|
Name |
Accession |
Description |
Interval |
E-value |
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-538 |
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: 723.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSVSVCGAGN--RVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGILEVSGgSARVLGEDIVT 89
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGtvEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHPSG-SILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 90 ASARRRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVERIYDAYPHQLSGG 169
Cdd:COG4172 81 LSERELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAYPHQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 170 QRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGT 249
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 250 RDEILARPSQNYTRRLVSSVPSLVPtQREAPGGEPVLRITGLGRTYAERRSLFGAT-RTVVAASEVDLTLRRGEILGIVG 328
Cdd:COG4172 241 TAELFAAPQHPYTRKLLAAEPRGDP-RPVPPDAPPLLEARDLKVWFPIKRGLFRRTvGHVKAVDGVSLTLRRGETLGLVG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 329 ESGSGKSTVARCIVRLIePSAGRMLLGETDIARLSGAGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGL--LNFGMPR 406
Cdd:COG4172 320 ESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLrvHGPGLSA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 407 AQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVS 486
Cdd:COG4172 399 AERRARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLA 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 489912973 487 VLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDAAP 538
Cdd:COG4172 479 YLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAP 530
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-543 |
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: 652.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 14 AAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGIleVSGGSARVLGEDIVTASAR 93
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGG--RISGEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 RRRELratrMAMVFQEPMTALNPVhRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQR 173
Cdd:COG1123 80 LRGRR----IGMVFQDPMTQLNPV-TVGDQIAEALEN-LGLSRAEARARVLELLEAVGL---ERRLDRYPHQLSGGQRQR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 174 IVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEI 253
Cdd:COG1123 151 VAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 254 LARPsqnytrRLVSSVPSLVPTQ----REAPGGEPVLRITGLGRTYAERRslfgaTRTVVAASEVDLTLRRGEILGIVGE 329
Cdd:COG1123 231 LAAP------QALAAVPRLGAARgraaPAAAAAEPLLEVRNLSKRYPVRG-----KGGVRAVDDVSLTLRRGETLGLVGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 330 SGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGLLNFG-MPRAQ 408
Cdd:COG1123 300 SGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGlLSRAE 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 409 ALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVL 488
Cdd:COG1123 380 RRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYL 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 489 FITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDAAPGRGWD 543
Cdd:COG1123 460 FISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-537 |
1.04e-159 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 465.72 E-value: 1.04e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 13 SAAVLAIRNLSVSVCGAG--NRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGILEVSGGSARVLGEDIVTA 90
Cdd:PRK15134 2 TQPLLAIENLSVAFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGESLLHA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 SARRRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVERIYDAYPHQLSGGQ 170
Cdd:PRK15134 82 SEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 171 RQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTR 250
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 251 DEILARPSQNYTRRLVSSVPS--LVPTQREAPggePVLRITGLGRTYAERRSLFgaTRTV---VAASEVDLTLRRGEILG 325
Cdd:PRK15134 242 ATLFSAPTHPYTQKLLNSEPSgdPVPLPEPAS---PLLDVEQLQVAFPIRKGIL--KRTVdhnVVVKNISFTLRPGETLG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 326 IVGESGSGKSTVARCIVRLIePSAGRMLLGETDIARLSGAGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGlLNFGMP 405
Cdd:PRK15134 317 LVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSSLNPRLNVLQIIEEG-LRVHQP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 406 RAQALVRAARTLGV---VGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRER 482
Cdd:PRK15134 395 TLSAAQREQQVIAVmeeVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 483 TGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDAA 537
Cdd:PRK15134 475 HQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-538 |
1.70e-149 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 443.14 E-value: 1.70e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 1 MPYAPYPPAGDtsaaVLAIRNLSVSVCGAGNRV--VRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGILEVSGG 78
Cdd:PRK10261 1 MPHSDELDARD----VLAVENLNIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 79 -------SARVLgeDIVTASARRRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVH 151
Cdd:PRK10261 77 kmllrrrSRQVI--ELSEQSAAQMRHVRGADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 152 LPDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAE 231
Cdd:PRK10261 155 IPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 232 IADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVSSVPSL------------------VPTQREAPG-------GEPVL 286
Cdd:PRK10261 235 IADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAVPQLgamkgldyprrfplisleHPAKQEPPIeqdtvvdGEPIL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 287 RITGLGRTYAERRSLFG-ATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGA 365
Cdd:PRK10261 315 QVRNLVTRFPLRSGLLNrVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGLLNFGM-PRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCI 444
Cdd:PRK10261 395 KLQALRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICI 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 445 ARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTR 524
Cdd:PRK10261 475 ARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN 554
|
570
....*....|....
gi 489912973 525 PGHAYTRALIDAAP 538
Cdd:PRK10261 555 PQHPYTRKLMAAVP 568
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
16-284 |
2.05e-123 |
|
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: 365.14 E-value: 2.05e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVS-VCGAGN-RVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGIleVSGGSARVLGEDIVTASAR 93
Cdd:COG0444 1 LLEVRNLKVYfPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPG--ITSGEILFDGEDLLKLSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 RRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVERIYDAYPHQLSGGQRQR 173
Cdd:COG0444 79 ELRKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 174 IVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEI 253
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
250 260 270
....*....|....*....|....*....|...
gi 489912973 254 LARPSQNYTRRLVSSVPSLVPTQREAPG--GEP 284
Cdd:COG0444 239 FENPRHPYTRALLSSIPRLDPDGRRLIPipGEP 271
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
279-538 |
5.94e-120 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 356.73 E-value: 5.94e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 279 APGGEPVLRITGLGRTYAERRSLFGATRTVVAA-SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGET 357
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFPVRGGLFGRTVGVVKAvDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 358 DIARLSGAGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGLLNFGM-PRAQALVRAARTLGVVGLGPDVMRRYPHQFSG 436
Cdd:COG4608 81 DITGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLRPEHADRYPHEFSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 437 GQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIA 240
|
250 260
....*....|....*....|..
gi 489912973 517 AAQTVLTRPGHAYTRALIDAAP 538
Cdd:COG4608 241 PRDELYARPLHPYTQALLSAVP 262
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
285-551 |
1.00e-112 |
|
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: 337.80 E-value: 1.00e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLRITGLGRTYAERRslfgatRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEP---SAGRMLLGETDIAR 361
Cdd:COG0444 1 LLEVRNLKVYFPTRR------GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 362 LSGAGLRPLR-RKVQIVFQDPYRSLNPRRAVGESIIEGL-LNFGMPRAQALVRAARTLGVVGLGP--DVMRRYPHQFSGG 437
Cdd:COG0444 75 LSEKELRKIRgREIQMIFQDPMTSLNPVMTVGDQIAEPLrIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 438 QRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGA 517
Cdd:COG0444 155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGP 234
|
250 260 270
....*....|....*....|....*....|....
gi 489912973 518 AQTVLTRPGHAYTRALIDAAPGRGWDFRNFRPLP 551
Cdd:COG0444 235 VEELFENPRHPYTRALLSSIPRLDPDGRRLIPIP 268
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
285-516 |
5.35e-101 |
|
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: 304.43 E-value: 5.35e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLRITGLGRTYAERRslfgatRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSG 364
Cdd:cd03257 1 LLEVKNLSVSFPTGG------GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 365 AGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLG--PDVMRRYPHQFSGGQRQRL 442
Cdd:cd03257 75 RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 443 CIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
286-540 |
4.79e-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: 300.18 E-value: 4.79e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRslfgatRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARlsgA 365
Cdd:COG1124 2 LEVRNLSVSYGQGG------RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR---R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGLLNFGMPRAQAlvRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIA 445
Cdd:COG1124 73 RRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREE--RIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 446 RALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
250
....*....|....*
gi 489912973 526 GHAYTRALIDAAPGR 540
Cdd:COG1124 231 KHPYTRELLAASLAF 245
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
16-248 |
1.07e-97 |
|
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: 295.95 E-value: 1.07e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVCGAG--NRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIvTASAR 93
Cdd:cd03257 1 LLEVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLL-----KPTSGSIIFDGKDL-LKLSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 RRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRsVHLPDVERIYDAYPHQLSGGQRQR 173
Cdd:cd03257 75 RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLL-VGVGLPEEVLNRYPHELSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 174 IVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
7-275 |
6.24e-95 |
|
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: 298.74 E-value: 6.24e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 7 PPAGDTSAAVLAIRNLSVS---VCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVL 83
Cdd:COG1123 251 APAAAAAEPLLEVRNLSKRypvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR-----PTSGSILFD 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 84 GEDIvTASARRRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPdvERIYDAYP 163
Cdd:COG1123 326 GKDL-TKLSRRSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 164 HQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGD 243
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
250 260 270
....*....|....*....|....*....|..
gi 489912973 244 LTETGTRDEILARPSQNYTRRLVSSVPSLVPT 275
Cdd:COG1123 483 IVEDGPTEEVFANPQHPYTRALLAAVPSLDPA 514
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
282-539 |
6.77e-87 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 271.84 E-value: 6.77e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 282 GEPVLRITGLGRTYAERRSLFGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARcIVRLIE-PSAGRMLLGETDIA 360
Cdd:PRK11308 2 QQPLLQAIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLAR-LLTMIEtPTGGELYYQGQDLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 361 RLSGAGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGLL-NFGMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQR 439
Cdd:PRK11308 81 KADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLiNTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 440 QRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQ 519
Cdd:PRK11308 161 QRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKE 240
|
250 260
....*....|....*....|
gi 489912973 520 TVLTRPGHAYTRALIDAAPG 539
Cdd:PRK11308 241 QIFNNPRHPYTQALLSATPR 260
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
7-272 |
1.42e-84 |
|
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: 272.33 E-value: 1.42e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 7 PPAGDTSAAVLAIRNLSVSVCGAGN---------RVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegilevSG 77
Cdd:COG4172 266 RPVPPDAPPLLEARDLKVWFPIKRGlfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP------SE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 78 GSARVLGEDIvTASARRRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRR-MPRAQRRAKVLEMFRSVHLPdvE 156
Cdd:COG4172 340 GEIRFDGQDL-DGLSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVHGPgLSAAERRARVAEALEEVGLD--P 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 157 RIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRI 236
Cdd:COG4172 417 AARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRV 496
|
250 260 270
....*....|....*....|....*....|....*.
gi 489912973 237 VVMNRGDLTETGTRDEILARPSQNYTRRLVSSVPSL 272
Cdd:COG4172 497 MVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAAPLL 532
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
283-540 |
1.09e-82 |
|
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: 267.32 E-value: 1.09e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAerrslfGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSA----GRMLLGETD 358
Cdd:COG4172 4 MPLLSVEDLSVAFG------QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 359 IARLSGAGLRPLR-RKVQIVFQDPYRSLNPRRAVGESIIEGL-LNFGMPRAQALVRAARTLGVVGLgPDVMRR---YPHQ 433
Cdd:COG4172 78 LLGLSERELRRIRgNRIAMIFQEPMTSLNPLHTIGKQIAEVLrLHRGLSGAAARARALELLERVGI-PDPERRldaYPHQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 434 FSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVV 513
Cdd:COG4172 157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIV 236
|
250 260
....*....|....*....|....*..
gi 489912973 514 ETGAAQTVLTRPGHAYTRALIDAAPGR 540
Cdd:COG4172 237 EQGPTAELFAAPQHPYTRKLLAAEPRG 263
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-272 |
2.03e-82 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 260.43 E-value: 2.03e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 5 PYPPAGDTSAAVLAIRNLSVSVCGAGNRV--VRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-PEGILevsGGSAR 81
Cdd:PRK09473 1 TVPLAQQQADALLDVKDLRVTFSTPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLaANGRI---GGSAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 82 VLGEDIVTASARRRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVERIYDA 161
Cdd:PRK09473 78 FNGREILNLPEKELNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 162 YPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNR 241
Cdd:PRK09473 158 YPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYA 237
|
250 260 270
....*....|....*....|....*....|.
gi 489912973 242 GDLTETGTRDEILARPSQNYTRRLVSSVPSL 272
Cdd:PRK09473 238 GRTMEYGNARDVFYQPSHPYSIGLLNAVPRL 268
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-273 |
1.20e-81 |
|
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: 255.11 E-value: 1.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVS--VCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEgilevSGGSARVLGEDIvtasARR 94
Cdd:COG1124 2 LEVRNLSVSygQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP-----WSGEVTFDGRPV----TRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 RRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRrakVLEMFRSVHLPdvERIYDAYPHQLSGGQRQRI 174
Cdd:COG1124 73 RRKAFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHGLPDREER---IAELLEQVGLP--PSFLDRYPHQLSGGQRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 175 VIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEIL 254
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
250
....*....|....*....
gi 489912973 255 ARPSQNYTRRLVSSVPSLV 273
Cdd:COG1124 228 AGPKHPYTRELLAASLAFE 246
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
12-277 |
2.48e-78 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 249.65 E-value: 2.48e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSV------SVCGAGNRVVR---NLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARV 82
Cdd:COG4608 3 MAEPLLEVRDLKKhfpvrgGLFGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLE-----EPTSGEILF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 83 LGEDIvTASARRRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPdvERIYDAY 162
Cdd:COG4608 78 DGQDI-TGLSGRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLR--PEHADRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 163 PHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLG 234
|
250 260 270
....*....|....*....|....*....|....*
gi 489912973 243 DLTETGTRDEILARPSQNYTRRLVSSVPSLVPTQR 277
Cdd:COG4608 235 KIVEIAPRDELYARPLHPYTQALLSAVPVPDPERR 269
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
306-538 |
5.54e-73 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 235.76 E-value: 5.54e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 306 RTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRML-LGEtDIARLSGAGLRPLRRKVQIVFQDPYRS 384
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwLGK-DLLGMKDDEWRAVRSDIQMIFQDPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 385 LNPRRAVGESIIEGLLNF--GMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTYhpKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 463 ALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDAAP 538
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
286-539 |
8.11e-72 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 233.05 E-value: 8.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAerrslfGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGA 365
Cdd:COG1135 2 IELENLSKTFP------TKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRPLRRKVQIVFQDPyrSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIA 445
Cdd:COG1135 76 ELRAARRKIGMIFQHF--NLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 446 RALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232
|
250
....*....|....
gi 489912973 526 GHAYTRALIDAAPG 539
Cdd:COG1135 233 QSELTRRFLPTVLN 246
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
34-267 |
5.93e-71 |
|
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: 226.87 E-value: 5.93e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 34 VRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGILEVSGgSARVLGEDIvtasarRRRELRATRMAMVFQEPMTA 113
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPGLTQTSG-EILLDGRPL------LPLSIRGRHIATIMQNPRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 114 LNPVHRVGSQVDEVLRLHRRmPRAQRRAKVLEMFRSVHLPDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPT 193
Cdd:TIGR02770 75 FNPLFTMGNHAIETLRSLGK-LSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 194 TALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVS 267
Cdd:TIGR02770 154 TDLDVVNQARVLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKHETTRKLLS 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
15-282 |
7.56e-70 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 227.32 E-value: 7.56e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVC--GAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL--PEgilEVSGGSARVLGEDIVTA 90
Cdd:PRK11022 2 ALLNVDKLSVHFGdeSAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPG---RVMAEKLEFNGQDLQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 SARRRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVERIYDAYPHQLSGGQ 170
Cdd:PRK11022 79 SEKERRNLVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 171 RQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTR 250
Cdd:PRK11022 159 SQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKA 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489912973 251 DEILARPSQNYTRRL-------------VSSVPSLVPTQREAPGG 282
Cdd:PRK11022 239 HDIFRAPRHPYTQALlralpefaqdkarLASLPGVVPGKYDRPNG 283
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
283-534 |
2.69e-69 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 223.95 E-value: 2.69e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERRSLFGaTRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGET----- 357
Cdd:COG4167 2 SALLEVRNLSKTFKYRTGLFR-RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleyg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 358 DIARLSgaglrplrRKVQIVFQDPYRSLNPRRAVGEsIIEG--LLNFGMPRAQALVRAARTLGVVGLGPDVMRRYPHQFS 435
Cdd:COG4167 81 DYKYRC--------KHIRMIFQDPNTSLNPRLNIGQ-ILEEplRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 436 GGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVET 515
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEY 231
|
250
....*....|....*....
gi 489912973 516 GAAQTVLTRPGHAYTRALI 534
Cdd:COG4167 232 GKTAEVFANPQHEVTKRLI 250
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
29-277 |
1.01e-65 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 216.75 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 29 AGNRVVRNL---SLDVHAGETVCVVGESGSGKSvtSLAVMGLLpegILEVSGGSARVLGEDiVTASARRRRELRATRMAM 105
Cdd:PRK11308 23 KPERLVKALdgvSFTLERGKTLAVVGESGCGKS--TLARLLTM---IETPTGGELYYQGQD-LLKADPEAQKLLRQKIQI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 106 VFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHL-PDverIYDAYPHQLSGGQRQRIVIAMALILEP 184
Cdd:PRK11308 97 VFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrPE---HYDRYPHMFSGGQRQRIAIARALMLDP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 185 KLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRR 264
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQA 253
|
250
....*....|...
gi 489912973 265 LVSSVPSLVPTQR 277
Cdd:PRK11308 254 LLSATPRLNPDDR 266
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
285-526 |
1.01e-64 |
|
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: 210.90 E-value: 1.01e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLRITGLGRTYAERRslfgatRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSG 364
Cdd:cd03258 1 MIELKNVSKVFGDTG------GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 365 AGLRPLRRKVQIVFQDpYRSLNpRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCI 444
Cdd:cd03258 75 KELRKARRRIGMIFQH-FNLLS-SRTVFENVALPLEIAGVPKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 445 ARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTR 524
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
..
gi 489912973 525 PG 526
Cdd:cd03258 232 PQ 233
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
285-515 |
2.53e-63 |
|
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: 208.12 E-value: 2.53e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLRITGLGRTYAERrSLFGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSG 364
Cdd:TIGR02769 2 LLEVRDVTHTYRTG-GLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 365 AGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGLLNF-GMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLC 443
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSPSAVNPRMTVRQIIGEPLRHLtSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVET 515
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
34-270 |
4.98e-61 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 204.55 E-value: 4.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 34 VRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIvTASARRRRELRATRMAMVFQEPMTA 113
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLV-----KATDGEVAWLGKDL-LGMKDDEWRAVRSDIQMIFQDPLAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 114 LNPVHRVGSQVDEVLRLHR-RMPRAQRRAKVLEMFRSVHLpdVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEP 192
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTYHpKLSRQEVKDRVKAMMLKVGL--LPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEP 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 193 TTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVSSVP 270
Cdd:PRK15079 189 VSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVP 266
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
284-540 |
9.63e-61 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 201.45 E-value: 9.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 284 PVLRITGLGRTYAERrSLFGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS 363
Cdd:PRK10419 2 TLLNVSGLSHHYAHG-GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 364 GAGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGLLNF-GMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRL 442
Cdd:PRK10419 81 RAQRKAFRRDIQMVFQDSISAVNPRKTVREIIREPLRHLlSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 443 CIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVET---GAAQ 519
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvGDKL 240
|
250 260
....*....|....*....|.
gi 489912973 520 TVLTRPGHAYTRALIDAAPGR 540
Cdd:PRK10419 241 TFSSPAGRVLQNAVLPAFPVR 261
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
314-525 |
1.91e-59 |
|
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: 196.78 E-value: 1.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYRSLnprraVGE 393
Cdd:COG1122 20 VSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKN---LRELRRKVGLVFQNPDDQL-----FAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIE----GLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:COG1122 92 TVEEdvafGPENLGLPREEIRERVEEALELVGLE-HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGR 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 470 AQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:COG1122 171 RELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
308-538 |
2.23e-59 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 199.95 E-value: 2.23e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 308 VVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPS---AGRMLLGETDIARLSGAGLRPLR-RKVQIVFQDPYR 383
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKLRaEQISMIFQDPMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 384 SLNPRRAVGESIIEGL-LNFGMPRAQALVRAARTLGVVGLgPDV---MRRYPHQFSGGQRQRLCIARALVMDPEVLVADE 459
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLmLHKGMSKAEAFEESVRMLDAVKM-PEArkrMKMYPHEFSGGMRQRVMIAMALLCRPKLLIADE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 460 AVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDAAP 538
Cdd:PRK09473 188 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVP 266
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
287-537 |
3.69e-59 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 200.03 E-value: 3.69e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 287 RITGLGRTYAerrslfGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAG 366
Cdd:PRK11153 3 ELKNISKVFP------QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 367 LRPLRRKVQIVFQdpYRSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIAR 446
Cdd:PRK11153 77 LRKARRQIGMIFQ--HFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 447 ALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPG 526
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPK 233
|
250
....*....|.
gi 489912973 527 HAYTRALIDAA 537
Cdd:PRK11153 234 HPLTREFIQST 244
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
15-271 |
9.42e-59 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 198.59 E-value: 9.42e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVCGAGNRV--VRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPE------------GI--LEVSGG 78
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVkaVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtadrfrwnGIdlLKLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 79 SAR-VLGEDIvtasarrrrelratrmAMVFQEPMTALNPVHRVGSQVDEVL-------RLHRRmpRAQRRAKVLEMFRSV 150
Cdd:COG4170 82 ERRkIIGREI----------------AMIFQEPSSCLDPSAKIGDQLIEAIpswtfkgKWWQR--FKWRKKRAIELLHRV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 151 HLPDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVA 230
Cdd:COG4170 144 GIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESIS 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 489912973 231 EIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVSSVPS 271
Cdd:COG4170 224 QWADTITVLYCGQTVESGPTEQILKSPHHPYTKALLRSMPD 264
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
15-268 |
3.22e-57 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 192.36 E-value: 3.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVCGAGN-------RVVRNLSLDVHAGETVCVVGESGSGKSvtSLAVMgllPEGILEVSGGSARVLGEDI 87
Cdd:COG4167 3 ALLEVRNLSKTFKYRTGlfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKS--TLAKM---LAGIIEPTSGEILINGHKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 88 VTASARRRRELratrMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHL-PDVeriYDAYPHQL 166
Cdd:COG4167 78 EYGDYKYRCKH----IRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPEH---ANFYPHML 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTE 246
Cdd:COG4167 151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|..
gi 489912973 247 TGTRDEILARPSQNYTRRLVSS 268
Cdd:COG4167 231 YGKTAEVFANPQHEVTKRLIES 252
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
298-535 |
4.50e-57 |
|
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: 192.09 E-value: 4.50e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 298 RRSLFGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRK-VQI 376
Cdd:cd03294 27 KEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKkISM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 377 VFQDpyRSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDvMRRYPHQFSGGQRQRLCIARALVMDPEVLV 456
Cdd:cd03294 107 VFQS--FALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGW-EHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 457 ADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALID 535
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFR 262
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
283-514 |
5.42e-56 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 187.56 E-value: 5.42e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAErrslfGATRtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARL 362
Cdd:COG1136 2 SPLLELRNLTKSYGT-----GEGE-VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 SGAGLRPLRR-KVQIVFQDPYrsLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQR 441
Cdd:COG1136 76 SERELARLRRrHIGFVFQFFN--LLPELTALENVALPLLLAGVSRKERRERARELLERVGLG-DRLDHRPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 442 LCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVE 514
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
30-522 |
8.77e-56 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 195.79 E-value: 8.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSV-------------TSLAV---MGLLPE----GILEVSGGSARVLGEDIVT 89
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVlmhvlrgmdqyepTSGRIiyhVALCEKcgyvERPSKVGEPCPVCGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 90 ASA------RRRRELRATRMAMVFQEPMtALNPVHRVgsqVDEVLRlhrRMPRAQRRAKVlEMFRSVHLPDVERIYDAYP 163
Cdd:TIGR03269 92 EEVdfwnlsDKLRRRIRKRIAIMLQRTF-ALYGDDTV---LDNVLE---ALEEIGYEGKE-AVGRAVDLIEMVQLSHRIT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 164 H---QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMN 240
Cdd:TIGR03269 164 HiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 241 RGDLTETGTRDEILARPSQNYtrrlvssvpSLVPTQREAPGGEPVLRITGLGRTYaerrslFGATRTVVAASE-VDLTLR 319
Cdd:TIGR03269 244 NGEIKEEGTPDEVVAVFMEGV---------SEVEKECEVEVGEPIIKVRNVSKRY------ISVDRGVVKAVDnVSLEVK 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 320 RGEILGIVGESGSGKSTVARCIVRLIEPSAGRM--LLGE--TDIARLSGAGLRPLRRKVQIVFQDpyRSLNPRRAVGESI 395
Cdd:TIGR03269 309 EGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDewVDMTKPGPDGRGRAKRYIGILHQE--YDLYPHRTVLDNL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 396 IEGLlNFGMPRAQALVRAARTLGVVGLGPD----VMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:TIGR03269 387 TEAI-GLELPDELARMKAVITLKMVGFDEEkaeeILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVD 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 489912973 472 VLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVL 522
Cdd:TIGR03269 466 VTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
286-516 |
3.62e-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: 185.03 E-value: 3.62e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAErrslfgatrtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSga 365
Cdd:cd03259 1 LELKGLSKTYGS----------VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 glrPLRRKVQIVFQDPyrSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIA 445
Cdd:cd03259 69 ---PERRNIGMVFQDY--ALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALA 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 446 RALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03259 143 RALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
307-551 |
7.60e-55 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 188.19 E-value: 7.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 307 TVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPS----AGRMLLGETDIARLSGAGLRPL-RRKVQIVFQDP 381
Cdd:COG4170 19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSPRERRKIiGREIAMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 YRSLNPRRAVGESIIEGLLN-----FGMPRAQA-LVRAARTLGVVGLG--PDVMRRYPHQFSGGQRQRLCIARALVMDPE 453
Cdd:COG4170 99 SSCLDPSAKIGDQLIEAIPSwtfkgKWWQRFKWrKKRAIELLHRVGIKdhKDIMNSYPHELTEGECQKVMIAMAIANQPR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 454 VLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRAL 533
Cdd:COG4170 179 LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKAL 258
|
250
....*....|....*...
gi 489912973 534 IDAAPgrgwDFRnfRPLP 551
Cdd:COG4170 259 LRSMP----DFR--QPLP 270
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
314-532 |
1.08e-54 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 184.43 E-value: 1.08e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIArLSGAGLRPLRRKVQIVFQdpyrSLN--PRRAV 391
Cdd:COG1126 20 ISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKLRRKVGMVFQ----QFNlfPHLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIIEGLLN-FGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQA 470
Cdd:COG1126 95 LENVTLAPIKvKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 471 QVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRA 532
Cdd:COG1126 174 EVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
303-538 |
4.28e-54 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 191.46 E-value: 4.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 303 GATRTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIePS------AGRMLLGETDIARLSGAGLRPLR-RKVQ 375
Cdd:PRK15134 19 QTVRTVV--NDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGVRgNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 376 IVFQDPYRSLNPRRAVGESIIEGL-LNFGMPRAQALVRAARTLGVVGL--GPDVMRRYPHQFSGGQRQRLCIARALVMDP 452
Cdd:PRK15134 96 MIFQEPMVSLNPLHTLEKQLYEVLsLHRGMRREAARGEILNCLDRVGIrqAAKRLTDYPHQLSGGERQRVMIAMALLTRP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 453 EVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRA 532
Cdd:PRK15134 176 ELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQK 255
|
....*.
gi 489912973 533 LIDAAP 538
Cdd:PRK15134 256 LLNSEP 261
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
313-511 |
7.12e-53 |
|
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: 178.81 E-value: 7.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYRSL-NPRraV 391
Cdd:cd03225 19 DISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS---LKELRRKVGLVFQNPDDQFfGPT--V 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:cd03225 94 EEEVAFGLENLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489912973 472 VLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGK 511
Cdd:cd03225 173 LLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
286-512 |
8.69e-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: 178.84 E-value: 8.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAerrslfGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGA 365
Cdd:cd03255 1 IELKNLSKTYG------GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRPLRRK-VQIVFQDPYrsLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCI 444
Cdd:cd03255 75 ELAAFRRRhIGFVFQSFN--LLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 445 ARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQvCDTIAVMQHGKV 512
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
283-534 |
1.27e-52 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 179.99 E-value: 1.27e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERRSLFgATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLgetDIARL 362
Cdd:PRK15112 2 ETLLEVRNLSKTFRYRTGWF-RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI---DDHPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 SGAGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGL-LNFGMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQR 441
Cdd:PRK15112 78 HFGDYSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLrLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 442 LCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTV 521
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
250
....*....|...
gi 489912973 522 LTRPGHAYTRALI 534
Cdd:PRK15112 238 LASPLHELTKRLI 250
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
35-521 |
1.94e-52 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 186.39 E-value: 1.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 35 RNLSLDVHAGETVCVVGESGSGKSvtSL--AVMGLLP--EG-IL----EVSGGS---ARVLGedivtasarrrrelratr 102
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKS--TLmkILYGLYQpdSGeILidgkPVRIRSprdAIALG------------------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 103 MAMVFQEPMtaLNPVHRVgsqVDEVL-----RLHRRMPRAQRRAKVLEMFRSVHLP-DVeriyDAYPHQLSGGQRQRIVI 176
Cdd:COG3845 82 IGMVHQHFM--LVPNLTV---AENIVlglepTKGGRLDRKAARARIRELSERYGLDvDP----DAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 177 AMALILEPKLLIADEPTTALdvTTQ--KQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEI- 253
Cdd:COG3845 153 LKALYRGARILILDEPTAVL--TPQeaDELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETs 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 254 ---LARpsqnytrRLVSSVPSLVPTQREAPGGEPVLRITGLgrTYAERRSlfgatrtVVAASEVDLTLRRGEILGIVGES 330
Cdd:COG3845 230 eeeLAE-------LMVGREVLLRVEKAPAEPGEVVLEVENL--SVRDDRG-------VPALKDVSLEVRAGEILGIAGVA 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 331 GSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRplRRKVQIVFQDPYRS-LNPRRAVGESII------EGLLNFG 403
Cdd:COG3845 294 GNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERR--RLGVAYIPEDRLGRgLVPDMSVAENLIlgryrrPPFSRGG 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 404 MPRAQALVRAARTL----GVVGLGPDVMRRyphQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQV 479
Cdd:COG3845 372 FLDRKAIRAFAEELieefDVRTPGPDTPAR---SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL 448
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 489912973 480 RERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTV 521
Cdd:COG3845 449 RDA-GAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
284-529 |
3.54e-52 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 181.45 E-value: 3.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 284 PVLRITGLGRTYAErrslfgatrtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS 363
Cdd:COG3842 4 PALELENVSKRYGD----------VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 364 gaglrPLRRKVQIVFQD----PYRSlnprraVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQR 439
Cdd:COG3842 74 -----PEKRNVGMVFQDyalfPHLT------VAENVAFGLRMRGVPKAEIRARVAELLELVGLE-GLADRYPHQLSGGQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 440 QRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQ 519
Cdd:COG3842 142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPE 221
|
250
....*....|
gi 489912973 520 TVLTRPGHAY 529
Cdd:COG3842 222 EIYERPATRF 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
273-541 |
5.04e-52 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 187.76 E-value: 5.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 273 VPTQREAPGGEpVLRITGLGRTYAERRSLFGATRtvvaasEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAG-- 350
Cdd:PRK10261 1 MPHSDELDARD-VLAVENLNIAFMQEQQKIAAVR------NLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 351 ---RMLLGE-----TDIARLSGAGLRPLR-RKVQIVFQDPYRSLNPRRAVGESIIEGL-LNFGMPRAQALVRAARTLGVV 420
Cdd:PRK10261 74 qcdKMLLRRrsrqvIELSEQSAAQMRHVRgADMAMIFQEPMTSLNPVFTVGEQIAESIrLHQGASREEAMVEAKRMLDQV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 421 GLgPD---VMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVA 497
Cdd:PRK10261 154 RI-PEaqtILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVV 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489912973 498 AQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDAAPGRG 541
Cdd:PRK10261 233 AEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAAVPQLG 276
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
282-523 |
1.01e-51 |
|
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: 176.71 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 282 GEPVLRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIAR 361
Cdd:COG1127 2 SEPMIEVRNLTKSFGDRVVLDG----------VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 362 LSGAGLRPLRRKVQIVFQDP--YRSLNprraVGESIIEGLL-NFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQ 438
Cdd:COG1127 72 LSEKELYELRRRIGMLFQGGalFDSLT----VFENVAFPLReHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 439 RQRLCIARALVMDPEVLVADEAVSALD-VSVqAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGA 517
Cdd:COG1127 147 RKRVALARALALDPEILLYDEPTAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
....*.
gi 489912973 518 AQTVLT 523
Cdd:COG1127 226 PEELLA 231
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
12-255 |
1.12e-51 |
|
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: 176.71 E-value: 1.12e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSVSVcgaGNRVV-RNLSLDVHAGETVCVVGESGSGKSVTsLAVMGllpeGILEVSGGSARVLGEDIvTA 90
Cdd:COG1127 1 MSEPMIEVRNLTKSF---GDRVVlDGVSLDVPRGEILAIIGGSGSGKSVL-LKLII----GLLRPDSGEILVDGQDI-TG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 SARRRRELRATRMAMVFQEP-----MTalnpvhrvgsqVDE-V---LRLHRRMPRAQRRAKVLEMFRSVHLPDVEriyDA 161
Cdd:COG1127 72 LSEKELYELRRRIGMLFQGGalfdsLT-----------VFEnVafpLREHTDLSEAEIRELVLEKLELVGLPGAA---DK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 162 YPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNR 241
Cdd:COG1127 138 MPSELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLAD 217
|
250
....*....|....
gi 489912973 242 GDLTETGTRDEILA 255
Cdd:COG1127 218 GKIIAEGTPEELLA 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
13-513 |
2.22e-51 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 183.30 E-value: 2.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 13 SAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVtasA 92
Cdd:COG1129 1 AEPLLEMRGISKSF--GGVKALDGVSLELRPGEVHALLGENGAGKS-TLMKILS----GVYQPDSGEILLDGEPVR---F 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 93 RRRRELRATRMAMVFQEP-----MTalnpvhrvgsqVDEVLRLHR------RMPRAQRRAKVLEMFRSVHLP-DVERIYD 160
Cdd:COG1129 71 RSPRDAQAAGIAIIHQELnlvpnLS-----------VAENIFLGReprrggLIDWRAMRRRARELLARLGLDiDPDTPVG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 161 ayphQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqTAVLFITHDFGVVAEIADRIVVMN 240
Cdd:COG1129 140 ----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQG-VAIIYISHRLDEVFEIADRVTVLR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 241 RGDLTETGTRDEIlarpsqnyTR-RLVS-----SVPSLVPTqREAPGGEPVLRITGLGRtyaerrslfgatRTVVaaSEV 314
Cdd:COG1129 215 DGRLVGTGPVAEL--------TEdELVRlmvgrELEDLFPK-RAAAPGEVVLEVEGLSV------------GGVV--RDV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 315 DLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS-------GAGLRPLRRKVQIVFQDpyrslnp 387
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSprdairaGIAYVPEDRKGEGLVLD------- 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 388 rRAVGE----SIIEGLLNFGMPRAQALVRAART----LGVVGLGPDVMRRyphQFSGGQRQRLCIARALVMDPEVLVADE 459
Cdd:COG1129 345 -LSIREnitlASLDRLSRGGLLDRRRERALAEEyikrLRIKTPSPEQPVG---NLSGGNQQKVVLAKWLATDPKVLILDE 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 460 AVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVV 513
Cdd:COG1129 421 PTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
286-511 |
8.26e-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: 172.37 E-value: 8.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGA 365
Cdd:cd03229 1 LELKNVSKRYGQKTVLND----------VSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 gLRPLRRKVQIVFQDPyrSLNPRRAVGESIIEGLlnfgmpraqalvraartlgvvglgpdvmrryphqfSGGQRQRLCIA 445
Cdd:cd03229 71 -LPPLRRRIGMVFQDF--ALFPHLTVLENIALGL-----------------------------------SGGQQQRVALA 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 446 RALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGK 511
Cdd:cd03229 113 RALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
17-242 |
1.70e-50 |
|
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: 172.67 E-value: 1.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRV--VRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTASARR 94
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKS-TLLNILG----GLDRPTSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 RRELRATRMAMVFQEP-----MTALNPVhrvgsqvdEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGG 169
Cdd:cd03255 76 LAAFRRRHIGFVFQSFnllpdLTALENV--------ELPLLLAGVPKKERRERAEELLERVGLGDRL---NHYPSELSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 170 QRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFgVVAEIADRIVVMNRG 242
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDG 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
302-516 |
2.43e-50 |
|
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: 173.07 E-value: 2.43e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGaTRTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRKVQIVFQDP 381
Cdd:cd03261 10 FG-GRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 --YRSLNprraVGESIIEGLL-NFGMPRAQALVRAARTLGVVGLGPDVmRRYPHQFSGGQRQRLCIARALVMDPEVLVAD 458
Cdd:cd03261 87 alFDSLT----VFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 459 EAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03261 162 EPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
284-513 |
2.95e-50 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 173.32 E-value: 2.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 284 PVLRITGLGRTYAERRslfgatrtvVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS 363
Cdd:COG3638 1 PMLELRNLSKRYPGGT---------PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 364 GAGLRPLRRKVQIVFQDPYrsLNPRRAVGESIIEGLLN--------FGMPRAQALVRAARTLGVVGLGPDVMRRyPHQFS 435
Cdd:COG3638 72 GRALRRLRRRIGMIFQQFN--LVPRLSVLTNVLAGRLGrtstwrslLGLFPPEDRERALEALERVGLADKAYQR-ADQLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 436 GGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVV 513
Cdd:COG3638 149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
283-515 |
9.11e-50 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 172.20 E-value: 9.11e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERrslfGATRTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGetdiarl 362
Cdd:COG1116 5 APALELRGVSKRFPTG----GGGVTAL--DDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 sGAGLRPLRRKVQIVFQDPyrSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRL 442
Cdd:COG1116 72 -GKPVTGPGPDRGVVFQEP--ALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 443 CIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQH--GKVVET 515
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-279 |
3.75e-49 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 170.65 E-value: 3.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVCGAgnrVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGiLEVSGGSARVLGEDIVtasarrR 95
Cdd:PRK10418 4 QIELRNIALQAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAG-VRQTAGRVLLDGKPVA------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEmfrSVHLPDVERIYDAYPHQLSGGQRQRIV 175
Cdd:PRK10418 74 CALRGRKIATIMQNPRSAFNPLHTMHTHARETCLALGKPADDATLTAALE---AVGLENAARVLKLYPFEMSGGMLQRMM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 176 IAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILA 255
Cdd:PRK10418 151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
250 260
....*....|....*....|....
gi 489912973 256 RPSQNYTRRLVSSVPSLVPTQREA 279
Cdd:PRK10418 231 APKHAVTRSLVSAHLALYGMELAS 254
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
286-515 |
4.13e-49 |
|
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: 169.19 E-value: 4.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAerrslfGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGetdiarlsGA 365
Cdd:cd03293 1 LEVRNVSKTYG------GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD--------GE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRPLRRKVQIVFQDPyrSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIA 445
Cdd:cd03293 67 PVTGPGPDRGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 446 RALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVM--QHGKVVET 515
Cdd:cd03293 144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAE 215
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-257 |
2.09e-48 |
|
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: 167.51 E-value: 2.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGaGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEgilevSGGSARVLGEDIvtasARRRR 96
Cdd:COG1122 1 IELENLSFSYPG-GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKP-----TSGEVLVDGKDI----TKKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEPMTALnpvhrVGSQV-DEV---LRlHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQ 172
Cdd:COG1122 71 RELRRKVGLVFQNPDDQL-----FAPTVeEDVafgPE-NLGLPREEIRERVEEALELVGLEHLA---DRPPHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 173 RIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDE 252
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKT-VIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
....*
gi 489912973 253 ILARP 257
Cdd:COG1122 221 VFSDY 225
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
14-246 |
2.25e-48 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 167.53 E-value: 2.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 14 AAVLAIRNLSVSVcGAGN---RVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTA 90
Cdd:COG1136 2 SPLLELRNLTKSY-GTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKS-TLLNILG----GLDRPTSGEVLIDGQDISSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 SARRRRELRATRMAMVFQEP-----MTAL-NpvhrvgsqVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPH 164
Cdd:COG1136 76 SERELARLRRRHIGFVFQFFnllpeLTALeN--------VALPLLL-AGVSRKERRERARELLERVGLGDRL---DHRPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFgVVAEIADRIVVMNRGDL 244
Cdd:COG1136 144 QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRI 222
|
..
gi 489912973 245 TE 246
Cdd:COG1136 223 VS 224
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
286-524 |
4.00e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.16 E-value: 4.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGA 365
Cdd:COG1131 1 IEVRGLTKRYGDKTALDG----------VSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 glrpLRRKVQIVFQDP--YRSLNPRRAVgeSIIEGLlnFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLC 443
Cdd:COG1131 71 ----VRRRIGYVPQEPalYPDLTVRENL--RFFARL--YGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLT 523
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
.
gi 489912973 524 R 524
Cdd:COG1131 221 R 221
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-242 |
4.29e-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: 167.96 E-value: 4.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSVS--VCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvt 89
Cdd:COG1116 3 AAAPALELRGVSKRfpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKS-TLLRLIA----GLEKPTSGEVLVDGKPV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 90 asarrrrELRATRMAMVFQEP-----MTAL-NpvhrvgsqVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYP 163
Cdd:COG1116 76 -------TGPGPDRGVVFQEPallpwLTVLdN--------VALGLEL-RGVPKAERRERARELLELVGLAGFE---DAYP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 164 HQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDfgvVAE---IADRIVVMN 240
Cdd:COG1116 137 HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDEavfLADRVVVLS 213
|
..
gi 489912973 241 RG 242
Cdd:COG1116 214 AR 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
285-523 |
6.14e-48 |
|
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: 167.14 E-value: 6.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLRITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSG 364
Cdd:COG1120 1 MLEAENLSVGYGGRPVL----------DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 365 aglRPLRRKVQIVFQDPYRSLNPRraVGESIIEGLL----NFGMPRAQALVRAARTLGVVGLGPDVMRRYpHQFSGGQRQ 440
Cdd:COG1120 71 ---RELARRIAYVPQEPPAPFGLT--VRELVALGRYphlgLFGRPSAEDREAVEEALERTGLEHLADRPV-DELSGGERQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 441 RLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQT 520
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
...
gi 489912973 521 VLT 523
Cdd:COG1120 225 VLT 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
310-538 |
9.71e-48 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 169.15 E-value: 9.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIE----PSAGRMLLGETDIARLSGAGLRPL-RRKVQIVFQDPYRS 384
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDypgrVMAEKLEFNGQDLQRISEKERRNLvGAEVAMIFQDPMTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 385 LNPRRAVGESIIEGL-LNFGMPRAQALVRAARTLGVVGLgPDVMRR---YPHQFSGGQRQRLCIARALVMDPEVLVADEA 460
Cdd:PRK11022 102 LNPCYTVGFQIMEAIkVHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 461 VSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDAAP 538
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALP 258
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
283-534 |
2.88e-47 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 165.48 E-value: 2.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERRslfgatrtvvAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGE-----T 357
Cdd:PRK11701 4 QPLLSVRGLTKLYGPRK----------GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 358 DIARLSGAGLRPL-RRKVQIVFQDPYRSLNPRRAVGESIIEGLL-----NFGMPRAQAlvraARTLGVVGLGPDVMRRYP 431
Cdd:PRK11701 74 DLYALSEAERRRLlRTEWGFVHQHPRDGLRMQVSAGGNIGERLMavgarHYGDIRATA----GDWLERVEIDAARIDDLP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 432 HQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGK 511
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250 260
....*....|....*....|...
gi 489912973 512 VVETGAAQTVLTRPGHAYTRALI 534
Cdd:PRK11701 230 VVESGLTDQVLDDPQHPYTQLLV 252
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
19-255 |
2.94e-47 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 164.60 E-value: 2.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVcgaGNRVV-RNLSLDVHAGETVCVVGESGSGKSVTsLAVMGllpeGILEVSGGSARVLGEDIvTASARRRRE 97
Cdd:cd03261 3 LRGLTKSF---GGRTVlKGVDLDVRRGEILAIIGPSGSGKSTL-LRLIV----GLLRPDSGEVLIDGEDI-SGLSEAELY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 98 LRATRMAMVFQEP--MTALNpvhrVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIV 175
Cdd:cd03261 74 RLRRRMGMLFQSGalFDSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE---DLYPAELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 176 IAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILA 255
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
19-294 |
6.33e-47 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 167.18 E-value: 6.33e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVCGAGNRV--VRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLpEgilEVSGGSARVLGEDIvTASARRRR 96
Cdd:COG1135 4 LENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKS-TLIRCINLL-E---RPTSGSVLVDGVDL-TALSEREL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEPmtALnpvhrvgsqvdevlrLHRR--------------MPRAQRRAKVLEMFRSVHLPDVEriyDAY 162
Cdd:COG1135 78 RAARRKIGMIFQHF--NL---------------LSSRtvaenvalpleiagVPKAEIRKRVAELLELVGLSDKA---DAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 163 PHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:COG1135 138 PSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENG 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 243 DLTETGTRDEILARPSQNYTRRLVSSVPSLVPTQ------REAPGGEPVLRITGLGRT 294
Cdd:COG1135 218 RIVEQGPVLDVFANPQSELTRRFLPTVLNDELPEellarlREAAGGGRLVRLTFVGES 275
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
302-536 |
1.75e-46 |
|
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: 162.86 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATRTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAglrPLRRKVQIVFQDP 381
Cdd:cd03295 10 YGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV---ELRRKIGYVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 yrSLNPRRAVGESI--IEGLLnfGMPRAQALVRAARTLGVVGLGPD-VMRRYPHQFSGGQRQRLCIARALVMDPEVLVAD 458
Cdd:cd03295 85 --GLFPHMTVEENIalVPKLL--KWPKEKIRERADELLALVGLDPAeFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 459 EAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDA 536
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
16-269 |
3.28e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 162.09 E-value: 3.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLpEgilEVSGGSARVLGEDIvtASARRR 95
Cdd:COG1126 1 MIEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKS-TLLRCINLL-E---EPDSGTITVDGEDL--TDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRATRMAMVFQE----P-MTAL-NpvhrvgsqVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGG 169
Cdd:COG1126 72 INKLRRKVGMVFQQfnlfPhLTVLeN--------VTLAPIKVKKMSKAEAEERAMELLERVGLADKA---DAYPAQLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 170 QRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTETGT 249
Cdd:COG1126 141 QQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVV-VTHEMGFAREVADRVVFMDGGRIVEEGP 219
|
250 260
....*....|....*....|
gi 489912973 250 RDEILARPSQNYTRRLVSSV 269
Cdd:COG1126 220 PEEFFENPQHERTRAFLSKV 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
17-256 |
5.01e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.38 E-value: 5.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTslavMGLLpEGILEVSGGSARVLGEDIVTASARRRR 96
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTT----IRML-LGLLRPTSGEVRVLGEDVARDPAEVRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ElratrMAMVFQEP-----MTALnpvhrvgsqvdEVLRLHRR---MPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSG 168
Cdd:COG1131 74 R-----IGYVPQEPalypdLTVR-----------ENLRFFARlygLPRKEARERIDELLELFGLTDAA---DRKVGTLSG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:COG1131 135 GMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADG 213
|
....*...
gi 489912973 249 TRDEILAR 256
Cdd:COG1131 214 TPDELKAR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-242 |
7.18e-46 |
|
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: 160.33 E-value: 7.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEgilevSGGSARVLGEDIVTASARRRREL 98
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-----TSGEVLVDGKDLTKLSLKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 99 ratrMAMVFQEPMTALnpvhrVGSQV-DEV---LRlHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRI 174
Cdd:cd03225 77 ----VGLVFQNPDDQF-----FGPTVeEEVafgLE-NLGLPEEEIEERVEEALELVGLEGLR---DRSPFTLSGGQKQRV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 175 VIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKT-IIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
17-241 |
1.02e-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: 159.94 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNR--VVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVtasarr 94
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKS-TLLRIIA----GLERPTSGEVLVDGEPVT------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 rreLRATRMAMVFQEPmtALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRI 174
Cdd:cd03293 70 ---GPGPDRGYVFQQD--ALLPWLTVLDNVALGLEL-QGVPKAEARERAEELLELVGLSGFE---NAYPHQLSGGMRQRV 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 175 VIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNR 241
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
314-536 |
1.68e-45 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 160.64 E-value: 1.68e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEP----SAGRMLLgetDIARLSGAGLRPlrRKVQIVFQDPYRSLNPRR 389
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLL---DGKPVAPCALRG--RKIATIMQNPRSAFNPLH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEGLLNFGMPRAQALVRAArtLGVVGLG--PDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVS 467
Cdd:PRK10418 97 TMHTHARETCLALGKPADDATLTAA--LEAVGLEnaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 468 VQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDA 536
Cdd:PRK10418 175 AQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
293-525 |
2.02e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 161.73 E-value: 2.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 293 RTYAERRSLFgatrtvvaasEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDI-ARLSGAGLRPLR 371
Cdd:PRK13634 15 KTPFERRALY----------DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItAGKKNKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 372 RKVQIVFQDPYRSLNpRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMD 451
Cdd:PRK13634 85 KKVGIVFQFPEHQLF-EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAME 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 452 PEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
286-519 |
2.35e-45 |
|
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: 159.66 E-value: 2.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRslfgatrtvVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGA 365
Cdd:cd03256 1 IEVENLSKTYPNGK---------KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRPLRRKVQIVFQDPyrSLNPRRAVGESIIEGLLN--------FGMPRAQALVRAARTLGVVGLGPDVMRRyPHQFSGG 437
Cdd:cd03256 72 ALRQLRRQIGMIFQQF--NLIERLSVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVGLLDKAYQR-ADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 438 QRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGA 517
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
|
..
gi 489912973 518 AQ 519
Cdd:cd03256 229 PA 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
302-530 |
2.62e-45 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 163.01 E-value: 2.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATRtvvAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIArlsgAGLRPLRRKVQIVFQDP 381
Cdd:COG1118 12 FGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF----TNLPPRERRVGFVFQHY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 --YRSLNprraVGESIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADE 459
Cdd:COG1118 85 alFPHMT----VAENIAFGLRVRPPSKAEIRARVEELLELVQL-EGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 460 AVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYT 530
Cdd:COG1118 160 PFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFV 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
314-512 |
6.21e-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: 157.69 E-value: 6.21e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIArLSGAGLRPLRRKVQIVFQDpyRSLNPRRAVGE 393
Cdd:cd03262 19 IDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELRQKVGMVFQQ--FNLFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLN-FGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQV 472
Cdd:cd03262 96 NITLAPIKvKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEV 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489912973 473 LELIEQVrERTGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:cd03262 175 LDVMKDL-AEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
308-518 |
9.36e-45 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 157.52 E-value: 9.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 308 VVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRKVQIVFQDpYRSLnP 387
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD-FRLL-P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 388 RRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVS 467
Cdd:COG2884 93 DRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489912973 468 VQAQVLELIEQVReRTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAA 518
Cdd:COG2884 172 TSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
13-257 |
3.16e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 160.26 E-value: 3.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 13 SAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVT--SLAvmgllpeGILEVSGGSARVLGEDIVTA 90
Cdd:COG3842 2 AMPALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLlrMIA-------GFETPDSGRILLDGRDVTGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 SARRRRelratrMAMVFQEP-----MTALnpvhrvgsqvDEV---LRlHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAY 162
Cdd:COG3842 73 PPEKRN------VGMVFQDYalfphLTVA----------ENVafgLR-MRGVPKAEIRARVAELLELVGLEGLA---DRY 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 163 PHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:COG3842 133 PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDG 212
|
250
....*....|....*
gi 489912973 243 DLTETGTRDEILARP 257
Cdd:COG3842 213 RIEQVGTPEEIYERP 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
314-529 |
5.16e-44 |
|
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: 166.16 E-value: 5.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYrsLNPRravge 393
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLRRQIGVVLQDVF--LFSG----- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLnFGMPRA--QALVRAARtlgVVGLGPDVMRRyPH-----------QFSGGQRQRLCIARALVMDPEVLVADEA 460
Cdd:COG2274 564 TIRENIT-LGDPDAtdEEIIEAAR---LAGLHDFIEAL-PMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEA 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 461 VSALDVSVQAQVLELIEQVRErtGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLTRPGHAY 529
Cdd:COG2274 639 TSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYA 704
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
17-248 |
1.02e-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: 154.60 E-value: 1.02e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIVTASARRRR 96
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLER-----PDSGEILIDGRDVTGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 elratrMAMVFQEPmtALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVI 176
Cdd:cd03259 74 ------IGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGLL---NRYPHELSGGQQQRVAL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03259 142 ARALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
309-525 |
1.54e-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: 154.70 E-value: 1.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIArlsgaGLRPLRRKVQIVFQDpYrSLNPR 388
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHKRPVNTVFQN-Y-ALFPH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSV 468
Cdd:cd03300 87 LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 469 QAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:cd03300 166 RKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEP 222
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
16-286 |
2.11e-43 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 157.27 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVCGAGNRV--VRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGiLEVSGGSARVLGEDIVTASAR 93
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDN-WRVTADRMRFDDIDLLRLSPR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 RRRELRATRMAMVFQEPMTALNPVHRVGSQVDEVL-------RLHRRMPRAQRRAkvLEMFRSVHLPDVERIYDAYPHQL 166
Cdd:PRK15093 82 ERRKLVGHNVSMIFQEPQSCLDPSERVGRQLMQNIpgwtykgRWWQRFGWRKRRA--IELLHRVGIKDHKDAMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTE 246
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489912973 247 TGTRDEILARPSQNYTRRLVSSVP----SLVPTQR--EAPGGEPVL 286
Cdd:PRK15093 240 TAPSKELVTTPHHPYTQALIRAIPdfgsAMPHKSRlnTLPGAIPLL 285
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
33-258 |
3.18e-43 |
|
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: 153.89 E-value: 3.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLL--PegilevSGGSARVLGEDIvTASARRRRELRATRMAMVFQEp 110
Cdd:cd03258 20 ALKDVSLSVPKGEIFGIIGRSGAGKS-TLIRCINGLerP------TSGSVLVDGTDL-TLLSGKELRKARRRIGMIFQH- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 111 mTALNPVHRVGSQVDEVLRLHRrMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPKLLIAD 190
Cdd:cd03258 91 -FNLLSSRTVFENVALPLEIAG-VPKAEIEERVLELLELVGLEDKA---DAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 191 EPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPS 258
Cdd:cd03258 166 EATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
312-525 |
4.70e-43 |
|
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: 153.65 E-value: 4.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRRKVQIVFQDpyRSLNPRRAV 391
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-----PEKRDISYVPQN--YALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 472 VLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:cd03299 168 LREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
314-535 |
5.40e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 153.75 E-value: 5.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDI--ARLSGAG---LRPLRRKVQIVFQDpyRSLNPR 388
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtARSLSQQkglIRQLRQHVGFVFQN--FNLFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIEG-LLNFGMPRAQALVRAARTLGVVGL-GPDvmRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDV 466
Cdd:PRK11264 100 RTVLENIIEGpVIVKGEPKEEATARARELLAKVGLaGKE--TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 467 SVQAQVLELIEQVRE--RTGVSVlfiTHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALID 535
Cdd:PRK11264 178 ELVGEVLNTIRQLAQekRTMVIV---THEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQFLE 245
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
314-524 |
1.17e-42 |
|
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: 153.35 E-value: 1.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGetDIARLSGAGLRPLRRKVQIVFQDPYRSLnprraVGe 393
Cdd:TIGR04520 21 VSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD--GLDTLDEENLWEIRKKVGMVFQNPDNQF-----VG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIE-----GLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSV 468
Cdd:TIGR04520 93 ATVEddvafGLENLGVPREEMRKRVDEALKLVGME-DFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKG 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 469 QAQVLELIEQVRERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLTR 524
Cdd:TIGR04520 172 RKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
20-283 |
1.18e-42 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 153.30 E-value: 1.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 20 RNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLAVMGLlpeGILEVSGGSARVLGEDiVTASARRRRELR 99
Cdd:PRK10419 14 AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKS--TLARLLV---GLESPSQGNVSWRGEP-LAKLNRAQRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 100 ATRMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDveRIYDAYPHQLSGGQRQRIVIAMA 179
Cdd:PRK10419 88 RRDIQMVFQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDD--SVLDKRPPQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 180 LILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILaRPSQ 259
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL-TFSS 244
|
250 260
....*....|....*....|....
gi 489912973 260 NYTRRLVSSVPSLVPTQREAPGGE 283
Cdd:PRK10419 245 PAGRVLQNAVLPAFPVRRRTTEKV 268
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
286-516 |
1.60e-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: 151.56 E-value: 1.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIE-----PSAGRMLLGETDIA 360
Cdd:cd03260 1 IELRDLNVYYGDKHALKD----------ISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 361 RLSGAGLRpLRRKVQIVFQDPyrslNPRRA-VGESIIEGLLNFGM-PRAQALVRAARTLGVVGLGPDVMRR-YPHQFSGG 437
Cdd:cd03260 71 DLDVDVLE-LRRRVGMVFQKP----NPFPGsIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDRlHALGLSGG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 438 QRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTgvSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03260 146 QQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-277 |
2.15e-42 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 160.79 E-value: 2.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSV---CGAGNRVVR------NLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGED 86
Cdd:PRK10261 313 ILQVRNLVTRFplrSGLLNRVTRevhaveKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV-----ESQGGEIIFNGQR 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 87 IVTASARRRRELRATrMAMVFQEPMTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDvERIYdAYPHQL 166
Cdd:PRK10261 388 IDTLSPGKLQALRRD-IQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLP-EHAW-RYPHEF 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTE 246
Cdd:PRK10261 465 SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVE 544
|
250 260 270
....*....|....*....|....*....|.
gi 489912973 247 TGTRDEILARPSQNYTRRLVSSVPSLVPTQR 277
Cdd:PRK10261 545 IGPRRAVFENPQHPYTRKLMAAVPVADPSRQ 575
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
33-280 |
6.01e-42 |
|
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: 151.50 E-value: 6.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDiVTASARRRRELRATRMAMVFQEPMT 112
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLE-----KPAQGTVSFRGQD-LYQLDRKQRRAFRRDVQLVFQDSPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 113 ALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDveRIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEP 192
Cdd:TIGR02769 100 AVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRS--EDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 193 TTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARpSQNYTRRLVSSVPSL 272
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSAVLPE 256
|
....*...
gi 489912973 273 VPTQREAP 280
Cdd:TIGR02769 257 HPVRRSIT 264
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
286-512 |
7.15e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 149.20 E-value: 7.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGA 365
Cdd:COG4619 1 LELEGLSFRVGGKPIL----------SPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRplrRKVQIVFQDPYRslnprraVGESIIEGL--------LNFGMPRAQALVRAartlgvVGLGPDVMRRYPHQFSGG 437
Cdd:COG4619 71 EWR---RQVAYVPQEPAL-------WGGTVRDNLpfpfqlreRKFDRERALELLER------LGLPPDILDKPVERLSGG 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 438 QRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:COG4619 135 ERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
34-268 |
9.95e-42 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 151.10 E-value: 9.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 34 VRNLSLDVHAGETVCVVGESGSGKSvtSLAVMgllPEGILEVSGGSARVLGEDIvtasARRRRELRATRMAMVFQEPMTA 113
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKS--TLAKM---LAGMIEPTSGELLIDDHPL----HFGDYSYRSQRIRMIFQDPSTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 114 LNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVERIYdaYPHQLSGGQRQRIVIAMALILEPKLLIADEPT 193
Cdd:PRK15112 100 LNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASY--YPHMLAPGQKQRLGLARALILRPKVIIADEAL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 194 TALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVSS 268
Cdd:PRK15112 178 ASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLIAG 252
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
12-254 |
1.18e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 149.85 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSL--AVMGLLPegileVSGGSARVLGEDIvt 89
Cdd:COG1121 2 MMMPAIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKS--TLlkAILGLLP-----PTSGTVRLFGKPP-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 90 asarrrrELRATRMAMVFQE-------PMTalnpvhrvgsqVDEVLRLHR-------RMPRAQRRAKVLEMFRSVHLPDV 155
Cdd:COG1121 71 -------RRARRRIGYVPQRaevdwdfPIT-----------VRDVVLMGRygrrglfRRPSRADREAVDEALERVGLEDL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 156 E--RIydaypHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLFITHDFGVVAEIA 233
Cdd:COG1121 133 AdrPI-----GELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELR-REGKTILVVTHDLGAVREYF 206
|
250 260
....*....|....*....|.
gi 489912973 234 DRIVVMNRGdLTETGTRDEIL 254
Cdd:COG1121 207 DRVLLLNRG-LVAHGPPEEVL 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
312-511 |
1.41e-41 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 147.14 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYRslnprraV 391
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLRKNIAYVPQDPFL-------F 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIIEGLLnfgmpraqalvraartlgvvglgpdvmrryphqfSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:cd03228 89 SGTIRENIL----------------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489912973 472 VLELIEQVRErtGVSVLFITHDLRVAAQvCDTIAVMQHGK 511
Cdd:cd03228 135 ILEALRALAK--GKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
313-525 |
3.52e-41 |
|
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: 152.18 E-value: 3.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGET---DIARlsGAGLRPLRRKVQIVFQDPyrSLNPRR 389
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSAR--GIFLPPHRRRIGYVFQEA--RLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVgesiiEGLLNFGMPRAQALVRAARTLGVV---GLGPdVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDV 466
Cdd:COG4148 93 SV-----RGNLLYGRKRAPRAERRISFDEVVellGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 467 SVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:COG4148 167 ARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
30-269 |
7.22e-41 |
|
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: 151.54 E-value: 7.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSVTslavMGLLPEgILEVSGGSARVLGEDIVTASARRRRELRATRMAMVFQE 109
Cdd:TIGR01186 5 GKKGVNDADLAIAKGEIFVIMGLSGSGKSTT----VRMLNR-LIEPTAGQIFIDGENIMKQSPVELREVRRKKIGMVFQQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 pmTALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPKLLIA 189
Cdd:TIGR01186 80 --FALFPHMTILQNTSLGPEL-LGWPEQERKEKALELLKLVGLEEYE---HRYPDELSGGMQQRVGLARALAAEPDILLM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 190 DEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVSSV 269
Cdd:TIGR01186 154 DEAFSALDPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
16-254 |
1.59e-40 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 147.11 E-value: 1.59e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvtasARRR 95
Cdd:COG1120 1 MLEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKS-TLLRALA----GLLKPSSGEVLLDGRDL----ASLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRATRMAMVFQEPMTAlnpvhrVGSQVDEVLRL----HRRM---PRAQRRAKVLEMFRSVHLPD-VERIYDayphQLS 167
Cdd:COG1120 70 RRELARRIAYVPQEPPAP------FGLTVRELVALgrypHLGLfgrPSAEDREAVEEALERTGLEHlADRPVD----ELS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 168 GGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTET 247
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
....*..
gi 489912973 248 GTRDEIL 254
Cdd:COG1120 220 GPPEEVL 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
34-270 |
1.85e-40 |
|
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: 147.40 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 34 VRNLSLDVHAGETVCVVGESGSGKSvTSLAVMgllpEGILEVSGGSARVLGEDIVTASARRRRELRATRMAMVFQEpmTA 113
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKS-TLLRCI----NRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQS--FA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 114 LNPvHR-VGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPKLLIADEP 192
Cdd:cd03294 113 LLP-HRtVLENVAFGLEV-QGVPRAEREERAAEALELVGLEGWE---HKYPDELSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 193 TTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVSSVP 270
Cdd:cd03294 188 FSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVD 265
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
314-460 |
4.72e-40 |
|
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: 142.40 E-value: 4.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPyrSLNPRRAVGE 393
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE---RKSLRKEIGYVFQDP--QLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLNFGMPRAQALVRAAR---TLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEA 460
Cdd:pfam00005 79 NLRLGLLLKGLSKREKDARAEEaleKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
308-551 |
5.61e-40 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 148.03 E-value: 5.61e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 308 VVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEP----SAGRMLLGETDIARLSGAGLRPL-RRKVQIVFQDPY 382
Cdd:PRK15093 20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLvGHNVSMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 383 RSLNPRRAVGESIIEGL----------LNFGMPRAqalvRAARTLGVVGLG--PDVMRRYPHQFSGGQRQRLCIARALVM 450
Cdd:PRK15093 100 SCLDPSERVGRQLMQNIpgwtykgrwwQRFGWRKR----RAIELLHRVGIKdhKDAMRSFPYELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 451 DPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYT 530
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYT 255
|
250 260
....*....|....*....|.
gi 489912973 531 RALIDAAPGRGwdfrnfRPLP 551
Cdd:PRK15093 256 QALIRAIPDFG------SAMP 270
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
285-528 |
9.10e-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: 145.00 E-value: 9.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLRITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSg 364
Cdd:COG4555 1 MIEVENLSKKYGKVPAL----------KDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 365 aglRPLRRKVQIVFQDPYrsLNPRRAVGESI-IEGLLNfGMPRAQALVRAARTLGVVGLGPDVMRRYpHQFSGGQRQRLC 443
Cdd:COG4555 70 ---REARRQIGVLPDERG--LYDRLTVRENIrYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRV-GELSTGMKKKVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLT 523
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
....*
gi 489912973 524 RPGHA 528
Cdd:COG4555 222 EIGEE 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
306-516 |
1.13e-39 |
|
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: 142.57 E-value: 1.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 306 RTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQdpyrsl 385
Cdd:cd03214 12 RTVL--DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS---PKELARKIAYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 386 nprravgesiiegllnfgmpraqalvrAARTLGVVGLgpdVMRRYpHQFSGGQRQRLCIARALVMDPEVLVADEAVSALD 465
Cdd:cd03214 81 ---------------------------ALELLGLAHL---ADRPF-NELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489912973 466 VSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03214 130 IAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
17-258 |
1.38e-39 |
|
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: 144.02 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgaGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGllpegILEVSGGSARVLGEDIVTASARRRR 96
Cdd:cd03299 1 LKVENLSKDW---KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAG-----FIKPDSGKILLNGKDITNLPPEKRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 elratrMAMVFQEpmTALNPVHRVGSQVDEVLRlHRRMPRAQRRAKVLEMFRSVHlpdVERIYDAYPHQLSGGQRQRIVI 176
Cdd:cd03299 73 ------ISYVPQN--YALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLG---IDHLLNRKPETLSGGEQQRVAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILAR 256
Cdd:cd03299 141 ARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
..
gi 489912973 257 PS 258
Cdd:cd03299 221 PK 222
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
314-516 |
1.60e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 151.86 E-value: 1.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYRslnprraVGE 393
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLRRQIGVVPQDTFL-------FSG 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLnFGMPRA--QALVRAARTLGVVglgpDVMRRYPHQF-----------SGGQRQRLCIARALVMDPEVLVADEA 460
Cdd:COG1132 429 TIRENIR-YGRPDAtdEEVEEAAKAAQAH----EFIEALPDGYdtvvgergvnlSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 461 VSALDVSVQAQVLELIEQVRE-RTgvsVLFITHDLRvAAQVCDTIAVMQHGKVVETG 516
Cdd:COG1132 504 TSALDTETEALIQEALERLMKgRT---TIVIAHRLS-TIRNADRILVLDDGRIVEQG 556
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
17-253 |
3.79e-39 |
|
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: 142.70 E-value: 3.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEGILEV-SGGSARVLGEDIVTASARRR 95
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKS-TLLRLLNRLNDLIPGApDEGEVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRAtrMAMVFQEPmtalNPVHrvGSQVDEV---LRLHRRMPRAQRRAKVLEMFRSVHLPD-VERiyDAYPHQLSGGQR 171
Cdd:cd03260 78 ELRRR--VGMVFQKP----NPFP--GSIYDNVaygLRLHGIKLKEELDERVEEALRKAALWDeVKD--RLHALGLSGGQQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 172 QRIVIAMALILEPKLLIADEPTTALD-VTTQKqILALIRELqdRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTR 250
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDpISTAK-IEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPT 224
|
...
gi 489912973 251 DEI 253
Cdd:cd03260 225 EQI 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
265-526 |
4.46e-39 |
|
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: 150.29 E-value: 4.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 265 LVSSVPSLVPTQREAPGGEPV-LRITGLGRTYAERRslfgatrtvVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVR 343
Cdd:COG4988 315 LDAPEPAAPAGTAPLPAAGPPsIELEDVSFSYPGGR---------PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 344 LIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYrsLnprraVGESIIEGLLnFGMPRA--QALVRAARTLGVvg 421
Cdd:COG4988 386 FLPPYSGSILINGVDLSDLD---PASWRRQIAWVPQNPY--L-----FAGTIRENLR-LGRPDAsdEELEAALEAAGL-- 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 422 lgPDVMRRYPHQF-----------SGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQV-RERTgvsVLF 489
Cdd:COG4988 453 --DEFVAALPDGLdtplgeggrglSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGRT---VIL 527
|
250 260 270
....*....|....*....|....*....|....*..
gi 489912973 490 ITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLTRPG 526
Cdd:COG4988 528 ITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
28-266 |
4.51e-39 |
|
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: 142.82 E-value: 4.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 28 GAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIvtasARRRRELRATRMAMVF 107
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI-----EPTSGEIFIDGEDI----REQDPVELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 108 QEpmTALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVErIYDAYPHQLSGGQRQRIVIAMALILEPKLL 187
Cdd:cd03295 82 QQ--IGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDPAE-FADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 188 IADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLV 266
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFV 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
282-525 |
7.17e-39 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 142.87 E-value: 7.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 282 GEPVLRITGLGRTyaerrslFGAtrtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIAR 361
Cdd:COG0411 1 SDPLLEVRGLTKR-------FGG---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 362 LS-----GAGlrpLRRKVQIVfqDPYRSL----N----PRRAVGESIIEGLLNFGMPRAQ---ALVRAARTLGVVGLGpD 425
Cdd:COG0411 71 LPphriaRLG---IARTFQNP--RLFPELtvleNvlvaAHARLGRGLLAALLRLPRARREereARERAEELLERVGLA-D 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 426 VMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIA 505
Cdd:COG0411 145 RADEPAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIV 224
|
250 260
....*....|....*....|
gi 489912973 506 VMQHGKVVETGAAQTVLTRP 525
Cdd:COG0411 225 VLDFGRVIAEGTPAEVRADP 244
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
307-518 |
1.27e-38 |
|
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: 140.97 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 307 TVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglRPLRRKVQIVFQDPyrSLN 386
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP----REVRRRIGIVFQDL--SVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 PRRAVGESI-IEGLLnFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALD 465
Cdd:cd03265 86 DELTGWENLyIHARL-YGVPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489912973 466 VSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAA 518
Cdd:cd03265 164 PQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
19-242 |
1.47e-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: 140.36 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEgileVSGGSARVLGEDIvtASARRRREL 98
Cdd:cd03262 3 IKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKS-TLLRCINLLEE----PDSGTIIIDGLKL--TDDKKNINE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 99 RATRMAMVFQ-----EPMTALNpvhrvgsQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQR 173
Cdd:cd03262 74 LRQKVGMVFQqfnlfPHLTVLE-------NITLAPIKVKGMSKAEAEERALELLEKVGLADKA---DAYPAQLSGGQQQR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 174 IVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRG 242
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVV-VTHEMGFAREVADRVIFMDDG 211
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
17-257 |
1.90e-38 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 144.13 E-value: 1.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVT--SLAvmgllpeGILEVSGGSARVLGEDIVTASARR 94
Cdd:COG1118 3 IEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLlrIIA-------GLETPDSGRIVLNGRDLFTNLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 RRElratrMAMVFQEP-----MTalnpvhrVGSQVDEVLRlHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGG 169
Cdd:COG1118 74 ERR-----VGFVFQHYalfphMT-------VAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLA---DRYPSQLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 170 QRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGT 249
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
....*...
gi 489912973 250 RDEILARP 257
Cdd:COG1118 218 PDEVYDRP 225
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
283-516 |
2.12e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.08 E-value: 2.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERRSLfgatrtvvAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETdiaRL 362
Cdd:PRK13635 3 EEIIRVEHISFRYPDAATY--------ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 SGAGLRPLRRKVQIVFQDPyrslnPRRAVGESIIE----GLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQ 438
Cdd:PRK13635 72 SEETVWDVRRQVGMVFQNP-----DNQFVGATVQDdvafGLENIGVPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 439 RQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVcDTIAVMQHGKVVETG 516
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQA-DRVIVMNKGEILEEG 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
307-516 |
2.75e-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: 139.70 E-value: 2.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 307 TVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIArlsgaGLRPLRRKVQIVFQDpYrSLN 386
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-----DLPPKDRDIAMVFQN-Y-ALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 PRRAVGESIIEGLLNFGMPRA---QALVRAARTLGVVGLgpdvMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSA 463
Cdd:cd03301 85 PHMTVYDNIAFGLKLRKVPKDeidERVREVAELLQIEHL----LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489912973 464 LDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
30-258 |
4.80e-38 |
|
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: 139.68 E-value: 4.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVtasarrRRELRATRMAMVFQE 109
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKT-TLLRLIA----GFETPTSGEILLDGKDIT------NLPPHKRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 pmTALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVERiydAYPHQLSGGQRQRIVIAMALILEPKLLIA 189
Cdd:cd03300 81 --YALFPHLTVFENIAFGLRL-KKLPKAEIKERVAEALDLVQLEGYAN---RKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 190 DEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPS 258
Cdd:cd03300 155 DEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
302-529 |
5.27e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 143.29 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATRTVvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIArlsgaGLRPLRRKVQIVFQDP 381
Cdd:COG3839 13 YGGVEAL---KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-----DLPPKDRNIAMVFQSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 --YRSLNprraVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADE 459
Cdd:COG3839 85 alYPHMT----VYENIAFPLKLRKVPKAEIDRRVREAAELLGLE-DLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 460 AVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAY 529
Cdd:COG3839 160 PLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLF 229
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
287-511 |
6.45e-38 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 136.99 E-value: 6.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 287 RITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgag 366
Cdd:cd00267 1 EIENLSFRYGGRTAL----------DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 367 LRPLRRKVQIVFQdpyrslnprravgesiiegllnfgmpraqalvraartlgvvglgpdvmrryphqFSGGQRQRLCIAR 446
Cdd:cd00267 68 LEELRRRIGYVPQ------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 447 ALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGK 511
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
19-294 |
9.33e-38 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 142.25 E-value: 9.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVCGAGNRV--VRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEGilevSGGSARVLGEDIvTASARRRR 96
Cdd:PRK11153 4 LKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKS-TLIRCINLLERP----TSGRVLVDGQDL-TALSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQepmtalnpvH-------RVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVeriYDAYPHQLSGG 169
Cdd:PRK11153 78 RKARRQIGMIFQ---------HfnllssrTVFDNVALPLEL-AGTPKAEIKARVTELLELVGLSDK---ADRYPAQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 170 QRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGT 249
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGT 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 489912973 250 RDEILARPSQNYTRRLVSSVPSL-VPTQREA-------PGGEPVLRITGLGRT 294
Cdd:PRK11153 225 VSEVFSHPKHPLTREFIQSTLHLdLPEDYLArlqaeptTGSGPLLRLEFTGES 277
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
309-533 |
1.18e-37 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 143.25 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRK-VQIVFQDpyRSLNP 387
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQS--FALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 388 RRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVS 467
Cdd:PRK10070 120 HMTVLDNTAFGMELAGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 468 VQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRAL 533
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTF 264
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
286-512 |
1.36e-37 |
|
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: 136.37 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGA 365
Cdd:cd03230 1 IEVRNLSKRYGKKTALDD----------ISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 glrpLRRKVQIVFQDP--YRSLNPRravgESIiegllnfgmpraqalvraartlgvvglgpdvmrryphQFSGGQRQRLC 443
Cdd:cd03230 71 ----VKRRIGYLPEEPslYENLTVR----ENL-------------------------------------KLSGGMKQRLA 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:cd03230 106 LAQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
309-516 |
1.42e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 140.30 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDI-ARLSGAGLRPLRRKVQIVFQDPYRSLNp 387
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITItHKTKDKYIRPVRKRIGMVFQFPESQLF- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 388 RRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVS 467
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489912973 468 VQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
313-516 |
1.77e-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: 137.81 E-value: 1.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRrGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGET--DIARLSgAGLRPLRRKVQIVFQDpyRSLNPRRA 390
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlFDSRKK-INLPPQQRKIGLVFQQ--YALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 391 VGESIIegllnFGMPR---AQALVRAARTLGVVGLGPdVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVS 467
Cdd:cd03297 92 VRENLA-----FGLKRkrnREDRISVDELLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489912973 468 VQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03297 166 LRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
17-242 |
2.32e-37 |
|
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: 135.99 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTASARRRR 96
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKT-TLIKIIL----GLLKPDSGEIKVLGKDIKKEPEEVKR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ElratrMAMVFQEPMtalnpvhrvgsqvdevlrLHRRMpraqrraKVLEMFRsvhlpdveriydayphqLSGGQRQRIVI 176
Cdd:cd03230 74 R-----IGYLPEEPS------------------LYENL-------TVRENLK-----------------LSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
326-534 |
2.75e-37 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 140.32 E-value: 2.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 326 IVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRRKVQIVFQDpyRSLNPRRAVGESIIEGLLNFGMP 405
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP-----PHLRHINMVFQS--YALFPHMTVEENVAFGLKMRKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 406 RAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGV 485
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489912973 486 SVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALI 534
Cdd:TIGR01187 153 TFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFI 201
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
279-534 |
2.89e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 138.25 E-value: 2.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 279 APGGEPVLRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIE--PSA---GRML 353
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDKQALKD----------INLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 354 LGETDIarlSGAGLRP--LRRKVQIVFQDPyrslNP-------------------RRAVGESIIEgllnfgmpraQALVR 412
Cdd:COG1117 75 LDGEDI---YDPDVDVveLRRRVGMVFQKP----NPfpksiydnvayglrlhgikSKSELDEIVE----------ESLRK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 413 AArtlgvvgLGPDV---MRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALD-VSVqAQVLELIEQVRERtgVSVL 488
Cdd:COG1117 138 AA-------LWDEVkdrLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpIST-AKIEELILELKKD--YTIV 207
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489912973 489 FITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALI 534
Cdd:COG1117 208 IVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
310-518 |
3.46e-37 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 137.84 E-value: 3.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARcIVRLIE-PSAGRMLLGETDI---ARLSGAGLRPLRRKVQIVFQDpYrSL 385
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLEtPDSGQLNIAGHQFdfsQKPSEKAIRLLRQKVGMVFQQ-Y-NL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 386 NPRRAVGESIIEGLLN-FGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSAL 464
Cdd:COG4161 94 WPHLTVMENLIEAPCKvLGLSKEQAREKAMKLLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 465 DVSVQAQVLELIEQVRErTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAA 518
Cdd:COG4161 173 DPEITAQVVEIIRELSQ-TGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA 225
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
18-248 |
6.84e-37 |
|
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: 134.87 E-value: 6.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 18 AIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvtasarrrre 97
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKS-TLLKTLA----GLLKPSSGEILLDGKDL---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 98 lratrmamvfqepmtalnpvhrvgsqvdevLRLHRRMpRAQRRA---KVLEMFRSVHLpdVERIYDayphQLSGGQRQRI 174
Cdd:cd03214 64 ------------------------------ASLSPKE-LARKIAyvpQALELLGLAHL--ADRPFN----ELSGGERQRV 106
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 175 VIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03214 107 LLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
309-529 |
6.95e-37 |
|
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: 136.70 E-value: 6.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRRKVQIVFQdpYRSLNPR 388
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP-----VQERNVGFVFQ--HYALFRH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIEGL----LNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSAL 464
Cdd:cd03296 89 MTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQL-DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 465 DVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAY 529
Cdd:cd03296 168 DAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
315-534 |
7.27e-37 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 136.42 E-value: 7.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 315 DLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRRKVQIVFQDpyRSLNPRRAVGES 394
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-----PAERPVSMLFQE--NNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 395 IIEGL---LNFGMPRAQALVRAARTLGVVGLGPdvmrRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:COG3840 92 IGLGLrpgLKLTAEQRAQVEQALERVGLAGLLD----RLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 472 VLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALI 534
Cdd:COG3840 168 MLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-252 |
1.24e-36 |
|
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: 136.02 E-value: 1.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSVSVCGAGNRVV--RNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVT 89
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELTilKGISLEVEAGESVAIVGASGSGKS-TLLGLLA----GLDRPTSGTVRLAGQDLFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 90 ASARRRRELRATRMAMVFQE----P-MTALNPVhrvgsqvdeVLRLH-RRMPRAQRRAKvlEMFRSVHLpdVERIyDAYP 163
Cdd:COG4181 79 LDEDARARLRARHVGFVFQSfqllPtLTALENV---------MLPLElAGRRDARARAR--ALLERVGL--GHRL-DHYP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 164 HQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGvVAEIADRIVVMNRGD 243
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPA-LAARCDRVLRLRAGR 223
|
....*....
gi 489912973 244 LTETGTRDE 252
Cdd:COG4181 224 LVEDTAATA 232
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
313-525 |
2.63e-36 |
|
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: 138.71 E-value: 2.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLL-GETDIARLSGAGLRPLRRKVQIVFQDPyrSLNPRRAV 391
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLnGRTLFDSRKGIFLPPEKRRIGYVFQEA--RLFPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESiieglLNFGMPRA---QALVRAARTLGVVGLGPdVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSV 468
Cdd:TIGR02142 93 RGN-----LRYGMKRArpsERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 469 QAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:TIGR02142 167 KYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
17-242 |
2.92e-36 |
|
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: 133.08 E-value: 2.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIVTASARRRR 96
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLE-----EPDSGSILIDGEDLTDLEDELPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATrmAMVFQEPmtALNPvhrvgsqvdevlrlhrrmpraqrrakvlemfrsvHLPDVERIydAYPhqLSGGQRQRIVI 176
Cdd:cd03229 74 LRRRI--GMVFQDF--ALFP----------------------------------HLTVLENI--ALG--LSGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
15-242 |
3.60e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.18 E-value: 3.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVCGaGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLpegiLEVSGGSARVLGEDIvTASARR 94
Cdd:COG3638 1 PMLELRNLSKRYPG-GTPALDDVSLEIERGEFVALIGPSGAGKS-TLLRCLNGL----VEPTSGEILVDGQDV-TALRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 RRELRATRMAMVFQEPmtALNPVHRVgsqVDEVL--RLHR--------RMPRAQRRAKVLEMFRSVHLPDVeriydAY-- 162
Cdd:COG3638 74 ALRRLRRRIGMIFQQF--NLVPRLSV---LTNVLagRLGRtstwrsllGLFPPEDRERALEALERVGLADK-----AYqr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 163 PHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:COG3638 144 ADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDG 223
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
302-525 |
3.95e-36 |
|
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: 134.49 E-value: 3.95e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGAtrtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS-----GAGlrpLRRKVQI 376
Cdd:cd03219 10 FGG---LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpheiaRLG---IGRTFQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 377 VfqDPYRSL----NPRRAVGESIIEGLLNFGMPR--AQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVM 450
Cdd:cd03219 84 P--RLFPELtvleNVMVAAQARTGSGLLLARARReeREARERAEELLERVGLA-DLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 451 DPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNP 234
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
19-242 |
6.46e-36 |
|
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: 131.60 E-value: 6.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIvtasarrrrel 98
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK-----PTSGEILIDGKDI----------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 99 ratrmamvfqepmtalnpvhrvgsqvdevlrlhRRMPRAQRRAKVlemfrsvhlpdveriydAYPHQLSGGQRQRIVIAM 178
Cdd:cd00267 64 ---------------------------------AKLPLEELRRRI-----------------GYVPQLSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 179 ALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPELAELAADRVIVLKDG 156
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
283-519 |
7.19e-36 |
|
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: 133.71 E-value: 7.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAerrslfGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARL 362
Cdd:COG4181 6 APIIELRGLTKTVG------TGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 SG---AGLRplRRKVQIVFQD----PyrSLNprravgesiieGLLNFGMP-----RAQALVRAARTLGVVGLGpDVMRRY 430
Cdd:COG4181 80 DEdarARLR--ARHVGFVFQSfqllP--TLT-----------ALENVMLPlelagRRDARARARALLERVGLG-HRLDHY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 431 PHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQvCDTIAVMQHG 510
Cdd:COG4181 144 PAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAG 222
|
....*....
gi 489912973 511 KVVETGAAQ 519
Cdd:COG4181 223 RLVEDTAAT 231
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
19-514 |
8.49e-36 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 140.20 E-value: 8.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVcgaGNRVV-RNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEdivtasarrrre 97
Cdd:COG0488 1 LENLSKSF---GGRPLlDDVSLSINPGDRIGLVGRNGAGKS-TLLKILA----GELEPDSGEVSIPKG------------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 98 lraTRMAMVFQEP-----MTALnpvHRVGSQVDEVLRLHRRMPRAQ-----------RRAKVLEMFRSVHL----PDVER 157
Cdd:COG0488 61 ---LRIGYLPQEPpldddLTVL---DTVLDGDAELRALEAELEELEaklaepdedleRLAELQEEFEALGGweaeARAEE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 158 I----------YDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTqkqILALIRELQDRhQTAVLFITHD-- 225
Cdd:COG0488 135 IlsglgfpeedLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWLEEFLKNY-PGTVLVVSHDry 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 226 FgvVAEIADRIVVMNRGDLTE-TG-------TRDEILARPSQNYTRR--------------------------------- 264
Cdd:COG0488 211 F--LDRVATRILELDRGKLTLyPGnysayleQRAERLEQEAAAYAKQqkkiakeeefirrfrakarkakqaqsrikalek 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 265 -------LVSSVPSL-VPTQREApgGEPVLRITGLGRTYAERRsLFgatrtvvaaSEVDLTLRRGEILGIVGESGSGKST 336
Cdd:COG0488 289 lereeppRRDKTVEIrFPPPERL--GKKVLELEGLSKSYGDKT-LL---------DDLSLRIDRGDRIGLIGPNGAGKST 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 337 VARCIVRLIEPSAGRMLLGETdiarlsgaglrplrrkVQIVF--QDpYRSLNPrravGESIIEGLLNFGMPRAQALVRAa 414
Cdd:COG0488 357 LLKLLAGELEPDSGTVKLGET----------------VKIGYfdQH-QEELDP----DKTVLDELRDGAPGGTEQEVRG- 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 415 rTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDV-SVQAqvleLIEQVRERTGvSVLFITHD 493
Cdd:COG0488 415 -YLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIeTLEA----LEEALDDFPG-TVLLVSHD 488
|
570 580
....*....|....*....|.
gi 489912973 494 LRVAAQVCDTIAVMQHGKVVE 514
Cdd:COG0488 489 RYFLDRVATRILEFEDGGVRE 509
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
12-269 |
1.44e-35 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 133.90 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSVSVcgaGNRV-VRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTA 90
Cdd:PRK11701 2 MDQPLLSVRGLTKLY---GPRKgCRDVSFDLYPGEVLGIVGESGSGKT-TLLNALS----ARLAPDAGEVHYRMRDGQLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 SARRRRELRATRMA-----MVFQEPMTALNPVHRVGSQVDEvlrlhRRMPRAQR-----RAKVLEMFRSVHLpDVERIYD 160
Cdd:PRK11701 74 DLYALSEAERRRLLrtewgFVHQHPRDGLRMQVSAGGNIGE-----RLMAVGARhygdiRATAGDWLERVEI-DAARIDD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 161 AyPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMN 240
Cdd:PRK11701 148 L-PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMK 226
|
250 260
....*....|....*....|....*....
gi 489912973 241 RGDLTETGTRDEILARPSQNYTRRLVSSV 269
Cdd:PRK11701 227 QGRVVESGLTDQVLDDPQHPYTQLLVSSV 255
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
17-244 |
2.35e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.48 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGagNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIVTASARRRR 96
Cdd:COG4619 1 LELEGLSFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDP-----PTSGEIYLDGKPLSAMPPPEWR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELratrMAMVFQEPmtALNPvHRVGSQVDEVLRLHRRMPRaqrRAKVLEMFRSVHLPdvERIYDAYPHQLSGGQRQRIVI 176
Cdd:COG4619 74 RQ----VAYVPQEP--ALWG-GTVRDNLPFPFQLRERKFD---RERALELLERLGLP--PDILDKPVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDL 244
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
32-258 |
2.63e-35 |
|
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: 132.46 E-value: 2.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvtasarRRRELRATRMAMVFQEpm 111
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKT-TLLRLIA----GLERPDSGTILFGGEDA------TDVPVQERNVGFVFQH-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 TALNPVHRVGSQVD---EVLRLHRRMPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIVIAMALILEPKLLI 188
Cdd:cd03296 83 YALFRHMTVFDNVAfglRVKPRSERPPEAEIRAKVHELLKLVQL---DWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 189 ADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPS 258
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
32-281 |
3.71e-35 |
|
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: 135.16 E-value: 3.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIvtasarRRRELRATRMAMVFQEpm 111
Cdd:TIGR03265 18 TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLE-----RQTAGTIYQGGRDI------TRLPPQKRDYGIVFQS-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 TALNPVHRVGSQVDEVLRlHRRMPRAQRRAKVLEMFRSVHLPDVERiydAYPHQLSGGQRQRIVIAMALILEPKLLIADE 191
Cdd:TIGR03265 85 YALFPNLTVADNIAYGLK-NRGMGRAEVAERVAELLDLVGLPGSER---KYPGQLSGGQQQRVALARALATSPGLLLLDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 192 PTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVSSVPS 271
Cdd:TIGR03265 161 PLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEVNW 240
|
250
....*....|
gi 489912973 272 LvPTQREAPG 281
Cdd:TIGR03265 241 L-PGTRGGGS 249
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
16-244 |
4.09e-35 |
|
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: 131.29 E-value: 4.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVcGAGN---RVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvTASA 92
Cdd:TIGR02982 1 VISIRNLNHYY-GHGSlrkQVLFDINLEINPGEIVILTGPSGSGKT-TLLTLIG----GLRSVQEGSLKVLGQEL-HGAS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 93 RRRRELRATRMAMVFQ-----EPMTALNPVhRVGsqvdevLRLHRRMPRAQRRAKVLEMFRSVHLPDveRIyDAYPHQLS 167
Cdd:TIGR02982 74 KKQLVQLRRRIGYIFQahnllGFLTARQNV-QMA------LELQPNLSYQEARERARAMLEAVGLGD--HL-NYYPHNLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 168 GGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDfGVVAEIADRIVVMNRGDL 244
Cdd:TIGR02982 144 GGQKQRVAIARALVHHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
274-529 |
4.85e-35 |
|
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: 138.75 E-value: 4.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 274 PTQREAPGGEPVLRITGLGRTYAerrslfGATRTVVAAseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRML 353
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYP------GAGRPVLDG--LSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSIT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 354 LGETDIARLSGAGlrpLRRKVQIVFQDPYrslnprrAVGESIIEGLLnFGMPRA--QALVRAARTlgvVGLGPDVmRRYP 431
Cdd:COG4987 394 LGGVDLRDLDEDD---LRRRIAVVPQRPH-------LFDTTLRENLR-LARPDAtdEELWAALER---VGLGDWL-AALP 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 432 H-----------QFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELI-EQVRERTgvsVLFITHDLRVAAQ 499
Cdd:COG4987 459 DgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLlEALAGRT---VLLITHRLAGLER 535
|
250 260 270
....*....|....*....|....*....|
gi 489912973 500 VcDTIAVMQHGKVVETGAAQTVLTRPGHAY 529
Cdd:COG4987 536 M-DRILVLEDGRIVEQGTHEELLAQNGRYR 564
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
313-529 |
9.46e-35 |
|
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: 130.74 E-value: 9.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYRSLNprravg 392
Cdd:cd03249 21 GLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRSQIGLVSQEPVLFDG------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 393 eSIIEGLLnFGMPRAQA--LVRAARTLG----VVGLgPDvmrRY-----PH--QFSGGQRQRLCIARALVMDPEVLVADE 459
Cdd:cd03249 92 -TIAENIR-YGKPDATDeeVEEAAKKANihdfIMSL-PD---GYdtlvgERgsQLSGGQKQRIAIARALLRNPKILLLDE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 460 AVSALDVSVQAQVLELIEQVRE-RTgvsVLFITHDLRvAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAY 529
Cdd:cd03249 166 ATSALDAESEKLVQEALDRAMKgRT---TIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
302-525 |
1.03e-34 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 134.08 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGaTRTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAglrplRRKVQIVFQDp 381
Cdd:PRK11432 16 FG-SNTVI--DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-----QRDICMVFQS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 YrSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAV 461
Cdd:PRK11432 87 Y-ALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLA-GFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 462 SALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK11432 165 SNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
15-257 |
1.70e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 133.27 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVT--SLAvmgllpeGILEVSGGSARVLGEDiVTASA 92
Cdd:COG3839 2 ASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLlrMIA-------GLEDPTSGEILIGGRD-VTDLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 93 RRRRElratrMAMVFQEP-----MTalnpvhrvgsqvdeV-------LRLhRRMPRAQRRAKVLEMFRSVHLpdvERIYD 160
Cdd:COG3839 72 PKDRN-----IAMVFQSYalyphMT--------------VyeniafpLKL-RKVPKAEIDRRVREAAELLGL---EDLLD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 161 AYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFgvvAE---IADRIV 237
Cdd:COG3839 129 RKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQ---VEamtLADRIA 205
|
250 260
....*....|....*....|
gi 489912973 238 VMNRGDLTETGTRDEILARP 257
Cdd:COG3839 206 VMNDGRIQQVGTPEELYDRP 225
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
286-519 |
1.72e-34 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 130.52 E-value: 1.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRSLFgatrtvvaasEVDLTLRRGEILGIVGESGSGKSTVARcIVRLIE-PSAGrmllgETDIA---- 360
Cdd:PRK11124 3 IQLNGINCFYGAHQALF----------DITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLEmPRSG-----TLNIAgnhf 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 361 ----RLSGAGLRPLRRKVQIVFQDpYrSLNPRRAVGESIIEGLLN-FGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFS 435
Cdd:PRK11124 67 dfskTPSDKAIRELRRNVGMVFQQ-Y-NLWPHLTVQQNLIEAPCRvLGLSKDQALARAEKLLERLRLK-PYADRFPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 436 GGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRErTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVET 515
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKTASRVVYMENGHIVEQ 222
|
....
gi 489912973 516 GAAQ 519
Cdd:PRK11124 223 GDAS 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
28-250 |
2.12e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.40 E-value: 2.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 28 GAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLavMGLLPeGILEVSGGSARVLGEDIVTASARRrrelratrMA--- 104
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKS--TL--LKLLY-GEERPTSGQVLVNGQDLSRLKRRE--------IPylr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 105 ----MVFQEpmtalnpvHR------VGSQVDEVLRLHRrMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRI 174
Cdd:COG2884 79 rrigVVFQD--------FRllpdrtVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKA---KALPHELSGGEQQRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 175 VIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTR 250
Cdd:COG2884 147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEAR 221
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-256 |
2.30e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 2.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-PE-GILEVSGgsaRVLGEDIVTASAR 93
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlPEaGTITVGG---MVLSEETVWDVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 RrrelratrMAMVFQEPMTALnpvhrVGSQV--DEVLRLHRR-MPRAQRRAKVLEMFRSVHLPDverIYDAYPHQLSGGQ 170
Cdd:PRK13635 82 Q--------VGMVFQNPDNQF-----VGATVqdDVAFGLENIgVPREEMVERVDQALRQVGMED---FLNREPHRLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 171 RQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTETGTR 250
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTP 224
|
....*.
gi 489912973 251 DEILAR 256
Cdd:PRK13635 225 EEIFKS 230
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
284-493 |
2.57e-34 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 130.37 E-value: 2.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 284 PVLRITGLGRTYAerrslfGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLgetDIARLS 363
Cdd:COG4525 2 SMLTVRHVSVRYP------GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL---DGVPVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 364 GAGLRplrRKVqiVFQDpyRSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLC 443
Cdd:COG4525 73 GPGAD---RGV--VFQK--DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVG 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHD 493
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
283-523 |
2.71e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.82 E-value: 2.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERrslfgatrtvVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRmllgetdiARL 362
Cdd:COG1121 4 MPAIELENLTVSYGGR----------PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGT--------VRL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 SGAGLRPLRRKVQIVfqdPYRSLNPRRA---VGESIIEGLLN----FGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFS 435
Cdd:COG1121 66 FGKPPRRARRRIGYV---PQRAEVDWDFpitVRDVVLMGRYGrrglFRRPSRADREAVDEALERVGLE-DLADRPIGELS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 436 GGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGkVVET 515
Cdd:COG1121 142 GGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAH 219
|
....*...
gi 489912973 516 GAAQTVLT 523
Cdd:COG1121 220 GPPEEVLT 227
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
24-242 |
4.25e-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: 4.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 24 VSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSL-AVMGLLPEgilevSGGSARVLGEDIvtasarrrrELRATR 102
Cdd:cd03235 5 LTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKS-TLLkAILGLLKP-----TSGSIRVFGKPL---------EKERKR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 103 MAMVFQE-------PMTALNPVH--RVGSqvdevLRLHRRMPRAQRRaKVLEMFRSVHLPDVE--RIydaypHQLSGGQR 171
Cdd:cd03235 70 IGYVPQRrsidrdfPISVRDVVLmgLYGH-----KGLFRRLSKADKA-KVDEALERVGLSELAdrQI-----GELSGGQQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 172 QRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:cd03235 139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMT-ILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
17-257 |
7.63e-34 |
|
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: 128.32 E-value: 7.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTASARRRR 96
Cdd:cd03219 1 LEVRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKT-TLFNLIS----GFLRPTSGSVLFDGEDITGLPPHEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRatrMAMVFQEP-----MTALNPVhRVGSQVDE---VLRLHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSG 168
Cdd:cd03219 74 RLG---IGRTFQIPrlfpeLTVLENV-MVAAQARTgsgLLLARARREEREARERAEELLERVGLADLA---DRPAGELSY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGIT-VLLVEHDMDVVMSLADRVTVLDQGRVIAEG 225
|
....*....
gi 489912973 249 TRDEILARP 257
Cdd:cd03219 226 TPDEVRNNP 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
283-510 |
8.44e-34 |
|
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: 127.94 E-value: 8.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYaeRRSLFGATRtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLL----GETD 358
Cdd:COG4778 2 TTLLEVENLSKTF--TLHLQGGKR-LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 359 IARLSGAGLRPLRRKV-----QivFqdpyrsLN--PRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRYP 431
Cdd:COG4778 79 LAQASPREILALRRRTigyvsQ--F------LRviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLPP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 432 HQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHG 510
Cdd:COG4778 151 ATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
283-525 |
1.31e-33 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 128.55 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARL 362
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKG----------VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 SGAG----------LRPLRRKVQIVFQdpYRSLNPRRAVGESIIEGLLN-FGMPRAQALVRAARTLGVVGLGPDVMRRYP 431
Cdd:PRK10619 73 RDKDgqlkvadknqLRLLRTRLTMVFQ--HFNLWSHMTVLENVMEAPIQvLGLSKQEARERAVKYLAKVGIDERAQGKYP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 432 HQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGK 511
Cdd:PRK10619 151 VHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
250
....*....|....
gi 489912973 512 VVETGAAQTVLTRP 525
Cdd:PRK10619 230 IEEEGAPEQLFGNP 243
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
302-525 |
1.31e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 127.90 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATrTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIaRLSGAGLRPLRRKVQIVFQDP 381
Cdd:PRK09493 11 FGPT-QVL--HNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERLIRQEAGMVFQQF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 YrsLNPRRAVGESIIEGLLNF-GMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEA 460
Cdd:PRK09493 87 Y--LFPHLTALENVMFGPLRVrGASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 461 VSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
309-521 |
1.46e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 129.01 E-value: 1.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARlSGAGLRPLRRKVQIVFQDPYRSLNpR 388
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQYPEYQLF-E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMR-RYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVS 467
Cdd:PRK13637 99 ETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 468 VQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTV 521
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
302-515 |
1.80e-33 |
|
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: 124.85 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGAtrtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrplrrkvqivfqdp 381
Cdd:cd03216 10 FGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 yrslnprravgesiiegllnfgmpraqalVRAARTLGVvglgpdvmrRYPHQFSGGQRQRLCIARALVMDPEVLVADEAV 461
Cdd:cd03216 69 -----------------------------PRDARRAGI---------AMVYQLSVGERQMVEIARALARNARLLILDEPT 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 462 SALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVET 515
Cdd:cd03216 111 AALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
16-260 |
2.32e-33 |
|
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: 127.28 E-value: 2.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTASARRR 95
Cdd:COG4555 1 MIEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKT-TLLRMLA----GLLKPDSGSILIDGEDVRKEPREAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RElratrMAMVFQEP-----MTALnpvhrvgsqvdEVLRLH---RRMPRAQRRAKVLEMfrsVHLPDVERIYDAYPHQLS 167
Cdd:COG4555 74 RQ-----IGVLPDERglydrLTVR-----------ENIRYFaelYGLFDEELKKRIEEL---IELLGLEEFLDRRVGELS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 168 GGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDrHQTAVLFITHDFGVVAEIADRIVVMNRGDLTET 247
Cdd:COG4555 135 TGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKK-EGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQ 213
|
250
....*....|...
gi 489912973 248 GTRDEILARPSQN 260
Cdd:COG4555 214 GSLDELREEIGEE 226
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
28-327 |
5.06e-33 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 127.90 E-value: 5.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 28 GAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLpegiLEVSGGSARVLGEDIvtasarrrrelratrmamvf 107
Cdd:COG1125 12 PDGTVAVDDLSLTIPAGEFTVLVGPSGCGKT-TTLRMINRL----IEPTSGRILIDGEDI-------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 108 qepmTALNPV-----------------HR-VGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLpDVERIYDAYPHQLSGG 169
Cdd:COG1125 67 ----RDLDPVelrrrigyviqqiglfpHMtVAENIATVPRL-LGWDKERIRARVDELLELVGL-DPEEYRDRYPHELSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 170 QRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGT 249
Cdd:COG1125 141 QQQRVGVARALAADPPILLMDEPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 250 RDEILARPSQNYTRRLVSS-----VPSLVPTQREAPGGEPVLRITGLGRTYAERRSLFGATRTVVaaseVDltlRRGEIL 324
Cdd:COG1125 221 PEEILANPANDFVADFVGAdrglrRLSLLRVEDLMLPEPPTVSPDASLREALSLMLERGVDWLLV----VD---EDGRPL 293
|
...
gi 489912973 325 GIV 327
Cdd:COG1125 294 GWL 296
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
33-248 |
5.53e-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: 5.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDiVTASARRRRElratrMAMVFQEpmT 112
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLE-----EPTSGRIYIGGRD-VTDLPPKDRD-----IAMVFQN--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 113 ALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMfrsVHLPDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEP 192
Cdd:cd03301 82 ALYPHMTVYDNIAFGLKL-RKVPKDEIDERVREV---AELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 193 TTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
32-257 |
5.94e-33 |
|
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: 127.18 E-value: 5.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvTASARRRRELRATRMAMVFQEP- 110
Cdd:TIGR04521 19 KALDDVSLTIEDGEFVAIIGHTGSGKS-TLIQHLN----GLLKPTSGTVTIDGRDI-TAKKKKKLKDLRKKVGLVFQFPe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 111 -----MTALNPV----HRVGSQVDEvlrlhrrmprAQRRAKvlEMFRSVHLPdvERIYDAYPHQLSGGQRQRIVIAMALI 181
Cdd:TIGR04521 93 hqlfeETVYKDIafgpKNLGLSEEE----------AEERVK--EALELVGLD--EEYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 182 LEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
310-534 |
6.12e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 129.57 E-value: 6.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRRKVQIVFQDpyRSLNPRR 389
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-----PYQRPINMMFQS--YALFPHM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLR 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 470 AQV-LELIEqVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALI 534
Cdd:PRK11607 186 DRMqLEVVD-ILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
310-525 |
8.34e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 126.64 E-value: 8.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaGLRPLRRKVQIVFQDPYRSLnPRR 389
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKLVGIVFQNPETQF-VGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:PRK13644 94 TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 470 AQVLELIEQVRERtGVSVLFITHDLRvAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK13644 173 IAVLERIKKLHEK-GKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
284-525 |
1.03e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 128.91 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 284 PVLRITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS 363
Cdd:PRK09452 13 PLVELRGISKSFDGKEVI----------SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 364 gaglrPLRRKVQIVFQDpYrSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLC 443
Cdd:PRK09452 83 -----AENRHVNTVFQS-Y-ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLT 523
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
..
gi 489912973 524 RP 525
Cdd:PRK09452 235 EP 236
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
17-253 |
1.44e-32 |
|
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: 124.15 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTslavMGLLpEGILEVSGGSARVLGEDIVTASARRRR 96
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTT----LKML-TGELRPTSGTAYINGYSIRTDRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ElratrMAMVFQ-----EPMTALnpvhrvgsqvdEVLRLHRRM---PRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSG 168
Cdd:cd03263 76 S-----LGYCPQfdalfDELTVR-----------EHLRFYARLkglPKSEIKEEVELLLRVLGLTDKA---NKRARTLSG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELqdRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03263 137 GMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
....*
gi 489912973 249 TRDEI 253
Cdd:cd03263 215 SPQEL 219
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
33-272 |
1.58e-32 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 124.91 E-value: 1.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvtasarRRRELRATRMAMVFQEpmT 112
Cdd:TIGR00968 15 ALDDVNLEVPTGSLVALLGPSGSGKS-TLLRIIA----GLEQPDSGRIRLNGQDA------TRVHARDRKIGFVFQH--Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 113 ALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEP 192
Cdd:TIGR00968 82 ALFKHLTVRDNIAFGLEI-RKHPKAKIKARVEELLELVQL---EGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 193 TTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVSSVPSL 272
Cdd:TIGR00968 158 FGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
30-512 |
1.90e-32 |
|
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: 130.33 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGILEvsgGSARVLGEDIVTASARRRRELRatrMAMVFQE 109
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWD---GEIYWSGSPLKASNIRDTERAG---IVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 PMtaLNPVHRVGSQV---DEVLRLHRRM--PRAQRRAKvlEMFRSVHLPDverIYDAYP-HQLSGGQRQRIVIAMALILE 183
Cdd:TIGR02633 87 LT--LVPELSVAENIflgNEITLPGGRMayNAMYLRAK--NLLRELQLDA---DNVTRPvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 184 PKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLFITHDFGVVAEIADRIVVMNRGDltETGTRDEILARPSQNYTR 263
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ--HVATKDMSTMSEDDIITM 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 264 RLVSSVPSLVPTQREAPGGEpVLRITGLGRTYAERRSlfgatrtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVR 343
Cdd:TIGR02633 237 MVGREITSLYPHEPHEIGDV-ILEARNLTCWDVINPH-------RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 344 LIEPS-AGRMLLGETDIARLSGAglRPLRRKVQIVFQDPYR-SLNPRRAVGESIIEGLLNFGMPRAQalVRAARTLGVVG 421
Cdd:TIGR02633 309 AYPGKfEGNVFINGKPVDIRNPA--QAIRAGIAMVPEDRKRhGIVPILGVGKNITLSVLKSFCFKMR--IDAAAELQIIG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 422 LGPDVMR-RYPHQF------SGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDL 494
Cdd:TIGR02633 385 SAIQRLKvKTASPFlpigrlSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSEL 463
|
490
....*....|....*...
gi 489912973 495 RVAAQVCDTIAVMQHGKV 512
Cdd:TIGR02633 464 AEVLGLSDRVLVIGEGKL 481
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
32-246 |
2.12e-32 |
|
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: 124.00 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTASARRRRELRATRMAMVFQ--- 108
Cdd:TIGR02211 19 RVLKGVSLSIGKGEIVAIVGSSGSGKS-TLLHLLG----GLDNPTSGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQfhh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 --EPMTALNPVHRvgsqvdEVLRLHRRMPRAQRRAKvlEMFRSVHLPDveRIyDAYPHQLSGGQRQRIVIAMALILEPKL 186
Cdd:TIGR02211 94 llPDFTALENVAM------PLLIGKKSVKEAKERAY--EMLEKVGLEH--RI-NHRPSELSGGERQRVAIARALVNQPSL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 187 LIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGvVAEIADRIVVMNRGDLTE 246
Cdd:TIGR02211 163 VLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLE-LAKKLDRVLEMKDGQLFN 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
314-513 |
2.26e-32 |
|
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: 123.14 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARlsgaglRPLRRKVQIVFQDPYRSLNpRRAVGE 393
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRKSIGYVMQDVDYQLF-TDSVRE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLNfgMPRAQALVRAA-RTLGVVGLgpdvMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQV 472
Cdd:cd03226 92 ELLLGLKE--LDAGNEQAETVlKDLDLYAL----KERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489912973 473 LELIEQVrERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVV 513
Cdd:cd03226 166 GELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
49-319 |
2.26e-32 |
|
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: 126.84 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 49 VVGESGSGKSVtslaVMGLLPeGILEVSGGSARVLGEDIVtasarrRRELRATRMAMVFQEpmTALNPVHRVGSQVDEVL 128
Cdd:TIGR01187 1 LLGPSGCGKTT----LLRLLA-GFEQPDSGSIMLDGEDVT------NVPPHLRHINMVFQS--YALFPHMTVEENVAFGL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 129 RLhRRMPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALI 208
Cdd:TIGR01187 68 KM-RKVPRAEIKPRVLEALRLVQL---EEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLEL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 209 RELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVSSVPSLVPTQREApGGEPVLRI 288
Cdd:TIGR01187 144 KTIQEQLGITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVFEATVIER-KSEQVVLA 222
|
250 260 270
....*....|....*....|....*....|.
gi 489912973 289 TGLGRTYAERRSLfgatrTVVAASEVDLTLR 319
Cdd:TIGR01187 223 GVEGRRCDIYTDV-----PVEKDQPLHVVLR 248
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
313-525 |
2.78e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 125.71 E-value: 2.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRM-LLGETDIARLSGAGLRPLRRKVQIVFQDPYRSLNpRRAV 391
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTItIAGYHITPETGNKNLKKLRKKVSLVFQFPEAQLF-ENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 472 VLELIEQVrERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK13641 184 MMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
313-521 |
5.33e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.09 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETdiaRLSGAGLRPLRRKVQIVFQDPYRSLnprraVG 392
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEKLRKHIGIVFQNPDNQF-----VG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 393 eSIIE-----GLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVS 467
Cdd:PRK13648 99 -SIVKydvafGLENHAVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 468 VQAQVLELIEQVRERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTV 521
Cdd:PRK13648 177 ARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
310-522 |
1.12e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 124.08 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAG-LRPLRRKVQIVFQDPYRSLNpR 388
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIKPVRKKVGVVFQFPESQLF-E 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSV 468
Cdd:PRK13643 100 ETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 469 QAQVLELIEQVRErTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVL 522
Cdd:PRK13643 180 RIEMMQLFESIHQ-SGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
316-526 |
1.19e-31 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 129.84 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 316 LTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGaglRPLRRKVQIVFQDPyrsLNPRRAVGESI 395
Cdd:TIGR00958 502 FTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH---HYLHRQVALVGQEP---VLFSGSVRENI 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 396 IEGLLNFGMPRAQALVRAARTLGVVGLGPD----VMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAq 471
Cdd:TIGR00958 576 AYGLTDTPDEEIMAAAKAANAHDFIMEFPNgydtEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ- 654
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 472 vleLIEQVRERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLTRPG 526
Cdd:TIGR00958 655 ---LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
310-527 |
1.27e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 123.80 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIaRLSGAGLRPLRRKVQIVFQDPYRSLNpRR 389
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRESVGMVFQDPDNQLF-SA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPdvMRRYP-HQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSV 468
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH--LKDKPtHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 469 QAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG-------------AAQTVLTRPGH 527
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpkevfaekemlrKVNLRLPRIGH 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
313-524 |
1.40e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.30 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLgetDIARLSGAGLRPLRRKVQIVFQDPYRSLnprraVG 392
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII---DGDLLTEENVWDIRHKIGMVFQNPDNQF-----VG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 393 ESIIE----GLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSV 468
Cdd:PRK13650 97 ATVEDdvafGLENKGIPHEEMKERVNEALELVGM-QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 469 QAQVLELIEQVRERTGVSVLFITHDLRVAAqVCDTIAVMQHGKVVETGAAQTVLTR 524
Cdd:PRK13650 176 RLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
313-531 |
1.77e-31 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 121.57 E-value: 1.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYrslnprrAVG 392
Cdd:cd03251 20 DISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT---LASLRRQIGLVSQDVF-------LFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 393 ESIIEGLLnFGMPRA--QALVRAARTLGVVglgpDVMRRYPHQF-----------SGGQRQRLCIARALVMDPEVLVADE 459
Cdd:cd03251 90 DTVAENIA-YGRPGAtrEEVEEAARAANAH----EFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 460 AVSALDVSVQAQVLELIEQ-VRERTgvsVLFITHDLRVAAQVcDTIAVMQHGKVVETGAAQTVLTRPGhAYTR 531
Cdd:cd03251 165 ATSALDTESERLVQAALERlMKNRT---TFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQGG-VYAK 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
314-530 |
1.82e-31 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 122.33 E-value: 1.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIE--PSA---GRMLLGETDIARLSgagLRPLRRKVQIVFQDPyrSLNPR 388
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMD---VIELRRRVQMVFQIP--NPIPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIEGL-LN-FGMPRAQALVRAARTLGVVGLGPDVMRRY---PHQFSGGQRQRLCIARALVMDPEVLVADEAVSA 463
Cdd:PRK14247 97 LSIFENVALGLkLNrLVKSKKELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPTAN 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 464 LDVSVQAQVLELIEQVRERtgVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYT 530
Cdd:PRK14247 177 LDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
314-529 |
1.86e-31 |
|
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: 121.82 E-value: 1.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRplrRKVQIVFQDpyrSLNPRRAVGE 393
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLR---RQVGVVLQE---NVLFNRSIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIieGLLNFGMPRaQALVRAARTLGvvglGPDVMRRYPHQF-----------SGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:cd03252 95 NI--ALADPGMSM-ERVIEAAKLAG----AHDFISELPEGYdtivgeqgaglSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 463 ALDVSVQAQVLELIEQVRErtGVSVLFITHDLRvAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAY 529
Cdd:cd03252 168 ALDYESEHAIMRNMHDICA--GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENGLYA 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
17-255 |
2.44e-31 |
|
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: 121.00 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIvtaSARRRR 96
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP-----PRSGSIRFDGRDI---TGLPPH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQE-----PMTalnpvhrvgsqVDEVLRL----HRRMPRAQRRAKVLEMFrsvhlPDVERIYDAYPHQLS 167
Cdd:cd03224 71 ERARAGIGYVPEGrrifpELT-----------VEENLLLgayaRRRAKRKARLERVYELF-----PRLKERRKQLAGTLS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 168 GGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDLTET 247
Cdd:cd03224 135 GGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
....*...
gi 489912973 248 GTRDEILA 255
Cdd:cd03224 214 GTAAELLA 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
307-512 |
2.44e-31 |
|
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: 120.59 E-value: 2.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 307 TVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRKVQIVFQDpYRSLn 386
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD-FRLL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 PRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDV 466
Cdd:cd03292 91 PDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489912973 467 SVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:cd03292 170 DTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-239 |
2.49e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 122.28 E-value: 2.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVCGAGNR--VVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTASA 92
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPqpALQDVSLTIESGEFVVALGASGCGKT-TLLNLIA----GFLAPSSGEITLDGVPVTGPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 93 RRrrelratrmAMVFQEpmTALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVERiydAYPHQLSGGQRQ 172
Cdd:COG4525 77 DR---------GVVFQK--DALLPWLNVLDNVAFGLRL-RGVPKAERRARAEELLALVGLADFAR---RRIWQLSGGMRQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 173 RIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDfgvVAE---IADRIVVM 239
Cdd:COG4525 142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS---VEEalfLATRLVVM 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
17-253 |
2.51e-31 |
|
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: 121.52 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvTASARRRR 96
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKS-TLLRCLN----GLVEPTSGSVLIDGTDI-NKLKGKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEpmtaLNPVHRVgSQVDEVLrlhrrMPRAQRRAKVLEMFRSVHLPDVERIYDA--------YPHQ--- 165
Cdd:cd03256 74 RQLRRQIGMIFQQ----FNLIERL-SVLENVL-----SGRLGRRSTWRSLFGLFPKEEKQRALAAlervglldKAYQrad 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 -LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDL 244
Cdd:cd03256 144 qLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
....*....
gi 489912973 245 TETGTRDEI 253
Cdd:cd03256 224 VFDGPPAEL 232
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
17-242 |
3.07e-31 |
|
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: 119.02 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIvtasARRRR 96
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLY-----DPTSGEILIDGVDL----RDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEPMtalnpvhrvgsqvdevlrlhrrmpraqrrakvleMF-RSVHlpdvERIydayphqLSGGQRQRIV 175
Cdd:cd03228 72 ESLRKNIAYVPQDPF----------------------------------LFsGTIR----ENI-------LSGGQRQRIA 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 176 IAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqtAVLFITHDFGVVaEIADRIVVMNRG 242
Cdd:cd03228 107 IARALLRDPPILILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
14-269 |
3.12e-31 |
|
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: 121.86 E-value: 3.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 14 AAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGILEVSGGSARVLGEDIVTASAR 93
Cdd:TIGR02323 1 KPLLQVSGLSKSY--GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 RRRELRATRMAMVFQEPMTALNPVHRVGSQVDEvlrlhRRMPRAQR-----RAKVLEMFRSVHLpDVERIyDAYPHQLSG 168
Cdd:TIGR02323 79 ERRRLMRTEWGFVHQNPRDGLRMRVSAGANIGE-----RLMAIGARhygniRATAQDWLEEVEI-DPTRI-DDLPRAFSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:TIGR02323 152 GMQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESG 231
|
250 260
....*....|....*....|.
gi 489912973 249 TRDEILARPSQNYTRRLVSSV 269
Cdd:TIGR02323 232 LTDQVLDDPQHPYTQLLVSSI 252
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
309-516 |
5.20e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 121.73 E-value: 5.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGagLRPLRRKVQIVFQdpyrslNPR 388
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LWDIRNKAGMVFQ------NPD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIE-----GLLNFGMPRAQALVRAARTLGVVGLGPdvMRRY-PHQFSGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:PRK13633 96 NQIVATIVEedvafGPENLGIPPEEIRERVDESLKKVGMYE--YRRHaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 463 ALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVcDTIAVMQHGKVVETG 516
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEA-DRIIVMDSGKVVMEG 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
286-516 |
8.86e-31 |
|
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: 118.86 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGa 365
Cdd:cd03268 1 LKTNDLTKTYGKKRVL----------DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 glrPLRRKVQIVfqdPYRSLNPRRAVGESIIEGLLNFGMPRAqalvRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIA 445
Cdd:cd03268 70 ---ALRRIGALI---EAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIA 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 446 RALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRErTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03268 139 LALLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
315-516 |
9.56e-31 |
|
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: 119.13 E-value: 9.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 315 DLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRRKVQIVFQDpyRSLNPRRAVGES 394
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-----PADRPVSMLFQE--NNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 395 IIEGL---LNFGMPRAQALVRAARTLGVVGLgpdvMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:cd03298 91 VGLGLspgLKLTAEDRQAIEVALARVGLAGL----EKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489912973 472 VLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03298 167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
8-256 |
1.12e-30 |
|
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: 126.03 E-value: 1.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 8 PAGDTSAAVLAIRNLSVSVcGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDI 87
Cdd:COG4988 328 PLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKS-TLLNLLL----GFLPPYSGSILINGVDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 88 vtasARRRRELRATRMAMVFQEPmtALNPvhrvGSqVDEVLRLHR------RMPRAQRRAKVLEMFRSvhLPD-VERIYD 160
Cdd:COG4988 402 ----SDLDPASWRRQIAWVPQNP--YLFA----GT-IRENLRLGRpdasdeELEAALEAAGLDEFVAA--LPDgLDTPLG 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 161 AYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTaVLFITHDFGVVAEiADRIVVMN 240
Cdd:COG4988 469 EGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRT-VILITHRLALLAQ-ADRILVLD 545
|
250
....*....|....*.
gi 489912973 241 RGDLTETGTRDEILAR 256
Cdd:COG4988 546 DGRIVEQGTHEELLAK 561
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
19-245 |
1.15e-30 |
|
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: 118.51 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVcGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEgilevSGGSARVLGEDIvtasarrRREL 98
Cdd:cd03226 2 IENISFSY-KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE-----SSGSILLNGKPI-------KAKE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 99 RATRMAMVFQEPMTALnpvhrVGSQV-DEVLRLHRRMPRAQRRA-KVLEMFrsvhlpDVERIYDAYPHQLSGGQRQRIVI 176
Cdd:cd03226 69 RRKSIGYVMQDVDYQL-----FTDSVrEELLLGLKELDAGNEQAeTVLKDL------DLYALKERHPLSLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDLT 245
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
30-253 |
1.38e-30 |
|
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: 119.01 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIVtasarRRRELRATRMAMVFQE 109
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLK-----PTSGRATVAGHDVV-----REPREVRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 P-----MTALnpvhrvgsqvdEVLRLHRRM---PRAQRRAKVLEMFRSVHLPDV-ERIYDAYphqlSGGQRQRIVIAMAL 180
Cdd:cd03265 82 LsvddeLTGW-----------ENLYIHARLygvPGAERRERIDELLDFVGLLEAaDRLVKTY----SGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 181 ILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEI 253
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
11-258 |
1.96e-30 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 119.52 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 11 DTSAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLpegilEV-SGGSARVLGEDIVT 89
Cdd:COG4598 3 DTAPPALEVRDLHKSF--GDLEVLKGVSLTARKGDVISIIGSSGSGKS-TFLRCINLL-----ETpDSGEIRVGGEEIRL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 90 ASARRRRELRA---------TRMAMVFQE-----PMTALN-----PVHrvgsqvdeVLRlhrrMPRAQRRAKVLEMFRSV 150
Cdd:COG4598 75 KPDRDGELVPAdrrqlqrirTRLGMVFQSfnlwsHMTVLEnvieaPVH--------VLG----RPKAEAIERAEALLAKV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 151 HLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVA 230
Cdd:COG4598 143 GLADKR---DAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLV-VTHEMGFAR 218
|
250 260
....*....|....*....|....*...
gi 489912973 231 EIADRIVVMNRGDLTETGTRDEILARPS 258
Cdd:COG4598 219 DVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
33-257 |
2.02e-30 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 119.04 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEgileVSGGSARVLGEDIvtASARRRRELRATRMAMVFQE--- 109
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKS-TLLRCINKLEE----ITSGDLIVDGLKV--NDPKVDERLIRQEAGMVFQQfyl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 -P-MTALNPVHRVGSQVdevlrlhRRMPRAQRRAKVLEMFRSVHLPdvERIyDAYPHQLSGGQRQRIVIAMALILEPKLL 187
Cdd:PRK09493 89 fPhLTALENVMFGPLRV-------RGASKEEAEKQARELLAKVGLA--ERA-HHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 188 IADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVI-VTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNP 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
314-527 |
2.64e-30 |
|
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: 118.49 E-value: 2.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPyrslnprrAVGE 393
Cdd:cd03253 20 VSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLRRAIGVVPQDT--------VLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLNFGMPRA--QALVRAARTLGVvglgPDVMRRYPHQF-----------SGGQRQRLCIARALVMDPEVLVADEA 460
Cdd:cd03253 89 DTIGYNIRYGRPDAtdEEVIEAAKAAQI----HDKIMRFPDGYdtivgerglklSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 461 VSALDVSVQAQVLELIEQVreRTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLTRPGH 527
Cdd:cd03253 165 TSALDTHTEREIQAALRDV--SKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGGL 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
313-526 |
4.00e-30 |
|
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: 117.71 E-value: 4.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYrsLNPRravg 392
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLRSMIGVVLQDTF--LFSG---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 393 eSIIEGLLnFGMPRAQA--LVRAARTLGvvglGPDVMRRYP-----------HQFSGGQRQRLCIARALVMDPEVLVADE 459
Cdd:cd03254 92 -TIMENIR-LGRPNATDeeVIEAAKEAG----AHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 460 AVSALDVSVQAQVLELIEQVRE-RTgvsVLFITHDLRVAAQVcDTIAVMQHGKVVETGAAQTVLTRPG 526
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKgRT---SIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
32-258 |
4.07e-30 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 120.96 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvtasarRRRELRATRMAMVFQ--- 108
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKT-TLLRIIA----GLEHQTSGHIRFHGTDV------SRLHARDRKVGFVFQhya 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 --EPMTALNPVhrvgSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIVIAMALILEPKL 186
Cdd:PRK10851 85 lfRHMTVFDNI----AFGLTVLPRRERPNAAAIKAKVTQLLEMVQL---AHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 187 LIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPS 258
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPA 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
314-517 |
4.36e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.04 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGrmlLGETDIARLSGAGLRPLRRKVQIVFQDPYRSLnPRRAVGE 393
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEG---KVKIDGELLTAENVWNLRRKIGMVFQNPDNQF-VGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVL 473
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489912973 474 ELIEQVRERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGA 517
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAA 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
314-522 |
4.39e-30 |
|
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: 117.54 E-value: 4.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAglRPLRRKVQIVFQDpyRSLNPRRAVGE 393
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH--ERARAGIGYVPEG--RRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLNFGMPRAQALVRAartlgVVGLGPDVMRRYPH---QFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQA 470
Cdd:cd03224 95 NLLLGAYARRRAKRKARLER-----VYELFPRLKERRKQlagTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489912973 471 QVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVL 522
Cdd:cd03224 170 EIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
34-194 |
4.77e-30 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 115.05 E-value: 4.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 34 VRNLSLDVHAGETVCVVGESGSGKSvTSLAVMgllpEGILEVSGGSARVLGEDIvtasARRRRELRATRMAMVFQEPmtA 113
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKS-TLLKLI----AGLLSPTEGTILLDGQDL----TDDERKSLRKEIGYVFQDP--Q 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 114 LNPVHRVGSQVDEVLRLHRRMPRA--QRRAKVLEMFRSVHLPDveRIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADE 191
Cdd:pfam00005 70 LFPRLTVRENLRLGLLLKGLSKREkdARAEEALEKLGLGDLAD--RPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDE 147
|
...
gi 489912973 192 PTT 194
Cdd:pfam00005 148 PTA 150
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
286-519 |
4.90e-30 |
|
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: 117.22 E-value: 4.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAerrslfgaTRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARlsga 365
Cdd:cd03263 1 LQIRNLTKTYK--------KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRPLRRKVQIVFQDP--YRSLNPRRAVgesIIEGLLNfGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLC 443
Cdd:cd03263 69 DRKAARQSLGYCPQFDalFDELTVREHL---RFYARLK-GLPKSEIKEEVELLLRVLGLT-DKANKRARTLSGGMKRKLS 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTgvSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQ 519
Cdd:cd03263 144 LAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
11-254 |
5.89e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.55 E-value: 5.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 11 DTSAAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSlavmGLLpEGILEVSGGSARVLGEDIvta 90
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTIS----KIL-TGLLKPQSGEIKIDGITI--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 sARRRRELRATRMAMVFQepmtalNPVHR-VGSQVDEVLRL---HRRMPRAQRRAKVLEMFRSVhlpDVERIYDAYPHQL 166
Cdd:PRK13632 74 -SKENLKEIRKKIGIIFQ------NPDNQfIGATVEDDIAFgleNKKVPPKKMKDIIDDLAKKV---GMEDYLDKEPQNL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAeIADRIVVMNRGDLTE 246
Cdd:PRK13632 144 SGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIA 222
|
....*...
gi 489912973 247 TGTRDEIL 254
Cdd:PRK13632 223 QGKPKEIL 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
312-493 |
5.99e-30 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.81 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEP---SAGRMLLGETDIARLSgaglrPLRRKVQIVFQDPYrsLNPR 388
Cdd:COG4136 18 APLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALP-----AEQRRIGILFQDDL--LFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIEGLLNfGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSV 468
Cdd:COG4136 91 LSVGENLAFALPP-TIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
|
170 180
....*....|....*....|....*.
gi 489912973 469 QAQVLELI-EQVRERtGVSVLFITHD 493
Cdd:COG4136 169 RAQFREFVfEQIRQR-GIPALLVTHD 193
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
310-523 |
7.92e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 118.17 E-value: 7.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPyrslnPRR 389
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN---LKEIRKKIGIIFQNP-----DNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGES----IIEGLLNFGMPRA--QALVRAARTlgVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSA 463
Cdd:PRK13632 96 FIGATveddIAFGLENKKVPPKkmKDIIDDLAK--KVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 464 LDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLT 523
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
302-525 |
1.29e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 119.80 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATRTVvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAglrplRRKVQIVFQdp 381
Cdd:PRK10851 12 FGRTQVL---NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR-----DRKVGFVFQ-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 YRSLNPRRAVGESIIEGLLNfgMPRAQALVRAA------RTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVL 455
Cdd:PRK10851 82 HYALFRHMTVFDNIAFGLTV--LPRRERPNAAAikakvtQLLEMVQLA-HLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 456 VADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
286-497 |
1.43e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 117.11 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETdiaRLSGA 365
Cdd:PRK11248 2 LQISHLYADYGGKPAL----------EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGK---PVEGP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRplrRKVqiVFQDpyRSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIA 445
Cdd:PRK11248 69 GAE---RGV--VFQN--EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLE-GAEKRYIWQLSGGQRQRVGIA 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489912973 446 RALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVA 497
Cdd:PRK11248 141 RALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
16-512 |
1.65e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 122.08 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPE--GILEVSG--------GSARVLGe 85
Cdd:PRK15439 11 LLCARSISKQY--SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPdsGTLEIGGnpcarltpAKAHQLG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 86 divtasarrrrelratrMAMVFQEPMtaLNPVHRVGSQVdeVLRLHRRmPRAQRRAKVLEMFRSVHLPdveriYDAYPHQ 165
Cdd:PRK15439 88 -----------------IYLVPQEPL--LFPNLSVKENI--LFGLPKR-QASMQKMKQLLAALGCQLD-----LDSSAGS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDL- 244
Cdd:PRK15439 141 LEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIa 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 245 ----TETGTRDEILA---RPSQNY----TRRLVSSVPSLVPTQREapgGEPVLRITGLgrtyaerrslfgatrTVVAASE 313
Cdd:PRK15439 220 lsgkTADLSTDDIIQaitPAAREKslsaSQKLWLELPGNRRQQAA---GAPVLTVEDL---------------TGEGFRN 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS-----GAGL--RPLRRKVQIVFQDPYRSLN 386
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStaqrlARGLvyLPEDRQSSGLYLDAPLAWN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 PrravgESIIEGLLNFGMPRAQ---ALVRAARTLGVVGLGPDVMRRyphQFSGGQRQRLCIARALVMDPEVLVADEAVSA 463
Cdd:PRK15439 362 V-----CALTHNRRGFWIKPARenaVLERYRRALNIKFNHAEQAAR---TLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 489912973 464 LDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
313-512 |
2.55e-29 |
|
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: 114.96 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRRKVQIVFQDpyRSLNPRRAVG 392
Cdd:TIGR01277 16 EFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLFQE--NNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 393 ESIIEGL---LNFGMPRAQALVRAARTLGVvglgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:TIGR01277 89 QNIGLGLhpgLKLNAEQQEKVVDAAQQVGI----ADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489912973 470 AQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:TIGR01277 165 EEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
306-523 |
2.69e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.41 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 306 RTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGL---RP-LRRKVQIVFqdP 381
Cdd:PRK13548 15 RTLL--DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELarrRAvLPQHSSLSF--P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 YRslnprraVGESIIEGL--LNFGMPRAQALVRAArtLGVVGLGPDVMRRYPhQFSGGQRQRLCIARALV------MDPE 453
Cdd:PRK13548 91 FT-------VEEVVAMGRapHGLSRAEDDALVAAA--LAQVDLAHLAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 454 VLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLT 523
Cdd:PRK13548 161 WLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
31-251 |
3.05e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 115.88 E-value: 3.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 31 NRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLL--PE-GILEVSGGSArvlgeDIVTASARRRRELRATRMAMVF 107
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKS-SLLRVLNLLemPRsGTLNIAGNHF-----DFSKTPSDKAIRELRRNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 108 QE----P-MTALN-----PVHRVGsqvdevlrlhrrMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIA 177
Cdd:PRK11124 89 QQynlwPhLTVQQnlieaPCRVLG------------LSKDQALARAEKLLERLRLKPYA---DRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 178 MALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTETGTRD 251
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVI-VTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
31-258 |
4.06e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 118.28 E-value: 4.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 31 NRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGL-LPegilevSGGSARVLGEDiVTASARRRRElratrMAMVFQE 109
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLeKP------TEGQIFIDGED-VTHRSIQQRD-----ICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 pmTALNPVHRVGSQVDEVLRLHRRmPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPKLLIA 189
Cdd:PRK11432 87 --YALFPHMSLGENVGYGLKMLGV-PKEERKQRVKEALELVDLAGFE---DRYVDQISGGQQQRVALARALILKPKVLLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 190 DEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPS 258
Cdd:PRK11432 161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
16-253 |
5.14e-29 |
|
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: 115.09 E-value: 5.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVsVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMgllpEGILEVSGGSARVLGEDIvTASARRR 95
Cdd:TIGR02315 1 MLEVENLSK-VYPNGKQALKNINLNINPGEFVAIIGPSGAGKS-TLLRCI----NRLVEPSSGSILLEGTDI-TKLRGKK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRATRMAMVFQE-----PMTAL-NPVH-RVGSQvDEVLRLHRRMPRAQRRaKVLEMFRSVHLPDverIYDAYPHQLSG 168
Cdd:TIGR02315 74 LRKLRRRIGMIFQHynlieRLTVLeNVLHgRLGYK-PTWRSLLGRFSEEDKE-RALSALERVGLAD---KAYQRADQLSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
....*
gi 489912973 249 TRDEI 253
Cdd:TIGR02315 229 APSEL 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
310-525 |
5.43e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 116.05 E-value: 5.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRKVQIVFQDPYRSLnPRR 389
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVGIVFQNPDNQF-VGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:PRK13640 101 TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 470 AQVLELIEQVRERTGVSVLFITHDLRVAAQVcDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK13640 180 EQILKLIRKLKKKNNLTVISITHDIDEANMA-DQVLVLDDGKLLAQGSPVEIFSKV 234
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
314-517 |
5.44e-29 |
|
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: 114.51 E-value: 5.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLsgaGLRPLRRKVQIVFQDPY------RS-LN 386
Cdd:cd03244 23 ISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLRSRISIIPQDPVlfsgtiRSnLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 PRRAVGESIIEgllnfgmpraQALVRAA---RTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSA 463
Cdd:cd03244 100 PFGEYSDEELW----------QALERVGlkeFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATAS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 464 LDVSVQAQVLELIEqvRERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGA 517
Cdd:cd03244 170 VDPETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
283-521 |
5.52e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 120.12 E-value: 5.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTyaerrslFGAtrtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARL 362
Cdd:COG1129 2 EPLLEMRGISKS-------FGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 SGAglRPLRRKVQIVFQDPyrSLNPRRAVGESIIEG--LLNFGMPRAQALVRAAR----TLGVvGLGPDV-MRRYphqfS 435
Cdd:COG1129 72 SPR--DAQAAGIAIIHQEL--NLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARellaRLGL-DIDPDTpVGDL----S 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 436 GGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVET 515
Cdd:COG1129 143 VAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGT 221
|
....*.
gi 489912973 516 GAAQTV 521
Cdd:COG1129 222 GPVAEL 227
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
312-526 |
6.64e-29 |
|
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: 121.39 E-value: 6.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRplrRKVQIVFQDpyrSLNPRRAV 391
Cdd:TIGR01846 474 SNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLR---RQMGVVLQE---NVLFSRSI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIieGLLNFGMPRAQaLVRAARTLGVVglgpDVMRRYPHQF-----------SGGQRQRLCIARALVMDPEVLVADEA 460
Cdd:TIGR01846 548 RDNI--ALCNPGAPFEH-VIHAAKLAGAH----DFISELPQGYntevgekganlSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 461 VSALDVSVQAQVLE-LIEQVRERTgvsVLFITHDLRvAAQVCDTIAVMQHGKVVETGAAQTVLTRPG 526
Cdd:TIGR01846 621 TSALDYESEALIMRnMREICRGRT---VIIIAHRLS-TVRACDRIIVLEKGQIAESGRHEELLALQG 683
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
297-521 |
7.91e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 115.61 E-value: 7.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 297 ERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS-GAGLRPLRRKVQ 375
Cdd:PRK13649 19 EGRALFD----------VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQIRKKVG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 376 IVFQDPYRSLNpRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVL 455
Cdd:PRK13649 89 LVFQFPESQLF-EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 456 VADEAVSALDVSVQAQVLELIEQVRErTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTV 521
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLFKKLHQ-SGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-282 |
1.09e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 117.83 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 34 VRNLSLDVHAGETVCVVGESGSGKSVtslavMGLLPEGILEVSGGSARVLGEDIVTASARRRRELRATRMAMVFQEpmTA 113
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKST-----MVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQS--FA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 114 LNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPT 193
Cdd:PRK10070 117 LMPHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGL---ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 194 TALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRL-----VSS 268
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFfrgvdISQ 272
|
250
....*....|....
gi 489912973 269 VPSLVPTQREAPGG 282
Cdd:PRK10070 273 VFSAKDIARRTPNG 286
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
32-514 |
1.16e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 119.50 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSvtslAVMGLLpEGILEVSGGSARVLGEDIvtaSARRRRELRATRMAMVFQEpM 111
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKS----TLMKVL-SGIHEPTKGTITINNINY---NKLDHKLAAQLGIGIIYQE-L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 TALNPVhrvgsQVDEVLRLHRRMPR----------AQRRAKVLEMFRSVhlpDVERIYDAYPHQLSGGQRQRIVIAMALI 181
Cdd:PRK09700 90 SVIDEL-----TVLENLYIGRHLTKkvcgvniidwREMRVRAAMMLLRV---GLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 182 LEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG-----TRDEILar 256
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGmvsdvSNDDIV-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 257 pSQNYTRRLVSSVPSLVPTQReapggepvlriTGLGRTYAERRSLFGATRTVVaaSEVDLTLRRGEILGIVGESGSGKST 336
Cdd:PRK09700 239 -RLMVGRELQNRFNAMKENVS-----------NLAHETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTE 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 337 VARCIVRlIEPSAGrmllGETdiaRLSGAGLRPlrrkvqivfQDPYRSLNPRRA-VGESIIE-GLL-NFGMPRAQALVRA 413
Cdd:PRK09700 305 LMNCLFG-VDKRAG----GEI---RLNGKDISP---------RSPLDAVKKGMAyITESRRDnGFFpNFSIAQNMAISRS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 414 ---ARTLGVVGLGPDVM-RRYPHQ------------------FSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:PRK09700 368 lkdGGYKGAMGLFHEVDeQRTAENqrellalkchsvnqniteLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAE 447
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 489912973 472 VLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVE 514
Cdd:PRK09700 448 IYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-259 |
1.60e-28 |
|
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: 119.49 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 4 APYPPAGDTSAAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVmgLLpeGILEVSGGSARVL 83
Cdd:COG4987 321 EPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKS-TLLAL--LL--RFLDPQSGSITLG 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 84 GEDIvtasARRRRELRATRMAMVFQEPmtalnpvHRVGSQVDEVLRLHR------RMPRAQRRAKVLEMFRSvhLPD-VE 156
Cdd:COG4987 396 GVDL----RDLDEDDLRRRIAVVPQRP-------HLFDTTLRENLRLARpdatdeELWAALERVGLGDWLAA--LPDgLD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 157 RIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRE-LQDRhqtAVLFITHDFgVVAEIADR 235
Cdd:COG4987 463 TWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGR---TVLLITHRL-AGLERMDR 538
|
250 260
....*....|....*....|....
gi 489912973 236 IVVMNRGDLTETGTRDEILARPSQ 259
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELLAQNGR 562
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
312-529 |
1.99e-28 |
|
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: 120.23 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYrslnprrAV 391
Cdd:TIGR01193 491 SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLRQFINYLPQEPY-------IF 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIIEGLLNFGMPRA--QALVRAARTLGV--------VGLGPDvMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAV 461
Cdd:TIGR01193 561 SGSILENLLLGAKENVsqDEIWAACEIAEIkddienmpLGYQTE-LSEEGSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 462 SALDVSVQAQVLELIEQVRERTgvsVLFITHDLRVAAQVcDTIAVMQHGKVVETGAAQTVLTRPGHAY 529
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDKT---IIFVAHRLSVAKQS-DKIIVLDHGKIIEQGSHDELLDRNGFYA 703
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
286-516 |
2.03e-28 |
|
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: 112.85 E-value: 2.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRslfgatRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARlsga 365
Cdd:cd03266 2 ITADALTKRFRDVK------KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 glRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRYpHQFSGGQRQRLCIA 445
Cdd:cd03266 72 --EPAEARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRV-GGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 446 RALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRErTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA-LGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
14-257 |
2.50e-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: 112.77 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 14 AAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIvtasar 93
Cdd:COG0410 1 MPMLEVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLP-----PRSGSIRFDGEDI------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 rrrelratrmamvfqepmTALNPVHRV---------GSQ------VDEVLRLHRRMPRAQRRAKvlemfrsvhlPDVERI 158
Cdd:COG0410 68 ------------------TGLPPHRIArlgigyvpeGRRifpsltVEENLLLGAYARRDRAEVR----------ADLERV 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 159 YDAYPH----------QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGV 228
Cdd:COG0410 120 YELFPRlkerrrqragTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARF 198
|
250 260
....*....|....*....|....*....
gi 489912973 229 VAEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:COG0410 199 ALEIADRAYVLERGRIVLEGTAAELLADP 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
17-256 |
2.54e-28 |
|
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: 119.55 E-value: 2.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLA--VMGLLpegilEVSGGSARVLGEDIvtasARR 94
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKS--TLLklLLGLY-----EPTSGRILIDGIDL----RQI 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 RRELRATRMAMVFQEPM----TalnpvhrvgsqVDEVLRLHRRMPRAQRRAKVLEMFrSVHlPDVERIYDAYPHQ----- 165
Cdd:COG2274 543 DPASLRRQIGVVLQDVFlfsgT-----------IRENITLGDPDATDEEIIEAARLA-GLH-DFIEALPMGYDTVvgegg 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 --LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELqdRHQTAVLFITHDFGVVAeIADRIVVMNRGD 243
Cdd:COG2274 610 snLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIR-LADRIIVLDKGR 686
|
250
....*....|...
gi 489912973 244 LTETGTRDEILAR 256
Cdd:COG2274 687 IVEDGTHEELLAR 699
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
30-267 |
4.36e-28 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 112.92 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEGilevSGGSARVLGEDIVTASARRRRELRATRM----AM 105
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKT-TLLRCINLLEQP----EAGTIRVGDITIDTARSLSQQKGLIRQLrqhvGF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 106 VFQEpmTALNPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPK 185
Cdd:PRK11264 90 VFQN--FNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 186 LLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRL 265
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVI-VTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQF 243
|
..
gi 489912973 266 VS 267
Cdd:PRK11264 244 LE 245
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
309-525 |
6.46e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.86 E-value: 6.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIaRLSGAGLRPLRRKVQIVFQDPYRSL-NP 387
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKTVGIVFQNPDDQLfAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 388 RraVGESIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVS 467
Cdd:PRK13639 95 T--VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 468 VQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-242 |
7.14e-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: 109.44 E-value: 7.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTslaVMGLLpEGILEVSGGSARVLGEDIvtasarrrr 96
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKS-T---LMKIL-SGLYKPDSGEILVDGKEV--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 elratrmamvfqepmtalnpvhrvgsqvdevlrlHRRMPRAQRRAKVlEMFrsvhlpdveriydaypHQLSGGQRQRIVI 176
Cdd:cd03216 65 ----------------------------------SFASPRDARRAGI-AMV----------------YQLSVGERQMVEI 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQG-VAVIFISHRLDEVFEIADRVTVLRDG 158
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
36-244 |
7.58e-28 |
|
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: 110.85 E-value: 7.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 36 NLSLDVhAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTASARRRRELRATRMAMVFQEpmTALN 115
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKS-TLLRCIA----GLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQ--YALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 116 PVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFrsvhlpDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTA 195
Cdd:cd03297 88 PHLNVRENLAFGLKRKRNREDRISVDELLDLL------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489912973 196 LDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDL 244
Cdd:cd03297 162 LDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
36-253 |
9.09e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 112.83 E-value: 9.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 36 NLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIvtASARRRRELRATRMAMVFQEPM---- 111
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLL-----KPTSGKIIIDGVDI--TDKKVKLSDIRKKVGLVFQYPEyqlf 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 -------TALNPVhRVGSQVDEVLRlhrrmpraqrraKVLEMFRSVHLpDVERIYDAYPHQLSGGQRQRIVIAMALILEP 184
Cdd:PRK13637 98 eetiekdIAFGPI-NLGLSEEEIEN------------RVKRAMNIVGL-DYEDYKDKSPFELSGGQKRRVAIAGVVAMEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 185 KLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEI 253
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
306-531 |
1.07e-27 |
|
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: 117.12 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 306 RTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPY--- 382
Cdd:TIGR02203 343 RDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQVALVSQDVVlfn 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 383 RSLNPRRAVGEsiiegLLNFGMPRAQALVRAARTLGVVGLGPD----VMRRYPHQFSGGQRQRLCIARALVMDPEVLVAD 458
Cdd:TIGR02203 420 DTIANNIAYGR-----TEQADRAEIERALAAAYAQDFVDKLPLgldtPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 459 EAVSALDVSVQAQVLELIEQV-RERTGvsvLFITHDLRvAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHaYTR 531
Cdd:TIGR02203 495 EATSALDNESERLVQAALERLmQGRTT---LVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLARNGL-YAQ 563
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
314-513 |
1.31e-27 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 110.73 E-value: 1.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRKVQIVFQDPYRSLNprRAVGE 393
Cdd:PRK10908 21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIGMIFQDHHLLMD--RTVYD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVL 473
Cdd:PRK10908 99 NVAIPLIIAGASGDDIRRRVSAALDKVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGIL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 489912973 474 ELIEQVrERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVV 513
Cdd:PRK10908 178 RLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
15-225 |
1.47e-27 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 109.88 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSvsvCGAGNRVV-RNLSLDVHAGETVCVVGESGSGKsvTSL--AVMGLLPegileVSGGSARVLGEDIvtas 91
Cdd:COG4133 1 MMLEAENLS---CRRGERLLfSGLSFTLAAGEALALTGPNGSGK--TTLlrILAGLLP-----PSAGEVLWNGEPI---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 92 aRRRRELRATRMAMVFQEP-----MTALnpvhrvgsqvdEVLRLHRRM-PRAQRRAKVLEMFRSVHLPDVEriyDAYPHQ 165
Cdd:COG4133 67 -RDAREDYRRRLAYLGHADglkpeLTVR-----------ENLRFWAALyGLRADREAIDEALEAVGLAGLA---DLPVRQ 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHD 225
Cdd:COG4133 132 LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
282-525 |
1.50e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 113.02 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 282 GEPVLRITGLGRTYAERRSlfgatRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGE----- 356
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQE-----NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 357 -TDIARLSGAGL-------RPLRRKVQIVFQDPYRSLNpRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMR 428
Cdd:PRK13631 93 kKNNHELITNPYskkiknfKELRRRVSMVFQFPEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYLE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 429 RYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVReRTGVSVLFITHDLRVAAQVCDTIAVMQ 508
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTMEHVLEVADEVIVMD 250
|
250
....*....|....*..
gi 489912973 509 HGKVVETGAAQTVLTRP 525
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQ 267
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
309-512 |
1.71e-27 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 109.93 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRmllgetdiARLSGAGLRPLRRKVQIVFQdpYRSLNPR 388
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGS--------IRVFGKPLEKERKRIGYVPQ--RRSIDRD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 R--AVGESIIEGLLN----FGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:cd03235 83 FpiSVRDVVLMGLYGhkglFRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489912973 463 ALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:cd03235 162 GVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
33-258 |
2.83e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.43 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-----PEGILEVSGGSarvLGEDIVTASARRrrelratrMAMVF 107
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddnPNSKITVDGIT---LTAKTVWDIREK--------VGIVF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 108 QEPMTALnpvhrVGSQV-DEV---LRlHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILE 183
Cdd:PRK13640 91 QNPDNQF-----VGATVgDDVafgLE-NRAVPRPEMIKIVRDVLADVGMLDYI---DSEPANLSGGQKQRVAIAGILAVE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 184 PKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGvVAEIADRIVVMNRGDLTETGTRDEILARPS 258
Cdd:PRK13640 162 PKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
284-497 |
3.12e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 109.91 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 284 PVLRITGLGRTYAErrslfGATRTVVAaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS 363
Cdd:PRK11629 4 ILLQCDNLCKRYQE-----GSVQTDVL-HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 364 GAGLRPLR-RKVQIVFQdpYRSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRyPHQFSGGQRQRL 442
Cdd:PRK11629 78 SAAKAELRnQKLGFIYQ--FHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHR-PSELSGGERQRV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 443 CIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVA 497
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
310-525 |
3.24e-27 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 110.46 E-value: 3.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRplRRKVQIVFQDP--YRSLN- 386
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA--RMGVVRTFQHVrlFREMTv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 -------PRRAVGESIIEGLLN---FGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLV 456
Cdd:PRK11300 98 ienllvaQHQQLKTGLFSGLLKtpaFRRAESEALDRAATWLERVGLL-EHANRQAGNLAYGQQRRLEIARCMVTQPEILM 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 457 ADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK11300 177 LDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-256 |
3.82e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 111.72 E-value: 3.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMgllpEGILEVSGGSARVLGedivtasarrrrelratrmamvfqepm 111
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKS-TTIKML----TGILVPTSGEVRVLG--------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 taLNP-------VHRVG------SQ------VDEVLRLHRRM---PRAQRRAKVLEMfrsVHLPDVERIYDAYPHQLSGG 169
Cdd:COG4586 84 --YVPfkrrkefARRIGvvfgqrSQlwwdlpAIDSFRLLKAIyriPDAEYKKRLDEL---VELLDLGELLDTPVRQLSLG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 170 QRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGT 249
Cdd:COG4586 159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
....*..
gi 489912973 250 RDEILAR 256
Cdd:COG4586 239 LEELKER 245
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
29-249 |
3.83e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 109.72 E-value: 3.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 29 AGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLL--PE-GILEVSGGSArvlgeDIVTASARRRRELRATRMAM 105
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLetPDsGQLNIAGHQF-----DFSQKPSEKAIRLLRQKVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 106 VFQE----P-MTALN-----PVHRVGsqvdevlrlhrrMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIV 175
Cdd:COG4161 87 VFQQynlwPhLTVMEnlieaPCKVLG------------LSKEQAREKAMKLLARLRLTDKA---DRFPLHLSGGQQQRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 176 IAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTETGT 249
Cdd:COG4161 152 IARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVI-VTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
314-516 |
4.09e-27 |
|
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: 109.22 E-value: 4.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDP---YRSLNprra 390
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRRNIGYVPQDVtlfYGTLR---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 391 vgESIiegllNFGMPRA--QALVRAARTLGVVglgpDVMRRYPHQF-----------SGGQRQRLCIARALVMDPEVLVA 457
Cdd:cd03245 96 --DNI-----TLGAPLAddERILRAAELAGVT----DFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 458 DEAVSALDVSVQAQVLELIEQV-RERTgvsVLFITHDLRVaAQVCDTIAVMQHGKVVETG 516
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLlGDKT---LIIITHRPSL-LDLVDRIIVMDSGRIVADG 220
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
33-242 |
4.57e-27 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 109.06 E-value: 4.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSvtSLAVM---GLLPegilevSGGSARVLGE----DIVTASARRRRELRATRMAM 105
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKS--TLLKCiygNYLP------DSGSILVRHDggwvDLAQASPREILALRRRTIGY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 106 VFQepmtALNPVHRVgSQVDEVLR--LHRRMPRAQRRAKVLEMFRSVHLPdvERIYDAYPHQLSGGQRQRIVIAMALILE 183
Cdd:COG4778 98 VSQ----FLRVIPRV-SALDVVAEplLERGVDREEARARARELLARLNLP--ERLWDLPPATFSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 184 PKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
273-527 |
6.48e-27 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.06 E-value: 6.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 273 VPTQREAPGGEPVLRITGLGR------TYAERRSlfgatrtvvAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIE 346
Cdd:PRK13657 316 VPDVRDPPGAIDLGRVKGAVEfddvsfSYDNSRQ---------GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 347 PSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPY---RSLNPRRAVG-ESIIEGLLNFGMPRAQALVRAARTLGvvGL 422
Cdd:PRK13657 387 PQSGRILIDGTDIRTVT---RASLRRNIAVVFQDAGlfnRSIEDNIRVGrPDATDEEMRAAAERAQAHDFIERKPD--GY 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 423 GPDVMRRyPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRErtGVSVLFITHDLRVAAQVcD 502
Cdd:PRK13657 462 DTVVGER-GRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNA-D 537
|
250 260
....*....|....*....|....*
gi 489912973 503 TIAVMQHGKVVETGAAQTVLTRPGH 527
Cdd:PRK13657 538 RILVFDNGRVVESGSFDELVARGGR 562
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
303-524 |
8.15e-27 |
|
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: 114.46 E-value: 8.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 303 GATRTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLsgaglrplrrkvqivfqdpy 382
Cdd:COG4618 342 GSKRPIL--RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW-------------------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 383 rslnPRRAVGESI------IEgLLN---------FGMPRAQALVRAARTLGVvglgPDVMRRYP-----------HQFSG 436
Cdd:COG4618 400 ----DREELGRHIgylpqdVE-LFDgtiaeniarFGDADPEKVVAAAKLAGV----HEMILRLPdgydtrigeggARLSG 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 437 GQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRvAAQVCDTIAVMQHGKVVETG 516
Cdd:COG4618 471 GQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS-LLAAVDKLLVLRDGRVQAFG 548
|
....*...
gi 489912973 517 AAQTVLTR 524
Cdd:COG4618 549 PRDEVLAR 556
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
314-516 |
9.56e-27 |
|
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: 107.50 E-value: 9.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIarlSGAGLRPLRRKVQIVFQDPYrslnprrAVGE 393
Cdd:cd03369 27 VSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSSLTIIPQDPT-------LFSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLNFGMPRAQALVRAartLGVVGLGPDvmrryphqFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVL 473
Cdd:cd03369 97 TIRSNLDPFDEYSDEEIYGA---LRVSEGGLN--------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489912973 474 ELIEQvrERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETG 516
Cdd:cd03369 166 KTIRE--EFTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
270-531 |
9.83e-27 |
|
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: 114.66 E-value: 9.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 270 PSLVPTQREAPGGEPVLRITGlgrtYAERRSL-FGATRTVVAASE-VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEP 347
Cdd:TIGR03796 456 PLLEEPEGSAATSEPPRRLSG----YVELRNItFGYSPLEPPLIEnFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQP 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 348 SAGRMLL-GET--DIARlsgaglRPLRRKVQIVFQDPyrslnprravgeSIIEG-------LLNFGMPRAqALVRAARTL 417
Cdd:TIGR03796 532 WSGEILFdGIPreEIPR------EVLANSVAMVDQDI------------FLFEGtvrdnltLWDPTIPDA-DLVRACKDA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 418 GVVGlgpDVMRR---YPHQ-------FSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIeqvRERtGVSV 487
Cdd:TIGR03796 593 AIHD---VITSRpggYDAElaegganLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL---RRR-GCTC 665
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489912973 488 LFITHDLRvAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHaYTR 531
Cdd:TIGR03796 666 IIVAHRLS-TIRDCDEIIVLERGKVVQRGTHEELWAVGGA-YAR 707
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
19-299 |
9.87e-27 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 111.62 E-value: 9.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-PEGILevsgGSARVLGEDIVtasarrRRE 97
Cdd:TIGR03258 6 IRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVkAAGLT----GRIAIADRDLT------HAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 98 LRATRMAMVFQEpmTALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVERiydAYPHQLSGGQRQRIVIA 177
Cdd:TIGR03258 76 PHKRGLALLFQN--YALFPHLKVEDNVAFGLRA-QKMPKADIAERVADALKLVGLGDAAA---HLPAQLSGGMQQRIAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 178 MALILEPKLLIADEPTTALDVTTQKQILALIRELQDR-HQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILAR 256
Cdd:TIGR03258 150 RAIAIEPDVLLLDEPLSALDANIRANMREEIAALHEElPELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 489912973 257 PSQNYTRRLVSS---VPSLVPTQREAPGGEPVLRITGLGRTYAERR 299
Cdd:TIGR03258 230 PADGFAAEFLGAaniLPAIALGITEAPGLVDVSCGGAVIFAFGDGR 275
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
284-493 |
1.01e-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: 107.56 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 284 PVLRITGLGRTYAERRsLFgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARls 363
Cdd:COG4133 1 MMLEAENLSCRRGERL-LF---------SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 364 gaglRPLRRKVQIVFQDPYRSLNPRRAVGEsiiegLLNF-----GMPRAQALVRAArtLGVVGLGPdVMRRYPHQFSGGQ 438
Cdd:COG4133 69 ----AREDYRRRLAYLGHADGLKPELTVRE-----NLRFwaalyGLRADREAIDEA--LEAVGLAG-LADLPVRQLSAGQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 439 RQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHD 493
Cdd:COG4133 137 KRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
17-256 |
1.07e-26 |
|
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: 108.47 E-value: 1.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtslAVMGLLPEgILEVSGGSARVLGEDIvtasARRRR 96
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKS----TLVNLIPR-FYDVDSGRILIDGHDV----RDYTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEpmtalnpVHRVGSQVDEVLRLHRrmPRAQrRAKVLEMFRSVHLPD-VERIYDAYPH-------QLSG 168
Cdd:cd03251 72 ASLRRQIGLVSQD-------VFLFNDTVAENIAYGR--PGAT-REEVEEAARAANAHEfIMELPEGYDTvigergvKLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTAvLFITHDFGVVaEIADRIVVMNRGDLTETG 248
Cdd:cd03251 142 GQRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTT-FVIAHRLSTI-ENADRIVVLEDGKIVERG 218
|
....*...
gi 489912973 249 TRDEILAR 256
Cdd:cd03251 219 THEELLAQ 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
16-266 |
1.18e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.58 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvtasarRR 95
Cdd:PRK09452 14 LVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKT-TVLRLIA----GFETPDSGRIMLDGQDI------TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRATRMAMVFQEpmTALNPVHRVGSQVDEVLRLHRRmPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIV 175
Cdd:PRK09452 81 VPAENRHVNTVFQS--YALFPHMTVFENVAFGLRMQKT-PAAEITPRVMEALRMVQL---EEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 176 IAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILA 255
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYE 234
|
250
....*....|.
gi 489912973 256 RPSQNYTRRLV 266
Cdd:PRK09452 235 EPKNLFVARFI 245
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
302-525 |
1.25e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.86 E-value: 1.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATRTVvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGaglRPLRRKVQIVFQDP 381
Cdd:PRK09536 13 FGDTTVL---DGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA---RAASRRVASVPQDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 YRSLNPRravGESIIE-------GLLNFGMPRAQALVRAARTLGVVGLGPDvmrRYPHQFSGGQRQRLCIARALVMDPEV 454
Cdd:PRK09536 87 SLSFEFD---VRQVVEmgrtphrSRFDTWTETDRAAVERAMERTGVAQFAD---RPVTSLSGGERQRVLLARALAQATPV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 455 LVADEAVSALDVSVQAQVLELIEQVRErTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-269 |
1.29e-26 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 111.47 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 5 PYPPAGDTSAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLG 84
Cdd:PRK11607 8 PQAKTRKALTPLLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKS-TLLRMLA----GFEQPTAGQIMLDG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 85 EDIvtasarRRRELRATRMAMVFQEpmTALNPVHRVGSQVDEVLRlHRRMPRAQRRAKVLEMFRSVHLPDVERiydAYPH 164
Cdd:PRK11607 81 VDL------SHVPPYQRPINMMFQS--YALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAK---RKPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDL 244
Cdd:PRK11607 149 QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKF 228
|
250 260
....*....|....*....|....*
gi 489912973 245 TETGTRDEILARPSQNYTRRLVSSV 269
Cdd:PRK11607 229 VQIGEPEEIYEHPTTRYSAEFIGSV 253
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
314-539 |
1.51e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 108.39 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETdiaRLSGAGLRP-------LRRKVQIVFQdpYRSLN 386
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEV---RLFGRNIYSpdvdpieVRREVGMVFQ--YPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 PRRAVGESIIEGLLNFGMPRAQALV--RAARTLGVVGLGPDVMRR---YPHQFSGGQRQRLCIARALVMDPEVLVADEAV 461
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVKSKKELdeRVEWALKKAALWDEVKDRlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 462 SALDVSVQAQVLELIEQVRERtgVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDAAPG 539
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGALG 253
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
303-512 |
1.70e-26 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 105.76 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 303 GATRTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLsgaGLRPLRRKVQIVFQDPy 382
Cdd:cd03246 12 GAEPPVL--RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW---DPNELGDHVGYLPQDD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 383 rslnprRAVGESIIEGLLnfgmpraqalvraartlgvvglgpdvmrryphqfSGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:cd03246 86 ------ELFSGSIAENIL----------------------------------SGGQRQRLGLARALYGNPRILVLDEPNS 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489912973 463 ALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQvCDTIAVMQHGKV 512
Cdd:cd03246 126 HLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
28-256 |
1.82e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.34 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 28 GAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTslaVMGLLPeGILEVSGGSARVLGEDIvtasARRRRELRATRMAMVF 107
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKS-T---LVNLLL-RFYDPTSGRILIDGVDI----RDLTLESLRRQIGVVP 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 108 QEP----MTALNPVhRVGSQ---VDEVLRlhrrmprAQRRAKVLEMFRSvhLPDVeriYDAY----PHQLSGGQRQRIVI 176
Cdd:COG1132 421 QDTflfsGTIRENI-RYGRPdatDEEVEE-------AAKAAQAHEFIEA--LPDG---YDTVvgerGVNLSGGQRQRIAI 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELqdRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEILAR 256
Cdd:COG1132 488 ARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELLAR 564
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
14-244 |
1.87e-26 |
|
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: 105.98 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 14 AAVLAIRNLSVSvcgagnRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIvtasar 93
Cdd:cd03215 2 EPVLEVRGLSVK------GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRP-----PASGEITLDGKPV------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 rrrelratrmamvfqepmtalnpvhrvgsqvdevlrlHRRMPRAQRRAKVlemfrsVHLPDvER----------IYD--A 161
Cdd:cd03215 65 -------------------------------------TRRSPRDAIRAGI------AYVPE-DRkreglvldlsVAEniA 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 162 YPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNR 241
Cdd:cd03215 101 LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYE 179
|
...
gi 489912973 242 GDL 244
Cdd:cd03215 180 GRI 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
297-525 |
1.98e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 108.74 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 297 ERRSLFGATRTVVAASE-VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARlsgAGLRPLRRKVQ 375
Cdd:PRK13652 5 ETRDLCYSYSGSKEALNnINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 376 IVFQDPYRSL-NPrrAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEV 454
Cdd:PRK13652 82 LVFQNPDDQIfSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 455 LVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
283-525 |
2.15e-26 |
|
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: 107.38 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARL 362
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHG----------VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 S-------GAGLRPLRRKVqivfqdpYRSLnprravgeSIIEGLLnFGMPRAQALVRAARTLgvvglgPDVMRRYP---- 431
Cdd:COG0410 71 PphriarlGIGYVPEGRRI-------FPSL--------TVEENLL-LGAYARRDRAEVRADL------ERVYELFPrlke 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 432 --HQF----SGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIA 505
Cdd:COG0410 129 rrRQRagtlSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAY 207
|
250 260
....*....|....*....|
gi 489912973 506 VMQHGKVVETGAAQTVLTRP 525
Cdd:COG0410 208 VLERGRIVLEGTAAELLADP 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
282-512 |
2.66e-26 |
|
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: 105.59 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 282 GEPVLRITGLGRTYAERrslfgatrtvvaasEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIAR 361
Cdd:cd03215 1 GEPVLEVRGLSVKGAVR--------------DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTR 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 362 LS-------GAGLRPLRRKVQIVFQDpyrslnprravgESIIEgllNFGMPRaqalvraartlgvvglgpdvmrryphQF 434
Cdd:cd03215 67 RSprdairaGIAYVPEDRKREGLVLD------------LSVAE---NIALSS--------------------------LL 105
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 435 SGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
33-275 |
2.96e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 113.28 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEGilevSGGSARVLGEDIVTASARRRRELRATRMAMVFQE--P 110
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLDKP----TSGTYRVAGQDVATLDADALAQLRREHFGFIFQRyhL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 111 MTALNPVHRVgsqvdEVLRLHRRMPRAQRRAKVLEMFRSVHLPdvERIyDAYPHQLSGGQRQRIVIAMALILEPKLLIAD 190
Cdd:PRK10535 98 LSHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGLE--DRV-EYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 191 EPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEiADRIVVMNRGdltetgtrdEILARPSQNYTRRLVSSVP 270
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGHT-VIIVTHDPQVAAQ-AERVIEIRDG---------EIVRNPPAQEKVNVAGGTE 238
|
....*
gi 489912973 271 SLVPT 275
Cdd:PRK10535 239 PVVNT 243
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
314-512 |
2.98e-26 |
|
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: 106.79 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGaglRPLRRKVQIVFQDPYRSlnpRRAVGE 393
Cdd:cd03248 33 VSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH---KYLHSKVSLVGQEPVLF---ARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLNFGMPRAQALVRAARTLGVV-----GLGPDVMRRyPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSV 468
Cdd:cd03248 107 NIAYGLQSCSFECVKEAAQKAHAHSFIselasGYDTEVGEK-GSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489912973 469 QAQVLELIEQVRERTgvSVLFITHDLRVAAQVcDTIAVMQHGKV 512
Cdd:cd03248 186 EQQVQQALYDWPERR--TVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
310-517 |
3.58e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 108.17 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIArlsgAGLRP------LRRKVQIVFQDPYR 383
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIP----ANLKKikevkrLRKEIGLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 384 SLNpRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSA 463
Cdd:PRK13645 102 QLF-QETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 464 LDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGA 517
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
17-267 |
4.12e-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: 106.46 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIvtasarrrr 96
Cdd:TIGR03410 1 LEVSNLNVYY--GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLP-----VKSGSIRLDGEDI--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 elratrmamvfqepmTALNPVHRV---------GSQ------VDEVLRLhrrmpraqrrakVLEMFRSVHLPDVERIYDA 161
Cdd:TIGR03410 65 ---------------TKLPPHERAragiayvpqGREifprltVEENLLT------------GLAALPRRSRKIPDEIYEL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 162 YP--HQ--------LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAE 231
Cdd:TIGR03410 118 FPvlKEmlgrrggdLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARE 197
|
250 260 270
....*....|....*....|....*....|....*.
gi 489912973 232 IADRIVVMNRGDLTETGTRDEIlarpSQNYTRRLVS 267
Cdd:TIGR03410 198 LADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
298-548 |
4.48e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 112.51 E-value: 4.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 298 RRSLFGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRK-VQI 376
Cdd:PRK10535 11 RRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREhFGF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 377 VFQDpYRSLNPRRAVGESIIEGLLNfGMPRAQALVRAARTLGVVGLGPDVMRRyPHQFSGGQRQRLCIARALVMDPEVLV 456
Cdd:PRK10535 91 IFQR-YHLLSHLTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQ-PSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 457 ADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVcDTIAVMQHGKVVETGAAQtvLTRPGHAYTRALIDA 536
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQA-ERVIEIRDGEIVRNPPAQ--EKVNVAGGTEPVVNT 243
|
250
....*....|..
gi 489912973 537 APGRGWDFRNFR 548
Cdd:PRK10535 244 ASGWRQFVSGFR 255
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
315-528 |
8.26e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.82 E-value: 8.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 315 DLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRRKVQIVFQDpyRSLNPRRAVGES 394
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-----PSRRPVSMLFQE--NNLFSHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 395 IIEGL---LNFGMPRAQALVRAARTLGVvglgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:PRK10771 92 IGLGLnpgLKLNAAQREKLHAIARQMGI----EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 472 VLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTrpGHA 528
Cdd:PRK10771 168 MLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS--GKA 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
313-534 |
9.42e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 106.28 E-value: 9.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIE------PSAGRMLLGETDIARLSGAglrPLRRKVQIVFQDPyrSLN 386
Cdd:PRK14246 28 DITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAI---KLRKEVGMVFQQP--NPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 PRRAVGESIIEGLLNFGMPRAQALVR-AARTLGVVGLGPDVMRRY---PHQFSGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKREIKKiVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 463 ALDVSVQAQVLELIEQVRERtgVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALI 534
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
285-524 |
1.32e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.55 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLRITGLGRTY----AERRSLFGA--------TRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRM 352
Cdd:COG1134 4 MIEVENVSKSYrlyhEPSRSLKELllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 353 LLGEtdiaRLS-----GAGLRP---LRRKVQIVfqdpyrslnprravgesiieGLLNfGMPRAQALVRAARTLGVVGLGP 424
Cdd:COG1134 84 EVNG----RVSallelGAGFHPeltGRENIYLN--------------------GRLL-GLSRKEIDEKFDEIVEFAELGD 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 425 --DV-MRRYphqfSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVC 501
Cdd:COG1134 139 fiDQpVKTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLC 213
|
250 260
....*....|....*....|...
gi 489912973 502 DTIAVMQHGKVVETGAAQTVLTR 524
Cdd:COG1134 214 DRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
36-257 |
1.66e-25 |
|
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: 107.88 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 36 NLSLDVH---AGETVCVV-GESGSGKsvTSL--AVMGLLPegileVSGGSARVLGEDIVTASARRRRELRATRMAMVFQE 109
Cdd:COG4148 13 GFTLDVDftlPGRGVTALfGPSGSGK--TTLlrAIAGLER-----PDSGRIRLGGEVLQDSARGIFLPPHRRRIGYVFQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 PmtALNPvHRvgsQVDEVLRL-HRRMPRAQRRAKVLEMfrsVHLPDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLI 188
Cdd:COG4148 86 A--RLFP-HL---SVRGNLLYgRKRAPRAERRISFDEV---VELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 189 ADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:COG4148 157 MDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
34-259 |
2.00e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 34 VRNLSLDVHAGETVCVVGESGSGKSVTSLavmglLPEGILEVSGGSARVLGEDIVtasaRRRRELRATRMAMVFQEPMTA 113
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVR-----LIDGLLEAESGQIIIDGDLLT----EENVWDIRHKIGMVFQNPDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 114 LnpvhrVGSQVDEVLRL---HRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPKLLIAD 190
Cdd:PRK13650 94 F-----VGATVEDDVAFgleNKGIPHEEMKERVNEALELVGMQDFK---EREPARLSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 191 EPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAeIADRIVVMNRGDLTETGTRDEILARPSQ 259
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
36-257 |
2.11e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.45 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 36 NLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTASARRRRelratrMAMVFQEP----- 110
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKS-TLLNLIA----GFLPPDSGRILWNGQDLTALPPAERP------VSMLFQENnlfph 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 111 MTALNpvhRVGSQVDEVLRLhrrmpRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPKLLIAD 190
Cdd:COG3840 86 LTVAQ---NIGLGLRPGLKL-----TAEQRAQVEQALERVGLAGLL---DRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 191 EPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
30-512 |
2.93e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 109.25 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVM-GLLPEGILEvsgGSARVLGEDIVtasARRRRELRATRMAMVFQ 108
Cdd:PRK13549 17 GVKALDNVSLKVRAGEIVSLCGENGAGKS-TLMKVLsGVYPHGTYE---GEIIFEGEELQ---ASNIRDTERAGIAIIHQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 EPMtaLNPVHRVGSQV---DEVLRlHRRM--PRAQRRAKvlEMFRSVHLpdveriyDAYPH----QLSGGQRQRIVIAMA 179
Cdd:PRK13549 90 ELA--LVKELSVLENIflgNEITP-GGIMdyDAMYLRAQ--KLLAQLKL-------DINPAtpvgNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 180 LILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLFITHDFGVVAEIADRIVVMNRG-----DLTETGTRDEIL 254
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACIYISHKLNEVKAISDTICVIRDGrhigtRPAAGMTEDDII 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 255 ArpsQNYTRRLVssvpSLVPTQREAPgGEPVLR---ITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESG 331
Cdd:PRK13549 237 T---MMVGRELT----ALYPREPHTI-GEVILEvrnLTAWDPVNPHIKRV----------DDVSFSLRRGEILGIAGLVG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 332 SGKSTVARCIVRLIE-PSAGRMLLG--ETDIARLSGAglrpLRRKVQIVFQDPYR-SLNPRRAVGESIIegLLNFGMPRA 407
Cdd:PRK13549 299 AGRTELVQCLFGAYPgRWEGEIFIDgkPVKIRNPQQA----IAQGIAMVPEDRKRdGIVPVMGVGKNIT--LAALDRFTG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 408 QALVRAARTLGVVGLGPDVMR-RYPHQF------SGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVR 480
Cdd:PRK13549 373 GSRIDDAAELKTILESIQRLKvKTASPElaiarlSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV 452
|
490 500 510
....*....|....*....|....*....|..
gi 489912973 481 ERtGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:PRK13549 453 QQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
8-267 |
2.96e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 104.73 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 8 PAGDTSAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEGILEVS-GGSARVLGED 86
Cdd:COG1117 3 APASTLEPKIEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKS-TLLRCLNRMNDLIPGARvEGEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 87 IvtASARRRRELRATRMAMVFQEPmtalNPVHRvgSQVDEV---LRLHRRMPRAQRRAKVLEMFRSVHLPD-VERIYDAY 162
Cdd:COG1117 80 I--YDPDVDVVELRRRVGMVFQKP----NPFPK--SIYDNVaygLRLHGIKSKSELDEIVEESLRKAALWDeVKDRLKKS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 163 PHQLSGGQRQRIVIAMALILEPKLLIADEPTTALD-VTTQKqILALIRELQDRHqtAVLFITHDFGVVAEIADRIVVMNR 241
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDpISTAK-IEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYL 228
|
250 260
....*....|....*....|....*.
gi 489912973 242 GDLTETGTRDEILARPSQNYTRRLVS 267
Cdd:COG1117 229 GELVEFGPTEQIFTNPKDKRTEDYIT 254
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-519 |
2.98e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 110.60 E-value: 2.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 24 VSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLavMGLLpEGILEVSGGSARVLGEDivtasarrrrelratrM 103
Cdd:NF033858 7 VSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKS--SL--LSLI-AGARKIQQGRVEVLGGD----------------M 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 104 AmvfqepmtalNPVHR--VGSQ-----------------VDEVLRLHRRM---PRAQRRAKVLEMFRSVHL-PDVERiyd 160
Cdd:NF033858 66 A----------DARHRraVCPRiaympqglgknlyptlsVFENLDFFGRLfgqDAAERRRRIDELLRATGLaPFADR--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 161 ayPH-QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIREL-QDRHQTAVLfithdfgvVA----EIAD 234
Cdd:NF033858 133 --PAgKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGMSVL--------VAtaymEEAE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 235 R---IVVMNRGDLTETGTRDEILAR-PSQN---------------YTRRLVssvpslVPTQREAPGGEPVLRITGLgrTy 295
Cdd:NF033858 203 RfdwLVAMDAGRVLATGTPAELLARtGADTleaafiallpeekrrGHQPVV------IPPRPADDDDEPAIEARGL--T- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 296 aeRRslFGatrTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRmllgetdiARLSGaglRPLrrkvq 375
Cdd:NF033858 274 --MR--FG---DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGE--------AWLFG---QPV----- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 376 ivfqDPyRSLNPRRAVG----------E-SIIEGLL----NFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQ 440
Cdd:NF033858 331 ----DA-GDIATRRRVGymsqafslygElTVRQNLElharLFHLPAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQ 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 441 RLCIARALVMDPEVLVADEAVSALDVSVQAQVLE-LIEQVRERtGVSVlFI-THDLRVAAQvCDTIAVMQHGKVVETGAA 518
Cdd:NF033858 405 RLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRlLIELSRED-GVTI-FIsTHFMNEAER-CDRISLMHAGRVLASDTP 481
|
.
gi 489912973 519 Q 519
Cdd:NF033858 482 A 482
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
32-248 |
3.21e-25 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 104.34 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSVTslavMGLLpEGILEVSGGSARVLGEDivtasARRRRELRATRMAMVFQEPM 111
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTT----LKIL-SGLLQPTSGEVRVAGLV-----PWKRRKKFLRRIGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 TA---LNPVhrvgsqvdEVLRLHRRMPR------AQRRAKVLEMFrsvhlpDVERIYDAYPHQLSGGQRQRIVIAMALIL 182
Cdd:cd03267 105 QLwwdLPVI--------DSFYLLAAIYDlpparfKKRLDELSELL------DLEELLDTPVRQLSLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 183 EPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
37-255 |
3.51e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.17 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 37 LSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPE--GILEVSGgsARVLGEDIVTASARrrrelratrMAMVFQEPMTAL 114
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfeGKVKIDG--ELLTAENVWNLRRK---------IGMVFQNPDNQF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 115 npvhrVGSQVDEVLRL---HRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPKLLIADE 191
Cdd:PRK13642 95 -----VGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNMLDFK---TREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 192 PTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEILA 255
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
286-516 |
8.07e-25 |
|
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: 102.27 E-value: 8.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGeILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIarlsGA 365
Cdd:cd03264 1 LQLENLTKRYGKKRAL----------DGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LK 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRPLRRKVQIVFQDP--YRSLNPRRAVGESiieGLLNfGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLC 443
Cdd:cd03264 66 QPQKLRRRIGYLPQEFgvYPNFTVREFLDYI---AWLK-GIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRErtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03264 141 IAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
304-539 |
1.14e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 103.64 E-value: 1.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 304 ATRTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPL---RRKVQIVFQD 380
Cdd:PRK14271 32 AGKTVL--DQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVlefRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 381 PyrslNP-RRAVGESIIEGLLNFGM-PRAQALVRAARTLGVVGLGPDVMRRY---PHQFSGGQRQRLCIARALVMDPEVL 455
Cdd:PRK14271 110 P----NPfPMSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLWDAVKDRLsdsPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 456 VADEAVSALDVSVQAQVLELIEQVRERtgVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALID 535
Cdd:PRK14271 186 LLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
....
gi 489912973 536 AAPG 539
Cdd:PRK14271 264 GLSG 267
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
30-256 |
1.90e-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: 101.85 E-value: 1.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSvtslAVMGLLpEGILEVSGGSARVLGEDIVTASARRRRELratrMAMVFQE 109
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKS----TVVSLL-ERFYDPTSGEILLDGVDIRDLNLRWLRSQ----IGLVSQE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 PMTALNPVH------RVGSQVDEVLRlhrrmprAQRRAKVLEMFRSvhLPDVeriYD----AYPHQLSGGQRQRIVIAMA 179
Cdd:cd03249 86 PVLFDGTIAenirygKPDATDEEVEE-------AAKKANIHDFIMS--LPDG---YDtlvgERGSQLSGGQKQRIAIARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 180 LILEPKLLIADEPTTALDVTTQKQIL-ALIRELQDRhqtAVLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEILAR 256
Cdd:cd03249 154 LLRNPKILLLDEATSALDAESEKLVQeALDRAMKGR---TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-269 |
2.00e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.87 E-value: 2.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 9 AGDTSAAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEgilEVSG----GSARVLG 84
Cdd:PRK14271 12 AADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKT-TFLRTLNRMND---KVSGyrysGDVLLGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 85 EDIVTASARRRRELRatrMAMVFQEPmtalNPVHRvgSQVDEVL---RLHRRMPRAQRRAKVLEMFRSVHLPDV--ERIY 159
Cdd:PRK14271 88 RSIFNYRDVLEFRRR---VGMLFQRP----NPFPM--SIMDNVLagvRAHKLVPRKEFRGVAQARLTEVGLWDAvkDRLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 160 DAyPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhqTAVLFITHDFGVVAEIADRIVVM 239
Cdd:PRK14271 159 DS-PFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALF 235
|
250 260 270
....*....|....*....|....*....|
gi 489912973 240 NRGDLTETGTRDEILARPSQNYTRRLVSSV 269
Cdd:PRK14271 236 FDGRLVEEGPTEQLFSSPKHAETARYVAGL 265
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
16-255 |
2.71e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 106.43 E-value: 2.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVCGAGNRVVR---NLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLP--EGILEVSggsarvLGEDIV-- 88
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEptSGEVNVR------VGDEWVdm 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 89 TASARRRRELRATRMAMVFQEpmTALNPVHRVGSQVDEVLRLHrrMPRAQRRAKVLEMFRSVHLPD--VERIYDAYPHQL 166
Cdd:TIGR03269 353 TKPGPDGRGRAKRYIGILHQE--YDLYPHRTVLDNLTEAIGLE--LPDELARMKAVITLKMVGFDEekAEEILDKYPDEL 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTE 246
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVK 508
|
....*....
gi 489912973 247 TGTRDEILA 255
Cdd:TIGR03269 509 IGDPEEIVE 517
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
281-521 |
2.88e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.26 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 281 GGEPVLRITGLGRTyaerrslFGAtrtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLG--ETD 358
Cdd:COG3845 1 MMPPALELRGITKR-------FGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkPVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 359 I-----ARLSGAGLrplrrkvqiVFQDPyrSLNPRRAVGESII---EGLLNFGMPRAQALVRAARTLGVVGLG--PDvmr 428
Cdd:COG3845 71 IrsprdAIALGIGM---------VHQHF--MLVPNLTVAENIVlglEPTKGGRLDRKAARARIRELSERYGLDvdPD--- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 429 RYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALdvsVQAQVLELIEQVRE--RTGVSVLFITHDLRVAAQVCDTIAV 506
Cdd:COG3845 137 AKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL---TPQEADELFEILRRlaAEGKSIIFITHKLREVMAIADRVTV 213
|
250
....*....|....*
gi 489912973 507 MQHGKVVETGAAQTV 521
Cdd:COG3845 214 LRRGKVVGTVDTAET 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
308-517 |
3.40e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 104.34 E-value: 3.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 308 VVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETdiaRLSGagLRPLRRKVQIVFQDpYrSLNP 387
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMND--VPPAERGVGMVFQS-Y-ALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 388 RRAVGESIIEGLLNFGMPRAQALVR---AARTLGVVGLgpdvMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSAL 464
Cdd:PRK11000 89 HLSVAENMSFGLKLAGAKKEEINQRvnqVAEVLQLAHL----LDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489912973 465 DVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGA 517
Cdd:PRK11000 165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
17-225 |
4.65e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 100.25 E-value: 4.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVM-GLLPEGIlEVSGgsaRVL--GEDIVTASAR 93
Cdd:COG4136 2 LSLENLTITL--GGRPLLAPLSLTVAPGEILTLMGPSGSGKS-TLLAAIaGTLSPAF-SASG---EVLlnGRRLTALPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 RRRelratrMAMVFQEPMtaLNPVHRVGsqvdEVLR--LHRRMPRAQRRAKVLEMFRSVHLPDverIYDAYPHQLSGGQR 171
Cdd:COG4136 75 QRR------IGILFQDDL--LFPHLSVG----ENLAfaLPPTIGRAQRRARVEQALEEAGLAG---FADRDPATLSGGQR 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 172 QRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHD 225
Cdd:COG4136 140 ARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
33-253 |
5.21e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.70 E-value: 5.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-PegilevSGGSARVLGEDivtASARRRRELRATRMAMVFQEPM 111
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiP------SEGKVYVDGLD---TSDEENLWDIRNKAGMVFQNPD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 TALnpvhrVGSQVDEVLRL---HRRMPRAQRRAKVLEMFRSVHLPDVERiydAYPHQLSGGQRQRIVIAMALILEPKLLI 188
Cdd:PRK13633 96 NQI-----VATIVEEDVAFgpeNLGIPPEEIRERVDESLKKVGMYEYRR---HAPHLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 189 ADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEI 253
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
282-512 |
5.62e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 101.29 E-value: 5.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 282 GEPVLrITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGEtdiar 361
Cdd:PRK11247 10 GTPLL-LNAVSKRYGERTVL----------NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 362 lsgAGLRPLRRKVQIVFQDPyrSLNPRRAVGESIIEGLLnfGMPRAQALvraaRTLGVVGLGpDVMRRYPHQFSGGQRQR 441
Cdd:PRK11247 74 ---APLAEAREDTRLMFQDA--RLLPWKKVIDNVGLGLK--GQWRDAAL----QALAAVGLA-DRANEWPAALSGGQKQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 442 LCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
314-516 |
5.90e-24 |
|
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: 98.92 E-value: 5.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAglrpLRRKVQIVFQDPYrslnprravge 393
Cdd:cd03247 21 LSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LSSLISVLNQRPY----------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 siiegllnfgmpraqalvraartLGVVGLGPDVMRRyphqFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVL 473
Cdd:cd03247 86 -----------------------LFDTTLRNNLGRR----FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489912973 474 ELI-EQVRERTgvsVLFITHDLRVAAQVcDTIAVMQHGKVVETG 516
Cdd:cd03247 139 SLIfEVLKDKT---LIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
30-248 |
5.99e-24 |
|
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: 99.60 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDivtasarrrrelratrmamvFQE 109
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIK-----PDSGEITFDGKS--------------------YQK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 PMTALNpvhRVGSQVD-----------EVLRLHRRMPRAqRRAKVLEMFRSVHLpdveriyDAYPH----QLSGGQRQRI 174
Cdd:cd03268 67 NIEALR---RIGALIEapgfypnltarENLRLLARLLGI-RKKRIDEVLDVVGL-------KDSAKkkvkGFSLGMKQRL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 175 VIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03268 136 GIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQGIT-VLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
285-516 |
6.04e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 102.11 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLRITGLGRTYAERRslfgatrtvvAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRmllgetdiARLSG 364
Cdd:COG4152 1 MLELKGLTKRFGDKT----------AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGE--------VLWDG 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 365 aglRPLRRKVQIVFQdpY----RSLNPRRAVGESIIE-GLLNfGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQR 439
Cdd:COG4152 63 ---EPLDPEDRRRIG--YlpeeRGLYPKMKVGEQLVYlARLK-GLSKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 440 QRLCIARALVMDPEVLVADEAVSALD-VSVQAQVLELIEQVRErtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:COG4152 136 QKVQLIAALLHDPELLILDEPFSGLDpVNVELLKDVIRELAAK--GTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
314-522 |
6.09e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 102.09 E-value: 6.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAG-----------------------RMLLGETDIARLSGAglRPL 370
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekekvleKLVIQKTRFKKIKKI--KEI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 371 RRKVQIVFQDPYRSLNpRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVM 450
Cdd:PRK13651 104 RRRVGVVFQFAEYQLF-EQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAM 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 451 DPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVL 522
Cdd:PRK13651 183 EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDIL 253
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
314-527 |
8.90e-24 |
|
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: 99.85 E-value: 8.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRrkvQIVFQDpyRSLNPRRAVGE 393
Cdd:TIGR01184 4 VNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----PDR---MVVFQN--YSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SII----EGLLNFGMPRAQALVRaaRTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:TIGR01184 74 NIAlavdRVLPDLSKSERRAIVE--EHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 470 AQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTV-LTRPGH 527
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
306-516 |
9.21e-24 |
|
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: 99.28 E-value: 9.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 306 RTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLlgetdiarLSGAGLRPLRRKvQIVFQDPYRSL 385
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVL--------FDGKPLDIAARN-RIGYLPEERGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 386 NPRravgESIIEGLLNF----GMPRAQALVRAARTLGVVGLGPDVMRRYpHQFSGGQRQRLCIARALVMDPEVLVADEAV 461
Cdd:cd03269 82 YPK----MKVIDQLVYLaqlkGLKKEEARRRIDEWLERLELSEYANKRV-EELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 462 SALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
302-523 |
9.29e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.47 E-value: 9.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATRTVvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGaglRPLRRKVQIVFQ-- 379
Cdd:PRK11231 12 YGTKRIL---NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS---RQLARRLALLPQhh 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 380 ----------------DPYRSLNPRRAVGEsiiEGLLNFGMPRAQALVRAARTLGvvglgpdvmrryphQFSGGQRQRLC 443
Cdd:PRK11231 86 ltpegitvrelvaygrSPWLSLWGRLSAED---NARVNQAMEQTRINHLADRRLT--------------DLSGGQRQRAF 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRE--RTGVSVLfitHDLRVAAQVCDTIAVMQHGKVVETGAAQTV 521
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTqgKTVVTVL---HDLNQASRYCDHLVVLANGHVMAQGTPEEV 225
|
..
gi 489912973 522 LT 523
Cdd:PRK11231 226 MT 227
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
15-257 |
1.13e-23 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 102.61 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVCGaGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLlpEgilEVSGG----SARVLGE----- 85
Cdd:PRK11650 2 AGLKLQAVRKSYDG-KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL--E---RITSGeiwiGGRVVNElepad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 86 -DIvtasarrrrelratrmAMVFQEpmTALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLpdvERIYDAYPH 164
Cdd:PRK11650 76 rDI----------------AMVFQN--YALYPHMSVRENMAYGLKI-RGMPKAEIEERVAEAARILEL---EPLLDRKPR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDfGVVA-EIADRIVVMNRGD 243
Cdd:PRK11650 134 ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHD-QVEAmTLADRVVVMNGGV 212
|
250
....*....|....
gi 489912973 244 LTETGTRDEILARP 257
Cdd:PRK11650 213 AEQIGTPVEVYEKP 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-254 |
1.75e-23 |
|
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: 99.39 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNlsVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKS-VTSLAvMGLLPEGilevSGGSARVLGED------- 86
Cdd:COG1119 2 PLLELRN--VTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKStLLSLI-TGDLPPT----YGNDVRLFGERrggedvw 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 87 -------IVTASarrrrelratrMAMVFQEPMTALNpVhrVGSQVDEVLRLHRRMPRAQR-RAK-VLEMFRSVHLPDveR 157
Cdd:COG1119 75 elrkrigLVSPA-----------LQLRFPRDETVLD-V--VLSGFFDSIGLYREPTDEQReRAReLLELLGLAHLAD--R 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 158 IYdaypHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDfgvVAEIAD--- 234
Cdd:COG1119 139 PF----GTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHH---VEEIPPgit 211
|
250 260
....*....|....*....|
gi 489912973 235 RIVVMNRGDLTETGTRDEIL 254
Cdd:COG1119 212 HVLLLKDGRVVAAGPKEEVL 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
283-522 |
1.78e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.33 E-value: 1.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERrslfgatrTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDI--- 359
Cdd:COG1137 1 MMTLEAENLVKSYGKR--------TVV--KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 360 -----ARLsGAGLRPlrrkvqivfQDP--YRSLNprraVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPdVMRRYPH 432
Cdd:COG1137 71 pmhkrARL-GIGYLP---------QEAsiFRKLT----VEDNILAVLELRKLSKKEREERLEELLEEFGITH-LRKSKAY 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 433 QFSGGQRQRLCIARALVMDPEVLVADEAVSALD-VSVqAQVLELIEQVRERtGVSVLfIT-HDLRVAAQVCDTIAVMQHG 510
Cdd:COG1137 136 SLSGGERRRVEIARALATNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKER-GIGVL-ITdHNVRETLGICDRAYIISEG 212
|
250
....*....|..
gi 489912973 511 KVVETGAAQTVL 522
Cdd:COG1137 213 KVLAEGTPEEIL 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
36-253 |
2.49e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.83 E-value: 2.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 36 NLSLDVHAGETVCVVGESGSGKSVTSLAVMGllpegILEVSGGsaRVLGEDivTASARRRRELRATRMAMVFQEPMTALn 115
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIG-----IEKVKSG--EIFYNN--QAITDDNFEKLRKHIGIVFQNPDNQF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 116 pvhrVGSQV--DEVLRLHRRM-PRAQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPKLLIADEP 192
Cdd:PRK13648 97 ----VGSIVkyDVAFGLENHAvPYDEMHRRVSEALKQVDMLERA---DYEPNALSGGQKQRVAIAGVLALNPSVIILDEA 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 193 TTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEI 253
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
19-256 |
2.73e-23 |
|
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: 98.45 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVcGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLlpegiLEVSGGSARVLGEDIVTasarRRREL 98
Cdd:cd03254 5 FENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRF-----YDPQKGQILIDGIDIRD----ISRKS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 99 RATRMAMVFQEPmtalnpvHRVGSQVDEVLRLHRrmPRAqRRAKVLEMFRSVHLPD-VERIYDAYPHQ-------LSGGQ 170
Cdd:cd03254 75 LRSMIGVVLQDT-------FLFSGTIMENIRLGR--PNA-TDEEVIEAAKEAGAHDfIMKLPNGYDTVlgenggnLSQGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 171 RQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELqdRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTETGTR 250
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKL--MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTH 221
|
....*.
gi 489912973 251 DEILAR 256
Cdd:cd03254 222 DELLAK 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
283-523 |
3.41e-23 |
|
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: 98.62 E-value: 3.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGR--MLLGEtdia 360
Cdd:COG1119 1 DPLLELRNVTVRRGGKTIL----------DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGE---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 361 RLSGAGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGLlnFGM------PRAQALVRAARTLGVVGLGPDVMRRYpHQF 434
Cdd:COG1119 67 RRGGEDVWELRKRIGLVSPALQLRFPRDETVLDVVLSGF--FDSiglyrePTDEQRERARELLELLGLAHLADRPF-GTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 435 SGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVE 514
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVA 223
|
....*....
gi 489912973 515 TGAAQTVLT 523
Cdd:COG1119 224 AGPKEEVLT 232
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-266 |
3.87e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 98.97 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 9 AGDTSAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPE---GILEVSGgSARVLGE 85
Cdd:PRK14246 3 AGKSAEDVFNISRLYLYI--NDKAILKDITIKIPNNSIFGIMGPSGSGKS-TLLKVLNRLIEiydSKIKVDG-KVLYFGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 86 DIVtasaRRRRELRATRMAMVFQEPmtalNPVHRVgSQVDEV---LRLHRRMPRAQRRAKVLEMFRSVHL-PDVERIYDA 161
Cdd:PRK14246 79 DIF----QIDAIKLRKEVGMVFQQP----NPFPHL-SIYDNIaypLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLNS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 162 YPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELqdRHQTAVLFITHDFGVVAEIADRIVVMNR 241
Cdd:PRK14246 150 PASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYN 227
|
250 260
....*....|....*....|....*
gi 489912973 242 GDLTETGTRDEILARPSQNYTRRLV 266
Cdd:PRK14246 228 GELVEWGSSNEIFTSPKNELTEKYV 252
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
34-278 |
4.30e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 99.47 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 34 VRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIVTASARRRRELRATRMAMVFQEPMTA 113
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALL-----KPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQFPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 114 L--NPVHRvgsqvdEVLRLHR--RMPRAQRRAKVLEMFRSVHLPdvERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIA 189
Cdd:PRK13646 98 LfeDTVER------EIIFGPKnfKMNLDEVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 190 DEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILArpSQNYTRRLVSSV 269
Cdd:PRK13646 170 DEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK--DKKKLADWHIGL 247
|
....*....
gi 489912973 270 PSLVPTQRE 278
Cdd:PRK13646 248 PEIVQLQYD 256
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
286-525 |
4.73e-23 |
|
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: 98.00 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAerrslfgaTRTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLsga 365
Cdd:cd03218 1 LRAENLSKRYG--------KRKVV--NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 glrPLRRKVQ--IVF--QDP--YRSLNprraVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPdVMRRYPHQFSGGQR 439
Cdd:cd03218 68 ---PMHKRARlgIGYlpQEAsiFRKLT----VEENILAVLEIRGLSKKEREEKLEELLEEFHITH-LRKSKASSLSGGER 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 440 QRLCIARALVMDPEVLVADEAVSALD-VSVQaQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAA 518
Cdd:cd03218 140 RRVEIARALATNPKFLLLDEPFAGVDpIAVQ-DIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
....*..
gi 489912973 519 QTVLTRP 525
Cdd:cd03218 218 EEIAANE 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-254 |
5.15e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 98.31 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTslavMGLLpEGILEVSGGSARVLGEDIvtasarr 94
Cdd:PRK13548 1 AMLEARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRAL-SGELSPDSGEVRLNGRPL------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 rRELRATRMAMvfqepMTALNPVHRVGS---QVDEVLRLHRrMPRAQRRAKVLEMFRSV-HLPDVERIYDAYPHQLSGGQ 170
Cdd:PRK13548 67 -ADWSPAELAR-----RRAVLPQHSSLSfpfTVEEVVAMGR-APHGLSRAEDDALVAAAlAQVDLAHLAGRDYPQLSGGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 171 RQRIVIAMALI------LEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDL 244
Cdd:PRK13548 140 QQRVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRL 219
|
250
....*....|
gi 489912973 245 TETGTRDEIL 254
Cdd:PRK13548 220 VADGTPAEVL 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
306-516 |
5.75e-23 |
|
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: 97.22 E-value: 5.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 306 RTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS-GAGLRPlrrkvqivfqdpyrS 384
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGlGGGFNP--------------E 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 385 LNPRravgESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDV---MRRYphqfSGGQRQRLCIARALVMDPEVLVADEAV 461
Cdd:cd03220 99 LTGR----ENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIdlpVKTY----SSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 462 SALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:cd03220 171 AVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-239 |
6.24e-23 |
|
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: 102.36 E-value: 6.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 2 PYAPYPPAGDTSAAVLAIRNLSVSVCGAGNrVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSAR 81
Cdd:TIGR02857 307 PLAGKAPVTAAPASSLEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-----PTEGSIA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 82 VLGEDIvtasARRRRELRATRMAMVFQEPmtalnpvHRVGSQVDEVLRLHRR------MPRAQRRAKVLEMFRSvhLPD- 154
Cdd:TIGR02857 381 VNGVPL----ADADADSWRDQIAWVPQHP-------FLFAGTIAENIRLARPdasdaeIREALERAGLDEFVAA--LPQg 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 155 VERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqtAVLFITHDFGVVAEiAD 234
Cdd:TIGR02857 448 LDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGR--TVLLVTHRLALAAL-AD 524
|
....*
gi 489912973 235 RIVVM 239
Cdd:TIGR02857 525 RIVVL 529
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
33-257 |
9.24e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 97.73 E-value: 9.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLP---EGILEVSGGSARVL--GEDIVTASARRRRELRATRMAMVF 107
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKS-TFLRCINFLEkpsEGSIVVNGQTINLVrdKDGQLKVADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 108 QE-----PMTALNPVHRVGSQVdevlrlhRRMPRAQRRAKVLEMFRSVHLPdvERIYDAYPHQLSGGQRQRIVIAMALIL 182
Cdd:PRK10619 99 QHfnlwsHMTVLENVMEAPIQV-------LGLSKQEARERAVKYLAKVGID--ERAQGKYPVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 183 EPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
273-507 |
9.81e-23 |
|
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: 101.59 E-value: 9.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 273 VPTQREAPGGE---PVLRITGLGRTYAERRslfgatrtvVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSA 349
Cdd:TIGR02857 306 RPLAGKAPVTAapaSSLEFSGVSVAYPGRR---------PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 350 GRMLLGETDIARLSGAGlrpLRRKVQIVFQDPYrslnprrAVGESIIEGLLnFGMPRA--QALVRAARTLGVVGLGPDVM 427
Cdd:TIGR02857 377 GSIAVNGVPLADADADS---WRDQIAWVPQHPF-------LFAGTIAENIR-LARPDAsdAEIREALERAGLDEFVAALP 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 428 RRY-------PHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRErtGVSVLFITHDLRVAAqV 500
Cdd:TIGR02857 446 QGLdtpigegGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-L 522
|
....*..
gi 489912973 501 CDTIAVM 507
Cdd:TIGR02857 523 ADRIVVL 529
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
37-368 |
1.02e-22 |
|
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: 99.80 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 37 LSLDVHAGETVCVVGESGSGKSVTSLAVMGLL--PEGILEVSGgsaRVLGEdivtASARRRRELRATRMAMVFQEpmTAL 114
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrpDEGEIVLNG---RTLFD----SRKGIFLPPEKRRIGYVFQE--ARL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 115 NPVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLpdVERiydaYPHQLSGGQRQRIVIAMALILEPKLLIADEPTT 194
Cdd:TIGR02142 87 FPHLSVRGNLRYGMKRARPSERRISFERVIELLGIGHL--LGR----LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 195 ALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNY-TRRLVSSVPS-- 271
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWlAREDQGSLIEgv 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 272 --------------------LVPTQREAPGGEPVLRITG----LGRTYAERRSLFGATRTVVAASEVDLTLRRGeilgiV 327
Cdd:TIGR02142 241 vaehdqhygltalrlggghlWVPENLGPTGARLRLRVPArdvsLALQKPEATSIRNILPARVVEIEDSDIGRVG-----V 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 489912973 328 GESGSGKSTVARcIVRL------IEPsaGRMLlgetdIARLSGAGLR 368
Cdd:TIGR02142 316 VLESGGKTLWAR-ITRWardelgIAP--GTPV-----FAQIKAVALR 354
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
8-253 |
1.22e-22 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 101.26 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 8 PAGDTSAAVLAIRNLSVsVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDI 87
Cdd:COG3845 249 APAEPGEVVLEVENLSV-RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP-----PASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 88 vtaSARRRRELRATRMAMVFQEPM-TALNPvhrvGSQVDE--VLRLHRRMP----------RAQRRAK-VLEMFRsVHLP 153
Cdd:COG3845 323 ---TGLSPRERRRLGVAYIPEDRLgRGLVP----DMSVAEnlILGRYRRPPfsrggfldrkAIRAFAEeLIEEFD-VRTP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 154 DVeriyDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIA 233
Cdd:COG3845 395 GP----DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALS 469
|
250 260
....*....|....*....|
gi 489912973 234 DRIVVMNRGDLTETGTRDEI 253
Cdd:COG3845 470 DRIAVMYEGRIVGEVPAAEA 489
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
40-257 |
1.28e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 98.17 E-value: 1.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 40 DVHA----GETVCVVGESGSGKSvTSLAVMgllpEGILEVSGGSARvLGEDIVTASARRRR-ELRATRMAMVFQEPMtal 114
Cdd:PRK13634 25 DVNVsipsGSYVAIIGHTGSGKS-TLLQHL----NGLLQPTSGTVT-IGERVITAGKKNKKlKPLRKKVGIVFQFPE--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 115 npvhrvgSQVDE--VLR------LHRRMPRAQRRAKVLEMFRSVHLPdvERIYDAYPHQLSGGQRQRIVIAMALILEPKL 186
Cdd:PRK13634 96 -------HQLFEetVEKdicfgpMNFGVSEEDAKQKAREMIELVGLP--EELLARSPFELSGGQMRRVAIAGVLAMEPEV 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 187 LIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:PRK13634 167 LVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
30-256 |
1.34e-22 |
|
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: 96.53 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSvtslAVMGLLPEgILEVSGGSARVLGEDI--VTASARRRRelratrMAMVF 107
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKS----TILRLLFR-FYDVSSGSILIDGQDIreVTLDSLRRA------IGVVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 108 QEPM----TALNPVH--RVGSQVDEVLRlhrrmprAQRRAKVlemfrsvHlPDVERIYDAYPHQ-------LSGGQRQRI 174
Cdd:cd03253 82 QDTVlfndTIGYNIRygRPDATDEEVIE-------AAKAAQI-------H-DKIMRFPDGYDTIvgerglkLSGGEKQRV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 175 VIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTavLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEIL 254
Cdd:cd03253 147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTT--IVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
..
gi 489912973 255 AR 256
Cdd:cd03253 224 AK 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
302-525 |
1.48e-22 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATRTVvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGaglRPLRRKVQIVFQDP 381
Cdd:COG4604 11 YGGKVVL---DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS---RELAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 yrSLNPRRAVGEsiiegLLNFG---------MPRAQALVRAArtLGVVGLGPdvMR-RYPHQFSGGQRQRLCIARALVMD 451
Cdd:COG4604 85 --HINSRLTVRE-----LVAFGrfpyskgrlTAEDREIIDEA--IAYLDLED--LAdRYLDELSGGQRQRAFIAMVLAQD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 452 PEVLVADEAVSALDVSVQAQVLELIEQ-VRE--RTGVSVLfitHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:COG4604 154 TDYVLLDEPLNNLDMKHSVQMMKLLRRlADElgKTVVIVL---HDINFASCYADHIVAMKDGRVVAQGTPEEIITPE 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
16-257 |
1.52e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.46 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVcGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVmgllpEGILEVSGGSARVLGEDIvtASARRR 95
Cdd:PRK13639 1 ILETRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHF-----NGILKPTSGEVLIKGEPI--KYDKKS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRATRMAMVFQEPMTALnpvhrVGSQVDE-----VLRLHRRMPRAQRRAKvlEMFRSVHLPDVERiydAYPHQLSGGQ 170
Cdd:PRK13639 73 LLEVRKTVGIVFQNPDDQL-----FAPTVEEdvafgPLNLGLSKEEVEKRVK--EALKAVGMEGFEN---KPPHHLSGGQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 171 RQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDLTETGTR 250
Cdd:PRK13639 143 KKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGIT-IIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
....*..
gi 489912973 251 DEILARP 257
Cdd:PRK13639 222 KEVFSDI 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
31-242 |
2.90e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 95.04 E-value: 2.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 31 NRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLP--EGILEVSGGSARVLGEDivtasarrrrelratRMAMVFQ 108
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILpdSGEVLFDGKPLDIAARN---------------RIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 EpmTALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVE--RIydaypHQLSGGQRQRIVIAMALILEPKL 186
Cdd:cd03269 78 E--RGLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYAnkRV-----EELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 187 LIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIRELARAGKT-VILSTHQMELVEELCDRVLLLNKG 204
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-267 |
2.96e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.14 E-value: 2.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVCGAgnRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEGILEVS-GGSARVLGEDIVTASAR 93
Cdd:PRK14247 2 NKIEIRDLKVSFGQV--EVLDGVNLEIPDNTITALMGPSGSGKS-TLLRVFNRLIELYPEARvSGEVYLDGQDIFKMDVI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 RRRELratrMAMVFQEPmtalNPVHRVG--SQVDEVLRLHRRM-PRAQRRAKVLEMFRSVHLPD-VERIYDAYPHQLSGG 169
Cdd:PRK14247 79 ELRRR----VQMVFQIP----NPIPNLSifENVALGLKLNRLVkSKKELQERVRWALEKAQLWDeVKDRLDAPAGKLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 170 QRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELqdRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGT 249
Cdd:PRK14247 151 QQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLEL--KKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGP 228
|
250
....*....|....*...
gi 489912973 250 RDEILARPSQNYTRRLVS 267
Cdd:PRK14247 229 TREVFTNPRHELTEKYVT 246
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
33-257 |
3.33e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 100.95 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSvtslAVMGLLpEGILEVSGGSARVLGEDIVtasaRRRRELRATRMAMVFQEPmt 112
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKS----TVAALL-QNLYQPTGGQVLLDGVPLV----QYDHHYLHRQVALVGQEP-- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 113 alnpVHRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVERIYDAY--PH--QLSGGQRQRIVIAMALILEPKLLI 188
Cdd:TIGR00958 565 ----VLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgEKgsQLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 189 ADEPTTALDVTTQkQILALIRELQDRhqtAVLFITHDFGVVaEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:TIGR00958 641 LDEATSALDAECE-QLLQESRSRASR---TVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
309-534 |
3.64e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 96.00 E-value: 3.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRL--IEPSA---GRMLLGETDiarLSGAGLRP--LRRKVQIVFQDP 381
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFrveGKVTFHGKN---LYAPDVDPveVRRRIGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 Y---RSLNPRRAVGESI--IEGLLNFGMPRAqaLVRAARTLGVvglgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLV 456
Cdd:PRK14243 101 NpfpKSIYDNIAYGARIngYKGDMDELVERS--LRQAALWDEV----KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 457 ADEAVSALDVSVQAQVLELIEQVRERtgVSVLFITHDLRVAAQVCDTIAVM---------QHGKVVETGAAQTVLTRPGH 527
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQ 252
|
....*..
gi 489912973 528 AYTRALI 534
Cdd:PRK14243 253 QATRDYV 259
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
314-527 |
3.92e-22 |
|
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: 100.28 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPyrslnprraVge 393
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT---QASLRAAIGIVPQDT---------V-- 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 siiegLLN--------FGMPRA-QALVRAARTLGVVGlgpDVMRRYPHQF-----------SGGQRQRLCIARALVMDPE 453
Cdd:COG5265 443 -----LFNdtiayniaYGRPDAsEEEVEAAARAAQIH---DFIESLPDGYdtrvgerglklSGGEKQRVAIARTLLKNPP 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 454 VLVADEAVSALDVSVQAQVLELIEQV-RERTgvsVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLTRPGH 527
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVaRGRT---TLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLAQGGL 585
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
14-256 |
4.88e-22 |
|
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: 99.82 E-value: 4.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 14 AAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLAVMgLLpeGILEVSGGSARVLGEDIvtasar 93
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKS--TLARL-LV--GVWPPTAGSVRLDGADL------ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 rrrelratrmamvFQEPMTALNPvhRVG--------------------SQVD--EVLRlhrrmprAQRRAKVLEMFrsVH 151
Cdd:COG4618 397 -------------SQWDREELGR--HIGylpqdvelfdgtiaeniarfGDADpeKVVA-------AAKLAGVHEMI--LR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 152 LPDVeriYD----AYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFG 227
Cdd:COG4618 453 LPDG---YDtrigEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPS 528
|
250 260
....*....|....*....|....*....
gi 489912973 228 VVAeIADRIVVMNRGDLTETGTRDEILAR 256
Cdd:COG4618 529 LLA-AVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
29-271 |
5.16e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.54 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 29 AGNRVVRNLSLDVHAGETVCVVGESGSGKsvTSLAVmglLPEGILEVSGGSARVLGEDIVTASARRrrelratrmAMVFQ 108
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGK--TTLLN---LIAGFVPYQHGSITLDGKPVEGPGAER---------GVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 EpmTALNPVHRVGSQVDEVLRLhRRMPRAQRRAKVLEMFRSVHLPDVERiydAYPHQLSGGQRQRIVIAMALILEPKLLI 188
Cdd:PRK11248 78 N--EGLLPWRNVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLEGAEK---RYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 189 ADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDltetgtrDEILARPSQNYTRRLVSS 268
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGP-------GRVVERLPLNFARRFVAG 224
|
...
gi 489912973 269 VPS 271
Cdd:PRK11248 225 ESS 227
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
29-256 |
5.44e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 96.33 E-value: 5.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 29 AGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGllpegILEVSGGSARVLGEdivtasarrrrelratrmamvfq 108
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILG-----ILAPDSGEVLWDGE----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 ePMTAlNPVHRVG-----------SQVDEVL----RLHRrMPRAQRRAKVLEMFRSVHLPD-----VEriydayphQLSG 168
Cdd:COG4152 64 -PLDP-EDRRRIGylpeerglypkMKVGEQLvylaRLKG-LSKAEAKRRADEWLERLGLGDrankkVE--------ELSK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:COG4152 133 GNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
|
....*...
gi 489912973 249 TRDEILAR 256
Cdd:COG4152 212 SVDEIRRQ 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-513 |
5.56e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.22 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 13 SAAVLAIRNLSVSVCGAgnRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEdivTASA 92
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGV--KALDDISFDCRAGQVHALMGENGAGKS-TLLKILS----GNYQPDAGSILIDGQ---EMRF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 93 RRRRELRATRMAMVFQE-----PMT-ALN------PvHRVGSqvdevlrLHRRMPRAQRRAKVLEMFRSVHlPDVERIYd 160
Cdd:PRK11288 71 ASTTAALAAGVAIIYQElhlvpEMTvAENlylgqlP-HKGGI-------VNRRLLNYEAREQLEHLGVDID-PDTPLKY- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 161 ayphqLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMN 240
Cdd:PRK11288 141 -----LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 241 RGdltetgtrdeilarpsqnytrRLVSSVPSLVPTQREAPGGEPVLRitGLGRTYAERRSLFGATRTVVA-------ASE 313
Cdd:PRK11288 215 DG---------------------RYVATFDDMAQVDRDQLVQAMVGR--EIGDIYGYRPRPLGEVRLRLDglkgpglREP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLL-GETDIARLSGAGLR------PLRRKVQ-IVfqdpyrsl 385
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIRSPRDAIRagimlcPEDRKAEgII-------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 386 nPRRAVGESI----------IEGLLNFGMPRAQALVRAARTlgvvglgpDVMRRYPHQ----FSGGQRQRLCIARALVMD 451
Cdd:PRK11288 344 -PVHSVADNInisarrhhlrAGCLINNRWEAENADRFIRSL--------NIKTPSREQlimnLSGGNQQKAILGRWLSED 414
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 452 PEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVV 513
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-273 |
5.97e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 95.82 E-value: 5.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVCGA-GNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-PEgilevsggSARVLGEDIVTASARRRR 96
Cdd:PRK13644 2 IRLENVSYSYPdGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQ--------KGKVLVSGIDTGDFSKLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATrMAMVFQEPMTALnpvhrVGSQVDEVLRLHRR---MPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQR 173
Cdd:PRK13644 74 GIRKL-VGIVFQNPETQF-----VGRTVEEDLAFGPEnlcLPPIEIRKRVDRALAEIGL---EKYRHRSPKTLSGGQGQC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 174 IVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVaEIADRIVVMNRGDLTETGTRDEI 253
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT-IVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENV 222
|
250 260
....*....|....*....|
gi 489912973 254 LARPSQNYtrrLVSSVPSLV 273
Cdd:PRK13644 223 LSDVSLQT---LGLTPPSLI 239
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
17-254 |
6.04e-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: 93.75 E-value: 6.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLlPEgiLEVSGGSARVLGEDIvtaSARRRR 96
Cdd:cd03217 1 LEIKDLHVSV--GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PK--YEVTEGEILFKGEDI---TDLPPE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEPMtalnpvhrvgsQVDEVlrlhrrmpraqrraKVLEMFRSVHLpdveriydayphQLSGGQRQRIVI 176
Cdd:cd03217 73 ERARLGIFLAFQYPP-----------EIPGV--------------KNADFLRYVNE------------GFSGGEKKRNEI 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqTAVLFITHdFGVVAE--IADRIVVMNRGDLTETGTRDEIL 254
Cdd:cd03217 116 LQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEG-KSVLIITH-YQRLLDyiKPDRVHVLYDGRIVKSGDKELAL 193
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
314-526 |
6.05e-22 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 100.03 E-value: 6.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPyrslnprRAVGE 393
Cdd:TIGR03797 472 VSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD---VQAVRRQLGVVLQNG-------RLMSG 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SI---IEGLLNFGMPRAQAlvrAARtlgVVGLGPDVmRRYPHQF-----------SGGQRQRLCIARALVMDPEVLVADE 459
Cdd:TIGR03797 542 SIfenIAGGAPLTLDEAWE---AAR---MAGLAEDI-RAMPMGMhtvisegggtlSGGQRQRLLIARALVRKPRILLFDE 614
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 460 AVSALDVSVQAQVLELIEQVRertgVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLTRPG 526
Cdd:TIGR03797 615 ATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMAREG 676
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
284-531 |
6.30e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.49 E-value: 6.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 284 PVLRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS 363
Cdd:PRK14258 6 PAIKVNNLSFYYDTQKILEG----------VSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEFFNQN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 364 ----GAGLRPLRRKVQIVFQDPyrSLNPRrAVGESIIEGLLNFGM-PRAQ--ALVRAArtLGVVGLGPDV---MRRYPHQ 433
Cdd:PRK14258 76 iyerRVNLNRLRRQVSMVHPKP--NLFPM-SVYDNVAYGVKIVGWrPKLEidDIVESA--LKDADLWDEIkhkIHKSALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 434 FSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQH---- 509
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenr 230
|
250 260
....*....|....*....|...
gi 489912973 510 -GKVVETGAAQTVLTRPGHAYTR 531
Cdd:PRK14258 231 iGQLVEFGLTKKIFNSPHDSRTR 253
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-256 |
8.19e-22 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 99.27 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 7 PPAGDTSAAVlAIRNLSVSVCGAGnRVVRNLSLDVHAGETVCVVGESGSGKSVTslavMGLLpEGILEVSGGSARVLGED 86
Cdd:PRK13657 326 IDLGRVKGAV-EFDDVSFSYDNSR-QGVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLL-QRVFDPQSGRILIDGTD 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 87 IVTASARRRRELratrMAMVFQEPMTALNPVH---RVG--SQVDEVLRlhrrmpRAQRRAKVLEMfrsvhlpdVERIYDA 161
Cdd:PRK13657 399 IRTVTRASLRRN----IAVVFQDAGLFNRSIEdniRVGrpDATDEEMR------AAAERAQAHDF--------IERKPDG 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 162 YP-------HQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELqdRHQTAVLFITHDFGVVAEiAD 234
Cdd:PRK13657 461 YDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTVRN-AD 537
|
250 260
....*....|....*....|..
gi 489912973 235 RIVVMNRGDLTETGTRDEILAR 256
Cdd:PRK13657 538 RILVFDNGRVVESGSFDELVAR 559
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
283-519 |
8.45e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.08 E-value: 8.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIE----PSAGRMLLGET- 357
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHA----------VDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGRTv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 358 -DIARLSGaGLRPLRRKVQIVFQDpyRSLNPRRAVGESIIEGLLN-----------FGMPRAQalvRAARTLGVVGlgpd 425
Cdd:PRK09984 72 qREGRLAR-DIRKSRANTGYIFQQ--FNLVNRLSVLENVLIGALGstpfwrtcfswFTREQKQ---RALQALTRVG---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 426 vMRRYPHQ----FSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVC 501
Cdd:PRK09984 142 -MVHFAHQrvstLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYC 220
|
250
....*....|....*...
gi 489912973 502 DTIAVMQHGKVVETGAAQ 519
Cdd:PRK09984 221 ERIVALRQGHVFYDGSSQ 238
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
314-525 |
8.53e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 96.84 E-value: 8.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRRKVQIVFQDpYrSLNPRRAVGE 393
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE-----PADRDIAMVFQN-Y-ALYPHMSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRyPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQV- 472
Cdd:PRK11650 96 NMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRK-PRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMr 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489912973 473 LElIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PRK11650 175 LE-IQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKP 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
149-278 |
9.37e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 95.25 E-value: 9.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 149 SVHLPDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGV 228
Cdd:PRK13652 121 ALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDL 200
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489912973 229 VAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRL-VSSVPSLVPTQRE 278
Cdd:PRK13652 201 VPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARVHLdLPSLPKLIRSLQA 251
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-242 |
9.54e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 94.77 E-value: 9.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcGAG----NRVVRNLSLDVHAGETVCVVGESGSGKSvTSL-AVMGLLPegileVSGGSARVLGEDIVTAS 91
Cdd:COG1101 2 LELKNLSKTF-NPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKS-TLLnAIAGSLP-----PDSGSILIDGKDVTKLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 92 ARRRRELratrMAMVFQEPM--TALNpvhrvgSQVDEVLRLHRRmpRAQRR-------AKVLEMFR----SVHLpDVERI 158
Cdd:COG1101 75 EYKRAKY----IGRVFQDPMmgTAPS------MTIEENLALAYR--RGKRRglrrgltKKRRELFRellaTLGL-GLENR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 159 YDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITH------DFGvvaei 232
Cdd:COG1101 142 LDTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeqalDYG----- 216
|
250
....*....|
gi 489912973 233 aDRIVVMNRG 242
Cdd:COG1101 217 -NRLIMMHEG 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
33-249 |
9.75e-22 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.11 E-value: 9.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTASARRRRELRATRMAMVFQ---- 108
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKS-TLLHLLG----GLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFIYQfhhl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 -EPMTALNPVhrvgsqvdEVLRLHRRMPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIVIAMALILEPKLL 187
Cdd:PRK11629 99 lPDFTALENV--------AMPLLIGKKKPAEINSRALEMLAAVGL---EHRANHRPSELSGGERQRVAIARALVNNPRLV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 188 IADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGvVAEIADRIVVMNRGDLTETGT 249
Cdd:PRK11629 168 LADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDGRLTAELS 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
313-521 |
1.20e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.48 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGET---DIArlSGAGLRPLRRKVQIVFQDPyrSLNPRR 389
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAE--KGICLPPEKRRIGYVFQDA--RLFPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVgesiiEGLLNFGMpRAQALVRAARTLGVVGLGPdVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:PRK11144 92 KV-----RGNLRYGM-AKSMVAQFDKIVALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489912973 470 AQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTV 521
Cdd:PRK11144 165 RELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
34-259 |
1.57e-21 |
|
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: 93.30 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 34 VRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvtasarrrrELRATRMAMVFQEpmTA 113
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKS-TLLNLIS----GLAQPTSGGVILEGKQI---------TEPGPDRMVVFQN--YS 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 114 LNP----VHRVGSQVDEVLRlhrRMPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIA 189
Cdd:TIGR01184 65 LLPwltvRENIALAVDRVLP---DLSKSERRAIVEEHIALVGL---TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 190 DEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEI-LARPSQ 259
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPRD 209
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
322-541 |
1.57e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 99.28 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 322 EILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLsgaGLRPLRRKVQIVFQDPYrslnprravgesIIEGLLN 401
Cdd:PLN03232 1263 EKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTDLRRVLSIIPQSPV------------LFSGTVR 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 402 FGM-PRAQ--------ALVRAARTlgvvglgpDVMRRYP-----------HQFSGGQRQRLCIARALVMDPEVLVADEAV 461
Cdd:PLN03232 1328 FNIdPFSEhndadlweALERAHIK--------DVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 462 SALDVSVQAQVLELIEQvrERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLTRPGHAYTRALIDAAPGRG 541
Cdd:PLN03232 1400 ASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPANA 1476
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
314-510 |
1.68e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.24 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrP--LRRKVQIVFQDPyrSLnprraV 391
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK-----PeiYRQQVSYCAQTP--TL-----F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIIEGLLNFGMPRAQA--LVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:PRK10247 94 GDTVYDNLIFPWQIRNQQpdPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489912973 470 AQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHG 510
Cdd:PRK10247 174 HNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
17-256 |
1.69e-21 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 98.25 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtslAVMGLLPEgILEVSGGSARVLGEDIvtasARRRR 96
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKS----TLVNLIPR-FYEPDSGQILLDGHDL----ADYTL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEPM-----TALNPVHRVGSQVDevlrlhrrmpraqrRAKVLEMFRSVHLPDVeriYDAYP---HQ--- 165
Cdd:TIGR02203 402 ASLRRQVALVSQDVVlfndtIANNIAYGRTEQAD--------------RAEIERALAAAYAQDF---VDKLPlglDTpig 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 -----LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTavLFITHDFGVVaEIADRIVVMN 240
Cdd:TIGR02203 465 engvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTT--LVIAHRLSTI-EKADRIVVMD 541
|
250
....*....|....*.
gi 489912973 241 RGDLTETGTRDEILAR 256
Cdd:TIGR02203 542 DGRIVERGTHNELLAR 557
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
285-537 |
2.28e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.92 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLRITGLGRTYAERRSLFGATrtvvaasevdLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLgETDIARLSG 364
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLN----------LDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLW-QGKPLDYSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 365 AGLRPLRRKVQIVFQDPYRSLNpRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGlgPDVMRRYPHQ-FSGGQRQRLC 443
Cdd:PRK13638 70 RGLLALRQQVATVFQDPEQQIF-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVD--AQHFRHQPIQcLSHGQKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAaqtvlt 523
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA------ 219
|
250
....*....|....*
gi 489912973 524 rPGHAYTRA-LIDAA 537
Cdd:PRK13638 220 -PGEVFACTeAMEQA 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-253 |
2.45e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.01 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 6 YPPAGDTSAA-VLAIRNLSVsvcgagNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLG 84
Cdd:COG1129 245 FPKRAAAPGEvVLEVEGLSV------GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADP-----ADSGEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 85 EDIVtasarrrrelratrmamvFQEPMTALNpvHRVG-----------------------SQVDEVLRlHRRMPRAQRRA 141
Cdd:COG1129 314 KPVR------------------IRSPRDAIR--AGIAyvpedrkgeglvldlsirenitlASLDRLSR-GGLLDRRRERA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 142 KVLEMFRSVHL--PDVERIYDayphQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAV 219
Cdd:COG1129 373 LAEEYIKRLRIktPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAV 447
|
250 260 270
....*....|....*....|....*....|....
gi 489912973 220 LFITHDFGVVAEIADRIVVMNRGDLTETGTRDEI 253
Cdd:COG1129 448 IVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
314-517 |
2.45e-21 |
|
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: 92.97 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAglRPLRRKVQIVFQDpyRSLNPRRAVGE 393
Cdd:TIGR03410 19 VSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH--ERARAGIAYVPQG--REIFPRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLlnFGMPRAQALVRAArtlgVVGLGP---DVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQA 470
Cdd:TIGR03410 95 NLLTGL--AALPRRSRKIPDE----IYELFPvlkEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489912973 471 QVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGA 517
Cdd:TIGR03410 169 DIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
17-242 |
3.90e-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: 3.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLAVMGLlpeGILEVSGGSARVLGEDIvtasarrrr 96
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKS--TLARLIL---GLLRPTSGRVRLDGADI--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 elratrmamvfqepmtalnpvhrvgSQVDevlrlhrrmpRAQRRAKVLEMFRSVHLPD---VERIydayphqLSGGQRQR 173
Cdd:cd03246 67 -------------------------SQWD----------PNELGDHVGYLPQDDELFSgsiAENI-------LSGGQRQR 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 174 IVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEiADRIVVMNRG 242
Cdd:cd03246 105 LGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIV-IAHRPETLAS-ADRILVLEDG 171
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
19-249 |
3.96e-21 |
|
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: 92.17 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIVTASARRRREL 98
Cdd:cd03244 5 FKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLV-----ELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 99 ratrMAMVFQEPMT-------ALNPVHRVGsqvDEvlRLHRRMPRAQRRAKVLEMfrSVHLPDVEriyDAYPHQLSGGQR 171
Cdd:cd03244 80 ----ISIIPQDPVLfsgtirsNLDPFGEYS---DE--ELWQALERVGLKEFVESL--PGGLDTVV---EEGGENLSVGQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 172 QRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRElqDRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTETGT 249
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
283-534 |
4.05e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.92 E-value: 4.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDiarL 362
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKAL----------NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIV---Y 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 SGAGLRP-------LRRKVQIVFQDPyrslNP-RRAVGESIIEGLLNFGMPRAQALVRAA-RTLGVVGLGPDVMRRYpHQ 433
Cdd:PRK14239 70 NGHNIYSprtdtvdLRKEIGMVFQQP----NPfPMSIYENVVYGLRLKGIKDKQVLDEAVeKSLKGASIWDEVKDRL-HD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 434 ----FSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtgVSVLFITHDLRVAAQVCDTIAVMQH 509
Cdd:PRK14239 145 salgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD--YTMLLVTRSMQQASRISDRTGFFLD 222
|
250 260
....*....|....*....|....*
gi 489912973 510 GKVVETGAAQTVLTRPGHAYTRALI 534
Cdd:PRK14239 223 GDLIEYNDTKQMFMNPKHKETEDYI 247
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
17-251 |
4.46e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 92.44 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLlPEgiLEVSGGSARVLGEDIVtasarrrr 96
Cdd:COG0396 1 LEIKNLHVSV--EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PK--YEVTSGSILLDGEDIL-------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 elratRMA----------MVFQEPM------------TALNPVHRvgsqvdevlrlhRRMPRAQRRAKVLEMFRSVHLPD 154
Cdd:COG0396 68 -----ELSpderaragifLAFQYPVeipgvsvsnflrTALNARRG------------EELSAREFLKLLKEKMKELGLDE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 155 --VERIYDAyphQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqTAVLFITHDFGVVAEI 232
Cdd:COG0396 131 dfLDRYVNE---GFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPD-RGILIITHYQRILDYI 206
|
250 260
....*....|....*....|
gi 489912973 233 -ADRIVVMNRGDLTETGTRD 251
Cdd:COG0396 207 kPDFVHVLVDGRIVKSGGKE 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
303-523 |
5.35e-21 |
|
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: 96.65 E-value: 5.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 303 GATRTVVAASevdLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMllgetdiaRLSGAGLRPLRRkvqivfqdpy 382
Cdd:TIGR01842 329 GKKPTLRGIS---FSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV--------RLDGADLKQWDR---------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 383 RSLNPRraVGE----------SIIEGLLNFG-MPRAQALVRAARTLGVvglgPDVMRRYPHQF-----------SGGQRQ 440
Cdd:TIGR01842 388 ETFGKH--IGYlpqdvelfpgTVAENIARFGeNADPEKIIEAAKLAGV----HELILRLPDGYdtvigpggatlSGGQRQ 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 441 RLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVcDTIAVMQHGKVVETGAAQT 520
Cdd:TIGR01842 462 RIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCV-DKILVLQDGRIARFGERDE 539
|
...
gi 489912973 521 VLT 523
Cdd:TIGR01842 540 VLA 542
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
314-525 |
6.99e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.49 E-value: 6.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIarlSGAGLRPLRRKVQIVFQDPYRSLNPRrAVGE 393
Cdd:PRK13647 24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREV---NAENEKWVRSKVGLVFQDPDDQVFSS-TVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEGLLNFGMPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVL 473
Cdd:PRK13647 100 DVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489912973 474 ELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGaAQTVLTRP 525
Cdd:PRK13647 179 EILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDE 228
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
17-281 |
8.07e-21 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 92.05 E-value: 8.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGILEVSGGSARV--LGEDIvtasarr 94
Cdd:PRK11247 13 LLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLaeAREDT------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 rrelratrmAMVFQEpmTALNPVHRVgsqVDEV-LRLhrrmpRAQRRAKVLEMFRSVHLPDveRIYDaYPHQLSGGQRQR 173
Cdd:PRK11247 84 ---------RLMFQD--ARLLPWKKV---IDNVgLGL-----KGQWRDAALQALAAVGLAD--RANE-WPAALSGGQKQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 174 IVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDei 253
Cdd:PRK11247 142 VALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVD-- 219
|
250 260 270
....*....|....*....|....*....|....*...
gi 489912973 254 LARPSQNYTRRL----------VSSVPSLVPTQREAPG 281
Cdd:PRK11247 220 LPRPRRRGSARLaeleaevlqrVMSRGESEPTRLRWAG 257
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-256 |
1.20e-20 |
|
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: 91.01 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKS-VTSLAVMGLLPEgilevsggSARVL--GEDIVTASAR 93
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKStLTKLIQRFYVPE--------NGRVLvdGHDLALADPA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 RRRELratrMAMVFQEPMTALNPVHRVGSQVDEVLRLHRrMPRAQRRAKVLEMFRsvHLPD-VERIYDAYPHQLSGGQRQ 172
Cdd:cd03252 73 WLRRQ----VGVVLQENVLFNRSIRDNIALADPGMSMER-VIEAAKLAGAHDFIS--ELPEgYDTIVGEQGAGLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 173 RIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqtAVLFITHDFGVVAEiADRIVVMNRGDLTETGTRDE 252
Cdd:cd03252 146 RIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDE 222
|
....
gi 489912973 253 ILAR 256
Cdd:cd03252 223 LLAE 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-269 |
1.98e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 91.06 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 18 AIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL---PEGILEvsgGSARVLGEDIVTASARR 94
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelnEEARVE---GEVRLFGRNIYSPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 RRELRAtrMAMVFQEP-----MTALNPVhRVGSQVDEVLR----LHRRMPRAQRRAKVLEMFRsvhlpdvERIYDaYPHQ 165
Cdd:PRK14267 81 IEVRRE--VGMVFQYPnpfphLTIYDNV-AIGVKLNGLVKskkeLDERVEWALKKAALWDEVK-------DRLND-YPSN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqtAVLFITHDFGVVAEIADRIVVMNRGDLT 245
Cdd:PRK14267 150 LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
250 260
....*....|....*....|....
gi 489912973 246 ETGTRDEILARPSQNYTRRLVSSV 269
Cdd:PRK14267 228 EVGPTRKVFENPEHELTEKYVTGA 251
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
314-513 |
1.98e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 90.92 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaglrPLRRKVQI--VFQDPYRSLNPRRAV 391
Cdd:COG1101 25 LNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-----EYKRAKYIgrVFQDPMMGTAPSMTI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GEsiiegllNFGMpraqALVRAARTlgvvGLGPDVMRRYPHQF----------------------SGGQRQRLciarALV 449
Cdd:COG1101 100 EE-------NLAL----AYRRGKRR----GLRRGLTKKRRELFrellatlglglenrldtkvgllSGGQRQAL----SLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 450 M----DPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVV 513
Cdd:COG1101 161 MatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
33-248 |
2.02e-20 |
|
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: 89.73 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIVTASARRRRELRATRMAMVFQEPMT 112
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLL-----EPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 113 ALNPVHRVGsqvdevlRLHRrMPRAQRRAKVLEMFRSVhlpDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEP 192
Cdd:cd03266 95 ARENLEYFA-------GLYG-LKGDELTARLEELADRL---GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 193 TTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
17-248 |
2.15e-20 |
|
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: 89.56 E-value: 2.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVcVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVtasarRRR 96
Cdd:cd03264 1 LQLENLTKRY--GKKRALDGVSLTLGPGMYG-LLGPNGAGKT-TLMRILA----TLTPPSSGTIRIDGQDVL-----KQP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEPMTalNPVHRVGSQVDEVLRLHRrMPRAQRRAKVLEMFRSVHLPDVeriYDAYPHQLSGGQRQRIVI 176
Cdd:cd03264 68 QKLRRRIGYLPQEFGV--YPNFTVREFLDYIAWLKG-IPSKEVKARVDEVLELVNLGDR---AKKKIGSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIREL-QDRhqtAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELgEDR---IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
316-522 |
2.19e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.00 E-value: 2.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 316 LTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGaglRPLRRKVQIVFQD--PYRSLNPRR--AV 391
Cdd:PRK10575 32 LTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS---KAFARKVAYLPQQlpAAEGMTVRElvAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIIEGLLnfGMPRAQALVRAARTLGVVGLGPdVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:PRK10575 109 GRYPWHGAL--GRFGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489912973 472 VLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVL 522
Cdd:PRK10575 186 VLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-257 |
3.03e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 91.84 E-value: 3.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 3 YAPYPPAGDTsaaVLAIRNLSVSVCGAGN---RVVRNLSLDVHAGETVCVVGESGSGKS--VTSLavmgllpEGILEVSG 77
Cdd:PRK13631 11 KVPNPLSDDI---ILRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKStlVTHF-------NGLIKSKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 78 GSARVlgEDIVTASARRRRELRAT--------------RMAMVFQEPMTAL-----------NPVhrvgsqvdeVLRLHR 132
Cdd:PRK13631 81 GTIQV--GDIYIGDKKNNHELITNpyskkiknfkelrrRVSMVFQFPEYQLfkdtiekdimfGPV---------ALGVKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 133 RMPRaQRRAKVLEMFrSVHLPDVERiydaYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQ 212
Cdd:PRK13631 150 SEAK-KLAKFYLNKM-GLDDSYLER----SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489912973 213 DRHQTaVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:PRK13631 224 ANNKT-VFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
38-248 |
4.01e-20 |
|
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: 88.76 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 38 SLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTASARRRRelratrMAMVFQEP--MTALN 115
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKS-TLLNLIA----GFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENnlFAHLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 116 PVHRVGSQVDEVLRLHrrmprAQRRAKVLEMFRSVHLPDverIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTA 195
Cdd:TIGR01277 87 VRQNIGLGLHPGLKLN-----AEQQEKVVDAAQQVGIAD---YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489912973 196 LDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:TIGR01277 159 LDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-246 |
4.78e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 89.07 E-value: 4.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVcGAGNRVVRNLS---LDVHAGETVCVVGESGSGKSvTSLAVMGLLPEGilevSGGSARVLGEDIVTASA 92
Cdd:PRK10584 6 IVEVHHLKKSV-GQGEHELSILTgveLVVKRGETIALIGESGSGKS-TLLAILAGLDDG----SSGEVSLVGQPLHQMDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 93 RRRRELRATRMAMVFQEPM--TALNPVHRVgsqvdEVLRLHRRMPRAQRRAKVLEMFRSVHLPdvERIyDAYPHQLSGGQ 170
Cdd:PRK10584 80 EARAKLRAKHVGFVFQSFMliPTLNALENV-----ELPALLRGESSRQSRNGAKALLEQLGLG--KRL-DHLPAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 171 RQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNrGDLTE 246
Cdd:PRK10584 152 QQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVN-GQLQE 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
314-531 |
4.94e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 94.42 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLsgaGLRPLRRKVQIVFQDPYrslnprravge 393
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDLRKVLGIIPQAPV----------- 1323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 sIIEGLLNFGM-PRAQ--------ALVRAARTlgvvglgpDVMRRYP-----------HQFSGGQRQRLCIARALVMDPE 453
Cdd:PLN03130 1324 -LFSGTVRFNLdPFNEhndadlweSLERAHLK--------DVIRRNSlgldaevseagENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 454 VLVADEAVSALDVSVQAQVLELIEQvrERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLTRPGHAYTR 531
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGSAFSK 1469
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
286-516 |
5.37e-20 |
|
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: 89.31 E-value: 5.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAER----------RSLF-GATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRmll 354
Cdd:cd03267 1 IEVSNLSKSYRVYskepgligslKSLFkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 355 getdiarLSGAGLRPLRRKVQIVFQ---------------DPYRSLNPRRAVgesiiegllnFGMPRAQALVRAARTLGV 419
Cdd:cd03267 78 -------VRVAGLVPWKRRKKFLRRigvvfgqktqlwwdlPVIDSFYLLAAI----------YDLPPARFKKRLDELSEL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 420 VGLGPdVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQ 499
Cdd:cd03267 141 LDLEE-LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEA 219
|
250
....*....|....*..
gi 489912973 500 VCDTIAVMQHGKVVETG 516
Cdd:cd03267 220 LARRVLVIDKGRLLYDG 236
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
36-244 |
5.55e-20 |
|
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: 88.62 E-value: 5.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 36 NLSLDVHAGETVCVVGESGSGKSvtslAVMGLLpEGILEVSGGSARVLGEDiVTASARRRRELRATRMAMVFQEpmTALN 115
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKS----TLLKLI-YKEELPTSGTIRVNGQD-VSDLRGRAIPYLRRKIGVVFQD--FRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 116 PVHRVGSQVDEVLRLHRRMPRAQRRaKVLEMFRSVHLPDVERiydAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTA 195
Cdd:cd03292 91 PDRNVYENVAFALEVTGVPPREIRK-RVPAALELVGLSHKHR---ALPAELSGGEQQRVAIARAIVNSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489912973 196 LDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDL 244
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTT-VVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
310-529 |
6.77e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 93.16 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYR-----S 384
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT---LASLRNQVALVSQNVHLfndtiA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 385 LNPRRAVGESiiegllnfgMPRAQaLVRAARtlgvVGLGPDVMRRYPHQF-----------SGGQRQRLCIARALVMDPE 453
Cdd:PRK11176 435 NNIAYARTEQ---------YSREQ-IEEAAR----MAYAMDFINKMDNGLdtvigengvllSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 454 VLVADEAVSALDV----SVQAQVLELieqVRERTgvsVLFITHDLRVAAQVcDTIAVMQHGKVVETGAAQTVLTRPGhAY 529
Cdd:PRK11176 501 ILILDEATSALDTeserAIQAALDEL---QKNRT---SLVIAHRLSTIEKA-DEILVVEDGEIVERGTHAELLAQNG-VY 572
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
165-494 |
8.37e-20 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 92.95 E-value: 8.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqtAVLFITHDFGVVAEIADRIVVM----- 239
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEHDLAVLDYLADNVHIAygepg 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 240 NRGDLTET-GTRDEI-------LarPSQNYTRRlVSSVPSLVPTQREAPGGEPVLRITGLGRTYaerrslfGATRTVVAA 311
Cdd:PRK13409 290 AYGVVSKPkGVRVGIneylkgyL--PEENMRIR-PEPIEFEERPPRDESERETLVEYPDLTKKL-------GDFSLEVEG 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVdltlRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLgETDIArlsgagLRP--LRRKVQIVFQDPYRSLNPRr 389
Cdd:PRK13409 360 GEI----YEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKIS------YKPqyIKPDYDGTVEDLLRSITDD- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 aVGESIIEGLLnfgmpraqalvraARTLGVvglgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:PRK13409 428 -LGSSYYKSEI-------------IKPLQL----ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 489
|
330 340
....*....|....*....|....*
gi 489912973 470 AQVLELIEQVRERTGVSVLFITHDL 494
Cdd:PRK13409 490 LAVAKAIRRIAEEREATALVVDHDI 514
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
30-512 |
8.49e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 92.37 E-value: 8.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMgllpEGILEVSGGSARVLGEDIVtasARRRRELRATRMAMVFQE 109
Cdd:PRK10762 16 GVKALSGAALNVYPGRVMALVGENGAGKS-TMMKVL----TGIYTRDAGSILYLGKEVT---FNGPKSSQEAGIGIIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 pmtaLN----------------PVHRVGSqVDevlrlHRRM-PRAQRRAKVLEMFRSVHLPDVEriydayphqLSGGQRQ 172
Cdd:PRK10762 88 ----LNlipqltiaeniflgreFVNRFGR-ID-----WKKMyAEADKLLARLNLRFSSDKLVGE---------LSIGEQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 173 RIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVlFITHDFGVVAEIADRIVVMNRG---------D 243
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIV-YISHRLKEIFEICDDVTVFRDGqfiaerevaD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 244 LTETGTRDEILArpsqnytRRLVSSVPSLvptqrEAPGGEPVLRITGlgrtyaerrsLFGAtrtvvAASEVDLTLRRGEI 323
Cdd:PRK10762 228 LTEDSLIEMMVG-------RKLEDQYPRL-----DKAPGEVRLKVDN----------LSGP-----GVNDVSFTLRKGEI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 324 LGIVGESGSGKSTVARCIVRLIEPSAGRMLL-GETDIARLSGAGLrplrrKVQIVfqdpYRSLNPRR---AVGESIIEGL 399
Cdd:PRK10762 281 LGVSGLMGAGRTELMKVLYGALPRTSGYVTLdGHEVVTRSPQDGL-----ANGIV----YISEDRKRdglVLGMSVKENM 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 400 ----LNFGMPRAQALVRAARTLGVVglgpDVMR----RYPHQ------FSGGQRQRLCIARALVMDPEVLVADEAVSALD 465
Cdd:PRK10762 352 sltaLRYFSRAGGSLKHADEQQAVS----DFIRlfniKTPSMeqaiglLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 489912973 466 VSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:PRK10762 428 VGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
36-281 |
9.35e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 89.50 E-value: 9.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 36 NLSLDVHAGETVCVVGESGSGKSvtslAVMGLLpEGILEVSGGSARVLGEDIVTASARRRRELRATRMAMVFQEPMTAL- 114
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKS----TLMQHF-NALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPEAQLf 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 115 -NPVhrvgsqVDEVLRLHRRMPRAQRRAK--VLEMFRSVHLPdvERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADE 191
Cdd:PRK13641 100 eNTV------LKDVEFGPKNFGFSEDEAKekALKWLKKVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 192 PTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARPSQNYTRRLVSSVPS 271
Cdd:PRK13641 172 PAAGLDPEGRKEMMQLFKDYQKAGHTVIL-VTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWLKKHYLDEPATS 250
|
250
....*....|
gi 489912973 272 LVPTQREAPG 281
Cdd:PRK13641 251 RFASKLEKGG 260
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
35-492 |
1.01e-19 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 92.39 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 35 RNLSLD---VHAGETVCVVGESGSGKSVTSLAVMGLLP--EG--------ILEVSGGSARVLGEDIvtasarrrrelrat 101
Cdd:PRK10938 17 KTLQLPsltLNAGDSWAFVGANGSGKSALARALAGELPllSGerqsqfshITRLSFEQLQKLVSDE-------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 102 rmamvFQEPMTALNPVHR--VGSQVDEVLRLHRRMPraQRRAKVLEMFRSVHLPDVERIYdayphqLSGGQRQRIVIAMA 179
Cdd:PRK10938 83 -----WQRNNTDMLSPGEddTGRTTAEIIQDEVKDP--ARCEQLAQQFGITALLDRRFKY------LSTGETRKTLLCQA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 180 LILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARP-- 257
Cdd:PRK10938 150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL-VLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQAlv 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 258 SQ-NYTRRLV-SSVP-SLVPTQREA-PGGEPVLRITGLGRTYAERRSLFGATRTVvaasevdltlRRGEILGIVGESGSG 333
Cdd:PRK10938 229 AQlAHSEQLEgVQLPePDEPSARHAlPANEPRIVLNNGVVSYNDRPILHNLSWQV----------NPGEHWQIVGPNGAG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 334 KSTvarcIVRLI---EP---SAGRMLLGETdiaRLSGAGLRPLRRKVQIV---FQDPYRSLNPRRAVgesIIEGLLN-FG 403
Cdd:PRK10938 299 KST----LLSLItgdHPqgySNDLTLFGRR---RGSGETIWDIKKHIGYVsssLHLDYRVSTSVRNV---ILSGFFDsIG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 404 MPRA-----QALvrAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQ 478
Cdd:PRK10938 369 IYQAvsdrqQKL--AQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDV 446
|
490
....*....|....
gi 489912973 479 VRERTGVSVLFITH 492
Cdd:PRK10938 447 LISEGETQLLFVSH 460
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
253-526 |
1.02e-19 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 92.47 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 253 ILARPSQNYTR--RLVSSVPSLVPTQREAPGGEPVLRITGLGRTYAerrslfGATRTVVaaSEVDLTLRRGEILGIVGES 330
Cdd:PRK10789 279 IVERGSAAYSRirAMLAEAPVVKDGSEPVPEGRGELDVNIRQFTYP------QTDHPAL--ENVNFTLKPGQMLGICGPT 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 331 GSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYrslnprraVGESIIEGLLNFGMPRA--Q 408
Cdd:PRK10789 351 GSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSRLAVVSQTPF--------LFSDTVANNIALGRPDAtqQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 409 ALVRAARTLGVvglgPDVMRRYPHQF-----------SGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIE 477
Cdd:PRK10789 420 EIEHVARLASV----HDDILRLPQGYdtevgergvmlSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLR 495
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489912973 478 QVRErtGVSVLFITHDLRvAAQVCDTIAVMQHGKVVETGAAQTVLTRPG 526
Cdd:PRK10789 496 QWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
17-272 |
2.21e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 2.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVsvcGAGN-RVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-PE-GILEVSGG-----SARVLGEDIv 88
Cdd:PRK11231 3 LRTENLTV---GYGTkRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQsGTVFLGDKpismlSSRQLARRL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 89 tasarrrrelratrmAMVFQEPMTAlnpvhrVGSQVDEV--------LRLHRRMPRA--QRRAKVLEMFRSVHLPDvERI 158
Cdd:PRK11231 79 ---------------ALLPQHHLTP------EGITVRELvaygrspwLSLWGRLSAEdnARVNQAMEQTRINHLAD-RRL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 159 YDayphqLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVV 238
Cdd:PRK11231 137 TD-----LSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKT-VVTVLHDLNQASRYCDHLVV 210
|
250 260 270
....*....|....*....|....*....|....
gi 489912973 239 MNRGDLTETGTRDEILarpsqnyTRRLVSSVPSL 272
Cdd:PRK11231 211 LANGHVMAQGTPEEVM-------TPGLLRTVFDV 237
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
280-524 |
2.49e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.71 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 280 PGGEPVLRITGLGRTYAERrslfgatrTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGR-MLLGETD 358
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDK--------LVV--DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSiSLCGEPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 359 IARLSGAglrplRRKVQIVFQdpYRSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRRYpHQFSGGQ 438
Cdd:PRK13537 72 PSRARHA-----RQRVGVVPQ--FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKV-GELSGGM 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 439 RQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAA 518
Cdd:PRK13537 144 KRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
....*.
gi 489912973 519 QTVLTR 524
Cdd:PRK13537 223 HALIES 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
19-254 |
2.76e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 87.45 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 19 IRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLpegiLEVSGGSARVLGEDIVTASARRRREL 98
Cdd:COG4604 4 IKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKS-TLLSMISRL----LPPDSGEVLVDGLDVATTPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 99 ratrMAMVFQEPMTalnpvhrvgsqvdeVLRL-------------HRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQ 165
Cdd:COG4604 77 ----LAILRQENHI--------------NSRLtvrelvafgrfpySKGRLTAEDREIIDEAIAYLDLEDLA---DRYLDE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLT 245
Cdd:COG4604 136 LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVV 215
|
....*....
gi 489912973 246 ETGTRDEIL 254
Cdd:COG4604 216 AQGTPEEII 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-255 |
3.00e-19 |
|
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: 90.87 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLAVMGLlpeGILEVSGGSARVLGEDIVTASARRR 95
Cdd:TIGR01842 316 HLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKS--TLARLIV---GIWPPTSGSVRLDGADLKQWDRETF 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRATRMAMVFQEPMTALNPVHRVGSQVDEvlrlhRRMPRAQRRAKVLEMFRSvhLPDVeriYDAY----PHQLSGGQR 171
Cdd:TIGR01842 391 GKHIGYLPQDVELFPGTVAENIARFGENADP-----EKIIEAAKLAGVHELILR--LPDG---YDTVigpgGATLSGGQR 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 172 QRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVaEIADRIVVMNRGDLTETGTRD 251
Cdd:TIGR01842 461 QRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGIT-VVVITHRPSLL-GCVDKILVLQDGRIARFGERD 538
|
....
gi 489912973 252 EILA 255
Cdd:TIGR01842 539 EVLA 542
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
38-255 |
3.26e-19 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 86.94 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 38 SLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDivtasaRRRRELRATRMAMVFQEP--MTALN 115
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKS-TLLNLIA----GFLTPASGSLTLNGQD------HTTTPPSRRPVSMLFQENnlFSHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 116 PVHRVGSQVDEVLRLHrrmprAQRRAKVLEMFRSVHLPD-VERIydayPHQLSGGQRQRIVIAMALILEPKLLIADEPTT 194
Cdd:PRK10771 88 VAQNIGLGLNPGLKLN-----AAQREKLHAIARQMGIEDlLARL----PGQLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 195 ALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILA 255
Cdd:PRK10771 159 ALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
274-529 |
3.71e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.04 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 274 PTQREAPGGEPVLRITGLGRTYAERRSLfgatrtvvAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRML 353
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFTYPDQPQP--------VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 354 LGETDIARLSGAGLRP----LRRKVQIvFQDPYRSlNPRRAVGESIIEGLLnfgmpraQALVRaartlgvVGLGPDVMRR 429
Cdd:PRK11160 399 LNGQPIADYSEAALRQaisvVSQRVHL-FSATLRD-NLLLAAPNASDEALI-------EVLQQ-------VGLEKLLEDD 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 430 YP---------HQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQV-RERTgvsVLFITHDLRVAAQ 499
Cdd:PRK11160 463 KGlnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaQNKT---VLMITHRLTGLEQ 539
|
250 260 270
....*....|....*....|....*....|
gi 489912973 500 VcDTIAVMQHGKVVETGAAQTVLTRPGHAY 529
Cdd:PRK11160 540 F-DRICVMDNGQIIEQGTHQELLAQQGRYY 568
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
149-242 |
3.81e-19 |
|
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: 84.04 E-value: 3.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 149 SVHLPDVERIydAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTqkqILALIRELQDrHQTAVLFITHDFGV 228
Cdd:cd03221 56 IVTWGSTVKI--GYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES---IEALEEALKE-YPGTVILVSHDRYF 129
|
90
....*....|....
gi 489912973 229 VAEIADRIVVMNRG 242
Cdd:cd03221 130 LDQVATKIIELEDG 143
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
314-514 |
5.37e-19 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 85.99 E-value: 5.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGR-MLLGEtDIARLSGAGLRPLR-RKVQIVFQD----PyrSLNP 387
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEvSLVGQ-PLHQMDEEARAKLRaKHVGFVFQSfmliP--TLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 388 RRAVGesiIEGLLNfGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVS 467
Cdd:PRK10584 106 LENVE---LPALLR-GESSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQ 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489912973 468 VQAQVLELIEQVRERTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVE 514
Cdd:PRK10584 181 TGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
32-255 |
5.78e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.37 E-value: 5.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSVtslavMGLLPEGILEVSGGSARVLGEDI-VTASARRRRELRATRMAMVFQEP 110
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKST-----MIQLTNGLIISETGQTIVGDYAIpANLKKIKEVKRLRKEIGLVFQFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 111 M-----------TALNPVHrVGSQVDEVLRlhrrmpraqrraKVLEMFRSVHLPdvERIYDAYPHQLSGGQRQRIVIAMA 179
Cdd:PRK13645 100 EyqlfqetiekdIAFGPVN-LGENKQEAYK------------KVPELLKLVQLP--EDYVKRSPFELSGGQKRRVALAGI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 180 LILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILA 255
Cdd:PRK13645 165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-248 |
6.06e-19 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 84.67 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAvmglLPEGILEVSGGSARVLGEDIVTAsarrrr 96
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKS-TLLQ----LLTGDLKPQQGEITLDGVPVSDL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 elratrmamvfqepmtalnpvhrvgsqvdevlrlhrrmpRAQRRAKVLEMFRSVHLPDVErIYDAYPHQLSGGQRQRIVI 176
Cdd:cd03247 70 ---------------------------------------EKALSSLISVLNQRPYLFDTT-LRNNLGRRFSGGERQRLAL 109
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRE-LQDRhqtAVLFITHDFGVVaEIADRIVVMNRGDLTETG 248
Cdd:cd03247 110 ARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEvLKDK---TLIWITHHLTGI-EHMDKILFLENGKIIMQG 178
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
165-506 |
6.63e-19 |
|
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: 90.23 E-value: 6.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVttqKQILA---LIRELQDRHqTAVLFITHDFGVVAEIADRIVVMN- 240
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI---YQRLNvarLIRELAEEG-KYVLVVEHDLAILDYLADYVHILYg 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 241 ----RGDLTET-GTRDEI-------LarPSQNYTRRlVSSVPSLVPTQREAPGGEPVLRITGLGRTYAErrslFgatRTV 308
Cdd:COG1245 288 epgvYGVVSKPkSVRVGInqyldgyL--PEENVRIR-DEPIEFEVHAPRREKEEETLVEYPDLTKSYGG----F---SLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVdltlRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMllgETDIaRLSgagLRP--LRRKVQIVFQDPYRSLN 386
Cdd:COG1245 358 VEGGEI----REGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDL-KIS---YKPqyISPDYDGTVEEFLRSAN 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 PRRaVGESIIEGLLnfgmpraqalvraARTLGVvglgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDV 466
Cdd:COG1245 427 TDD-FGSSYYKTEI-------------IKPLGL----EKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 489912973 467 SVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAV 506
Cdd:COG1245 489 EQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
273-494 |
7.75e-19 |
|
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: 89.73 E-value: 7.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 273 VPTQREAPGGEPVLRITGLGRTYAerrslfGATRtvvAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRM 352
Cdd:TIGR02868 322 APAAGAVGLGKPTLELRDLSAGYP------GAPP---VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 353 LLGETDIARLSGAglrPLRRKVQIVFQDPYrslnprraVGESIIEGLLNFGMPRA--QALVRAARTlgvVGLGPDVmRRY 430
Cdd:TIGR02868 393 TLDGVPVSSLDQD---EVRRRVSVCAQDAH--------LFDTTVRENLRLARPDAtdEELWAALER---VGLADWL-RAL 457
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 431 PH-----------QFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRErtGVSVLFITHDL 494
Cdd:TIGR02868 458 PDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
288-513 |
9.20e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.45 E-value: 9.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 288 ITGLGRTY--AERRSLFGAT---------RTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRmllge 356
Cdd:COG4586 4 VENLSKTYrvYEKEPGLKGAlkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGE----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 357 tdiarLSGAGLRPLRRKV----QI--VF------------QDPYRsLNprRAVgesiiegllnFGMPRAQALVRAARTLG 418
Cdd:COG4586 79 -----VRVLGYVPFKRRKefarRIgvVFgqrsqlwwdlpaIDSFR-LL--KAI----------YRIPDAEYKKRLDELVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 419 VVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAA 498
Cdd:COG4586 141 LLDLG-ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIE 219
|
250
....*....|....*
gi 489912973 499 QVCDTIAVMQHGKVV 513
Cdd:COG4586 220 ALCDRVIVIDHGRII 234
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
37-248 |
1.15e-18 |
|
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: 84.85 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 37 LSLDVHAGETVCVVGESGSGKSvTSLAvmglLPEGILEVSGGSARVLGEDIVTASARRRRelratrMAMVFQEP--MTAL 114
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKS-TLLN----LIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENnlFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 115 NPVHRVGSQVDEVLRLhrrmpRAQRRAKVLEMFRSVHLPDVERiydAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTT 194
Cdd:cd03298 86 TVEQNVGLGLSPGLKL-----TAEDRQAIEVALARVGLAGLEK---RLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 195 ALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
30-257 |
1.71e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 85.56 E-value: 1.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVmgllpEGILEVSGGSARVLGEDIvtasARRRRELRATRMAMVFQE 109
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHL-----NGIYLPQRGRVKVMGREV----NAENEKWVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 P------MT-----ALNPVHrVGSQVDEVLRlhrrmpRAQRRAKVLEMFRSVHLPdveriydayPHQLSGGQRQRIVIAM 178
Cdd:PRK13647 88 PddqvfsSTvwddvAFGPVN-MGLDKDEVER------RVEEALKAVRMWDFRDKP---------PYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 179 ALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDLTETGTRdEILARP 257
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKT-VIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDE 228
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
33-257 |
2.67e-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: 88.46 E-value: 2.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLP--EGILEVSGGSARVLGEDIVTASarrrrelratrMAMVFQEp 110
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQpwSGEILFDGIPREEIPREVLANS-----------VAMVDQD- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 111 mtalnpVHRVGSQVDEVLRL------HRRMPRAQRRAKVLEmfrsvhlpDVERIYDAYPHQL-------SGGQRQRIVIA 177
Cdd:TIGR03796 562 ------IFLFEGTVRDNLTLwdptipDADLVRACKDAAIHD--------VITSRPGGYDAELaegganlSGGQRQRLEIA 627
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 178 MALILEPKLLIADEPTTALDVTTQKQILALIRelqdRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEILARP 257
Cdd:TIGR03796 628 RALVRNPSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
308-524 |
2.76e-18 |
|
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: 87.94 E-value: 2.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 308 VVAASEVDLTLRRGEILGIVGESGSGKST---------------------VARC--IVRLIEPS---------AGRMLLG 355
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVlmhvlrgmdqyeptsgriiyhVALCekCGYVERPSkvgepcpvcGGTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 356 ETDIARLSGAGLRPLRRKVQIVFQDPYrSLNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDVMRrYPHQFS 435
Cdd:TIGR03269 93 EVDFWNLSDKLRRRIRKRIAIMLQRTF-ALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITH-IARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 436 GGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVET 515
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE 250
|
....*....
gi 489912973 516 GAAQTVLTR 524
Cdd:TIGR03269 251 GTPDEVVAV 259
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
29-239 |
2.92e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.05 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 29 AGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVtasarrrrelratrmAMVFQ 108
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKS-TLLKVLA----GVLRPTSGTVRRAGGARV---------------AYVPQ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 E-------PMTalnpvhrvgsqVDEVLRLHR-------RMPRAQRRAKVLEMFRSVHLPDVERiydAYPHQLSGGQRQRI 174
Cdd:NF040873 63 RsevpdslPLT-----------VRDLVAMGRwarrglwRRLTRDDRAAVDDALERVGLADLAG---RQLGELSGGQRQRA 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 175 VIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEiADRIVVM 239
Cdd:NF040873 129 LLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRR-ADPCVLL 191
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
12-224 |
2.97e-18 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 87.94 E-value: 2.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSVSvCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSL--AVMGLLPEGilevSGGSARVLGEDivt 89
Cdd:COG4178 358 SEDGALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKS--TLlrAIAGLWPYG----SGRIARPAGAR--- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 90 asarrrrelratrMAMVFQEPMTALnpvhrvGSqVDEVL---RLHRRMPRAQRRAkVLEMfrsVHLPD-VERIYDAYP-- 163
Cdd:COG4178 428 -------------VLFLPQRPYLPL------GT-LREALlypATAEAFSDAELRE-ALEA---VGLGHlAERLDEEADwd 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 164 HQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIR-ELQDrhqTAVLFITH 224
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLReELPG---TTVISVGH 542
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
314-516 |
3.02e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.96 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRL--IEPSAGRMLLGETDIARLSgAGLRPlRRKVQIVFQDPYRslnprrav 391
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLP-PEERA-RLGIFLAFQYPPE-------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 gesiIEGllnfgmpraqalVRAARTLGVVGLGpdvmrryphqFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:cd03217 89 ----IPG------------VKNADFLRYVNEG----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489912973 472 VLELIEQVRERtGVSVLFITHDLRVAAQV-CDTIAVMQHGKVVETG 516
Cdd:cd03217 143 VAEVINKLREE-GKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
302-520 |
3.77e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.29 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGAtrtVVAASEVDLTLRRGEILGIVGESGSGKSTVARcIVRLIEPSA---GRMLL-GETDIARlsgaGLRPLRRK-VQI 376
Cdd:PRK13549 15 FGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHGtyeGEIIFeGEELQAS----NIRDTERAgIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 377 VFQDpyRSLNPRRAVGESIIEG--LLNFG-MPRAQALVRAARTLGVVGLGPDVMRRYPHqFSGGQRQRLCIARALVMDPE 453
Cdd:PRK13549 87 IHQE--LALVKELSVLENIFLGneITPGGiMDYDAMYLRAQKLLAQLKLDINPATPVGN-LGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 454 VLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQT 520
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAG 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-248 |
4.12e-18 |
|
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: 83.47 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGilevsggsARVLGEdivtasarrrrelratrmAMVFQEPM 111
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGG--------GTTSGQ------------------ILFNGQPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 TALNPVHRVG--SQVDE---------------VLRLHRRMPRAQRRaKVLEMFRSVHLPDvERIYDAYPHQLSGGQRQRI 174
Cdd:cd03234 75 KPDQFQKCVAyvRQDDIllpgltvretltytaILRLPRKSSDAIRK-KRVEDVLLRDLAL-TRIGGNLVKGISGGERRRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 175 VIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
28-256 |
4.13e-18 |
|
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: 87.87 E-value: 4.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 28 GAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGILEVSGGSARVLGEDIVTASARrrrelratrMAMVF 107
Cdd:TIGR01193 484 GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF---------INYLP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 108 QEPMTAlnpvhrVGSQVDEVLRlhrrmpRAQRRAKVLEMFRSVHLP----DVERIYDAYPHQL-------SGGQRQRIVI 176
Cdd:TIGR01193 555 QEPYIF------SGSILENLLL------GAKENVSQDEIWAACEIAeikdDIENMPLGYQTELseegssiSGGQKQRIAL 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhqtAVLFITHDFGvVAEIADRIVVMNRGDLTETGTRDEILAR 256
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
13-267 |
5.14e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 83.67 E-value: 5.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 13 SAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKS--VTSLAVMG-LLPEGILEvsgGSARVLGEDIVT 89
Cdd:PRK14239 2 TEPILQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKStlLRSINRMNdLNPEVTIT---GSIVYNGHNIYS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 90 ASARRRRELRAtrMAMVFQEPmtalNPV-HRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPD--VERIYDAyPHQL 166
Cdd:PRK14239 77 PRTDTVDLRKE--IGMVFQQP----NPFpMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDevKDRLHDS-ALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELqdRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTE 246
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISDRTGFFLDGDLIE 227
|
250 260
....*....|....*....|.
gi 489912973 247 TGTRDEILARPSQNYTRRLVS 267
Cdd:PRK14239 228 YNDTKQMFMNPKHKETEDYIS 248
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
309-522 |
5.15e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.27 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRM-LLGETDIARLsgaglRPLRRKVQIVFQ----DP-- 381
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGVPVPARA-----RLARARIGVVPQfdnlDLef 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 -----------YRSLNPRRAvgESIIEGLLNFGMPRAQALVRAArtlgvvglgpdvmrryphQFSGGQRQRLCIARALVM 450
Cdd:PRK13536 130 tvrenllvfgrYFGMSTREI--EAVIPSLLEFARLESKADARVS------------------DLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 451 DPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVL 522
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
32-253 |
6.88e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 84.03 E-value: 6.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSvtslAVMGLLpEGILEVSGGSARVLGEDIVTASARRRRELRATRMAMVFQEPM 111
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKS----TIMQLL-NGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQFPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 ------TALNPV----HRVGSQVDEVLRLHRrmpraqrrakvlEMFRSVHLPdvERIYDAYPHQLSGGQRQRIVIAMALI 181
Cdd:PRK13649 96 sqlfeeTVLKDVafgpQNFGVSQEEAEALAR------------EKLALVGIS--ESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 182 LEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTETGTRDEI 253
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVL-VTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
35-256 |
9.27e-18 |
|
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: 86.41 E-value: 9.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 35 RNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDI--VTASARRRRelratrMAMVFQEPM- 111
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY-----DVTSGRILIDGQDIrdVTQASLRAA------IGIVPQDTVl 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 ---TALNPVH--RVGSQVDEVLRlhrrmprAQRRAKVLEMFRSvhLPD-----V-ERIYdayphQLSGGQRQRIVIAMAL 180
Cdd:COG5265 444 fndTIAYNIAygRPDASEEEVEA-------AARAAQIHDFIES--LPDgydtrVgERGL-----KLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 181 ILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTavLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEILAR 256
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQAALREVARGRTT--LVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLAQ 582
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
17-258 |
1.03e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 85.28 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGilevsGGSARVLGEDIvtasARRRR 96
Cdd:PRK09536 4 IDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-----AGTVLVAGDDV----EALSA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEPMTALNPVHRvgsQVDEVLRL-HR----RMPRAQRRAKVLEMFRSvhlpDVERIYDAYPHQLSGGQR 171
Cdd:PRK09536 73 RAASRRVASVPQDTSLSFEFDVR---QVVEMGRTpHRsrfdTWTETDRAAVERAMERT----GVAQFADRPVTSLSGGER 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 172 QRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFItHDFGVVAEIADRIVVMNRGDLTETGTRD 251
Cdd:PRK09536 146 QRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPA 224
|
....*..
gi 489912973 252 EILARPS 258
Cdd:PRK09536 225 DVLTADT 231
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
30-256 |
1.73e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 82.97 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVmgllpEGILEVSGGsaRVLGEDIVTASARRRRELRATRMAMVFQE 109
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNL-----NGILKPSSG--RILFDGKPIDYSRKGLMKLRESVGMVFQD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 PMTAL-----------NPVHrVGSQVDEVlrlHRRMPRAQRRAkvlemfrsvhlpDVERIYDAYPHQLSGGQRQRIVIAM 178
Cdd:PRK13636 91 PDNQLfsasvyqdvsfGAVN-LKLPEDEV---RKRVDNALKRT------------GIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 179 ALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILAR 256
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
15-255 |
2.20e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 81.86 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEgilevSGGSARVLGEDIvtaSARR 94
Cdd:PRK10895 2 ATLTAKNLAKAY--KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPR-----DAGNIIIDDEDI---SLLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 RRELRATRMAMVFQEPmtalnPVHRVGSQVDE---VLRLHRRMPRAQRRAKVLEMFRSVHlpdVERIYDAYPHQLSGGQR 171
Cdd:PRK10895 72 LHARARRGIGYLPQEA-----SIFRRLSVYDNlmaVLQIRDDLSAEQREDRANELMEEFH---IEHLRDSMGQSLSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 172 QRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRD 251
Cdd:PRK10895 144 RRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPT 222
|
....
gi 489912973 252 EILA 255
Cdd:PRK10895 223 EILQ 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
15-257 |
2.36e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.61 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 15 AVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIvtasarr 94
Cdd:COG1137 2 MTLEAENLVKSY--GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGRIFLDGEDI------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 95 rrelratrmamvfqepmTALnPVHR-----VG--SQ---------VDE----VLRLhRRMPRAQRRAKV---LEMFRsvh 151
Cdd:COG1137 68 -----------------THL-PMHKrarlgIGylPQeasifrkltVEDnilaVLEL-RKLSKKEREERLeelLEEFG--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 152 lpdVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLfIT-HDfgvVA 230
Cdd:COG1137 126 ---ITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVL-ITdHN---VR 197
|
250 260 270
....*....|....*....|....*....|
gi 489912973 231 E---IADRIVVMNRGDLTETGTRDEILARP 257
Cdd:COG1137 198 EtlgICDRAYIISEGKVLAEGTPEEILNNP 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
283-521 |
2.42e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.84 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTyaerrslFGAtrtVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARL 362
Cdd:PRK09700 3 TPYISMAGIGKS-------FGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 SGAGLRPLrrKVQIVFQDpyRSLNPRRAVGESIIEGLLN----FGMP---RAQALVRAARTLGVVGLGPDvMRRYPHQFS 435
Cdd:PRK09700 73 DHKLAAQL--GIGIIYQE--LSVIDELTVLENLYIGRHLtkkvCGVNiidWREMRVRAAMMLLRVGLKVD-LDEKVANLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 436 GGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVReRTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVET 515
Cdd:PRK09700 148 ISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCS 226
|
....*.
gi 489912973 516 GAAQTV 521
Cdd:PRK09700 227 GMVSDV 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-268 |
3.35e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.62 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 13 SAAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKS--VTSLAVMGLLpEGILEVSGgSARVLGEDIVTA 90
Cdd:PRK14258 2 SKLIPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKStfLKCLNRMNEL-ESEVRVEG-RVEFFNQNIYER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 SARRRRELRAtrMAMVFQEPmtALNPVhRVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPD-VERIYDAYPHQLSGG 169
Cdd:PRK14258 80 RVNLNRLRRQ--VSMVHPKP--NLFPM-SVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDeIKHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 170 QRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVM----NR-GDL 244
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgneNRiGQL 234
|
250 260
....*....|....*....|....
gi 489912973 245 TETGTRDEILARPSQNYTRRLVSS 268
Cdd:PRK14258 235 VEFGLTKKIFNSPHDSRTREYVLS 258
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-253 |
3.41e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.33 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSvsvcGAGnrvVRNLSLDVHAGETVCVVGESGSGKsvTSLA--VMGLLPegileVSGGSARVLGEDIvt 89
Cdd:PRK15439 264 AGAPVLTVEDLT----GEG---FRNISLEVRAGEILGLAGVVGAGR--TELAetLYGLRP-----ARGGRIMLNGKEI-- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 90 asarrrrelratrmamvfqepmTALNPVHRV--------------GSQVDEVLR------LHRRMP---RAQRRAKVLEM 146
Cdd:PRK15439 328 ----------------------NALSTAQRLarglvylpedrqssGLYLDAPLAwnvcalTHNRRGfwiKPARENAVLER 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 147 FR---SVHLPDVERIYdaypHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLFIT 223
Cdd:PRK15439 386 YRralNIKFNHAEQAA----RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIA-AQNVAVLFIS 460
|
250 260 270
....*....|....*....|....*....|
gi 489912973 224 HDFGVVAEIADRIVVMNRGDLTETGTRDEI 253
Cdd:PRK15439 461 SDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-253 |
3.48e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 81.57 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 13 SAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvtasa 92
Cdd:PRK11300 2 SQPLLSVSGLMMRF--GGLLAVNNVNLEVREQEIVSLIGPNGAGKT-TVFNCLT----GFYKPTGGTILLRGQHI----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 93 RRRRELRATRMAMV--FQ-----EPMTALNPV----HRvgsQVDE-VLRLHRRMPrAQRRAKVLEMFRSVHLPDVERIYD 160
Cdd:PRK11300 70 EGLPGHQIARMGVVrtFQhvrlfREMTVIENLlvaqHQ---QLKTgLFSGLLKTP-AFRRAESEALDRAATWLERVGLLE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 161 AYPHQ---LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIV 237
Cdd:PRK11300 146 HANRQagnLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIY 225
|
250
....*....|....*.
gi 489912973 238 VMNRGDLTETGTRDEI 253
Cdd:PRK11300 226 VVNQGTPLANGTPEEI 241
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-324 |
4.18e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.16 E-value: 4.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 25 SVCGAGNRVV--RNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLlpEGIleVSG----GSARVlgEDIvtasarrrrEL 98
Cdd:PRK11000 8 NVTKAYGDVVisKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL--EDI--TSGdlfiGEKRM--NDV---------PP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 99 RATRMAMVFQEpmTALNPVHRVGSQVDEVLRLHR--RMPRAQRRAKVLEMFRSVHLpdVERiydaYPHQLSGGQRQRIVI 176
Cdd:PRK11000 73 AERGVGMVFQS--YALYPHLSVAENMSFGLKLAGakKEEINQRVNQVAEVLQLAHL--LDR----KPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEI--- 253
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhy 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 254 ---------LARPSQNYTRRLVSSV-PSLVptQREAPGGEPV-LRITGLGRTYAERRSLFGATRTVVAASEVDLTLrRGE 322
Cdd:PRK11000 225 panrfvagfIGSPKMNFLPVKVTATaIEQV--QVELPNRQQVwLPVEGRGVQVGANMSLGIRPEHLLPSDIADVTL-EGE 301
|
..
gi 489912973 323 IL 324
Cdd:PRK11000 302 VQ 303
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
32-248 |
5.66e-17 |
|
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: 79.88 E-value: 5.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVM-GLLP--EGILEVSGGSARVLGedivtasarrrrelratrMAMVFQ 108
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKS-TLLRLLaGIYPpdSGTVTVRGRVSSLLG------------------LGGGFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 EPMTALNPVHRVGsqvdevlRLHrRMPRAQRRAKVLEMfrsVHLPDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLI 188
Cdd:cd03220 97 PELTGRENIYLNG-------RLL-GLSRKEIDEKIDEI---IEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 189 ADEPTTALDVTTQKQILALIRELQdRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:cd03220 166 IDEVLAVGDAAFQEKCQRRLRELL-KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
26-493 |
7.19e-17 |
|
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: 83.45 E-value: 7.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 26 VCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARvLGEDIvtasarrrrelratRMAM 105
Cdd:TIGR03719 13 VVPPKKEILKDISLSFFPGAKIGVLGLNGAGKS-TLLRIMA----GVDKDFNGEAR-PQPGI--------------KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 106 VFQEPmtALNPVHRVGSQVDEVLRLHRRM-------------PRAQ------RRAKVLEMFRSVHLPDVERI-------- 158
Cdd:TIGR03719 73 LPQEP--QLDPTKTVRENVEEGVAEIKDAldrfneisakyaePDADfdklaaEQAELQEIIDAADAWDLDSQleiamdal 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 159 ----YDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTqkqILALIRELQDrHQTAVLFITHDFGVVAEIAD 234
Cdd:TIGR03719 151 rcppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQE-YPGTVVAVTHDRYFLDNVAG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 235 RIVVMNRGD-----------LTETGTRDEILARPSQNYTRRL------VSSVP---------------SLVPTQRE---- 278
Cdd:TIGR03719 227 WILELDRGRgipwegnysswLEQKQKRLEQEEKEESARQKTLkrelewVRQSPkgrqakskarlaryeELLSQEFQkrne 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 279 ------APG---GEPVLRITGLGRTYAERrslfgatrtvVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSA 349
Cdd:TIGR03719 307 taeiyiPPGprlGDKVIEAENLTKAFGDK----------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDS 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 350 GRMLLGETdiarlsgaglrplrrkVQIVFQDPYR-SLNPRRAVGESIIEGLLNFGMPRAQALVRAartlgVVGL----GP 424
Cdd:TIGR03719 377 GTIEIGET----------------VKLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRfnfkGS 435
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 425 DVMRRYpHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVsvqaQVLELIEQVRERTGVSVLFITHD 493
Cdd:TIGR03719 436 DQQKKV-GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD 499
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
20-255 |
7.31e-17 |
|
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: 84.15 E-value: 7.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 20 RNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvtasarrrrelr 99
Cdd:TIGR03375 467 RNVSFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKS-TLLKLLL----GLYQPTEGSVLLDGVDI------------ 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 100 atrmamvfqepmTALNPV---HRVG--SQvDEVL------------RLH---RRMPRAQRRAKVLEMFRSvhLPDveriy 159
Cdd:TIGR03375 530 ------------RQIDPAdlrRNIGyvPQ-DPRLfygtlrdnialgAPYaddEEILRAAELAGVTEFVRR--HPD----- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 160 dAYPHQ-------LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQIL-ALIRELQDRhqTAVLfITHDFGVVaE 231
Cdd:TIGR03375 590 -GLDMQigergrsLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKdRLKRWLAGK--TLVL-VTHRTSLL-D 664
|
250 260
....*....|....*....|....
gi 489912973 232 IADRIVVMNRGDLTETGTRDEILA 255
Cdd:TIGR03375 665 LVDRIIVMDNGRIVADGPKDQVLE 688
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
39-291 |
8.29e-17 |
|
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: 79.51 E-value: 8.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 39 LDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIVTASARRRRELRATRMAMVFqepmtALNPVH 118
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIP-----PAKGTVKVAGASPGKGWRHIGYVPQRHEFAWDF-----PISVAH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 119 RVGSQVDEVLRLHRRMPRAQRRAkVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDV 198
Cdd:TIGR03771 71 TVMSGRTGHIGWLRRPCVADFAA-VRDALRRVGL---TELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 199 TTQKQILALIRELQdRHQTAVLFITHDFGVVAEIADRIVVMNrGDLTETGTRDEILArpsqnytrrlvssvPSLVPTQRE 278
Cdd:TIGR03771 147 PTQELLTELFIELA-GAGTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQLQD--------------PAPWMTTFG 210
|
250
....*....|...
gi 489912973 279 APGGEPVLRITGL 291
Cdd:TIGR03771 211 VSDSSPLLRIVGA 223
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
309-498 |
8.82e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRmllgetdiarLSGAGLRPLRRKVQIVFQDPYRSLNPR 388
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT----------VRRAGGARVAYVPQRSEVPDSLPLTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSV 468
Cdd:NF040873 76 DLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAES 154
|
170 180 190
....*....|....*....|....*....|
gi 489912973 469 QAQVLELIEQVRERtGVSVLFITHDLRVAA 498
Cdd:NF040873 155 RERIIALLAEEHAR-GATVVVVTHDLELVR 183
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
308-521 |
1.17e-16 |
|
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: 82.95 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 308 VVAASEVDLTLRRGEILGIVGESGSGKSTVARcIVRLIEPSA---GRMLLGEtdiARLSGAGLRPLRRK-VQIVFQDpyR 383
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHGtwdGEIYWSG---SPLKASNIRDTERAgIVIIHQE--L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 384 SLNPRRAVGESIIEG---LLNFG-MPRAQALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADE 459
Cdd:TIGR02633 88 TLVPELSVAENIFLGneiTLPGGrMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 460 AVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTV 521
Cdd:TIGR02633 168 PSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
293-523 |
1.31e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.03 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 293 RTYAERRSLFGATRTVvaASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGaglRPLRR 372
Cdd:PRK10253 7 RLRGEQLTLGYGKYTV--AENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS---KEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 373 KVQIVFQDpyrSLNPrravGESIIEGLLNFGMPRAQ------------ALVRAARTLGVVglgpDVMRRYPHQFSGGQRQ 440
Cdd:PRK10253 82 RIGLLAQN---ATTP----GDITVQELVARGRYPHQplftrwrkedeeAVTKAMQATGIT----HLADQSVDTLSGGQRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 441 RLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQT 520
Cdd:PRK10253 151 RAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
...
gi 489912973 521 VLT 523
Cdd:PRK10253 231 IVT 233
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-282 |
1.36e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 82.84 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIVTASARRRR 96
Cdd:PRK10790 341 IDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYP-----LTEGEIRLDGRPLSSLSHSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELratrMAMVFQEPmtalnpVHRVGSQVDEVlrlhrRMPRAQRRAKVLEMFRSVHLPDVER-----IYDAYPHQ---LSG 168
Cdd:PRK10790 415 QG----VAMVQQDP------VVLADTFLANV-----TLGRDISEEQVWQALETVQLAELARslpdgLYTPLGEQgnnLSV 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQI---LALIRElqdrhQTAVLFITHDFGVVAEiADRIVVMNRGDLT 245
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDSGTEQAIqqaLAAVRE-----HTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489912973 246 ETGTRDEILA---RPSQNYTRRLVSSvpSLVPTQREAPGG 282
Cdd:PRK10790 554 EQGTHQQLLAaqgRYWQMYQLQLAGE--ELAASVREEESL 591
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-256 |
1.72e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.57 E-value: 1.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLavMGLLPEGiLEVSGGSARVLGEDIvtas 91
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKS--TL--LQLLTRA-WDPQQGEILLNGQPI---- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 92 ARRRRELRATRMAMVFQEpmtalnpVHRVGSQVDEVLRLhrrmprAQRRA---KVLEMFRSV----HLPDVERIyDAY-- 162
Cdd:PRK11160 405 ADYSEAALRQAISVVSQR-------VHLFSATLRDNLLL------AAPNAsdeALIEVLQQVglekLLEDDKGL-NAWlg 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 163 --PHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTaVLFITHDFGVVAEIaDRIVVMN 240
Cdd:PRK11160 471 egGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKT-VLMITHRLTGLEQF-DRICVMD 547
|
250
....*....|....*.
gi 489912973 241 RGDLTETGTRDEILAR 256
Cdd:PRK11160 548 NGQIIEQGTHQELLAQ 563
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
30-254 |
1.76e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.16 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMgllpEGILEVSGGSARVlGEDIVTASARRRREL-RATRMAMVFQ 108
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKS-TLLQHL----NGLLQPTEGKVTV-GDIVVSSTSKQKEIKpVRKKVGVVFQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 EPMT-----------ALNPvHRVGSQVDEVLRLhrrmpraqrRAKVLEMfrsVHLPdvERIYDAYPHQLSGGQRQRIVIA 177
Cdd:PRK13643 92 FPESqlfeetvlkdvAFGP-QNFGIPKEKAEKI---------AAEKLEM---VGLA--DEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 178 MALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTETGTRDEIL 254
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVL-VTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
313-532 |
2.08e-16 |
|
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: 83.07 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLsgaGLRPLRRKVQIVFQDPY-------RSL 385
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI---GLHDLRFKITIIPQDPVlfsgslrMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 386 NPRRAVGESIIEGLLNFgmpraqalvraARTLGVVGLGPDvmrRYPHQ-------FSGGQRQRLCIARALVMDPEVLVAD 458
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALEL-----------AHLKTFVSALPD---KLDHEcaeggenLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 459 EAVSALDVSVQAQVLELIEQVRErtGVSVLFITHDLRVAAQVCDTIaVMQHGKVVETGAAQTVLTRPGHAYTRA 532
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYTRVI-VLDKGEVAEFGAPSNLLQQRGIFYSMA 1517
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
33-263 |
2.21e-16 |
|
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: 82.48 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKS-VTSLAVMGLLPEGilevsgGSARVLGEDIvtasARRRRELRATRMAMVFQEPm 111
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKStLTKLLQRLYTPQH------GQVLVDGVDL----AIADPAWLRRQMGVVLQEN- 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 talnpVHRVGSQVDEVLRLHRRMPRAQRRAK---------VLEMFRSVHLPDVERiydayPHQLSGGQRQRIVIAMALIL 182
Cdd:TIGR01846 541 -----VLFSRSIRDNIALCNPGAPFEHVIHAaklagahdfISELPQGYNTEVGEK-----GANLSGGQRQRIAIARALVG 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 183 EPKLLIADEPTTALDVTTQKQILALIRELQdRHQTaVLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEILARPSqNYT 262
Cdd:TIGR01846 611 NPRILIFDEATSALDYESEALIMRNMREIC-RGRT-VIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLALQG-LYA 686
|
.
gi 489912973 263 R 263
Cdd:TIGR01846 687 R 687
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-256 |
2.35e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 79.28 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-PEgilevsggSARVLGEDIVTASARRRRELRATRMAMVFQEPM 111
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ--------KGAVLWQGKPLDYSKRGLLALRQQVATVFQDPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 TALnpvhrVGSQVDEVLRLHRR---MPRAQRRAKVLEmfrSVHLPDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLI 188
Cdd:PRK13638 88 QQI-----FYTDIDSDIAFSLRnlgVPEAEITRRVDE---ALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 189 ADEPTTALDVTTQKQILALIREL--QDRHqtaVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILAR 256
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIvaQGNH---VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAC 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
166-493 |
2.82e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 81.92 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTqkqILALIRELQDrHQTAVLFITHDFGVVAEIADRIVVMNRGDLT 245
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IEWLEGFLKT-FQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 246 E---------TGTRDEILARPSQN--YTRRLvssvpslvpTQREA--PGGEPVLRITGLGRTYA---------ERRSLFG 303
Cdd:PRK11147 233 SypgnydqylLEKEEALRVEELQNaeFDRKL---------AQEEVwiRQGIKARRTRNEGRVRAlkalrrersERREVMG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 304 ATRTVVAAS--------EVD----------------LTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGEtdi 359
Cdd:PRK11147 304 TAKMQVEEAsrsgkivfEMEnvnyqidgkqlvkdfsAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGT--- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 360 arlsgaglrplrrKVQIVFQDPYRS-LNPRRAVGESIIEG----------------LLNFGMP--RAQALVRAartlgvv 420
Cdd:PRK11147 381 -------------KLEVAYFDQHRAeLDPEKTVMDNLAEGkqevmvngrprhvlgyLQDFLFHpkRAMTPVKA------- 440
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 421 glgpdvmrryphqFSGGQRQRLCIARALVMDPEVLVADEAVSALDVsvqaQVLELIEQVRERTGVSVLFITHD 493
Cdd:PRK11147 441 -------------LSGGERNRLLLARLFLKPSNLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
286-511 |
3.42e-16 |
|
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: 75.56 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 286 LRITGLGRTYAERrSLFgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETdiarlsga 365
Cdd:cd03221 1 IELENLSKTYGGK-LLL---------KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 glrplrrkvqivfqdpyrslnprravgesiieglLNFGmpraqalvraartlgvvglgpdvmrrYPHQFSGGQRQRLCIA 445
Cdd:cd03221 63 ----------------------------------VKIG--------------------------YFEQLSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 446 RALVMDPEVLVADEAVSALDV-SVQAqvleLIEQVRERTGvSVLFITHDLRVAAQVCDTIAVMQHGK 511
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLeSIEA----LEEALKEYPG-TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
17-256 |
4.59e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.22 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVtslaVMGLLPEgILEVSGGSARVLGEDIvtasARRRR 96
Cdd:PRK11176 342 IEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTR-FYDIDEGEILLDGHDL----RDYTL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEpmtalnpVHRVGSQV---------DEVLRlhRRMPRAQRRAKVLEMFRsvHLPD-VERIYDAYPHQL 166
Cdd:PRK11176 413 ASLRNQVALVSQN-------VHLFNDTIanniayartEQYSR--EQIEEAARMAYAMDFIN--KMDNgLDTVIGENGVLL 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQ-DRhqtAVLFITHDFGVVaEIADRIVVMNRGDLT 245
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQkNR---TSLVIAHRLSTI-EKADEILVVEDGEIV 557
|
250
....*....|.
gi 489912973 246 ETGTRDEILAR 256
Cdd:PRK11176 558 ERGTHAELLAQ 568
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
32-256 |
4.92e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEdivtasarrrrelratrMAMVFqEPM 111
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKS-TLLKLIA----GILEPTSGRVEVNGR-----------------VSALL-ELG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 TALNP-------VHRVGsqvdevlRLHrRMPRAQRRAKV--------LEMFrsVHLPdVeRIYdayphqlSGGQRQRIVI 176
Cdd:COG1134 97 AGFHPeltgrenIYLNG-------RLL-GLSRKEIDEKFdeivefaeLGDF--IDQP-V-KTY-------SSGMRARLAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILAR 256
Cdd:COG1134 158 AVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRT-VIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-249 |
5.82e-16 |
|
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: 76.68 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIVTASARRRR 96
Cdd:cd03369 7 IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFL-----EAEEGKIEIDGIDISTIPLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELratrMAMVFQEPmTALNPVHRvgSQVDevlrlhrrmpraqrrakVLEMFRSVHLPDVERIYDAyPHQLSGGQRQRIVI 176
Cdd:cd03369 82 SS----LTIIPQDP-TLFSGTIR--SNLD-----------------PFDEYSDEEIYGALRVSEG-GLNLSQGQRQLLCL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDrhQTAVLFITHDFGVVAEIaDRIVVMNRGDLTETGT 249
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT--NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
32-257 |
6.69e-16 |
|
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: 77.20 E-value: 6.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPegileVSGGSARVLGEDIVTASARRRRELRATRMAmvfQEP- 110
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVK-----PDSGKILLDGQDITKLPMHKRARLGIGYLP---QEAs 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 111 ----MTalnpvhrVGSQVDEVLRLHRrMPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIVIAMALILEPKL 186
Cdd:cd03218 86 ifrkLT-------VEENILAVLEIRG-LSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 187 LIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
17-242 |
6.90e-16 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 76.86 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvtasARRRR 96
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKS-TLLKLLA----GLYKPTSGSVLLDGTDI----RQLDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEPM----------TALNPVHRvgsqvDEvlrlhrRMPRAQRRAKVLEMFR----SVHLPDVERIYday 162
Cdd:cd03245 74 ADLRRNIGYVPQDVTlfygtlrdniTLGAPLAD-----DE------RILRAAELAGVTDFVNkhpnGLDLQIGERGR--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 163 phQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLfITHDFGVVaEIADRIVVMNRG 242
Cdd:cd03245 140 --GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLII-ITHRPSLL-DLVDRIIVMDSG 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
33-244 |
7.40e-16 |
|
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: 76.74 E-value: 7.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSvtslAVMGLLpEGILEVSGGSARVLGEDIvtasARRRRELRATRMAMVFQEPMT 112
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKS----TVVALL-ENFYQPQGGQVLLDGKPI----SQYEHKYLHSKVSLVGQEPVL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 113 ALNPVHR---VGSQVDEVLRLHRRMPRAQRRAKVLEMfrsVHLPDVEriYDAYPHQLSGGQRQRIVIAMALILEPKLLIA 189
Cdd:cd03248 100 FARSLQDniaYGLQSCSFECVKEAAQKAHAHSFISEL---ASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 190 DEPTTALDVTTQKQILALIRELQDRHqtAVLFITHDFGVVaEIADRIVVMNRGDL 244
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTV-ERADQILVLDGGRI 226
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
33-255 |
8.24e-16 |
|
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: 80.51 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVtslaVMGLLPEgILEVSGGSARVLGEDIVtasaRRRRELRATRMAMVFQEPMT 112
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKST----LFQLLLR-FYDPQSGRILLDGVDLR----QLDPAELRARMALVPQDPVL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 113 ALNPVH------RVGSQVDEVLRlhrrmprAQRRAKVLEMFRSvhLPDVeriYDAYPHQ----LSGGQRQRIVIAMALIL 182
Cdd:TIGR02204 426 FAASVMenirygRPDATDEEVEA-------AARAAHAHEFISA--LPEG---YDTYLGErgvtLSGGQRQRIAIARAILK 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 183 EPKLLIADEPTTALDVTTQKQI-LALIRELQDRhqtAVLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEILA 255
Cdd:TIGR02204 494 DAPILLLDEATSALDAESEQLVqQALETLMKGR---TTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIA 563
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
302-525 |
8.83e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.08 E-value: 8.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATRTVvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLlgetdiarlsgaglRPLRRKVQIVFQ-- 379
Cdd:PRK09544 14 FGQRRVL---SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGKLRIGYVPQkl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 380 --DPYRSLNPRRAVgesiiegLLNFGMPRAQAL-----VRAARTLgvvglgpdvmrRYPHQ-FSGGQRQRLCIARALVMD 451
Cdd:PRK09544 77 ylDTTLPLTVNRFL-------RLRPGTKKEDILpalkrVQAGHLI-----------DAPMQkLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 452 PEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLR-VAAQVCDTIAVMQHgkVVETGAAQTVLTRP 525
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHlVMAKTDEVLCLNHH--ICCSGTPEVVSLHP 211
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
44-252 |
1.13e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 44 GETVCVVGESGSGKSVTSLAVMGLLPEGiLEVSGgsarvlgeDIVTASARRRRELRATRMAMVFQEPMTalnpvhrVGS- 122
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPKG-VKGSG--------SVLLNGMPIDAKEMRAISAYVQQDDLF-------IPTl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 123 QVDEVL------RLHRRMPRAQRRAKVLEMFRSVHLPDVE--RIYDAYPHQ-LSGGQRQRIVIAMALILEPKLLIADEPT 193
Cdd:TIGR00955 115 TVREHLmfqahlRMPRRVTKKEKRERVDEVLQALGLRKCAntRIGVPGRVKgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 194 TALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDE 252
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQ 253
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
30-253 |
1.16e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.89 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKsvTSL--AVMGLLP-EGILEVSGGSARVLgedivtasarrRRELRATRMAMV 106
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGK--TSLlnALLGFLPyQGSLKINGIELREL-----------DPESWRKHLSWV 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 107 FQEPM---------TALNPVHRVGSQVDEVLRlhrrmpraqrRAKVLEMfrsvhlpdVERIYDAYPHQ-------LSGGQ 170
Cdd:PRK11174 429 GQNPQlphgtlrdnVLLGNPDASDEQLQQALE----------NAWVSEF--------LPLLPQGLDTPigdqaagLSVGQ 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 171 RQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTaVLFITHDFGVVAEIaDRIVVMNRGDLTETGTR 250
Cdd:PRK11174 491 AQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQT-TLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDY 567
|
...
gi 489912973 251 DEI 253
Cdd:PRK11174 568 AEL 570
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
166-515 |
1.33e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 79.39 E-value: 1.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDLT 245
Cdd:PRK10982 135 LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 246 ETG-----TRDEILA-RPSQNYTRRLvssvpslvPTQREAPgGEPVLRITGLgrTYAERRSLfgatrtvvaaSEVDLTLR 319
Cdd:PRK10982 214 ATQplaglTMDKIIAmMVGRSLTQRF--------PDKENKP-GEVILEVRNL--TSLRQPSI----------RDVSFDLH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 320 RGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgaGLRPLRRKVQIVFQDpyrslnpRRAVGesiIEGL 399
Cdd:PRK10982 273 KGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN--ANEAINHGFALVTEE-------RRSTG---IYAY 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 400 LNFGMPRAQALVRAART-LGVVGLGP---------DVMR-RYP-HQ-----FSGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:PRK10982 341 LDIGFNSLISNIRNYKNkVGLLDNSRmksdtqwviDSMRvKTPgHRtqigsLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 463 ALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKV---VET 515
Cdd:PRK10982 421 GIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLVagiVDT 475
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
294-513 |
1.53e-15 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 75.28 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 294 TYAERRSLFGATRTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIvrliepsAGRmllgeTDIARLSGA-------- 365
Cdd:cd03213 10 TVTVKSSPSKSGKQLL--KNVSGKAKPGELTAIMGPSGAGKSTLLNAL-------AGR-----RTGLGVSGEvlingrpl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRPLRRKVQIVFQDPYrsLNPRRAVGEsiiegllnfgmpraqALVRAARTLGVvglgpdvmrryphqfSGGQRQRLCIA 445
Cdd:cd03213 76 DKRSFRKIIGYVPQDDI--LHPTLTVRE---------------TLMFAAKLRGL---------------SGGERKRVSIA 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 446 RALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRErTGVSVLFITHDLRVAA-QVCDTIAVMQHGKVV 513
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD-TGRTIICSIHQPSSEIfELFDKLLLLSQGRVI 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
284-517 |
1.90e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.94 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 284 PVLRITGLGRTYAERRSLFGatrtvvaaseVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLS 363
Cdd:PRK15439 10 PLLCARSISKQYSGVEVLKG----------IDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 364 GAGLRPLrrKVQIVFQDPYrsLNPRRAVGESIIegllnFGMPRAQ-ALVRAARTLGVVG--LGPDVmrryphqfSGG--- 437
Cdd:PRK15439 80 PAKAHQL--GIYLVPQEPL--LFPNLSVKENIL-----FGLPKRQaSMQKMKQLLAALGcqLDLDS--------SAGsle 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 438 --QRQRLCIARALVMDPEVLVADEAVSALdvsVQAQVLELIEQVRE--RTGVSVLFITHDLRVAAQVCDTIAVMQHGKVV 513
Cdd:PRK15439 143 vaDRQIVEILRGLMRDSRILILDEPTASL---TPAETERLFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
....
gi 489912973 514 ETGA 517
Cdd:PRK15439 220 LSGK 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-254 |
4.03e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 75.26 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVsvcgaGNRVvRNLSLDVHAGETVCVVGESGSGKSvTSLAVM-GLLPegilevSGGSARVLGEDIvtasARRR 95
Cdd:COG4138 1 LQLNDVAV-----AGRL-GPISAQVNAGELIHLIGPNGAGKS-TLLARMaGLLP------GQGEILLNGRPL----SDWS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRATRMAMVFQEPMTALN-PVHrvgsqvdEVLRLHR-RMPRAQRRAKVLEmfrsvHLPDVERIYDAYP---HQLSGGQ 170
Cdd:COG4138 64 AAELARHRAYLSQQQSPPFAmPVF-------QYLALHQpAGASSEAVEQLLA-----QLAEALGLEDKLSrplTQLSGGE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 171 RQRIVIAMALI-------LEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGD 243
Cdd:COG4138 132 WQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQ-GITVVMSSHDLNHTLRHADRVWLLKQGK 210
|
250
....*....|.
gi 489912973 244 LTETGTRDEIL 254
Cdd:COG4138 211 LVASGETAEVM 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
310-518 |
4.57e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.92 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAglRPLRRKVQIVFQDpyRSLNPRR 389
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIMREAVAIVPEG--RRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEGllNFGMPRAQALVRAARtlgVVGLGPDVMRRYPHQ---FSGGQRQRLCIARALVMDPEVLVADEAVSALDV 466
Cdd:PRK11614 96 TVEENLAMG--GFFAERDQFQERIKW---VYELFPRLHERRIQRagtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 467 SVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVV--ETGAA 518
Cdd:PRK11614 171 IIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVleDTGDA 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
312-492 |
5.35e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.93 E-value: 5.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRmllgetdIARLSGAglrplrrkvQIVF--QDPYrslnprr 389
Cdd:COG4178 380 EDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR-------IARPAGA---------RVLFlpQRPY------- 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 avgesIIEGLLnfgmprAQALV-----------RAARTLGVVGLGP-----DVMRRYPHQFSGGQRQRLCIARALVMDPE 453
Cdd:COG4178 437 -----LPLGTL------REALLypataeafsdaELREALEAVGLGHlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPD 505
|
170 180 190
....*....|....*....|....*....|....*....
gi 489912973 454 VLVADEAVSALDVSVQAQVLELIEQvrERTGVSVLFITH 492
Cdd:COG4178 506 WLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-225 |
5.50e-15 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 77.79 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 2 PYAPYPPAGDTSAAVLAIRNLSVSVCGAgNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLP--EGILEVSGGS 79
Cdd:TIGR02868 320 GSAPAAGAVGLGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDplQGEVTLDGVP 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 80 ARVLGEDIVtasarrrrelrATRMAMVFQEPmtalnpvHRVGSQVDEVLRLHR------RMPRAQRRAKVLEMFRSvhLP 153
Cdd:TIGR02868 399 VSSLDQDEV-----------RRRVSVCAQDA-------HLFDTTVRENLRLARpdatdeELWAALERVGLADWLRA--LP 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 154 D-VERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhqTAVLFITHD 225
Cdd:TIGR02868 459 DgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSG--RTVVLITHH 529
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
136-255 |
5.91e-15 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 78.53 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 136 RAQRRAKVLEMFRSvhLPDVeriYDA----YPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIREL 211
Cdd:PTZ00265 1330 RACKFAAIDEFIES--LPNK---YDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 489912973 212 QDRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTET-----GTRDEILA 255
Cdd:PTZ00265 1405 KDKADKTIITIAHRIASIKR-SDKIVVFNNPDRTGSfvqahGTHEELLS 1452
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
306-522 |
6.07e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.54 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 306 RTVVaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLsgaglrPL----RRKVQIVFQDP 381
Cdd:PRK10895 16 RRVV--EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL------PLharaRRGIGYLPQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 yrSLNPRRAVGESIIEGL-LNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEA 460
Cdd:PRK10895 88 --SIFRRLSVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIE-HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489912973 461 VSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVL 522
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIL 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
300-492 |
6.77e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.84 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 300 SLFGATRTVV---AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIepsagrmllgetdiarlsgaglrpLRRKVQI 376
Cdd:COG2401 32 EAFGVELRVVeryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGAL------------------------KGTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 377 VFQDPYRSLNPRRavgeSIIEGLlnfgmPRAQALVRAARTLGVVGLG-PDVMRRYPHQFSGGQRQRLCIARALVMDPEVL 455
Cdd:COG2401 88 CVDVPDNQFGREA----SLIDAI-----GRKGDFKDAVELLNAVGLSdAVLWLRRFKELSTGQKFRFRLALLLAERPKLL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 489912973 456 VADEAVSALDVSVqAQVLELIEQ--VReRTGVSVLFITH 492
Cdd:COG2401 159 VIDEFCSHLDRQT-AKRVARNLQklAR-RAGITLVVATH 195
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
138-255 |
9.37e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 75.12 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 138 QRRAKVLEMfrsVHLPdvERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQT 217
Cdd:PRK13651 143 KRAAKYIEL---VGLD--ESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKT 217
|
90 100 110
....*....|....*....|....*....|....*...
gi 489912973 218 AVLfITHDFGVVAEIADRIVVMNRGDLTETGTRDEILA 255
Cdd:PRK13651 218 IIL-VTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILS 254
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
326-529 |
9.55e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 77.07 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 326 IVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGaglRPLRRKVQIVFQDPY---RSLNPRRAVGESIIEGLLNF 402
Cdd:PRK10790 372 LVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLRQGVAMVQQDPVvlaDTFLANVTLGRDISEEQVWQ 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 403 GMPRAQaLVRAARTLgvvglgPD-VMRRYPHQ---FSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQ 478
Cdd:PRK10790 449 ALETVQ-LAELARSL------PDgLYTPLGEQgnnLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489912973 479 VRERTGVSVlfITHDLRVAAQVcDTIAVMQHGKVVETGAAQTVLTRPGHAY 529
Cdd:PRK10790 522 VREHTTLVV--IAHRLSTIVEA-DTILVLHRGQAVEQGTHQQLLAAQGRYW 569
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
312-511 |
1.13e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 72.89 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIvrliepsagrmlLGETDiaRLSGAGLRPlrRKVQIVFQDPYrslnprrAV 391
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSAL------------LGELE--KLSGSVSVP--GSIAYVSQEPW-------IQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIIEGLLnFGMP----RAQALVRAArtlgvvGLGPDvMRRYPHQ-----------FSGGQRQRLCIARALVMDPEVLV 456
Cdd:cd03250 79 NGTIRENIL-FGKPfdeeRYEKVIKAC------ALEPD-LEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 457 ADEAVSALDVSVQAQvleLIEQV------RERTgvsVLFITHDLRVAAQvCDTIAVMQHGK 511
Cdd:cd03250 151 LDDPLSAVDAHVGRH---IFENCilglllNNKT---RILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
166-257 |
1.51e-14 |
|
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: 76.53 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQkqilALIRELQDRHQTAVLFITHDFGVVAEiADRIVVMNRGDLT 245
Cdd:TIGR03797 589 LSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQ----AIVSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVV 663
|
90
....*....|..
gi 489912973 246 ETGTRDEILARP 257
Cdd:TIGR03797 664 QQGTYDELMARE 675
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
17-242 |
2.24e-14 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 72.12 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGA---GNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLAvMGLLPEgiLEVSGGSARVLGedivtasar 93
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKS--SLL-SALLGE--LEKLSGSVSVPG--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 rrrelratRMAMVFQEP--MTAlnpvhrvgsQVDEVLRLHRRMpRAQRRAKVLemfRSVHL-PDVEriydAYPHQ----- 165
Cdd:cd03250 67 --------SIAYVSQEPwiQNG---------TIRENILFGKPF-DEERYEKVI---KACALePDLE----ILPDGdltei 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 ------LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQIL--ALIRELQDrHQTAVLfITHDFGVVAEiADRIV 237
Cdd:cd03250 122 gekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFenCILGLLLN-NKTRIL-VTHQLQLLPH-ADQIV 198
|
....*
gi 489912973 238 VMNRG 242
Cdd:cd03250 199 VLDNG 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-242 |
3.04e-14 |
|
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: 71.43 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 14 AAVLAIRNLSVSV----CGAGNRVVRNLSLDVHAGETVCVVGESGSGKsvTSL--AVMGLLPEGILEvsgGSARVLGEDI 87
Cdd:cd03213 1 GVTLSFRNLTVTVksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGK--STLlnALAGRRTGLGVS---GEVLINGRPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 88 vtasarrRRELRATRMAMVFQEPMtalnpVHrvGSQ-VDEVLrlhrrmpraqrrakvleMFrSVHLpdveriydaypHQL 166
Cdd:cd03213 76 -------DKRSFRKIIGYVPQDDI-----LH--PTLtVRETL-----------------MF-AAKL-----------RGL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITH-----DFGVvaeiADRIVVMNR 241
Cdd:cd03213 113 SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRT-IICSIHqpsseIFEL----FDKLLLLSQ 187
|
.
gi 489912973 242 G 242
Cdd:cd03213 188 G 188
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
169-513 |
3.06e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.21 E-value: 3.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIADRIVV---------- 238
Cdd:NF040905 143 GKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSII-ISHKLNEIRRVADSITVlrdgrtietl 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 239 -MNRGDLTEtgtrDEILarpsqnytRRLVS-SVPSLVPtQREAPGGEPVLRITGLGRTYAERRSlfgatRTVVaaSEVDL 316
Cdd:NF040905 222 dCRADEVTE----DRII--------RGMVGrDLEDRYP-ERTPKIGEVVFEVKNWTVYHPLHPE-----RKVV--DDVSL 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 317 TLRRGEILGIVGESGSGK-----------------------------STVARCIvrliepSAG-------RMLLG---ET 357
Cdd:NF040905 282 NVRRGEIVGIAGLMGAGRtelamsvfgrsygrnisgtvfkdgkevdvSTVSDAI------DAGlayvtedRKGYGlnlID 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 358 DIAR-LSGAGLRPLRRKVQIvfqdpyrSLNPRRAVGESIiegllnfgmpRAQALVRAARTLGVVGlgpdvmrryphQFSG 436
Cdd:NF040905 356 DIKRnITLANLGKVSRRGVI-------DENEEIKVAEEY----------RKKMNIKTPSVFQKVG-----------NLSG 407
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 437 GQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVV 513
Cdd:NF040905 408 GNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
30-248 |
3.56e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.99 E-value: 3.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIvtasarrRRELRATRMAMVFQ- 108
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFV-----RLASGKISILGQPT-------RQALQKNLVAYVPQs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 EPMTALNPVhrvgsQVDEVLRLHR-------RMPRAQRRAKVLEMFRSVHLPDveriydaYPH----QLSGGQRQRIVIA 177
Cdd:PRK15056 87 EEVDWSFPV-----LVEDVVMMGRyghmgwlRRAKKRDRQIVTAALARVDMVE-------FRHrqigELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 178 MALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADrIVVMNRGDLTETG 248
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKT-MLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
7-255 |
3.63e-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: 75.75 E-value: 3.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 7 PPAGDTSAAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMgllpeGILEVSGGSARVLGED 86
Cdd:TIGR00957 1275 PPSGWPPRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLF-----RINESAEGEIIIDGLN 1349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 87 IVTASARRrrelratrmaMVFQEPMTALNPVHRVGSqvdevLRLHRRMPRAQRRAKVLEMFRSVHLPD-VERIYDAYPHQ 165
Cdd:TIGR00957 1350 IAKIGLHD----------LRFKITIIPQDPVLFSGS-----LRMNLDPFSQYSDEEVWWALELAHLKTfVSALPDKLDHE 1414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 -------LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDrhQTAVLFITHDFGVVAEIAdRIVV 238
Cdd:TIGR00957 1415 caeggenLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFE--DCTVLTIAHRLNTIMDYT-RVIV 1491
|
250
....*....|....*..
gi 489912973 239 MNRGDLTETGTRDEILA 255
Cdd:TIGR00957 1492 LDKGEVAEFGAPSNLLQ 1508
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
136-254 |
4.66e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.51 E-value: 4.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 136 RAQRRAKVLEMFRSVHL-PDVERIYDAyphqLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDR 214
Cdd:PRK10575 121 GAADREKVEEAISLVGLkPLAHRLVDS----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQE 196
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489912973 215 HQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEIL 254
Cdd:PRK10575 197 RGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
321-525 |
4.74e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.59 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 321 GEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIArlsGAGLRPLRRKVQIVFQDPYRSLNPRRAVGESIIEGll 400
Cdd:PTZ00243 1336 REKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG---AYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEA-- 1410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 401 nfgmprAQALVRAArtLGVVGLGPDVMRRYP----------HQFSGGQRQRLCIARALV-MDPEVLVADEAVS----ALD 465
Cdd:PTZ00243 1411 ------SSAEVWAA--LELVGLRERVASESEgidsrvleggSNYSVGQRQLMCMARALLkKGSGFILMDEATAnidpALD 1482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 466 VSVQAQVLELIeqvrerTGVSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLTRP 525
Cdd:PTZ00243 1483 RQIQATVMSAF------SAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAEMGSPRELVMNR 1535
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
314-524 |
5.71e-14 |
|
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: 71.86 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYR-------SLN 386
Cdd:cd03288 40 VKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP---LHTLRSRLSIILQDPILfsgsirfNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 PRRAVGESIIegllnfgmprAQALVRAARTLGVVGL--GPD-VMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSA 463
Cdd:cd03288 117 PECKCTDDRL----------WEALEIAQLKNMVKSLpgGLDaVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATAS 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 464 LDVSVQaQVLE--LIEQVRERTGVSVLFITHDLRVAaqvcDTIAVMQHGKVVETGAAQTVLTR 524
Cdd:cd03288 187 IDMATE-NILQkvVMTAFADRTVVTIAHRVSTILDA----DLVLVLSRGILVECDTPENLLAQ 244
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
30-245 |
5.87e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.44 E-value: 5.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIvTASARRRRELRATRMAMVFQE 109
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKS-TLLKLIC----GIERPSAGKIWFSGHDI-TRLKNREVPFLRRQIGMIFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 PMTALN---------PVHRVGSQVDEVlrlHRRMPRAQRRAKVLEMFRSvhlpdveriydaYPHQLSGGQRQRIVIAMAL 180
Cdd:PRK10908 88 HHLLMDrtvydnvaiPLIIAGASGDDI---RRRVSAALDKVGLLDKAKN------------FPIQLSGGEQQRVGIARAV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 181 ILEPKLLIADEPTTALDVTTQKQILALIRELqDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLT 245
Cdd:PRK10908 153 VNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-256 |
1.04e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 5 PYPPAGDTSAAVLAiRNLSvsvCGAGNRV-VRNLSLDVHAGETVCVVGESGSGKSVTslavMGLLpEGILEVSGGSARVL 83
Cdd:NF033858 256 PRPADDDDEPAIEA-RGLT---MRFGDFTaVDHVSFRIRRGEIFGFLGSNGCGKSTT----MKML-TGLLPASEGEAWLF 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 84 GE-----DIVTAsarrrrelratrmamvfqepmtalnpvHRVG--SQ---------VDEVLRLHRR---MPRAQRRAKVL 144
Cdd:NF033858 327 GQpvdagDIATR---------------------------RRVGymSQafslygeltVRQNLELHARlfhLPAAEIAARVA 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 145 EMFRSVHLPDVEriyDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLFI-T 223
Cdd:NF033858 380 EMLERFDLADVA---DALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELS-REDGVTIFIsT 455
|
250 260 270
....*....|....*....|....*....|...
gi 489912973 224 HdFGVVAEIADRIVVMNRGDLTETGTRDEILAR 256
Cdd:NF033858 456 H-FMNEAERCDRISLMHAGRVLASDTPAALVAA 487
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
304-522 |
1.26e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.00 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 304 ATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLL-GETDIARLSgAGLrplrrkvqivfqdpy 382
Cdd:PRK13546 33 KNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRnGEVSVIAIS-AGL--------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 383 rslNPRRAVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:PRK13546 97 ---SGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELG-EFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 463 ALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVL 522
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKEQ-NKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
312-519 |
1.42e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.95 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRKVQIVFQDP--YRSLNPRR 389
Cdd:PRK11831 24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGalFTDMNVFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEgllNFGMPRAQALVRAARTLGVVGL--GPDVMrryPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVS 467
Cdd:PRK11831 104 NVAYPLRE---HTQLPAPLLHSTVMMKLEAVGLrgAAKLM---PSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489912973 468 VQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQ 519
Cdd:PRK11831 178 TMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
314-518 |
1.63e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.44 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIV-----RLIEpsaGRMLLGETDIARLSgAGLRPlRRKVQIVFQDPYR----- 383
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAghpayKILE---GDILFKGESILDLE-PEERA-HLGIFLAFQYPIEipgvs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 384 -------SLNPRR-AVGESIIEGLLNFGMPRAQalvraartLGVVGLGPDVMRRYPHQ-FSGGQRQRLCIARALVMDPEV 454
Cdd:CHL00131 101 nadflrlAYNSKRkFQGLPELDPLEFLEIINEK--------LKLVGMDPSFLSRNVNEgFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 455 LVADEAVSALDVSVQAQVLELIEQVReRTGVSVLFITHDLRVAAQVC-DTIAVMQHGKVVETGAA 518
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLM-TSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDA 236
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
17-224 |
1.71e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 68.33 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVcGAGNRVVRNLSLDVHAGETVCVVGESGSGKsvTSL--AVMGLLP--EGILEVSGGSArvlgedivtasa 92
Cdd:cd03223 1 IELENLSLAT-PDGRVLLKDLSFEIKPGDRLLITGPSGTGK--SSLfrALAGLWPwgSGRIGMPEGED------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 93 rrrrelratrMAMVFQEPMtalnpvhrvgsqvdevlrlhrrMPRAQRRAKVlemfrsvhlpdveriydAYP--HQLSGGQ 170
Cdd:cd03223 66 ----------LLFLPQRPY----------------------LPLGTLREQL-----------------IYPwdDVLSGGE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489912973 171 RQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRElqdrHQTAVLFITH 224
Cdd:cd03223 97 QQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE----LGITVISVGH 146
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
309-526 |
2.08e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.96 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 309 VAASEVDLTLRRGEILGIVGESGSGKSTvarcivrLIEpsagrMLLG----ETDIaRLSGAGLRPL-----RRKVQIVFQ 379
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTS-------LLN-----ALLGflpyQGSL-KINGIELRELdpeswRKHLSWVGQ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 380 DPyrslnprRAVGESIIEGLLnFGMPRA------QALVRA-------ARTLGV---VGlgpDVMRRyphqFSGGQRQRLC 443
Cdd:PRK11174 431 NP-------QLPHGTLRDNVL-LGNPDAsdeqlqQALENAwvseflpLLPQGLdtpIG---DQAAG----LSVGQAQRLA 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 444 IARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTgvSVLFITHDLRVAAQvCDTIAVMQHGKVVETGAAQTVLT 523
Cdd:PRK11174 496 LARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQ 572
|
...
gi 489912973 524 RPG 526
Cdd:PRK11174 573 AGG 575
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
7-256 |
2.57e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 7 PPAGDTsaaVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSaRVLGED 86
Cdd:COG0488 309 ERLGKK---VLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKS-TLLKLLA----GELEPDSGT-VKLGET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 87 IVtasarrrrelratrMAMVFQEpMTALNPVHRVgsqVDEVLRLHRRMPRAQRRAkVLE--MFRSvhlpdvERIYdAYPH 164
Cdd:COG0488 378 VK--------------IGYFDQH-QEELDPDKTV---LDELRDGAPGGTEQEVRG-YLGrfLFSG------DDAF-KPVG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTqkqILALIRELQDrHQTAVLFITHDFGVVAEIADRIVVMNRGDL 244
Cdd:COG0488 432 VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET---LEALEEALDD-FPGTVLLVSHDRYFLDRVATRILEFEDGGV 507
|
250
....*....|...
gi 489912973 245 TE-TGTRDEILAR 256
Cdd:COG0488 508 REyPGGYDDYLEK 520
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
283-524 |
2.97e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAerrslfgatrTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARL 362
Cdd:PRK11288 2 SPYLSFDGIGKTFP----------GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 363 S-----GAGlrplrrkVQIVFQDPYrsLNPRRAVGESIIEGLL--NFGMPRAQALVRAART----LGvVGLGPDVMRRYp 431
Cdd:PRK11288 72 SttaalAAG-------VAIIYQELH--LVPEMTVAENLYLGQLphKGGIVNRRLLNYEAREqlehLG-VDIDPDTPLKY- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 432 hqFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGK 511
Cdd:PRK11288 141 --LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAE-GRVILYVSHRMEEIFALCDAITVFKDGR 217
|
250
....*....|...
gi 489912973 512 VVETGAAQTVLTR 524
Cdd:PRK11288 218 YVATFDDMAQVDR 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
37-254 |
4.86e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 4.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 37 LSLDVHAGETVCVVGESGSGKSvTSLAVM-GLLPegilevSGGSARVLGEDIVTASARRRRELRatrmAMVFQEPMTALN 115
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKS-TLLARMaGLLP------GSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 116 -PVHrvgsqvdEVLRLHR--RMPRAQRRAKVLEMFRSVHLPD-VERIYdaypHQLSGGQRQRIVIAmALIL--------E 183
Cdd:PRK03695 84 mPVF-------QYLTLHQpdKTRTEAVASALNEVAEALGLDDkLGRSV----NQLSGGEWQRVRLA-AVVLqvwpdinpA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 184 PKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEIL 254
Cdd:PRK03695 152 GQLLLLDEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
12-257 |
5.69e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 69.41 E-value: 5.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSVSvcgAGNRVV-RNLSLDVHAGETVCVVGESGSGKSvTSLAVMGllpeGILEVSGGSARVLGEDIVTA 90
Cdd:PRK11831 3 SVANLVDMRGVSFT---RGNRCIfDNISLTVPRGKITAIMGPSGIGKT-TLLRLIG----GQIAPDHGEILFDGENIPAM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 SARRRRELRATrMAMVFQEP--MTALNpvhrVGSQVDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVERIYdayPHQLSG 168
Cdd:PRK11831 75 SRSRLYTVRKR-MSMLFQSGalFTDMN----VFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLM---PSELSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETG 248
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
|
....*....
gi 489912973 249 TRDEILARP 257
Cdd:PRK11831 227 SAQALQANP 235
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
150-257 |
6.98e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.90 E-value: 6.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 150 VHLPDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVV 229
Cdd:PRK11144 113 VALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEI 192
|
90 100
....*....|....*....|....*...
gi 489912973 230 AEIADRIVVMNRGDLTETGTRDEILARP 257
Cdd:PRK11144 193 LRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
313-494 |
1.35e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.83 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLgeTDIARLSGAGLRPLRRKVQIVFQDP----------- 381
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLKWWRSKIGVVSQDPllfsnsiknni 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 ------------------------YRSLNPRRAV----------------GESIIEGLLNFGMPRAQALVRAARTLGV-- 419
Cdd:PTZ00265 481 kyslyslkdlealsnyynedgndsQENKNKRNSCrakcagdlndmsnttdSNELIEMRKNYQTIKDSEVVDVSKKVLIhd 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 420 -VGLGPD----VMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDL 494
Cdd:PTZ00265 561 fVSALPDkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
288-528 |
2.41e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.61 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 288 ITGLGRTYAERRSLFGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVArCIVRLIEPSAGRMLLgetdiaRLSG--A 365
Cdd:NF000106 6 ISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPW------RF*TwcA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 366 GLRPLRRKVqivfqDPYRSLNPRRAVGESIIEGLLNFG----MPRAQALVRAARTLGVVGLgPDVMRRYPHQFSGGQRQR 441
Cdd:NF000106 79 NRRALRRTI-----G*HRPVR*GRRESFSGRENLYMIGr*ldLSRKDARARADELLERFSL-TEAAGRAAAKYSGGMRRR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 442 LCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVrERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG----- 516
Cdd:NF000106 153 LDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSM-VRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGkvdel 231
|
250
....*....|....*.
gi 489912973 517 ----AAQTVLTRPGHA 528
Cdd:NF000106 232 ktkvGGRTLQIRPAHA 247
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
302-510 |
2.44e-12 |
|
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: 66.59 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRR-KVQIVFQD 380
Cdd:cd03290 8 FSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRySVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 381 PYRsLNPrrAVGESIIegllnFGMP----RAQALVRAArtlgvvGLGPDVmRRYPH-----------QFSGGQRQRLCIA 445
Cdd:cd03290 88 PWL-LNA--TVEENIT-----FGSPfnkqRYKAVTDAC------SLQPDI-DLLPFgdqteigergiNLSGGQRQRICVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 446 RALVMDPEVLVADEAVSALDVSV-----QAQVLELIeQVRERTgvsVLFITHDLRVAAQVcDTIAVMQHG 510
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFL-QDDKRT---LVLVTHKLQYLPHA-DWIIAMKDG 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
314-492 |
2.95e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGlrplrrkvQIVFQDPYRSLNPRRAVGE 393
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE--------ACHYLGHRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 sIIEGLLNFgmpRAQALVRAARTLGVVGLGPDVMRRYPHqFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVL 473
Cdd:PRK13539 93 -NLEFWAAF---LGGEELDIAAALEAVGLAPLAHLPFGY-LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
170
....*....|....*....
gi 489912973 474 ELIEQVRERTGvSVLFITH 492
Cdd:PRK13539 168 ELIRAHLAQGG-IVIAATH 185
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
16-267 |
3.26e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.73 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEGIlevsgGSARVLGE----DIVTAS 91
Cdd:PRK14243 10 VLRTENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKS-TILRCFNRLNDLI-----PGFRVEGKvtfhGKNLYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 92 ARRRRELRATRMAMVFQEPmtalNPV-----------HRV-GSQVDevlrLHRRMPRAQRRA----KVLEMFRSVHLpdv 155
Cdd:PRK14243 82 PDVDPVEVRRRIGMVFQKP----NPFpksiydniaygARInGYKGD----MDELVERSLRQAalwdEVKDKLKQSGL--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 156 eriydayphQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqtAVLFITHDFGVVAEIADR 235
Cdd:PRK14243 151 ---------SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDM 219
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489912973 236 IVVMNrGDLTETGTR----------DEILARPSQNYTRRLVS 267
Cdd:PRK14243 220 TAFFN-VELTEGGGRygylvefdrtEKIFNSPQQQATRDYVS 260
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
312-497 |
4.16e-12 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 65.21 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLrrkVQIVFQDPYRSLnprrav 391
Cdd:cd03231 17 SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGL---LYLGHAPGIKTT------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 gESIIEGLLNFGMPRAQALVRAArtLGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQ 471
Cdd:cd03231 88 -LSVLENLRFWHADHSDEQVEEA--LARVGLN-GFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|....*.
gi 489912973 472 VLELIEQVRERTGVSVLFITHDLRVA 497
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHQDLGLS 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
6-255 |
5.43e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.11 E-value: 5.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 6 YP----PAGDTSaavLAIRNLSvsvcGAGnrvVRNLSLDVHAGETVCVVGESGSGKsvTSLavMGLLpEGILEVSGGSAR 81
Cdd:PRK10762 246 YPrldkAPGEVR---LKVDNLS----GPG---VNDVSFTLRKGEILGVSGLMGAGR--TEL--MKVL-YGALPRTSGYVT 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 82 VLGEDIVTASARRRRELRAT-----------RMAMVFQEPM--TALNPVHRVGSQVDevlrlhrrmpRAQRRAKV---LE 145
Cdd:PRK10762 311 LDGHEVVTRSPQDGLANGIVyisedrkrdglVLGMSVKENMslTALRYFSRAGGSLK----------HADEQQAVsdfIR 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 146 MFrSVHLPDVERIYDayphQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHD 225
Cdd:PRK10762 381 LF-NIKTPSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIIL-VSSE 454
|
250 260 270
....*....|....*....|....*....|....*
gi 489912973 226 FGVVAEIADRIVVMNRGDLT-----ETGTRDEILA 255
Cdd:PRK10762 455 MPEVLGMSDRILVMHEGRISgeftrEQATQEKLMA 489
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
312-492 |
5.59e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 64.10 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLlgetdiarlsgaglRPLRRKVQIVFQDPYrslnprrav 391
Cdd:cd03223 18 KDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------------MPEGEDLLFLPQRPY--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 gesIIEGLLnfgmprAQALVraartlgvvglgpdvmrrYP--HQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:cd03223 75 ---LPLGTL------REQLI------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180
....*....|....*....|...
gi 489912973 470 AQVLELIEQVrertGVSVLFITH 492
Cdd:cd03223 128 DRLYQLLKEL----GITVISVGH 146
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-242 |
6.09e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 6.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 13 SAAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGIlevsgGSARVLGEdivtasa 92
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA-----GKITVLGV------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 93 rrrrelratrmamvfQEPMTALNPVHRVG--SQVD---------EVLRLHRRMPRAQRRAKVLEMFRSVHLPDVERIYDA 161
Cdd:PRK13536 104 ---------------PVPARARLARARIGvvPQFDnldleftvrENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 162 YPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNR 241
Cdd:PRK13536 169 RVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVLEA 247
|
.
gi 489912973 242 G 242
Cdd:PRK13536 248 G 248
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
33-256 |
7.60e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 66.37 E-value: 7.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGllpegILEVSGGSARVLGEDIvtasarrrrelratrmamvfqePMT 112
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLG-----LTHPDAGSISLCGEPV----------------------PSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 113 ALNPVHRVGS-----------QVDEVLRLHRR---MPRAQRRAKVLEMFRSVHLpdvERIYDAYPHQLSGGQRQRIVIAM 178
Cdd:PRK13537 75 ARHARQRVGVvpqfdnldpdfTVRENLLVFGRyfgLSAAAARALVPPLLEFAKL---ENKADAKVGELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 179 ALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILAR 256
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKT-ILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
32-239 |
9.38e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.59 E-value: 9.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGileVSGGSARVLGEDivtasarrrrelratrmamvFQEPM 111
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGT---PVAGCVDVPDNQ--------------------FGREA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 TALNPVHRVGSQVDEVLRLHRrmpraqrrakvlemfrsVHLPDVErIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADE 191
Cdd:COG2401 101 SLIDAIGRKGDFKDAVELLNA-----------------VGLSDAV-LWLRRFKELSTGQKFRFRLALLLAERPKLLVIDE 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489912973 192 PTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVM 239
Cdd:COG2401 163 FCSHLDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIF 210
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
23-241 |
1.32e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.75 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 23 SVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLP--EGILEVSGGSarvlgedivtasarrrrelra 100
Cdd:PRK09544 9 NVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApdEGVIKRNGKL--------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 101 trmamvfqepmtalnpvhRVGsQVDEVLRLHRRMPRAQRRAKVLE--MFRSVHLPDVERIYDAYPHQ-----LSGGQRQR 173
Cdd:PRK09544 68 ------------------RIG-YVPQKLYLDTTLPLTVNRFLRLRpgTKKEDILPALKRVQAGHLIDapmqkLSGGETQR 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 174 IVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNR 241
Cdd:PRK09544 129 VLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
310-523 |
1.40e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 65.29 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVrliepsaGRMLLGETDIARLSGAGLRPLRRK-VQIVFQDPYRSLNPR 388
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALM-------GFVRLASGKISILGQPTRQALQKNlVAYVPQSEEVDWSFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIEG------LLNFGMPRAQALVRAArtLGVVGLgPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:PRK15056 95 VLVEDVVMMGryghmgWLRRAKKRDRQIVTAA--LARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 463 ALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDtIAVMQHGKVVETGAAQTVLT 523
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDE-GKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
12-225 |
1.48e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 12 TSAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLpegileVSGGSARVL--GEDIVT 89
Cdd:PRK10247 3 ENSPLLQLQNVGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKS-TLLKIVASL------ISPTSGTLLfeGEDIST 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 90 ASARRRRELratrMAMVFQEPMTALNPVHrvgsqvDEVL---RLHRRMPRAQRRAKVLEMFrsvHLPdvERIYDAYPHQL 166
Cdd:PRK10247 74 LKPEIYRQQ----VSYCAQTPTLFGDTVY------DNLIfpwQIRNQQPDPAIFLDDLERF---ALP--DTILTKNIAEL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHD 225
Cdd:PRK10247 139 SGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
31-242 |
2.05e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.65 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 31 NRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-----PEGILEVSGGSARV---LGEDIvtasarrrrELRATR 102
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksAGSHIELLGRTVQRegrLARDI---------RKSRAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 103 MAMVFQEpmtaLNPVHRVgSQVDEVL----------RLHRRMPRAQRRAKVLEMFRSVHLPDveriydaYPHQ----LSG 168
Cdd:PRK09984 88 TGYIFQQ----FNLVNRL-SVLENVLigalgstpfwRTCFSWFTREQKQRALQALTRVGMVH-------FAHQrvstLSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
155-260 |
2.22e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 66.37 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 155 VERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIAD 234
Cdd:PRK13409 443 LERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISD 522
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489912973 235 RIVV--------------------MNR--GDLTETGTRDEILARPSQN 260
Cdd:PRK13409 523 RLMVfegepgkhghasgpmdmregMNRflKELGITFRRDEETGRPRVN 570
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
317-526 |
3.52e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 317 TLRRGEILGIVGESGSGKSTVARCIVRLIePSAGRMLLGETDIARLSGAGLRPLR-------RKVQI--VFQDPYRSLNP 387
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRaylsqqqTPPFAmpVFQYLTLHQPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 388 RRAVGESiiegllnfgmprAQALVRAARTLGVVglgpDVMRRYPHQFSGGQRQR-------LCIARALVMDPEVLVADEA 460
Cdd:PRK03695 97 KTRTEAV------------ASALNEVAEALGLD----DKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 461 VSALDVSVQAQVLELIEQVrERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPG 526
Cdd:PRK03695 161 MNSLDVAQQAALDRLLSEL-CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
30-254 |
3.59e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 3.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 30 GNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGileVSGGSARVLGEdiVTASARRRRELRATRMAMVFQE 109
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGG---GAPRGARVTGD--VTLNGEPLAAIDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 110 PMTALNPVHRVgsQVDEVLRLHRrMPRAQRRAKVLEMFRSVHLPDVERIyDAYP------HQLSGGQRQRIVIAMAL--- 180
Cdd:PRK13547 88 LPQAAQPAFAF--SAREIVLLGR-YPHARRAGALTHRDGEIAWQALALA-GATAlvgrdvTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 181 ------ILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEIL 254
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
317-549 |
4.15e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.20 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 317 TLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIArlsgagLRPlrRKVQIVFQDPYRSLNprravgESII 396
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------YKP--QYIKADYEGTVRDLL------SSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 397 EGLLNfgmpRAQALVRAARTLGVVGLgpdvMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELI 476
Cdd:cd03237 87 KDFYT----HPYFKTEIAKPLQIEQI----LDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 477 EQVRERTGVSVLFITHDLRVAAQVCDTIAVMQhGKVVETGAAQTVLT-RPGHAYTRALIDAAPGRgwDFRNFRP 549
Cdd:cd03237 159 RRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGVANPPQSlRSGMNRFLKNLDITFRR--DPETGRP 229
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
166-257 |
4.73e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.12 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRelQDRHQTAVLFITHDFGVVAEiADRIVVMNRGDLT 245
Cdd:PRK10789 452 LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLR--QWGEGRTVIISAHRLSALTE-ASEILVMQHGHIA 528
|
90
....*....|..
gi 489912973 246 ETGTRDEILARP 257
Cdd:PRK10789 529 QRGNHDQLAQQS 540
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
155-257 |
7.03e-11 |
|
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: 64.81 E-value: 7.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 155 VERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIAD 234
Cdd:COG1245 445 LEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISD 524
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489912973 235 RIVV--------------------MNR--GDLTETGTRDEILARP 257
Cdd:COG1245 525 RLMVfegepgvhghasgpmdmregMNRflKELGITFRRDEETGRP 569
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-210 |
8.51e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 8.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSvsvCGAGNRVV-RNLSLDVHAGETVCVVGESGSGKSvTSLAVM-GLLPegileVSGGSARVLGEDIVTASAR 93
Cdd:PRK13539 2 MLEGEDLA---CVRGGRVLfSGLSFTLAAGEALVLTGPNGSGKT-TLLRLIaGLLP-----PAAGTIKLDGGDIDDPDVA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 94 RrrelratrmAMVFQEPMTALNPVHRVGsqvdEVLRLHRRMpRAQRRAKVLEMFRSVHLPDVERIYDAYphqLSGGQRQR 173
Cdd:PRK13539 73 E---------ACHYLGHRNAMKPALTVA----ENLEFWAAF-LGGEELDIAAALEAVGLAPLAHLPFGY---LSAGQKRR 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 489912973 174 IVIAMALILEPKLLIADEPTTALDVTTQKQILALIRE 210
Cdd:PRK13539 136 VALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
155-260 |
9.07e-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: 62.43 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 155 VERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIAD 234
Cdd:cd03237 105 IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLAD 184
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 489912973 235 RIVV--------------------MNR--GDLTETGTRDEILARPSQN 260
Cdd:cd03237 185 RLIVfegepsvngvanppqslrsgMNRflKNLDITFRRDPETGRPRIN 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
165-255 |
9.89e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 64.18 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHqTAVLFITHDFGVVAEIADRIVVMN---- 240
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHegkl 483
|
90
....*....|....*.
gi 489912973 241 RGDLTETG-TRDEILA 255
Cdd:PRK13549 484 KGDLINHNlTQEQVME 499
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
166-279 |
1.15e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.31 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLT 245
Cdd:PRK10253 144 LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIV 223
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 489912973 246 ETGTRDEILARP--SQNYTRRL------VSSVPSLVPTQREA 279
Cdd:PRK10253 224 AQGAPKEIVTAEliERIYGLRCmiiddpVAGTPLVVPLGRTA 265
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-224 |
1.56e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.84 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSvcGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEgilevSGGSARVLGEDIVTASARRRR 96
Cdd:TIGR01189 1 LAARNLACS--RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-----DSGEVRWNGTPLAEQRDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEPMTALnpvhrvgsqvdEVLRLHRRMPRAQRRAkVLEMFRSVHLPDVEriyDAYPHQLSGGQRQRIVI 176
Cdd:TIGR01189 74 NILYLGHLPGLKPELSAL-----------ENLHFWAAIHGGAQRT-IEDALAAVGLTGFE---DLPAAQLSAGQQRRLAL 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITH 224
Cdd:TIGR01189 139 ARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHLAR-GGIVLLTTH 185
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
310-523 |
1.71e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 63.37 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLL--GETDIARLSGaglrplrrkvqivfqdpyrsLNP 387
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkgSAALIAISSG--------------------LNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 388 RRAVGESI-IEGLLnFGMPRAQALVRAARTLGVVGLGpdvmrRYPHQ----FSGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:PRK13545 99 QLTGIENIeLKGLM-MGLTKEKIKEIIPEIIEFADIG-----KFIYQpvktYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 463 ALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLT 523
Cdd:PRK13545 173 VGDQTFTKKCLDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
165-255 |
2.06e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.26 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDL 244
Cdd:PRK09700 409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRL 487
|
90
....*....|....*..
gi 489912973 245 TE------TGTRDEILA 255
Cdd:PRK09700 488 TQiltnrdDMSEEEIMA 504
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
312-492 |
2.68e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.06 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRplrrkvQIVFQDPYRSLNPRRAV 391
Cdd:TIGR01189 17 EGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHE------NILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESiieglLNFGMPRAQALVRAART-LGVVGLGpDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQA 470
Cdd:TIGR01189 91 LEN-----LHFWAAIHGGAQRTIEDaLAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|..
gi 489912973 471 QVLELIEQVRERTGvSVLFITH 492
Cdd:TIGR01189 165 LLAGLLRAHLARGG-IVLLTTH 185
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
16-248 |
3.25e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.58 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGllpEGILEVSGGSARVLGEDIVtasARRR 95
Cdd:PRK09580 1 MLSIKDLHVSV--EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG---REDYEVTGGTVEFKGKDLL---ELSP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRATRMAMVFQEPM------------TALNPVHRVGSQvdEVLRLHRRMPRAQRRAKVLEM-----FRSVHLpdveri 158
Cdd:PRK09580 73 EDRAGEGIFMAFQYPVeipgvsnqfflqTALNAVRSYRGQ--EPLDRFDFQDLMEEKIALLKMpedllTRSVNV------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 159 ydayphQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQtAVLFITHDFGVVAEIA-DRIV 237
Cdd:PRK09580 145 ------GFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIKpDYVH 217
|
250
....*....|.
gi 489912973 238 VMNRGDLTETG 248
Cdd:PRK09580 218 VLYQGRIVKSG 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
312-516 |
3.40e-10 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 60.36 E-value: 3.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEpsAGRMLLGETDIArlsGAGLRP--LRRKVQIVFQDPYrsLNPRR 389
Cdd:cd03234 24 NDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFN---GQPRKPdqFQKCVAYVRQDDI--LLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEgLLNFGMPRAQA-LVRAART----LGVVGLGPdVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSAL 464
Cdd:cd03234 97 TVRETLTY-TAILRLPRKSSdAIRKKRVedvlLRDLALTR-IGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 465 DvSVQAqvLELIEQVRE--RTGVSVLFITHDLRVAA-QVCDTIAVMQHGKVVETG 516
Cdd:cd03234 175 D-SFTA--LNLVSTLSQlaRRNRIVILTIHQPRSDLfRLFDRILLLSSGEIVYSG 226
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
308-515 |
5.53e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 61.73 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 308 VVAASEVDLTLRRGEILGIVGESGSGKSTVARcIVRLIEPSA---GRMLL-GET----DIaRLSGAglrplrRKVQIVFQ 379
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMK-VLSGVYPHGsyeGEILFdGEVcrfkDI-RDSEA------LGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 380 D----PYRSL-------NPRRAVGesIIEgllnfgmpRAQALVRAARTLGVVGLGPDvmrryPHQFSG----GQRQRLCI 444
Cdd:NF040905 86 ElaliPYLSIaeniflgNERAKRG--VID--------WNETNRRARELLAKVGLDES-----PDTLVTdigvGKQQLVEI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 445 ARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVET 515
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
314-538 |
6.61e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 62.27 E-value: 6.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAGLRPLRRKVQIVFQDPyrsLNPRRAvgE 393
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKA---LNEKYY--Q 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 394 SIIEG--LLnfgmPRAQALVRAART-LGVVGLgpdvmrryphQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQA 470
Cdd:TIGR00957 732 QVLEAcaLL----PDLEILPSGDRTeIGEKGV----------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 471 QVLE-LIEQVRERTGVSVLFITHDLRVAAQVcDTIAVMQHGKVVETGAAQTVLTRPGhAYTRALIDAAP 538
Cdd:TIGR00957 798 HIFEhVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG-AFAEFLRTYAP 864
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
310-516 |
6.93e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.34 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 310 AASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIArlsgAGLRPLRRKVQIVFQdpYRSLNPRR 389
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE----TNLDAVRQSLGMCPQ--HNILFHHL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEGLLNFGMPRAQALVRAARTLGVVGLGPDvMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHK-RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489912973 470 AQVLELIeqVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:TIGR01257 1098 RSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
166-466 |
7.61e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTqkqILALIRELQDrHQTAVLFITHDFGVVAEIADRIVVMNRGD-- 243
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VAWLEQFLHD-YPGTVVAVTHDRYFLDNVAGWILELDRGRgi 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 244 ---------LTETGTRDEILARPSQNYTRRL------VSSVP---------------SLVPTQREA----------PG-- 281
Cdd:PRK11819 240 pwegnysswLEQKAKRLAQEEKQEAARQKALkrelewVRQSPkarqakskarlaryeELLSEEYQKrnetneifipPGpr 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 282 -GEPVLRITGLGRTYAERrslfgatrtvVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETdia 360
Cdd:PRK11819 320 lGDKVIEAENLSKSFGDR----------LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGET--- 386
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 361 rlsgaglrplrrkVQIVFQDPYR-SLNPRRAVGESIIEGL--LNFG---MP-RAqalvraartlgVVGL----GPDVMRR 429
Cdd:PRK11819 387 -------------VKLAYVDQSRdALDPNKTVWEEISGGLdiIKVGnreIPsRA-----------YVGRfnfkGGDQQKK 442
|
330 340 350
....*....|....*....|....*....|....*..
gi 489912973 430 YpHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDV 466
Cdd:PRK11819 443 V-GVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-271 |
8.06e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 8.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGllpegILEVSGGSARVLGEDIVTASARRRRELratrMAMVFQEPMT 112
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFR-----IVELEKGRIMIDDCDVAKFGLTDLRRV----LSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 113 ALNPVhrvgsqvdevlRLHRRMPRAQRRAKVLEMFRSVHLPDVERI----YDAYPHQ----LSGGQRQRIVIAMALILEP 184
Cdd:PLN03232 1322 FSGTV-----------RFNIDPFSEHNDADLWEALERAHIKDVIDRnpfgLDAEVSEggenFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 185 KLLIADEPTTALDVTTQKQILALIRElqDRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTETGTRDEILARPSQNYTRR 264
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFRM 1467
|
....*..
gi 489912973 265 LVSSVPS 271
Cdd:PLN03232 1468 VHSTGPA 1474
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
166-255 |
1.22e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.61 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLFITHDFGVVAEIADRIVVMNRG--- 242
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLA-QEGVAIIVVSSELAEVLGLSDRVLVIGEGklk 482
|
90
....*....|....*
gi 489912973 243 -DLTETG-TRDEILA 255
Cdd:TIGR02633 483 gDFVNHAlTQEQVLA 497
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
166-254 |
1.74e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQtAVLFITHDFGVVAEIADRIVVMNRGDL- 244
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGITDRILVMSNGLVa 470
|
90
....*....|....
gi 489912973 245 ----TETGTRDEIL 254
Cdd:PRK10982 471 givdTKTTTQNEIL 484
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
304-527 |
1.80e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 304 ATRTVVAASEVDLTLRRGEILGIVGESGSGKSTVARCIV-RLIEPSAGRMLLGETDIArLSGaglRPLRRKvqivfqDPY 382
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAPRGARVTGDVT-LNG---EPLAAI------DAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 383 RsLNPRRAVGESIIEGLLNFGM------------PRAQALVR-----AARTLGVVGLGPdVMRRYPHQFSGGQRQRLCIA 445
Cdd:PRK13547 80 R-LARLRAVLPQAAQPAFAFSAreivllgryphaRRAGALTHrdgeiAWQALALAGATA-LVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 446 RAL---------VMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETG 516
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
250
....*....|.
gi 489912973 517 AAQTVLTrPGH 527
Cdd:PRK13547 238 APADVLT-PAH 247
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
329-509 |
2.21e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.43 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 329 ESGSGKSTVarcivrlIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYrslnprrAVGESIIEGLlNFGMPRA- 407
Cdd:PTZ00265 1263 EGGSGEDST-------VFKNSGKILLDGVDICDYN---LKDLRNLFSIVSQEPM-------LFNMSIYENI-KFGKEDAt 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 408 -QALVRAARTLGV------------VGLGPdvmrrYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLE 474
Cdd:PTZ00265 1325 rEDVKRACKFAAIdefieslpnkydTNVGP-----YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
|
170 180 190
....*....|....*....|....*....|....*.
gi 489912973 475 LIEQVRERTGVSVLFITHdlRVAA-QVCDTIAVMQH 509
Cdd:PTZ00265 1400 TIVDIKDKADKTIITIAH--RIASiKRSDKIVVFNN 1433
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
28-242 |
2.50e-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: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 28 GAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGllpegilEVSGGSARVLGEDIVTASARRRRELRATRMAMVF 107
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG-------EMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 108 --QEPMTaLNpvhrvgSQVDEVLRLHRrmPRAQRRAKVLEMFRSVHlPDVeriyDAYPH-----------QLSGGQRQRI 174
Cdd:cd03290 84 aaQKPWL-LN------ATVEENITFGS--PFNKQRYKAVTDACSLQ-PDI----DLLPFgdqteigergiNLSGGQRQRI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 175 VIAMALILEPKLLIADEPTTALDVTTQKQIL--ALIRELQDRHQTAVLfITHDFGVVAEiADRIVVMNRG 242
Cdd:cd03290 150 CVARALYQNTNIVFLDDPFSALDIHLSDHLMqeGILKFLQDDKRTLVL-VTHKLQYLPH-ADWIIAMKDG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
285-528 |
2.86e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 59.75 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLRITGLGRTYaerrslfGATRtvvAASEVDLTLRRGEILGIVGESGSGKSTVARCI--VRLIEpsAGR-MLLGEtDIAR 361
Cdd:NF033858 1 VARLEGVSHRY-------GKTV---ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagARKIQ--QGRvEVLGG-DMAD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 362 lsgaglRPLRRKV--QIVF--QDPYRSLNPRRAVGESI-IEGLLnFGMPRAQALVRAARTLGVVGLGPdVMRRYPHQFSG 436
Cdd:NF033858 68 ------ARHRRAVcpRIAYmpQGLGKNLYPTLSVFENLdFFGRL-FGQDAAERRRRIDELLRATGLAP-FADRPAGKLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 437 GQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVR-ERTGVSVLfithdlrVA------AQVCDTIAVMQH 509
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRaERPGMSVL-------VAtaymeeAERFDWLVAMDA 212
|
250
....*....|....*....
gi 489912973 510 GKVVETGAAQTVLTRPGHA 528
Cdd:NF033858 213 GRVLATGTPAELLARTGAD 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
17-249 |
3.13e-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: 60.03 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEgilevSGGSARVLGEDIVTASARRRR 96
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP-----TSGTVLVGGKDIETNLDAVRQ 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ElratrMAMVFQEpmtalNPVHRVGSQVDEVLRLHRRMPRAQRRAKvLEMFRSVHLPDVERIYDAYPHQLSGGQRQRIVI 176
Cdd:TIGR01257 1004 S-----LGMCPQH-----NILFHHLTVAEHILFYAQLKGRSWEEAQ-LEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 177 AMALILEPKLLIADEPTTALDVTTQKQILALIreLQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGT 249
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
11-249 |
3.48e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 57.73 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 11 DTSAAVLAIRNLSVSVcgAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGILEvsgGSARVLGEDIVta 90
Cdd:CHL00131 2 NKNKPILEIKNLHASV--NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKILE---GDILFKGESIL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 sARRRRELRATRMAMVFQepmtalNPVHRVGSQVDEVLRL---HRRMPRAQRRAKVLEmFRSVHLPDVErIYDAYPHQL- 166
Cdd:CHL00131 75 -DLEPEERAHLGIFLAFQ------YPIEIPGVSNADFLRLaynSKRKFQGLPELDPLE-FLEIINEKLK-LVGMDPSFLs 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 -------SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITH-----DFgvvaEIAD 234
Cdd:CHL00131 146 rnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITHyqrllDY----IKPD 220
|
250
....*....|....*
gi 489912973 235 RIVVMNRGDLTETGT 249
Cdd:CHL00131 221 YVHVMQNGKIIKTGD 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
314-514 |
3.73e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 59.04 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLgetDIARLSGAGLRPLRRKVQIVFQDPY---RSLNPRRA 390
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL---DGQPVTADNREAYRQLFSAVFSDFHlfdRLLGLDGE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 391 VGESIIEGLLN-FGMpraQALVR-AARTLGVVGLgpdvmrryphqfSGGQRQRLciarALVM----DPEVLVADEAvsAL 464
Cdd:COG4615 428 ADPARARELLErLEL---DHKVSvEDGRFSTTDL------------SQGQRKRL----ALLValleDRPILVFDEW--AA 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 465 DvsvqaQ--------VLELIEQVRERtGVSVLFITHDLRvAAQVCDTIAVMQHGKVVE 514
Cdd:COG4615 487 D-----QdpefrrvfYTELLPELKAR-GKTVIAISHDDR-YFDLADRVLKMDYGKLVE 537
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
164-239 |
3.92e-09 |
|
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: 55.83 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 164 HQLSGGQRQRIVIAMALILEPK----LLIADEPTTALDVTTQKQILALIRELQDrHQTAVLFITHDFGvVAEIADRIVVM 239
Cdd:cd03227 76 LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLV-KGAQVIVITHLPE-LAELADKLIHI 153
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
152-260 |
4.99e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 4.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 152 LPD-VERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVa 230
Cdd:PTZ00265 565 LPDkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI- 643
|
90 100 110
....*....|....*....|....*....|
gi 489912973 231 EIADRIVVMNRGDLTETGTRDEILARPSQN 260
Cdd:PTZ00265 644 RYANTIFVLSNRERGSTVDVDIIGEDPTKD 673
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
166-252 |
5.00e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.65 E-value: 5.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQtAVLFITHDFGVVAEIADRIVVMNRGDLT 245
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGK-GVIVISSELPELLGMCDRIYVMNEGRIT 483
|
....*..
gi 489912973 246 ETGTRDE 252
Cdd:NF040905 484 GELPREE 490
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
314-493 |
5.15e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.83 E-value: 5.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLgetDIARLSGAGLRPLRRKVQIVFQDPY---RSLNPR-R 389
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL---DGKPVTAEQPEDYRKLFSAVFTDFHlfdQLLGPEgK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEGLLNFGMPRAQALVRAARTLGVvglgpdvmrryphQFSGGQRQRLCIARALVMDPEVLVADEAvsALDVSVQ 469
Cdd:PRK10522 419 PANPALVEKWLERLKMAHKLELEDGRISNL-------------KLSKGQKKRLALLLALAEERDILLLDEW--AADQDPH 483
|
170 180
....*....|....*....|....*..
gi 489912973 470 AQ---VLELIEQVRErTGVSVLFITHD 493
Cdd:PRK10522 484 FRrefYQVLLPLLQE-MGKTIFAISHD 509
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
16-224 |
5.26e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 5.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 16 VLAIRNLSvsvCGAGNRVV-RNLSLDVHAGETVCVVGESGSGKsvTSLAVM--GLLP--EGILEVSGGSARVLGEDivta 90
Cdd:PRK13538 1 MLEARNLA---CERDERILfSGLSFTLNAGELVQIEGPNGAGK--TSLLRIlaGLARpdAGEVLWQGEPIRRQRDE---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 91 sarrrrelratrmamvFQEPMTALNpvHRVGSQVD----EVLRLHRRMPRAQRRAKVLEMFRSVHLPDVEriyDAYPHQL 166
Cdd:PRK13538 72 ----------------YHQDLLYLG--HQPGIKTEltalENLRFYQRLHGPGDDEALWEALAQVGLAGFE---DVPVRQL 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIrelqDRHQTA---VLFITH 224
Cdd:PRK13538 131 SAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL----AQHAEQggmVILTTH 187
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
312-499 |
5.42e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSG------------AGLRPLrrkvqivfq 379
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeyhqdllylghqPGIKTE--------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 380 dpyrsLNPrravgesiIEGLLNF----GMPRAQALVRAartLGVVGLG--PDVmrryP-HQFSGGQRQRLCIARALVMDP 452
Cdd:PRK13538 89 -----LTA--------LENLRFYqrlhGPGDDEALWEA---LAQVGLAgfEDV----PvRQLSAGQQRRVALARLWLTRA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489912973 453 EVLVADEAVSALDVSVQAQVLELIEQVRERTGVsVLFITH-DLRVAAQ 499
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQHAEQGGM-VILTTHqDLPVASD 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
166-252 |
7.11e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 7.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRhQTAVLFITHDFGVVAEIADRIVVMNRGDLT 245
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
....*..
gi 489912973 246 ETGTRDE 252
Cdd:PRK11288 476 GELAREQ 482
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
32-255 |
1.56e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 32 RVVRNLSLDVHAGETVCVVGESGSGKSvTSLAVMGLLPEGilevSGGSARVLGEDIVTASArrrrelratrmAMVFQEPM 111
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKT-TLLGTLCGDPRA----TSGRIVFDGKDITDWQT-----------AKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 112 TALNPVHRVGSQ--VDEVLRL----HRRMPRAQRRAKVLEMFRSVHLPDVERiydayPHQLSGGQRQRIVIAMALILEPK 185
Cdd:PRK11614 83 AIVPEGRRVFSRmtVEENLAMggffAERDQFQERIKWVYELFPRLHERRIQR-----AGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 186 LLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEILA 255
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMT-IFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
17-236 |
2.05e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 54.42 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSvsvCGAGNRVV-RNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLPEGILEVS---GGSARVLGEdivtasa 92
Cdd:cd03231 1 LEADELT---CERDGRALfSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlngGPLDFQRDS------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 93 rrrrelRATRMAMVFQEP--MTALNPVhrvgsqvdEVLRLHRRMpraQRRAKVLEMFRSVHLPDVEriyDAYPHQLSGGQ 170
Cdd:cd03231 71 ------IARGLLYLGHAPgiKTTLSVL--------ENLRFWHAD---HSDEQVEEALARVGLNGFE---DRPVAQLSAGQ 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 171 RQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRI 236
Cdd:cd03231 131 QRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
154-239 |
2.34e-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: 55.07 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 154 DVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQdRHQTAVLFITHDFGVVAEIA 233
Cdd:cd03236 128 ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELA-EDDNYVLVVEHDLAVLDYLS 206
|
....*.
gi 489912973 234 DRIVVM 239
Cdd:cd03236 207 DYIHCL 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
308-515 |
3.48e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 55.89 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 308 VVAASEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAglRPLRRKVQIVFQDpyrsLNP 387
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSK--EALENGISMVHQE----LNL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 388 --RRAVGESIIEGLlnfgMPRAQALVRAAR----TLGVVG-LGPDV-MRRYPHQFSGGQRQRLCIARALVMDPEVLVADE 459
Cdd:PRK10982 85 vlQRSVMDNMWLGR----YPTKGMFVDQDKmyrdTKAIFDeLDIDIdPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 460 AVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVMQHGKVVET 515
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIAT 215
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
166-238 |
5.24e-08 |
|
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: 52.96 E-value: 5.24e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVV 238
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHV 144
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
281-516 |
5.84e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 281 GGEPvlRITGLGRTYAERRSLFGATRTVVAasevdltlrrGEILGIVGESGSGKSTVARCIVRLIEPS--AGRMLLGETD 358
Cdd:PLN03211 66 GHKP--KISDETRQIQERTILNGVTGMASP----------GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 359 IARlsgaglrPLRRKVQIVFQDPYrsLNPRRAVGESIIEGLLnFGMPRA---QALVRAART----LGVVGLGPDVM-RRY 430
Cdd:PLN03211 134 PTK-------QILKRTGFVTQDDI--LYPHLTVRETLVFCSL-LRLPKSltkQEKILVAESviseLGLTKCENTIIgNSF 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 431 PHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHG 510
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
....*.
gi 489912973 511 KVVETG 516
Cdd:PLN03211 284 RCLFFG 289
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
315-493 |
7.44e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 315 DLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLgETD--IARLSgaglrplrrkvqivfQDPyrslnPRRAVG 392
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDliVARLQ---------------QDP-----PRNVEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 393 ---ESIIEGLLNFG------------------------MPRAQALV----------RAARTLGVVGLGPDVMRRyphQFS 435
Cdd:PRK11147 82 tvyDFVAEGIEEQAeylkryhdishlvetdpseknlneLAKLQEQLdhhnlwqlenRINEVLAQLGLDPDAALS---SLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 436 GGQRQRLCIARALVMDPEVLVADEAVSALDVsvqaQVLELIEQVRERTGVSVLFITHD 493
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
134-253 |
9.42e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 54.36 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 134 MPRAQRRAKVLEMFRSVHLPDVERIYDAyphQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQd 213
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAA---KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMV- 191
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 489912973 214 RHQTAVLFITHDFGVVAEIADRIVVMNRGDLTETGTRDEI 253
Cdd:NF000106 192 RDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
9-274 |
9.94e-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: 55.40 E-value: 9.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 9 AGDTSAAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGllpegILEVSGGSARVLGEDIV 88
Cdd:TIGR01257 1930 SGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG-----DTTVTSGDATVAGKSIL 2004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 89 TASARRRRELRATRMAMVFQEPMTAlnpvhrvgsqvDEVLRLHRRMpraqrrakvlemfRSVHLPDVERIYD-------- 160
Cdd:TIGR01257 2005 TNISDVHQNMGYCPQFDAIDDLLTG-----------REHLYLYARL-------------RGVPAEEIEKVANwsiqslgl 2060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 161 -AYPHQL----SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQ----ILALIRElqdrhQTAVLFITHDFGVVAE 231
Cdd:TIGR01257 2061 sLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMlwntIVSIIRE-----GRAVVLTSHSMEECEA 2135
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 489912973 232 IADRIVVMNRGDLTETGTRDEILARPSQNY--TRRLVSSVPSLVP 274
Cdd:TIGR01257 2136 LCTRLAIMVKGAFQCLGTIQHLKSKFGDGYivTMKIKSPKDDLLP 2180
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
313-474 |
1.17e-07 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 53.32 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMllgetdiaRLSGaglrplrrkvQIVFQDPYRSLNPrRAVG 392
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------KHSG----------RISFSSQFSWIMP-GTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 393 ESIIEGlLNFGMPRAQALVRAARTLGVVGLGPD----VMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSV 468
Cdd:cd03291 116 ENIIFG-VSYDEYRYKSVVKACQLEEDITKFPEkdntVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
....*.
gi 489912973 469 QAQVLE 474
Cdd:cd03291 195 EKEIFE 200
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
312-516 |
1.17e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.74 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTvarcivrLIepSAgrmLLGEtdIARLSGAGLrPLRRKVQIVfqdPYRSLNPRRAV 391
Cdd:PLN03130 634 SNINLDVPVGSLVAIVGSTGEGKTS-------LI--SA---MLGE--LPPRSDASV-VIRGTVAYV---PQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 392 GESIIegllnFGMPRAQAlvRAARTLGVVGLGPDVMRRYPH----------QFSGGQRQRLCIARALVMDPEVLVADEAV 461
Cdd:PLN03130 696 RDNIL-----FGSPFDPE--RYERAIDVTALQHDLDLLPGGdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 462 SALDVSVQAQVLE--LIEQVRERTGVSVlfiTHDLRVAAQVcDTIAVMQHGKVVETG 516
Cdd:PLN03130 769 SALDAHVGRQVFDkcIKDELRGKTRVLV---TNQLHFLSQV-DRIILVHEGMIKEEG 821
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
320-496 |
1.58e-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: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 320 RGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSGAglrplrrkvqivfqdpyrslnprravgesiiegl 399
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVL---------------------------------- 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 400 lnfgmpraqalvraartlgvVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIE-- 477
Cdd:smart00382 47 --------------------DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|..
gi 489912973 478 ---QVRERTGVSVLFITHDLRV 496
Cdd:smart00382 107 lllLLKSEKNLTVILTTNDEKD 128
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
44-242 |
1.87e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 44 GETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDivtasaRRRRELRATRMAMVFQEPMTALNPVHRVGSQ 123
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRI-----QGNNFTGTILANN------RKPTKQILKRTGFVTQDDILYPHLTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 124 VDEVLRLHRRMPRAQRRAKVLEMFRSVHLPDVER--IYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQ 201
Cdd:PLN03211 163 FCSLLRLPKSLTKQEKILVAESVISELGLTKCENtiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 489912973 202 KQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:PLN03211 243 YRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEG 283
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
167-271 |
2.19e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRElqDRHQTAVLFITHDFGVVAEiADRIVVMNRGDLTE 246
Cdd:PLN03130 1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
|
90 100
....*....|....*....|....*
gi 489912973 247 TGTRDEILARPSQNYTRRLVSSVPS 271
Cdd:PLN03130 1453 FDTPENLLSNEGSAFSKMVQSTGAA 1477
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
319-507 |
2.22e-07 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 2.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 319 RRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLlGETD----------------IARLSGAGLRPLRrKVQIVFQDPy 382
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDwdeildefrgselqnyFTKLLEGDVKVIV-KPQYVDLIP- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 383 rslnprRAVGESIIEgLLNfgmpRAQALVRAARTLGVVGLGPdVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVS 462
Cdd:cd03236 101 ------KAVKGKVGE-LLK----KKDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSS 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489912973 463 ALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVCDTIAVM 507
Cdd:cd03236 169 YLDIKQRLNAARLIRELAED-DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
315-524 |
2.36e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 315 DLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETDIARLSgagLRPLRRKVQIVFQDPYRSL------NPR 388
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLS---FEQLQKLVSDEWQRNNTDMlspgedDTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 RAVGESIIEGLLNfgMPRAQALvraARTLGVVGLgpdVMRRYPHQFSGGQRQRLcIARALVMDPEVLVADEAVSALDVSV 468
Cdd:PRK10938 100 RTTAEIIQDEVKD--PARCEQL---AQQFGITAL---LDRRFKYLSTGETRKTL-LCQALMSEPDLLILDEPFDGLDVAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 469 QAQVLELIEQVRERTGVSVLFITHDLRVAAQVcDTIAVMQHGKVVETGAAQTVLTR 524
Cdd:PRK10938 171 RQQLAELLASLHQSGITLVLVLNRFDEIPDFV-QFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
283-511 |
3.83e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 52.70 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 EPVLRITGLGRTYAERRSLFGATRTVVAasevdltlrrGEILGIVGESGSGKSTVARCIVRLIEPSAGRML-LGETdiAR 361
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYP----------GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILyLGKE--VT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 362 LSG------AGlrplrrkVQIVFQDpyrsLN--PRRAVGESI--------IEGLLNFGMPRAQALVRAARtLGVvglgpd 425
Cdd:PRK10762 70 FNGpkssqeAG-------IGIIHQE----LNliPQLTIAENIflgrefvnRFGRIDWKKMYAEADKLLAR-LNL------ 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 426 vmRRYPHQFSG----GQRQRLCIARALVMDPEVLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHDLRVAAQVC 501
Cdd:PRK10762 132 --RFSSDKLVGelsiGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEIC 208
|
250
....*....|
gi 489912973 502 DTIAVMQHGK 511
Cdd:PRK10762 209 DDVTVFRDGQ 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
166-242 |
6.56e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 6.56e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 166 LSGGQRQRIVIA--MALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEiADRIVVMNRG 242
Cdd:cd03238 88 LSGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNT-VILIEHNLDVLSS-ADWIIDFGPG 164
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
166-245 |
8.81e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.03 E-value: 8.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLI-ADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRGDL 244
Cdd:TIGR00956 902 LNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGGQ 981
|
.
gi 489912973 245 T 245
Cdd:TIGR00956 982 T 982
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
166-346 |
1.00e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.75 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPK--LLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAeIADRIVVMNR-- 241
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRDQGNT-VLLVEHDEQMIS-LADRIIDIGPga 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 242 ----GDLTETGTRDEILARPSQNYTRRLVSSVPSLVPTQREAPGGEPVLritglgrTYAERRSLfgatrtvvaaSEVDLT 317
Cdd:PRK00635 555 gifgGEVLFNGSPREFLAKSDSLTAKYLRQELTIPIPEKRTNSLGTLTL-------SKATKHNL----------KDLTIS 617
|
170 180 190
....*....|....*....|....*....|....
gi 489912973 318 LRRGEILGIVGESGSGKS-----TVARCIVRLIE 346
Cdd:PRK00635 618 LPLGRLTVVTGVSGSGKSslindTLVPAVEEFIE 651
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
44-243 |
1.26e-06 |
|
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: 48.14 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 44 GETVCVVGESGSGKSVTSLAVMGLLPE---GILEVSGGsarvlgedivtasarrrrelratrmamvfqepmtalnpvhrv 120
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPpggGVIYIDGE------------------------------------------ 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 121 gsqvdevlrlhrrmpraqrrakvlEMFRSVHLPDVERIYDAYPHQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTT 200
Cdd:smart00382 40 ------------------------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQ 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489912973 201 QKQILALIRELQD-----RHQTAVLFITHDFGVVAE-----IADRIVVMNRGD 243
Cdd:smart00382 96 EALLLLLEELRLLlllksEKNLTVILTTNDEKDLGPallrrRFDRRIVLLLIL 148
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
166-336 |
1.36e-06 |
|
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: 51.17 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMAL--ILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEiADRIVVM---- 239
Cdd:TIGR00630 489 LSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNT-LIVVEHDEDTIRA-ADYVIDIgpga 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 240 --NRGDLTETGTRDEILARPsQNYTRRLVSSVPSL-VPTQREAPGGEpVLRITGlgrtyAERRSLfgatrtvvaaSEVDL 316
Cdd:TIGR00630 567 geHGGEVVASGTPEEILANP-DSLTGQYLSGRKKIeVPAERRPGNGK-FLTLKG-----ARENNL----------KNITV 629
|
170 180
....*....|....*....|
gi 489912973 317 TLRRGEILGIVGESGSGKST 336
Cdd:TIGR00630 630 SIPLGLFTCITGVSGSGKST 649
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-258 |
1.42e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.32 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMgllpeGILEVSGGSARVLGEDIvtasARRRRELRATRMAMVFQEPMT 112
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFM-----RMVEVCGGEIRVNGREI----GAYGLRELRRQFSMIPQDPVL 1395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 113 ALNPVHrvgSQVDEVLrlhrrmpraqrRAKVLEMFRSVHLPDV-ERI------YDAYPHQ----LSGGQRQRIVIAMALI 181
Cdd:PTZ00243 1396 FDGTVR---QNVDPFL-----------EASSAEVWAALELVGLrERVasesegIDSRVLEggsnYSVGQRQLMCMARALL 1461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 182 LEPKLLI-ADEPTTALDVTTQKQILALIRELQDRHqtAVLFITHDFGVVAEIaDRIVVMNRGDLTETGTRDEILARPS 258
Cdd:PTZ00243 1462 KKGSGFIlMDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQ 1536
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
173-493 |
1.55e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 173 RIVIAMALILEPKLLIADEPTTALDVTTqkqILALIRELQDRHQTAVLfITHD--F--GVVAEIADrivvMNRGDLT-ET 247
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLDINT---IRWLEDVLNERNSTMII-ISHDrhFlnSVCTHMAD----LDYGELRvYP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 248 GTRDEILARPSQNYTRRL---------VSSVPSLV-----------------------------PTQREAP-----GGEP 284
Cdd:PRK15064 235 GNYDEYMTAATQARERLLadnakkkaqIAELQSFVsrfsanaskakqatsrakqidkikleevkPSSRQNPfirfeQDKK 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 285 VLR----ITGLGRTYaERRSLFgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGETdiA 360
Cdd:PRK15064 315 LHRnaleVENLTKGF-DNGPLF---------KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN--A 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 361 RLsgaGLRPlrrkvqivfQDPYRSLnprrAVGESIIEGLLNFGMPR--AQAlVRAarTLGVVGLGPDVMRRYPHQFSGGQ 438
Cdd:PRK15064 383 NI---GYYA---------QDHAYDF----ENDLTLFDWMSQWRQEGddEQA-VRG--TLGRLLFSQDDIKKSVKVLSGGE 443
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 439 RQRLCIARALVMDPEVLVADEAVSALDV-SVQA--QVLELIEQvrertgvSVLFITHD 493
Cdd:PRK15064 444 KGRMLFGKLMMQKPNVLVMDEPTNHMDMeSIESlnMALEKYEG-------TLIFVSHD 494
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
166-256 |
2.31e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 50.71 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALI--RELQDRHQTAVLfITHDFGVVAEIaDRIVVMNRGD 243
Cdd:TIGR00957 761 LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigPEGVLKNKTRIL-VTHGISYLPQV-DVIIVMSGGK 838
|
90
....*....|...
gi 489912973 244 LTETGTRDEILAR 256
Cdd:TIGR00957 839 ISEMGSYQELLQR 851
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
4-255 |
2.62e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 4 APYPPAgDTSAAVLAIRNLSVSVCGAGNR-VVRNLSLDVHAGETVCVVGESGSGKsvTSL--AVMGLLPEgileVSGGSA 80
Cdd:PLN03130 603 LPNPPL-EPGLPAISIKNGYFSWDSKAERpTLSNINLDVPVGSLVAIVGSTGEGK--TSLisAMLGELPP----RSDASV 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 81 RVLGedivtasarrrrelratRMAMVFQEPMTaLNPVHR----VGSQVDEvlrlhrrmPRAQRRAKVLEMFRSVH-LP-- 153
Cdd:PLN03130 676 VIRG-----------------TVAYVPQVSWI-FNATVRdnilFGSPFDP--------ERYERAIDVTALQHDLDlLPgg 729
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 154 DVERIYDAYPHqLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQIL--ALIRELqdRHQTAVLfITHDFGVVAE 231
Cdd:PLN03130 730 DLTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFdkCIKDEL--RGKTRVL-VTNQLHFLSQ 805
|
250 260
....*....|....*....|....
gi 489912973 232 IaDRIVVMNRGDLTETGTRDEILA 255
Cdd:PLN03130 806 V-DRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
167-512 |
2.82e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTqkqILALIRELQDRHQTAVLfITHDFGVVAEIADRIVVMNRGDLTE 246
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLIL-ISHDRDFLDPIVDKIIHIEQQSLFE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 247 -TGT-------RDEILARPS-------------QNYTRRL----------VSSVPSLVPTQREAPGG------------- 282
Cdd:PRK10636 227 yTGNyssfevqRATRLAQQQamyesqqervahlQSYIDRFrakatkakqaQSRIKMLERMELIAPAHvdnpfhfsfrape 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 283 ---EPVLRITGLGRTYAERRSLfgatrtvvaaSEVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGrmllgetDI 359
Cdd:PRK10636 307 slpNPLLKMEKVSAGYGDRIIL----------DSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-------EI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 360 ARLSGAGLRPLRRKvQIVFQdpyrslnprRAvGESIIEGLLNFGMPRAQALVRaaRTLGVVGLGPDVMRRYPHQFSGGQR 439
Cdd:PRK10636 370 GLAKGIKLGYFAQH-QLEFL---------RA-DESPLQHLARLAPQELEQKLR--DYLGGFGFQGDKVTEETRRFSGGEK 436
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 440 QRLCIARALVMDPEVLVADEAVSALDVSV-QAqvleLIEQVRERTGVSVLfITHDLRVAAQVCDTIAVMQHGKV 512
Cdd:PRK10636 437 ARLVLALIVWQRPNLLLLDEPTNHLDLDMrQA----LTEALIDFEGALVV-VSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
166-337 |
3.54e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALIL---EPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVaEIADRIVVM--- 239
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHT-VVIIEHNMHVV-KVADYVLELgpe 887
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 240 --NRGD-LTETGTRDEI--LARPSQNYTRRLVSSVPSLvPTQREAPGGEPVLRITGLGRTYAERrslfgatrtvvaASEV 314
Cdd:PRK00635 888 ggNLGGyLLASCSPEELihLHTPTAKALRPYLSSPQEL-PYLPDPSPKPPVPADITIKNAYQHN------------LKHI 954
|
170 180
....*....|....*....|...
gi 489912973 315 DLTLRRGEILGIVGESGSGKSTV 337
Cdd:PRK00635 955 DLSLPRNALTAVTGPSASGKHSL 977
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
166-242 |
3.66e-06 |
|
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: 48.03 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLF--------ITHDFgvvaeiaDRIV 237
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVslyqasdeIYDLF-------DKVL 191
|
....*
gi 489912973 238 VMNRG 242
Cdd:cd03233 192 VLYEG 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
409-466 |
3.86e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 3.86e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 409 ALVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDV 466
Cdd:PLN03073 320 AEARAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
317-507 |
4.66e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.42 E-value: 4.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 317 TLRRGEILGIVGESGSGKSTVARCIVRLIEPSagrmlLGETD--------------------IARLSGAGLRPLRrKVQI 376
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEeepswdevlkrfrgtelqnyFKKLYNGEIKVVH-KPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 377 VFQDPyrslnprRAVGESIIEgllnfgmpraqaLVRAARTLGV-------VGLGPdVMRRYPHQFSGGQRQRLCIARALV 449
Cdd:PRK13409 169 VDLIP-------KVFKGKVRE------------LLKKVDERGKldevverLGLEN-ILDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489912973 450 MDPEVLVADEAVSALDVSVQAQVLELIeqvRERT-GVSVLFITHDLRVAAQVCDTIAVM 507
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQRLNVARLI---RELAeGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
318-528 |
9.30e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.50 E-value: 9.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 318 LRRGEILGIVGESGSGKSTvarcivrLIEPSAGRM---LLGETDIArLSG--AGLRPLRRKVQIVFQDP--------YRS 384
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTT-------LMNALAFRSpkgVKGSGSVL-LNGmpIDAKEMRAISAYVQQDDlfiptltvREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 385 LN-------PRRAVGES---IIEGLLnfgmpRAQALVRAARTL-GVvglgPDVMRryphQFSGGQRQRLCIARALVMDPE 453
Cdd:TIGR00955 120 LMfqahlrmPRRVTKKEkreRVDEVL-----QALGLRKCANTRiGV----PGRVK----GLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 454 VLVADEAVSALDVSVQAQVLELIEQVRERtGVSVLFITHdlRVAAQV---CDTIAVMQHGKVVETGaaqtvltRPGHA 528
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQK-GKTIICTIH--QPSSELfelFDKIILMAEGRVAYLG-------SPDQA 254
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
312-516 |
1.13e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 312 SEVDLTLRRGEILGIVGESGSGKSTvarcivrLIEPSAGRMLLGETDIARLSG-------------AGLRPlrrkvQIVF 378
Cdd:PLN03232 634 SDINLEIPVGSLVAIVGGTGEGKTS-------LISAMLGELSHAETSSVVIRGsvayvpqvswifnATVRE-----NILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 379 QDPYRSLNPRRAVGESIIEGLLNfgmpraqalVRAARTLGVVG-LGPDVmrryphqfSGGQRQRLCIARALVMDPEVLVA 457
Cdd:PLN03232 702 GSDFESERYWRAIDVTALQHDLD---------LLPGRDLTEIGeRGVNI--------SGGQKQRVSMARAVYSNSDIYIF 764
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 458 DEAVSALDVSVQAQVLE--LIEQVRERTGVsvlFITHDLRVAAQVcDTIAVMQHGKVVETG 516
Cdd:PLN03232 765 DDPLSALDAHVAHQVFDscMKDELKGKTRV---LVTNQLHFLPLM-DRIILVSEGMIKEEG 821
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
165-512 |
1.29e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVttqKQILALIRELQDRHQTaVLFITH--DF--GVVAEI---ADRIV 237
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL---HAVLWLETYLLKWPKT-FIVVSHarEFlnTVVTDIlhlHGQKL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 238 VMNRGDL-TETGTRDEIL-----ARPSQNYTR----------RLVSSVPSLV--------------------------PT 275
Cdd:PLN03073 420 VTYKGDYdTFERTREEQLknqqkAFESNERSRshmqafidkfRYNAKRASLVqsrikaldrlghvdavvndpdykfefPT 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 276 QREAPGGePVLRITGLGRTYAERRSLFGATRTvvaasEVDLTLRrgeiLGIVGESGSGKSTVARCIVRLIEPSAGRMllg 355
Cdd:PLN03073 500 PDDRPGP-PIISFSDASFGYPGGPLLFKNLNF-----GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTV--- 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 356 etdiarlsgaglrplrrkvqivfqdpYRSLNPRRAV-GESIIEGL------LNF------GMPRAQalVRAArtLGVVGL 422
Cdd:PLN03073 567 --------------------------FRSAKVRMAVfSQHHVDGLdlssnpLLYmmrcfpGVPEQK--LRAH--LGSFGV 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 423 GPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDV-SVQAqvleLIEQVRERTGvSVLFITHDLRVAAQVC 501
Cdd:PLN03073 617 TGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLdAVEA----LIQGLVLFQG-GVLMVSHDEHLISGSV 691
|
410
....*....|.
gi 489912973 502 DTIAVMQHGKV 512
Cdd:PLN03073 692 DELWVVSEGKV 702
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
314-516 |
2.05e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 46.32 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIV--RLIEPSAGRMLLGETDIARLSgaglrPLRRK---VQIVFQDPYRslnpr 388
Cdd:PRK09580 20 LNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELS-----PEDRAgegIFMAFQYPVE----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 389 ravgesiIEGLLN-FGMPRAQALVRAAR----------------TLGVVGLGPDVMRRYPHQ-FSGGQRQRLCIARALVM 450
Cdd:PRK09580 90 -------IPGVSNqFFLQTALNAVRSYRgqepldrfdfqdlmeeKIALLKMPEDLLTRSVNVgFSGGEKKRNDILQMAVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 451 DPEVLVADEAVSALDVSVQAQVLELIEQVRERTGvSVLFITHDLRVAAQV-CDTIAVMQHGKVVETG 516
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYQRILDYIkPDYVHVLYQGRIVKSG 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
317-507 |
2.49e-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: 47.09 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 317 TLRRGEILGIVGESGSGKSTVARCIVRLIEPSagrmlLGETD--------IARLSGAGLRP-LRR----KVQIVFQDPYR 383
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSGELKPN-----LGDYDeepswdevLKRFRGTELQDyFKKlangEIKVAHKPQYV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 384 SLNPRRAVGEsiIEGLLNfgmpRAQALVRAARTLGVVGLGPdVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSA 463
Cdd:COG1245 170 DLIPKVFKGT--VRELLE----KVDERGKLDELAEKLGLEN-ILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489912973 464 LDVSVQAQVLELIeqvRE--RTGVSVLFITHDLRVAAQVCDTIAVM 507
Cdd:COG1245 243 LDIYQRLNVARLI---RElaEEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
17-210 |
2.76e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 46.00 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-PEGILEVSGGSArvlgeDIVTASARRR 95
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLnTEGDIQIDGVSW-----NSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 96 RELRATRMAMVFQEPMTA-LNPvhrVGSQVDEvlrlhrrmpraqrrakvlEMFRSVHLPDVERIYDAYPHQ--------- 165
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKnLDP---YGKWSDE------------------EIWKVAEEVGLKSVIEQFPGQldfvlvdgg 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489912973 166 --LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRE 210
Cdd:cd03289 137 cvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQ 183
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-201 |
2.77e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.21 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 13 SAAVLAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL-PEGILEVSGGSArvlgeDIVTAS 91
Cdd:TIGR01271 1214 SGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLsTEGEIQIDGVSW-----NSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 92 ARRRRELRATRMAMVFQEPMTA-LNPVHRVGSQ-----VDEV-LRlhrrmpraqrraKVLEMFrsvhlPD-VERIYDAYP 163
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFIFSGTFRKnLDPYEQWSDEeiwkvAEEVgLK------------SVIEQF-----PDkLDFVLVDGG 1351
|
170 180 190
....*....|....*....|....*....|....*....
gi 489912973 164 HQLSGGQRQRIVIAMALILEPKLLIADEPTTALD-VTTQ 201
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDpVTLQ 1390
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
167-254 |
3.58e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAEIADRIVVMNRGDLTE 246
Cdd:PRK13546 145 SSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKT-IFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
....*...
gi 489912973 247 TGTRDEIL 254
Cdd:PRK13546 224 YGELDDVL 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
313-516 |
3.84e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 313 EVDLTLRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLlGETDIAR------LSGAGLRPlrrkvQIVFQDPYRSLN 386
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-AERSIAYvpqqawIMNATVRG-----NILFFDEEDAAR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 387 PRRAVGESIIEGLLnfgmprAQALVRAARTLGVVGLgpdvmrryphQFSGGQRQRLCIARALVMDPEVLVADEAVSALDV 466
Cdd:PTZ00243 752 LADAVRVSQLEADL------AQLGGGLETEIGEKGV----------NLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489912973 467 SVQAQVLE--LIEQVRERTGVsvlFITHDLRVAAQVcDTIAVMQHGKVVETG 516
Cdd:PTZ00243 816 HVGERVVEecFLGALAGKTRV---LATHQVHVVPRA-DYVVALGDGRVEFSG 863
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
302-526 |
3.91e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.49 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 302 FGATRTVVAASEVdltlRRGEILGIVGESGSGKSTVARCIVRLIEPSAGRMLLGetdiarlsgaglrplrrKVQIVFQDP 381
Cdd:cd03222 10 YGVFFLLVELGVV----KEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-----------------GITPVYKPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 382 YRSLnprravgesiiegllnfgmpraqalvraartlgvvglgpdvmrryphqfSGGQRQRLCIARALVMDPEVLVADEAV 461
Cdd:cd03222 69 YIDL-------------------------------------------------SGGELQRVAIAAALLRNATFYLFDEPS 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 462 SALDVSVQAQVLELIEQVRERTGVSVLFITHDLRVAAQVCDTIAVMQHGKVVETGAAQTVLTRPG 526
Cdd:cd03222 100 AYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREG 164
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
17-256 |
4.11e-05 |
|
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: 45.28 E-value: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 17 LAIRNLSVSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLLpegilEVSGGSARVLGEDIvtasARRRR 96
Cdd:cd03288 20 IKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMV-----DIFDGKIVIDGIDI----SKLPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 ELRATRMAMVFQEPMT-------ALNPVHRVGSQvdevlrlhrRMPRAQRRAKVLEMFRSvhLPD-VERIYDAYPHQLSG 168
Cdd:cd03288 91 HTLRSRLSIILQDPILfsgsirfNLDPECKCTDD---------RLWEALEIAQLKNMVKS--LPGgLDAVVTEGGENFSV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 169 GQRQRIVIAMALILEPKLLIADEPTTALDVTTQkQIL--ALIRELQDRhqtAVLFITHDFGVVAEiADRIVVMNRGDLTE 246
Cdd:cd03288 160 GQRQLFCLARAFVRKSSILIMDEATASIDMATE-NILqkVVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVE 234
|
250
....*....|
gi 489912973 247 TGTRDEILAR 256
Cdd:cd03288 235 CDTPENLLAQ 244
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
166-301 |
4.27e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.51 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVAEIaDRIVVMNRGDLT 245
Cdd:PLN03232 741 ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVL-VTNQLHFLPLM-DRIILVSEGMIK 818
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 489912973 246 ETGTRDEILArpSQNYTRRLVSSVPSLVPTQREAPGGEPVLRITGLGRTYAERRSL 301
Cdd:PLN03232 819 EEGTFAELSK--SGSLFKKLMENAGKMDATQEVNTNDENILKLGPTVTIDVSERNL 872
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
166-242 |
5.21e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 46.38 E-value: 5.21e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLFITHDFGVVAEIADRIVVMNRG 242
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRG 1096
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
24-239 |
5.71e-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: 44.56 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 24 VSVCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLAVMGLLPEG---ILEVSGGSAR----VLGEDIVTASARRRR 96
Cdd:cd03270 1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKS--SLAFDTIYAEGqrrYVESLSAYARqflgQMDKPDVDSIEGLSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 97 elratrmAMVFQEPMTALNPVHRVGSqVDEV---LR-LHRRMPRAQRrakvLEMFRSVHLP--DVERIYDAyphqLSGGQ 170
Cdd:cd03270 79 -------AIAIDQKTTSRNPRSTVGT-VTEIydyLRlLFARVGIRER----LGFLVDVGLGylTLSRSAPT----LSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489912973 171 RQRIVIAMAL--ILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVaEIADRIVVM 239
Cdd:cd03270 143 AQRIRLATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNT-VLVVEHDEDTI-RAADHVIDI 211
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
246-281 |
9.70e-05 |
|
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: 40.46 E-value: 9.70e-05
10 20 30
....*....|....*....|....*....|....*.
gi 489912973 246 ETGTRDEILARPSQNYTRRLVSSVPSLVPTQREAPG 281
Cdd:pfam08352 2 EEGPTDDILENPLHPYTRALLNSVPRLDPPKRPLYT 37
|
|
| oligo_HPY |
pfam08352 |
Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ... |
513-538 |
1.15e-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: 40.46 E-value: 1.15e-04
10 20
....*....|....*....|....*.
gi 489912973 513 VETGAAQTVLTRPGHAYTRALIDAAP 538
Cdd:pfam08352 1 VEEGPTDDILENPLHPYTRALLNSVP 26
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
166-205 |
1.66e-04 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 44.52 E-value: 1.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQIL 205
Cdd:TIGR01271 549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIF 588
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-256 |
1.82e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 4 APYPPAGDTSAAV-----LAIRNLSVSVcGAGNRVVRNLSLDVHAGETVCVVGESGSGKSvtSLAvmgLLPEGILEVSGG 78
Cdd:PRK10522 305 APYKAEFPRPQAFpdwqtLELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKS--TLA---MLLTGLYQPQSG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 79 SARVLGEDIvtasARRRRELRATRMAMVFqepmTALNPVHRV----GSQVDEVLrlhrrmprAQRRAKVLEMFRSVHLPD 154
Cdd:PRK10522 379 EILLDGKPV----TAEQPEDYRKLFSAVF----TDFHLFDQLlgpeGKPANPAL--------VEKWLERLKMAHKLELED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 155 vERIYDAyphQLSGGQRQRIVIAMALILEPKLLIADEptTALDVTTQ------KQILALIRELqdrhQTAVLFITHD--- 225
Cdd:PRK10522 443 -GRISNL---KLSKGQKKRLALLLALAEERDILLLDE--WAADQDPHfrrefyQVLLPLLQEM----GKTIFAISHDdhy 512
|
250 260 270
....*....|....*....|....*....|..
gi 489912973 226 FgvvaEIADRIVVMNRGDLTE-TGTRDEILAR 256
Cdd:PRK10522 513 F----IHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
318-492 |
2.05e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 44.35 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 318 LRRGEILGIVGESGSGKSTVARCIV--------RLIEPSAGRMLLgetdIARLSGAGLRPLRRkvQIVFQDPYRSLNpRR 389
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFY----VPQRPYMTLGTLRD--QIIYPDSSEDMK-RR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 390 AVGESIIEGLLNfgmpraqaLVRAARTLGVVGlGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVQ 469
Cdd:TIGR00954 548 GLSDKDLEQILD--------NVQLTHILEREG-GWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE 618
|
170 180
....*....|....*....|...
gi 489912973 470 AQVLELIEQVrertGVSVLFITH 492
Cdd:TIGR00954 619 GYMYRLCREF----GITLFSVSH 637
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-204 |
2.54e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 43.31 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 21 NLSVS-VCGAGNRVVRNLSLDVHAGETVCVVGESGSGKSVTSLAVMGLL--PEGILEVSGgsaRVlgedivtasarRRRE 97
Cdd:cd03291 39 NLFFSnLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELepSEGKIKHSG---RI-----------SFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 98 LRATRMAMVFQEPMTAlnpvhrvGSQVDEvlrlHRrmpraqrrakvlemFRSV-HLPDVERIYDAYPHQ----------- 165
Cdd:cd03291 105 QFSWIMPGTIKENIIF-------GVSYDE----YR--------------YKSVvKACQLEEDITKFPEKdntvlgeggit 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQI 204
Cdd:cd03291 160 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEI 198
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
166-237 |
2.94e-04 |
|
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: 42.60 E-value: 2.94e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 166 LSGGQRQRIVIAMALILE---PKLLIADEPTTALDVTTQKQILALIRELQDRHQTaVLFITHDFGVVAeIADRIV 237
Cdd:cd03271 170 LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNT-VVVIEHNLDVIK-CADWII 242
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
33-224 |
4.51e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 42.06 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 33 VVRNL-SLDVHAGETVcVVGESGSGKS--VTSLAV-MGLLPEgilevsGGSArvlGEDIVTasarrrrelratrmamvfq 108
Cdd:COG3910 26 AVRNLeGLEFHPPVTF-FVGENGSGKStlLEAIAVaAGFNPE------GGSK---NFRFST------------------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 109 epmtalnpvHRVGSQVDEVLRLHRRMPRAQR----RAkvlEMFRSV--HL----PDVERIYDAYP----HQLSGGQRqri 174
Cdd:COG3910 77 ---------RESESALGEYLRLSRGLPKPRDgfflRA---ESFFNVatYLdelaAEGPGILDSYGgrslHEQSHGES--- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489912973 175 viAMALILE----PKLLIADEPTTALDVTTQKQILALIRELQDRH-QtavlFI--TH 224
Cdd:COG3910 142 --FLALFENrfrgNGLYLLDEPEAALSPSRQLALLALIHDLVREGsQ----FIiaTH 192
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
166-255 |
6.14e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.57 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVttqKQILALIRELqDRHQTAVLFITHDFGVVAEIADRIVVMNRGDLT 245
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDM---ESIESLNMAL-EKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
90
....*....|.
gi 489912973 246 E-TGTRDEILA 255
Cdd:PRK15064 515 DfSGTYEEYLR 525
|
|
| oligo_HPY |
TIGR01727 |
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ... |
511-541 |
9.82e-04 |
|
oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 38.50 E-value: 9.82e-04
10 20 30
....*....|....*....|....*....|.
gi 489912973 511 KVVETGAAQTVLTRPGHAYTRALIDAAPGRG 541
Cdd:TIGR01727 1 KIVETGPAEEIFKNPLHPYTKALLSAIPTIK 31
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
166-237 |
1.01e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489912973 166 LSGGQRQRIVIAMALILE---PKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLfITHDFGVVaEIADRIV 237
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVV-IEHNLDVI-KTADYII 902
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
167-255 |
1.56e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 41.63 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 167 SGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDrhqtavlfITHDFGVVA---------EIADRIV 237
Cdd:TIGR00956 211 SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSAN--------ILDTTPLVAiyqcsqdayELFDKVI 282
|
90
....*....|....*...
gi 489912973 238 VMNRGDLTETGTRDEILA 255
Cdd:TIGR00956 283 VLYEGYQIYFGPADKAKQ 300
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
164-245 |
1.90e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.00 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 164 HQLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTqkqILALIRELQdRHQTAVLFITHDFGVVAEIADRIVVMNRGD 243
Cdd:PLN03073 626 YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLV-LFQGGVLMVSHDEHLISGSVDELWVVSEGK 701
|
..
gi 489912973 244 LT 245
Cdd:PLN03073 702 VT 703
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
165-225 |
2.60e-03 |
|
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: 39.51 E-value: 2.60e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489912973 165 QLSGGQRQ------RIVIAMALILEPKLLIADEPTTALDV-TTQKQILALIRELQDRHQTAVLFITHD 225
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHD 182
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
165-200 |
2.66e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.49 E-value: 2.66e-03
10 20 30
....*....|....*....|....*....|....*.
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVTT 200
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
165-225 |
3.25e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 3.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489912973 165 QLSGGQRQRIVIAMALILEPKLLIADEPTTALDVtTQKQIL---------ALIRELQDRH----QTAVLFITHD 225
Cdd:PRK10636 430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL-DMRQALtealidfegALVVVSHDRHllrsTTDDLYLVHD 502
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
412-493 |
5.30e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 412 RAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMDPEVLVADEAVSALDVSVqaqVLELIEQVRERTGVSVLfIT 491
Cdd:PRK10636 128 RAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLIL-IS 203
|
..
gi 489912973 492 HD 493
Cdd:PRK10636 204 HD 205
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
314-502 |
6.17e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 38.39 E-value: 6.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 314 VDLTLRRGEILGIVGESGSGKSTVARCIV------RLIE--PSAGRMLLGETDIARL-SGAGLRPlrrkvQIVFQDPYRS 384
Cdd:cd03270 14 VDVDIPRNKLVVITGVSGSGKSSLAFDTIyaegqrRYVEslSAYARQFLGQMDKPDVdSIEGLSP-----AIAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 385 LNPRRAVGeSIIEGLLNFGMPRAQA-LVRAARTLGVVGLGPDVMRRYPHQFSGGQRQRLCIARALVMD-PEVL-VADEAV 461
Cdd:cd03270 89 RNPRSTVG-TVTEIYDYLRLLFARVgIRERLGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGlTGVLyVLDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489912973 462 SALDVSVQAQVLELIEQVRERtGVSVLFITHD---LRVAAQVCD 502
Cdd:cd03270 168 IGLHPRDNDRLIETLKRLRDL-GNTVLVVEHDedtIRAADHVID 210
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
166-255 |
7.31e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489912973 166 LSGGQRQRIVIAMALILEPKLLIADEPTTALDVTTQKQILALIRELQDRHQTAVLF-ITHDFGVVAEIADRIVVMNRGDL 244
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMsLLQPAPETFDLFDDIILLSEGQI 416
|
90
....*....|.
gi 489912973 245 TETGTRDEILA 255
Cdd:PLN03140 417 VYQGPRDHILE 427
|
|
| |
