|
Name |
Accession |
Description |
Interval |
E-value |
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
34-626 |
0e+00 |
|
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes related subunits from formate dehydrogenase complexes. [Energy metabolism, Electron transport]
Pssm-ID: 273904 [Multi-domain] Cd Length: 602 Bit Score: 776.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 34 VFIDDKKVLVDPGMTILQACALVGVDIPRFCYHDRLSIAGNCRMCLVEVEKSVKPVASCAMPVMNGMKVKTNSDFVKKAR 113
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 114 EGVMEFMLNNHPLDCPICDQGGECDLQDQAMNFGSDRGRLqsrFDGKRALEDKNIGPLVKTVMTRCIQCTRCVRFANEVA 193
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRF---REKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 194 AFPDFGTTGRGQDLQIGTYVEKFFASELSGNIIDICPVGALTSKQYAFTARPWETRKTESVDVMDATGSNIVLSHRTGEL 273
Cdd:TIGR01973 158 GVEDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 274 LRVIPKINDDINEEWIGDQSRFAVDGLKVQ-RLLTPMIRGADGQLKPATWEEALFTVAAKLRETpaEQKAAVAGGLNDVE 352
Cdd:TIGR01973 238 MRILPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKAS--SRIGGIAGPRSSLE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 353 SLVALKDLFNRFNSENVMTEEEFPDVGSggSDLRSNYVFNDGIASVENADAILLVGTNPRFEAPTLNARIRKSFLYSDVQ 432
Cdd:TIGR01973 316 ELFALKKLVRKLGSENFDLRIRNYEFES--ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 433 VGVIGAETE-LTY-----EYDYLGASAKAIDEILAGKG-DFAKILSSATTPLIIVGAQALKGEAGAALLGKLQQLADKLG 505
Cdd:TIGR01973 394 VALIGIEKWnLTYpantnLVFHPGLSPKKLDDIASGAHsDIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIK 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 506 S-GKEVKVLNVLQRWAGQAGALDVGYK--AGTAGIRKTPIKFLYLLGAD----EGKVTKANL-DPSAFVVYQGHHGDAGA 577
Cdd:TIGR01973 474 VrRKEWNGLNILSSGANSVGLLDLGGEstGLDAALNLGAADALFLLGADleraLDKTARDALsKADAFIIYQGHHGTETA 553
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 17565758 578 EMADVVLPGAAYTEKEGTYVNTEGRSQRAYPAVSPPGDARVDWKIIRAV 626
Cdd:TIGR01973 554 EKADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
252-630 |
0e+00 |
|
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: 616.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 252 ESVDVMDATGSNIVLSHRTGELLRVIPKINDDINEEWIGDQSRFAVDGLKVQRLLTPMIRGAdGQLKPATWEEALFTVAA 331
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKN-GKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 332 KLRETPAEQKAAVAGGLNDVESLVALKDLFNRFNSENVMTEEEFPDVGSggsDLRSNYVFNDGIASVENADAILLVGTNP 411
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA---DLRSNYLFNTTIAGIEEADAVLLVGTNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 412 RFEAPTLNARIRKSFLYSDVQVGVIGAETELTYEYDYLGASAKAIDEILAGKGDFAKILSSATTPLIIVGAQALKGEAGA 491
Cdd:cd02773 157 RFEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 492 ALLGKLQQLADKLG-SGKEVKVLNVLQRWAGQAGALDVGYKAGTAGIRK-TPIKFLYLLGADEGKVTKanLDPSAFVVYQ 569
Cdd:cd02773 237 AILAAVAKLAKKNGvVREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKsGPPKVLYLLGADEIDITP--IPKDAFVVYQ 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17565758 570 GHHGDAGAEMADVVLPGAAYTEKEGTYVNTEGRSQRAYPAVSPPGDARVDWKIIRAVSEVS 630
Cdd:cd02773 315 GHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
31-655 |
0e+00 |
|
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: 591.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 31 KVEVFIDDKKVLVDPGMTILQACALVGVDIPRFCYHDRLSIAGNCRMCLVEVEKSVKPVASCAMPVMNGMKVKTNSDFVK 110
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 111 KAREGVMEFMLNNHPLDCPICDQGGECDLQDQAMNFGSDRgrlqSRFDG-KRALEDKNIGPLVKTVMTRCIQCTRCVRFA 189
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDE----SRYEEeKRTVPKKDLGPLILLDMNRCILCTRCVRFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 190 NEVAAFPDFGTTGRGQDLQIGTYVEKFFASELSGNIIDICPVGALTSKQYAFTARPWETRKTESVDVMDATGSNIVLSHR 269
Cdd:COG1034 157 DEIAGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 270 TGELLRVIPKINDDINEEWIGDQSRFAVDGLKV-QRLLTPMIRGaDGQLKPATWEEALFTVAAKLretpaeqkaavaggl 348
Cdd:COG1034 237 GGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRK-DGELVEASWEEALAAAAEGL--------------- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 349 ndveslvalkdlfnrfnsenvmteeefpdvgsggsdlrsnyvfndgiasvenadaillvgtnprfeaptlnarirksfly 428
Cdd:COG1034 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 429 sdvqvgvigaeteltyeydylgasakaideilagkgdfaKILSSAttpliivgaqalKGEAGAALLGKLQQLADKLgsgk 508
Cdd:COG1034 301 ---------------------------------------KALKKA------------ENSVGAALLGALPDAAAIL---- 325
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 509 evkvlnvlqrwagqagaldvgykagtAGIRKTPIKFLYLLGADE----GKVTKANLDPSAFVVYQGHHGDAGAEMADVVL 584
Cdd:COG1034 326 --------------------------EAAEAGKLKALVLLGADPydldPAAALAALAKADFVVVLDHFGSATAERADVVL 379
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17565758 585 PGAAYTEKEGTYVNTEGRSQRAYPAVSPPGDARVDWKIIRAVSEVSGKSLPYSDLKEIRQRLNEIAPHLVR 655
Cdd:COG1034 380 PAAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVS 450
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
252-629 |
3.47e-146 |
|
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: 432.09 E-value: 3.47e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 252 ESVDVMDATGSNIVLSHRTGELLRVIPKINDDINEEWIGDQSRFAVDGLKV-QRLLTPMIRGaDGQLKPATWEEALFTVA 330
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSrQRLTQPLIKK-GGKLVPVSWEEALKTVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 331 AKLRETPAEQKAAVAGGLNDVESLVALKDLFNRFNSENVMTEEEFPDVGSGGsDLRSNYVFNDGIASVENADAILLVGTN 410
Cdd:cd02768 80 EGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADN-RLRGNYLFNTSIAEIEEADAVLLIGSN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 411 PRFEAPTLNARIRKSFLYSDVQVGVIGAET-----ELTYEYDYLGASAKAIDEILAGKG--DFAKILSSATTPLIIVGAQ 483
Cdd:cd02768 159 LRKEAPLLNARLRKAVKKKGAKIAVIGPKDtdliaDLTYPVSPLGASLATLLDIAEGKHlkPFAKSLKKAKKPLIILGSS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 484 ALKGEaGAALLGKLQQLADKLGSG-KEVKVLNVLQRWAGQAGA--LDVGYKAGTAGIRKtpikfLYLLGADEGKVTKANL 560
Cdd:cd02768 239 ALRKD-GAAILKALANLAAKLGTGaGLWNGLNVLNSVGARLGGagLDAGLALLEPGKAK-----LLLLGEDELDRSNPPA 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17565758 561 D-----PSAFVVYQGHHGDAGAEmADVVLPGAAYTEKEGTYVNTEGRSQRAYPAVSPPGDARVDWKIIRAVSEV 629
Cdd:cd02768 313 AvalaaADAFVVYQGHHGDTGAQ-ADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
304-629 |
2.67e-124 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 374.81 E-value: 2.67e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 304 RLLTPMIRGADGQLKPATWEEALFTVAAKLRETPAEQK------AAVAGGLNDVESLVALKDLFNRFNSENVMTEEEFPD 377
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKYGpdaiaiNGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 378 VGSG-----GSDLRSNYVFNDGIASVENADAILLVGTNPRFEAPTLNARIRKSFLYSDVQVGVIGAETELTYEYDYLGAS 452
Cdd:pfam00384 81 LCTAaaaafGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 453 AKAIDEI-LAGKGDFAKILS----SATTPLIIVGAQALKGEAGAALLGKLQQLADKLGS----GKEVKVLNVLQRWAGQA 523
Cdd:pfam00384 161 PGTDLALaLAGAHVFIKELKkdkdFAPKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNigrpGGGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 524 GALDVGYKAG------TAGIRKTPIKFLYLLG-------ADEGKVTKANLDPSAFVVYQGHHGDAGAEMADVVLPGAAYT 590
Cdd:pfam00384 241 GALDLGLVPGiksvemINAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 17565758 591 EKEGTYVNTEGRSQRAYPAVSPPGDARVDWKIIRAVSEV 629
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
28-651 |
1.40e-112 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 358.87 E-value: 1.40e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 28 PPKKVEVFIDDKKVLVDPGMTILQACALVGVDIPRFCYHDRLSIAGNCRMCLVEVEKSVKPVASCAMPVMNGMKVKT--N 105
Cdd:PRK07860 1 PPDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 106 SDFVKKAREGVMEFMLNNHPLDCPICDQGGECDLQDQAMNfgsdRGRLQSRFDG-KRALEdKNIgPLVKTVM---TRCIQ 181
Cdd:PRK07860 81 SPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMS----NGRAESRFTDvKRTFP-KPI-NISTQVLldrERCVL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 182 CTRCVRFANEVAAFPDFGTTGRGQDLQIGTYVEKFFASELSGNIIDICPVGALTSKQYAFTARPWETRKTESVDVMDATG 261
Cdd:PRK07860 155 CARCTRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 262 SNIVLSHRTGELLRVIPKINDDINEEWIGDQSRFAVD-GLKVQRLLTPMIRGADGQLKPATWEEALFTVAAKLREtpAEQ 340
Cdd:PRK07860 235 CAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAA--ARG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 341 KAAV-AGGLNDVE--------SLVALK----DLFNRFNSENvmtEEEFPDVGSGGSDLRSNYvfndgiASVENADAILLV 407
Cdd:PRK07860 313 RVGVlVGGRLTVEdayayakfARVALGtndiDFRARPHSAE---EADFLAARVAGRGLGVTY------ADLEKAPAVLLV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 408 GTNPRFEAPTLNARIRKSFLYSDVQVGVIG--AETELTYEYDYL-----GASAKAIDEILAGKGDFAKILSSATTpLIIV 480
Cdd:PRK07860 384 GFEPEEESPIVFLRLRKAARKHGLKVYSIApfATRGLEKMGGTLlrtapGGEAAALDALATGAPDVAELLRTPGA-VILV 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 481 GaQALKGEAGAalLGKLQQLADKLGSGkevkvLNVLQRWAGQAGALDVG------------------------------- 529
Cdd:PRK07860 463 G-ERLATVPGA--LSAAARLADATGAR-----LAWVPRRAGERGALEAGalptllpggrpvadpaaraevaaawgvdelp 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 530 --YKAGTAGIrktpikflyLLGADEGK--------VTKANL-DPSA---------FVVYQGHHGDAGAEMADVVLPGAAY 589
Cdd:PRK07860 535 aaPGRDTAGI---------LAAAAAGElgallvggVEPADLpDPAAalaaldaagFVVSLELRHSAVTERADVVLPVAPV 605
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17565758 590 TEKEGTYVNTEGRSqRAYPAVSPPGDARVDWKIIRAVSEVSGKSLPYSDLKEIRQRLNEIAP 651
Cdd:PRK07860 606 AEKAGTFLNWEGRL-RPFEAALRTTGALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
252-628 |
4.83e-68 |
|
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: 228.37 E-value: 4.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 252 ESVDVMDATGSNIVLSHRTGELLRVIPKINDDINEEWIGDQSRFAVDGLK-VQRLLTPMIR-GADGQLKPATWEEALFTV 329
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYsPDRLKYPLIRvGGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 330 AAKLRETPAEQK----AAVAGGLNDVESLVALKDLFNRFNSENVMTEEEFPDVGSG-GSDLRSNYVFNDGIASVENADAI 404
Cdd:cd00368 81 AEKLKEIREKYGpdaiAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVaALKAFGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 405 LLVGTNPRFEAPTLNARIRKSfLYSDVQVGVIG-AETELTYEYDY-------------LGASAKAI-----DEILAgkgd 465
Cdd:cd00368 161 LLWGSNPAETHPVLAARLRRA-KKRGAKLIVIDpRRTETAAKADEwlpirpgtdaalaLAEWAAEItgvpaETIRA---- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 466 FAKILSSATTPLIIVG---AQALKGEAGAALLGKLQQLadklgsgkevkvlnvlqrwAGQAGALDVGYKAGTAGIRKTPi 542
Cdd:cd00368 236 LAREFAAAKRAVILWGmglTQHTNGTQNVRAIANLAAL-------------------TGNIGRPGGGLGPGGNPLVSAP- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 543 kflyllgaDEGKVTKANLDPSAFVVYQGHHGDAgAEMADVVLPGAAYTEKEGTYVNTEGRSQRAYPAVSPPGDARVDWKI 622
Cdd:cd00368 296 --------DANRVRAALKKLDFVVVIDIFMTET-AAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEI 366
|
....*.
gi 17565758 623 IRAVSE 628
Cdd:cd00368 367 LRELAK 372
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
252-626 |
1.55e-64 |
|
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex I, the second domain of the Nad11/75-kDa subunit of some protists. NADH-quinone oxidoreductase 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. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH-quinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. The Nad11 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: 239175 [Multi-domain] Cd Length: 366 Bit Score: 218.77 E-value: 1.55e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 252 ESVDVMDATGSNIVLSHRTGELLRVIPKINDDINEEWIGDQSRFAVDGLKVQRLLTPMIRGADGQLKPATWEEALFTVAA 331
Cdd:cd02774 1 ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIGWKTAFKFLNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 332 KLRETPAEQKAAVAGGLNDVESLVALKDLFNRFNSENVMTEEEFPDVGSGGSDlRSNYVFNDGIASVENADAILLVGTNP 411
Cdd:cd02774 81 FILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFLENNNYFNLD-LENYLFNNSLKNLDKSDLCLLIGSNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 412 RFEAPTLNARIRKSFLYSDVQVGVIGAETELTYEYDYLGASAKAIDEILAGKGDFAKILSSATTPLIIVGAQALKGEAGA 491
Cdd:cd02774 160 RVESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEGKHLFCKQLKKSKKPLIIIGSSFSLRKNYS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 492 ALLGKLQQLadklgSGKEVKVLNVLQrwaGQAGAL-DVGYKAGTAGIRKTPIKFLYLlgaDEGKVTKANLDpsAFVVYQG 570
Cdd:cd02774 240 FIISKLKNF-----SSNNENNFNFLN---IISNSLyYLGIKKFNSNNKKNLSNLYYI---KETNFQKFNKN--NFVIYQG 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 17565758 571 HHGDAGAEMADVVLPGAAYTEKEGTYVNTEGRSQRAYPAVSPPGDARVDWKIIRAV 626
Cdd:cd02774 307 HHFLNLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSDDNIIFSL 362
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
2-234 |
3.88e-53 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 185.63 E-value: 3.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 2 HRVGGQ-IVRGVSKAQQkrslsvaAPAPPKKVeVFIDDKKVLVDPGM-TILQACALVGVDIPRFCYHDRLSIAGNCRMCL 79
Cdd:PTZ00305 46 HRGGVEaAAEGVAAGQY-------AEHKPRAI-MFVNKRPVEIIPQEeNLLEVLEREGIRVPKFCYHPILSVAGNCRMCL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 80 VEVEKSVKPVASCAMPVMNGMKVKTNSDFVKKAREGVMEFMLNNHPLDCPICDQGGECDLQDQAMNFGSDRGRLQsrfDG 159
Cdd:PTZ00305 118 VQVDGTQNLVVSCATVALPGMSIITDSRLVRDAREGNVELILINHPNDCPICEQATNCDLQNVSMNYGTDIPRYK---ED 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17565758 160 KRALEDKNIGPLVKTVMTRCIQCTRCVRFANEVAAFPDFGTTGRGQDLQIGTYVEKF-FASELSGNIIDICPVGAL 234
Cdd:PTZ00305 195 KRAVQDFYFDPQTRVVLNRCIHCTRCVRFLNEHAQDFNLGMIGRGGLSEISTFLDELeVKTDNNMPVSQLCPVGKL 270
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
253-625 |
7.67e-49 |
|
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: 177.16 E-value: 7.67e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 253 SVDVMDATGSNIVLSHRTGELLRVIPKINDDINEEWIGDQSRFAVDGLKVQ-RLLTPMIRGaDGQLKPATWEEALFTVAA 331
Cdd:cd02772 2 SVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEdRLTKPMIKK-DGQWQEVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 332 KLRETPAEQKAAVAGGL----NDVESLVALKDLFNRFNSENV---MTEEEFPDVGSggsdLRSNYVFNDGIASVENADAI 404
Cdd:cd02772 81 GLSAIIKKHGADQIGALasphSTLEELYLLQKLARGLGSDNIdhrLRQSDFRDDAK----ASGAPWLGMPIAEISELDRV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 405 LLVGTNPRFEAPTLNARIRKSFLYSdVQVGVIGA-ETELTYEYDY------------LGASAKAIDEI------------ 459
Cdd:cd02772 157 LVIGSNLRKEHPLLAQRLRQAVKKG-AKLSAINPaDDDFLFPLSGkaivapsalanaLAQVAKALAEEkglavpdedakv 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 460 --LAGKGDFAKILSSATTPLIIVGAQALKGEAGAALLGKLQQLADKLGSgkevkVLNVLQRWAG-----QAGALDVGYKA 532
Cdd:cd02772 236 eaSEEARKIAASLVSAERAAVFLGNLAQNHPQAATLRALAQEIAKLTGA-----TLGVLGEGANsvgayLAGALPHGGLN 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 533 GTAgIRKTPIKFLYLLGA------DEGKVTKANLDPSAFVVYQGHHGDAGAE-MADVVLPGAAYTEKEGTYVNTEGRSQR 605
Cdd:cd02772 311 AAA-MLEQPRKAYLLLNVepeldcANPAQALAALNQAEFVVALSAFASAALLdYADVLLPIAPFTETSGTFVNLEGRVQS 389
|
410 420
....*....|....*....|
gi 17565758 606 AYPAVSPPGDARVDWKIIRA 625
Cdd:cd02772 390 FKGVVKPLGEARPAWKVLRV 409
|
|
| 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 ... |
259-638 |
6.67e-40 |
|
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: 153.31 E-value: 6.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 259 ATGSNIVLSHRTGELLRVIPKINDDINEEWIGDQSRFAVDGLKVQ-RLLTPMIRGaDGQLKPATWEEALFTVAAKLREtp 337
Cdd:cd02771 8 SVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRdRLTQPLIRR-GGTLVPVSWNEALDVAAARLKE-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 338 AEQKAAVAGGLN-DVESLVALKDLFNRFNSenvMTEEEFPDVGSGGSDLRSNYVFNDGIASVENADAILLVGTNPRFEAP 416
Cdd:cd02771 85 AKDKVGGIGSPRaSNESNYALQKLVGAVLG---TNNVDHRARRLIAEILRNGPIYIPSLRDIESADAVLVLGEDLTQTAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 417 TLNARIRKS--------FLYSDVQVGVIGAETELTYEYDY----LGASAKAIDEILAG-----KGDFAKILSSAttplii 479
Cdd:cd02771 162 RIALALRQAarrkavelAALSGIPKWQDAAVRNIAQGAKSplfiVNALATRLDDIAAEsirasPGGQARLGAAL------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 480 vgAQALKGEAGAAL----LGKLQQLADKLGSGK------------------EVKVLNVLQRwAGQAGALDVGYKAGT--- 534
Cdd:cd02771 236 --ARAVDASAAGVSglapKEKAARIAARLTGAKkplivsgtlsgslelikaAANLAKALKR-RGENAGLTLAVEEGNspg 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 535 -------------------AGIRKTPIKFLYLLG------ADEGKVTKAnLDPSAFVVYQGHHGDAGAEMADVVLPGAAY 589
Cdd:cd02771 313 llllgghvtepgldldgalAALEDGSADALIVLGndlyrsAPERRVEAA-LDAAEFVVVLDHFLTETAERADVVLPAASF 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 17565758 590 TEKEGTYVNTEGRSQRAYPAV-SPPGDARVDWKIIRAVSEVSGKSLPYSD 638
Cdd:cd02771 392 AEKSGTFVNYEGRAQRFFKAYdDPAGDARSDWRWLHALAAKLGGKLVPSD 441
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
259-650 |
7.10e-36 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 144.64 E-value: 7.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 259 ATGSNIVLSHRTGELLRVIPKINDDINEEWIGDQSRFAVDGL-KVQRLLTPMIRgADGQLKPATWEEALFTVAAKLRETP 337
Cdd:COG3383 15 GVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVnSPDRLTTPLIR-RGGEFREVSWDEALDLVAERLREIQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 338 AE----------------------QKAAVAG-GLNDVE---------SLVALKDLFnrfnsenvmteeefpdvgsgGSDL 385
Cdd:COG3383 94 AEhgpdavafygsgqltneenyllQKLARGVlGTNNIDnnarlcmasAVAGLKQSF--------------------GSDA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 386 RSNyvfndGIASVENADAILLVGTNPRFEAPTLNARIRKS-----------------------FLY----SDVQV----- 433
Cdd:COG3383 154 PPN-----SYDDIEEADVILVIGSNPAEAHPVLARRIKKAkkngaklivvdprrtetarladlHLQikpgTDLALlngll 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 434 GVIGAE--------TELTYEYDYLGASAKAID----EILAG--KGD---FAKILSSATTPLIIVG---AQALKGEAGAAL 493
Cdd:COG3383 229 HVIIEEglvdedfiAERTEGFEELKASVAKYTpervAEITGvpAEDireAARLIAEAKRAMILWGmgvNQHTQGTDNVNA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 494 LGKLQQLADKLGsgKEVKVLNVLqrwAGQA---GALDVGYKA----------------------GTAGIRKTP------- 541
Cdd:COG3383 309 IINLALATGNIG--RPGTGPFPL---TGQNnvqGGRDMGALPnvlpgyrdvtdpehrakvadawGVPPLPDKPgltavem 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 542 --------IKFLYLLG-------ADEGKVTKA--NLDpsaFVVYQGHHGDAGAEMADVVLPGAAYTEKEGTYVNTEGRSQ 604
Cdd:COG3383 384 fdaiadgeIKALWIIGenpavsdPDANHVREAleKLE---FLVVQDIFLTETAEYADVVLPAASWAEKDGTFTNTERRVQ 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 17565758 605 RAYPAVSPPGDARVDWKIIRAVSEVSGKSLPYSDLKEIRqrlNEIA 650
Cdd:COG3383 461 RVRKAVEPPGEARPDWEIIAELARRLGYGFDYDSPEEVF---DEIA 503
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
36-237 |
9.50e-36 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 135.16 E-value: 9.50e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 36 IDDKKVLVDPGMTILQACALVGVDIPRFCYHDRLSIAGNCRMCLVEVEKSVKPVASCAMPVMNGMKVKTNSDFVKKAREG 115
Cdd:PRK07569 8 IDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQEYRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 116 VMEFML--NNHPldCPICDQGGECDLQDQAMNFGSDRGRLQSRFDgKRALE--------DKNigplvktvmtRCIQCTRC 185
Cdd:PRK07569 88 IVELLFaeGNHV--CAVCVANGNCELQDLAIEVGMDHVRFPYLFP-RRPVDishprfgiDHN----------RCVLCTRC 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 17565758 186 VRFANEVAAFPDFGTTGRGQDLQIGTYVEKFFASELS----GNIIDICPVGALTSK 237
Cdd:PRK07569 155 VRVCDEIEGAHTWDVAGRGAKSRVITDLNQPWGTSETctscGKCVQACPTGAIFRK 210
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
31-253 |
6.51e-31 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 129.83 E-value: 6.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 31 KVEVFIDDKKVLVDPGMTILQACALVGVDIPRFCYHDRLSIAGNCRMCLVEVEKsvKPVASCAMPVMNGMKVKTNSDFVK 110
Cdd:PRK08493 1 MITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEADG--KRVYSCNTKAKEGMNILTNTPNLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 111 KAREGVMEFMLNNHPLDCPICDQGGECDLQDQAMNFGSDRGRLQSRfDGKRALE-------DKNIgplvktvmtrCIQCT 183
Cdd:PRK08493 79 DERNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVNHQPYAIK-DTHKPHKhwgkinyDPSL----------CIVCE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 184 RCVRFANEVAAFPDFGTTGRGQDLQIGTYVEK------------------FFASELS-----GNIIDICPVGALTSKQYA 240
Cdd:PRK08493 148 RCVTVCKDKIGESALKTVPRGLDAPDKSFKESmpkdayavwskkqksligPVGGETLdcsfcGECIAVCPVGALSSSDFQ 227
|
250
....*....|...
gi 17565758 241 FTARPWETRKTES 253
Cdd:PRK08493 228 YTSNAWELKKIPA 240
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
259-660 |
1.64e-29 |
|
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: 123.48 E-value: 1.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 259 ATGSNIVLSHRTGELLRVIPKINDDINEEWIGDQSRFAVDGLKV-QRLLTPMIRgADGQLKPATWEEALFTVAAKLRE-- 335
Cdd:cd02753 8 GVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSkDRLTKPLIR-KNGKFVEASWDEALSLVASRLKEik 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 336 ---------------TPAE-----QK-AAVAGGLNDVE---------SLVALKDLFnrfnsenvmteeefpdvGSGGSdl 385
Cdd:cd02753 87 dkygpdaiaffgsakCTNEenylfQKlARAVGGTNNVDhcarlchspTVAGLAETL-----------------GSGAM-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 386 rSNyvfndGIASVENADAILLVGTNPRFEAPTLNARIRKSfLYSDVQVGVIGA-ETELTYEYDY------------LGAS 452
Cdd:cd02753 148 -TN-----SIADIEEADVILVIGSNTTEAHPVIARRIKRA-KRNGAKLIVADPrRTELARFADLhlqlrpgtdvalLNAM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 453 AKAI-----------DEILAGKGDFAKILSSAT----TPLIIVGAQALK------GEAGAAL----LGKLQQ-------- 499
Cdd:cd02753 221 AHVIieeglydeefiEERTEGFEELKEIVEKYTpeyaERITGVPAEDIReaarmyATAKSAAilwgMGVTQHshgtdnvm 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 500 ----LADKLGS-GKEVKVLNVLqrwAGQ---AGALDVGykagtagirKTP------IKFLYLLG-------ADEGKVTKA 558
Cdd:cd02753 301 alsnLALLTGNiGRPGTGVNPL---RGQnnvQGACDMG---------ALPnvlpgyVKALYIMGenpalsdPNTNHVRKA 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 559 --NLDpsaFVVYQGHHGDAGAEMADVVLPGAAYTEKEGTYVNTEGRSQRAYPAVSPPGDARVDWKIIRAVSEVSGKSLPY 636
Cdd:cd02753 369 leSLE---FLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFY 445
|
490 500
....*....|....*....|....*.
gi 17565758 637 SDLKEIRQRLNEIAPHL--VRYRDLE 660
Cdd:cd02753 446 SHPEEIFDEIARLTPQYagISYERLE 471
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
259-663 |
3.36e-20 |
|
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: 94.99 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 259 ATGSNIVLSHRTGELLRVIPKINDDINeewigdQSRFAVDGL-------KVQRLLTPMIRGADGQLKPATWEEALFTVAA 331
Cdd:cd02754 8 GVGCGVEIGVKDGKVVAVRGDPEHPVN------RGRLCIKGLnlhktlnGPERLTRPLLRRNGGELVPVSWDEALDLIAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 332 KLRETPAEQkaavagglnDVESlVALkdlfnrFNSENVMTEEEF--PDVGSGGsdLRSNYVfnDG-----IAS------- 397
Cdd:cd02754 82 RFKAIQAEY---------GPDS-VAF------YGSGQLLTEEYYaaNKLAKGG--LGTNNI--DTnsrlcMASavagykr 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 398 -------------VENADAILLVGTNPRFEAPTLNARIRKSfLYSDVQVGVIGAETELTyeydylgASAKAIDEILAGK- 463
Cdd:cd02754 142 sfgadgppgsyddIEHADCFFLIGSNMAECHPILFRRLLDR-KKANPGAKIIVVDPRRT-------RTADIADLHLPIRp 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 464 -GDFAkiLSSATTPLII--------------VGAQALKGEAG-------AALLG----KLQQLADKLGSGKEVKVL---N 514
Cdd:cd02754 214 gTDLA--LLNGLLHVLIeeglidrdfidahtEGFEELKAFVAdytpekvAEITGvpeaDIREAARLFGEARKVMSLwtmG 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 515 VLQR----WAGQA----------------------------GALDVGYKAGTAG------------------------IR 538
Cdd:cd02754 292 VNQStqgtAANNAiinlhlatgkigrpgsgpfsltgqpnamGGREVGGLANLLPghrsvnnpehraevakfwgvpegtIP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 539 KTP---------------IKFLYLLG-------ADEGKVTKAnLDPSAFVVYQghhgDA-----GAEMADVVLPGAAYTE 591
Cdd:cd02754 372 PKPglhavemfeaiedgeIKALWVMCtnpavslPNANRVREA-LERLEFVVVQ----DAfadteTAEYADLVLPAASWGE 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 592 KEGTYVNTEGRSQRAYPAVSPPGDARVDWKIIRAVSEVSGK--SLPYSDLKEI--------RQRLNEIAPhlVRYRDLEA 661
Cdd:cd02754 447 KEGTMTNSERRVSLLRAAVEPPGEARPDWWILADVARRLGFgeLFPYTSPEEVfeeyrrlsRGRGADLSG--LSYERLRD 524
|
..
gi 17565758 662 SP 663
Cdd:cd02754 525 GG 526
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
304-666 |
8.21e-20 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 94.14 E-value: 8.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 304 RLLTPMIRG---ADGQLKPATWEEALFTVAAKLRETPAEQKA-AVA--------GGLNDVESLVALKdLFNRFNSENvmt 371
Cdd:COG0243 78 RLTYPMKRVgprGSGKFERISWDEALDLIAEKLKAIIDEYGPeAVAfytsggsaGRLSNEAAYLAQR-FARALGTNN--- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 372 eeeFPDVGS---GGSDLRSNYVFNDGIASV-----ENADAILLVGTNPRFEAPTLNARIRKSFLYSDVQVGVI------- 436
Cdd:COG0243 154 ---LDDNSRlchESAVAGLPRTFGSDKGTVsyedlEHADLIVLWGSNPAENHPRLLRRLREAAKKRGAKIVVIdprrtet 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 437 ---------------GA----------ETELtYEYDYLGASAKAIDEILAgkgdFAKilssATTPliivgaqalkgEAGA 491
Cdd:COG0243 231 aaiadewlpirpgtdAAlllalahvliEEGL-YDRDFLARHTVGFDELAA----YVA----AYTP-----------EWAA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 492 ALLG----KLQQLADKLGSGK---------------------EVKVLNVLQrwaGQ-----AGALDVGYKAGTAGiRKTP 541
Cdd:COG0243 291 EITGvpaeDIRELAREFATAKpavilwgmglqqhsngtqtvrAIANLALLT---GNigkpgGGPFSLTGEAILDG-KPYP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 542 IKFLYLLG-------ADEGKVTKA--NLDpsaFVVYQGHHGDAGAEMADVVLPGAAYTEKEGTYVNTE-GRSQRAYPAVS 611
Cdd:COG0243 367 IKALWVYGgnpavsaPDTNRVREAlrKLD---FVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVE 443
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 17565758 612 PPGDARVDWKIIRAVSEVSGKSLPYSDLKE----IRQRLNEIAPHLVRYRDLEASPFVK 666
Cdd:COG0243 444 PPGEARSDWEIFAELAKRLGFEEAFPWGRTeedyLRELLEATRGRGITFEELREKGPVQ 502
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
30-106 |
2.07e-18 |
|
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.
Pssm-ID: 433268 [Multi-domain] Cd Length: 82 Bit Score: 80.28 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 30 KKVEVFIDDKKVLVDPGMTILQACALVGVDIPRFCYHDR----LSIAGNCRMCLVEVEKsVKPVASCAMPVMNGMKVKTN 105
Cdd:pfam13510 2 RPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDG-VPNVRACTTPVREGMVVRTQ 80
|
.
gi 17565758 106 S 106
Cdd:pfam13510 81 N 81
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
113-152 |
6.50e-16 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 71.71 E-value: 6.50e-16
10 20 30 40
....*....|....*....|....*....|....*....|
gi 17565758 113 REGVMEFMLNNHPLDCPICDQGGECDLQDQAMNFGSDRGR 152
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
30-139 |
7.97e-16 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 81.31 E-value: 7.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 30 KKVEVFIDDKKVLVDPGMTILQACALVGVDIPRFCYHDRLSIAGNCRMCLVEVEKSVKPVASCAMPVMNGMKVKTNSDFV 109
Cdd:PRK12814 2 NTISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETENAEL 81
|
90 100 110
....*....|....*....|....*....|
gi 17565758 110 KKAREGVMEFMLNNHPLDCPicdqgGECDL 139
Cdd:PRK12814 82 HAMRRQSLERLIEQHCGDCL-----GPCEL 106
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
113-152 |
8.02e-15 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 68.76 E-value: 8.02e-15
10 20 30 40
....*....|....*....|....*....|....*....|
gi 17565758 113 REGVMEFMLNNHPLDCPICDQGGECDLQDQAMNFGSDRGR 152
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQR 40
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
31-103 |
3.40e-11 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 59.72 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 31 KVEVFIDDKKVLVDPGMTILQACALVGVDIPRFCYHdrlsiaGNCRMCLVEVEK----------------SVKPVASCAM 94
Cdd:cd00207 2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQT 75
|
....*....
gi 17565758 95 PVMNGMKVK 103
Cdd:cd00207 76 RVTDGLVIE 84
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
303-669 |
9.76e-10 |
|
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: 61.50 E-value: 9.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 303 QRLLTPMIR--GADGQLKPATWEEALFTVAAKLRETPAEQKAAV------AG--GLNDVESLVALkdlfnrFNSENVMTE 372
Cdd:cd02766 54 DRLLTPLKRvgRKGGQWERISWDEALDTIAAKLKEIKAEYGPESilpysyAGtmGLLQRAARGRF------FHALGASEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 373 EEFPDVGSGGSDLRSNY--VFNDGIASVENADAILLVGTNPR----------FEA-----------PTLNARIRKSFLYS 429
Cdd:cd02766 128 RGTICSGAGIEAQKYDFgaSLGNDPEDMVNADLIVIWGINPAatnihlmriiQEArkrgakvvvidPYRTATAARADLHI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 430 DVQVGVIGA---------ETELTYEYDYLGASAKAIDEILA--GKGDFAKILSSATTPLIIVGAQA-LKGEAGAALLgkl 497
Cdd:cd02766 208 QIRPGTDGAlalgvakvlFREGLYDRDFLARHTEGFEELKAhlETYTPEWAAEITGVSAEEIEELArLYGEAKPPSI--- 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 498 qqladKLGSGkevkvlnvLQRWA--GQA-------GAL--DVGYKAGTA--GIRKTPIKFLYLLGA-------DEGKVTK 557
Cdd:cd02766 285 -----RLGYG--------MQRYRngGQNvraidalPALtgNIGVPGGGAfySNSGPPVKALWVYNSnpvaqapDSNKVRK 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 558 ANLDPSAFVVYQGHHGDAGAEMADVVLPGAAYTEKE-------GTYVntegrsQRAYPAVSPPGDARVDWKIIRAVSevs 630
Cdd:cd02766 352 GLAREDLFVVVHDQFMTDTARYADIVLPATTFLEHEdvyasywHYYL------QYNEPAIPPPGEARSNTEIFRELA--- 422
|
410 420 430
....*....|....*....|....*....|....*....
gi 17565758 631 gkslpysdlkeirQRLNEIAPhlVRYRDLEAspFVKQAL 669
Cdd:cd02766 423 -------------KRLGFGEP--PFEESDEE--WLDQAL 444
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
668-707 |
2.76e-07 |
|
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at the C-terminus of NADH dehydrogenases subunit G or NADH-ubiquinone oxidoreductase subunit G. EC:1.6.99.5.
Pssm-ID: 462757 Cd Length: 41 Bit Score: 47.22 E-value: 2.76e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 17565758 668 ALQLAQPTGSIDVDVSPVLRELSDYYQTNVISRYSRSMAQ 707
Cdd:pfam09326 1 ALVLALAGAKGKLSGAPLKSPIEDFYMTDPISRASATMAK 40
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
561-623 |
3.91e-07 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 53.75 E-value: 3.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17565758 561 DPSAFVVYQGHHGDAGAEMADVVLPGAAYTEKEGTYVNTEGRSQRAYPAVSPPGDARVD-WKII 623
Cdd:PRK13532 502 NPDNFIVVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV 565
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
304-617 |
3.47e-06 |
|
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: 50.18 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 304 RLLTPMIRGADGQLKPATWEEALFTVAAKLRETPAEQKAAVAGGLNDVESLVALKDLFNR--FNSENVM----------- 370
Cdd:cd02764 99 RAQGPLRRGIDGAYVASDWADFDAKVAEQLKAVKDGGKLAVLSGNVNSPTTEALIGDFLKkyPGAKHVVydplsaedvne 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 371 -TEEEFPD---------------------VGSGGSDLRSNYVFNDGIASVENADAILLVGTNPrfeAPTL---NARIRKS 425
Cdd:cd02764 179 aWQASFGKdvvpgydfdkaevivsidadfLGSWISAIRHRHDFAAKRRLGAEEPMSRLVAAES---VYTLtgaNADVRLA 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 426 FLYSDV---------QVGVIGAETELTYEYDYLGASAKAID--EILAGKGDF----AKILSSATTPLIIVGAqALKGEAG 490
Cdd:cd02764 256 IRPSQEkafalglahKLIKKGAGSSLPDFFRALNLAFKPAKvaELTVDLDKAlaalAKALAAAGKSLVVAGS-ELSQTAG 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 491 AALLGKLQQLADKLGS-GKEVKVLN-VLQRWAGQAGALDVGYKAGTAGIRKTPIKF----LYLLGADEGkVTKAnLDPSA 564
Cdd:cd02764 335 ADTQVAVNALNSLLGNdGKTVDHARpIKGGELGNQQDLKALASRINAGKVSALLVYdvnpVYDLPQGLG-FAKA-LEKVP 412
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 17565758 565 FVVYQGHHGDAGAEMADVVLPGAAYTEKEGTYVNTEGRSQRAYPAVSPPGDAR 617
Cdd:cd02764 413 LSVSFGDRLDETAMLCDWVAPMSHGLESWGDAETPDGTYSICQPVIAPLFDTR 465
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
539-654 |
4.46e-06 |
|
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: 50.01 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 539 KTPIKFLYLLG--------ADEGKVTKANLDPSA---FVVYQGHHGDAGAEMADVVLPGAAYTEKEGtYVNTEGRSQRAY 607
Cdd:cd02770 406 KSNIKMIWNYAgntlinqhSDDNNTTRALLDDESkceFIVVIDNFMTPSARYADILLPDTTELERED-IVLTSNAGMMEY 484
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 17565758 608 -----PAVSPPGDARVDWKIIRAVSEVSGKSLPYSDLKEIRQRLNEIAPHLV 654
Cdd:cd02770 485 liysqKAIEPLYECKSDYEICAELAKRLGVEDQFTEGKTEQEWLEELYGQTR 536
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
574-636 |
1.34e-05 |
|
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: 48.08 E-value: 1.34e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 574 DAGAEMADVVLPGAAYTEK-------EGTYVNTEGrsqrayPAVSPPGDARVDWKIIRAVSevsgKSLPY 636
Cdd:cd02750 374 DSTALYSDIVLPAATWYEKhdlsttdMHPFIHPFS------PAVDPLWEAKSDWEIFKALA----KKVPW 433
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
530-649 |
1.97e-05 |
|
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: 47.99 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 530 YKAGTAGIRKTPIKFLYLLGA-------DEGKVTKANLDPSaFVVYQGHHGDAGAEMADVVLPGAAYTEKE--GTYVNTE 600
Cdd:cd02751 395 FTANGKLKTYPDIKMIYWAGGnplhhhqDLNRLIKALRKDE-TIVVHDIFWTASARYADIVLPATTSLERNdiGLTGNYS 473
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 17565758 601 GRSQRAYPAVSPP-GDARVDWKIIRAVSEVSGKSLPYSDLKEIRQRLNEI 649
Cdd:cd02751 474 NRYLIAMKQAVEPlGEARSDYEIFAELAKRLGVEEEFTEGRDEMEWLEHL 523
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
269-421 |
4.85e-05 |
|
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: 46.70 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 269 RTGELLRVIPKinddineEWIG-DQSRFAVDGL-KVQR------LLTPMIR---GADGQLKPATWEEALFTVAAKLRETP 337
Cdd:cd02765 19 RDGKIVKVEPN-------EWPDkTYKRGCTRGLsHLQRvyspdrLKYPMKRvgeRGEGKFERITWDEALDTIADKLTEAK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 338 AEQKAAVAGGLNDVESLVALKDLFNR-FNSENVMTEEEFPDVG-SGGSDLRSNYVFNDG---IASVENADAILLVGTNPr 412
Cdd:cd02765 92 REYGGKSILWMSSSGDGAILSYLRLAlLGGGLQDALTYGIDTGvGQGFNRVTGGGFMPPtneITDWVNAKTIIIWGSNI- 170
|
....*....
gi 17565758 413 FEAPTLNAR 421
Cdd:cd02765 171 LETQFQDAE 179
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
304-411 |
5.37e-05 |
|
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: 46.62 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 304 RLLTPMIRgADGQLKPATWEEALFTVAAKL---RETPAEQKAAV----------AGGLNDVESLVALKDLfNRFNSEnvm 370
Cdd:cd02762 54 RLRTPMRR-RGGSFEEIDWDEAFDEIAERLraiRARHGGDAVGVyggnpqahthAGGAYSPALLKALGTS-NYFSAA--- 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 17565758 371 TEEEFPdvgsggSDLRSNYVFNDG----IASVENADAILLVGTNP 411
Cdd:cd02762 129 TADQKP------GHFWSGLMFGHPglhpVPDIDRTDYLLILGANP 167
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
34-82 |
1.74e-04 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 40.59 E-value: 1.74e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 17565758 34 VFIDDKKVLV---DPGMTILQACALVGVDIPRFCYHdrlsiaGNCRMCLVEV 82
Cdd:pfam00111 1 VTINGKGVTIevpDGETTLLDAAEEAGIDIPYSCRG------GGCGTCAVKV 46
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
303-335 |
4.67e-04 |
|
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: 43.44 E-value: 4.67e-04
10 20 30
....*....|....*....|....*....|....*.
gi 17565758 303 QRLLTPMIRGA---DGQLKPATWEEALFTVAAKLRE 335
Cdd:cd02755 54 DRLKKPLIRVGergEGKFREASWDEALQYIASKLKE 89
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
549-628 |
5.16e-04 |
|
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: 43.54 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 549 GADEGKVTKA--NLD--------PSAFVVYQGHHGDAGAEMADVV--LPGAAYTEKEGTYVNTeGRS-QRAYPAVSPPGD 615
Cdd:cd02752 347 FPNANKVRRAldKLDwlvvidpfPTETAAFWKNPGMDPKSIQTEVflLPAACQYEKEGSITNS-GRWlQWRYKVVEPPGE 425
|
90
....*....|...
gi 17565758 616 ARVDWKIIRAVSE 628
Cdd:cd02752 426 AKSDGDILVELAK 438
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
304-411 |
1.55e-03 |
|
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: 41.66 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17565758 304 RLLTPMIR-------GADGQLKPATWEEALFTVAAKLRETPAE---QKAAVAGGLNDVESLVALKDLFNRFNSENVMTE- 372
Cdd:cd02757 56 RILYPMKRtnprkgrDVDPKFVPISWDEALDTIADKIRALRKEnepHKIMLHRGRYGHNNSILYGRFTKMIGSPNNISHs 135
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 17565758 373 ---EEFPDVGSggSDLRSNYVFNDgiASVENADAILLVGTNP 411
Cdd:cd02757 136 svcAESEKFGR--YYTEGGWDYNS--YDYANAKYILFFGADP 173
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
554-622 |
4.27e-03 |
|
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: 40.54 E-value: 4.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17565758 554 KVTKANLDPSA-FVVYQGHHGDAGAEMADVVLPGAAYTEKEGTYVNTEGRSQRAY-PAVSPPGDARVDWKI 622
Cdd:cd02756 486 CLIGDAIQPGGlFIVVQDIYPTKLAEDAHVILPAAANGEMNETSMNGHERRLRLYeKFMDPPGEAMPDWWI 556
|
|
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