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALrsdVQMIFQDP--FASlnp 374
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR---VSVCAQDAhlFDT--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 rqTVGQIVMTG-PLVQGVSKADAERRARELLGLVGLPAAAFERFpHE----FSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:TIGR02868 424 --TVRENLRLArPDATDEELWAALERVGLADWLRALPDGLDTVL-GEggarLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|...
gi 1331382268 450 ALDALIQVQILE-LLESLQRRfrlSIVFITHDL 481
Cdd:TIGR02868 501 HLDAETADELLEdLLAALSGR---TVVLITHHL 530
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-238 |
2.18e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVES-----GRLVFRDEDLA 76
Cdd:PRK09984 3 TIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShiellGRTVQREGRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 77 drseEAMRQLRGRdISMVFQEpmsaLNPLMRVGEQIDETLRAHGVAA---------ARVRRQRVVDLLGYVGLPDPERLR 147
Cdd:PRK09984 79 ----RDIRKSRAN-TGYIFQQ----FNLVNRLSVLENVLIGALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 148 LAypfELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVL 227
Cdd:PRK09984 150 VS---TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVAL 226
|
250
....*....|.
gi 1331382268 228 EKGRVVEQGTA 238
Cdd:PRK09984 227 RQGHVFYDGSS 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-242 |
2.56e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.60 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLAD-RSEEAMRQlrgrDISMVFQEpm 99
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKT----TLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMRE----AVAIVPEG-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 salnplMRVGEQ--IDETLRAHGVAAARVRRQ----RVVDLLgyvglPDPERLRLAYPFELSGGQRQRVVIAMALAFDPA 173
Cdd:PRK11614 89 ------RRVFSRmtVEENLAMGGFFAERDQFQerikWVYELF-----PRLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 174 LLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVL 242
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
298-479 |
2.88e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 75.23 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLgrclvrlLRAdsgriewlgreVAGL---SEGRLRaLRSDVQMIF--QDPF--- 369
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTL-------LRA-----------IAGLwpyGSGRIA-RPAGARVLFlpQRPYlpl 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASLnpRQtvgqiVMTGPlvQGVSKADAERrARELLGLVGLPAAAfERF------PHEFSGGQRQRIGIARALAVEPKVLI 443
Cdd:COG4178 440 GTL--RE-----ALLYP--ATAEAFSDAE-LREALEAVGLGHLA-ERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLF 508
|
170 180 190
....*....|....*....|....*....|....*.
gi 1331382268 444 ADECVSALDALIQVQILELLesLQRRFRLSIVFITH 479
Cdd:COG4178 509 LDEATSALDEENEAALYQLL--REELPGTTVISVGH 542
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-252 |
2.98e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 72.89 E-value: 2.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLR--QLPDPLKVEsGRLVFRDEDLADRSEEAMrQLRGRdISMVFQEPm 99
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlnDLIPGFRVE-GKVTFHGKNLYAPDVDPV-EVRRR-IGMVFQKP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 salNPLMR-VGEQIDETLRAHGVAA------ARVRRQ-----RVVDLLGYVGLpdperlrlaypfELSGGQRQRVVIAMA 167
Cdd:PRK14243 101 ---NPFPKsIYDNIAYGARINGYKGdmdelvERSLRQaalwdEVKDKLKQSGL------------SLSGGQQQRLCIARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 168 LAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDkgMALLFITHDFAVVEAIAD-----RVLVLEK----GRVVEQGTA 238
Cdd:PRK14243 166 IAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDmtaffNVELTEGggryGYLVEFDRT 243
|
250
....*....|....
gi 1331382268 239 PAVLRVPREDYTRQ 252
Cdd:PRK14243 244 EKIFNSPQQQATRD 257
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
298-503 |
3.18e-14 |
|
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: 71.40 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRL--LRADSGRIEWLGREVAGLS-EGRLRAlrsDVQMIFQDPfaslnp 374
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPpEERARL---GIFLAFQYP------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 rqtvgqivmtgPLVQGVSKADaerrarellglvglpaaaFERFPHE-FSGGQRQRIGIARALAVEPKVLIADECVSALDa 453
Cdd:cd03217 87 -----------PEIPGVKNAD------------------FLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 454 liqVQILELLESLQRRFR---LSIVFITHDLRVAARL-CDRIAVMRKGRVVEQG 503
Cdd:cd03217 137 ---IDALRLVAEVINKLReegKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
23-263 |
3.30e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 3.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAMrqlrGRDISMVFQEPMSAL 102
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKT----TLLRAINGTLTPTAGTVLVAGDDVEALSARAA----SRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 N-------------PLMRVGEQIDETLRAHGVAAARVRRQRVVDllgyvglpdperlrlaYPF-ELSGGQRQRVVIAMAL 168
Cdd:PRK09536 91 EfdvrqvvemgrtpHRSRFDTWTETDRAAVERAMERTGVAQFAD----------------RPVtSLSGGERQRVLLARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 169 AFDPALLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPRed 248
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADT-- 231
|
250
....*....|....*
gi 1331382268 249 ytrqLLAAVSAQPLV 263
Cdd:PRK09536 232 ----LRAAFDARTAV 242
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-213 |
4.44e-14 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 74.70 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 4 LSVEHLRIALPAGADrshALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPlkveSGRLVFRDEDLADRSEEAM 83
Cdd:TIGR02868 335 LELRDLSAGYPGAPP---VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL----QGEVTLDGVPVSSLDQDEV 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 84 RqlrgRDISMVFQEPMSalnplmrVGEQIDETLRahgVAAARVRRQRVVDLLGYVGLPD-PERLRLAYPFE-------LS 155
Cdd:TIGR02868 408 R----RRVSVCAQDAHL-------FDTTVRENLR---LARPDATDEELWAALERVGLADwLRALPDGLDTVlgeggarLS 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqqDKGMALLFITHD 213
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITHH 529
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
298-518 |
4.53e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.54 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQ----------- 366
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQapvlfsgtvrf 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 367 --DPFASLNprqtvgqivmTGPLVQGVSKA---DAERRARellglVGLPAAAFERfPHEFSGGQRQRIGIARALAVEPKV 441
Cdd:PLN03130 1332 nlDPFNEHN----------DADLWESLERAhlkDVIRRNS-----LGLDAEVSEA-GENFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 442 LIADECVSAL----DALIQVQILElleslqrRFRLSIVFIthdlrVAARL-----CDRIAVMRKGRVVEQGETAALFADA 512
Cdd:PLN03130 1396 LVLDEATAAVdvrtDALIQKTIRE-------EFKSCTMLI-----IAHRLntiidCDRILVLDAGRVVEFDTPENLLSNE 1463
|
....*.
gi 1331382268 513 RHPYTR 518
Cdd:PLN03130 1464 GSAFSK 1469
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-237 |
5.15e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.50 E-value: 5.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 26 LSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkvESGRLVFRDEDLADRSEEAMRQlrgrDISMVFQEPM----SA 101
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-----YQGSLKINGIELRELDPESWRK----HLSWVGQNPQlphgTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGEQIDETLRAHGVAAARVrrQRVVDLLGyvglpdperLRLAYPFE-----LSGGQRQRVVIAMALAFDPALLI 176
Cdd:PRK11174 440 RDNVLLGNPDASDEQLQQALENAWV--SEFLPLLP---------QGLDTPIGdqaagLSVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 177 ADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAIaDRVLVLEKGRVVEQGT 237
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGD 566
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
154-254 |
5.23e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVV 233
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
90 100
....*....|....*....|.
gi 1331382268 234 EQGTapavlrvPREDYTRQLL 254
Cdd:PRK10253 224 AQGA-------PKEIVTAELI 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
296-500 |
6.43e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.00 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGrlRALRSDVQMIFQDpfasLNP- 374
Cdd:PRK10982 12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK--EALENGISMVHQE----LNLv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQT-------VGQIVMTGPLVqgvskaDAERRAREllglvglPAAAFERF-----PHE----FSGGQRQRIGIARALAVE 438
Cdd:PRK10982 86 LQRsvmdnmwLGRYPTKGMFV------DQDKMYRD-------TKAIFDELdididPRAkvatLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 439 PKVLIADECVSALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVV 500
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
287-518 |
1.03e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 74.24 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 287 SGWWGRRTTQALDaVQLQLREG---------------ETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVA--GL 349
Cdd:PLN03232 1227 SGWPSRGSIKFED-VHLRYRPGlppvlhglsffvspsEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfGL 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 350 SEGRlRALRSDVQ--MIFQ-------DPFASLNprqtvgqivmTGPLVQGVSKA---DAERRARellglVGLPAAAFERf 417
Cdd:PLN03232 1306 TDLR-RVLSIIPQspVLFSgtvrfniDPFSEHN----------DADLWEALERAhikDVIDRNP-----FGLDAEVSEG- 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 418 PHEFSGGQRQRIGIARALAVEPKVLIADECVSAL----DALIQVQILELLESlqrrfrLSIVFITHDLRVAARlCDRIAV 493
Cdd:PLN03232 1369 GENFSVGQRQLLSLARALLRRSKILVLDEATASVdvrtDSLIQRTIREEFKS------CTMLVIAHRLNTIID-CDKILV 1441
|
250 260
....*....|....*....|....*
gi 1331382268 494 MRKGRVVEQGETAALFADARHPYTR 518
Cdd:PLN03232 1442 LSSGQVLEYDSPQELLSRDTSAFFR 1466
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
23-242 |
1.33e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.21 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkVESGRLVFRDEDLADRSEEAMRQlrgrDISMVFQEPMSal 102
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP----LTEGEIRLDGRPLSSLSHSVLRQ----GVAMVQQDPVV-- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 nplmrvgeqIDETLRAHGVAAARVRRQRVVDLLGYV-------GLPDPERLRLAypfE----LSGGQRQRVVIAMALAFD 171
Cdd:PRK10790 427 ---------LADTFLANVTLGRDISEEQVWQALETVqlaelarSLPDGLYTPLG---EqgnnLSVGQKQLLALARVLVQT 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 172 PALLIADEPTSALDVTTQAQILDLLRKIQQDKgmALLFITHDFA-VVEaiADRVLVLEKGRVVEQGTAPAVL 242
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAHRLStIVE--ADTILVLHRGQAVEQGTHQQLL 562
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-242 |
1.37e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDplkvESGRLVFRDEDLADRSEEAmRQLRGrdISMVFQEP-----M 99
Cdd:PRK10895 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPR----DAGNIIIDDEDISLLPLHA-RARRG--IGYLPQEAsifrrL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 SALNPLMRVgEQIDETLrahgvaAARVRRQRVVDLLGYVGLpdpERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADE 179
Cdd:PRK10895 94 SVYDNLMAV-LQIRDDL------SAEQREDRANELMEEFHI---EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 180 PTSALDVTTqaqILDLLRKIQ--QDKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVL 242
Cdd:PRK10895 164 PFAGVDPIS---VIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-243 |
1.38e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.01 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGAdrshALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVE----SGRLVFRDEDLAdr 78
Cdd:PRK13547 1 MLTADHLHVARRHRA----ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGAPRgarvTGDVTLNGEPLA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 79 SEEAMRQLRGRDISMVFQEPMSALNplmrVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPFELSGGQ 158
Cdd:PRK13547 75 AIDAPRLARLRAVLPQAAQPAFAFS----AREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 159 RQRVVIAMALA---------FDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEK 229
Cdd:PRK13547 151 LARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLAD 230
|
250
....*....|....
gi 1331382268 230 GRVVEQGTAPAVLR 243
Cdd:PRK13547 231 GAIVAHGAPADVLT 244
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
25-212 |
2.02e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.13 E-value: 2.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLAD-RSEEAMRQLRGRDismvfqepmsALN 103
Cdd:PRK13539 20 GLSFTLAAGEALVLTGPNGSGKT----TLLRLIAGLLPPAAGTIKLDGGDIDDpDVAEACHYLGHRN----------AMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 104 PLMRVGEQID---ETLRAH--GVAAArvrrqrvvdlLGYVGLPDPERLRLAYpfeLSGGQRQRVVIAMALAFDPALLIAD 178
Cdd:PRK13539 86 PALTVAENLEfwaAFLGGEelDIAAA----------LEAVGLAPLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|....
gi 1331382268 179 EPTSALDVTTQAQILDLLRKIQQDKGMALLfITH 212
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLAQGGIVIA-ATH 185
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-249 |
2.11e-13 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 69.67 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKS----MLAkALLRqlPDplkveSGRLVFRDEDLa 76
Cdd:COG1137 1 MMTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTttfyMIV-GLVK--PD-----SGRIFLDGEDI- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 77 drSEEAM--RQLRGrdISMVFQEP-----MSALNPLMRVGEQIDETlrahgvaaARVRRQRVVDLLGYVGLpdpERLRLA 149
Cdd:COG1137 68 --THLPMhkRARLG--IGYLPQEAsifrkLTVEDNILAVLELRKLS--------KKEREERLEELLEEFGI---THLRKS 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 150 YPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLfIThDFAVVE--AIADRVLVL 227
Cdd:COG1137 133 KAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGVL-IT-DHNVREtlGICDRAYII 209
|
250 260
....*....|....*....|....
gi 1331382268 228 EKGRVVEQGTAPAVLRVP--REDY 249
Cdd:COG1137 210 SEGKVLAEGTPEEILNNPlvRKVY 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
313-510 |
2.14e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.83 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 313 IVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEgrlRALRSDVQMIFQDPfaslnprqtvgqIVMTGPLVQGVS 392
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQGVAMVQQDP------------VVLADTFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 393 --KADAERRARELLGLV-------GLPAAAFERFPHE---FSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQIL 460
Cdd:PRK10790 437 lgRDISEEQVWQALETVqlaelarSLPDGLYTPLGEQgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQ 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 461 ELLESLqrRFRLSIVFITHDLR--VAArlcDRIAVMRKGRVVEQGETAALFA 510
Cdd:PRK10790 517 QALAAV--REHTTLVVIAHRLStiVEA---DTILVLHRGQAVEQGTHQQLLA 563
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-236 |
3.76e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.91 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 22 ALYDLSLQLNRGECLCVVGESGSGKSMLAKALLrqlpDPLKVESGRLVFrdedLADRSEEAMRQlrgrdiSMVFQEPMSa 101
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALM----GFVRLASGKISI----LGQPTRQALQK------NLVAYVPQS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 lnplmrvgEQID---ETLRAHGVAAARV------------RRQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAM 166
Cdd:PRK15056 87 --------EEVDwsfPVLVEDVVMMGRYghmgwlrrakkrDRQIVTAALARVDMVEFRHRQIG---ELSGGQKKRVFLAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 167 ALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVlVLEKGRVVEQG 236
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASG 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
290-481 |
5.43e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 290 WGRRttQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwlgrevaglsegRLRALRSDV--QMIFQD 367
Cdd:PRK09544 14 FGQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------RNGKLRIGYvpQKLYLD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 368 PFASLnprqTVGQIVMTGPlvqGVSKADAerrareLLGLVGLPAAAFERFP-HEFSGGQRQRIGIARALAVEPKVLIADE 446
Cdd:PRK09544 80 TTLPL----TVNRFLRLRP---GTKKEDI------LPALKRVQAGHLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|....*
gi 1331382268 447 CVSALDALIQVQILELLESLQRRFRLSIVFITHDL 481
Cdd:PRK09544 147 PTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-227 |
8.20e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 8.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 1 MTLLSVEHLRIALpagaDRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRqlpdplkvesgrLVFRDEDLADRSE 80
Cdd:PRK09544 2 TSLVSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLG------------LVAPDEGVIKRNG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 81 eamrQLRgrdISMVFQEpmSALNPLMRVGEQIDETLRAhGVAAARVrrqrvvdllgyvgLPDPERLRLAYPFE-----LS 155
Cdd:PRK09544 66 ----KLR---IGYVPQK--LYLDTTLPLTVNRFLRLRP-GTKKEDI-------------LPALKRVQAGHLIDapmqkLS 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 156 GGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVL 227
Cdd:PRK09544 123 GGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
297-486 |
1.42e-12 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 66.49 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSdvqmifqdpfASLNPRQ 376
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEVPDS----------LPLTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TV--GQIVMTGPLvqGVSKADAERRARELLGLVGLpaAAFERFP-HEFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:NF040873 77 LVamGRWARRGLW--RRLTRDDRAAVDDALERVGL--ADLAGRQlGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|...
gi 1331382268 454 LIQVQILELLESLQRRFRlSIVFITHDLRVAAR 486
Cdd:NF040873 153 ESRERIIALLAEEHARGA-TVVVVTHDLELVRR 184
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
23-246 |
1.52e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkvESGRLVFRDEDLADRSEEAMRQLRGrdisMVFQEPMSAl 102
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-----GSGSIQFAGQPLEAWSAAELARHRA----YLSQQQTPP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 nPLMRVGEQIDETLRAHgvAAARVRRQRVVDLLGYVGLPDperlRLAYPF-ELSGGQRQRVVIAMA-LAFDPA------L 174
Cdd:PRK03695 82 -FAMPVFQYLTLHQPDK--TRTEAVASALNEVAEALGLDD----KLGRSVnQLSGGEWQRVRLAAVvLQVWPDinpagqL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 175 LIADEPTSALDVTTQAQILDLLRKIQQdKGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGTAPAVLRVPR 246
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
298-498 |
1.96e-12 |
|
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: 64.78 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWlgrevaglsegrlralrsdvqmifqdpfaslNPRQT 377
Cdd:cd03221 16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-------------------------------GSTVK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 VGQivmtgplvqgvskadaerrarellglvglpaaaferFPHeFSGGQRQRIGIARALAVEPKVLIADECVSALDaliqV 457
Cdd:cd03221 65 IGY------------------------------------FEQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNHLD----L 103
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1331382268 458 QILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGR 498
Cdd:cd03221 104 ESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
298-500 |
2.00e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.59 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLG------------REVAG-----LSEG------RL 354
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdppRNVEGtvydfVAEGieeqaeYL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 355 RALRSDVQMIFQDPFAS-LNPRQTVGQIVMTGPLVQgvskadAERRARELLGLVGLPAaafERFPHEFSGGQRQRIGIAR 433
Cdd:PRK11147 99 KRYHDISHLVETDPSEKnLNELAKLQEQLDHHNLWQ------LENRINEVLAQLGLDP---DAALSSLSGGWLRKAALGR 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 434 ALAVEPKVLIADECVSALDaliqVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVV 500
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
26-219 |
2.62e-12 |
|
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: 65.84 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 26 LSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAMRQlrgrdisMVFQEPMSALNPL 105
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKT----TLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHEN-------ILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 106 MRVGEQIDETLRAHGVAaarvrRQRVVDLLGYVGLPDPERLRLAYpfeLSGGQRQRVVIAMALAFDPALLIADEPTSALD 185
Cdd:TIGR01189 88 LSALENLHFWAAIHGGA-----QRTIEDALAAVGLTGFEDLPAAQ---LSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180 190
....*....|....*....|....*....|....
gi 1331382268 186 VTTQAQILDLLRKIQQDKGMALLFITHDFAVVEA 219
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
296-508 |
3.10e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 67.84 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 296 QALDAVQLQLREGETLGIVGESGSGKSTlGRCLVRLLRADSGRIEW------LGREVAGLSEGRLRALRSDVQmifqdpf 369
Cdd:NF000106 27 KAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWrf*twcANRRALRRTIG*HRPVR*GRR------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ASLNPRQtvgQIVMTGPLVQgVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIGIARALAVEPKVLIADECVS 449
Cdd:NF000106 99 ESFSGRE---NLYMIGR*LD-LSRKDARARADELLERFSLTEAA-GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 450 ALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAAL 508
Cdd:NF000106 174 GLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
292-512 |
3.46e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 66.83 E-value: 3.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAglsegrlRALRSD-VQMIFQDPFA 370
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR-------QALQKNlVAYVPQSEEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SLNPRQTVGQIVMTGPL--VQGVSKADAERRARELLGLVGLPAAAFE-RFPHEFSGGQRQRIGIARALAVEPKVLIADEC 447
Cdd:PRK15056 90 DWSFPVLVEDVVMMGRYghMGWLRRAKKRDRQIVTAALARVDMVEFRhRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 448 VSALDALIQVQILELLESLQRRFRLSIVfITHDLRVAARLCDrIAVMRKGRVVEQGETAALFADA 512
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLV-STHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTAE 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
271-515 |
3.50e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.92 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 271 PVVLKAEALGKVFCS----RSGWWGRRTT-QALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRAD---SGRIEWL 342
Cdd:TIGR00955 9 DVFGRVAQDGSWKQLvsrlRGCFCRERPRkHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 343 GREVaGLSEgrLRALRSDVQmifQDP--FASLNPRQtvgQIVMTGPLVQGVSKADAERRAR--ELLGLVGLPAAAFERFP 418
Cdd:TIGR00955 89 GMPI-DAKE--MRAISAYVQ---QDDlfIPTLTVRE---HLMFQAHLRMPRRVTKKEKRERvdEVLQALGLRKCANTRIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 419 HE-----FSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRLSIVFI---THDLrvaARLCDR 490
Cdd:TIGR00955 160 VPgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIhqpSSEL---FELFDK 236
|
250 260
....*....|....*....|....*...
gi 1331382268 491 IAVMRKGRVVEQG---ETAALFADARHP 515
Cdd:TIGR00955 237 IILMAEGRVAYLGspdQAVPFFSDLGHP 264
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
153-228 |
3.85e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.68 E-value: 3.85e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 153 ELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLE 228
Cdd:PRK13409 453 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
298-503 |
4.75e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 69.04 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDP--FASlnpr 375
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYG---LRELRRQFSMIPQDPvlFDG---- 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 qTVGQIVmtGPLVQGVSkadAER-RARELLGLVGLPAAAFERFPH-------EFSGGQRQRIGIARALAVEPKVLI-ADE 446
Cdd:PTZ00243 1399 -TVRQNV--DPFLEASS---AEVwAALELVGLRERVASESEGIDSrvleggsNYSVGQRQLMCMARALLKKGSGFIlMDE 1472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 447 CVS----ALDALIQVQILELLESlqrrfrLSIVFITHDLRVAARlCDRIAVMRKGRVVEQG 503
Cdd:PTZ00243 1473 ATAnidpALDRQIQATVMSAFSA------YTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
297-503 |
5.02e-12 |
|
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: 68.89 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglsEGRLRALRSDVQMIFQDPFasLNPRQ 376
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQSLGMCPQHNI--LFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERfPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQ 456
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEE-AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1331382268 457 VQILELLesLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQG 503
Cdd:TIGR01257 1098 RSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
295-508 |
6.05e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 67.95 E-value: 6.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLrADSGRIEWLGREvagLSEGRLRALRSDVQMIFQDPfasLNP 374
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIE---LRELDPESWRKHLSWVGQNP---QLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 RQTVGQ-IVMTGP------LVQGVSKADA-ERRARELLGL---VGLPAAAFerfphefSGGQRQRIGIARALAVEPKVLI 443
Cdd:PRK11174 436 HGTLRDnVLLGNPdasdeqLQQALENAWVsEFLPLLPQGLdtpIGDQAAGL-------SVGQAQRLALARALLQPCQLLL 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 444 ADECVSALDALIQVQILELLESLQRrfRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAAL 508
Cdd:PRK11174 509 LDEPTASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAEL 570
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
153-238 |
7.04e-12 |
|
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: 67.89 E-value: 7.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 153 ELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEkGRV 232
Cdd:COG1245 455 DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GEP 533
|
....*.
gi 1331382268 233 VEQGTA 238
Cdd:COG1245 534 GVHGHA 539
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
298-479 |
1.34e-11 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 62.94 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwlgrevaglsegrlRALRSDVQMIFQDPFaslnprqt 377
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------------MPEGEDLLFLPQRPY-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 vgqivmtgpLVQGvskadaerRARELLglvglpaaafeRFP--HEFSGGQRQRIGIARALAVEPKVLIADECVSALDALI 455
Cdd:cd03223 75 ---------LPLG--------TLREQL-----------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|....
gi 1331382268 456 QVQILELLESLqrrfRLSIVFITH 479
Cdd:cd03223 127 EDRLYQLLKEL----GITVISVGH 146
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-238 |
1.37e-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: 64.74 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 30 LNRGECLCVVGESGSGKSMLAKALlrqlpdplkveSGRLvfrdedladRSEEAMRQLRGRDISMVFQEpMSALNPlMRVG 109
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKML-----------AGVL---------KPDEGDIEIELDTVSYKPQY-IKADYE-GTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 110 EQIDETLRAHGVAAarVRRQRVVDLLGYVGLPDPERLrlaypfELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQ 189
Cdd:cd03237 80 DLLSSITKDFYTHP--YFKTEIAKPLQIEQILDREVP------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 190 AQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEkGRVVEQGTA 238
Cdd:cd03237 152 LMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGVA 199
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
294-498 |
2.79e-11 |
|
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: 62.87 E-value: 2.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 294 TTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGReVAglsegrlralrsdvqmifqdpFASLN 373
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-IA---------------------YVSQE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 P---RQTVGQ-IVMTGPLvqgvskaDAERRARellglVgLPAAAFER----FPH-------E----FSGGQRQRIGIARA 434
Cdd:cd03250 75 PwiqNGTIREnILFGKPF-------DEERYEK-----V-IKACALEPdleiLPDgdlteigEkginLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 435 LAVEPKVLIADECVSALDALIQVQILE-LLESLQRRFRlSIVFITHDLRVAARlCDRIAVMRKGR 498
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNK-TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
298-517 |
5.64e-11 |
|
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: 63.00 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSegrLRALRSDVQMIFQDPFA------- 370
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILfsgsirf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SLNPRQTVGQivmtGPLVQGVSKADAERRARELLGlvGLPAAAFERfPHEFSGGQRQRIGIARALAVEPKVLIADECVSA 450
Cdd:cd03288 114 NLDPECKCTD----DRLWEALEIAQLKNMVKSLPG--GLDAVVTEG-GENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 451 LDALIQvQILE--LLESLQRRfrlSIVFITHdlRVAARL-CDRIAVMRKGRVVEQGETAALFADARHPYT 517
Cdd:cd03288 187 IDMATE-NILQkvVMTAFADR---TVVTIAH--RVSTILdADLVLVLSRGILVECDTPENLLAQEDGVFA 250
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-242 |
8.93e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 8.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEEAMRqlrgRDISMVFQEPM--- 99
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV----ELEKGRIMIDDCDVAKFGLTDLR----RVLSIIPQSPVlfs 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 ----SALNPLmrvGEQIDETLRAhgvAAARVRRQRVVDLLGYvGLpDPERLRLAYPFelSGGQRQRVVIAMALAFDPALL 175
Cdd:PLN03232 1324 gtvrFNIDPF---SEHNDADLWE---ALERAHIKDVIDRNPF-GL-DAEVSEGGENF--SVGQRQLLSLARALLRRSKIL 1393
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 176 IADEPTSALDVTTQAQILDLLRkiQQDKGMALLFITHDFAVVeAIADRVLVLEKGRVVEQGTAPAVL 242
Cdd:PLN03232 1394 VLDEATASVDVRTDSLIQRTIR--EEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELL 1457
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
293-504 |
1.80e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 293 RTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGrevaglsegrlralrsDVQMIFQDpfASL 372
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----------------EVSVIAIS--AGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 373 NPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLpaAAFERFP-HEFSGGQRQRIGIARALAVEPKVLIADECVSAL 451
Cdd:PRK13546 97 SGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSEL--GEFIYQPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 452 DALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGE 504
Cdd:PRK13546 175 DQTFAQKCLDKIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGE 226
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-236 |
2.17e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.96 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRIALPAGAdrshALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQlpDPLKVESGRLVFRDEDLADRSEEa 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKA----ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGR--EDYEVTGGTVEFKGKDLLELSPE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 mrQLRGRDISMVFQEPMSalnpLMRVGEQIdeTLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPFEL-------- 154
Cdd:PRK09580 74 --DRAGEGIFMAFQYPVE----IPGVSNQF--FLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLltrsvnvg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 155 -SGGQRQRVVIAMALAFDPALLIADEPTSALDV---TTQAQILDLLRkiqqDKGMALLFITHDFAVVEAIA-DRVLVLEK 229
Cdd:PRK09580 146 fSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalKIVADGVNSLR----DGKRSFIIVTHYQRILDYIKpDYVHVLYQ 221
|
....*..
gi 1331382268 230 GRVVEQG 236
Cdd:PRK09580 222 GRIVKSG 228
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-238 |
2.90e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 2 TLLSVEHLRialpAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQlPDpLKVESGRLVFRDEDLADRSEE 81
Cdd:CHL00131 6 PILEIKNLH----ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH-PA-YKILEGDILFKGESILDLEPE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 82 aMRQLRGrdISMVFQepmsalNPLMRVGEQIDETLRAhgvaAARVRRQrvvdllgYVGLPDPERLRLaypFEL------- 154
Cdd:CHL00131 80 -ERAHLG--IFLAFQ------YPIEIPGVSNADFLRL----AYNSKRK-------FQGLPELDPLEF---LEIineklkl 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 155 ----------------SGGQRQRVVI-AMALaFDPALLIADEPTSALDVttqaqilDLLRKIQQ------DKGMALLFIT 211
Cdd:CHL00131 137 vgmdpsflsrnvnegfSGGEKKRNEIlQMAL-LDSELAILDETDSGLDI-------DALKIIAEginklmTSENSIILIT 208
|
250 260
....*....|....*....|....*...
gi 1331382268 212 HDFAVVEAIA-DRVLVLEKGRVVEQGTA 238
Cdd:CHL00131 209 HYQRLLDYIKpDYVHVMQNGKIIKTGDA 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
284-465 |
3.82e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 59.29 E-value: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 284 CSRSGwwgrrtTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRalrsdvQM 363
Cdd:TIGR01189 8 CSRGE------RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE------NI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 364 IFQDPFASLNPRQTVGQ-IVMTGPLVQGvskadAERRARELLGLVGLpaAAFERFP-HEFSGGQRQRIGIARALAVEPKV 441
Cdd:TIGR01189 76 LYLGHLPGLKPELSALEnLHFWAAIHGG-----AQRTIEDALAAVGL--TGFEDLPaAQLSAGQQRRLALARLWLSRRPL 148
|
170 180
....*....|....*....|....
gi 1331382268 442 LIADECVSALDALIQVQILELLES 465
Cdd:TIGR01189 149 WILDEPTTALDKAGVALLAGLLRA 172
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
26-224 |
4.17e-10 |
|
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: 59.43 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 26 LSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAMRqlrgrdiSMVFQEPMSALNPL 105
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKT----TLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR-------GLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 106 MRVGEQIDETLRAHGvaaarvrRQRVVDLLGYVGLPDPERLRLAYpfeLSGGQRQRVVIAMALAFDPALLIADEPTSALD 185
Cdd:cd03231 88 LSVLENLRFWHADHS-------DEQVEEALARVGLNGFEDRPVAQ---LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1331382268 186 VTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRV 224
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
23-237 |
5.44e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 62.45 E-value: 5.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLadrSEEAMRQLRgRDISMVFQEPM--- 99
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIV----ELERGRILIDGCDI---SKFGLMDLR-KVLGIIPQAPVlfs 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 ----SALNPLmrvGEQIDETL-----RAHGVAAarVRRQRVvdllgyvGLpDPERLRLAYPFelSGGQRQRVVIAMALAF 170
Cdd:PLN03130 1327 gtvrFNLDPF---NEHNDADLwesleRAHLKDV--IRRNSL-------GL-DAEVSEAGENF--SVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 171 DPALLIADEPTSALDVTTQAQILDLLRkiQQDKGMALLFITHDFAVVeaI-ADRVLVLEKGRVVEQGT 237
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIR--EEFKSCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDT 1455
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
154-254 |
6.07e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.47 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAIADRVLVLEKGRVV 233
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
90 100
....*....|....*....|.
gi 1331382268 234 EQgtapavlrVPREDYTRQLL 254
Cdd:PRK11288 476 GE--------LAREQATERQA 488
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
273-497 |
1.25e-09 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.18 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGKVFCSRSgwwgrrtTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglseg 352
Cdd:TIGR01257 1937 ILRLNELTKVYSGTS-------SPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI------ 2003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 353 rLRALrSDVQ--MIFQDPFASLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQRIG 430
Cdd:TIGR01257 2004 -LTNI-SDVHqnMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYA-DRLAGTYSGGNKRKLS 2080
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 431 IARALAVEPKVLIADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKG 497
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-236 |
1.37e-09 |
|
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: 57.33 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLrqlpdplkvesgrlvfrdedladrseEAMRQLRGRDISMVFQEpms 100
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGL--------------------------YASGKARLISFLPKFSR--- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 alNPLMRVGEQidetlrahgvaaarvrrQRVVDL-LGYvglpdperLRLAYPFE-LSGGQRQRVVIA--MALAFDPALLI 176
Cdd:cd03238 60 --NKLIFIDQL-----------------QFLIDVgLGY--------LTLGQKLStLSGGELQRVKLAseLFSEPPGTLFI 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 177 ADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAiADRVLVLEK------GRVVEQG 236
Cdd:cd03238 113 LDEPSTGLHQQDINQLLEVIKGL-IDLGNTVILIEHNLDVLSS-ADWIIDFGPgsgksgGKVVFSG 176
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
305-493 |
1.38e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 58.57 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 305 LREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVA-------GLSEGRLRA-LRSDVQMIFQDPFAS---LN 373
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikADYEGTVRDlLSSITKDFYTHPYFKteiAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQTVGQIvmtgplvqgvskadaERRARELlglvglpaaaferfphefSGGQRQRIGIARALAVEPKVLIADECVSALDa 453
Cdd:cd03237 102 PLQIEQIL---------------DREVPEL------------------SGGELQRVAIAACLSKDADIYLLDEPSAYLD- 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1331382268 454 liqVQILELLESLQRRFRL----SIVFITHDLRVAARLCDRIAV 493
Cdd:cd03237 148 ---VEQRLMASKVIRRFAEnnekTAFVVEHDIIMIDYLADRLIV 188
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
33-236 |
1.97e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 60.28 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 33 GECLCVVGESGSGKSMLAKALlrqlpdplkveSGRL---VFRDEDLADRSEEAMRQLRgrDISMVFQEPMsaLNPLMRVG 109
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNAL-----------AGRIqgnNFTGTILANNRKPTKQILK--RTGFVTQDDI--LYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 110 EQID--ETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYPF--ELSGGQRQRVVIAMALAFDPALLIADEPTSALD 185
Cdd:PLN03211 159 ETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNSFirGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 186 VTTQAQILDLLRKIQQdKGMALLFITHD-FAVVEAIADRVLVLEKGRVVEQG 236
Cdd:PLN03211 239 ATAAYRLVLTLGSLAQ-KGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
290-497 |
2.14e-09 |
|
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: 57.73 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 290 WGRRTTqALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRAL-RSDVQMIFQDP 368
Cdd:cd03290 10 WGSGLA-TLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 369 FAsLNPrqTVGQ-IVMTGPL----VQGVSKADAERRARELLGLvGLPAAAFERFPHeFSGGQRQRIGIARALAVEPKVLI 443
Cdd:cd03290 89 WL-LNA--TVEEnITFGSPFnkqrYKAVTDACSLQPDIDLLPF-GDQTEIGERGIN-LSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 444 ADECVSALDA-----LIQVQILELLESLQRrfrlSIVFITHDLRVAARlCDRIAVMRKG 497
Cdd:cd03290 164 LDDPFSALDIhlsdhLMQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-246 |
3.01e-09 |
|
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: 59.96 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRseeAMRQLRGRdISMVFQEPM--- 99
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRIN----ESAEGEIIIDGLNIAKI---GLHDLRFK-ITIIPQDPVlfs 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 ----SALNPLMRVGEQidETLRAHGVAaarvrrqrvvDLLGYV-GLPDPERLRLAYPFE-LSGGQRQRVVIAMALAFDPA 173
Cdd:TIGR00957 1374 gslrMNLDPFSQYSDE--EVWWALELA----------HLKTFVsALPDKLDHECAEGGEnLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 174 LLIADEPTSALDVTTQAQILDLLRkiQQDKGMALLFITHDfavVEAIAD--RVLVLEKGRVVEQGtAPAVLRVPR 246
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTIR--TQFEDCTVLTIAHR---LNTIMDytRVIVLDKGEVAEFG-APSNLLQQR 1510
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
144-228 |
3.55e-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: 56.04 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 144 ERLRLAYP---FELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAI 220
Cdd:cd03222 59 DGITPVYKpqyIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYL 138
|
....*...
gi 1331382268 221 ADRVLVLE 228
Cdd:cd03222 139 SDRIHVFE 146
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
25-228 |
3.94e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.74 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFRDEDLADRSEEAMRQLrgrdismVFQEPMSALNP 104
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKT----SLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDL-------LYLGHQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVgeqiDETLRAHGVAAARVRRQRVVDLLGYVGLPDPERLRLAYpfeLSGGQRQRVVIAMALAFDPALLIADEPTSAL 184
Cdd:PRK13538 88 ELTA----LENLRFYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQ---LSAGQQRRVALARLWLTRAPLWILDEPFTAI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1331382268 185 DVTTQAQILDLLRKIQQDKGMALLfITHDFAVVEAIADRVLVLE 228
Cdd:PRK13538 161 DKQGVARLEALLAQHAEQGGMVIL-TTHQDLPVASDKVRKLRLG 203
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
273-466 |
4.25e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 273 VLKAEALGkvfCSRsGWwgRRTTQALDavqLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSE- 351
Cdd:PRK13538 1 MLEARNLA---CER-DE--RILFSGLS---FTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 352 --------GRLRALRSDVQmifqdPFASLNPRQTVGQivmtgplvqgvsKADAErRARELLGLVGLpaAAFERFP-HEFS 422
Cdd:PRK13538 72 yhqdllylGHQPGIKTELT-----ALENLRFYQRLHG------------PGDDE-ALWEALAQVGL--AGFEDVPvRQLS 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1331382268 423 GGQRQRIGIARALAVEPKVLIADECVSALDaliqVQILELLESL 466
Cdd:PRK13538 132 AGQQRRVALARLWLTRAPLWILDEPFTAID----KQGVARLEAL 171
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
154-246 |
4.67e-09 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 57.31 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAIADRVLVLEKGRVV 233
Cdd:PRK11300 154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPL 233
|
90
....*....|...
gi 1331382268 234 EQGTAPAVLRVPR 246
Cdd:PRK11300 234 ANGTPEEIRNNPD 246
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-234 |
6.23e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 6.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPLKvesGRLVFRD-EDLADRSEEAMRQlrgrDISMVFQEPM---- 99
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILK-LIERLYDPTE---GDIIINDsHNLKDINLKWWRS----KIGVVSQDPLlfsn 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 ----------SALNPLMRVGEQIDE----------------------------TLRAHGVAAAR-----VRRQRVVDLLG 136
Cdd:PTZ00265 475 siknnikyslYSLKDLEALSNYYNEdgndsqenknkrnscrakcagdlndmsnTTDSNELIEMRknyqtIKDSEVVDVSK 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 137 YV-------GLPDP-ERLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALL 208
Cdd:PTZ00265 555 KVlihdfvsALPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
|
250 260
....*....|....*....|....*....
gi 1331382268 209 FITHDFAVVEaIADRVLVL---EKGRVVE 234
Cdd:PTZ00265 635 IIAHRLSTIR-YANTIFVLsnrERGSTVD 662
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-230 |
6.45e-09 |
|
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: 56.19 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFRDEDLADRSEEAMRQLRGRDISMVFQEPMsAL 102
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEM----QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPW-LL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPlmRVGEQIdetlrAHGVAAARVRRQRVVDLLGYvgLPDPERLrlayPF-----------ELSGGQRQRVVIAMALAFD 171
Cdd:cd03290 92 NA--TVEENI-----TFGSPFNKQRYKAVTDACSL--QPDIDLL----PFgdqteigergiNLSGGQRQRICVARALYQN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 172 PALLIADEPTSALDV-----TTQAQILDLLrkiqQDKGMALLFITHDFAVVEAiADRVLVLEKG 230
Cdd:cd03290 159 TNIVFLDDPFSALDIhlsdhLMQEGILKFL----QDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-244 |
8.06e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.50 E-value: 8.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdpLKVESgRLVFRDEDLADRSEEAMRQ------------------- 85
Cdd:PTZ00265 1186 DLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYD--LKNDH-HIVFKNEHTNDMTNEQDYQgdeeqnvgmknvnefsltk 1262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 86 ------------------LRGRDI------------SMVFQEPMsALNplMRVGEQI-----DETLRAhgvaAARVRRQR 130
Cdd:PTZ00265 1263 eggsgedstvfknsgkilLDGVDIcdynlkdlrnlfSIVSQEPM-LFN--MSIYENIkfgkeDATRED----VKRACKFA 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 131 VVDLLgYVGLPDPERLRLA-YPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDKGMALLF 209
Cdd:PTZ00265 1336 AIDEF-IESLPNKYDTNVGpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1331382268 210 ITHDFAVVEAiADRVLVLEK----GRVVE-QGTAPAVLRV 244
Cdd:PTZ00265 1415 IAHRIASIKR-SDKIVVFNNpdrtGSFVQaHGTHEELLSV 1453
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-231 |
1.04e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.30 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 32 RGECLCVVGESGSGKSMLAKALLRQLPDPlkvESGRLVFRDEDLADRSEEAMRQLrgrdismvfqepmsalnplmrvgeq 111
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPP---GGGVIYIDGEDILEEVLDQLLLI------------------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 112 idetlrahgvaaarvrrqrvvdllgyvglpdperLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQ 191
Cdd:smart00382 53 ----------------------------------IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAL 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 192 ILDLLR-----KIQQDKGMALLFITHDF-----AVVEAIADRVLVLEKGR 231
Cdd:smart00382 99 LLLLEElrlllLLKSEKNLTVILTTNDEkdlgpALLRRRFDRRIVLLLIL 148
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
305-464 |
1.09e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 55.27 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 305 LREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglsegrlralrsdvqmIFQDPFAS---------LNPR 375
Cdd:PRK13539 25 LAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-----------------DDPDVAEAchylghrnaMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 QTVGQIVMTGPLVQGvskaDAERRARELLGLVGLPAAAFERFpHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALI 455
Cdd:PRK13539 88 LTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
....*....
gi 1331382268 456 QVQILELLE 464
Cdd:PRK13539 163 VALFAELIR 171
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
308-504 |
1.10e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.58 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 308 GETLGIVGESGSGKSTLgrclvrlLRADSGRIEWLGREVAGLSEGR--LRALRSDVQMIFQDPFasLNPRQTVGQIVMTG 385
Cdd:PLN03211 94 GEILAVLGPSGSGKSTL-------LNALAGRIQGNNFTGTILANNRkpTKQILKRTGFVTQDDI--LYPHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 386 PLVQ---GVSKADAERRARELLGLVGLPAAAFERFPHEF----SGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQ 458
Cdd:PLN03211 165 SLLRlpkSLTKQEKILVAESVISELGLTKCENTIIGNSFirgiSGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYR 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1331382268 459 ILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGE 504
Cdd:PLN03211 245 LVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGK 290
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
155-236 |
1.40e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 56.67 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 155 SGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVLEKGRVVE 234
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
..
gi 1331382268 235 QG 236
Cdd:NF000106 225 DG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
144-230 |
2.32e-08 |
|
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: 54.17 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 144 ERLRL-AYPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHD-FAVVEAIA 221
Cdd:cd03232 98 EALRFsALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIHQpSASIFEKF 176
|
....*....
gi 1331382268 222 DRVLVLEKG 230
Cdd:cd03232 177 DRLLLLKRG 185
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
421-501 |
2.50e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.96 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 421 FSGGQRQRIGIARALAVEPKVLIADECVSALDA----LIQVQILELLESLQRrfrlSIVFITHdlRVAA-RLCDRIAVM- 494
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSnsekLIEKTIVDIKDKADK----TIITIAH--RIASiKRSDKIVVFn 1432
|
90
....*....|
gi 1331382268 495 ---RKGRVVE 501
Cdd:PTZ00265 1433 npdRTGSFVQ 1442
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
153-243 |
3.79e-08 |
|
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: 56.56 E-value: 3.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 153 ELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQdkGMALLFITHDFAVVEAIADRVLVLEKGRV 232
Cdd:TIGR01257 1061 DLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
90
....*....|.
gi 1331382268 233 VEQGTaPAVLR 243
Cdd:TIGR01257 1139 YCSGT-PLFLK 1148
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
154-230 |
3.90e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 3.90e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLI-ADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHD-FAVVEAIADRVLVLEKG 230
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL-ADHGQAILCTIHQpSAILFEEFDRLLLLQKG 979
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
295-512 |
3.99e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSDvqmIFQDPFAS-LN 373
Cdd:PRK10938 16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSD---EWQRNNTDmLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 374 PRQ-----TVGQIVMTGplvqgvskADAERRARELLGLVGLPAAAFERFPHeFSGGQRQRIGIARALAVEPKVLIADECV 448
Cdd:PRK10938 93 PGEddtgrTTAEIIQDE--------VKDPARCEQLAQQFGITALLDRRFKY-LSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 449 SALDALIQVQILELLESLQRRfRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETAALFADA 512
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQA 226
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
23-258 |
4.68e-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: 56.07 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDPLKVE-SGRLVFrdedladrSEEAMRQLRG--RDiSMVFqep 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELePSEGKIKhSGRISF--------SPQTSWIMPGtiKD-NIIF--- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 99 msalnplmrvGEQIDETLRAHGVAAARVRRQRVVdllgyvgLPDPERLRLAYP-FELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:TIGR01271 510 ----------GLSYDEYRYTSVIKACQLEEDIAL-------FPEKDKTVLGEGgITLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 178 DEPTSALDVTTQAQILD-LLRKIQQDKGMALlfITHDFAVVEAiADRVLVLEKGRVVEQGTApAVLRVPREDYTRQLLAA 256
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFEsCLCKLMSNKTRIL--VTSKLEHLKK-ADKILLLHEGVCYFYGTF-SELQAKRPDFSSLLLGL 648
|
..
gi 1331382268 257 VS 258
Cdd:TIGR01271 649 EA 650
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
23-254 |
5.19e-08 |
|
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: 54.48 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDPLKVE-SGRLVFRDEdladrseeamrqlrgrdismvfqepMS 100
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELePSEGKIKhSGRISFSSQ-------------------------FS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 ALNPlmrvgEQIDETLRAhGVAAARVRRQRVV-------DLLGYvglPDPERLRLAYP-FELSGGQRQRVVIAMALAFDP 172
Cdd:cd03291 108 WIMP-----GTIKENIIF-GVSYDEYRYKSVVkacqleeDITKF---PEKDNTVLGEGgITLSGGQRARISLARAVYKDA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 173 ALLIADEPTSALDVTTQAQILD-LLRKIQQDKGMALlfITHDFAVVEaIADRVLVLEKGRVVEQGTAPAvLRVPREDYTR 251
Cdd:cd03291 179 DLYLLDSPFGYLDVFTEKEIFEsCVCKLMANKTRIL--VTSKMEHLK-KADKILILHEGSSYFYGTFSE-LQSLRPDFSS 254
|
...
gi 1331382268 252 QLL 254
Cdd:cd03291 255 KLM 257
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
297-504 |
5.66e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 55.28 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGrevaglsEGRLRALRSdvqmifqdpfaSLNPRQ 376
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------SAALIAISS-----------GLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 T-VGQIVMTGpLVQGVSKadaeRRARELLGLVgLPAAAFERFPHE----FSGGQRQRIGIARALAVEPKVLIADECVSAL 451
Cdd:PRK13545 101 TgIENIELKG-LMMGLTK----EKIKEIIPEI-IEFADIGKFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALSVG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 452 DALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVMRKGRVVEQGE 504
Cdd:PRK13545 175 DQTFTKKCLDKMNEFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGD 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
292-515 |
6.17e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 6.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIewLGREVAGLSEGRLRALRSDVQMIFQDP--- 368
Cdd:PTZ00265 395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDI--IINDSHNLKDINLKWWRSKIGVVSQDPllf 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 369 --------------------------------FASLNPRQTVgQIVMTGPLVQGVSKADAE-----RRARELLGLVGLPA 411
Cdd:PTZ00265 473 snsiknnikyslyslkdlealsnyynedgndsQENKNKRNSC-RAKCAGDLNDMSNTTDSNeliemRKNYQTIKDSEVVD 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 412 AAFERFPHEF-------------------SGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESLQ-RRFR 471
Cdd:PTZ00265 552 VSKKVLIHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENR 631
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1331382268 472 LSIVfITHDLRvAARLCDRIAVMRKGrvvEQGETAALFADARHP 515
Cdd:PTZ00265 632 ITII-IAHRLS-TIRYANTIFVLSNR---ERGSTVDVDIIGEDP 670
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
306-494 |
6.42e-08 |
|
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: 53.91 E-value: 6.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 306 REGETLGIVGESGSGKSTLGRCLVRLLRADSGRI----EWLG--REVAG--LSEGRLRALRSDVQMIFQDPFASLNPRQT 377
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDEilDEFRGseLQNYFTKLLEGDVKVIVKPQYVDLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 378 VGQivmTGPLVQGVSKADAERRARELLGLVGLpaaaFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQV 457
Cdd:cd03236 104 KGK---VGELLKKKDERGKLDELVDQLELRHV----LDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180 190
....*....|....*....|....*....|....*..
gi 1331382268 458 QILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVM 494
Cdd:cd03236 177 NAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL 212
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
298-504 |
6.66e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.64 E-value: 6.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLV--RLLRADSGRIEWLGREVAGLSEGRlRAlRSDVQMIFQDPF------ 369
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RA-GEGIFMAFQYPVeipgvs 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 ------ASLNP-RQTVGQivmtgplvQGVSKADAERRARELLGLVGLPAAAFERFPHE-FSGGQRQRIGIARALAVEPKV 441
Cdd:PRK09580 95 nqfflqTALNAvRSYRGQ--------EPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVLEPEL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 442 LIADECVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARL-CDRIAVMRKGRVVEQGE 504
Cdd:PRK09580 167 CILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIkPDYVHVLYQGRIVKSGD 229
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
153-227 |
1.07e-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: 53.14 E-value: 1.07e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 153 ELSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVL 227
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-242 |
1.13e-07 |
|
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: 54.95 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplKVEsGRLVFRDEdLADRSEEAMRQLRGRDISMVFQEPmsaL 102
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD---KVE-GHVHMKGS-VAYVPQQAWIQNDSLRENILFGKA---L 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPlmrvgEQIDETLRAHGVAAarvrrqrvvDLlgyVGLPDPERLRLAYP-FELSGGQRQRVVIAMALAFDPALLIADEPT 181
Cdd:TIGR00957 726 NE-----KYYQQVLEACALLP---------DL---EILPSGDRTEIGEKgVNLSGGQKQRVSLARAVYSNADIYLFDDPL 788
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 182 SALDVTTQAQILDllrKIQQDKGM----ALLFITHDFAVVEAIaDRVLVLEKGRVVEQGTAPAVL 242
Cdd:TIGR00957 789 SAVDAHVGKHIFE---HVIGPEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELL 849
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
308-496 |
1.53e-07 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.83 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 308 GETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLgrevaglsegrlralrsdvqmifqdpfaslnprqtvgqivmtgpl 387
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYI--------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 388 vqgvskaDAERRARELlgLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILEL----- 462
Cdd:smart00382 37 -------DGEDILEEV--LDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrl 107
|
170 180 190
....*....|....*....|....*....|....
gi 1331382268 463 LESLQRRFRLSIVFITHDLRVAARLCDRIAVMRK 496
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRR 141
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
298-484 |
1.80e-07 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 51.72 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 298 LDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGRevaGLSEGRLRALRSDVQMIFQDPF-ASLNPRQ 376
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---PLDFQRDSIARGLLYLGHAPGIkTTLSVLE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 TvgqivmtgplVQGVSKADAERRARELLGLVGLpaAAFERFP-HEFSGGQRQRIGIARALAVEPKVLIADECVSALDALI 455
Cdd:cd03231 93 N----------LRFWHADHSDEQVEEALARVGL--NGFEDRPvAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
170 180
....*....|....*....|....*....
gi 1331382268 456 QVQILELLESLQRRFRLSIVFITHDLRVA 484
Cdd:cd03231 161 VARFAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
128-499 |
2.22e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 128 RQRVVDLLGYVGLPDPERLRLAYPFelSGGQRQRVVIAMALAFDPALLIADEPTSALDVttQAQILdlLRKIQQDKGMAL 207
Cdd:PRK10636 126 RSRAASLLHGLGFSNEQLERPVSDF--SGGWRMRLNLAQALICRSDLLLLDEPTNHLDL--DAVIW--LEKWLKSYQGTL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 208 LFITHDFAVVEAIADRVLVLEKGRVVE-------------------------QGTAPAVLRVPREDYTRQLLAAVSAQP- 261
Cdd:PRK10636 200 ILISHDRDFLDPIVDKIIHIEQQSLFEytgnyssfevqratrlaqqqamyesQQERVAHLQSYIDRFRAKATKAKQAQSr 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 262 --LVPRTQVAGPV-------------------VLKAEalgKVfcsrSGWWGRRTTqaLDAVQLQLREGETLGIVGESGSG 320
Cdd:PRK10636 280 ikMLERMELIAPAhvdnpfhfsfrapeslpnpLLKME---KV----SAGYGDRII--LDSIKLNLVPGSRIGLLGRNGAG 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 321 KSTLGRCLVRLLRADSGRIEWL-GREVAGLSEGRLRALRSDVQMIfqDPFASLNPRQTvgqivmtgplvqgvskadaERR 399
Cdd:PRK10636 351 KSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRADESPL--QHLARLAPQEL-------------------EQK 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 400 ARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILELLESlqrrFRLSIVFITH 479
Cdd:PRK10636 410 LRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID----FEGALVVVSH 485
|
410 420
....*....|....*....|
gi 1331382268 480 DLRVAARLCDRIAVMRKGRV 499
Cdd:PRK10636 486 DRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
295-510 |
2.53e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 295 TQALDAVQLQLREGETLGIVGESGSGKSTL-----GrclVRLLRadSGRIEWLGREVAGlsegrlRALRSDVQ-----M- 363
Cdd:NF033858 14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSLlsliaG---ARKIQ--QGRVEVLGGDMAD------ARHRRAVCpriayMp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 364 ------------IFQ--DPFASLnprqtVGQivmtgplvqgvSKADAERRARELLGLVGLpaAAF-ERFPHEFSGGQRQR 428
Cdd:NF033858 83 qglgknlyptlsVFEnlDFFGRL-----FGQ-----------DAAERRRRIDELLRATGL--APFaDRPAGKLSGGMKQK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 429 IGIARALAVEPKVLIADECVSALDALIQVQILELLESL-QRRFRLSIVFITHDLRVAARlCDRIAVMRKGRVVEQGETAA 507
Cdd:NF033858 145 LGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAE 223
|
...
gi 1331382268 508 LFA 510
Cdd:NF033858 224 LLA 226
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
291-503 |
2.60e-07 |
|
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: 51.11 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 291 GRRTTQALDAVQLQLREGETLGIVGESGSGKSTLgrclvrlLRADSGRIEWLGRevaglSEGRLRAlrSDVQMifqDPFA 370
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTL-------LKALANRTEGNVS-----VEGDIHY--NGIPY---KEFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 371 SLNPRQTVGqivmtgplvqgVSKAD---AERRARELLGLVG-LPAAAFERfphEFSGGQRQRIGIARALAVEPKVLIADE 446
Cdd:cd03233 79 EKYPGEIIY-----------VSEEDvhfPTLTVRETLDFALrCKGNEFVR---GISGGERKRVSIAEALVSRASVLCWDN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1331382268 447 CVSALDALIQVQILELLESLQRRFRLSIVF--------ITHdlrvaarLCDRIAVMRKGRVVEQG 503
Cdd:cd03233 145 STRGLDSSTALEILKCIRTMADVLKTTTFVslyqasdeIYD-------LFDKVLVLYEGRQIYYG 202
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
23-237 |
2.78e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.44 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPdplkvesgrlvfrdedladRSEEAMRQLRGR-----DISMVFQE 97
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-------------------HAETSSVVIRGSvayvpQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 PM-------SALNPlMRVGEQIDETLRAHGVaaarvrrqrvvDLLgyvglPDPERLRLA-YPFELSGGQRQRVVIAMALA 169
Cdd:PLN03232 694 TVrenilfgSDFES-ERYWRAIDVTALQHDL-----------DLL-----PGRDLTEIGeRGVNISGGQKQRVSMARAVY 756
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 170 FDPALLIADEPTSALDVTTQAQILDLLRKiQQDKGMALLFITHDFAVVEAIaDRVLVLEKGRVVEQGT 237
Cdd:PLN03232 757 SNSDIYIFDDPLSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGT 822
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-237 |
3.73e-07 |
|
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: 51.46 E-value: 3.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 19 RSHALYDLSLQLNRGECLCVVGESGSGKS-----MLAKALLRQL------PDPLKVESG-----RLVFRDEDLADRSEEA 82
Cdd:cd03271 7 RENNLKNIDVDIPLGVLTCVTGVSGSGKSslindTLYPALARRLhlkkeqPGNHDRIEGlehidKVIVIDQSPIGRTPRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 -----------MRQL-------------------RGRDISMVFQepmsalnplMRVGEqidetlrAHGVAAARVRRQRVV 132
Cdd:cd03271 87 npatytgvfdeIRELfcevckgkrynretlevryKGKSIADVLD---------MTVEE-------ALEFFENIPKIARKL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 133 DLLGYVGLpdpERLRLAYP-FELSGGQRQRVVIAMALAF---DPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALL 208
Cdd:cd03271 151 QTLCDVGL---GYIKLGQPaTTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKGNTVV 226
|
250 260 270
....*....|....*....|....*....|....*
gi 1331382268 209 FITHDFAVVeAIADRVLVL------EKGRVVEQGT 237
Cdd:cd03271 227 VIEHNLDVI-KCADWIIDLgpeggdGGGQVVASGT 260
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
20-237 |
4.58e-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: 53.09 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 20 SHALYDLSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGrlvfrDEDLADRSeeAMRQLRGRDISMVFQEPM 99
Cdd:TIGR01257 1952 SPAVDRLCVGVRPGECFGLLGVNGAGKT----TTFKMLTGDTTVTSG-----DATVAGKS--ILTNISDVHQNMGYCPQF 2020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 100 SALNPLMRVGEQIDETLRAHGVAAARVRR--QRVVDLLGYVGLPDperlRLAYPFelSGGQRQRVVIAMALAFDPALLIA 177
Cdd:TIGR01257 2021 DAIDDLLTGREHLYLYARLRGVPAEEIEKvaNWSIQSLGLSLYAD----RLAGTY--SGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 178 DEPTSALDVTTQAQILDLLRKIQQDkGMALLFITHDFAVVEAIADRVLVLEKGRVVEQGT 237
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGT 2153
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
422-503 |
4.89e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 4.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 422 SGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILE--LLESLQRRFRlsiVFITHDLRVAARLcDRIAVMRKGRV 499
Cdd:PLN03130 742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGKTR---VLVTNQLHFLSQV-DRIILVHEGMI 817
|
....
gi 1331382268 500 VEQG 503
Cdd:PLN03130 818 KEEG 821
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
304-506 |
5.48e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 50.70 E-value: 5.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 304 QLREGETLGIVGESGSGKSTLGRCLVRLLRAdSGRIEWLGREVAGLSEGRLRALRSdvQMIFQDPFASLNPrqtVGQ-IV 382
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHRA--YLSQQQTPPFAMP---VFQyLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 383 MTGPlvQGVSKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARA-LAVEP------KVLIADECVSALDaLI 455
Cdd:PRK03695 92 LHQP--DKTRTEAVASALNEVAEALGL-DDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLLDEPMNSLD-VA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 456 QVQILELLESLQRRFRLSIVFITHDLRVAARLCDRIAVMRKGRVVEQGETA 506
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRD 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
18-234 |
6.79e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 6.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 18 DRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMRQLrgrdISMVFQE 97
Cdd:PRK10522 334 DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAM-LLTGLYQP---QSGEILLDGKPVTAEQPEDYRKL----FSAVFTD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 98 PMSALNPLMRVGEQIDETLrahgVAA--ARVRRQRVVDLLGyvglpdpERLRLaypFELSGGQRQRVVIAMALAFDPALL 175
Cdd:PRK10522 406 FHLFDQLLGPEGKPANPAL----VEKwlERLKMAHKLELED-------GRISN---LKLSKGQKKRLALLLALAEERDIL 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1331382268 176 IADEPTSALDVTTQAQILDLLRKIQQDKGMALLFITHDFAVVEAiADRVLVLEKGRVVE 234
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
290-510 |
7.32e-07 |
|
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: 52.26 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 290 WGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLR--ALRSDVqmIFQD 367
Cdd:TIGR00957 646 WARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQndSLRENI--LFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 368 PfasLNPR--QTVGQIVMTGPLVQGVSKADaerraRELLGLVGLpaaaferfphEFSGGQRQRIGIARALAVEPKVLIAD 445
Cdd:TIGR00957 724 A---LNEKyyQQVLEACALLPDLEILPSGD-----RTEIGEKGV----------NLSGGQKQRVSLARAVYSNADIYLFD 785
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 446 ECVSALDALIQVQILE-------LLESLQRrfrlsiVFITHDLRVAARLcDRIAVMRKGRVVEQGETAALFA 510
Cdd:TIGR00957 786 DPLSAVDAHVGKHIFEhvigpegVLKNKTR------ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
303-501 |
1.13e-06 |
|
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: 51.34 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 303 LQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSEGRLRALRSdvqMIFQDP--FASLnprqtvgq 380
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFS---AVFSDFhlFDRL-------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 381 ivmtgplvQGVSKADAERRARELL------GLVGLPAAAFERFphEFSGGQRQRIGIARALAVEPKVLIADECvsALD-- 452
Cdd:COG4615 422 --------LGLDGEADPARARELLerleldHKVSVEDGRFSTT--DLSQGQRKRLALLVALLEDRPILVFDEW--AADqd 489
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 453 -ALIQVQILELLESLQRRFRlSIVFITHDLRvAARLCDRIAVMRKGRVVE 501
Cdd:COG4615 490 pEFRRVFYTELLPELKARGK-TVIAISHDDR-YFDLADRVLKMDYGKLVE 537
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
422-509 |
1.36e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.52 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 422 SGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILE--LLESLQRRFRlsiVFITHDLRVAArLCDRIAVMRKGRV 499
Cdd:PLN03232 742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDscMKDELKGKTR---VLVTNQLHFLP-LMDRIILVSEGMI 817
|
90
....*....|
gi 1331382268 500 VEQGETAALF 509
Cdd:PLN03232 818 KEEGTFAELS 827
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
23-238 |
2.59e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLPDPLKVESGRLVFRDEDLadrsEEAMRQLRGRDIsmvfqepMSAL 102
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVEGVITYDGITP----EEIKKHYRGDVV-------YNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 N----PLMRVGEQIDETLRAHGVA------AARVRRQRVVDL-LGYVGLPDPERLRLAYPF--ELSGGQRQRVVIAMALA 169
Cdd:TIGR00956 146 TdvhfPHLTVGETLDFAARCKTPQnrpdgvSREEYAKHIADVyMATYGLSHTRNTKVGNDFvrGVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1331382268 170 FDPALLIADEPTSALDVTTQAQILDLLRKIQQdkgmallfITHDFAVVEA---------IADRVLVLEKGRVVEQGTA 238
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSAN--------ILDTTPLVAIyqcsqdayeLFDKVIVLYEGYQIYFGPA 295
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
297-501 |
3.24e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVaglSEGRLRALRSDVQMIFQD--PFASLnp 374
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYRKLFSAVFTDfhLFDQL-- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 375 rqtvgqivmTGPLVQGVSKADAERRArELLGLVGLPAAAFERFPH-EFSGGQRQRIGIARALAVEPKVLIADECVSALDA 453
Cdd:PRK10522 413 ---------LGPEGKPANPALVEKWL-ERLKMAHKLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 454 LI-QVQILELLESLQRRFRlSIVFITHDLRVAARlCDRIAVMRKGRVVE 501
Cdd:PRK10522 483 HFrREFYQVLLPLLQEMGK-TIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
23-245 |
3.39e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLvfrdedLADRSeeamrqlrgrdISMVFQEP--MS 100
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF----EISEGRV------WAERS-----------IAYVPQQAwiMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 AL---NPLMrvgeqIDETLRAHGVAAARVRrQRVVDLLGYVGLPDPERLRLAypFELSGGQRQRVVIAMALAFDPALLIA 177
Cdd:PTZ00243 735 ATvrgNILF-----FDEEDAARLADAVRVS-QLEADLAQLGGGLETEIGEKG--VNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1331382268 178 DEPTSALDV-----TTQAQILDLLRkiqqdkGMALLFITHDFAVVeAIADRVLVLEKGRVVEQGTAPAVLRVP 245
Cdd:PTZ00243 807 DDPLSALDAhvgerVVEECFLGALA------GKTRVLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
303-500 |
4.97e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.12 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 303 LQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWlgrevaglSEGrlralrSDVQMIFQDPFASLNPRQTVgqiv 382
Cdd:PRK15064 340 LLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW--------SEN------ANIGYYAQDHAYDFENDLTL---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 383 mTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALDaliqvqiLEL 462
Cdd:PRK15064 402 -FDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD-------MES 473
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1331382268 463 LESLQ---RRFRLSIVFITHDLRVAARLCDRIAVMRKGRVV 500
Cdd:PRK15064 474 IESLNmalEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-225 |
6.13e-06 |
|
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: 46.58 E-value: 6.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSMLAKALLrqlpdplkvesgrLVFrdedladrseeAMRQLRGRDISmvfqepms 100
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIG-------------LAL-----------GGAQSATRRRS-------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 101 alnplmrvgeqidETLRAHGVAAARVRRQRVVDllgyvglpdperlrlaypfELSGGQRQRVVIAMALA---FDPA-LLI 176
Cdd:cd03227 57 -------------GVKAGCIVAAVSAELIFTRL-------------------QLSGGEKELSALALILAlasLKPRpLYI 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 177 ADEPTSALDVTTQAQILDLLRKiQQDKGMALLFITHDFAVVEaIADRVL 225
Cdd:cd03227 105 LDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAE-LADKLI 151
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
26-245 |
7.25e-06 |
|
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: 48.64 E-value: 7.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 26 LSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLADRSEEAMRQLrgrdISMVFQepmsalnpl 105
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAK-LLTGLYRP---ESGEILLDGQPVTADNREAYRQL----FSAVFS--------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 106 mrvgeqiDETLRAHgvaaarvrrqrvvdLLGYVGLPDPERLR--LAY-------PFE--------LSGGQRQRVVIAMAL 168
Cdd:COG4615 414 -------DFHLFDR--------------LLGLDGEADPARARelLERleldhkvSVEdgrfsttdLSQGQRKRLALLVAL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 169 AFDPALLIADEptSALDvttQ---------AQILDLLRKiqqdKGMALLFITHD---FAVveaiADRVLVLEKGRVVEqG 236
Cdd:COG4615 473 LEDRPILVFDE--WAAD---QdpefrrvfyTELLPELKA----RGKTVIAISHDdryFDL----ADRVLKMDYGKLVE-L 538
|
....*....
gi 1331382268 237 TAPAVLRVP 245
Cdd:COG4615 539 TGPAALAAS 547
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
16-236 |
1.16e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 46.48 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 16 GAdRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALL-----RQLpdplkVESGRLVFRdEDLADRSEEAMRQLRGRD 90
Cdd:cd03270 5 GA-REHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIyaegqRRY-----VESLSAYAR-QFLGQMDKPDVDSIEGLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 91 ISMVFQEPMSALNPLMRVGE--QIDETLRahgVAAARVRRQRVVDLLGYVGLpdpERLRLAYPFE-LSGGQRQRVVIAMA 167
Cdd:cd03270 78 PAIAIDQKTTSRNPRSTVGTvtEIYDYLR---LLFARVGIRERLGFLVDVGL---GYLTLSRSAPtLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 168 L--AFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAiADRVLVL------EKGRVVEQG 236
Cdd:cd03270 152 IgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA-ADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
305-494 |
1.39e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 305 LREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIE----W-----------LGREVAGLSEGRLRALRSdVQMIfqdpf 369
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepsWdevlkrfrgteLQNYFKKLYNGEIKVVHK-PQYV----- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 aSLNPRQ---TVGQIVMtgplvqgvsKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADE 446
Cdd:PRK13409 170 -DLIPKVfkgKVRELLK---------KVDERGKLDEVVERLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1331382268 447 CVSALDALIQVQILELLESLQRrfRLSIVFITHDLRVAARLCDRIAVM 494
Cdd:PRK13409 239 PTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
21-227 |
1.43e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 21 HALYDLSLQLNRGECLCVVGESGSGKSML--------AKALLRQLPDP-LKVESG---RLVFRDEDLADRSEEA------ 82
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSSLindtlvpaVEEFIEQGFCSnLSIQWGaisRLVHITRDLPGRSQRSipltyi 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 -----MRQL-----RGRDISMV-----FQEPMSALNPLMRVGEQI---DETL----RAHG------VAAARVRRQRVVDL 134
Cdd:PRK00635 689 kafddLRELfaeqpRSKRLGLTkshfsFNTPLGACAECQGLGSITttdNRTSipcpSCLGkrflpqVLEVRYKGKNIADI 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 135 LGYVG-------LPDPE---------RLRLAY-----P-FELSGGQRQRVVIAMALAF---DPALLIADEPTSAL---DV 186
Cdd:PRK00635 769 LEMTAyeaekffLDEPSihekihalcSLGLDYlplgrPlSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLhthDI 848
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1331382268 187 ttQAQILDLLRKIQQdkGMALLFITHDFAVVEaIADRVLVL 227
Cdd:PRK00635 849 --KALIYVLQSLTHQ--GHTVVIIEHNMHVVK-VADYVLEL 884
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
269-452 |
1.68e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 46.00 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 269 AGPVVLKAEALGkvfcsrsgwWGRRTTQALDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAG 348
Cdd:PRK13543 7 TAPPLLAAHALA---------FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 349 LSEGRLRALRSDVQMIFQDPFASLNPRqtvgqivmtgpLVQGVSKADAERRARELLGLVGLPAAAfERFPHEFSGGQRQR 428
Cdd:PRK13543 78 GDRSRFMAYLGHLPGLKADLSTLENLH-----------FLCGLHGRRAKQMPGSALAIVGLAGYE-DTLVRQLSAGQKKR 145
|
170 180
....*....|....*....|....
gi 1331382268 429 IGIARALAVEPKVLIADECVSALD 452
Cdd:PRK13543 146 LALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-218 |
2.00e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLvfrdeDLADRSEEAMrqlrgrdismvFQEPMSALNP 104
Cdd:PRK11147 337 DFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQL----QADSGRI-----HCGTKLEVAY-----------FDQHRAELDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 105 LMRVGEQIDE---TLRAHGvaaarvrRQRVVdlLGYvgLPD----PERLRLayPFE-LSGGQRQRVVIAmALAFDPA-LL 175
Cdd:PRK11147 397 EKTVMDNLAEgkqEVMVNG-------RPRHV--LGY--LQDflfhPKRAMT--PVKaLSGGERNRLLLA-RLFLKPSnLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1331382268 176 IADEPTSALDVTTqaqiLDLLRKIQQDKGMALLFITHDFAVVE 218
Cdd:PRK11147 463 ILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHDRQFVD 501
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-346 |
2.33e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.52 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 138 VGLP--DPERlRLAypfELSGGQRQRVVIAMALAFDPA--LLIADEPTSALDVTTQAQILDLLRKIQqDKGMALLFITHD 213
Cdd:PRK00635 463 LGLPylTPER-ALA---TLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLR-DQGNTVLLVEHD 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 214 FAVVeAIADRVLVLEK------GRVVEQGTapavlrvPREdytrqLLA---AVSAQPLVPRTQVAGPVVlKAEALGKVFC 284
Cdd:PRK00635 538 EQMI-SLADRIIDIGPgagifgGEVLFNGS-------PRE-----FLAksdSLTAKYLRQELTIPIPEK-RTNSLGTLTL 603
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 285 SRSgwwgrrTTQALDAVQLQLREGETLGIVGESGSGKS-----TLGRCLVRLLRADSG---RIEW--LGREV 346
Cdd:PRK00635 604 SKA------TKHNLKDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFIEQGFCsnlSIQWgaISRLV 669
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
38-492 |
2.38e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 38 VVGESGSGKSMLAKAL---------------------LRQLP--DPLK-----VESGrlVFRDEDLADRSEEamrqlrgr 89
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMagvdkefegearpapgikvgyLPQEPqlDPEKtvrenVEEG--VAEVKAALDRFNE-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 90 dISMVFQEPMSALNPLM----RVGEQIDeTLRAHGVAAarvRRQRVVDLLGyvgLPDPErlrlAYPFELSGGQRQRVVIA 165
Cdd:PRK11819 108 -IYAAYAEPDADFDALAaeqgELQEIID-AADAWDLDS---QLEIAMDALR---CPPWD----AKVTKLSGGERRRVALC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 166 MALAFDPALLIADEPTSALDVTTqaqILDLLRKIQQDKGmALLFITHDFAVVEAIADRVLVLEKGRVV----------EQ 235
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHDYPG-TVVAVTHDRYFLDNVAGWILELDRGRGIpwegnysswlEQ 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 236 GTApavlRVP---REDYTRQL-----------------------------LAAVSAQPLVPRTQV---AGP----VVLKA 276
Cdd:PRK11819 252 KAK----RLAqeeKQEAARQKalkrelewvrqspkarqakskarlaryeeLLSEEYQKRNETNEIfipPGPrlgdKVIEA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 277 EALGKVFcsrsgwwGRRTTqaLDAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEwLGrevaglsegrlra 356
Cdd:PRK11819 328 ENLSKSF-------GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IG------------- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 357 lrSDVQMIFQDPF-ASLNPRQTVGQIVMTGPLVQGVSKADAERRARellglvglpAAAF-------ERFPHEFSGGQRQR 428
Cdd:PRK11819 385 --ETVKLAYVDQSrDALDPNKTVWEEISGGLDIIKVGNREIPSRAY---------VGRFnfkggdqQKKVGVLSGGERNR 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 429 IGIARALAVEPKVLIADECVSALDaliqVQILELLESLQRRFRLSIVFITHD---LrvaarlcDRIA 492
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPTNDLD----VETLRALEEALLEFPGCAVVISHDrwfL-------DRIA 509
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
154-237 |
2.76e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.04 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILD-LLRKIQQDKGMALL-----FITHdfavveaiADRVLVL 227
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkCIKDELRGKTRVLVtnqlhFLSQ--------VDRIILV 812
|
90
....*....|
gi 1331382268 228 EKGRVVEQGT 237
Cdd:PLN03130 813 HEGMIKEEGT 822
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
304-479 |
2.95e-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: 46.67 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 304 QLREGETLGIVGESGSGKSTLGRCLV--------RLLRADSGRIEWLGREvAGLSEGRLRAlrsdvQMIFQDpfaslnpr 375
Cdd:TIGR00954 474 EVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQR-PYMTLGTLRD-----QIIYPD-------- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 376 qTVGQIVMtgplvQGVSKADAErrarELLGLVGLPA--------AAFERFPHEFSGGQRQRIGIARALAVEPKVLIADEC 447
Cdd:TIGR00954 540 -SSEDMKR-----RGLSDKDLE----QILDNVQLTHilereggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDEC 609
|
170 180 190
....*....|....*....|....*....|..
gi 1331382268 448 VSAldalIQVQILELLESLQRRFRLSIVFITH 479
Cdd:TIGR00954 610 TSA----VSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
292-480 |
3.52e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.70 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 292 RRTTQAL-DAVQLQLREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIE--------WLGREVAGLSEGRL-------- 354
Cdd:PRK10636 10 RRGVRVLlDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlaWVNQETPALPQPALeyvidgdr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 355 --RALRSDVQmifqdpfaSLNPRQTVGQIVMTGPLVQGVSKADAERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIA 432
Cdd:PRK10636 90 eyRQLEAQLH--------DANERNDGHAIATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 433 RALAVEPKVLIADECVSA--LDALIqvqileLLESLQRRFRLSIVFITHD 480
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHldLDAVI------WLEKWLKSYQGTLILISHD 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
422-507 |
3.86e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 3.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 422 SGGQRQRIGIARALAVEPKVLIADECVSALDALIQVQILE--LLESLQRRFRlsiVFITHDLRVAARlCDRIAVMRKGRV 499
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEecFLGALAGKTR---VLATHQVHVVPR-ADYVVALGDGRV 859
|
....*...
gi 1331382268 500 VEQGETAA 507
Cdd:PTZ00243 860 EFSGSSAD 867
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
154-324 |
4.46e-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: 46.16 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMAL--AFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGMALLFITHDFAVVEAiADRVLVL---- 227
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTIRA-ADYVIDIgpga 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 228 --EKGRVVEQGTAPAVLRVPRedytrqllaAVSAQPLVPRTQVAGPVVlKAEALGKVFCSRsgwwGRRTTQaLDAVQLQL 305
Cdd:TIGR00630 567 geHGGEVVASGTPEEILANPD---------SLTGQYLSGRKKIEVPAE-RRPGNGKFLTLK----GARENN-LKNITVSI 631
|
170
....*....|....*....
gi 1331382268 306 REGETLGIVGESGSGKSTL 324
Cdd:TIGR00630 632 PLGLFTCITGVSGSGKSTL 650
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-228 |
6.68e-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: 45.70 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQ-LPDPLKVESGRLVfrdeDLA--DRSEEAMRqlrgrDISMVFQEpMSA 101
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQeQPDSGTIEIGETV----KLAyvDQSRDALD-----PNKTVWEE-ISG 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 102 LNPLMRVGeqidetlrahgvaaarvrrQRVVDLLGYVGlpdperlrlAYPF----------ELSGGQRQRVVIAMALAFD 171
Cdd:TIGR03719 410 GLDIIKLG-------------------KREIPSRAYVG---------RFNFkgsdqqkkvgQLSGGERNRVHLAKTLKSG 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1331382268 172 PALLIADEPTSALDVTTqaqildlLRKIQQdkgmALL-------FITHDFAVVEAIADRVLVLE 228
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVET-------LRALEE----ALLnfagcavVISHDRWFLDRIATHILAFE 514
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
305-494 |
7.78e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.55 E-value: 7.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 305 LREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIE----W-----------LGREVAGLSEGRLRALRSdVQMIfqdpf 369
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepsWdevlkrfrgteLQDYFKKLANGEIKVAHK-PQYV----- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 370 aSLNPRQ---TVGQIVMtgplvqgvsKADAERRARELLGLVGLpAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADE 446
Cdd:COG1245 170 -DLIPKVfkgTVRELLE---------KVDERGKLDELAEKLGL-ENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1331382268 447 CVSALDALIQVQILELLESLQRRFRlSIVFITHDLRVAARLCDRIAVM 494
Cdd:COG1245 239 PSSYLDIYQRLNVARLIRELAEEGK-YVLVVEHDLAILDYLADYVHIL 285
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
130-241 |
1.11e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 130 RVVDLLGYVGLpdpERLRLAYP-FELSGGQRQRVVIAMAL---AFDPALLIADEPTSALDVTTQAQILDLLRKIqQDKGM 205
Cdd:TIGR00630 808 RKLQTLCDVGL---GYIRLGQPaTTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGN 883
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1331382268 206 ALLFITHDFAVVEAiADRVLVL------EKGRVVEQGTAPAV 241
Cdd:TIGR00630 884 TVVVIEHNLDVIKT-ADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
396-452 |
1.30e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 396 AERRARELLGLVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPKVLIADECVSALD 452
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
154-229 |
1.34e-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: 42.98 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQ------RVVIAMALAFDPALLIADEPTSALDV-TTQAQILDLLRKIQQDKGMALLFITHDFAVVEAiADRVLV 226
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDA-ADHIYR 194
|
...
gi 1331382268 227 LEK 229
Cdd:cd03240 195 VEK 197
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
30-242 |
1.49e-04 |
|
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: 43.74 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 30 LNRGECLCVVGESGSGKSMLAKALLRQLpdplKVESGRLVFrdeDLADRSEEAMRQLRGRdISMVFQEPM-------SAL 102
Cdd:cd03288 44 IKPGQKVGICGRTGSGKSSLSLAFFRMV----DIFDGKIVI---DGIDISKLPLHTLRSR-LSIILQDPIlfsgsirFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPLMRVGEqiDETLRAHGVAAARVRRQRVVDLLGYVGLPDPErlrlaypfELSGGQRQRVVIAMALAFDPALLIADEPTS 182
Cdd:cd03288 116 DPECKCTD--DRLWEALEIAQLKNMVKSLPGGLDAVVTEGGE--------NFSVGQRQLFCLARAFVRKSSILIMDEATA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 183 ALDVTTQAQILDLLRKIQQDKgmALLFITHDFAVVEAiADRVLVLEKGRVVEQGTAPAVL 242
Cdd:cd03288 186 SIDMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
305-503 |
1.87e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 305 LREGETLGIVGESGSGKSTLGRCL----VRLLRADSGRIEWLGrevAGLSEGRlRALRSDVQMIFQDP--FASLnprqTV 378
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDG---ITPEEIK-KHYRGDVVYNAETDvhFPHL----TV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 379 GQ-----IVMTGP--LVQGVSKAD-AERRARELLGLVGLPAAAFERFPHEF----SGGQRQRIGIARALAVEPKVLIADE 446
Cdd:TIGR00956 156 GEtldfaARCKTPqnRPDGVSREEyAKHIADVYMATYGLSHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAKIQCWDN 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 447 CVSALDALIQVQILELLESlQRRFRLSIVFIT-----HDlrvAARLCDRIAVMRKGRVVEQG 503
Cdd:TIGR00956 236 ATRGLDSATALEFIRALKT-SANILDTTPLVAiyqcsQD---AYELFDKVIVLYEGYQIYFG 293
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
154-237 |
8.51e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.14 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRQRVVIAMALAFDPALLIADEPTSALDVTTQAQILDLLRKiQQDKGMALLFITH--DFAVVEAIADRVLVLEKGR 231
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN-TVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQ 1098
|
....*.
gi 1331382268 232 VVEQGT 237
Cdd:PLN03140 1099 VIYSGP 1104
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
500-521 |
8.94e-04 |
|
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: 37.77 E-value: 8.94e-04
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
25-237 |
9.40e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 9.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 25 DLSLQLNRGECLCVVGESGSGKSMLAKALLRQL-PDPLKV---ESGRLVFRDEDLADRSE------EAMRQLR--GRDIS 92
Cdd:PRK15064 337 NLNLLLEAGERLAIIGENGVGKTTLLRTLVGELePDSGTVkwsENANIGYYAQDHAYDFEndltlfDWMSQWRqeGDDEQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 93 MVfqepMSALNPLMRVGEQIDEtlrahgvaAARVrrqrvvdllgyvglpdperlrlaypfeLSGGQRQRVVIAMALAFDP 172
Cdd:PRK15064 417 AV----RGTLGRLLFSQDDIKK--------SVKV---------------------------LSGGEKGRMLFGKLMMQKP 457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1331382268 173 ALLIADEPTSALDVTTqaqILDLLRKIQQDKGmALLFITHDFAVVEAIADRVLVLEKGRVVE-QGT 237
Cdd:PRK15064 458 NVLVMDEPTNHMDMES---IESLNMALEKYEG-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGT 519
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
23-212 |
1.18e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 40.32 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 23 LYDLSLQLNRGECLCVVGESGSGKSMLAKaLLRQLPDPlkvESGRLVFRDEDLaDRSEEAMRQlrgrdiSMVFQEPMSAL 102
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLK-LIAGLLNP---EKGEILFERQSI-KKDLCTYQK------QLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 103 NPLMRVGEQIDETLRAHGVAAARVRRQRVVDLLGYVGLPDPErlrlaypfeLSGGQRQRVVIAMALAFDPALLIADEPTS 182
Cdd:PRK13540 86 NPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL---------LSSGQKRQVALLRLWMSKAKLWLLDEPLV 156
|
170 180 190
....*....|....*....|....*....|..
gi 1331382268 183 ALDvttQAQILDLLRKIQ--QDKGMALLFITH 212
Cdd:PRK13540 157 ALD---ELSLLTIITKIQehRAKGGAVLLTSH 185
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
154-228 |
1.27e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 154 LSGGQRqrvvIAMALAFDPA----------LLIADEPTSALDVTTQAQILDL----LRKIQQdkgmaLLFITHDFAVVEA 219
Cdd:PRK03918 789 LSGGER----IALGLAFRLAlslylagnipLLILDEPTPFLDEERRRKLVDImeryLRKIPQ-----VIIVSHDEELKDA 859
|
....*....
gi 1331382268 220 iADRVLVLE 228
Cdd:PRK03918 860 -ADYVIRVS 867
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
297-503 |
1.30e-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: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 297 ALDAVQLQLREGETLGIVGESGSGKSTLgrCLvrllradsgriewlgrevAGLSEGRLRALRSDVQMIFQDPfaslnprq 376
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKSTL--VN------------------EGLYASGKARLISFLPKFSRNK-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 377 tvgqIVMTGPLvQGVSKadaerrarellglVGLPAAAFERFPHEFSGGQRQRIGIARALAVEPK--VLIADECVSALDal 454
Cdd:cd03238 62 ----LIFIDQL-QFLID-------------VGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH-- 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1331382268 455 iQVQILELLESLQRRFRL--SIVFITHDLRVaARLCDRIAVMRK------GRVVEQG 503
Cdd:cd03238 122 -QQDINQLLEVIKGLIDLgnTVILIEHNLDV-LSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
299-481 |
1.57e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.99 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 299 DAVQLQLREGETLgIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVAGLSE-------------GRLRALRSDVQMIF 365
Cdd:COG0419 15 DTETIDFDDGLNL-IVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSeeasvelefehggKRYRIERRQGEFAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 366 qdpFASLNP---RQTVGQIVMTGPLVQGVS-----KADAERRARELLGLVGLPAAAFERF-----PHEFSGGQRQRIGIA 432
Cdd:COG0419 94 ---FLEAKPserKEALKRLLGLEIYEELKErlkelEEALESALEELAELQKLKQEILAQLsgldpIETLSGGERLRLALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1331382268 433 RALAvepkvLIADecVSALDALIQVQILELLESLQrrfrlsivFITHDL 481
Cdd:COG0419 171 DLLS-----LILD--FGSLDEERLERLLDALEELA--------IITHVI 204
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
305-376 |
1.69e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 305 LREGETLGIVGESGSGKSTLGRCLVRLLRADSGRIEWLGREVA------GLSEGRLRA-------LRSDVQMIFQDPFAS 371
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVykpqyiDLSGGELQRvaiaaalLRNATFYLFDEPSAY 101
|
....*
gi 1331382268 372 LNPRQ 376
Cdd:cd03222 102 LDIEQ 106
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
153-212 |
1.84e-03 |
|
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: 40.89 E-value: 1.84e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1331382268 153 ELSGGQRQRvvIAMALAF--DPALLIADEPTSALDVTTQAQILDLLRkiqqDKGMALLFITH 212
Cdd:TIGR00954 582 VLSGGEKQR--IAMARLFyhKPQFAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-232 |
2.21e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 36 LCVVGESGSGKSmlakALLRQLPDPLKVESGRlVFRDED--LADRSEEamrQLRGRDISMvfqepmsalNPL---MR--- 107
Cdd:PLN03073 538 IAMVGPNGIGKS----TILKLISGELQPSSGT-VFRSAKvrMAVFSQH---HVDGLDLSS---------NPLlymMRcfp 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 108 -VGEQideTLRAHgvaaarvrrqrvvdlLGYVGLPDpeRLRLAYPFELSGGQRQRVVIAMALAFDPALLIADEPTSALDv 186
Cdd:PLN03073 601 gVPEQ---KLRAH---------------LGSFGVTG--NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD- 659
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1331382268 187 ttqaqiLDLLRKIQQdkGMAL-----LFITHDFAVVEAIADRVLVLEKGRV 232
Cdd:PLN03073 660 ------LDAVEALIQ--GLVLfqggvLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
15-63 |
2.56e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 39.77 E-value: 2.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1331382268 15 AGADRSHALYDLSLQLNRGECLCVV-GESGSGKSMLAKALLRQLPDPLKV 63
Cdd:COG3267 24 LSPSHREALARLEYALAQGGGFVVLtGEVGTGKTTLLRRLLERLPDDVKV 73
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
409-497 |
4.66e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 38.79 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 409 LPAAAFERF---PHE-FSGGQRQRIGIARALAVEPKV----------LIADECVSALDALIQVQILELLESLQRRFRLsI 474
Cdd:cd03279 108 LPQGEFDRFlarPVStLSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFGTLDPEALEAVATALELIRTENRM-V 186
|
90 100
....*....|....*....|...
gi 1331382268 475 VFITHDLRVAARLCDRIAVMRKG 497
Cdd:cd03279 187 GVISHVEELKERIPQRLEVIKTP 209
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
26-185 |
4.88e-03 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 38.68 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 26 LSLQLNRGECLCVVGESGSGKSmlakALLRQLPDPLKVESGRLVFrDEDLADRSEeamrqlRGRDISMVFQEPmsALNPL 105
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKT----TLLRVLAGLLHVESGQIQI-DGKTATRGD------RSRFMAYLGHLP--GLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 106 MRVGEQIDETLRAHGvaaaRVRRQRVVDLLGYVGLPDPERLRLAypfELSGGQRQRVVIAMaLAFDPA-LLIADEPTSAL 184
Cdd:PRK13543 97 LSTLENLHFLCGLHG----RRAKQMPGSALAIVGLAGYEDTLVR---QLSAGQKKRLALAR-LWLSPApLWLLDEPYANL 168
|
.
gi 1331382268 185 D 185
Cdd:PRK13543 169 D 169
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-232 |
5.56e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 5.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 3 LLSVEHLRialpAGADRSHALYDLSLQLNRGECLCVVGESGSGKSMLAKALLRQLpDPLKVESGrlVFRDEDLADRSEEA 82
Cdd:PRK10636 312 LLKMEKVS----AGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGEL-APVSGEIG--LAKGIKLGYFAQHQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 83 MRQLRGRDismvfqepmSALNPLMRVGEQIDEtlrahgvaaarvrrQRVVDLLGYVGLPDPERLRLAYPFelSGGQRQRV 162
Cdd:PRK10636 385 LEFLRADE---------SPLQHLARLAPQELE--------------QKLRDYLGGFGFQGDKVTEETRRF--SGGEKARL 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1331382268 163 VIAMALAFDPALLIADEPTSALDVTTQAQILDLLrkiqQDKGMALLFITHDFAVVEAIADRVLVLEKGRV 232
Cdd:PRK10636 440 VLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL----IDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| AAA_22 |
pfam13401 |
AAA domain; |
35-58 |
6.69e-03 |
|
AAA domain;
Pssm-ID: 379165 [Multi-domain] Cd Length: 129 Bit Score: 36.94 E-value: 6.69e-03
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
153-197 |
8.75e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 38.05 E-value: 8.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1331382268 153 ELSGGQRQRVVIAMALA---FDPA-LLIADEPTSALDVTTQAQILDLLR 197
Cdd:cd03273 166 ELSGGQRSLVALSLILAlllFKPApMYILDEVDAALDLSHTQNIGRMIK 214
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
155-186 |
9.84e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 38.69 E-value: 9.84e-03
10 20 30
....*....|....*....|....*....|..
gi 1331382268 155 SGGQRQRVVIAMALAFDPALLIADEPTSALDV 186
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| |
