|
Name |
Accession |
Description |
Interval |
E-value |
| bisC_fam |
TIGR00509 |
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares ... |
7-766 |
0e+00 |
|
molybdopterin guanine dinucleotide-containing S/N-oxide reductases; This enzyme family shares sequence similarity and a requirement for a molydenum cofactor as the only prosthetic group. The form of the cofactor is a single molybdenum atom coordinated by two molybdopterin guanine dinucleotide molecules. Members of the family include biotin sulfoxide reductase, dimethylsulfoxide reductase, and trimethylamine-N-oxide reductase, although a single member may show all those activities and related activities; it may not be possible to resolve the primary function for members of this family by sequence comparison alone. A number of similar molybdoproteins in which the N-terminal region contains a CXXXC motif and may bind an iron-sulfur cluster are excluded from this set, including formate dehydrogenases and nitrate reductases. Also excluded is the A chain of a heteromeric, anaerobic DMSO reductase, which also contains the CXXXC motif.
Pssm-ID: 273110 [Multi-domain] Cd Length: 770 Bit Score: 1165.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 7 ATHWGVFTARVHGGDIAAVAALASDTNPAPQLQNLPGAVRHRSRIANPAVRRGWLQHG-PGPSSARGAEEFVEVSWDELI 85
Cdd:TIGR00509 1 ASHWGVFTATVQDGRIVAVTPFESDPNPTPMLEGVPDQVYSESRIKYPMVRKGFLENGvKSDRSGRGREEFVRVSWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 86 ELLASELRRTVDRYGNEAIYGSSYGWASAGRFHHAQSQVHRFLNMLGGYTASRHSYSAGASEVIFPHIVGAalFEALAET 165
Cdd:TIGR00509 81 DLVAEELKRVRKTHGPSAIFAGSYGWKSAGRLHNASTLLQRMLNLLGGYVGHAGDYSTGAAQVIMPHVVGD--MEVYEQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 166 TTWDVIVDHTALLVAFGGLPVKNTAvMPGGTTAHPDRDYVGRYRARGGRLVSVSPLRDDIAAIAGplddrCRWLAPVPGT 245
Cdd:TIGR00509 159 TTWPVILENSEVLVLWGADPLKTSQ-IAWGIPDHGGYEYLERLKAKGKRVISIDPVRTETVEFFG-----AEWIPPNPQT 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 246 DVAIMLGLAYVLATESLADRAFLGRYCTGYERFERYLLGLDDGIPKTPEWAAALSGLAAGDLRDLARRMAEHRTLITTSL 325
Cdd:TIGR00509 233 DVALMLGLAHTLVTEGLYDKDFLAKYTSGFEKFLPYLLGETDGTPKTAEWASKITGVPAETIKELARLFASKRTMLAAGW 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 326 SLQRIEHGEQTVWMAATLAAMLGQIGLPGGGFGHGYSSNGvGNPPLACGlPALPQGNNPVS------------TFIPVAA 393
Cdd:TIGR00509 313 SMQRMQHGEQPHWMLVTLAAMLGQIGLPGGGFGFSYHYSG-GGTPSASG-PALSQGSNSVSstagpewddgsaSVIPVAR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 394 ISELLQRPGQRLAYNGRLLELPDIKCVYWAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTTTSFER 473
Cdd:TIGR00509 391 ISDALLNPGKEIDYNGKELKLPDIKMVYWAGGNPFHHHQDTNRLIKAWRKLETIIVHEPQWTPTAKHADIVLPATTSFER 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 474 DDF--AASKTNPTLIAMPAMVPPYANARDDYHTFSALAHRLGFGKQFTEGRSAREWLEHMYDKWSAELD---FPVPSFAE 548
Cdd:TIGR00509 471 NDLtmAGDYSNTGILAMKQVVPPQFEARNDYDIFAALAERLGVEEAFTEGKDEMGWLKHLYEKAAKQAKadgVEMPAFDA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 549 FWRTGRLELPTRTG--LTWLADFRADPAAHPLGTPSGRIEIFSDTVDAFALPDCAGHPTWYEPSEWLGGPRAARYPLHLI 626
Cdd:TIGR00509 551 FWAEGIVEFPVPEGadFVRYAAFREDPLLNPLGTPSGLIEIYSKTIAKMGYDDCPGHPTWMEPAEWLGGPRGAKYPLHLI 630
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 627 ANQPRTRLHSQLDHGGASMASKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQLSTGAWFD 706
Cdd:TIGR00509 631 SPHPKYRLHSQLDHTELRQAYKVQGREPVMIHPDDAAARGIADGDIVRVFNARGQILAGAVVTDGIRKGVVQIHEGAWYD 710
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 707 PADPRDPDSMCVHGNPNALSNDSGTSSLAHGSTGQHVLVQIERFTGELPPVRAHEPPRLA 766
Cdd:TIGR00509 711 PADVREPGGLCKYGNPNVLTADIGTSSLAQGNSGNTVLVEIEKYTGPAPPLTAFDQPAAA 770
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
5-613 |
0e+00 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239170 [Multi-domain] Cd Length: 609 Bit Score: 930.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 5 TSATHWGVFTARVHGGDIAAVAALASDTNPAPQLQNLPGAVRHRSRIANPAVRRGWLQHGPG-PSSARGAEEFVEVSWDE 83
Cdd:cd02769 1 PTASHWGAFRARVKDGRIVGVRPFEEDPDPSPLLDGVPDAVYSPTRIKYPMVRRGWLEKGPGsDRSLRGKEEFVRVSWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 84 LIELLASELRRTVDRYGNEAIYGSSYGWASAGRFHHAQSQVHRFLNMLGGYTASRHSYSAGASEVIFPHIVGAALFEaLA 163
Cdd:cd02769 81 ALDLVAAELKRVRKTYGNEAIFGGSYGWSSAGRFHHAQSLLHRFLNLAGGYVGSVGDYSTGAAQVILPHVVGSMEVY-TE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 164 ETTTWDVIVDHTALLVAFGGLPVKNTAVMPGGTTAHPDRDYVGRYRARGGRLVSVSPLRDDIAAIAGplddrCRWLAPVP 243
Cdd:cd02769 160 QQTSWPVIAEHTELVVAFGADPLKNAQIAWGGIPDHQAYSYLKALKDRGIRFISISPLRDDTAAELG-----AEWIAIRP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 244 GTDVAIMLGLAYVLATESLADRAFLGRYCTGYERFERYLLGLDDGIPKTPEWAAALSGLAAGDLRDLARRMAEHRTLITT 323
Cdd:cd02769 235 GTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLGESDGVPKTPEWAAAICGIPAETIRELARRFASKRTMIMA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 324 SLSLQRIEHGEQTVWMAATLAAMLGQIGLPGGGFGHGYSSNGVGNPPLACG-LPALPQGNNPVSTFIPVAAISELLQRPG 402
Cdd:cd02769 315 GWSLQRAHHGEQPHWMAVTLAAMLGQIGLPGGGFGFGYHYSNGGGPPRGAApPPALPQGRNPVSSFIPVARIADMLLNPG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 403 QRLAYNGRLLELPDIKCVYWAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDDFAASKTN 482
Cdd:cd02769 395 KPFDYNGKKLTYPDIKLVYWAGGNPFHHHQDLNRLIRAWQKPETVIVHEPFWTATARHADIVLPATTSLERNDIGGSGDN 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 483 PTLIAMPAMVPPYANARDDYHTFSALAHRLGFGKQFTEGRSAREWLEHMYDKWS---AELDFPVPSFAEFWRTGRLELPT 559
Cdd:cd02769 475 RYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQFTEGRDEMEWLRHLYEESRaqaAARGVEMPSFDEFWAQGYVELPI 554
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 624384294 560 RT-GLTWLADFRADPAAHPLGTPSGRIEIFSDTVDAFALPDCAGHPTWYEPSEWL 613
Cdd:cd02769 555 PEaDFVRLADFREDPEANPLGTPSGRIEIFSETIAGFGYDDCPGHPTWLEPAEWL 609
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
5-613 |
0e+00 |
|
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 811.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 5 TSATHWGVFTARVHGGDIAAVAALASD-TNPAPQLQNLPGAVRHRSRIANPAVRRGWLQHGPGPSSARGAEEFVEVSWDE 83
Cdd:cd02751 1 PTACHWGPFKAHVKDGVIVRVEPDDTDqPRPCPRGRSVRDRVYSPDRIKYPMKRVGWLGNGPGSRELRGEGEFVRISWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 84 LIELLASELRRTVDRYGNEAIYGSSYGWASAGRFHHAQSQVHRFLNMLGGYTASRHSYSAGASEVIFPHIVGAAlfEALA 163
Cdd:cd02751 81 ALDLVASELKRIREKYGNEAIFGGSYGWASAGRLHHAQSLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSD--EVYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 164 ETTTWDVIVDHTALLVAFGGLPVKNTAVMPGGTtAHPDRDYVGRYRARGGRLVSVSPLRDDIAAIAGplddrCRWLAPVP 243
Cdd:cd02751 159 QGTSWDDIAEHSDLVVLFGANPLKTRQGGGGGP-DHGSYYYLKQAKDAGVRFICIDPRYTDTAAVLA-----AEWIPIRP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 244 GTDVAIMLGLAYVLATESLADRAFLGRYCTGYERFERYLLGLDDGIPKTPEWAAALSGLAAGDLRDLARRMAEHRTLITT 323
Cdd:cd02751 233 GTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYLLGESDGVPKTPEWAAEITGVPAETIRALAREIASKRTMIAQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 324 SLSLQRIEHGEQTVWMAATLAAMLGQIGLPGGGFGHGY-SSNGVGNPPLACGLPALPQGNNPVSTFIPVAAISELLQRPG 402
Cdd:cd02751 313 GWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYgYSNGGGPPRGGAGGPGLPQGKNPVKDSIPVARIADALLNPG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 403 QRLAYNGRLLELPDIKCVYWAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDDFAASKT- 481
Cdd:cd02751 393 KEFTANGKLKTYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTGNy 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 482 -NPTLIAMPAMVPPYANARDDYHTFSALAHRLGFGKQFTEGRSAREWLEHMYDKWSA---ELDFPVPSFAEFWRTGRLEL 557
Cdd:cd02751 473 sNRYLIAMKQAVEPLGEARSDYEIFAELAKRLGVEEEFTEGRDEMEWLEHLYEETRAkaaGPGPELPSFEEFWEKGIVRV 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 624384294 558 PTR-TGLTWLADFRADPAAHPLGTPSGRIEIFSDTVDAFALPDCAGHPTWYEPSEWL 613
Cdd:cd02751 553 PAApKPFVAFADFREDPEANPLGTPSGKIEIYSETLADFGYDDCPGHPTWIEPWEGL 609
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
5-763 |
0e+00 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 627.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 5 TSATHWGVFTARVHGGDIAAVAALASDTNPAPQLQNLPGAVRHRSRIANPAVRRGWLQHGPGPS-SARGAEEFVEVSWDE 83
Cdd:PRK15102 45 LTGSHWGAFRAKVKNGRFVEAKPFELDKYPTKMINGIKGHVYNPSRIRYPMVRLDWLRKRHKSDtSQRGDNRFVRVSWDE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 84 LIELLASELRRTVDRYGNEAIYGSSYGWASAGRFHHAQSQVHRFLNMLGGYTASRHSYSAGASEVIFPHIVGAAlfEALA 163
Cdd:PRK15102 125 ALDLFYEELERVQKTYGPSALHTGQTGWQSTGQFHSATGHMQRAIGMHGNSVGTVGDYSTGAGQVILPYVLGST--EVYE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 164 ETTTWDVIVDHTALLVAFGGLPVKNTAVmpgGTTA--HPDRDYVGRYRARGG----RLVSVSPLRDDIAAIAGplddrCR 237
Cdd:PRK15102 203 QGTSWPLILENSKTIVLWGSDPVKNLQV---GWNCetHESYAYLAQLKEKVAkgeiNVISIDPVVTKTQNYLG-----CE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 238 WLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTGYERFERYLLGLDDGIPKTPEWAAALSGLAAGDLRDLARRMAEH 317
Cdd:PRK15102 275 HLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLPYLLGEKDGVPKTPEWAEKICGIDAETIRELARQMAKG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 318 RTLITTSLSLQRIEHGEQTVWMAATLAAMLGQIGLPGGGFGHGYSSNGVGNPP-LACGLPALP----QGNNPV------- 385
Cdd:PRK15102 355 RTQIIAGWCIQRQQHGEQPYWMGAVLAAMLGQIGLPGGGISYGHHYSGIGVPSsGGAIPGGFPgnldTGQKPKhdnsdyk 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 386 --STFIPVAAISELLQRPGQRLAYNGRLLELPDIKCVYWAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYWTAMAKHADI 463
Cdd:PRK15102 435 gySSTIPVARFIDAILEPGKTINWNGKKVTLPPLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADI 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 464 VVPTTTSFERDDFAA--SKTNPTLIAMPAMVPPYANARDDYHTFSALAHRLGFGKQFTEGRSAREWLEHMYD--KWSAEL 539
Cdd:PRK15102 515 VLPACTQFERNDIDQygSYSNRGIIAMKKVVEPLFESRSDFDIFRELCRRFGREKEYTRGMDEMGWLKRLYQecKQQNKG 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 540 DFPVPSFAEFWRTGRLELPtrTGLTWL--ADFRADPAAHPLGTPSGRIEIFSDTVDAFALPDCAGHPTWYEPSEWL-GGP 616
Cdd:PRK15102 595 KFHMPEFDEFWKKGYVEFG--EGQPWVrhADFREDPELNPLGTPSGLIEIYSRKIADMGYDDCQGHPMWFEKIERShGGP 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 617 RAARYPLHLIANQPRTRLHSQLDHGGASMAS-KIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPK 695
Cdd:PRK15102 673 GSDKYPLWLQSVHPDKRLHSQLCESEELRETyTVQGREPVYINPQDAKARGIKDGDVVRVFNDRGQVLAGAVVSDRYPPG 752
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 624384294 696 VVQLSTGAWFDPADPRDPDSMCVHGNPNALSNDSGTSSLAHGSTGQHVLVQIERFTGELPPVRAHEPP 763
Cdd:PRK15102 753 VIRIHEGAWYGPDKGGEIGALCTYGDPNTLTLDIGTSQLAQATSAHTCLVEIEKYQGKVPPVTSFNGP 820
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
3-749 |
2.03e-174 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 516.32 E-value: 2.03e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 3 VYTSATHWGVF---TARVHGGDIAAVAAlaSDTNPAPQL------QNLPGAVRHRSRIANPAVRRGwlqhgpgpssARGA 73
Cdd:COG0243 24 VKTTCPGCGVGcglGVKVEDGRVVRVRG--DPDHPVNRGrlcakgAALDERLYSPDRLTYPMKRVG----------PRGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 74 EEFVEVSWDELIELLASELRRTVDRYGNEAIYGSSYGwASAGRFHHAQSQV-HRFLNMLGG---YTASRHSYSAGAseVI 149
Cdd:COG0243 92 GKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSG-GSAGRLSNEAAYLaQRFARALGTnnlDDNSRLCHESAV--AG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 150 FPHIVGAALFealaeTTTWDVIvDHTALLVAFGGLPVKNTAVMPGGTTAhpdrdyvgRYRARGGRLVSVSPLRDDIAAIA 229
Cdd:COG0243 169 LPRTFGSDKG-----TVSYEDL-EHADLIVLWGSNPAENHPRLLRRLRE--------AAKKRGAKIVVIDPRRTETAAIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 230 GplddrcRWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTGYERFERYLlglddgIPKTPEWAAALSGLAAGDLRD 309
Cdd:COG0243 235 D------EWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVGFDELAAYV------AAYTPEWAAEITGVPAEDIRE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 310 LARRMAEH-RTLITTSLSLQRIEHGEQTVWMAATLAAMLGQIglpgggfghgyssngvgnpplacGLPalpqGNNPVStf 388
Cdd:COG0243 303 LAREFATAkPAVILWGMGLQQHSNGTQTVRAIANLALLTGNI-----------------------GKP----GGGPFS-- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 389 IPVAAIsellqRPGQRlayngrllelPDIKCVYWAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTT 468
Cdd:COG0243 354 LTGEAI-----LDGKP----------YPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPAT 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 469 TSFERDDFAASKTNPTLIAMPAMVPPYANARDDYHTFSALAHRLGFGKQFTEGRSAREWLEHMYDKWsaelDFPVPSFAE 548
Cdd:COG0243 419 TWLERDDIVTNSEDRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWGRTEEDYLRELLEAT----RGRGITFEE 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 549 FWRTGRLELPTRTGLTWLADfradpaaHPLGTPSGRIEIFSDTVdafalpDCAGHPTWYEPSEWlGGPRAARYPLHLIAN 628
Cdd:COG0243 495 LREKGPVQLPVPPEPAFRND-------GPFPTPSGKAEFYSETL------ALPPLPRYAPPYEG-AEPLDAEYPLRLITG 560
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 629 QPRTRLHSQLDhgGASMASKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQLSTGAWFDPA 708
Cdd:COG0243 561 RSRDQWHSTTY--NNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWYEPA 638
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 624384294 709 DprdpdsmCVHGNPNALSNDSgTSSLAHGSTGQHVLVQIER 749
Cdd:COG0243 639 D-------DKGGNVNVLTPDA-TDPLSGTPAFKSVPVRVEK 671
|
|
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
45-749 |
1.51e-106 |
|
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.
Pssm-ID: 274006 [Multi-domain] Cd Length: 797 Bit Score: 344.06 E-value: 1.51e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 45 VRHRSRIANPAVRRGwlqhgpgpssARGAEEFVEVSWDELIELLASELRRTVDRYGNEAIY-----GSSYGWASAGRFHH 119
Cdd:TIGR02166 99 VYNPDRLKYPMKRVG----------KRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYvnygtGTTGGTMSRSWPPT 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 120 AqsqVHRFLNMLGGYTASRHSYSAGASEVIFPHIVGAALFEALAETttwdviVDHTALLVAFGGLPVKntAVMPGGTTAH 199
Cdd:TIGR02166 169 A---VARLLNLCGGYLNQYGSYSTAQINEAMPYTYGISADGSSLDD------IENSKLVVMFGNNPAE--TRMSGGGQTY 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 200 pdrDYVGRYRARGGRLVSVSPLRDDiaAIAGPLDDrcrWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTGYER-- 277
Cdd:TIGR02166 238 ---YFLQALEKSNARVIVIDPRYTD--TVAGREDE---WIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYCVGFDEkt 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 278 ----------FERYLLGL-DDGIPKTPEWAAALSGLAAGDLRDLARRMAEHR-TLITTSLSLQRIEHGEQTVWMAATLAA 345
Cdd:TIGR02166 310 lpasapkngsYKDYILGEgADGTPKTPEWASKITGIPADTIIKLAREIGNAKpAFISQGWGPQRHANGEQAARAIMMLAL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 346 MLGQIGLpgggfghgyssNGVGNPPL-ACGL---PALPQGNNPVSTFIPVAAISELLQRPGQRLAYNGRL-----LELPd 416
Cdd:TIGR02166 390 LTGNVGI-----------KGGNNGAReGNYSlpfARMPELPNPVKTSISCFLWTDAIDRGTEMTAIKDGVrgkdkLDSN- 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 417 IKCVYWAGGNPF-HHHQNLPRLRRAL---SRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDDF---AASKTNPTLIAMP 489
Cdd:TIGR02166 458 IKFLWNYAGNCLiNQHSDINRTHKILqdeSKCEMIVVIDNHMTSSAKYADILLPDTTTLEQNDFiedSYASNMSYLIFMQ 537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 490 AMVPPYANARDDYHTFSALAHRLGFGKQFTEGRSAREWLEHMYDKwSAELDFPVPSFAEFWRTGRLELPTRTG-LTWLAD 568
Cdd:TIGR02166 538 KAIEPLFECKPIYDMLSEVAKRLGVEAEFTEGRTQEEWLEHLYAQ-TRAADPALPSFAELRKQGIYKAKSAPGpFVAFED 616
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 569 FRADPAAHPLGTPSGRIEIFSDTVDAFA-------------LPDCAghPTWYEPSEwlggPRAARYPLHLIANQPRTRLH 635
Cdd:TIGR02166 617 FRRDPEANPLKTPSGKIEIYSERLAQIAhtwelpegdvitpLPEYV--PTFEGPDD----PLRKDFPLQLTGFHYKGRTH 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 636 SQLdhgGASMASKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQLSTGAWFDP-ADPRDpd 714
Cdd:TIGR02166 691 STY---GNVDWLREAAPQELWINPIDAQKRGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGAWYQPdKNGID-- 765
|
730 740 750
....*....|....*....|....*....|....*
gi 624384294 715 smcVHGNPNALSNDSgTSSLAHGSTGQHVLVQIER 749
Cdd:TIGR02166 766 ---VGGCINTLTTQR-PSPLAKGNPQHTNLVEVEK 796
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
30-591 |
4.40e-100 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 321.96 E-value: 4.40e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 30 SDTNPAPQLQNLPGAVRHRS---------RIANPAVRRGWlqhgpgpssaRGAEEFVEVSWDELIELLASELRRTVDRYG 100
Cdd:cd02770 30 DTGDDDPGFHQIRACLRGRSqrkrvynpdRLKYPMKRVGK----------RGEGKFVRISWDEALDTIASELKRIIEKYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 101 NEAIYgSSYGWASAGRFHHAQSQVHRFLNMLGGYTASRHSYSAGASEVIFPHIVGAAlfealAETTTWDVIVDhTALLVA 180
Cdd:cd02770 100 NEAIY-VNYGTGTYGGVPAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYTYGAA-----ASGSSLDDLKD-SKLVVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 181 FGGLPVKNTavMPGGTTAHpdrdYVGRYRARGGRLVSVSPLRDDIAAIagpLDDrcRWLAPVPGTDVAIMLGLAYVLATE 260
Cdd:cd02770 173 FGHNPAETR--MGGGGSTY----YYLQAKKAGAKFIVIDPRYTDTAVT---LAD--EWIPIRPGTDAALVAAMAYVMITE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 261 SLADRAFLGRYCTGYER------------FERYLLGL-DDGIPKTPEWAAALSGLAAGDLRDLARRMAEHRT-LITTSLS 326
Cdd:cd02770 242 NLHDQAFLDRYCVGFDAehlpegappnesYKDYVLGTgYDGTPKTPEWASEITGVPAETIRRLAREIATTKPaAILQGWG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 327 LQRIEHGEQTVWMAATLAAMLGQIGLPGggfghgySSNGV--GNPPLACglPALPQGNNPVSTFIPVAAISELLQRPGQR 404
Cdd:cd02770 322 PQRHANGEQAARAIMMLAAMTGNVGIPG-------GNTGArpGGSAYNG--AGLPAGKNPVKTSIPCFMWTDAIERGEEM 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 405 LAYNGRLL---EL-PDIKCVY-WAGGNPFHHH----QNLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDD 475
Cdd:cd02770 393 TADDGGVKgadKLkSNIKMIWnYAGNTLINQHsddnNTTRALLDDESKCEFIVVIDNFMTPSARYADILLPDTTELERED 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 476 FAASKTNPT---LIAMPAMVPPYANARDDYHTFSALAHRLGFGKQFTEGRSAREWLEHMYDKwSAELDFPVPSFAEFWRT 552
Cdd:cd02770 473 IVLTSNAGMmeyLIYSQKAIEPLYECKSDYEICAELAKRLGVEDQFTEGKTEQEWLEELYGQ-TRAKEPGLPTYEEFREK 551
|
570 580 590
....*....|....*....|....*....|....*....
gi 624384294 553 GRLELPTRTGLTWLADFRADPAAHPLGTPSGRIEIFSDT 591
Cdd:cd02770 552 GIYRVPRALPFVAFEDFREDPENNPLKTPSGKIEIYSKA 590
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
48-749 |
3.76e-81 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 276.52 E-value: 3.76e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 48 RSRIANPavrrGWLQHGPGPSSARGAEEFVEVSWDELIELLASELRRTVDRYGNEAIYgSSYGWASAG-----RFHHAQS 122
Cdd:PRK14990 111 RRRVYNP----DRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIY-LNYGTGTLGgtmtrSWPPGNT 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 123 QVHRFLNMLGGYTASRHSYSAGAsevifphiVGAAL---FEALAETTTWDVIvDHTALLVAFGGLPvKNTAVMPGGTTAh 199
Cdd:PRK14990 186 LVARLMNCCGGYLNHYGDYSSAQ--------IAEGLnytYGGWADGNSPSDI-ENSKLVVLFGNNP-GETRMSGGGVTY- 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 200 pdrdYVGRYRARG-GRLVSVSPLRDDIAAiaGPLDDrcrWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTGYER- 277
Cdd:PRK14990 255 ----YLEQARQKSnARMIIIDPRYTDTGA--GREDE---WIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEk 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 278 -----------FERYLLGL-DDGIPKTPEWAAALSGLAAGDLRDLARRMAEHR-TLITTSLSLQRIEHGEQTVWMAATLA 344
Cdd:PRK14990 326 tlpasapknghYKAYILGEgPDGVAKTPEWASQITGVPADKIIKLAREIGSTKpAFISQGWGPQRHANGEIATRAISMLA 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 345 AMLGQIGLPGggfghgySSNGVGNPPLACGLPALPQGNNPVSTFIPVAAISELLQRPGQRLAYNGRL-----LELPdIKC 419
Cdd:PRK14990 406 ILTGNVGING-------GNSGAREGSYSLPFVRMPTLENPIQTSISMFMWTDAIERGPEMTALRDGVrgkdkLDVP-IKM 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 420 VY-WAGGNPFHHHQNLPRLRRALS---RVDTIVVHEQYWTAMAKHADIVVPTTTSFERDDFA--ASKTNPT-LIAMPAMV 492
Cdd:PRK14990 478 IWnYAGNCLINQHSEINRTHEILQddkKCELIVVIDCHMTSSAKYADILLPDCTASEQMDFAldASCGNMSyVIFNDQVI 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 493 PPYANARDDYHTFSALAHRLGFGKQFTEGRSAREWLEHMYDKwSAELDFPVPSFAEFWRTG--RLELPTRTGLTWLAdFR 570
Cdd:PRK14990 558 KPRFECKTIYEMTSELAKRLGVEQQFTEGRTQEEWMRHLYAQ-SREAIPELPTFEEFRKQGifKKRDPQGHHVAYKA-FR 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 571 ADPAAHPLGTPSGRIEIFSDTVDAFA----LP--DCAGHPTWYEPS-EWLGGPRAARYPLHLIANQPRTRLHSQldHGGA 643
Cdd:PRK14990 636 EDPQANPLTTPSGKIEIYSQALADIAatweLPegDVIDPLPIYTPGfESYQDPLNKQYPLQLTGFHYKSRVHST--YGNV 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 644 SMAsKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQLSTGAWFDPADPRDPDSMCVhgnpN 723
Cdd:PRK14990 714 DVL-KAACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWYDPDAKRVDKGGCI----N 788
|
730 740
....*....|....*....|....*.
gi 624384294 724 ALSNDSgTSSLAHGSTGQHVLVQIER 749
Cdd:PRK14990 789 VLTTQR-PSPLAKGNPSHTNLVQVEK 813
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
621-749 |
8.29e-76 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 240.61 E-value: 8.29e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 621 YPLHLIANQPRTRLHSQLDHGGASMASKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQLS 700
Cdd:cd02793 1 YPLHLLSNQPATRLHSQLDHGSLSRAYKVQGREPIRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGVVQLP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 624384294 701 TGAWFDPADPRDPDSMCVHGNPNALSNDSGTSSLAHGSTGQHVLVQIER 749
Cdd:cd02793 81 TGAWYDPDDPGEPGPLCKHGNPNVLTLDIGTSSLAQGCSAQTCLVQIEK 129
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
621-749 |
1.40e-59 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 197.42 E-value: 1.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 621 YPLHLIANQPRTRLHSQLDH-GGASMASKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQL 699
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNvPWLREAYKVKGREPVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 624384294 700 STGAWFdpaDPRDPDSMCVHGNPNALSNDSGTSSLAHGSTGQHVLVQIER 749
Cdd:cd02777 81 PEGAWY---DPDDNGGLDKGGNPNVLTSDIPTSKLAQGNPANTCLVEIEK 127
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
45-512 |
7.29e-56 |
|
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.
Pssm-ID: 238218 [Multi-domain] Cd Length: 374 Bit Score: 196.01 E-value: 7.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 45 VRHRSRIANPAVRRGWLqhgpgpssargaEEFVEVSWDELIELLASELRRTVDRYGNEAIYGSSYGWASAGRFHHAQSqv 124
Cdd:cd00368 49 LYSPDRLKYPLIRVGGR------------GKFVPISWDEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQK-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 125 hRFLNMLGGYTASRHSYSAGASEVIFPHIVGAALfealaeTTTWDVIvDHTALLVAFGGLPVKntavmpggtTAHPDRDY 204
Cdd:cd00368 115 -LLRALGSNNVDSHARLCHASAVAALKAFGGGAP------TNTLADI-ENADLILLWGSNPAE---------THPVLAAR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 205 VGRYRARGGRLVSVSPLRDDIAAIAgplddrCRWLAPVPGTDVAIMLGlayvlatESLADRAflgryctgyerferyllg 284
Cdd:cd00368 178 LRRAKKRGAKLIVIDPRRTETAAKA------DEWLPIRPGTDAALALA-------EWAAEIT------------------ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 285 lddGIPKtpewaaalsglaaGDLRDLARRMAEH-RTLITTSLSLQRIEHGEQTVWMAATLAAMLGQIGlpgggfghgyss 363
Cdd:cd00368 227 ---GVPA-------------ETIRALAREFAAAkRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIG------------ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 364 ngvgnpplacglpalpqgnnpvstfipvaaisellqRPGqrlayngrllelpdikCVYWAGGNPFHHHQNLPRLRRALSR 443
Cdd:cd00368 279 ------------------------------------RPG----------------GGLGPGGNPLVSAPDANRVRAALKK 306
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 624384294 444 VDTIVVHEQYWTAMAKHADIVVPTTTSFERDDFAASkTNPTLIAMPAMVPPYANARDDYHTFSALAHRL 512
Cdd:cd00368 307 LDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTN-TEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
40-717 |
3.30e-54 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 198.95 E-value: 3.30e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 40 NLPGAVRHRSRIANPAVRRGwlqhgpgpssargaEEFVEVSWDELIELLASELRRTVDRYGNEAI--YGSS-------Yg 110
Cdd:COG3383 51 FGFEFVNSPDRLTTPLIRRG--------------GEFREVSWDEALDLVAERLREIQAEHGPDAVafYGSGqltneenY- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 111 waSAGRFHHAqsqvhrFLNMLGGYTASR--HSYSAgasevifphivgAALFEAL---AETTTWDVIvDHTALLVAFGGlp 185
Cdd:COG3383 116 --LLQKLARG------VLGTNNIDNNARlcMASAV------------AGLKQSFgsdAPPNSYDDI-EEADVILVIGS-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 186 vkNTAVmpggttAHPDrdyVGRY----RARGGRLVSVSPLRDDIAAIAGplddrcRWLAPVPGTDVAIMLGLAYVLATES 261
Cdd:COG3383 173 --NPAE------AHPV---LARRikkaKKNGAKLIVVDPRRTETARLAD------LHLQIKPGTDLALLNGLLHVIIEEG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 262 LADRAFLGRYCTGYERFERYLLGLddgipkTPEWAAALSGLAAGDLRDLARRMAEH-RTLITTSLSLQRIEHGEQTVWMA 340
Cdd:COG3383 236 LVDEDFIAERTEGFEELKASVAKY------TPERVAEITGVPAEDIREAARLIAEAkRAMILWGMGVNQHTQGTDNVNAI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 341 ATLAAMLGQIGLPgggfghgyssnGVGNPPL--------AC---GLPALPQGNNPVST------FIPVAAISELLQRPGQ 403
Cdd:COG3383 310 INLALATGNIGRP-----------GTGPFPLtgqnnvqgGRdmgALPNVLPGYRDVTDpehrakVADAWGVPPLPDKPGL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 404 RLAYNGRLLELPDIKCVYWAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDdfaASKTNP 483
Cdd:COG3383 379 TAVEMFDAIADGEIKALWIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKD---GTFTNT 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 484 --TLIAMPAMVPPYANARDDYHTFSALAHRLGFGKQFTegrSARE-WLEHmydkwsAELdfpVPSFAEFwRTGRLElpTR 560
Cdd:COG3383 456 erRVQRVRKAVEPPGEARPDWEIIAELARRLGYGFDYD---SPEEvFDEI------ARL---TPDYSGI-SYERLE--AL 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 561 TGLTWLAdfradPAAHPLGTPSgrieIFSDtvdAFALPDCAGH---PTWYEPSEwlggPRAARYPLHLIANQPRTRLHSQ 637
Cdd:COG3383 521 GGVQWPC-----PSEDHPGTPR----LFTG---RFPTPDGKARfvpVEYRPPAE----LPDEEYPLVLTTGRLLDQWHTG 584
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 638 LDHGGASMASKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQLsTGAWFDPA------DPR 711
Cdd:COG3383 585 TRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVTDRVRPGTVFM-PFHWGEGAanaltnDAL 663
|
....*.
gi 624384294 712 DPDSMC 717
Cdd:COG3383 664 DPVSKQ 669
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
45-598 |
4.95e-54 |
|
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 194.39 E-value: 4.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 45 VRHRSRIANPAVRRGwlqhgpgpssaRGAEEFVEVSWDELIELLASELRRTVDRYGNEAIYGSSYgwasAGRFHHAQSQV 124
Cdd:cd02766 50 VYSPDRLLTPLKRVG-----------RKGGQWERISWDEALDTIAAKLKEIKAEYGPESILPYSY----AGTMGLLQRAA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 125 HRFLNMLGGYTASRHSYSAGASEVIFPHIVGAALFEALAEtttwdviVDHTALLVAFGglpvKNTAVmpggTTAHPDRdY 204
Cdd:cd02766 115 RGRFFHALGASELRGTICSGAGIEAQKYDFGASLGNDPED-------MVNADLIVIWG----INPAA----TNIHLMR-I 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 205 VGRYRARGGRLVSVSPLRDDIAAIAgplDDRCRwlaPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTGYERFERYLLg 284
Cdd:cd02766 179 IQEARKRGAKVVVIDPYRTATAARA---DLHIQ---IRPGTDGALALGVAKVLFREGLYDRDFLARHTEGFEELKAHLE- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 285 lddgiPKTPEWAAALSGLAAGDLRDLARRMAEH-RTLITTSLSLQRIEHGEQTVWMAATLAAMLGQIglpgggfghGYSS 363
Cdd:cd02766 252 -----TYTPEWAAEITGVSAEEIEELARLYGEAkPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNI---------GVPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 364 NGVgnpplacglpalpqgnnpvstfipVAAISEllqrpgqrlayngrllelPDIKCVYWAGGNPFHHHQNLPRLRRALSR 443
Cdd:cd02766 318 GGA------------------------FYSNSG------------------PPVKALWVYNSNPVAQAPDSNKVRKGLAR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 444 -VDTIVVHEQYWTAMAKHADIVVPTTTSFERDDFAASKTNPTLIAMPAMVPPYANARDDYHTFSALAHRLGFGKQFTEgR 522
Cdd:cd02766 356 eDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPPFE-E 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 624384294 523 SAREWLEHmydkwsaELDFPVPSFAEfwrtgrlELPTRTGLTWLADFRADP-AAHPLGTPSGRIEIFSDTVDAFALP 598
Cdd:cd02766 435 SDEEWLDQ-------ALDGTGLPLEG-------IDLERLLGPRKAGFPLVAwEDRGFPTPSGKFEFYSERAAKRGLP 497
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
50-697 |
4.23e-36 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 145.97 E-value: 4.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 50 RIANPAVRRGwlqhgpgpssARGAEEFVEVSWDELIELLASELRRTVDRYGNEAIYGSS-YGWASAGRFHHAQSqvhrfl 128
Cdd:PRK15488 98 RIVKPLKRVG----------ERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSkSGSLSSHLFHLATA------ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 129 nmLGGYTASRH-SYSAGASEVIFPHIVGAALFEALAetttwdvivdHTALLVAFG-----GLPVKNTavmpggttahpdR 202
Cdd:PRK15488 162 --FGSPNTFTHaSTCPAGYAIAAKVMFGGKLKRDLA----------NSKYIINFGhnlyeGINMSDT------------R 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 203 DYVGRYRARGGRLVSVSPlRDDIAAiagplDDRCRWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTGYERFERYL 282
Cdd:PRK15488 218 GLMTAQMEKGAKLVVFEP-RFSVVA-----SKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTSGFEELAASV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 283 LglddgiPKTPEWAAALSGLAAGDLRDLARRMAE----------HRTLITTS-LSLQRiehgeqtvwMAATLAAMLGQI- 350
Cdd:PRK15488 292 K------EYTPEWAEAISDVPADDIRRIARELAAaaphaivdfgHRATFTPEeFDMRR---------AIFAANVLLGNIe 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 351 ------GLPGGGFGHGYSSNGVGnPPLA-CGLPALPqgnNPVSTFIPVAaisellqrpGQRLAYNGR------------L 411
Cdd:PRK15488 357 rkgglyFGKNASVYNKLAGEKVA-PTLAkPGVKGMP---KPTAKRIDLV---------GEQFKYIAAgggvvqsiidatL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 412 LELP-DIKCVYWAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDDFAASKT--NPTLIAM 488
Cdd:PRK15488 424 TQKPyQIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPESTYLERDEEISDKSgkNPAYALR 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 489 PAMVPPYANARDDYHTFSALAHRLGFGKQFTegrsareWlEHMYDKWSAELDFPVPSFAEFWRTGRLELptrtGLTWL-- 566
Cdd:PRK15488 504 QRVVEPIGDTKPSWQIFKELGEKMGLGQYYP-------W-QDMETLQLYQVNGDHALLKELKKKGYVSF----GVPLLlr 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 567 -----ADFRAD-PAAHPLG------------TPSGRIEIFSDTVDAFAlpdcAGHptwyepsewlGGPR------AARYP 622
Cdd:PRK15488 572 epkmvAKFVARyPNAKAVDedgtygsqlkfkTPSGKIELFSAKLEALA----PGY----------GVPRyrdvalKKEDE 637
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 624384294 623 LHLIanQPRTRLHSQLDHGGASMASKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVV 697
Cdd:PRK15488 638 LYFI--QGKVAVHTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIRPDTL 710
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
45-593 |
2.05e-35 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 141.20 E-value: 2.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 45 VRHRSRIANPAVRRGwlqhgpgpssargaEEFVEVSWDELIELLASELRRTVDRYGNEAIYGssygWASAGRFHHAQSQV 124
Cdd:cd02753 49 VNSKDRLTKPLIRKN--------------GKFVEASWDEALSLVASRLKEIKDKYGPDAIAF----FGSAKCTNEENYLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 125 HRFLNMLGGY----TASR--HSYSagasevifphivGAALFEAL---AETTTWDVIVDhTALLVAFGglpvKNTAVmpgg 195
Cdd:cd02753 111 QKLARAVGGTnnvdHCARlcHSPT------------VAGLAETLgsgAMTNSIADIEE-ADVILVIG----SNTTE---- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 196 ttAHPdrdYVGRY--RA--RGGRLVSVSPLRDDIAAIAGplddrcRWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRY 271
Cdd:cd02753 170 --AHP---VIARRikRAkrNGAKLIVADPRRTELARFAD------LHLQLRPGTDVALLNAMAHVIIEEGLYDEEFIEER 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 272 CTGYERFERYLLGLddgipkTPEWAAALSGLAAGDLRDLARRMAE-HRTLITTSLSLQRIEHGEQTVWMAATLAAMLGQI 350
Cdd:cd02753 239 TEGFEELKEIVEKY------TPEYAERITGVPAEDIREAARMYATaKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 351 GLpgggfghgyssNGVGNPPL--------ACGLPALPQgnnpvstfipvaaisellqrpgqrlayngrllELPD-IKCVY 421
Cdd:cd02753 313 GR-----------PGTGVNPLrgqnnvqgACDMGALPN--------------------------------VLPGyVKALY 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 422 WAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDdfaASKTNptliAM-------PAMVPP 494
Cdd:cd02753 350 IMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKD---GTFTN----TErrvqrvrKAVEPP 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 495 YaNARDDYHTFSALAHRLGFGKQFtegRSAREWLEHMydkwsAELdfpVPSFAEF-WRtgRLELPtrTGLTWladfrADP 573
Cdd:cd02753 423 G-EARPDWEIIQELANRLGYPGFY---SHPEEIFDEI-----ARL---TPQYAGIsYE--RLERP--GGLQW-----PCP 481
|
570 580
....*....|....*....|
gi 624384294 574 AAHPLGTPSGRIEIFSdTVD 593
Cdd:cd02753 482 DEDHPGTPILHTERFA-TPD 500
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
50-511 |
3.04e-33 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 131.75 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 50 RIANPAVRRGwlqhgpgpssaRGaeEFVEVSWDELIELLASELRRTVDRYGNEAIY--GSSYGWASAGRFHHAQSQVHRF 127
Cdd:pfam00384 1 RLKYPMVRRG-----------DG--KFVRVSWDEALDLIAKKLKRIIKKYGPDAIAinGGSGGLTDVESLYALKKLLNRL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 128 LNMLGGYTASRHSYSAGASEVIFPHIVGAALFealaetTTWDVIVDHTALLVAFG-----GLPVKNTAVMPggttahpdr 202
Cdd:pfam00384 68 GSKNGNTEDHNGDLCTAAAAAFGSDLRSNYLF------NSSIADIENADLILLIGtnpreEAPILNARIRK--------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 203 dyvgRYRARGGRLVSVSPLRDDIAAIAgplddrcrWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRyctgyerferyl 282
Cdd:pfam00384 133 ----AALKGKAKVIVIGPRLDLTYADE--------HLGIKPGTDLALALAGAHVFIKELKKDKDFAPK------------ 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 283 lglddgipktpewaaalsglaagdlrdlarrmaehrTLITTSLSLQRIEHGEQTVWMAATLAAMLGQIGLPGGgfghgyS 362
Cdd:pfam00384 189 ------------------------------------PIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGG------G 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 363 SNGVGNpplacglpaLPQGNNPVSTFipvaaisELLQRPGQRLAYNGRLLELPDIKCVYWAGGNPFHHHQNLPRLRRALS 442
Cdd:pfam00384 227 WNGLNI---------LQGAASPVGAL-------DLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQ 290
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 443 RVDTIVVHEQYW-TAMAKHADIVVPTTTSFERDDFAASKTNPTLIAMPAMVPPYaNARDDYHTFSALAHR 511
Cdd:pfam00384 291 KLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPG-EAREDWKILRALSEV 359
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
40-609 |
9.69e-31 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 126.65 E-value: 9.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 40 NLPGAVRHRSRIANPAVRrgwlqHGPgpssaRGAEEFVEVSWDELIELLASELRRTVDRYGNEAIYGSSygwaSAGRFHH 119
Cdd:cd02759 44 AAPEIVYHPDRLLYPLKR-----VGE-----RGENKWERISWDEALDEIAEKLAEIKAEYGPESIATAV----GTGRGTM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 120 AQSQV--HRFLNMLGgytASRHSYSAgasevifpHIVGAALFEALAETTTWDVIVDHTallvafgGLPVKNTAVM----P 193
Cdd:cd02759 110 WQDSLfwIRFVRLFG---SPNLFLSG--------ESCYWPRDMAHALTTGFGLGYDEP-------DWENPECIVLwgknP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 194 GGTTAHPDRDYVGRYRARGGRLVSVSPLRDDIAAIAGplddrcRWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCT 273
Cdd:cd02759 172 LNSNLDLQGHWLVAAMKRGAKLIVVDPRLTWLAARAD------LWLPIRPGTDAALALGMLNVIINEGLYDKDFVENWCY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 274 GYERFERYLlglddgIPKTPEWAAALSGLAAGDLRDLARRMAEHR-TLITTSLSLQRIEHGEQTVWMAATLAAMLGQigl 352
Cdd:cd02759 246 GFEELAERV------QEYTPEKVAEITGVPAEKIRKAARLYATAKpACIQWGLAIDQQKNGTQTSRAIAILRAITGN--- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 353 pgggfghgyssngvgnpplacglpalpqgnnpvstfipvaaiselLQRPGqrlaynGRLLELPDIKCVYWAGGNPFHHHQ 432
Cdd:cd02759 317 ---------------------------------------------LDVPG------GNLLIPYPVKMLIVFGTNPLASYA 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 433 NLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDDF-AASKTNPTLIAMPAMVPPYANARDDYHTFSALAHR 511
Cdd:cd02759 346 DTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLrGGFEAENFVQLRQKAVEPYGEAKSDYEIVLELGKR 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 512 LGFGkqftegrsarewlEHMYDKwsaeldfpvpsfaefWRTGRLELPTRTGltwladfradpaahpLGTPSGRIEIFSDT 591
Cdd:cd02759 426 LGPE-------------EAEYYK---------------YEKGLLRPDGQPG---------------FNTPTGKVELYSTM 462
|
570
....*....|....*...
gi 624384294 592 VDAFALPDCaghPTWYEP 609
Cdd:cd02759 463 LEELGYDPL---PYYREP 477
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
40-518 |
1.26e-30 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 127.34 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 40 NLPGAVRHRSRIANPAVRRGwlqhgpgpssargAEEFVEVSWDELIELLASELRRTVDRYGNEAI--YGSsygwasaGRF 117
Cdd:cd02754 44 NLHKTLNGPERLTRPLLRRN-------------GGELVPVSWDEALDLIAERFKAIQAEYGPDSVafYGS-------GQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 118 HHAQSQVhrfLNMLG-GY-------TASRHSYSAGAsevifphivgAALFEAL---AETTTWDVIvDHTALLVAFGGlpv 186
Cdd:cd02754 104 LTEEYYA---ANKLAkGGlgtnnidTNSRLCMASAV----------AGYKRSFgadGPPGSYDDI-EHADCFFLIGS--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 187 kNTAVMpggttaHP-------DRdyvgRYRARGGRLVSVSPLRDDIAAIAgpldDRcrWLAPVPGTDVAIMLGLAYVLAT 259
Cdd:cd02754 167 -NMAEC------HPilfrrllDR----KKANPGAKIIVVDPRRTRTADIA----DL--HLPIRPGTDLALLNGLLHVLIE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 260 ESLADRAFLGRYCTGYERFERYLLGLddgipkTPEWAAALSGLAAGDLRDLARRMAEHRTLIttSLSLQRIEHGEQTVWM 339
Cdd:cd02754 230 EGLIDRDFIDAHTEGFEELKAFVADY------TPEKVAEITGVPEADIREAARLFGEARKVM--SLWTMGVNQSTQGTAA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 340 AAT---LAAMLGQIglpGGGFGHGYSSNGVGN-------PPLACGLPALPQGNNP-----VSTF--IPVAAISEllqRPG 402
Cdd:cd02754 302 NNAiinLHLATGKI---GRPGSGPFSLTGQPNamggrevGGLANLLPGHRSVNNPehraeVAKFwgVPEGTIPP---KPG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 403 QRlAYNG-RLLELPDIKCVYWAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYW-TAMAKHADIVVPTTTSFERDDFAask 480
Cdd:cd02754 376 LH-AVEMfEAIEDGEIKALWVMCTNPAVSLPNANRVREALERLEFVVVQDAFAdTETAEYADLVLPAASWGEKEGTM--- 451
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 624384294 481 TNP--TLIAMPAMVPPYANARDDYHTFSALAHRLGFGKQF 518
Cdd:cd02754 452 TNSerRVSLLRAAVEPPGEARPDWWILADVARRLGFGELF 491
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
70-519 |
1.74e-30 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 125.49 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 70 ARGAEEFVEVSWDELIELLASELRRTVDRYGNEAIygssygwASAGRFHHAQSQVHRFLNMLGGYTASRH------SYSA 143
Cdd:cd02755 65 ERGEGKFREASWDEALQYIASKLKEIKEQHGPESV-------LFGGHGGCYSPFFKHFAAAFGSPNIFSHestclaSKNL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 144 GASEVIFPHivgaalfealaeTTTWDVIVDHTALLVAFGglpvknTAVMPGGTTAHPDRdyVGRYRARGGRLVSVSPLRD 223
Cdd:cd02755 138 AWKLVIDSF------------GGEVNPDFENARYIILFG------RNLAEAIIVVDARR--LMKALENGAKVVVVDPRFS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 224 DIAAIAGplddrcRWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTGYERFEryllglDDGIPKTPEWAAALSGLA 303
Cdd:cd02755 198 ELASKAD------EWIPIKPGTDLAFVLALIHVLISENLYDAAFVEKYTNGFELLK------AHVKPYTPEWAAQITDIP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 304 AGDLRDLARRMAEH--RTLITTSLSLQRIEHGEQTVWMAATLAAMLGqiglpgggfghgyssnGVGNPplacGlpALPQG 381
Cdd:cd02755 266 ADTIRRIAREFAAAapHAVVDPGWRGTFYSNSFQTRRAIAIINALLG----------------NIDKR----G--GLYYA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 382 NNPvstfipvaaisellqRPGQrlayngrllelpdIKCVYWAGGNPFHHHQNLPRLRRALSRVDTIVVHEQYWTAMAKHA 461
Cdd:cd02755 324 GSA---------------KPYP-------------IKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYA 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 624384294 462 DIVVPTTTSFERDDFAASKTNPTL---IAMPAmVPPYANARDDYHTFSALAHRLGFGKQFT 519
Cdd:cd02755 376 DVILPEATYLERDEPFSDKGGPAPavaTRQRA-IEPLYDTRPGWDILKELARRLGLFGTPS 435
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
48-530 |
4.91e-30 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 125.59 E-value: 4.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 48 RSRIANPAVRRGWLQHGPGPSSA---RGAEEFVEVSWDELIELLASELRRTVDRYGNEAIYgssygwasagrFHHAQSQV 124
Cdd:cd02762 35 KGYICPKAAALGDYQNDPDRLRTpmrRRGGSFEEIDWDEAFDEIAERLRAIRARHGGDAVG-----------VYGGNPQA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 125 HRFLNM------LGGYTASRHSYSAGASEviFPHIVGAALFEALAETTTWDVIvDHTALLVAFGGlpvkNTAVMPGGTTA 198
Cdd:cd02762 104 HTHAGGayspalLKALGTSNYFSAATADQ--KPGHFWSGLMFGHPGLHPVPDI-DRTDYLLILGA----NPLQSNGSLRT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 199 HPDRD-YVGRYRARGGRLVSVSPLRDDIAAIAGplddrcRWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTGYER 277
Cdd:cd02762 177 APDRVlRLKAAKDRGGSLVVIDPRRTETAKLAD------EHLFVRPGTDAWLLAAMLAVLLAEGLTDRRFLAEHCDGLDE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 278 FERYLLGLddgipkTPEWAAALSGLAAGDLRDLARRMAEHRTL-ITTSLSLQRIEHGEQTVWMAATLAAMLGQIGLPGGG 356
Cdd:cd02762 251 VRAALAEF------TPEAYAPRCGVPAETIRRLAREFAAAPSAaVYGRLGVQTQLFGTLCSWLVKLLNLLTGNLDRPGGA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 357 FGHGYSSNGVGNPPL---ACGLPALPQGNNP-VSTFIPVAAISELLQRPGQrlaynGRllelpdIKCVYWAGGNPFHHHQ 432
Cdd:cd02762 325 MFTTPALDLVGQTSGrtiGRGEWRSRVSGLPeIAGELPVNVLAEEILTDGP-----GR------IRAMIVVAGNPVLSAP 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 433 NLPRLRRALSRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDDF-----AASKTNPTLiaMPAMVPPYANARDDYHTFSA 507
Cdd:cd02762 394 DGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPHAtffnlEFPRNAFRY--RRPLFPPPPGTLPEWEILAR 471
|
490 500 510
....*....|....*....|....*....|
gi 624384294 508 LAH------RLGF-GKQFTEGRSAREWLEH 530
Cdd:cd02762 472 LVEaldavlRAGFyGERAGGTLLLAALLER 501
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
69-609 |
1.22e-21 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 99.86 E-value: 1.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 69 SARGAEEFVEVSWDELIELLASELRRTVDRYGneaiyGSSYGWASAGRFHHAQSQVHRFLNMLGGY----TASRHSYSAG 144
Cdd:cd02765 64 GERGEGKFERITWDEALDTIADKLTEAKREYG-----GKSILWMSSSGDGAILSYLRLALLGGGLQdaltYGIDTGVGQG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 145 ASEVIfphivGAALFEALAETTTWDvivdHTALLVAFGGLPVKntavmpggtTAHPDRDYVGRYRARGGRLVSVSPLRDD 224
Cdd:cd02765 139 FNRVT-----GGGFMPPTNEITDWV----NAKTIIIWGSNILE---------TQFQDAEFFLDARENGAKIVVIDPVYST 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 225 IAAIAGplddrcRWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTG----YERFERYLLGLDDGIPKTPE----WA 296
Cdd:cd02765 201 TAAKAD------QWVPIRPGTDPALALGMINYILEHNWYDEAFLKSNTSApflvREDNGTLLRQADVTATPAEDgyvvWD 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 297 AALSGLAAGD----LRDLARRMAEHRTLITTSLSLQRIEHGEQTVWMAATLAAMLGQIGLPGGGFghgYSSNGVGNPPLA 372
Cdd:cd02765 275 TNSDSPEPVAatniNPALEGEYTINGVKVHTVLTALREQAASYPPKAAAEICGLEEAIIETLAEW---YATGKPSGIWGF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 373 CGLPALPQGNNPVSTFIPVAAISELLQRPGQRLAYngrllelpdIKCVyWAGGNPFHHHQ-NLPRLRRALSRVDTIVVHE 451
Cdd:cd02765 352 GGVDRYYHSHVFGRTAAILAALTGNIGRVGGGVGQ---------IKFM-YFMGSNFLGNQpDRDRWLKVMKNLDFIVVVD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 452 QYWTAMAKHADIVVPTTTSFERDD-FAASKTNPTLIAMPAMVPPYANARDDYHTFSALAHRLGFGKQFTEgrSAREWLEh 530
Cdd:cd02765 422 IFHTPTVRYADIVLPAAHWFEVEDlLVRYTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERLGLGDYFPK--TPEDYVR- 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 531 mydkwsAELDFPVPSFAEFwrtgRLELPTRTGLTWLADFRADPAAHPL----GTPSGRIEIFSDTvdafALPDCAGHPTW 606
Cdd:cd02765 499 ------AFMNSDDPALDGI----TWEALKEEGIIMRLATPEDPYVAYLdqkfGTPSGKLEFYNEA----APELEEALPLP 564
|
...
gi 624384294 607 YEP 609
Cdd:cd02765 565 EEP 567
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
50-530 |
3.61e-21 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 97.39 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 50 RIANPAVRRGwlqhgpgpssARGAEEFVEVSWDELIELLASELRRTVDRYGNEAIYGSSYgwasagrfHHAQSQVH---- 125
Cdd:cd02750 66 RVKYPLKRVG----------ARGEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSP--------IPAMSMVSyaag 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 126 -RFLNMLGGYTASRHSYSaGASEVIFPHIVGAALFEalAETTTWdvivDHTALLVAFGglpvKNTAVmpggtTAHPDRDY 204
Cdd:cd02750 128 sRFASLIGGVSLSFYDWY-GDLPPGSPQTWGEQTDV--PESADW----YNADYIIMWG----SNVPV-----TRTPDAHF 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 205 VGRYRARGGRLVSVSPlrdDIAAIAGPLDdrcRWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCtgyerferyllg 284
Cdd:cd02750 192 LTEARYNGAKVVVVSP---DYSPSAKHAD---LWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYT------------ 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 285 lDDGI-PKTPEWAAALSGLAAGDLRDLARRMAEH-RTLITTSLSLQRIEHGEQTVWMAATLAAMLGQIglpgggfghgyS 362
Cdd:cd02750 254 -DLPFlVYTPAWQEAITGVPRETVIRLAREFATNgRSMIIVGAGINHWYHGDLCYRALILLLALTGNE-----------G 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 363 SNGVGnpplacglpalpqgnnpVSTFIpvaaisellqrpGQrlayngrllelPDIKCVYWagGNPFHHHQNLPRLRRA-- 440
Cdd:cd02750 322 KNGGG-----------------WAHYV------------GQ-----------PRVLFVWR--GNLFGSSGKGHEYFEDap 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 441 LSRVDTIVVHEQYWTAMAKHADIVVPTTTSFERDDFAASKTNPTLIAMPAMVPPYANARDDYHTFSALAHRLGFgkqFTE 520
Cdd:cd02750 360 EGKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKVPW---RTL 436
|
490
....*....|
gi 624384294 521 GRSAREWLEH 530
Cdd:cd02750 437 TGRQQFYLDH 446
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
623-731 |
4.14e-21 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 88.87 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 623 LHLIANQPRTRLHSQLDHGGASMASKiRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQLSTG 702
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAK-PEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100
....*....|....*....|....*....
gi 624384294 703 AWFDPadprdpdsmcVHGNPNALSNDSGT 731
Cdd:pfam01568 80 WWYEP----------RGGNANALTDDATD 98
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
620-704 |
4.68e-19 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 83.57 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 620 RYPLHLIANQPRTRLHSQldHGGASMASKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQL 699
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQ--FSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTA 78
|
....*
gi 624384294 700 STGAW 704
Cdd:cd02785 79 EQGWW 83
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
630-732 |
1.35e-18 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 81.60 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 630 PRTRLHSQLDHGGASMAsKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQLSTGAWFDpad 709
Cdd:cd02775 1 LRDHFHSGTRTRNPWLR-ELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHR--- 76
|
90 100
....*....|....*....|...
gi 624384294 710 prdpdsMCVHGNPNALSNDSGTS 732
Cdd:cd02775 77 ------GGRGGNANVLTPDALDP 93
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
621-749 |
1.70e-16 |
|
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 76.18 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 621 YPLHLIANQPRTRLHSQLDHggasmASKIRGREP--IRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQ 698
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDN-----VPWLREAFPqeVWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 624384294 699 LSTGAWFDPadprDPDSMCVHGNPNALsNDSGTSSLAHGSTGQHVLVQIER 749
Cdd:cd02794 76 LPQGAWYEP----DANGIDKGGCINTL-TGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
621-747 |
3.91e-15 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 71.93 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 621 YPLHLIANQPRTRLHSQLdhggASMASKIR--GREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVq 698
Cdd:cd02786 1 YPLRLITPPAHNFLNSTF----ANLPELRAkeGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVV- 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 624384294 699 LSTGAWFDPADPRdpdsmcvHGNPNALSNDSGTsSLAHGSTGQHVLVQI 747
Cdd:cd02786 76 VAEGGWWREHSPD-------GRGVNALTSARLT-DLGGGSTFHDTRVEV 116
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
620-749 |
5.57e-11 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 60.78 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 620 RYPLHLIANQpRTR--LHSQLdHGGASMaskiRGREP---IRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRP 694
Cdd:cd02781 1 EYPLILTTGA-RSYyyFHSEH-RQLPSL----RELHPdpvAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRP 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 624384294 695 KVVQLSTGAWFDPADPRDPDSMCV-HGNPNALSNDSGTSSLAHGSTGQHVLVQIER 749
Cdd:cd02781 75 GVVRAEHGWWYPEREAGEPALGGVwESNANALTSDDWNDPVSGSSPLRSMLCKIYK 130
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
66-565 |
1.60e-10 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 64.38 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 66 GPSSARGAE-EFVEVSWDELIELLASELR--RTVDRYGNEAIYGSSYGwasagrfHHAQSQVHRFLNMLGgyTASRHSYS 142
Cdd:cd02757 65 NPRKGRDVDpKFVPISWDEALDTIADKIRalRKENEPHKIMLHRGRYG-------HNNSILYGRFTKMIG--SPNNISHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 143 AGASEVifpHIVGAALFEALAETTTWDVivDHTALLVAFGGLPVKNTAVMPggttaHPDRDYVGRyrARGGRLVSVSPLR 222
Cdd:cd02757 136 SVCAES---EKFGRYYTEGGWDYNSYDY--ANAKYILFFGADPLESNRQNP-----HAQRIWGGK--MDQAKVVVVDPRL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 223 DDIAAIAGplddrcRWLAPVPGTDVAIMLGLAYVLATESLADRAFLGRYCTGYERF-ERYLLGLDDGIPK---------- 291
Cdd:cd02757 204 SNTAAKAD------EWLPIKPGEDGALALAIAHVILTEGLWDKDFVGDFVDGKNYFkAGETVDEESFKEKsteglvkwwn 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 292 ------TPEWAAALSGLAAGDLRDLARRMA--EHRTLITTSLSLQRIEHGEQTVWMAATLAAMLGQIglpgggfghgYSS 363
Cdd:cd02757 278 lelkdyTPEWAAKISGIPAETIERVAREFAtaAPAAAAFTWRGATMQNRGSYNSMACHALNGLVGSI----------DSK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 364 NGVGNPplacglpalpqgnnpvstfipvaaisellqrpgqrlayngrlLELPDIKCVYWAGGNPFHHHQNLPRLRRALSR 443
Cdd:cd02757 348 GGLCPN------------------------------------------MGVPKIKVYFTYLDNPVFSNPDGMSWEEALAK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 444 VDTIVVHEQYWTAMAKHADIVVPTTTSFERDDFAASKTN--PTL-IAMPAMVPPYaNARDDYHTFSALAHRLGfGKQFTE 520
Cdd:cd02757 386 IPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQENNlhPWLsIRQPVVKSLG-EVREETEILIELAKKLD-PKGSDG 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 624384294 521 GRSAREWL-----EHMYDKWSAELDFPVPS-----FAEFWRTGRLELPTRTGLTW 565
Cdd:cd02757 464 MKRYAPGQfkdpeTGKNNRWEFENVFPTETgkfefYSETLKKYLQNHADKKKVSW 518
|
|
| Molybdopterin_N |
pfam18364 |
Molybdopterin oxidoreductase N-terminal domain; This is the N-terminal domain of pfam00384 ... |
6-46 |
2.68e-10 |
|
Molybdopterin oxidoreductase N-terminal domain; This is the N-terminal domain of pfam00384 found in a number of molybdopterin-containing oxidoreductases such as dimethyl sulfoxide/trimethylamine N-oxide reductase, also known as DMSO reductase (EC:1.7.2.3, EC:1.8.5.3).
Pssm-ID: 465726 [Multi-domain] Cd Length: 41 Bit Score: 55.86 E-value: 2.68e-10
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 624384294 6 SATHWGVFTARVHGGDIAAVAALASDTNPAPQLQNLPGAVR 46
Cdd:pfam18364 1 TASHWGAFRAVVKDGRIVGVEPFEGDPDPSPLLQGVPDAVY 41
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
43-315 |
1.11e-09 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 61.77 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 43 GAVRHRS--RIANPAVRRGwlqhgpgpssARGAEEFVEVSWDELIELLA---SELRRT--------VDRYGNEAIYG--- 106
Cdd:cd02763 45 GIMKQYSpaRLTKPLLRKG----------PRGSGQFEEIEWEEAFSIATkrlKAARATdpkkfaffTGRDQMQALTGwfa 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 107 SSYG---WASAGRFHHAqsqvhrflNMLGGYTasrhsYSAGASevifphivgaalfealaettTWDvivdhtallvaFGG 183
Cdd:cd02763 115 GQFGtpnYAAHGGFCSV--------NMAAGGL-----YSIGGS--------------------FWE-----------FGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 184 LPVKNTA--VMPGGTTAH---PDRDYVGRYRARGGRLVSVSPLRDDIAAIAgplDDrcrWLAPVPGTDVAIMLGLAYVLA 258
Cdd:cd02763 151 PDLEHTKyfMMIGVAEDHhsnPFKIGIQKLKRRGGKFVAVNPVRTGYAAIA---DE---WVPIKPGTDGAFILALAHELL 224
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 624384294 259 TESLADRAFLGRYCTGYERferyllglddgIPKTPEWAAALSGLAAGDLRDLARRMA 315
Cdd:cd02763 225 KAGLIDWEFLKRYTNAAEL-----------VDYTPEWVEKITGIPADTIRRIAKELG 270
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
37-351 |
2.18e-09 |
|
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239168 [Multi-domain] Cd Length: 574 Bit Score: 60.78 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 37 QLQNLPGA-VRHRSRIANPAVRRgwlqhgpgpssaRGAEEFVEVSWDELIELLASELRRTVD---------RYGNEAiyg 106
Cdd:cd02767 50 ELRTWSDYeLEHLGRLTYPMRYD------------AGSDHYRPISWDEAFAEIAARLRALDPdraafytsgRASNEA--- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 107 sSYGWASAGRfhhaqsqvhrflnMLGgyT-----ASR--HSysagASEVIFPHIVGAAlfealAETTTWDViVDHTALLV 179
Cdd:cd02767 115 -AYLYQLFAR-------------AYG--TnnlpdCSNmcHE----PSSVGLKKSIGVG-----KGTVSLED-FEHTDLIF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 180 AFGGLPVKNTAVMPGgttahpdrdYVGRYRARGGRLVSVSPLR-----------DDIAAIAGPLDDRCRWLAPVPGTDVA 248
Cdd:cd02767 169 FIGQNPGTNHPRMLH---------YLREAKKRGGKIIVINPLRepglerfanpqNPESMLTGGTKIADEYFQVRIGGDIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 249 IMLGLA-YVLATE----SLADRAFLGRYCTGYERFERYLLGLDD-------GIPKTpewaaalsglaagDLRDLARRMAE 316
Cdd:cd02767 240 LLNGMAkHLIERDdepgNVLDHDFIAEHTSGFEEYVAALRALSWdeierasGLSRE-------------EIEAFAAMYAK 306
|
330 340 350
....*....|....*....|....*....|....*.
gi 624384294 317 -HRTLITTSLSLQRIEHGEQTVWMAATLAAMLGQIG 351
Cdd:cd02767 307 sERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIG 342
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
657-728 |
1.47e-08 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 53.35 E-value: 1.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 624384294 657 IHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQLstgAWFDPAdpRDPDSMCVhgnpNALSND 728
Cdd:cd02791 39 IHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFV---PMHWGD--QFGRSGRV----NALTLD 101
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
619-697 |
4.15e-08 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 52.12 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 619 ARYPLHLIanqprT-RLhsqLDH-GGASMASKIRG-----REP-IRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDD 690
Cdd:cd00508 1 EEYPLVLT-----TgRL---LEHwHTGTMTRRSPRlaalaPEPfVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTD 72
|
....*..
gi 624384294 691 GLRPKVV 697
Cdd:cd00508 73 RVRPGTV 79
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
620-749 |
8.89e-08 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 51.62 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 620 RYPLHLIANQPRTRLHSQLDHGGASMaSKIRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVVQL 699
Cdd:cd02782 1 DYPFLLLIGRRHLRSNNSWLHNDPRL-VKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 624384294 700 STGAWFDpaDPRDPDSMCVHG-NPNALSNDSGTSSLAHGSTGQHVLVQIER 749
Cdd:cd02782 80 PHGWGHD--YPGVSGAGSRPGvNVNDLTDDTQRDPLSGNAAHNGVPVRLAR 128
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
650-697 |
2.49e-07 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 50.45 E-value: 2.49e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 624384294 650 RGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVV 697
Cdd:cd02776 28 RGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTV 75
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
621-702 |
3.43e-07 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 49.98 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 621 YPLHLIAnqPRTRLHSQldhggASMASK----IRGREPIRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKV 696
Cdd:cd02780 1 YPFILVT--FKSNLNSH-----RSANAPwlkeIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGV 73
|
....*.
gi 624384294 697 VQLSTG 702
Cdd:cd02780 74 VAIEHG 79
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
421-545 |
3.73e-06 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 50.48 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 421 YWAGGNPFHHHQNLPRLRRALSRVDTIVV---HEQYWTAMAKHAD----------IVVPTTTSFERDDfAASKTNPTLIA 487
Cdd:cd02752 337 YLGGQNPNSSFPNANKVRRALDKLDWLVVidpFPTETAAFWKNPGmdpksiqtevFLLPAACQYEKEG-SITNSGRWLQW 415
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 624384294 488 MPAMVPPYANARDDYHTFSALAHRLGFGKQFTEGRSAREWLEHMYDKWsaelDFPVPS 545
Cdd:cd02752 416 RYKVVEPPGEAKSDGDILVELAKRLGFLYEKEGGAFPEPITKWNYGYG----DEPTPE 469
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
655-709 |
1.73e-04 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 41.68 E-value: 1.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 624384294 655 IRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVV------------QLSTGAWfDPAD 709
Cdd:cd02779 35 IEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTfmlmahprpganGLVTPYV-DPET 100
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
601-697 |
2.28e-04 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 44.99 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 624384294 601 AGHPTWYEPSEWLGGPRAARY-----PLHLIANqpRTRLHSQLDhGGASMASKIRGREPIRIHPDDAAARELTDGDIVRV 675
Cdd:PRK14991 862 SGCPTWYPPRLADGTPLREQFpesqwPLLLISF--KSNLMSSMS-IASPRLRQVKPANPVALNPQDAARLGIQHGDRVRI 938
|
90 100
....*....|....*....|..
gi 624384294 676 FNDRGACLAGVVIDDGLRPKVV 697
Cdd:PRK14991 939 STPGGSVVAQASVLNGVMPGVI 960
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
655-697 |
2.22e-03 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 38.37 E-value: 2.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 624384294 655 IRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVV 697
Cdd:cd02790 37 VEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVV 79
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
655-697 |
2.33e-03 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 38.74 E-value: 2.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 624384294 655 IRIHPDDAAARELTDGDIVRVFNDRGACLAGVVIDDGLRPKVV 697
Cdd:cd02792 37 VEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEV 79
|
|
| |
