|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
151-532 |
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: 648.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLKRQRLTQPLVKDdSGQLVPTSWEDALAQVAG 230
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRK-NGKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 231 ALQGAKGGDIAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAgsDLRSNYLLNTGIAGIEEADLLLLVGTNPR 310
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 311 FEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGESPKVLQEIASGIHPFSQAVTKTKHPVVVVGSSCLQREDGAA 390
Cdd:cd02773 158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 391 VMAAVSSIARKAhvsGEVEETWKIVNVLHRVASQVAALDLGYKPGVKTIR-ENPPKVLFLLGADSGSVTRQdlPEDSLVI 469
Cdd:cd02773 238 ILAAVAKLAKKN---GVVREGWNGFNVLHRAASRVGALDLGFVPGAGAIRkSGPPKVLYLLGADEIDITPI--PKDAFVV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357711166 470 YQGHHGDVGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELA 532
Cdd:cd02773 313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
43-528 |
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: 584.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 43 VFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKAR 122
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 123 EGVMEFLLANHPLDCPICDQGGECDLQ----------------------------------------------------- 149
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQdqavmygsdrsrfrekkrtvenkylgpliktemtrcihctrcvrfanevagve 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 150 ------------------------------------------------------TESIDVLDAVGSNIVLSTRGGEVMRV 175
Cdd:TIGR01973 161 dlgvigrgnnveigtyegktleselsgnlidicpvgaltskpyafkarpwelksTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 176 LPRLNEDINEEWISDKTRFAYDGLKRQ-RLTQPLVKDDSGQLVPTSWEDALAQVAGALQGakGGDIAAVVGGLVEAEALV 254
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 255 CLKDLLNCLNSDSLCTEEVFPTAGAgSDLRSNYLLNTGIAGIEEADLLLLVGTNPRFEAPLFNARIRKSWLHNDLHVALL 334
Cdd:TIGR01973 319 ALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 335 GKP-VDLSY-----TYDHLGESPKVLQEIASGIHP-FSQAVTKTKHPVVVVGSSCLQREDGAAVMAAVSSIARkahVSGE 407
Cdd:TIGR01973 398 GIEkWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAK---VIKV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 408 VEETWKIVNVLHRVASQVAALDLGYKP--GVKTIRENPPKVLFLLGADSGS----VTRQDLP-EDSLVIYQGHHGDVGAP 480
Cdd:TIGR01973 475 RRKEWNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLERaldkTARDALSkADAFIIYQGHHGTETAE 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1357711166 481 MADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAI 528
Cdd:TIGR01973 555 KADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
42-560 |
1.71e-124 |
|
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: 375.72 E-value: 1.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 42 EVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKA 121
Cdd:COG1034 3 TITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVKKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQ---------------------------------------------------- 149
Cdd:COG1034 83 RKGVMEFLLINHPLDCPICDQGGECDLQdqameygvdesryeeekrtvpkkdlgplilldmnrcilctrcvrfcdeiagd 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 150 -------------------------------------------------------TESIDVLDAVGSNIVLSTRGGEVMR 174
Cdd:COG1034 163 pelgvigrgehseigtylgkpldsefsgncidvcpvgaltskpfrfkarpwelkkTPSICPHCSVGCNIRVDVRGGKVYR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 175 VLPRLNEDINEEWISDKTRFAYDGLKR-QRLTQPLVKDDsGQLVPTSWEDALAQVAGALQgakggdiaavvgGLVEAEal 253
Cdd:COG1034 243 VLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRKD-GELVEASWEEALAAAAEGLK------------ALKKAE-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 254 vclkdllnclnsdslcteevfptagagsdlrsnyllntgiagieeadllllvgtnprfeaplfNARirkswlhndlhval 333
Cdd:COG1034 308 ---------------------------------------------------------------NSV-------------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 334 lgkpvdlsytydhlgespkvlqeiasgihpfsqavtktkhpvvvvgssclqredGAAVMAAVSSIArkahvsgeveetwk 413
Cdd:COG1034 311 ------------------------------------------------------GAALLGALPDAA-------------- 322
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 414 ivnvlhrvasqvAALDlgykpgvkTIRENPPKVLFLLGAD----SGSVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGA 489
Cdd:COG1034 323 ------------AILE--------AAEAGKLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVLPAA 382
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357711166 490 AYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELAGVKLPYETLDEVRNRLAEVSPNLVRYDE 560
Cdd:COG1034 383 AFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
203-530 |
3.62e-110 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 335.52 E-value: 3.62e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 203 RLTQPLVKDDSGQLVPTSWEDALAQVAGALQG--AKGGD----IAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVF-- 274
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRiiKKYGPdaiaINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 275 ----PTAGAGSDLRSNYLLNTGIAGIEEADLLLLVGTNPRFEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGES 350
Cdd:pfam00384 81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 351 PKVLQEIASGI-HPFSQAVTKTK----HPVVVVGSSCLQREDGAAVMAAVSSIARKAHVSGEVEETWKIVNVLHRVASQV 425
Cdd:pfam00384 161 PGTDLALALAGaHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 426 AALDLGYKPGVK------TIRENPPKVLFLLG-------ADSGSVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGAAYT 492
Cdd:pfam00384 241 GALDLGLVPGIKsveminAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 1357711166 493 EKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISE 530
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
45-553 |
1.12e-60 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 216.35 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 45 VDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILT--NSDKTRKAR 122
Cdd:PRK07860 9 IDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlTSPVADKAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 123 EGVMEFLLANHPLDCPICDQGGECDLQ--------TES------------------------------------------ 152
Cdd:PRK07860 89 HGVMELLLINHPLDCPVCDKGGECPLQnqamsngrAESrftdvkrtfpkpinistqvlldrercvlcarctrfsdqiagd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 153 --IDVL--------------------------------------------------------DAVGSNIVLSTRGGEVMR 174
Cdd:PRK07860 169 pfIDLQergalqqvgiyegepfqsyfsgntvqicpvgaltgaayrfrarpfdlvstpsvcehCASGCAQRTDHRRGKVLR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 175 VLPRLNEDINEEWISDKTRFAYD-GLKRQRLTQPLVKDDSGQLVPTSWEDALAQVAGALQGAKGGdIAAVVGGLVEAE-- 251
Cdd:PRK07860 249 RLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARGR-VGVLVGGRLTVEda 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 252 ------ALVCLK----DLLNCLNSDSlctEEVFPTAG-AGSDLRSNYllntgiAGIEEADLLLLVGTNPRFEAPLFNARI 320
Cdd:PRK07860 328 yayakfARVALGtndiDFRARPHSAE---EADFLAARvAGRGLGVTY------ADLEKAPAVLLVGFEPEEESPIVFLRL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 321 RKSWLHNDLHVALLGKPVD--LSYTYDHL-----GESPKVLQEIASGIHPFSQAVtKTKHPVVVVGssclqrEDGAAVMA 393
Cdd:PRK07860 399 RKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDALATGAPDVAELL-RTPGAVILVG------ERLATVPG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 394 AVSSIARKAHVSGEveetwKIVNVLHRvASQVAALDLGYKP----------------------GVKTIRENPPKVL--FL 449
Cdd:PRK07860 472 ALSAAARLADATGA-----RLAWVPRR-AGERGALEAGALPtllpggrpvadpaaraevaaawGVDELPAAPGRDTagIL 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 450 LGADSGS--------VTRQDLPEDS-----------LVIYQGHHGDVgAPMADIILPGAAYTEKRGTYVNTEGRAQQTRV 510
Cdd:PRK07860 546 AAAAAGElgallvggVEPADLPDPAaalaaldaagfVVSLELRHSAV-TERADVVLPVAPVAEKAGTFLNWEGRLRPFEA 624
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1357711166 511 AVTPPGmAREDWRIIRAISELAGVKLPYETLDEVRNRLAEVSP 553
Cdd:PRK07860 625 ALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
43-154 |
7.94e-35 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 133.62 E-value: 7.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 43 VFVDGKPVMVEPGT-TVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKA 121
Cdd:PTZ00305 71 MFVNKRPVEIIPQEeNLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDA 150
|
90 100 110
....*....|....*....|....*....|...
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQTESID 154
Cdd:PTZ00305 151 REGNVELILINHPNDCPICEQATNCDLQNVSMN 183
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
41-115 |
5.29e-15 |
|
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: 70.26 E-value: 5.29e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357711166 41 LEVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHER----LSVAGNCRMCLVEIEKVQKpVAACAMPVMKGWNILTNS 115
Cdd:pfam13510 4 VTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRTQN 81
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
122-150 |
4.30e-13 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 63.76 E-value: 4.30e-13
10 20
....*....|....*....|....*....
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQT 150
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQD 29
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
580-612 |
4.21e-11 |
|
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: 58.00 E-value: 4.21e-11
10 20 30
....*....|....*....|....*....|...
gi 1357711166 580 ALLTEPLVPPqltVRDFYMTDPVSRASQTMAKC 612
Cdd:pfam09326 12 KLSGAPLKSP---IEDFYMTDPISRASATMAKC 41
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
41-111 |
1.13e-10 |
|
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: 58.18 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 41 LEVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHerlsvaGNCRMCLVEIEK----------------VQKPVAACAMP 104
Cdd:cd00207 3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQTR 76
|
....*..
gi 1357711166 105 VMKGWNI 111
Cdd:cd00207 77 VTDGLVI 83
|
|
| Fdx |
COG0633 |
Ferredoxin [Energy production and conversion]; |
46-92 |
3.24e-03 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440398 [Multi-domain] Cd Length: 87 Bit Score: 37.14 E-value: 3.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1357711166 46 DGKPVMVEPGTTVLQACERAGMQIPRFCyheRlsvAGNCRMCLVEIE 92
Cdd:COG0633 9 EGHTVEVPAGESLLEAALRAGIDLPYSC---R---SGACGTCHVRVL 49
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
151-532 |
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: 648.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLKRQRLTQPLVKDdSGQLVPTSWEDALAQVAG 230
Cdd:cd02773 1 ESIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRK-NGKLKPATWEEALAAIAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 231 ALQGAKGGDIAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAgsDLRSNYLLNTGIAGIEEADLLLLVGTNPR 310
Cdd:cd02773 80 ALKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENLACEQDGPDLPA--DLRSNYLFNTTIAGIEEADAVLLVGTNPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 311 FEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGESPKVLQEIASGIHPFSQAVTKTKHPVVVVGSSCLQREDGAA 390
Cdd:cd02773 158 FEAPVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 391 VMAAVSSIARKAhvsGEVEETWKIVNVLHRVASQVAALDLGYKPGVKTIR-ENPPKVLFLLGADSGSVTRQdlPEDSLVI 469
Cdd:cd02773 238 ILAAVAKLAKKN---GVVREGWNGFNVLHRAASRVGALDLGFVPGAGAIRkSGPPKVLYLLGADEIDITPI--PKDAFVV 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357711166 470 YQGHHGDVGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELA 532
Cdd:cd02773 313 YQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSEVL 375
|
|
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
43-528 |
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: 584.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 43 VFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKAR 122
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 123 EGVMEFLLANHPLDCPICDQGGECDLQ----------------------------------------------------- 149
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQdqavmygsdrsrfrekkrtvenkylgpliktemtrcihctrcvrfanevagve 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 150 ------------------------------------------------------TESIDVLDAVGSNIVLSTRGGEVMRV 175
Cdd:TIGR01973 161 dlgvigrgnnveigtyegktleselsgnlidicpvgaltskpyafkarpwelksTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 176 LPRLNEDINEEWISDKTRFAYDGLKRQ-RLTQPLVKDDSGQLVPTSWEDALAQVAGALQGakGGDIAAVVGGLVEAEALV 254
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKA--SSRIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 255 CLKDLLNCLNSDSLCTEEVFPTAGAgSDLRSNYLLNTGIAGIEEADLLLLVGTNPRFEAPLFNARIRKSWLHNDLHVALL 334
Cdd:TIGR01973 319 ALKKLVRKLGSENFDLRIRNYEFES-ADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 335 GKP-VDLSY-----TYDHLGESPKVLQEIASGIHP-FSQAVTKTKHPVVVVGSSCLQREDGAAVMAAVSSIARkahVSGE 407
Cdd:TIGR01973 398 GIEkWNLTYpantnLVFHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAK---VIKV 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 408 VEETWKIVNVLHRVASQVAALDLGYKP--GVKTIRENPPKVLFLLGADSGS----VTRQDLP-EDSLVIYQGHHGDVGAP 480
Cdd:TIGR01973 475 RRKEWNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLERaldkTARDALSkADAFIIYQGHHGTETAE 554
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1357711166 481 MADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAI 528
Cdd:TIGR01973 555 KADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
151-531 |
2.12e-158 |
|
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: 459.83 E-value: 2.12e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLK-RQRLTQPLVKDDsGQLVPTSWEDALAQVA 229
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNsRQRLTQPLIKKG-GKLVPVSWEEALKTVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 230 GALQGAKGGDIAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAGSDLRSNYLLNTGIAGIEEADLLLLVGTNP 309
Cdd:cd02768 80 EGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADNRLRGNYLFNTSIAEIEEADAVLLIGSNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 310 RFEAPLFNARIRKSWLHNDLHVALLG-----KPVDLSYTYDHLGESPKVLQEIASGIH--PFSQAVTKTKHPVVVVGSSc 382
Cdd:cd02768 160 RKEAPLLNARLRKAVKKKGAKIAVIGpkdtdLIADLTYPVSPLGASLATLLDIAEGKHlkPFAKSLKKAKKPLIILGSS- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 383 LQREDGAAVMAAVSSIARKAHVSGEVeetWKIVNVLHRVASQVAA--LDLGYKPGVKTIREnppkvLFLLGADSGSVTRQ 460
Cdd:cd02768 239 ALRKDGAAILKALANLAAKLGTGAGL---WNGLNVLNSVGARLGGagLDAGLALLEPGKAK-----LLLLGEDELDRSNP 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1357711166 461 DL-----PEDSLVIYQGHHGDVGAPmADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISEL 531
Cdd:cd02768 311 PAavalaAADAFVVYQGHHGDTGAQ-ADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
42-560 |
1.71e-124 |
|
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: 375.72 E-value: 1.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 42 EVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKA 121
Cdd:COG1034 3 TITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVKKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQ---------------------------------------------------- 149
Cdd:COG1034 83 RKGVMEFLLINHPLDCPICDQGGECDLQdqameygvdesryeeekrtvpkkdlgplilldmnrcilctrcvrfcdeiagd 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 150 -------------------------------------------------------TESIDVLDAVGSNIVLSTRGGEVMR 174
Cdd:COG1034 163 pelgvigrgehseigtylgkpldsefsgncidvcpvgaltskpfrfkarpwelkkTPSICPHCSVGCNIRVDVRGGKVYR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 175 VLPRLNEDINEEWISDKTRFAYDGLKR-QRLTQPLVKDDsGQLVPTSWEDALAQVAGALQgakggdiaavvgGLVEAEal 253
Cdd:COG1034 243 VLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRKD-GELVEASWEEALAAAAEGLK------------ALKKAE-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 254 vclkdllnclnsdslcteevfptagagsdlrsnyllntgiagieeadllllvgtnprfeaplfNARirkswlhndlhval 333
Cdd:COG1034 308 ---------------------------------------------------------------NSV-------------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 334 lgkpvdlsytydhlgespkvlqeiasgihpfsqavtktkhpvvvvgssclqredGAAVMAAVSSIArkahvsgeveetwk 413
Cdd:COG1034 311 ------------------------------------------------------GAALLGALPDAA-------------- 322
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 414 ivnvlhrvasqvAALDlgykpgvkTIRENPPKVLFLLGAD----SGSVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGA 489
Cdd:COG1034 323 ------------AILE--------AAEAGKLKALVLLGADpydlDPAAALAALAKADFVVVLDHFGSATAERADVVLPAA 382
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1357711166 490 AYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELAGVKLPYETLDEVRNRLAEVSPNLVRYDE 560
Cdd:COG1034 383 AFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPATVSAEG 453
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
203-530 |
3.62e-110 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 335.52 E-value: 3.62e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 203 RLTQPLVKDDSGQLVPTSWEDALAQVAGALQG--AKGGD----IAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVF-- 274
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRiiKKYGPdaiaINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 275 ----PTAGAGSDLRSNYLLNTGIAGIEEADLLLLVGTNPRFEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGES 350
Cdd:pfam00384 81 lctaAAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 351 PKVLQEIASGI-HPFSQAVTKTK----HPVVVVGSSCLQREDGAAVMAAVSSIARKAHVSGEVEETWKIVNVLHRVASQV 425
Cdd:pfam00384 161 PGTDLALALAGaHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 426 AALDLGYKPGVK------TIRENPPKVLFLLG-------ADSGSVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGAAYT 492
Cdd:pfam00384 241 GALDLGLVPGIKsveminAIKKGGIKVLYLLGnnpfvthADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 1357711166 493 EKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISE 530
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
151-528 |
7.82e-72 |
|
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: 236.11 E-value: 7.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLKRQRLTQPLVKDDSGQLVPTSWEDALAQVAG 230
Cdd:cd02774 1 ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIGWKTAFKFLNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 231 ALQGAKGGDIAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAGSDLRSNYLLNTGIAGIEEADLLLLVGTNPR 310
Cdd:cd02774 81 FILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFLENNNYFNLDLENYLFNNSLKNLDKSDLCLLIGSNLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 311 FEAPLFNARIRKSWLHNDLHVALLGKPVDLSYTYDHLGESPKVLQEIASGIHPFSQAVTKTKHPVVVVGSSCLQREDGAa 390
Cdd:cd02774 161 VESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEGKHLFCKQLKKSKKPLIIIGSSFSLRKNYS- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 391 vmaavSSIARKAHVSGEVEETWKIVNVLHRVasqvaALDLG-YKPGVKTIRenppKVLFLLGADSGSVTRQDlpEDSLVI 469
Cdd:cd02774 240 -----FIISKLKNFSSNNENNFNFLNIISNS-----LYYLGiKKFNSNNKK----NLSNLYYIKETNFQKFN--KNNFVI 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1357711166 470 YQGHHGDVGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAI 528
Cdd:cd02774 304 YQGHHFLNLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSDDNIIFSL 362
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
151-530 |
2.22e-64 |
|
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: 216.43 E-value: 2.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 151 ESIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLK-RQRLTQPLVKD-DSGQLVPTSWEDALAQV 228
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYsPDRLKYPLIRVgGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 229 AGALQGAK---GGD-IAAVVGGLVEAEALVCLKDLLNCLNSDSLCTEEVFPTAGAGSDLR--SNYLLNTGIAGIEEADLL 302
Cdd:cd00368 81 AEKLKEIRekyGPDaIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKafGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 303 LLVGTNPRFEAPLFNARIRKSWL-----------------HNDLHVA---------LLGKPVDlsytyDHLGESPKVLQE 356
Cdd:cd00368 161 LLWGSNPAETHPVLAARLRRAKKrgaklividprrtetaaKADEWLPirpgtdaalALAEWAA-----EITGVPAETIRA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 357 IAsgihpfsQAVTKTKHPVVVVGSSCLQREDGAAVMAAVSSIArkahvsgeveetwkivnvlhrvasqvAALDLGYKPGV 436
Cdd:cd00368 236 LA-------REFAAAKRAVILWGMGLTQHTNGTQNVRAIANLA--------------------------ALTGNIGRPGG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 437 KTI-RENPpkvlFLLGADSGSVTRQDLPEDSLVIYQGHHGDVGApMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPP 515
Cdd:cd00368 283 GLGpGGNP----LVSAPDANRVRAALKKLDFVVVIDIFMTETAA-YADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPP 357
|
410
....*....|....*
gi 1357711166 516 GMAREDWRIIRAISE 530
Cdd:cd00368 358 GEARSDWEILRELAK 372
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
45-553 |
1.12e-60 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 216.35 E-value: 1.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 45 VDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILT--NSDKTRKAR 122
Cdd:PRK07860 9 IDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlTSPVADKAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 123 EGVMEFLLANHPLDCPICDQGGECDLQ--------TES------------------------------------------ 152
Cdd:PRK07860 89 HGVMELLLINHPLDCPVCDKGGECPLQnqamsngrAESrftdvkrtfpkpinistqvlldrercvlcarctrfsdqiagd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 153 --IDVL--------------------------------------------------------DAVGSNIVLSTRGGEVMR 174
Cdd:PRK07860 169 pfIDLQergalqqvgiyegepfqsyfsgntvqicpvgaltgaayrfrarpfdlvstpsvcehCASGCAQRTDHRRGKVLR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 175 VLPRLNEDINEEWISDKTRFAYD-GLKRQRLTQPLVKDDSGQLVPTSWEDALAQVAGALQGAKGGdIAAVVGGLVEAE-- 251
Cdd:PRK07860 249 RLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAARGR-VGVLVGGRLTVEda 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 252 ------ALVCLK----DLLNCLNSDSlctEEVFPTAG-AGSDLRSNYllntgiAGIEEADLLLLVGTNPRFEAPLFNARI 320
Cdd:PRK07860 328 yayakfARVALGtndiDFRARPHSAE---EADFLAARvAGRGLGVTY------ADLEKAPAVLLVGFEPEEESPIVFLRL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 321 RKSWLHNDLHVALLGKPVD--LSYTYDHL-----GESPKVLQEIASGIHPFSQAVtKTKHPVVVVGssclqrEDGAAVMA 393
Cdd:PRK07860 399 RKAARKHGLKVYSIAPFATrgLEKMGGTLlrtapGGEAAALDALATGAPDVAELL-RTPGAVILVG------ERLATVPG 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 394 AVSSIARKAHVSGEveetwKIVNVLHRvASQVAALDLGYKP----------------------GVKTIRENPPKVL--FL 449
Cdd:PRK07860 472 ALSAAARLADATGA-----RLAWVPRR-AGERGALEAGALPtllpggrpvadpaaraevaaawGVDELPAAPGRDTagIL 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 450 LGADSGS--------VTRQDLPEDS-----------LVIYQGHHGDVgAPMADIILPGAAYTEKRGTYVNTEGRAQQTRV 510
Cdd:PRK07860 546 AAAAAGElgallvggVEPADLPDPAaalaaldaagfVVSLELRHSAV-TERADVVLPVAPVAEKAGTFLNWEGRLRPFEA 624
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1357711166 511 AVTPPGmAREDWRIIRAISELAGVKLPYETLDEVRNRLAEVSP 553
Cdd:PRK07860 625 ALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
152-531 |
5.05e-57 |
|
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: 197.96 E-value: 5.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 152 SIDVLDAVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLKRQ-RLTQPLVKDDsGQLVPTSWEDALAQVAG 230
Cdd:cd02772 2 SVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEdRLTKPMIKKD-GQWQEVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 231 ALQGAKGGDIAAVVGGLVEA----EALVCLKDLLNCLNSDSLCTEEVFPTAGAGSDLRSNYLLNTGIAGIEEADLLLLVG 306
Cdd:cd02772 81 GLSAIIKKHGADQIGALASPhstlEELYLLQKLARGLGSDNIDHRLRQSDFRDDAKASGAPWLGMPIAEISELDRVLVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 307 TNPRFEAPLFNARIRK--------SWLH---NDLHVALLGK----PVDLSYTydhLGESPKVLQEIASGIHPFSQ----A 367
Cdd:cd02772 161 SNLRKEHPLLAQRLRQavkkgaklSAINpadDDFLFPLSGKaivaPSALANA---LAQVAKALAEEKGLAVPDEDakveA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 368 VTKTKH----------PVVVVGSSCLQREDGAAVMAAVSSIARkahVSGEVeetwkiVNVLHRVASQVAALDLGYKPGV- 436
Cdd:cd02772 238 SEEARKiaaslvsaerAAVFLGNLAQNHPQAATLRALAQEIAK---LTGAT------LGVLGEGANSVGAYLAGALPHGg 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 437 ---KTIRENPPKVLFLLGA------DSGSVTRQDLPEDSLVIYQGHHgdVGAPM---ADIILPGAAYTEKRGTYVNTEGR 504
Cdd:cd02772 309 lnaAAMLEQPRKAYLLLNVepeldcANPAQALAALNQAEFVVALSAF--ASAALldyADVLLPIAPFTETSGTFVNLEGR 386
|
410 420
....*....|....*....|....*..
gi 1357711166 505 AQQTRVAVTPPGMAREDWRIIRAISEL 531
Cdd:cd02772 387 VQSFKGVVKPLGEARPAWKVLRVLGNL 413
|
|
| 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 ... |
158-553 |
4.21e-41 |
|
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: 155.62 E-value: 4.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 158 AVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLK-RQRLTQPLVKDDsGQLVPTSWEDALAQVAGALQGAK 236
Cdd:cd02771 8 SVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNsRDRLTQPLIRRG-GTLVPVSWNEALDVAAARLKEAK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 237 GGdIAAVVGGLVEAEALVCLKDL----LNCLNSDSLCTEevfptaGAGSDLRSNYLLNTGIAGIEEADLLLLVGTNPRFE 312
Cdd:cd02771 87 DK-VGGIGSPRASNESNYALQKLvgavLGTNNVDHRARR------LIAEILRNGPIYIPSLRDIESADAVLVLGEDLTQT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 313 APLFNARIRKSWLHNDLHVALL-GKPVDLSYTYDHLGESPKV-----------LQEIA---------------------- 358
Cdd:cd02771 160 APRIALALRQAARRKAVELAALsGIPKWQDAAVRNIAQGAKSplfivnalatrLDDIAaesiraspggqarlgaalarav 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 359 -------SGIHPFS------QAVTKTKHPVVVVGSSCLQREdgaavmaAVSSIARKAHVSGEVEETWKIVNVLHRVASQV 425
Cdd:cd02771 240 dasaagvSGLAPKEkaariaARLTGAKKPLIVSGTLSGSLE-------LIKAAANLAKALKRRGENAGLTLAVEEGNSPG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 426 AAL--DLGYKPG------VKTIRENPPKVLFLLGAD---SGSVTRQD--LPEDSLVIYQGHHGDVGAPMADIILPGAAYT 492
Cdd:cd02771 313 LLLlgGHVTEPGldldgaLAALEDGSADALIVLGNDlyrSAPERRVEaaLDAAEFVVVLDHFLTETAERADVVLPAASFA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357711166 493 EKRGTYVNTEGRAQQTRVAV-TPPGMAREDWRIIRAISELAGVKL---PYETLDEVRNRLAEVSP 553
Cdd:cd02771 393 EKSGTFVNYEGRAQRFFKAYdDPAGDARSDWRWLHALAAKLGGKLvpsDAAILDEIIALVPGKAP 457
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
43-154 |
7.94e-35 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 133.62 E-value: 7.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 43 VFVDGKPVMVEPGT-TVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKA 121
Cdd:PTZ00305 71 MFVNKRPVEIIPQEeNLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDA 150
|
90 100 110
....*....|....*....|....*....|...
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQTESID 154
Cdd:PTZ00305 151 REGNVELILINHPNDCPICEQATNCDLQNVSMN 183
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
158-563 |
1.37e-34 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 139.63 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 158 AVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGL-KRQRLTQPLVKDDsGQLVPTSWEDALAQVAGALQGAK 236
Cdd:COG3383 15 GVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVnSPDRLTTPLIRRG-GEFREVSWDEALDLVAERLREIQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 237 ---GGD-IAAVVGG--LVEAEALVC--LKDLLNCLNSDS---LCTEevfPTAGA-----GSDLRSNyllntGIAGIEEAD 300
Cdd:COG3383 94 aehGPDaVAFYGSGqlTNEENYLLQklARGVLGTNNIDNnarLCMA---SAVAGlkqsfGSDAPPN-----SYDDIEEAD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 301 LLLLVGTNPRFEAPLFNARIRKSWLHN-----------------DLH--------VALL---------GKPVDLSYTYDH 346
Cdd:COG3383 166 VILVIGSNPAEAHPVLARRIKKAKKNGaklivvdprrtetarlaDLHlqikpgtdLALLngllhviieEGLVDEDFIAER 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 347 -----------LGESPKVLQEI----ASGIHPFSQAVTKTKHPVVVVGSSCLQREDGAAvmaAVSSIARKAHVSGEVEET 411
Cdd:COG3383 246 tegfeelkasvAKYTPERVAEItgvpAEDIREAARLIAEAKRAMILWGMGVNQHTQGTD---NVNAIINLALATGNIGRP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 412 WKIVNVLH--------RVASQVAALDLGYKP--------------GVKTIRENP---------------PKVLFLLG--- 451
Cdd:COG3383 323 GTGPFPLTgqnnvqggRDMGALPNVLPGYRDvtdpehrakvadawGVPPLPDKPgltavemfdaiadgeIKALWIIGenp 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 452 ----ADSGSVtRQDLPEDSLVIYQghhgDV----GAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWR 523
Cdd:COG3383 403 avsdPDANHV-REALEKLEFLVVQ----DIflteTAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWE 477
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1357711166 524 IIRAISELAGVKLPYETLDEVRNRLAEVSPNL--VRYDEVEE 563
Cdd:COG3383 478 IIAELARRLGYGFDYDSPEEVFDEIARLTPDYsgISYERLEA 519
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
158-563 |
2.11e-24 |
|
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: 107.30 E-value: 2.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 158 AVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDKTRFAYDGLK-RQRLTQPLVKDDsGQLVPTSWEDALAQVAGALQGAK 236
Cdd:cd02753 8 GVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNsKDRLTKPLIRKN-GKFVEASWDEALSLVASRLKEIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 237 GGDIAAVVGGLVEA-----EALVCLKDLLNCL---NSDS---LC----TEEVFPTAGAGSDLRSnyllntgIAGIEEADL 301
Cdd:cd02753 87 DKYGPDAIAFFGSAkctneENYLFQKLARAVGgtnNVDHcarLChsptVAGLAETLGSGAMTNS-------IADIEEADV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 302 LLLVGTNPRFEAPLFNARI---------------RKSWLHN--DLH--------VALLG--------------------- 335
Cdd:cd02753 160 ILVIGSNTTEAHPVIARRIkrakrngaklivadpRRTELARfaDLHlqlrpgtdVALLNamahviieeglydeefieert 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 336 ----------KPVDLSYTYDHLGESPKVLQEIASGIHpfsqavtkTKHPVVVV-GSSCLQREDGA-AVMAavssIARKAH 403
Cdd:cd02753 240 egfeelkeivEKYTPEYAERITGVPAEDIREAARMYA--------TAKSAAILwGMGVTQHSHGTdNVMA----LSNLAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 404 VSGEVEETWKIVNVLhRVASQV-AALDLG----YKPG-VKTIR---ENPpkvlFLLGADSGSVtRQDLPEDSLVIYQghh 474
Cdd:cd02753 308 LTGNIGRPGTGVNPL-RGQNNVqGACDMGalpnVLPGyVKALYimgENP----ALSDPNTNHV-RKALESLEFLVVQ--- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 475 gDV----GAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMAREDWRIIRAISELAGVKLPYETLDEVRNRLAE 550
Cdd:cd02753 379 -DIflteTAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSHPEEIFDEIAR 457
|
490
....*....|....*
gi 1357711166 551 VSPNL--VRYDEVEE 563
Cdd:cd02753 458 LTPQYagISYERLER 472
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
45-155 |
1.07e-23 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 100.11 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 45 VDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKAREG 124
Cdd:PRK07569 8 IDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQEYRRM 87
|
90 100 110
....*....|....*....|....*....|...
gi 1357711166 125 VMEFLLA--NHPldCPICDQGGECDLQTESIDV 155
Cdd:PRK07569 88 IVELLFAegNHV--CAVCVANGNCELQDLAIEV 118
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
45-149 |
2.13e-22 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 102.09 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 45 VDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKvqKPVAACAMPVMKGWNILTNSDKTRKAREG 124
Cdd:PRK08493 6 INGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEADG--KRVYSCNTKAKEGMNILTNTPNLMDERNA 83
|
90 100
....*....|....*....|....*
gi 1357711166 125 VMEFLLANHPLDCPICDQGGECDLQ 149
Cdd:PRK08493 84 IMQTYDVNHPLECGVCDKSGECELQ 108
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
158-553 |
6.57e-21 |
|
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: 96.91 E-value: 6.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 158 AVGSNIVLSTRGGEVMRVLPRLNEDINEEWISDK-TRFAYDGLKRQRLTQPLVKDDSGQLVPTSWEDALAQVAG---ALQ 233
Cdd:cd02754 8 GVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKgLNLHKTLNGPERLTRPLLRRNGGELVPVSWDEALDLIAErfkAIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 234 GAKGGDIAAVVGG---LVEAEALV--CLKDLLNCLNSDS---LCTEevfpTAGAGsdlrsnYLLNTGIAG-------IEE 298
Cdd:cd02754 88 AEYGPDSVAFYGSgqlLTEEYYAAnkLAKGGLGTNNIDTnsrLCMA----SAVAG------YKRSFGADGppgsyddIEH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 299 ADLLLLVGTNPRFEAPLFNARIRKSWLHN-------------------DLH--------VALL----------------- 334
Cdd:cd02754 158 ADCFFLIGSNMAECHPILFRRLLDRKKANpgakiivvdprrtrtadiaDLHlpirpgtdLALLngllhvlieeglidrdf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 335 ---------------------------GKPV-DLSYTYDHLGESPKVLQEIASGIHPFSQAVTKTKHPVVVV-------- 378
Cdd:cd02754 238 idahtegfeelkafvadytpekvaeitGVPEaDIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHlatgkigr 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 379 -GSSCLQ----------REDG--AAVMAAVSSIARKAHVSgEVEETWKivnvlhrvasqVAALDLGYKPGVKT------I 439
Cdd:cd02754 318 pGSGPFSltgqpnamggREVGglANLLPGHRSVNNPEHRA-EVAKFWG-----------VPEGTIPPKPGLHAvemfeaI 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 440 RENPPKVLFLLG-------ADSGSVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAV 512
Cdd:cd02754 386 EDGEIKALWVMCtnpavslPNANRVREALERLEFVVVQDAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAV 465
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1357711166 513 TPPGMAREDWRIIRAISELAGVK--LPYETLDEVRNRLAEVSP 553
Cdd:cd02754 466 EPPGEARPDWWILADVARRLGFGelFPYTSPEEVFEEYRRLSR 508
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
45-148 |
5.94e-17 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 84.78 E-value: 5.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 45 VDGKPVMVEPGTTVLQACERAGMQIPRFCYHERLSVAGNCRMCLVEIEKVQKPVAACAMPVMKGWNILTNSDKTRKAREG 124
Cdd:PRK12814 8 INGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETENAELHAMRRQ 87
|
90 100
....*....|....*....|....
gi 1357711166 125 VMEFLLANHPLDCPicdqgGECDL 148
Cdd:PRK12814 88 SLERLIEQHCGDCL-----GPCEL 106
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
41-115 |
5.29e-15 |
|
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: 70.26 E-value: 5.29e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1357711166 41 LEVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHER----LSVAGNCRMCLVEIEKVQKpVAACAMPVMKGWNILTNS 115
Cdd:pfam13510 4 VTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRTQN 81
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
122-149 |
1.60e-13 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 64.78 E-value: 1.60e-13
10 20
....*....|....*....|....*...
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQ 149
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQ 28
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
122-150 |
4.30e-13 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 63.76 E-value: 4.30e-13
10 20
....*....|....*....|....*....
gi 1357711166 122 REGVMEFLLANHPLDCPICDQGGECDLQT 150
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQD 29
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
203-566 |
9.50e-12 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 67.95 E-value: 9.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 203 RLTQPLVKDD---SGQLVPTSWEDALAQVAGALQGAK---GGD-IAAVVGG----LVEAEALVCLKDLLNCL------NS 265
Cdd:COG0243 78 RLTYPMKRVGprgSGKFERISWDEALDLIAEKLKAIIdeyGPEaVAFYTSGgsagRLSNEAAYLAQRFARALgtnnldDN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 266 DSLCTE--EVFPTAGAGSDLRSNyllntGIAGIEEADLLLLVGTNP---------RFEA-------------PLFNARIR 321
Cdd:COG0243 158 SRLCHEsaVAGLPRTFGSDKGTV-----SYEDLEHADLIVLWGSNPaenhprllrRLREaakkrgakivvidPRRTETAA 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 322 KSwlhnDLHVALlgKP-------------------VDL----SYT--YDHLGE-----SPKVLQEIaSGIhP------FS 365
Cdd:COG0243 233 IA----DEWLPI--RPgtdaalllalahvlieeglYDRdflaRHTvgFDELAAyvaayTPEWAAEI-TGV-PaedireLA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 366 QAVTKTKhPVVVVGSSCLQR-EDG-------AAVMAAVSSIARK----AHVSGEveetwkivnvlhrvasqvaALDLGYK 433
Cdd:COG0243 305 REFATAK-PAVILWGMGLQQhSNGtqtvraiANLALLTGNIGKPgggpFSLTGE-------------------AILDGKP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 434 PGVKtirenppkVLFLLG-------ADSGsVTRQDLPEDSLVIYQGHHGDVGAPMADIILPGAAYTEKRGTYVNTE-GRA 505
Cdd:COG0243 365 YPIK--------ALWVYGgnpavsaPDTN-RVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRV 435
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1357711166 506 QQTRVAVTPPGMAREDWRIIRAISELAGVKLPY---ETLDE-VRNRLAEVSPNLVRYDEVEEANY 566
Cdd:COG0243 436 HLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFpwgRTEEDyLRELLEATRGRGITFEELREKGP 500
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
580-612 |
4.21e-11 |
|
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: 58.00 E-value: 4.21e-11
10 20 30
....*....|....*....|....*....|...
gi 1357711166 580 ALLTEPLVPPqltVRDFYMTDPVSRASQTMAKC 612
Cdd:pfam09326 12 KLSGAPLKSP---IEDFYMTDPISRASATMAKC 41
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
41-111 |
1.13e-10 |
|
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: 58.18 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1357711166 41 LEVFVDGKPVMVEPGTTVLQACERAGMQIPRFCYHerlsvaGNCRMCLVEIEK----------------VQKPVAACAMP 104
Cdd:cd00207 3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQTR 76
|
....*..
gi 1357711166 105 VMKGWNI 111
Cdd:cd00207 77 VTDGLVI 83
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
43-91 |
2.14e-06 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 45.59 E-value: 2.14e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1357711166 43 VFVDGKPVMVE---PGTTVLQACERAGMQIPRFCYHerlsvaGNCRMCLVEI 91
Cdd:pfam00111 1 VTINGKGVTIEvpdGETTLLDAAEEAGIDIPYSCRG------GGCGTCAVKV 46
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
477-525 |
5.97e-06 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 49.51 E-value: 5.97e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1357711166 477 VGAPMADIILPGAAYTEKRGTYVNTEGRAQQTRVAVTPPGMARED-WRII 525
Cdd:PRK13532 516 VSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV 565
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
476-541 |
1.65e-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: 47.70 E-value: 1.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1357711166 476 DVGAPMADIILPGAAYTEKRG-------TYVNTEGRAqqtrvaVTPPGMAREDWRIIRAISElagvKLPYETL 541
Cdd:cd02750 374 DSTALYSDIVLPAATWYEKHDlsttdmhPFIHPFSPA------VDPLWEAKSDWEIFKALAK----KVPWRTL 436
|
|
| Fdx |
COG0633 |
Ferredoxin [Energy production and conversion]; |
46-92 |
3.24e-03 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440398 [Multi-domain] Cd Length: 87 Bit Score: 37.14 E-value: 3.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1357711166 46 DGKPVMVEPGTTVLQACERAGMQIPRFCyheRlsvAGNCRMCLVEIE 92
Cdd:COG0633 9 EGHTVEVPAGESLLEAALRAGIDLPYSC---R---SGACGTCHVRVL 49
|
|
|