|
Name |
Accession |
Description |
Interval |
E-value |
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
15-707 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 864.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 15 VIETQCPFCSVQCKMTVTEGENGIpgqrraeYKVEGVPNA-ASEGRVCVKGMHAHQHAVHSQRLTHPLIRSKGELVPCSW 93
Cdd:COG3383 6 KVKTVCPYCGVGCGIDLEVKDGKI-------VKVEGDPDHpVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVSW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 94 DEAFAVASQHMQGILEQYGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAGSKTFGIDrGLTFR 173
Cdd:COG3383 79 DEALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSD-APPNS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 174 LADIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDEGLI 253
Cdd:COG3383 158 YDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 254 DETFIQARTNGYDELRVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATG 333
Cdd:COG3383 238 DEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 334 KIGREGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEKDRAYVASVWGVDAssLPGK-GVSAYEMMELIHQGGIKSL 412
Cdd:COG3383 318 NIGRPGTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPP--LPDKpGLTAVEMFDAIADGEIKAL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 413 FVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARHD 492
Cdd:COG3383 396 WIIGENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPD 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 493 WMILCSLADRLGKRhyFRFNEPEEIFNELRLASKggiaDYYGITYDRLRREKGVYWPCPSPEETGVGLLFQQSFAHPDGK 572
Cdd:COG3383 476 WEIIAELARRLGYG--FDYDSPEEVFDEIARLTP----DYSGISYERLEALGGVQWPCPSEDHPGTPRLFTGRFPTPDGK 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 573 AVFSVTE-GDPWKGVSEDYPLILTNGRVLSHYLTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSF 651
Cdd:COG3383 550 ARFVPVEyRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGEV 629
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1553133439 652 IVRSRIKDQIREDTLFVPMHWGGvQNVNYATRPELDPFCKMPGFKTSAVRIRSLKR 707
Cdd:COG3383 630 VLRARVTDRVRPGTVFMPFHWGE-GAANALTNDALDPVSKQPEYKACAVRVEKVAE 684
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
18-582 |
0e+00 |
|
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: 710.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 18 TQCPFCSVQCKMTVTEGENGIpgqrraeYKVEGVPNA-ASEGRVCVKGMHAHQHAVHSQRLTHPLIRSKG-ELVPCSWDE 95
Cdd:cd02754 2 TTCPYCGVGCGVEIGVKDGKV-------VAVRGDPEHpVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGgELVPVSWDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 96 AFAVASQHMQGILEQYGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAGSKTFGIDrGLTFRLA 175
Cdd:cd02754 75 ALDLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGAD-GPPGSYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 176 DIPLARCIVLAGTNIAECQPTLLPYFNQAKEN--GAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDEGLI 253
Cdd:cd02754 154 DIEHADCFFLIGSNMAECHPILFRRLLDRKKAnpGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 254 DETFIQARTNGYDELRVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATG 333
Cdd:cd02754 234 DRDFIDAHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 334 KIGREGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEKDRAYVASVWGVDASSLPGK-GVSAYEMMELIHQGGIKSL 412
Cdd:cd02754 314 KIGRPGSGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVPEGTIPPKpGLHAVEMFEAIEDGEIKAL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 413 FVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMF-MSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARH 491
Cdd:cd02754 394 WVMCTNPAVSLPNANRVREALERLEFVVVQDAFaDTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 492 DWMILCSLADRLGKRHYFRFNEPEEIFNELRLASKGGIADYYGITYDRLRReKGVYWPCPSPEETGVGLLFQ-QSFAHPD 570
Cdd:cd02754 474 DWWILADVARRLGFGELFPYTSPEEVFEEYRRLSRGRGADLSGLSYERLRD-GGVQWPCPDGPPEGTRRLFEdGRFPTPD 552
|
570
....*....|..
gi 1553133439 571 GKAVFSVTEGDP 582
Cdd:cd02754 553 GRARFVAVPYRP 564
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
18-702 |
0e+00 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 586.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 18 TQCPFCSVQCKMT-VTEGENGIpgqrRAEYKVEGVPNaasEGRVCVKGMHAHQHAVHSQRLTHPLIRSKGELVPCSWDEA 96
Cdd:TIGR01591 1 TVCPYCGVGCSLNlVVKDGKIV----RVEPYQGHKAN---RGHLCVKGYFAWEFINSKDRLTTPLIREGDKFREVSWDEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 97 FAVASQHMQGILEQYGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAGSKTFGIDRGlTFRLAD 176
Cdd:TIGR01591 74 ISYIAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAM-SNTISE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 177 IPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDEGLIDET 256
Cdd:TIGR01591 153 IENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 257 FIQARTNGYDELRVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIG 336
Cdd:TIGR01591 233 FIEKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 337 REGCGYGAITGQGNGQGGREHGQKADQLPGYRSIENEKDRAYVASVWGVdaSSLPGK-GVSAYEMMELIHQGGIKSLFVM 415
Cdd:TIGR01591 313 KPGGGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGV--VKLPAEpGLRIPEMIDAAADGDVKALYIM 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 416 GSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDWMI 495
Cdd:TIGR01591 391 GEDPLQSDPNTSKVRKALEKLELLVVQDIFMTETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEI 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 496 LCSLADRLGKRhyFRFNEPEEIFNELRLASKggiaDYYGITYDRLRREKGVYWPCPSPEETGVGLLFQQSFAHPDGKAVF 575
Cdd:TIGR01591 471 IQELANALGLD--WNYNHPQEIMDEIRELTP----LFAGLTYERLDELGSLQWPCNDSDASPTSYLYKDKFATPDGKAKF 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 576 -SVTEGDPWKGVSEDYPLILTNGRVLSHYLTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVR 654
Cdd:TIGR01591 545 iPLEWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRGEITLR 624
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1553133439 655 SRIKDQIREDTLFVPMHWGGVQnVNYATRPELDPFCKMPGFKTSAVRI 702
Cdd:TIGR01591 625 AKVSDRVNKGAIYITMHFWDGA-VNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
18-703 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 562.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 18 TQCPFCSVQC--KMTVTEGengipgqrRAeYKVEGVPNA-ASEGRVCVKGMHAHQHAVHSQRLTHPLIR----SKGELVP 90
Cdd:COG0243 26 TTCPGCGVGCglGVKVEDG--------RV-VRVRGDPDHpVNRGRLCAKGAALDERLYSPDRLTYPMKRvgprGSGKFER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 91 CSWDEAFAVASQHMQGILEQYGPDANAVYGGGS----LTNETAYLLGKFARvALGTRHIDYNGRFCMSAAASAGSKTFGI 166
Cdd:COG0243 97 ISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGsagrLSNEAAYLAQRFAR-ALGTNNLDDNSRLCHESAVAGLPRTFGS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 167 DRGlTFRLADIPLARCIVLAGTNIAECQPTLLPYFNQA-KENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLK 245
Cdd:COG0243 176 DKG-TVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAH 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 246 IIMDEGLIDETFIQARTNGYDELRVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHF 325
Cdd:COG0243 255 VLIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVRAI 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 326 LNLVLATGKIGREGCGYGAITGqgngqggrehgqkadqlpgyRSIENEKDRayvasvwgvdasslpgkgvsayemmelih 405
Cdd:COG0243 335 ANLALLTGNIGKPGGGPFSLTG--------------------EAILDGKPY----------------------------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 406 qgGIKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLE-GRVLLREAGRQ 484
Cdd:COG0243 366 --PIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVE 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 485 APGEARHDWMILCSLADRLGKRHYFRF-NEPEEIFNELRLASKGGiadyyGITYDRLRREKGVYWPCPSPEETGVgllfQ 563
Cdd:COG0243 444 PPGEARSDWEIFAELAKRLGFEEAFPWgRTEEDYLRELLEATRGR-----GITFEELREKGPVQLPVPPEPAFRN----D 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 564 QSFAHPDGKAVFSVTEG---------DPWKGVSE---DYPLILTNGRVLSHYLTgvQTRRSPTLLARELENFAEIHPNTA 631
Cdd:COG0243 515 GPFPTPSGKAEFYSETLalpplpryaPPYEGAEPldaEYPLRLITGRSRDQWHS--TTYNNPRLREIGPRPVVEINPEDA 592
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1553133439 632 QRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLFVPMHWG------GVQNVNYATRPELDPFCKMPGFKTSAVRIR 703
Cdd:COG0243 593 AALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWyepaddKGGNVNVLTPDATDPLSGTPAFKSVPVRVE 670
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
17-582 |
9.15e-175 |
|
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: 509.45 E-value: 9.15e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 17 ETQCPFCSVQCKMTVtEGENGIPgqrraeYKVEGVPNA-ASEGRVCVKGMHAHQHAVHSQRLTHPLIRSKGELVPCSWDE 95
Cdd:cd02753 1 KTVCPYCGVGCGLEL-WVKDNKI------VGVEPVKGHpVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 96 AFAVASQHMQGILEQYGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAGSKTFGIDRGlTFRLA 175
Cdd:cd02753 74 ALSLVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAM-TNSIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 176 DIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDEGLIDE 255
Cdd:cd02753 153 DIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 256 TFIQARTNGYDELRVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKI 335
Cdd:cd02753 233 EFIEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 336 GREGCGYGAITGQGNGQGGREHGQKADQLPGYrsienekdrayvasvwgvdasslpgkgvsayemmelihqggIKSLFVM 415
Cdd:cd02753 313 GRPGTGVNPLRGQNNVQGACDMGALPNVLPGY-----------------------------------------VKALYIM 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 416 GSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDWMI 495
Cdd:cd02753 352 GENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEI 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 496 LCSLADRLG-KRHYFRfnePEEIFNELRLASKggiaDYYGITYDRLRREKGVYWPCPSPEETGVGLLFQQSFAHPDGKAV 574
Cdd:cd02753 432 IQELANRLGyPGFYSH---PEEIFDEIARLTP----QYAGISYERLERPGGLQWPCPDEDHPGTPILHTERFATPDGKAR 504
|
....*...
gi 1553133439 575 FSVTEGDP 582
Cdd:cd02753 505 FMPVEYRP 512
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
17-503 |
5.44e-109 |
|
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: 335.45 E-value: 5.44e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 17 ETQCPFCSVQCKMTVTEGENGIpgqrraeYKVEGVPN-AASEGRVCVKGMHAHQHAVHSQRLTHPLIRS--KGELVPCSW 93
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKV-------VRIEGDPNhPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVggRGKFVPISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 94 DEAFAVASQHMQGILEQYGPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRFCMSAAAsAGSKTFGIDrGLTFR 173
Cdd:cd00368 74 DEALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLR-ALGSNNVDSHARLCHASAV-AALKAFGGG-APTNT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 174 LADIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAmlkiimdegli 253
Cdd:cd00368 151 LADIENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA----------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 254 detfiqartngydelrvylnsfdlSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATG 333
Cdd:cd00368 220 ------------------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 334 KIGREGCGYGAitgqgngqggrehgqkadqlpgyrsienekdrayvasvwgvdasslpgkgvsayemmelihqggikslf 413
Cdd:cd00368 276 NIGRPGGGLGP--------------------------------------------------------------------- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 414 vmGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDW 493
Cdd:cd00368 287 --GGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDW 364
|
490
....*....|
gi 1553133439 494 MILCSLADRL 503
Cdd:cd00368 365 EILRELAKRL 374
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
20-572 |
3.73e-90 |
|
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: 290.69 E-value: 3.73e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 20 CPF-CSVQCKMTVTEGENGIpgqrraeYKVEGVP-NAASEGRVCVKGMHAHQHAVHSQRLTHPLIRSK---GELVPCSWD 94
Cdd:cd02766 4 CPLdCPDTCSLLVTVEDGRI-------VRVEGDPaHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGrkgGQWERISWD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 95 EAFAVASQHMQGILEQYGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNgrFCMSAAASAGSKTFGIDRGLTfrL 174
Cdd:cd02766 77 EALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHALGASELRGT--ICSGAGIEAQKYDFGASLGND--P 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 175 ADIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDEGLID 254
Cdd:cd02766 153 EDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 255 ETFIQARTNGYDELRVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATGK 334
Cdd:cd02766 233 RDFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGN 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 335 IGREGCG--YGaitgqgngqggrehgqkadqlpgyrsienekdrayvasvwgvdasslpgkgvsayemmelIHQGGIKSL 412
Cdd:cd02766 313 IGVPGGGafYS------------------------------------------------------------NSGPPVKAL 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 413 FVMGSNPIVSNPNAGLVEEGL-KKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGR-VLLREAGRQAPGEAR 490
Cdd:cd02766 333 WVYNSNPVAQAPDSNKVRKGLaREDLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYyLQYNEPAIPPPGEAR 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 491 HDWMILCSLADRLGKRHYFrFNEPEEIFneLRLASKGGIADYYGITYDRLRRekgvYWPCPSPEEtgvgLLFQQSFAHPD 570
Cdd:cd02766 413 SNTEIFRELAKRLGFGEPP-FEESDEEW--LDQALDGTGLPLEGIDLERLLG----PRKAGFPLV----AWEDRGFPTPS 481
|
..
gi 1553133439 571 GK 572
Cdd:cd02766 482 GK 483
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
76-502 |
4.46e-76 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 248.85 E-value: 4.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 76 RLTHPLIR-SKGELVPCSWDEAFAVASQHMQGILEQYGPDANAVYG--GGSLTNETAYLLGKFARVALG--TRHIDYNGR 150
Cdd:pfam00384 1 RLKYPMVRrGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGgsGGLTDVESLYALKKLLNRLGSknGNTEDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 151 FCMSAAASAGSkTFGIDRGLTFRLADIPLARCIVLAGTNIAECQPTL-LPYFNQAKENGAKIVVIDPRKTATAAmgDMHL 229
Cdd:pfam00384 81 LCTAAAAAFGS-DLRSNYLFNSSIADIENADLILLIGTNPREEAPILnARIRKAALKGKAKVIVIGPRLDLTYA--DEHL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 230 PIRPGTDTVLADAMLKIIMDEGLIDETFiqartngydelrvylnsfdlseaagicglelghireaalaygeSDTGMVLTA 309
Cdd:pfam00384 158 GIKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------APKPIIIVG 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 310 RGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAITgqgNGQG-GREHGQKADQLPgyrsienekdrayvasvwgvdas 388
Cdd:pfam00384 195 AGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLN---ILQGaASPVGALDLGLV----------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 389 slpgKGVSAYEMMELIHQGGIKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFM-SETAQLADLVLPVTSYMENEG 467
Cdd:pfam00384 249 ----PGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNG 324
|
410 420 430
....*....|....*....|....*....|....*
gi 1553133439 468 TLTNLEGRVLLREAGRQAPGEARHDWMILCSLADR 502
Cdd:pfam00384 325 TYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
17-515 |
2.57e-73 |
|
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: 245.29 E-value: 2.57e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 17 ETQCPFCSVQCKmTVTEGENGipgqrRAEyKVEGVPN-AASEGRVCVKGMHAHQHAVHSQRLTHPLIRS--KGE--LVPC 91
Cdd:cd02759 1 KGTCPGCHSGCG-VLVYVKDG-----KLV-KVEGDPNhPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgeRGEnkWERI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 92 SWDEAFAVASQHMQGILEQYGPDANAVY-GGGSLTNE-TAYLLGKFARVaLGTRHIDYNGRFCMSAAASAGSKTFGIdrG 169
Cdd:cd02759 74 SWDEALDEIAEKLAEIKAEYGPESIATAvGTGRGTMWqDSLFWIRFVRL-FGSPNLFLSGESCYWPRDMAHALTTGF--G 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 170 LTFRLADIPLARCIVLAGTNIAECQPTLLPY-FNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIM 248
Cdd:cd02759 151 LGYDEPDWENPECIVLWGKNPLNSNLDLQGHwLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVII 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 249 DEGLIDETFIQARTNGYDELRVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNL 328
Cdd:cd02759 231 NEGLYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPACIQWGLAIDQQKNGTQTSRAIAIL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 329 VlatgkigregcgygAITGQGNGQGGrehgqkaDQLPGYRsienekdrayvasvwgvdasslpgkgvsayemmelihqgg 408
Cdd:cd02759 311 R--------------AITGNLDVPGG-------NLLIPYP---------------------------------------- 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 409 IKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGR--VLLREAGRQAP 486
Cdd:cd02759 330 VKMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAEnfVQLRQKAVEPY 409
|
490 500 510
....*....|....*....|....*....|.
gi 1553133439 487 GEARHDWMILCSLADRLGKR--HYFRFNEPE 515
Cdd:cd02759 410 GEAKSDYEIVLELGKRLGPEeaEYYKYEKGL 440
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
18-503 |
1.68e-71 |
|
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: 242.30 E-value: 1.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 18 TQCPFCSVQCKMTVTegengIPGQRRAeyKVEGVP-NAASEGRVCVKG--MHAHQHavHSQRLTHPLIRSKGELVPCSWD 94
Cdd:cd02762 2 RACILCEANCGLVVT-----VEDGRVA--SIRGDPdDPLSKGYICPKAaaLGDYQN--DPDRLRTPMRRRGGSFEEIDWD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 95 EAFAVASQHMQGILEQYGPDANAVYGGGSLTNEtaYLLGKFARV---ALGTRhidynGRFcmsAAASAGSKT-------- 163
Cdd:cd02762 73 EAFDEIAERLRAIRARHGGDAVGVYGGNPQAHT--HAGGAYSPAllkALGTS-----NYF---SAATADQKPghfwsglm 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 164 FGidRGLTFRLADIPLARCIVLAGTNIAECQ--PTLLPYF----NQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDT 237
Cdd:cd02762 143 FG--HPGLHPVPDIDRTDYLLILGANPLQSNgsLRTAPDRvlrlKAAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 238 VLADAMLKIIMDEGLIDETFIQARTNGYDELRVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTD 317
Cdd:cd02762 221 WLLAAMLAVLLAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 318 GHLAvrHFLN--LVLATGKIGREG---CGYGAITGQGN-GQGGREHGQKADQLPGYRSIENEkdrayvasvwgvdassLP 391
Cdd:cd02762 301 GTLC--SWLVklLNLLTGNLDRPGgamFTTPALDLVGQtSGRTIGRGEWRSRVSGLPEIAGE----------------LP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 392 GKGVSayEMMELIHQGGIKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMEN-EGTLT 470
Cdd:cd02762 363 VNVLA--EEILTDGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKpHATFF 440
|
490 500 510
....*....|....*....|....*....|....*.
gi 1553133439 471 NLE---GRVLLREAGRQAPGEARHDWMILCSLADRL 503
Cdd:cd02762 441 NLEfprNAFRYRRPLFPPPPGTLPEWEILARLVEAL 476
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
76-575 |
1.15e-65 |
|
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: 227.19 E-value: 1.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 76 RLTHPLIRSKGE--LVPCSWDEAFAVASQHMQGILeqygPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRFCM 153
Cdd:cd02767 64 RLTYPMRYDAGSdhYRPISWDEAFAEIAARLRALD----PDRAAFYTSGRASNEAAYLYQLFAR-AYGTNNLPDCSNMCH 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 154 SAAASAGSKTFGIDRGlTFRLADIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDPRK--------------- 218
Cdd:cd02767 139 EPSSVGLKKSIGVGKG-TVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPLRepglerfanpqnpes 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 219 --TATAAMGDMHLPIRPGTDTVLADAMLK--IIMDE---GLIDETFIQARTNGYDELRVYLNSFDLSEAAGICGLELGHI 291
Cdd:cd02767 218 mlTGGTKIADEYFQVRIGGDIALLNGMAKhlIERDDepgNVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEI 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 292 REAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAITGQGNGQGGREHG--QKADQLPgyrs 369
Cdd:cd02767 298 EAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGitEKPFPEF---- 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 370 ieneKDRayVASVWGVDASSLPGKGVSayEMMELIHQGGIKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSET 449
Cdd:cd02767 374 ----LDA--LEEVFGFTPPRDPGLDTV--EAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVATKLNRS 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 450 AQL---ADLVLPVTS--------------YMENEGTLTNL-------EGRVLLREAG------RQAPGEARHDWMILCSL 499
Cdd:cd02767 446 HLVhgeEALILPCLGrteidmqaggaqavTVEDSMSMTHTsrgrlkpASRVLLSEEAivagiaGARLGEAKPEWEILVED 525
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1553133439 500 ADRLgkRhyfrfNEPEEIFNElrlaskgGIADYygitYDRLRREKGVYWPCPSPEetgvgllfqQSFAHPDGKAVF 575
Cdd:cd02767 526 YDRI--R-----DEIAAVIYE-------GFADF----NQRGDQPGGFHLPNGARE---------RKFNTPSGKAQF 574
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
18-533 |
4.00e-65 |
|
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: 227.67 E-value: 4.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 18 TQCPFCSVQCKMTVtEGENGipgqrrAEYKVEGVP-NAASEGRVCVKGMHAHQHAVHSQRLTHPLIRS--KGELVPCSWD 94
Cdd:cd02752 2 TICPYCSVGCGLIA-YVQNG------VWVHQEGDPdHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRApgSGKWEEISWD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 95 EAFAVASQHMQGILEQ------------YGPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRFCMSAAASAGSK 162
Cdd:cd02752 75 EALDEIARKMKDIRDAsfveknaagvvvNRPDSIAFLGSAKLSNEECYLIRKFAR-ALGTNNLDHQARIUHSPTVAGLAN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 163 TFGidRG-LTFRLADIPLARCIVLAGTNIAECQPTLLPYFNQAKE-NGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLA 240
Cdd:cd02752 154 TFG--RGaMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEkNGAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 241 DAMLKiimdeglidetfiqartngydelrvYLNSFDLSEAAGICGLELGHIREAALAYGESD----TGMVLTARGVEQQT 316
Cdd:cd02752 232 GGMIN-------------------------YIIRYTPEEVEDICGVPKEDFLKVAEMFAATGrpdkPGTILYAMGWTQHT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 317 DGHLAVRHFLNLVLATGKIGREGCGYGAITGQGNGQGGREHGQKADQLPGYRSienekdrayvasvwgvdasslpgkgvs 396
Cdd:cd02752 287 VGSQNIRAMCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPGYLG--------------------------- 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 397 ayemmelihqggikslfvmGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLAD-------------LVLPVTSYM 463
Cdd:cd02752 340 -------------------GQNPNSSFPNANKVRRALDKLDWLVVIDPFPTETAAFWKnpgmdpksiqtevFLLPAACQY 400
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 464 ENEGTLTNlEGRVL-LREAGRQAPGEARHDWMILCSLADRLG-----------------KRHYFRFNEPEEIfneLRLAS 525
Cdd:cd02752 401 EKEGSITN-SGRWLqWRYKVVEPPGEAKSDGDILVELAKRLGflyekeggafpepitkwNYGYGDEPTPEEI---AREIN 476
|
....*...
gi 1553133439 526 KGGIADYY 533
Cdd:cd02752 477 GGALTDGY 484
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
20-702 |
2.74e-59 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 214.38 E-value: 2.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 20 CPFCSVQCKMTVTEGENGIpgqrraeYKVEGVPNA-ASEGRVCVKG------MHAHQhavhsqRLTHPLIRSK------- 85
Cdd:PRK13532 47 CRFCGTGCGVLVGTKDGRV-------VATQGDPDApVNRGLNCIKGyflskiMYGKD------RLTQPLLRMKdgkydke 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 86 GELVPCSWDEAFAVASQHMQGILEQYGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAGSKTFG 165
Cdd:PRK13532 114 GEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNIDPNARHCMASAVVGFMRTFG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 166 IDR--GLtfrLADIPLARCIVLAGTNIAECQPTLLPYFNQAK--ENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLAD 241
Cdd:PRK13532 194 IDEpmGC---YDDIEAADAFVLWGSNMAEMHPILWSRVTDRRlsNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILN 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 242 AMLKIIMDEGLIDETFIQARTN--------GY--------------------------DELRVYLNSFDLSEAAGICGLE 287
Cdd:PRK13532 271 YIANYIIQNNAVNWDFVNKHTNfrkgatdiGYglrpthplekaaknpgtagksepisfEEFKKFVAPYTLEKTAKMSGVP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 288 LGHIREAALAYGESDTGMV-LTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAITGQGNGQG-GREHGQKADQLP 365
Cdd:PRK13532 351 KEQLEQLAKLYADPNRKVVsFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGtAREVGTFSHRLP 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 366 GYRSIENEKDRAYVASVWGVDASSLPGK-GVSAYEMMELIHQGGIKSLFVMGSNPIVSNPNAGlvEEGLKKL----DFLM 440
Cdd:PRK13532 431 ADMVVTNPKHREIAEKIWKLPEGTIPPKpGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNIN--EERLPGWrnpdNFIV 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 441 VADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVllrEAGRQ---APGEARHD-WMILcsladRLGKRhyFRFNE--P 514
Cdd:PRK13532 509 VSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRT---QFWRQqvkAPGEAKSDlWQLV-----EFSKR--FKTEEvwP 578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 515 EEIfnelrLASKG--------------GIADYYGIT---------------------------------------YDRLR 541
Cdd:PRK13532 579 EEL-----LAKKPeyrgktlydvlfanGQVDKFPLSelaegylndeakhfgfyvqkglfeeyasfgrghghdlapFDTYH 653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 542 REKGVYWPCPSPEET--------------GVGLLFqqsFAHPDGKAV-FSVTEGDPWKGVSEDYPLILTNGRVLSHYLTG 606
Cdd:PRK13532 654 KVRGLRWPVVDGKETlwryregydpyvkaGEGFKF---YGKPDGKAViFALPYEPPAESPDEEYDLWLSTGRVLEHWHTG 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 607 VQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSfiVRSRIKDQIR----EDTLFVPmhW-GGVQNVNYA 681
Cdd:PRK13532 731 SMTRRVPELYRAFPEAVCFMHPEDAKARGLRRGDEVKVVSRRGE--VKSRVETRGRnkppRGLVFVP--FfDAAQLINKL 806
|
810 820
....*....|....*....|.
gi 1553133439 682 TRPELDPFCKMPGFKTSAVRI 702
Cdd:PRK13532 807 TLDATDPLSKQTDFKKCAVKI 827
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
18-547 |
7.24e-59 |
|
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: 209.39 E-value: 7.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 18 TQCPFCsvQCKMTVTEGEngIPGQRraeykvegvPNAASEGRVCVKGmHAHQHAVHSQ-RLTHPLIR------------- 83
Cdd:cd02751 2 TACHWG--PFKAHVKDGV--IVRVE---------PDDTDQPRPCPRG-RSVRDRVYSPdRIKYPMKRvgwlgngpgsrel 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 84 -SKGELVPCSWDEAFAVASQHMQGILEQYGPDA--NAVYGG---GSLTNETAyLLGKFARVALGtrHIDYNGRFCMSAAA 157
Cdd:cd02751 68 rGEGEFVRISWDEALDLVASELKRIREKYGNEAifGGSYGWasaGRLHHAQS-LLHRFLNLIGG--YLGSYGTYSTGAAQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 158 SAGSKTFGIDRGL--TFRLADIP-LARCIVLAGTNIAECQP--------TLLPYFNQAKENGAKIVVIDPRKTATAA-MG 225
Cdd:cd02751 145 VILPHVVGSDEVYeqGTSWDDIAeHSDLVVLFGANPLKTRQgggggpdhGSYYYLKQAKDAGVRFICIDPRYTDTAAvLA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 226 DMHLPIRPGTDTVLADAMLKIIMDEGLIDETFIQARTNGYDELRVYLnsfdLSE----------AAGICGLELGHIREAA 295
Cdd:cd02751 225 AEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFKDYL----LGEsdgvpktpewAAEITGVPAETIRALA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 296 LAYGESDTgMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAITGQGNGQGGREHGQKADQLP-GYRSIeneK 374
Cdd:cd02751 301 REIASKRT-MIAQGWGLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGAGGPGLPqGKNPV---K 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 375 DRAYVASVWgvDASSLPGKGVSAyeMMELIHQGGIKSLFVMGSNPIVS-NPNAGLVeEGLKKLDFLMVADMFMSETAQLA 453
Cdd:cd02751 377 DSIPVARIA--DALLNPGKEFTA--NGKLKTYPDIKMIYWAGGNPLHHhQDLNRLI-KALRKDETIVVHDIFWTASARYA 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 454 DLVLPVTSYMENE--GTLTNLEGRVLLreAGRQA--P-GEARHDWMILCSLADRLGKRHYFRFNEPE-----EIFNELRL 523
Cdd:cd02751 452 DIVLPATTSLERNdiGLTGNYSNRYLI--AMKQAvePlGEARSDYEIFAELAKRLGVEEEFTEGRDEmewleHLYEETRA 529
|
570 580
....*....|....*....|....
gi 1553133439 524 ASKGGIADYygITYDRLrREKGVY 547
Cdd:cd02751 530 KAAGPGPEL--PSFEEF-WEKGIV 550
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
59-547 |
2.72e-57 |
|
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: 205.25 E-value: 2.72e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 59 RVCVKGMHAHQHAVHSQRLTHPLIR----SKGELVPCSWDEAFAVASQHMQGILEQYGPDANAVYGGGSLTNETAYLLGK 134
Cdd:cd02770 42 RACLRGRSQRKRVYNPDRLKYPMKRvgkrGEGKFVRISWDEALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVPAGRGA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 135 FARV-ALGTRHIDYNGRFCMSAAASAGSKTFGIDrGLTFRLADIPLARCIVLAGTNIAECQPTLLP---YFNQAKENGAK 210
Cdd:cd02770 122 IARLlNLTGGYLNYYGTYSWAQITTATPYTYGAA-ASGSSLDDLKDSKLVVLFGHNPAETRMGGGGstyYYLQAKKAGAK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 211 IVVIDPRKTATAA-MGDMHLPIRPGTDTVLADAMLKIIMDEGLIDETFIQARTNGYDE------------LRVYLnsfdL 277
Cdd:cd02770 201 FIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITENLHDQAFLDRYCVGFDAehlpegappnesYKDYV----L 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 278 SE-----------AAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAit 346
Cdd:cd02770 277 GTgydgtpktpewASEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGA-- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 347 gqgngqggREHGQKAdQLPGYRSIENEKDRAYVASVWgVDAsSLPGKGVSAYEMMeliHQG------GIKSLFVMGSNPI 420
Cdd:cd02770 355 --------RPGGSAY-NGAGLPAGKNPVKTSIPCFMW-TDA-IERGEEMTADDGG---VKGadklksNIKMIWNYAGNTL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 421 VsNPNAGL------VEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTN----LEGRVLLREAGRQAPGEAR 490
Cdd:cd02770 421 I-NQHSDDnnttraLLDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTsnagMMEYLIYSQKAIEPLYECK 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1553133439 491 HDWMILCSLADRLGKRHYF-RFNEPEEIFNElrLASKGGIADYYGITYDRLrREKGVY 547
Cdd:cd02770 500 SDYEICAELAKRLGVEDQFtEGKTEQEWLEE--LYGQTRAKEPGLPTYEEF-REKGIY 554
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
20-528 |
3.44e-56 |
|
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: 198.29 E-value: 3.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 20 CPFCSVQCKMTVtEGENGipgqrRAeYKVEGVP-NAASEGRVCVKGMHAHQHAVHSQRLTHPLIRS----KGELVPCSWD 94
Cdd:cd02755 5 CEMCSSRCGILA-RVEDG-----RV-VKIDGNPlSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVgergEGKFREASWD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 95 EAFAVASQHMQGILEQYGPDAnAVYGGGSLTNETayLLGKFARvALGTRHIDYNGRFCMSAAASAGSKTFGIDRGLTfrL 174
Cdd:cd02755 78 EALQYIASKLKEIKEQHGPES-VLFGGHGGCYSP--FFKHFAA-AFGSPNIFSHESTCLASKNLAWKLVIDSFGGEV--N 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 175 ADIPLARCIVLAGTNIAEC-QPTLLPYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDEGLI 253
Cdd:cd02755 152 PDFENARYIILFGRNLAEAiIVVDARRLMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLY 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 254 DETFIQARTNGYDELRVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLtargveqqtdghlavrhflnlvlatg 333
Cdd:cd02755 232 DAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVV-------------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 334 kigregcgygaITGQgngqggreHGQKADQlpgyrsiENEKDRAYVA-----SVWGVDASSLPGKGVSAYEmmelihqgg 408
Cdd:cd02755 286 -----------DPGW--------RGTFYSN-------SFQTRRAIAIinallGNIDKRGGLYYAGSAKPYP--------- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 409 IKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEG---RVLLREAGRQA 485
Cdd:cd02755 331 IKALFIYRTNPFHSMPDRARLIKALKNLDLVVAIDILPSDTALYADVILPEATYLERDEPFSDKGGpapAVATRQRAIEP 410
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1553133439 486 PGEARHDWMILCSLADRLGkrhyfRFNEPE---EIFNeLRLASKGG 528
Cdd:cd02755 411 LYDTRPGWDILKELARRLG-----LFGTPSgkiELYS-PILAKAGY 450
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
22-575 |
6.53e-53 |
|
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: 191.92 E-value: 6.53e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 22 FCSVQC------KMTVTEGEngipgqrraEYKVE-GVPNAASEGRVCVKGMHAHQHAVHSQRLTHPLIR----SKGELVP 90
Cdd:cd02765 3 ACPPNCggrcplKCHVRDGK---------IVKVEpNEWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRvgerGEGKFER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 91 CSWDEAFAVASQHMQGILEQYGPDANAVYGGGSLTNETAYLLGkfaRVALGTRHIDYNGRFCMSAAASAGSKTFGIDRGL 170
Cdd:cd02765 74 ITWDEALDTIADKLTEAKREYGGKSILWMSSSGDGAILSYLRL---ALLGGGLQDALTYGIDTGVGQGFNRVTGGGFMPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 171 TFRLADIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDE 250
Cdd:cd02765 151 TNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 251 GLIDETFIQARTN--------------------------------------------------------------GYDEL 268
Cdd:cd02765 231 NWYDEAFLKSNTSapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeytingvkvhtVLTAL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 269 RVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGygaitgq 348
Cdd:cd02765 311 REQAASYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGG------- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 349 gngqggreHGQkadqlpgyrsienekdrayvasvwgvdasslpgkgvsayemmelihqggIKSLFVMGSNPIVSNPNAGL 428
Cdd:cd02765 384 --------VGQ-------------------------------------------------IKFMYFMGSNFLGNQPDRDR 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 429 VEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGR--VLLREAGRQAPGEARHDWMILCSLADRLGKR 506
Cdd:cd02765 407 WLKVMKNLDFIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHphVLLQQKAIEPLFESKSDFEIEKGLAERLGLG 486
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1553133439 507 HYfrFNEPEEIFNELRLASKGGIADyyGITYDRLrREKGVYWPCPSPEETGVGLLfQQSFAHPDGKAVF 575
Cdd:cd02765 487 DY--FPKTPEDYVRAFMNSDDPALD--GITWEAL-KEEGIIMRLATPEDPYVAYL-DQKFGTPSGKLEF 549
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
7-675 |
1.95e-52 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 194.12 E-value: 1.95e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 7 AEVTGSAAVIETQCPFCSVQCKMT--VTEGENgipgqrraeYKVEGVPNAAS-EGRVCVKGMHAHQHAVHSQRLTHPLIR 83
Cdd:PRK15488 35 AQLKGKTKLTPSICEMCSTRCPIEarVVNGKN---------VFIQGNPKAKSfGTKVCARGGSGHSLLYDPQRIVKPLKR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 84 S----KGELVPCSWDEAFAVASQHMQGILEQYGPDANAVyggGSLTNETAYLLGKFARvALGTRHIDYNGRFCMSAAASA 159
Cdd:PRK15488 106 VgergEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAF---SSKSGSLSSHLFHLAT-AFGSPNTFTHASTCPAGYAIA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 160 GSKTFGIDRGLtfrlaDIPLARCIV------LAGTNIAECQPtllpYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRP 233
Cdd:PRK15488 182 AKVMFGGKLKR-----DLANSKYIInfghnlYEGINMSDTRG----LMTAQMEKGAKLVVFEPRFSVVASKADEWHAIRP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 234 GTDTVLADAMLKIIMDEGLIDETFIQARTNGYDELRVYLNSFDLSEAAGICGLELGHIREAALAYGES------DTGMVL 307
Cdd:PRK15488 253 GTDLAVVLALCHVLIEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIARELAAAaphaivDFGHRA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 308 TARGVEQQTDGHLAVrhfLNLVLatGKIGREGCGYGAITGQGNGQGGREhgQKADQL-----PGYRSIENEK-DRA---- 377
Cdd:PRK15488 333 TFTPEEFDMRRAIFA---ANVLL--GNIERKGGLYFGKNASVYNKLAGE--KVAPTLakpgvKGMPKPTAKRiDLVgeqf 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 378 -YVASVWGVDASSLPGKgvsayeMMELIHQggIKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLADLV 456
Cdd:PRK15488 406 kYIAAGGGVVQSIIDAT------LTQKPYQ--IKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYLSESAAYADVV 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 457 LPVTSYMENEGTLTNLEGRV---LLREAGRQAPGEARHDWMILCSLADRLGKRHYFrfnePEEIFNELRLASKGGIADYY 533
Cdd:PRK15488 478 LPESTYLERDEEISDKSGKNpayALRQRVVEPIGDTKPSWQIFKELGEKMGLGQYY----PWQDMETLQLYQVNGDHALL 553
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 534 GitydRLRREKGVYWPCP--------------------SPEETGVgLLFQQSFAHPDGK-AVFS--VTEGDPWKGV---- 586
Cdd:PRK15488 554 K----ELKKKGYVSFGVPlllrepkmvakfvarypnakAVDEDGT-YGSQLKFKTPSGKiELFSakLEALAPGYGVpryr 628
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 587 ----SEDYPLILTNGRVLSHylTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIR 662
Cdd:PRK15488 629 dvalKKEDELYFIQGKVAVH--TNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGIR 706
|
730
....*....|...
gi 1553133439 663 EDTLFVPMHWGGV 675
Cdd:PRK15488 707 PDTLFAYMGFGSK 719
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
20-506 |
2.50e-50 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 182.59 E-value: 2.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 20 CPFCSVQCkmtvtegeNGIPGQRRAEYK-VEG-VPNAASEGRVCVKGMHAHQHAVHSQRLTHPLIRSKGELVPCSWDEAF 97
Cdd:cd02771 4 CHHCSVGC--------NISLGERYGELRrVENrYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 98 AVASQhmqgILEQYGpDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRfcMSAAASAgsKTFGIDRGltfRLADI 177
Cdd:cd02771 76 DVAAA----RLKEAK-DKVGGIGSPRASNESNYALQKLVGAVLGTNNVDHRAR--RLIAEIL--RNGPIYIP---SLRDI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 178 PLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDeglIDETF 257
Cdd:cd02771 144 ESADAVLVLGEDLTQTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDD---IAAES 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 258 IQARTNGYDELRVYLNSFDLSEAAGICGLelgHIREAALAYGESDTG--MVLTARGVEQQTDGhlAVRHFLNLVLATGKI 335
Cdd:cd02771 221 IRASPGGQARLGAALARAVDASAAGVSGL---APKEKAARIAARLTGakKPLIVSGTLSGSLE--LIKAAANLAKALKRR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 336 GrEGCGYGAITGQGNgqggrehgqkadqLPGYRSIENEKDRAyvasvwgvdasslpgkGVSAYEMMELIHQGGIKSLFVM 415
Cdd:cd02771 296 G-ENAGLTLAVEEGN-------------SPGLLLLGGHVTEP----------------GLDLDGALAALEDGSADALIVL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 416 GSNPIVSNPNAGlVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRV-LLREAGRQAPGEARHDWM 494
Cdd:cd02771 346 GNDLYRSAPERR-VEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAqRFFKAYDDPAGDARSDWR 424
|
490
....*....|..
gi 1553133439 495 ILCSLADRLGKR 506
Cdd:cd02771 425 WLHALAAKLGGK 436
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
588-703 |
1.50e-45 |
|
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: 158.05 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 588 EDYPLILTNGRVLSHYLTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLF 667
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVF 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1553133439 668 VPMHWGGV---QNVNYATRPELDPFCKMPGFKTSAVRIR 703
Cdd:cd00508 81 MPFHWGGEvsgGAANALTNDALDPVSGQPEFKACAVRIE 119
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
35-586 |
1.52e-39 |
|
Arsenite oxidase (Arsenite-Ox) 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. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 155.33 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 35 ENGIPGQRRAEYKVEGVPNAAS---EGRVCVKG------MHAHQHAVHSQRLTHPLIRSKGELVPCSWDEAFAVASQHMQ 105
Cdd:cd02756 67 HYVVVTQDGREVYIVIVPDKECpvnSGNYSTRGgtnaerIWSPDNRVGETRLTTPLVRRGGQLQPTTWDDAIDLVARVIK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 106 GILEQYGPDANAV-----YGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCMSAAASAGSktfgiDRG---LTFRLADI 177
Cdd:cd02756 147 GILDKDGNDDAVFasrfdHGGGGGGFENNWGVGKFFFMALQTPFVRIHNRPAYNSEVHATR-----EMGvgeLNNSYEDA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 178 PLARCIVLAGTNIAECQPT-----LLPYF--------NQAKENG-----AKIVVIDPRKTATAAMGD--------MHLPI 231
Cdd:cd02756 222 RLADTIVLWGNNPYETQTVyflnhWLPNLrgatvsekQQWFPPGepvppGRIIVVDPRRTETVHAAEaaagkdrvLHLQV 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 232 RPGTDTVLADAMLKIIMDeglidetfiqartnGYDELrvylnsfdLSEAAGICGLELGHIREAALAYGESDTG------M 305
Cdd:cd02756 302 NPGTDTALANAIARYIYE--------------SLDEV--------LAEAEQITGVPRAQIEKAADWIAKPKEGgyrkrvM 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 306 VLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAitgqgngQGGREHGQKADQLPGYRSIENEKDRAYVAsvwgv 385
Cdd:cd02756 360 FEYEKGIIWGNDNYRPIYSLVNLAIITGNIGRPGTGCVR-------QGGHQEGYVRPPPPPPPWYPQYQYAPYID----- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 386 dasslpgkgvsayemmELIHQGGIKSLFVMGSNPIVSNPNAG-----------LV--------------EEGLKKLD--- 437
Cdd:cd02756 428 ----------------QLLISGKGKVLWVIGCDPYKTTPNAQrlretinhrskLVtdaveaalyagtydREAMVCLIgda 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 438 ------FLMVADMFMSETAQLADLVLPVTSYME-NEGTLTNLEGRVLLREAGRQAPGEARHDWMILCSLADRL------- 503
Cdd:cd02756 492 iqpgglFIVVQDIYPTKLAEDAHVILPAAANGEmNETSMNGHERRLRLYEKFMDPPGEAMPDWWIAAMIANRIyelyqee 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 504 -----GKRHYFRFN--EPEEIF----NELRL-------ASKGGIADYYGITYDRLRR--EKGVYWPCPSPEETGVG---- 559
Cdd:cd02756 572 gkggsAQYQFFGFIwkTEEDNFmdgsQEFADggefsedYYVLGQERYEGVTYNRLKAvgVNGIQLPVTTDTVTKILvtnv 651
|
650 660
....*....|....*....|....*..
gi 1553133439 560 LLFQQSFAHPDGKAVFSVTegDPWKGV 586
Cdd:cd02756 652 LRTEGVFDTEDGKAYVIDL--APWPGL 676
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
17-503 |
1.56e-38 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 147.43 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 17 ETQCPFCSVQCKMTVTEGENGIpgqRRAEYKVEGVPNaasEGRVCVKGMHAHQHAVHSQRLTHPLIRSKGELVPCSWDEA 96
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEV---MRILPRENEAIN---EEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVSWEEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 97 FAVASQhmqgILEQYGPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRFcMSAAASAGSKTFGIdrgLTFRLAD 176
Cdd:cd02768 75 LKTVAE----GLKAVKGDKIGGIAGPRADLESLFLLKKLLN-KLGSNNIDHRLRQ-SDLPADNRLRGNYL---FNTSIAE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 177 IPLARCIVLAGTNIAECQPTLlpyfNQ-----AKENGAKIVVIDPRktataamgdmhlpirpgtdtvladamlkiiMDEG 251
Cdd:cd02768 146 IEEADAVLLIGSNLRKEAPLL----NArlrkaVKKKGAKIAVIGPK------------------------------DTDL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 252 LIDETFIqartngydelrVYLNSFDLseAAGICGLELGHIREAALAYGESDTGMVLTARGVeQQTDGHLAVRHFLNLVLA 331
Cdd:cd02768 192 IADLTYP-----------VSPLGASL--ATLLDIAEGKHLKPFAKSLKKAKKPLIILGSSA-LRKDGAAILKALANLAAK 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 332 TGKIGREGCGYGAItgqgngqggrehgqkadQLPGYRSIENEKDRAYVASvwgvdasslpgkgvsayemmeliHQGGIKS 411
Cdd:cd02768 258 LGTGAGLWNGLNVL-----------------NSVGARLGGAGLDAGLALL-----------------------EPGKAKL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 412 LFVMGSNPIVSNPNAGLVeegLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARH 491
Cdd:cd02768 298 LLLGEDELDRSNPPAAVA---LAAADAFVVYQGHHGDTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDARE 374
|
490
....*....|..
gi 1553133439 492 DWMILCSLADRL 503
Cdd:cd02768 375 DWKILRALSNLL 386
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
79-515 |
1.98e-38 |
|
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: 151.26 E-value: 1.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 79 HPLIRSKGELVPCSWDEAFAVASQHMQGILEQYGPDAnaVYGG-------GSLTNETAyLLGKFARVALG-TRHI-DYng 149
Cdd:cd02769 64 DRSLRGKEEFVRVSWDEALDLVAAELKRVRKTYGNEA--IFGGsygwssaGRFHHAQS-LLHRFLNLAGGyVGSVgDY-- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 150 rfcmSAAASA-------GSKTFGIDRGLTFRLAdIPLARCIVLAGTNIAECQPT---------LLPYFNQAKENGAKIVV 213
Cdd:cd02769 139 ----STGAAQvilphvvGSMEVYTEQQTSWPVI-AEHTELVVAFGADPLKNAQIawggipdhqAYSYLKALKDRGIRFIS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 214 IDPRKTATAAMGDM-HLPIRPGTDTVLADAMLKIIMDEGLIDETFIQARTNGYDELRVYLnsfdLSE----------AAG 282
Cdd:cd02769 214 ISPLRDDTAAELGAeWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYL----LGEsdgvpktpewAAA 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 283 ICGLELGHIREAALAYGESDTgMVLTARGVEQQTDGHLAvrHFLNLVLAT--GKIGREGCGYGAITGQGNGQGGREHGQK 360
Cdd:cd02769 290 ICGIPAETIRELARRFASKRT-MIMAGWSLQRAHHGEQP--HWMAVTLAAmlGQIGLPGGGFGFGYHYSNGGGPPRGAAP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 361 ADQLP-GYRSIeneKDRAYVASVwgVDASSLPGKgvsayemmELIHQGG------IKSLFVMGSNPIVSNPNAGLVEEGL 433
Cdd:cd02769 367 PPALPqGRNPV---SSFIPVARI--ADMLLNPGK--------PFDYNGKkltypdIKLVYWAGGNPFHHHQDLNRLIRAW 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 434 KKLDFLMVADMFMSETAQLADLVLPVTSYME-NEGTLTNLEGRVLlreAGRQA--P-GEARHDWMILCSLADRLGKRHYF 509
Cdd:cd02769 434 QKPETVIVHEPFWTATARHADIVLPATTSLErNDIGGSGDNRYIV---AMKQVvePvGEARDDYDIFADLAERLGVEEQF 510
|
....*.
gi 1553133439 510 RFNEPE 515
Cdd:cd02769 511 TEGRDE 516
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
49-509 |
4.67e-37 |
|
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: 144.77 E-value: 4.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 49 EGVPNAasEGRVCVKGMHAHQHAVHSQRLTHPLIRS----KGELVPCSWDEAFAVASQHMQGILEQYGPDANAVYGGGSL 124
Cdd:cd02750 41 PDLPDY--NPRGCQRGASFSWYLYSPDRVKYPLKRVgargEGKWKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 125 TNETAYllgkfarvALGTRHIDYNGRFCMSAAA------SAGSKTFGiDRGLTFRLADIPLARCIVLAGTNIAECQPTLL 198
Cdd:cd02750 119 MSMVSY--------AAGSRFASLIGGVSLSFYDwygdlpPGSPQTWG-EQTDVPESADWYNADYIIMWGSNVPVTRTPDA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 199 PYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDEGLIDETFIQARTNgyDELRVYlnsfDLS 278
Cdd:cd02750 190 HFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYTD--LPFLVY----TPA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 279 EAAGICGLELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGRegcgygaitgqgngqggrehg 358
Cdd:cd02750 264 WQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGK--------------------- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 359 qkadqlpgyrsienekdrayvasvwgvdasslPGKGVSAYEmmelihqGGIKSLFVMGSNPIVSNPNAGLVEEG--LKKL 436
Cdd:cd02750 323 --------------------------------NGGGWAHYV-------GQPRVLFVWRGNLFGSSGKGHEYFEDapEGKL 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 437 DFLMVADMFMSETAQLADLVLP-VTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDWMILCSLADRL------GKRHYF 509
Cdd:cd02750 364 DLIVDLDFRMDSTALYSDIVLPaATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKVpwrtltGRQQFY 443
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
588-703 |
7.22e-37 |
|
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: 133.90 E-value: 7.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 588 EDYPLILTNGRVLSHYLTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLF 667
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVF 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1553133439 668 VPMHWgGVQNVNYATRPELDPFCKMPGFKTSAVRIR 703
Cdd:cd02790 81 MPFHF-AEAAANLLTNAALDPVAKIPEFKVCAVRVE 115
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
16-516 |
3.30e-35 |
|
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: 140.27 E-value: 3.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 16 IETQCPFCSVQCkmtvtegenGIPGQRRAE--YKVEGVPNA-ASEGRVCVKGMHAHQHAVHSQRLTHPLIRS-------- 84
Cdd:cd02757 2 VPSTCQGCTAWC---------GLQAYVEDGrvTKVEGNPLHpGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnprkgrdv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 85 KGELVPCSWDEAFAVASQHMQGILEQYGPDANAV-YGGGSLTNETAYllGKFARvALGTRHIDYNGRFCMSAAASAGSKT 163
Cdd:cd02757 73 DPKFVPISWDEALDTIADKIRALRKENEPHKIMLhRGRYGHNNSILY--GRFTK-MIGSPNNISHSSVCAESEKFGRYYT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 164 fgiDRGLTFRLADIPLARCIVLAGTNIAECQpTLLPYFNQ---AKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLA 240
Cdd:cd02757 150 ---EGGWDYNSYDYANAKYILFFGADPLESN-RQNPHAQRiwgGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 241 DAMLKIIMDEGLIDETFIQARTNGYDELR----VYLNSF------DLSE-------------AAGICGLELGHIREAALA 297
Cdd:cd02757 226 LAIAHVILTEGLWDKDFVGDFVDGKNYFKagetVDEESFkeksteGLVKwwnlelkdytpewAAKISGIPAETIERVARE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 298 YGESDT-GMVLTARGVEQQTDGHLAVR--HFLNLVlaTGKIGREGcgyGAITGQGNGQggrehgqkadqlpgyrsienek 374
Cdd:cd02757 306 FATAAPaAAAFTWRGATMQNRGSYNSMacHALNGL--VGSIDSKG---GLCPNMGVPK---------------------- 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 375 drayvasvwgvdasslpgkgvsayemmelihqggIKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLAD 454
Cdd:cd02757 359 ----------------------------------IKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTYFAD 404
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1553133439 455 LVLPVTSYMENEGTL---TNLEGRVLLREAGRQAPGEARHDWMILCSLADRLG-------KRHYF-RFNEPEE 516
Cdd:cd02757 405 IVLPDGHHFERWDVMsqeNNLHPWLSIRQPVVKSLGEVREETEILIELAKKLDpkgsdgmKRYAPgQFKDPET 477
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
588-703 |
9.05e-33 |
|
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: 122.68 E-value: 9.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 588 EDYPLILTNGRVLSHYLTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLF 667
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1553133439 668 VPMHWGGVQN----VNYATRPELDPFCKMPGFKTSAVRIR 703
Cdd:cd02791 81 VPMHWGDQFGrsgrVNALTLDATDPVSGQPEFKHCAVRIE 120
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
588-703 |
4.88e-32 |
|
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: 120.41 E-value: 4.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 588 EDYPLILTNGRVLSHYLTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLF 667
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1553133439 668 VPMHWGGV-----QNVNYATRPELDPFCKMPGFKTSAVRIR 703
Cdd:cd02792 81 IPYHWGGMglvigDSANTLTPYVGDPNTQTPEYKAFLVNIE 121
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
592-699 |
6.04e-31 |
|
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: 116.99 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 592 LILTNGRVLSHYLTGVQTRRSPTLLARElENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLFVPMH 671
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPE-PEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|.
gi 1553133439 672 WGGV---QNVNYATRPELDPFCKMPGFKTSA 699
Cdd:pfam01568 80 WWYEprgGNANALTDDATDPLSGGPEFKTCA 110
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
61-676 |
2.48e-29 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 124.67 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 61 CVKGMHAHQHAVHSQRLTHPLIR-SKGELVPCSWDEAFAVASQHMQGILEQYGpdanaVYGGGSLTNETAYLLGKFARVA 139
Cdd:PRK07860 263 CDKGRWAFTYATQPDRITTPLVRdEDGELEPASWSEALAVAARGLAAARGRVG-----VLVGGRLTVEDAYAYAKFARVA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 140 LGTRHIDYNGRfcmsaAASAGSKTF------GIDRGLTFrlADIPLARCIVLAGTNIAECQPTL-LPYFNQAKENGAKIV 212
Cdd:PRK07860 338 LGTNDIDFRAR-----PHSAEEADFlaarvaGRGLGVTY--ADLEKAPAVLLVGFEPEEESPIVfLRLRKAARKHGLKVY 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 213 VIDPRKT-ATAAMGDMHLPIRPGTDTVLADAMLK--IIMDEGLidetfiqaRTNGydelRVYLNSFDLSEAAGicglelg 289
Cdd:PRK07860 411 SIAPFATrGLEKMGGTLLRTAPGGEAAALDALATgaPDVAELL--------RTPG----AVILVGERLATVPG------- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 290 hireaalaygesdtgmVLTArgveqqtdghlAVRhflnLVLATGK----IGREGCGYGAItgqgngqggrEHGQKADQLP 365
Cdd:PRK07860 472 ----------------ALSA-----------AAR----LADATGArlawVPRRAGERGAL----------EAGALPTLLP 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 366 GYRSIENEKDRAYVASVWGVDasSLPGK-GVSAYEMMELIHQGGIKSLFVMGSNPI-VSNPNAglVEEGLKKLDFLMVAD 443
Cdd:PRK07860 511 GGRPVADPAARAEVAAAWGVD--ELPAApGRDTAGILAAAAAGELGALLVGGVEPAdLPDPAA--ALAALDAAGFVVSLE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 444 MFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGeARHDWMILCSLADRLGKRhyFRFNEPEEIFNELrl 523
Cdd:PRK07860 587 LRHSAVTERADVVLPVAPVAEKAGTFLNWEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVD--LGLPTVAAARAEL-- 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 524 askggiadyygityDRLRREKGVYWPCPSPEETGVgllfqqsfAHPD-GKAVFSVtegdpWKgvsedypLILTNGRVL-- 600
Cdd:PRK07860 662 --------------ARLGAWDGARAAAPAVPAAAP--------PQPGaGEAVLAT-----WR-------MLLDDGRLQdg 707
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1553133439 601 SHYLTGvqTRRSPTllarelenfAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDqIREDTLFVPMHWGGVQ 676
Cdd:PRK07860 708 EPHLAG--TARPPV---------ARLSAATAAEIGVADGDAVTVSTERGSITLPLAITD-MPDRVVWLPLNSPGST 771
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
10-657 |
3.32e-28 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 120.90 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 10 TGSAAVIETQCPF-CSVQC--KMTVTEGE-NGIPGQRRAEYKVEGVpnaaSEGRVCVKGMHAHQHAVHSQRLTHPL---- 81
Cdd:PRK14990 53 KSDEKVIWSACTVnCGSRCplRMHVVDGEiKYVETDNTGDDNYDGL----HQVRACLRGRSMRRRVYNPDRLKYPMkrvg 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 82 IRSKGELVPCSWDEAFAVASQHMQGILEQYGPDANAV-YG----GGSLTNE---TAYLLGKFARVALGtrHIDYNGRFCM 153
Cdd:PRK14990 129 ARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLnYGtgtlGGTMTRSwppGNTLVARLMNCCGG--YLNHYGDYSS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 154 SAAASAGSKTFG--IDRGLTfrlADIPLARCIVLAGTNIAECQPT---LLPYFNQAKE-NGAKIVVIDPRKTATAA-MGD 226
Cdd:PRK14990 207 AQIAEGLNYTYGgwADGNSP---SDIENSKLVVLFGNNPGETRMSgggVTYYLEQARQkSNARMIIIDPRYTDTGAgRED 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 227 MHLPIRPGTDTVLADAMLKIIMDEGLIDETFIQARTNGYDELRV--------YLNSFDLSE-----------AAGICGLE 287
Cdd:PRK14990 284 EWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYCVGYDEKTLpasapkngHYKAYILGEgpdgvaktpewASQITGVP 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 288 LGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGcgygaitgqGNgQGGREHGQKadqLPGY 367
Cdd:PRK14990 364 ADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGING---------GN-SGAREGSYS---LPFV 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 368 R--SIENEKDRAYVASVW------GVDASSLPgKGVSAYEMMELihqgGIKSLFVMGSNPIVS-----NPNAGLVEEGlK 434
Cdd:PRK14990 431 RmpTLENPIQTSISMFMWtdaierGPEMTALR-DGVRGKDKLDV----PIKMIWNYAGNCLINqhseiNRTHEILQDD-K 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 435 KLDFLMVADMFMSETAQLADLVLPVTSYMEN-----EGTLTNLEgRVLLREAGRQAPGEARHDWMILCSLADRLGKRHYF 509
Cdd:PRK14990 505 KCELIVVIDCHMTSSAKYADILLPDCTASEQmdfalDASCGNMS-YVIFNDQVIKPRFECKTIYEMTSELAKRLGVEQQF 583
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 510 -RFNEPEEIFNELRLASKGGIADYygITYDRLRREkGVYW-----------------PCPSPEETGVGLLFQQSFAHPDG 571
Cdd:PRK14990 584 tEGRTQEEWMRHLYAQSREAIPEL--PTFEEFRKQ-GIFKkrdpqghhvaykafredPQANPLTTPSGKIEIYSQALADI 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 572 KAVFSVTEG---DPW-----------KGVSEDYPLILTNgrvlSHYLTGVQ-TRRSPTLLARELENFAEIHPNTAQRYRI 636
Cdd:PRK14990 661 AATWELPEGdviDPLpiytpgfesyqDPLNKQYPLQLTG----FHYKSRVHsTYGNVDVLKAACRQEMWINPLDAQKRGI 736
|
730 740
....*....|....*....|.
gi 1553133439 637 QDGEWVEILSEHGSFIVRSRI 657
Cdd:PRK14990 737 NNGDKVRIFNDRGEVHIEAKV 757
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
73-496 |
1.09e-27 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 116.30 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 73 HSQRLTHPLIRSKGELVPCSWDEAFAVASQHMQGILEQYGPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRfc 152
Cdd:cd02772 51 SEDRLTKPMIKKDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLAR-GLGSDNIDHRLR-- 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 153 mSAAASAGSKtFGIDRGLTFRLADIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDPrktataAMGDMHLPIr 232
Cdd:cd02772 128 -QSDFRDDAK-ASGAPWLGMPIAEISELDRVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINP------ADDDFLFPL- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 233 PGTDTVLADAMLKIIMDEglidetfiqartngydelrvylnsfdLSEAAGICGLELGHIREAALAYGEsdtgmvltARGV 312
Cdd:cd02772 199 SGKAIVAPSALANALAQV--------------------------AKALAEEKGLAVPDEDAKVEASEE--------ARKI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 313 EQQTDGHLAVRHFL-NLVLATGKIGREGCGYGAITGQGNGQGGReHGQKADqlpgyrsienekdrayvaSVWGVDASSLP 391
Cdd:cd02772 245 AASLVSAERAAVFLgNLAQNHPQAATLRALAQEIAKLTGATLGV-LGEGAN------------------SVGAYLAGALP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 392 GKGVSAYEMMELihqgGIKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQ-LADLVLPVTSYMENEGTLT 470
Cdd:cd02772 306 HGGLNAAAMLEQ----PRKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALLdYADVLLPIAPFTETSGTFV 381
|
410 420
....*....|....*....|....*.
gi 1553133439 471 NLEGRVLLREAGRQAPGEARHDWMIL 496
Cdd:cd02772 382 NLEGRVQSFKGVVKPLGEARPAWKVL 407
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
396-521 |
1.44e-27 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 116.48 E-value: 1.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 396 SAYEMMELIHQGGIKSLFVMGSNPIVSNPNAglVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLEGR 475
Cdd:COG1034 320 DAAAILEAAEAGKLKALVLLGADPYDLDPAA--ALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGR 397
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1553133439 476 VLLREAGRQAPGEARHDWMILCSLADRLGkrHYFRFNEPEEIFNEL 521
Cdd:COG1034 398 VQRFNAAVPPPGEARPDWRVLRALANALG--AGLPYDSLEEVRAEL 441
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
76-702 |
5.26e-27 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 117.07 E-value: 5.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 76 RLTHPLIRSKGE--LVPCSWDEAFAVASQHMQGILEqygPDANAVYGGGSLTNETAYLLGKFARvALGTRHIDYNGRFCM 153
Cdd:PRK09939 108 RLTQPLKYDAVSdcYKPLSWQQAFDEIGARLQSYSD---PNQVEFYTSGRTSNEAAFLYQLFAR-EYGSNNFPDCSNMCH 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 154 SAAASAGSKTFGIDRGlTFRLADIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDP-------RKTA------ 220
Cdd:PRK09939 184 EPTSVGLAASIGVGKG-TVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPlqergleRFTApqnpfe 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 221 -----TAAMGDMHLPIRPGTDTVLADAMLKIIMDE----------GLIDETFIQARTNGYDELRVYLNSFDLSEAAGICG 285
Cdd:PRK09939 263 mltnsETQLASAYYNVRIGGDMALLKGMMRLLIERddaasaagrpSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISG 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 286 LELGHIREAALAYGESDTGMVLTARGVEQQTDGHLAVRHFLNLVLATGKIGREGCGYGAITGQGNGQGGREHGqkADQLP 365
Cdd:PRK09939 343 LSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVG--ITEKP 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 366 GYRSIenekdrAYVASVWGVDASSLPGKgvSAYEMMELIHQGGIKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMF 445
Cdd:PRK09939 421 SAEFL------ARLGERYGFTPPHAPGH--AAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATK 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 446 MSETAQLA---DLVLPVTSYMEnegtltnlegrVLLREAGRQApgearhdwmilCSLADRLGKRHYFR-FNEPEEIFNEL 521
Cdd:PRK09939 493 LNRSHLLTarhSYILPVLGRSE-----------IDMQKSGAQA-----------VTVEDSMSMIHASRgVLKPAGVMLKS 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 522 RLASKGGIA-----------DYYGITYDRLRREKGVYWPCPSP------EETGVGLL---FQQSFAHPDGKAVFSVTEG- 580
Cdd:PRK09939 551 ECAVVAGIAqaalpqsvvawEYLVEDYDRIRNDIEAVLPEFADynqrirHPGGFHLInaaAERRWMTPSGKANFITSKGl 630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 581 --DPWKGVSEDypLILTNGRVLSHY---LTGVQTRRSPTLLARELenfAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRS 655
Cdd:PRK09939 631 leDPSSAFNSK--LVMATVRSHDQYnttIYGMDDRYRGVFGQRDV---VFMSAKQAKICRVKNGERVNLIALTPDGKRSS 705
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1553133439 656 RIKDQIRedTLFVPMHWGGV-----QNVNYATRPELDPFCKMPGFKTSAVRI 702
Cdd:PRK09939 706 RRMDRLK--VVIYPMADRSLvtyfpESNHMLTLDNHDPLSGIPGYKSIPVEL 755
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
599-696 |
2.38e-23 |
|
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: 95.08 E-value: 2.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 599 VLSHYLTGVQTRrSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLFVPMHWGGV--- 675
Cdd:cd02775 1 LRDHFHSGTRTR-NPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRggr 79
|
90 100
....*....|....*....|..
gi 1553133439 676 -QNVNYATRPELDPFCKMPGFK 696
Cdd:cd02775 80 gGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
58-586 |
2.18e-22 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 102.42 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 58 GRVCVKGMHAHQHAVHSQRLTHPLIR----SKGELVPCSWDEAF-AVASQ-------HMQG----------ILEQ---YG 112
Cdd:cd02758 65 ATACARGNAGLQYLYDPYRVLQPLKRvgprGSGKWKPISWEQLIeEVVEGgdlfgegHVEGlkairdldtpIDPDhpdLG 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 113 PDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFC---MSAAASAGSKTFGidrGLTFRLADIPLARCIVLAGTN 189
Cdd:cd02758 145 PKANQLLYTFGRDEGRTPFIKRFANQAFGTVNFGGHGSYCglsYRAGNGALMNDLD---GYPHVKPDFDNAEFALFIGTS 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 190 IAECQPtllPYFNQAK-------ENGAKIVVIDPRKTATA-AMGDMH--LPIRPGTDTVLADAMLKIIMDEGLIDETFIQ 259
Cdd:cd02758 222 PAQAGN---PFKRQARrlaeartEGNFKYVVVDPVLPNTTsAAGENIrwVPIKPGGDGALAMAMIRWIIENERYNAEYLS 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 260 ------ARTNGYDE-------------------LRVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTARGVEQ 314
Cdd:cd02758 299 ipskeaAKAAGEPSwtnathlvitvrvksalqlLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTM 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 315 QTDGHLAVRHFLNLVLATGKIGREGcgyGAITGQG----NGQGGR------------------EHGQKADQLPGYRSIEN 372
Cdd:cd02758 379 HSNGFYNAYAIRMLNALIGNLNWKG---GLLMSGGgfadNSAGPRydfkkffgevkpwgvpidRSKKAYEKTSEYKRKVA 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 373 EKDRAYVA-SVWgvdassLPGKGVSAYEMMELIHQG---GIKSLFVMGSNPIVSNPnaGL---VEEGLK---KLDFLMVA 442
Cdd:cd02758 456 AGENPYPAkRPW------YPLTPELYTEVIASAAEGypyKLKALILWMANPVYGAP--GLvkqVEEKLKdpkKLPLFIAI 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 443 DMFMSETAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQ----------APGEARHDWMILCSLADRLG-------- 504
Cdd:cd02758 528 DAFINETSAYADYIVPDTTYYESWGFSTPWGGVPTKASTARWpviapltektANGHPVSMESFLIDLAKALGlpgfgpna 607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 505 ----KRHYFRFNEPEEIFneLRLASKggiadyygITYDrlrREKGVywPCPSPEETgvgLLFQQSFAHPdgkAVFSVTEG 580
Cdd:cd02758 608 ikdgQGNKFPLNRAEDYY--LRVAAN--------IAYD---GKAPV--PDASEEEL---KLTGVNRPIP---ALKRTLKP 666
|
....*.
gi 1553133439 581 DPWKGV 586
Cdd:cd02758 667 EEWRKV 672
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
18-473 |
1.29e-19 |
|
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: 93.36 E-value: 1.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 18 TQCPFCSVQCKMTV--TEGEngipgqrrAEYkVEGVPN-AASEGRVCVKGMHAHQHAVHSQRLTHPLIRS----KGELVP 90
Cdd:cd02763 2 TTCYMCACRCGIRVhlRDGK--------VRY-IKGNPDhPLNKGVICAKGSSGIMKQYSPARLTKPLLRKgprgSGQFEE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 91 CSWDEAFAVASQHMqGILEQYGPDANAVYGGgslTNETAYLLGKFARvALGTRHIDYNGRFCMSAAASAGSKTFGiDRGL 170
Cdd:cd02763 73 IEWEEAFSIATKRL-KAARATDPKKFAFFTG---RDQMQALTGWFAG-QFGTPNYAAHGGFCSVNMAAGGLYSIG-GSFW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 171 TFRLADIPLARCIVLAGTNIAECQPTLLPYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDE 250
Cdd:cd02763 147 EFGGPDLEHTKYFMMIGVAEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 251 GLIDETFIQARTNGYdelrvYLNSFDLSEAAGICGL----------ELGHI-REAAL--------AYGESDTGMV----- 306
Cdd:cd02763 227 GLIDWEFLKRYTNAA-----ELVDYTPEWVEKITGIpadtirriakELGVTaRDQPIelpiawtdVWGRKHEKITgrpvs 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 307 -LTARGVEQQTDGHLAVRHFLNLVLATGKIGREG--------------CGYGAITGQGNGQGGREHG------QKADQLp 365
Cdd:cd02763 302 fHAMRGIAAHSNGFQTIRALFVLMMLLGTIDRPGgfrhkppyprhippLPKPPKIPSADKPFTPLYGpplgwpASPDDL- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 366 gyrSIENEK-----DRAYV----ASVWGVDASSLPgkgvSAYE---------MMELIHQGGIKSLFVMGSNPIVSNPNag 427
Cdd:cd02763 381 ---LVDEDGnplriDKAYSweypLAAHGCMQNVIT----NAWRgdpypidtlMIYMANMAWNSSMNTPEVREMLTDKD-- 451
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1553133439 428 lvEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEGTLTNLE 473
Cdd:cd02763 452 --ASGNYKIPFIIVCDAFYSEMVAFADLVLPDTTYLERHDAMSLLD 495
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
20-478 |
2.17e-17 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 85.08 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 20 CPFCSVQCK-MTVTEGENGIPGQRRAeykvegvpnaasegrvCVKGMHAHQHAVHsqRLTHPLIRSKgelvPCSWDEAFA 98
Cdd:cd02761 4 CPFCGLLCDdIEVEVEDNKITKVRNA----------------CRIGAAKFARYER--RITTPRIDGK----PVSLEEAIE 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 99 VASQHMQgilEQYGPdanAVYGGGSLTNE---TAYLLGKfarvALGTrHIDYNGRFCMSAAASAGsktfgIDRGLTF-RL 174
Cdd:cd02761 62 KAAEILK---EAKRP---LFYGLGTTVCEaqrAGIELAE----KLGA-IIDHAASVCHGPNLLAL-----QDSGWPTtTL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 175 ADIP-LARCIVLAGTNIAECQPTLL--------PYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLK 245
Cdd:cd02761 126 GEVKnRADVIVYWGTNPMHAHPRHMsrysvfprGFFREGGREDRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 246 IIMDEGLIDETfiqaRTNGYDElrvylnsfDLSEAAGIcgleLGHIREAALAYGesdtgmvltaRGVEQQTDGHLAVRHF 325
Cdd:cd02761 206 LLRGAGLVPDE----VAGIPAE--------TILELAER----LKNAKFGVIFWG----------LGLLPSRGAHRNIEAA 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 326 LNLVLATGKIGREGCgyGAITGQGNGQGgreHGQKADQLPGYrsienekdrayvasVWGVDASSLPGKGvSAYEMM--EL 403
Cdd:cd02761 260 IRLVKALNEYTKFAL--LPLRGHYNVRG---FNQVLTWLTGY--------------PFRVDFSRGYPRY-NPGEFTavDL 319
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1553133439 404 IHQGGIKSLFVMGSNPivSNPNAGLVEEGLKKLDfLMVADMFMSETAQLADLVLPV-TSYMENEGTLTNLEGRVLL 478
Cdd:cd02761 320 LAEGEADALLIIASDP--PAHFPQSAVKHLAEIP-VIVIDPPPTPTTRVADVVIPVaIPGIEAGGTAYRMDGVVVL 392
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
18-263 |
1.60e-15 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 80.40 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 18 TQCPFCSVQCKMTVTEGENGIPGQRRAEYKVEGVPNAasEGRVCVKGMHAHQHAVHSQRLTHPLIRS---KGE-----LV 89
Cdd:cd02760 2 TYCYNCVAGPDFMAVKVVDGVATEIEPNFAAEDIHPA--RGRVCVKAYGLVQKTYNPNRVLQPMKRTnpkKGRnedpgFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 90 PCSWDEAFAVASQHMQGILE------QYGPDANAVYGGGSLTNETAYLLGKFArVALGTrhIDYN----GRFCMSAAASA 159
Cdd:cd02760 80 PISWDEALDLVAAKLRRVREkglldeKGLPRLAATFGHGGTPAMYMGTFPAFL-AAWGP--IDFSfgsgQGVKCVHSEHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 160 GSKTFgiDRGLTFrLADIPLARCIVLAGTNI-AECQPTLLPYFNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTV 238
Cdd:cd02760 157 YGEFW--HRAFTV-AADTPLANYVISFGSNVeASGGPCAVTRHADARVRGYKRVQVEPHLSVTGACSAEWVPIRPKTDPA 233
|
250 260
....*....|....*....|....*...
gi 1553133439 239 LADAMLKIIMDE---GLIDETFIQARTN 263
Cdd:cd02760 234 FMFAMIHVMVHEqglGKLDVPFLRDRTS 261
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
58-503 |
4.31e-15 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 77.69 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 58 GRVCVKGMHahqhavhSQRLTHPLIRSKGELVPCSWDEAFAVASQHMQGIleqyGPDANAVYGGGSLTNETAYLLGKFAR 137
Cdd:cd02773 42 TRFAYDGLK-------RQRLDKPYIRKNGKLKPATWEEALAAIAKALKGV----KPDEIAAIAGDLADVESMVALKDLLN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 138 vALGTRHIDYNGRFCMSAAASAGSKTFGIdrgltfRLADIPLARCIVLAGTNIA-ECqptllPYFN-----QAKENGAKI 211
Cdd:cd02773 111 -KLGSENLACEQDGPDLPADLRSNYLFNT------TIAGIEEADAVLLVGTNPRfEA-----PVLNarirkAWLHGGLKV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 212 VVIDPRKTATAAMGdmHLpirpGTDtvlADAMLKIIMDEGLIDETFIQARTNgydelrvylnsfdlseaagicglelghi 291
Cdd:cd02773 179 GVIGPPVDLTYDYD--HL----GTD---AKTLQDIASGKHPFSKALKDAKKP---------------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 292 reaalaygesdtgMVLTARGVEQQTDGhlavrhflNLVLATgkIGREGCGYGAITGQGNGQggrehgqkadqlpgyrsie 371
Cdd:cd02773 222 -------------MIIVGSGALARKDG--------AAILAA--VAKLAKKNGVVREGWNGF------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 372 NEKDRAyVASVWGVDASSLPGKGvsayemmELIHQGGIKSLFVMGS---NPIVSNPNAGLVEEGLKkldflmvADMfmse 448
Cdd:cd02773 260 NVLHRA-ASRVGALDLGFVPGAG-------AIRKSGPPKVLYLLGAdeiDITPIPKDAFVVYQGHH-------GDR---- 320
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1553133439 449 TAQLADLVLPVTSYMENEGTLTNLEGRVLLREAGRQAPGEARHDWMILCSLADRL 503
Cdd:cd02773 321 GAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
16-237 |
2.79e-14 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 75.65 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 16 IETQCPFCSVQCKMTVtegengipGQRRAE-YKVEGVPNAA-SEGRVCVKGMHAHQHAVHSQRLTHPLIRSKGELVPCSW 93
Cdd:COG1034 218 TPSICPHCSVGCNIRV--------DVRGGKvYRVLPRENEAvNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELVEASW 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 94 DEAFAVASQhmqgILEQYGPDANAVyGggsltnetAYLLGKFARVAlgtrhidyngrfCMSAAASAGSktfgidrgltfr 173
Cdd:COG1034 290 EEALAAAAE----GLKALKKAENSV-G--------AALLGALPDAA------------AILEAAEAGK------------ 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1553133439 174 ladiplARCIVLAGTNIAECQPTLLpyfNQAKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDT 237
Cdd:COG1034 333 ------LKALVLLGADPYDLDPAAA---LAALAKADFVVVLDHFGSATAERADVVLPAAAFAEK 387
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
589-676 |
2.09e-13 |
|
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: 67.72 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 589 DYPLILTNG-RVLSHylTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLF 667
Cdd:cd02781 1 EYPLILTTGaRSYYY--FHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVR 78
|
90
....*....|
gi 1553133439 668 VPM-HWGGVQ 676
Cdd:cd02781 79 AEHgWWYPER 88
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
591-673 |
6.88e-13 |
|
The MopB_CT_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. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 65.76 E-value: 6.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 591 PLILTNGRVLSHylTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLFVPM 670
Cdd:cd02778 1 EFRLIYGKSPVH--THGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPH 78
|
...
gi 1553133439 671 HWG 673
Cdd:cd02778 79 GFG 81
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
200-527 |
2.69e-11 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 67.00 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 200 YFNQAKENGAK----IVVIDPRKTATAA-MGDMHLPIRPGTDTVLADAMLKIIMDEGLIDETFIQARTNGYDELRVYLns 274
Cdd:PRK15102 242 YLAQLKEKVAKgeinVISIDPVVTKTQNyLGCEHLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFLPYL-- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 275 fdLSE----------AAGICGLELGHIREAALAYGESDTGMVLtarGVEQQTDGHLAVRHFLNLVLAT--GKIGREGCGY 342
Cdd:PRK15102 320 --LGEkdgvpktpewAEKICGIDAETIRELARQMAKGRTQIIA---GWCIQRQQHGEQPYWMGAVLAAmlGQIGLPGGGI 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 343 ---------GAITGQGNGQGGREHGQKADQLPGYrsiENEKDRAYVASV----WgVDASSLPGKgvsayemmELIHQGG- 408
Cdd:PRK15102 395 syghhysgiGVPSSGGAIPGGFPGNLDTGQKPKH---DNSDYKGYSSTIpvarF-IDAILEPGK--------TINWNGKk 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 409 -----IKSLFVMGSNPIVSNPNAGLVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYME-NE----GTLTNlegRVLL 478
Cdd:PRK15102 463 vtlppLKMMIFSGTNPWHRHQDRNRMKEAFRKLETVVAIDNQWTATCRFADIVLPACTQFErNDidqyGSYSN---RGII 539
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1553133439 479 REAGRQAP-GEARHDWMILCSLADRLGKRHYF--RFNEPE---EIFNELRLASKG 527
Cdd:PRK15102 540 AMKKVVEPlFESRSDFDIFRELCRRFGREKEYtrGMDEMGwlkRLYQECKQQNKG 594
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
15-70 |
2.49e-10 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 56.15 E-value: 2.49e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1553133439 15 VIETQCPFCSVQCKMTVTEGENGIpgqrraeYKVEGVPNA-ASEGRVCVKGMHAHQH 70
Cdd:pfam04879 3 VVKTICPYCGVGCGLEVHVKDGKI-------VKVEGDPDHpVNEGRLCVKGRFGYER 52
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
47-467 |
5.45e-09 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 59.04 E-value: 5.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 47 KVEGVP-NAASEGrvcvkGMHAH-QHAVHS----QRLTHPLIRS-KGELVPCSWDEAFA-VASQHMQGileqYGPDANAV 118
Cdd:cd02764 69 KIEGNPdHPASLG-----GTSARaQASVLSlydpDRAQGPLRRGiDGAYVASDWADFDAkVAEQLKAV----KDGGKLAV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 119 YGGGSLTNETAYLLGKFARVALGTRHIDYNGrfcMSA--AASAGSKTFGIDRGLTFrlaDIPLARCIVLAGTNIAECQPT 196
Cdd:cd02764 140 LSGNVNSPTTEALIGDFLKKYPGAKHVVYDP---LSAedVNEAWQASFGKDVVPGY---DFDKAEVIVSIDADFLGSWIS 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 197 LLPYFNQ--------AKENGAKIVVIDPRKTATAAMGDMHLPIRPGTDTVLADAMLKIIMDEGlidetfiqARTNGYDEL 268
Cdd:cd02764 214 AIRHRHDfaakrrlgAEEPMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIKKG--------AGSSLPDFF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 269 RVYLNSFDLSEAAGICGLELGHIREAALAYGESDTGMVLTargveqqtdghlavrhflnlvlatgkigregcgyGAITGQ 348
Cdd:cd02764 286 RALNLAFKPAKVAELTVDLDKALAALAKALAAAGKSLVVA----------------------------------GSELSQ 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 349 GNGqggrehgqKADQLPGYRSieNEKDRAYVASVwGVDASSLPGKGVSAYEMMEL---IHQGGIKSLFVMGSNPIVSNPN 425
Cdd:cd02764 332 TAG--------ADTQVAVNAL--NSLLGNDGKTV-DHARPIKGGELGNQQDLKALasrINAGKVSALLVYDVNPVYDLPQ 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1553133439 426 AGLVEEGLKKLDFLMVADMFMSETAQLADLVLPVTSYMENEG 467
Cdd:cd02764 401 GLGFAKALEKVPLSVSFGDRLDETAMLCDWVAPMSHGLESWG 442
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
15-73 |
6.82e-09 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 52.25 E-value: 6.82e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 15 VIETQCPFCSVQCKMTVTEGENGIpgqrraeYKVEGVPN-AASEGRVCVKGMHAHQHAVH 73
Cdd:smart00926 3 WVPTVCPLCGVGCGLLVEVKDGRV-------VRVRGDPDhPVNRGRLCPKGRAGLEQVYS 55
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
590-705 |
8.34e-08 |
|
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: 50.92 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 590 YPLILTNGRVLSHYLTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLFVP 669
Cdd:cd02779 1 YKYWVNNGRANIIWQTAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFML 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1553133439 670 M-HWGGvqNVNYATRPELDPFCKMPGFKTSAVRIRSL 705
Cdd:cd02779 81 MaHPRP--GANGLVTPYVDPETIIPYYKGTWANIRKI 115
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
590-673 |
4.03e-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: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 590 YPLILTN--GRVLSHYLTGvqtrrSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLF 667
Cdd:cd02780 1 YPFILVTfkSNLNSHRSAN-----APWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVA 75
|
....*.
gi 1553133439 668 VPMHWG 673
Cdd:cd02780 76 IEHGYG 81
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
590-686 |
4.05e-07 |
|
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: 49.20 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 590 YPLILTNGRvlSHYLTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLFVP 669
Cdd:cd02786 1 YPLRLITPP--AHNFLNSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAE 78
|
90 100
....*....|....*....|..
gi 1553133439 670 MHW-----GGVQNVNYATRPEL 686
Cdd:cd02786 79 GGWwrehsPDGRGVNALTSARL 100
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
590-688 |
3.20e-06 |
|
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: 46.98 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 590 YPLILTNGRVLshYLTGVQTRRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLFVP 669
Cdd:cd02785 2 YPLACIQRHSR--FRVHSQFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAE 79
|
90 100
....*....|....*....|....*
gi 1553133439 670 MHW------GGvqNVNYATRPELDP 688
Cdd:cd02785 80 QGWwsryfqEG--SLQDLTSPFVNP 102
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
110-258 |
2.06e-05 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 48.07 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 110 QYGPDANAVYGGGSLTNETAYLLGKFARVALGTRHIDYNGRFCmsaaasagsktfgidrGLTFR------LADIPL---- 179
Cdd:PRK14991 216 EYGPKANQLLVTNASDEGRDAFIKRFAFNSFGTRNFGNHGSYC----------------GLAYRagsgalMGDLDKnphv 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 180 ------ARCIVLAGTNIAEC------QPTLLPyfNQAKENGAKIVVIDPRKTATA--AMGDMH--LPIRPGTDTVLADAM 243
Cdd:PRK14991 280 kpdwdnVEFALFIGTSPAQSgnpfkrQARQLA--NARTRGNFEYVVVAPALPLSSslAAGDNNrwLPIRPGTDSALAMGM 357
|
170
....*....|....*
gi 1553133439 244 LKIIMDEGLIDETFI 258
Cdd:PRK14991 358 IRWIIDNQRYNADYL 372
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
589-703 |
5.37e-04 |
|
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: 40.45 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1553133439 589 DYPLILTNGRvlsHYLTGVQT--RRSPTLLARELENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTL 666
Cdd:cd02782 1 DYPFLLLIGR---RHLRSNNSwlHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1553133439 667 FVPMHWG-------------GVqNVNYATRPE-LDPFCKMPGFKTSAVRIR 703
Cdd:cd02782 78 SLPHGWGhdypgvsgagsrpGV-NVNDLTDDTqRDPLSGNAAHNGVPVRLA 127
|
|
| MopB_CT_2 |
cd02783 |
The MopB_CT_2 CD includes a group of related uncharacterized bacterial and archaeal ... |
621-668 |
3.99e-03 |
|
The MopB_CT_2 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: 239184 [Multi-domain] Cd Length: 156 Bit Score: 38.59 E-value: 3.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1553133439 621 ENFAEIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLFV 668
Cdd:cd02783 31 RNYLYMHPKTAKELGIKDGDWVWVESVNGRVKGQARFTETVEPGTVWT 78
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
625-672 |
9.56e-03 |
|
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: 36.97 E-value: 9.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1553133439 625 EIHPNTAQRYRIQDGEWVEILSEHGSFIVRSRIKDQIREDTLFVpMHW 672
Cdd:cd02776 34 WMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFM-YHA 80
|
|
| |
