|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
219-637 |
0e+00 |
|
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: 669.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 219 PSIAPHDCVGGNIFLHSRWQEfvpqreVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKDGKWEAISWEDA 298
Cdd:cd02772 1 KSVSPHDALGSNLVVHVKNNK------VMRVVPRENEAINECWLSDRDRFSYEGLNSEDRLTKPMIKKDGQWQEVDWETA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 299 LRIVKEKTQAIIEKHGASQTGALLSPSATIEEYFLFQKWLRGLGSHNIDHRVRWQDFRDQNTFDAFPNLGMPITELENLN 378
Cdd:cd02772 75 LEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLARGLGSDNIDHRLRQSDFRDDAKASGAPWLGMPIAEISELD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 379 AILLIGSNVRFEQPLLSHRMNKAYGEGAKILAINPMDYPFVFGINEKMIVSPSALIPALADVAKALAKEKS--------- 449
Cdd:cd02772 155 RVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPADDDFLFPLSGKAIVAPSALANALAQVAKALAEEKGlavpdedak 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 450 ---SEKAKVIAETLVSAEKAAIFLGEHALHHPEAAKIREWAHFIAQQSGATVGLLTEGANSAGAWLAGALPHrrpggqrl 526
Cdd:cd02772 235 veaSEEARKIAASLVSAERAAVFLGNLAQNHPQAATLRALAQEIAKLTGATLGVLGEGANSVGAYLAGALPH-------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 527 dsPGLDAKAMLtTDPLKAYFLLNLEPEFDCAYPAQALHTLNQAEWVVAFTTFTTPTMESYADILLPIAPFSESGGTYVNA 606
Cdd:cd02772 307 --GGLNAAAML-EQPRKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALLDYADVLLPIAPFTETSGTFVNL 383
|
410 420 430
....*....|....*....|....*....|.
gi 1269139799 607 EGRWQWASAASVPEKDAQPAWKVLRVLGNYF 637
Cdd:cd02772 384 EGRVQSFKGVVKPLGEARPAWKVLRVLGNLL 414
|
|
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
4-633 |
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: 650.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 4 LEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVEKSGKPLPACATPVTAGMKVFTQSKKALEAQ 83
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 84 RAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHSNYEDTKRAVFSDDIGPLIETEMTRCIQCTRCVRFGEEIAGLP 163
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 164 ELGVINRGEKEAISTYVKHFMRSELSGNIIDICPVGALTDKPARYQGRGWEYRETPSIAPHDCVGGNIFLHSRWQefvpq 243
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNG----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 244 rEVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIK-KDGKWEAISWEDALRIVKEKTQAIiekhgaSQTGALL 322
Cdd:TIGR01973 236 -EIMRILPRENDEINEEWLCDKGRFGYDGLNRQDRLTKPLLRnQEGNLLEVSWAEALAIAAEKLKAS------SRIGGIA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 323 SPSATIEEYFLFQKWLRGLGSHNIDHRVRwqdFRDQNTFDAFPN--LGMPITELENLNAILLIGSNVRFEQPLLSHRMNK 400
Cdd:TIGR01973 309 GPRSSLEELFALKKLVRKLGSENFDLRIR---NYEFESADLRANylFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 401 AY-GEGAKILAINPMDYPFVFGINEKMIVSPSALIPALADVAkalakeksSEKAKVIAETLVSAEKAAIFLGEHALHHPE 479
Cdd:TIGR01973 386 AVkKGGAKVALIGIEKWNLTYPANTNLVFHPGLSPKKLDDIA--------SGAHSDIAAALKAAKKPLIIVGDSAISHLD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 480 AAKIREWAHFIAQQSG------ATVGLLTEGANSAGAWLAGALPHrrpggqrldspGLDAKAMLTTdpLKAYFLLNLEPE 553
Cdd:TIGR01973 458 GAALISAAANIAKVIKvrrkewNGLNILSSGANSVGLLDLGGEST-----------GLDAALNLGA--ADALFLLGADLE 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 554 FdcAYPAQALHTLNQAEWVVAFTTFT-TPTMESyADILLPIAPFSESGGTYVNAEGRWQWASAASVPEKDAQPAWKVLRV 632
Cdd:TIGR01973 525 R--ALDKTARDALSKADAFIIYQGHHgTETAEK-ADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRA 601
|
.
gi 1269139799 633 L 633
Cdd:TIGR01973 602 L 602
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
1-654 |
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: 602.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 1 MVELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVEKSGKPLPACATPVTAGMKVFTQSKKAL 80
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 81 EAQRAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHSNYEDTKRAVFSDDIGPLIETEMTRCIQCTRCVRFGEEIA 160
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 161 GLPELGVINRGEKEAISTYVKHFMRSELSGNIIDICPVGALTDKPARYQGRGWEYRETPSIAPHDCVGGNIFLHSRwqef 240
Cdd:COG1034 161 GDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVR---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 241 vpQREVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKDGKWEAISWEDALrivkektqaiiekhgasqtga 320
Cdd:COG1034 237 --GGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELVEASWEEAL--------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 321 llspsatieeyflfqkwlrglgshnidhrvrwqdfrdqntfdafpnlgmpitelenlnailligsnvrfeqpllshrmnk 400
Cdd:COG1034 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 401 aygegakilainpmdypfvfginekmivspsaliPALADVAKALAKEKssekakviaetlvsaekaaiflgehalhhpea 480
Cdd:COG1034 294 ----------------------------------AAAAEGLKALKKAE-------------------------------- 307
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 481 akirewahfiaqqsgatvglltegaNSAGAWLAGALPhrrpggqrldspglDAKAMLTTD---PLKAYFLLNLEPEFdcA 557
Cdd:COG1034 308 -------------------------NSVGAALLGALP--------------DAAAILEAAeagKLKALVLLGADPYD--L 346
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 558 YPAQALHTLNQAEWVVAFTTFTTPTMEsYADILLPIAPFSESGGTYVNAEGRWQWASAASVPEKDAQPAWKVLRVLGNYF 637
Cdd:COG1034 347 DPAAALAALAKADFVVVLDHFGSATAE-RADVVLPAAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANAL 425
|
650
....*....|....*..
gi 1269139799 638 dLPSFDYKTIEEVTREI 654
Cdd:COG1034 426 -GAGLPYDSLEEVRAEL 441
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
1-764 |
1.33e-112 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 360.80 E-value: 1.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 1 MVELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVEKSGKPLPACATPVTAGMKVFTQ--SKK 78
Cdd:PRK07860 4 LVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTQltSPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 79 ALEAQRAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHSNYEDTKRaVFSDDIGplIETEM----TRCIQCTRCVR 154
Cdd:PRK07860 84 ADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKR-TFPKPIN--ISTQVlldrERCVLCARCTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 155 FGEEIAGLPELGVINRGEKEAISTYVKHFMRSELSGNIIDICPVGALTDKPARYQGRGWEYRETPSIAPHDCVGGNIFL- 233
Cdd:PRK07860 161 FSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASGCAQRTd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 234 HSRWQefvpqreVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIK-KDGKWEAISWEDALRIVKEKTQAiiek 312
Cdd:PRK07860 241 HRRGK-------VLRRLAGDDPEVNEEWNCDKGRWAFTYATQPDRITTPLVRdEDGELEPASWSEALAVAARGLAA---- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 313 hGASQTGALLSPSATIEEYFLFQKWLR-GLGSHNIDHRVRWQDfRDQNTFDAFPNLGMPI----TELENLNAILLIGSNV 387
Cdd:PRK07860 310 -ARGRVGVLVGGRLTVEDAYAYAKFARvALGTNDIDFRARPHS-AEEADFLAARVAGRGLgvtyADLEKAPAVLLVGFEP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 388 RFEQPLLSHRMNKAY-GEGAKILAINpmdyPFVFGINEKMivsPSALIPAL----ADVAKALAkekssEKAKVIAETLvS 462
Cdd:PRK07860 388 EEESPIVFLRLRKAArKHGLKVYSIA----PFATRGLEKM---GGTLLRTApggeAAALDALA-----TGAPDVAELL-R 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 463 AEKAAIFLGEHALHHPEA--AKIRewahfIAQQSGATVGLLTEGANSAGAWLAGALPHRRPGGQRL-------------- 526
Cdd:PRK07860 455 TPGAVILVGERLATVPGAlsAAAR-----LADATGARLAWVPRRAGERGALEAGALPTLLPGGRPVadpaaraevaaawg 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 527 -----DSPGLDAKAMLTTDP---LKAYFLLNLEPEfDCAYPAQALHTLNQAEWVVAFTTFTTPTMEsYADILLPIAPFSE 598
Cdd:PRK07860 530 vdelpAAPGRDTAGILAAAAageLGALLVGGVEPA-DLPDPAAALAALDAAGFVVSLELRHSAVTE-RADVVLPVAPVAE 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 599 SGGTYVNAEGRWQwASAASVPEKDAQPAWKVLRVLGNYFDLPSFdYKTIEEVTREINDM-AHDKSRIEEGHSRSPISVEE 677
Cdd:PRK07860 608 KAGTFLNWEGRLR-PFEAALRTTGALSDLRVLDALADEMGVDLG-LPTVAAARAELARLgAWDGARAAAPAVPAAAPPQP 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 678 KPigendEEALtrFAPWPMVRVDHlvrRSLPLQETLAKEFKT--IRLNTKTAKKFNFNEGDQLTAIQGESRITLPLAIDD 755
Cdd:PRK07860 686 GA-----GEAV--LATWRMLLDDG---RLQDGEPHLAGTARPpvARLSAATAAEIGVADGDAVTVSTERGSITLPLAITD 755
|
....*....
gi 1269139799 756 rLADNTVLL 764
Cdd:PRK07860 756 -MPDRVVWL 763
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
216-762 |
7.05e-61 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 218.21 E-value: 7.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 216 RETPSIAPHdC-VGGNIFLHSRwqefvpQREVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKDGKWEAIS 294
Cdd:COG3383 5 KKVKTVCPY-CgVGCGIDLEVK------DGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 295 WEDALRIVKEKTQAIIEKHGASQTGALLSPSATIEEYFLFQKWLRG-LGSHNIDHRVRW------QDFRDQNTFDAFPNl 367
Cdd:COG3383 78 WDEALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARLcmasavAGLKQSFGSDAPPN- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 368 gmPITELENLNAILLIGSNVRFEQPLLSHRMNKAYGEGAKILAINP------------------MDYPFVFGI------- 422
Cdd:COG3383 157 --SYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPrrtetarladlhlqikpgTDLALLNGLlhviiee 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 423 ---NEKMIVSPSALIPALADVAKALAKEKSSEKAKV-------IAETLVSAEKAAIFLGEHALHHPEA-AKIREWAHfIA 491
Cdd:COG3383 235 glvDEDFIAERTEGFEELKASVAKYTPERVAEITGVpaedireAARLIAEAKRAMILWGMGVNQHTQGtDNVNAIIN-LA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 492 QQSG------ATVGLLTEGANSAGAWLAGALPHRRPGGQRLDS-------------------PGLDAKAML---TTDPLK 543
Cdd:COG3383 314 LATGnigrpgTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDpehrakvadawgvpplpdkPGLTAVEMFdaiADGEIK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 544 AYFLLnlepefdCAYPAQ-------ALHTLNQAEWVVAFTTFTTPTMEsYADILLPIAPFSESGGTYVNAEGRWQWASAA 616
Cdd:COG3383 394 ALWII-------GENPAVsdpdanhVREALEKLEFLVVQDIFLTETAE-YADVVLPAASWAEKDGTFTNTERRVQRVRKA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 617 SVPEKDAQPAWKVLRVLGNYFDLPsFDYKTIEEVTREINDMAHDKSRI----------------EEGHSRSPI------- 673
Cdd:COG3383 466 VEPPGEARPDWEIIAELARRLGYG-FDYDSPEEVFDEIARLTPDYSGIsyerlealggvqwpcpSEDHPGTPRlftgrfp 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 674 ---------SVEEKPIGENDEEAltrfapWPMV-----RVDH-----LVRRSLPLQETLAKEFktIRLNTKTAKKFNFNE 734
Cdd:COG3383 545 tpdgkarfvPVEYRPPAELPDEE------YPLVlttgrLLDQwhtgtRTRRSPRLNKHAPEPF--VEIHPEDAARLGIKD 616
|
650 660
....*....|....*....|....*...
gi 1269139799 735 GDQLTAIQGESRITLPLAIDDRLADNTV 762
Cdd:COG3383 617 GDLVRVSSRRGEVVLRARVTDRVRPGTV 644
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
18-201 |
6.53e-46 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 166.37 E-value: 6.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 18 SIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVEKSGKPLPACATPVTAGMKVFTQSKKALEAQRAVMEFLLINHPLD 97
Cdd:PTZ00305 86 NLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDAREGNVELILINHPND 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 98 CPICDQGGECELQDLAMGFGRAHSNYEDTKRAVFSDDIGPLIETEMTRCIQCTRCVRFGEEIAGLPELGVINRGEKEAIS 177
Cdd:PTZ00305 166 CPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTRVVLNRCIHCTRCVRFLNEHAQDFNLGMIGRGGLSEIS 245
|
170 180
....*....|....*....|....*
gi 1269139799 178 TYVKHF-MRSELSGNIIDICPVGAL 201
Cdd:PTZ00305 246 TFLDELeVKTDNNMPVSQLCPVGKL 270
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
278-636 |
8.56e-42 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 156.41 E-value: 8.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 278 RLYQPRIKK-DGKWEAISWEDALRIVKEKTQAIIEKHG--ASQTGALLSPSATIEEYFLFQKWLRGLGSHNIDHR----- 349
Cdd:pfam00384 1 RLKYPMVRRgDGKFVRVSWDEALDLIAKKLKRIIKKYGpdAIAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEdhngd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 350 -------VRWQDFRDQNTFdafpnlGMPITELENLNAILLIGSNVRFEQPLLSHRMNKAYGEG-AKILAINPmdyPFVFG 421
Cdd:pfam00384 81 lctaaaaAFGSDLRSNYLF------NSSIADIENADLILLIGTNPREEAPILNARIRKAALKGkAKVIVIGP---RLDLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 422 INEKMI-VSPSALIPALADVAKALAKEKSSEKAkviaetlvSAEKAAIFLGEHALHHPEAAKIR---------------- 484
Cdd:pfam00384 152 YADEHLgIKPGTDLALALAGAHVFIKELKKDKD--------FAPKPIIIVGAGVLQRQDGEAIFraianladltgnigrp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 485 --EWAHF-IAQQSGATVGLLTEGANSagawlagalphrrpggqrlDSPGLDAKAMLTTDPLKAYFLLNLEPEFDCAYPAQ 561
Cdd:pfam00384 224 ggGWNGLnILQGAASPVGALDLGLVP-------------------GIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENR 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1269139799 562 ALHTLNQAEWVVAFTTFTTPTMESYADILLPIAPFSESGGTYVNAEGRWQWASAASVPEKDAQPAWKVLRVLGNY 636
Cdd:pfam00384 285 VVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
1-76 |
6.39e-19 |
|
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: 81.82 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 1 MVELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKK----LSVAANCRMCLVEVEKSGKpLPACATPVTAGMKVFTQS 76
Cdd:pfam13510 3 PVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRTQN 81
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
83-123 |
3.50e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 75.31 E-value: 3.50e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1269139799 83 QRAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHSNY 123
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
2-72 |
3.73e-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: 57.02 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 2 VELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKklsvaaNCRMCLVEVEK----------------SGKPLPACATP 65
Cdd:cd00207 3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAG------ACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQTR 76
|
....*..
gi 1269139799 66 VTAGMKV 72
Cdd:cd00207 77 VTDGLVI 83
|
|
| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
690-767 |
6.56e-06 |
|
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant 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, 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 and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.
Pssm-ID: 239189 [Multi-domain] Cd Length: 96 Bit Score: 45.38 E-value: 6.56e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1269139799 690 RFAPWPMVR-VDHLVRRSLPLQETLAKEFktIRLNTKTAKKFNFNEGDQLTAIQGESRITLPLAIDDRLADNTVLLASG 767
Cdd:cd02788 2 QLVPYYHLFgSEELSQRSPVIAERAPAPY--ARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVGLPLG 78
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
219-637 |
0e+00 |
|
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: 669.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 219 PSIAPHDCVGGNIFLHSRWQEfvpqreVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKDGKWEAISWEDA 298
Cdd:cd02772 1 KSVSPHDALGSNLVVHVKNNK------VMRVVPRENEAINECWLSDRDRFSYEGLNSEDRLTKPMIKKDGQWQEVDWETA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 299 LRIVKEKTQAIIEKHGASQTGALLSPSATIEEYFLFQKWLRGLGSHNIDHRVRWQDFRDQNTFDAFPNLGMPITELENLN 378
Cdd:cd02772 75 LEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLARGLGSDNIDHRLRQSDFRDDAKASGAPWLGMPIAEISELD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 379 AILLIGSNVRFEQPLLSHRMNKAYGEGAKILAINPMDYPFVFGINEKMIVSPSALIPALADVAKALAKEKS--------- 449
Cdd:cd02772 155 RVLVIGSNLRKEHPLLAQRLRQAVKKGAKLSAINPADDDFLFPLSGKAIVAPSALANALAQVAKALAEEKGlavpdedak 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 450 ---SEKAKVIAETLVSAEKAAIFLGEHALHHPEAAKIREWAHFIAQQSGATVGLLTEGANSAGAWLAGALPHrrpggqrl 526
Cdd:cd02772 235 veaSEEARKIAASLVSAERAAVFLGNLAQNHPQAATLRALAQEIAKLTGATLGVLGEGANSVGAYLAGALPH-------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 527 dsPGLDAKAMLtTDPLKAYFLLNLEPEFDCAYPAQALHTLNQAEWVVAFTTFTTPTMESYADILLPIAPFSESGGTYVNA 606
Cdd:cd02772 307 --GGLNAAAML-EQPRKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALLDYADVLLPIAPFTETSGTFVNL 383
|
410 420 430
....*....|....*....|....*....|.
gi 1269139799 607 EGRWQWASAASVPEKDAQPAWKVLRVLGNYF 637
Cdd:cd02772 384 EGRVQSFKGVVKPLGEARPAWKVLRVLGNLL 414
|
|
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
4-633 |
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: 650.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 4 LEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVEKSGKPLPACATPVTAGMKVFTQSKKALEAQ 83
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 84 RAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHSNYEDTKRAVFSDDIGPLIETEMTRCIQCTRCVRFGEEIAGLP 163
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 164 ELGVINRGEKEAISTYVKHFMRSELSGNIIDICPVGALTDKPARYQGRGWEYRETPSIAPHDCVGGNIFLHSRWQefvpq 243
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNG----- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 244 rEVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIK-KDGKWEAISWEDALRIVKEKTQAIiekhgaSQTGALL 322
Cdd:TIGR01973 236 -EIMRILPRENDEINEEWLCDKGRFGYDGLNRQDRLTKPLLRnQEGNLLEVSWAEALAIAAEKLKAS------SRIGGIA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 323 SPSATIEEYFLFQKWLRGLGSHNIDHRVRwqdFRDQNTFDAFPN--LGMPITELENLNAILLIGSNVRFEQPLLSHRMNK 400
Cdd:TIGR01973 309 GPRSSLEELFALKKLVRKLGSENFDLRIR---NYEFESADLRANylFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRK 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 401 AY-GEGAKILAINPMDYPFVFGINEKMIVSPSALIPALADVAkalakeksSEKAKVIAETLVSAEKAAIFLGEHALHHPE 479
Cdd:TIGR01973 386 AVkKGGAKVALIGIEKWNLTYPANTNLVFHPGLSPKKLDDIA--------SGAHSDIAAALKAAKKPLIIVGDSAISHLD 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 480 AAKIREWAHFIAQQSG------ATVGLLTEGANSAGAWLAGALPHrrpggqrldspGLDAKAMLTTdpLKAYFLLNLEPE 553
Cdd:TIGR01973 458 GAALISAAANIAKVIKvrrkewNGLNILSSGANSVGLLDLGGEST-----------GLDAALNLGA--ADALFLLGADLE 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 554 FdcAYPAQALHTLNQAEWVVAFTTFT-TPTMESyADILLPIAPFSESGGTYVNAEGRWQWASAASVPEKDAQPAWKVLRV 632
Cdd:TIGR01973 525 R--ALDKTARDALSKADAFIIYQGHHgTETAEK-ADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRA 601
|
.
gi 1269139799 633 L 633
Cdd:TIGR01973 602 L 602
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
1-654 |
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: 602.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 1 MVELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVEKSGKPLPACATPVTAGMKVFTQSKKAL 80
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 81 EAQRAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHSNYEDTKRAVFSDDIGPLIETEMTRCIQCTRCVRFGEEIA 160
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 161 GLPELGVINRGEKEAISTYVKHFMRSELSGNIIDICPVGALTDKPARYQGRGWEYRETPSIAPHDCVGGNIFLHSRwqef 240
Cdd:COG1034 161 GDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVR---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 241 vpQREVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKDGKWEAISWEDALrivkektqaiiekhgasqtga 320
Cdd:COG1034 237 --GGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELVEASWEEAL--------------------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 321 llspsatieeyflfqkwlrglgshnidhrvrwqdfrdqntfdafpnlgmpitelenlnailligsnvrfeqpllshrmnk 400
Cdd:COG1034 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 401 aygegakilainpmdypfvfginekmivspsaliPALADVAKALAKEKssekakviaetlvsaekaaiflgehalhhpea 480
Cdd:COG1034 294 ----------------------------------AAAAEGLKALKKAE-------------------------------- 307
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 481 akirewahfiaqqsgatvglltegaNSAGAWLAGALPhrrpggqrldspglDAKAMLTTD---PLKAYFLLNLEPEFdcA 557
Cdd:COG1034 308 -------------------------NSVGAALLGALP--------------DAAAILEAAeagKLKALVLLGADPYD--L 346
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 558 YPAQALHTLNQAEWVVAFTTFTTPTMEsYADILLPIAPFSESGGTYVNAEGRWQWASAASVPEKDAQPAWKVLRVLGNYF 637
Cdd:COG1034 347 DPAAALAALAKADFVVVLDHFGSATAE-RADVVLPAAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANAL 425
|
650
....*....|....*..
gi 1269139799 638 dLPSFDYKTIEEVTREI 654
Cdd:COG1034 426 -GAGLPYDSLEEVRAEL 441
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
219-637 |
3.87e-143 |
|
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: 426.31 E-value: 3.87e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 219 PSIAPHDCVGGNIFLHSRWqefvpqREVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKDGKWEAISWEDA 298
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRG------GEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVSWEEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 299 LRIVKEKtqaiIEKHGASQTGALLSPSATIEEYFLFQKWLRGLGSHNIDHRVRWQDFRDQNTFDAFPNLGMPITELENLN 378
Cdd:cd02768 75 LKTVAEG----LKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQSDLPADNRLRGNYLFNTSIAEIEEAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 379 AILLIGSNVRFEQPLLSHRMNKAY-GEGAKILAINPMDYPfvFGINEKMIVSPS-ALIPALADVAKALAKekssekaKVI 456
Cdd:cd02768 151 AVLLIGSNLRKEAPLLNARLRKAVkKKGAKIAVIGPKDTD--LIADLTYPVSPLgASLATLLDIAEGKHL-------KPF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 457 AETLVSAEKAAIFLGEHALHHPEAAKIREWAHFIAQQ-SGATVGLLTEGANSAGAWLAGAlphrrpggqrldspGLDAKA 535
Cdd:cd02768 222 AKSLKKAKKPLIILGSSALRKDGAAILKALANLAAKLgTGAGLWNGLNVLNSVGARLGGA--------------GLDAGL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 536 MLtTDPLKAYFLLNLEPEFDCAYPAQALhTLNQAEWVVAFTTFTTPTMEsYADILLPIAPFSESGGTYVNAEGRWQWASA 615
Cdd:cd02768 288 AL-LEPGKAKLLLLGEDELDRSNPPAAV-ALAAADAFVVYQGHHGDTGA-QADVILPAAAFTEKSGTYVNTEGRVQRFKK 364
|
410 420
....*....|....*....|..
gi 1269139799 616 ASVPEKDAQPAWKVLRVLGNYF 637
Cdd:cd02768 365 AVSPPGDAREDWKILRALSNLL 386
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
1-764 |
1.33e-112 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 360.80 E-value: 1.33e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 1 MVELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVEKSGKPLPACATPVTAGMKVFTQ--SKK 78
Cdd:PRK07860 4 LVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTQltSPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 79 ALEAQRAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHSNYEDTKRaVFSDDIGplIETEM----TRCIQCTRCVR 154
Cdd:PRK07860 84 ADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKR-TFPKPIN--ISTQVlldrERCVLCARCTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 155 FGEEIAGLPELGVINRGEKEAISTYVKHFMRSELSGNIIDICPVGALTDKPARYQGRGWEYRETPSIAPHDCVGGNIFL- 233
Cdd:PRK07860 161 FSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASGCAQRTd 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 234 HSRWQefvpqreVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIK-KDGKWEAISWEDALRIVKEKTQAiiek 312
Cdd:PRK07860 241 HRRGK-------VLRRLAGDDPEVNEEWNCDKGRWAFTYATQPDRITTPLVRdEDGELEPASWSEALAVAARGLAA---- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 313 hGASQTGALLSPSATIEEYFLFQKWLR-GLGSHNIDHRVRWQDfRDQNTFDAFPNLGMPI----TELENLNAILLIGSNV 387
Cdd:PRK07860 310 -ARGRVGVLVGGRLTVEDAYAYAKFARvALGTNDIDFRARPHS-AEEADFLAARVAGRGLgvtyADLEKAPAVLLVGFEP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 388 RFEQPLLSHRMNKAY-GEGAKILAINpmdyPFVFGINEKMivsPSALIPAL----ADVAKALAkekssEKAKVIAETLvS 462
Cdd:PRK07860 388 EEESPIVFLRLRKAArKHGLKVYSIA----PFATRGLEKM---GGTLLRTApggeAAALDALA-----TGAPDVAELL-R 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 463 AEKAAIFLGEHALHHPEA--AKIRewahfIAQQSGATVGLLTEGANSAGAWLAGALPHRRPGGQRL-------------- 526
Cdd:PRK07860 455 TPGAVILVGERLATVPGAlsAAAR-----LADATGARLAWVPRRAGERGALEAGALPTLLPGGRPVadpaaraevaaawg 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 527 -----DSPGLDAKAMLTTDP---LKAYFLLNLEPEfDCAYPAQALHTLNQAEWVVAFTTFTTPTMEsYADILLPIAPFSE 598
Cdd:PRK07860 530 vdelpAAPGRDTAGILAAAAageLGALLVGGVEPA-DLPDPAAALAALDAAGFVVSLELRHSAVTE-RADVVLPVAPVAE 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 599 SGGTYVNAEGRWQwASAASVPEKDAQPAWKVLRVLGNYFDLPSFdYKTIEEVTREINDM-AHDKSRIEEGHSRSPISVEE 677
Cdd:PRK07860 608 KAGTFLNWEGRLR-PFEAALRTTGALSDLRVLDALADEMGVDLG-LPTVAAARAELARLgAWDGARAAAPAVPAAAPPQP 685
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 678 KPigendEEALtrFAPWPMVRVDHlvrRSLPLQETLAKEFKT--IRLNTKTAKKFNFNEGDQLTAIQGESRITLPLAIDD 755
Cdd:PRK07860 686 GA-----GEAV--LATWRMLLDDG---RLQDGEPHLAGTARPpvARLSAATAAEIGVADGDAVTVSTERGSITLPLAITD 755
|
....*....
gi 1269139799 756 rLADNTVLL 764
Cdd:PRK07860 756 -MPDRVVWL 763
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
219-637 |
9.12e-73 |
|
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: 242.23 E-value: 9.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 219 PSIAPHDCVGGNIFLHSRwqefvpQREVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKD--GKWEAISWE 296
Cdd:cd00368 1 PSVCPFCGVGCGILVYVK------DGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISWD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 297 DALRIVKEKTQAIIEKHGASQTGALLSPSATIEEYFLFQKWLRGLGSHNIDHRVRWQDFRDQN--TFDAFPNLGMPITEL 374
Cdd:cd00368 75 EALDEIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAalKAFGGGAPTNTLADI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 375 ENLNAILLIGSNVRFEQPLLSHRMNKAYGEGAKILAINPMDYPFVFGINEKMIVSPSalipalADVAkalakekssekak 454
Cdd:cd00368 155 ENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPG------TDAA------------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 455 viaetLVSAEKAAIFLGehalhhPEAAKIREWAHFIAqQSGATVGLLTEGAN-----SAGAWLAGALPHRRpgGQrLDSP 529
Cdd:cd00368 216 -----LALAEWAAEITG------VPAETIRALAREFA-AAKRAVILWGMGLTqhtngTQNVRAIANLAALT--GN-IGRP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 530 GLDAKAMltTDPLKAYfllnlepefdcAYPAQALHTLNQAEWVVAFTTFTTPTMEsYADILLPIAPFSESGGTYVNAEGR 609
Cdd:cd00368 281 GGGLGPG--GNPLVSA-----------PDANRVRAALKKLDFVVVIDIFMTETAA-YADVVLPAATYLEKEGTYTNTEGR 346
|
410 420
....*....|....*....|....*...
gi 1269139799 610 WQWASAASVPEKDAQPAWKVLRVLGNYF 637
Cdd:cd00368 347 VQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
216-762 |
7.05e-61 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 218.21 E-value: 7.05e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 216 RETPSIAPHdC-VGGNIFLHSRwqefvpQREVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKDGKWEAIS 294
Cdd:COG3383 5 KKVKTVCPY-CgVGCGIDLEVK------DGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 295 WEDALRIVKEKTQAIIEKHGASQTGALLSPSATIEEYFLFQKWLRG-LGSHNIDHRVRW------QDFRDQNTFDAFPNl 367
Cdd:COG3383 78 WDEALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGvLGTNNIDNNARLcmasavAGLKQSFGSDAPPN- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 368 gmPITELENLNAILLIGSNVRFEQPLLSHRMNKAYGEGAKILAINP------------------MDYPFVFGI------- 422
Cdd:COG3383 157 --SYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPrrtetarladlhlqikpgTDLALLNGLlhviiee 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 423 ---NEKMIVSPSALIPALADVAKALAKEKSSEKAKV-------IAETLVSAEKAAIFLGEHALHHPEA-AKIREWAHfIA 491
Cdd:COG3383 235 glvDEDFIAERTEGFEELKASVAKYTPERVAEITGVpaedireAARLIAEAKRAMILWGMGVNQHTQGtDNVNAIIN-LA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 492 QQSG------ATVGLLTEGANSAGAWLAGALPHRRPGGQRLDS-------------------PGLDAKAML---TTDPLK 543
Cdd:COG3383 314 LATGnigrpgTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDpehrakvadawgvpplpdkPGLTAVEMFdaiADGEIK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 544 AYFLLnlepefdCAYPAQ-------ALHTLNQAEWVVAFTTFTTPTMEsYADILLPIAPFSESGGTYVNAEGRWQWASAA 616
Cdd:COG3383 394 ALWII-------GENPAVsdpdanhVREALEKLEFLVVQDIFLTETAE-YADVVLPAASWAEKDGTFTNTERRVQRVRKA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 617 SVPEKDAQPAWKVLRVLGNYFDLPsFDYKTIEEVTREINDMAHDKSRI----------------EEGHSRSPI------- 673
Cdd:COG3383 466 VEPPGEARPDWEIIAELARRLGYG-FDYDSPEEVFDEIARLTPDYSGIsyerlealggvqwpcpSEDHPGTPRlftgrfp 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 674 ---------SVEEKPIGENDEEAltrfapWPMV-----RVDH-----LVRRSLPLQETLAKEFktIRLNTKTAKKFNFNE 734
Cdd:COG3383 545 tpdgkarfvPVEYRPPAELPDEE------YPLVlttgrLLDQwhtgtRTRRSPRLNKHAPEPF--VEIHPEDAARLGIKD 616
|
650 660
....*....|....*....|....*...
gi 1269139799 735 GDQLTAIQGESRITLPLAIDDRLADNTV 762
Cdd:COG3383 617 GDLVRVSSRRGEVVLRARVTDRVRPGTV 644
|
|
| 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 ... |
219-654 |
1.89e-49 |
|
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: 181.05 E-value: 1.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 219 PSIAPHDCVGGNIFLHSRWQEfvpqreVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKDGKWEAISWEDA 298
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGE------LRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 299 LRIVKEKTQAIIEKhgasqTGALLSPSATIEEYFLFQKWLRG-LGSHNIDHRVRWQDFRDQntfDAFPNLGMPITELENL 377
Cdd:cd02771 75 LDVAAARLKEAKDK-----VGGIGSPRASNESNYALQKLVGAvLGTNNVDHRARRLIAEIL---RNGPIYIPSLRDIESA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 378 NAILLIGSNVRFEQPLLSHRMNKA--------------------------YGEGAKILAINPMDYPFVFGINEKMIVSPS 431
Cdd:cd02771 147 DAVLVLGEDLTQTAPRIALALRQAarrkavelaalsgipkwqdaavrniaQGAKSPLFIVNALATRLDDIAAESIRASPG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 432 ALIPALADVAKALAKEKSS-------EKAKVIAETLVSAEKAAIFLGEHaLHHPEAAKirewahfiaqqSGATVGLLTEG 504
Cdd:cd02771 227 GQARLGAALARAVDASAAGvsglapkEKAARIAARLTGAKKPLIVSGTL-SGSLELIK-----------AAANLAKALKR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 505 ANSAGAWL----AGALPHRRPGGQRLDSPGLDAKAMLTTDP---LKAYFLLNLEPeFDCAYPAQALHTLNQAEWVVAFTT 577
Cdd:cd02771 295 RGENAGLTlaveEGNSPGLLLLGGHVTEPGLDLDGALAALEdgsADALIVLGNDL-YRSAPERRVEAALDAAEFVVVLDH 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 578 FTTPTMESyADILLPIAPFSESGGTYVNAEGRWQ-WASAASVPEKDAQPAWKVLRVLGNYFDLPS--FDYKTIEEVTREI 654
Cdd:cd02771 374 FLTETAER-ADVVLPAASFAEKSGTFVNYEGRAQrFFKAYDDPAGDARSDWRWLHALAAKLGGKLvpSDAAILDEIIALV 452
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
1-757 |
8.34e-47 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 179.13 E-value: 8.34e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 1 MVELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVekSGKPLPACATPVTAGMKVFTQSKKAL 80
Cdd:PRK08493 1 MITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEA--DGKRVYSCNTKAKEGMNILTNTPNLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 81 EAQRAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHSNY--EDTKRAVfsDDIGpLIETEMTRCIQCTRCVRFGEE 158
Cdd:PRK08493 79 DERNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVNHQPYaiKDTHKPH--KHWG-KINYDPSLCIVCERCVTVCKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 159 IAGLPELGVINRG------------EKEAISTYVKH------FMRSELS-----GNIIDICPVGALTDKPARYQGRGWEY 215
Cdd:PRK08493 156 KIGESALKTVPRGldapdksfkesmPKDAYAVWSKKqksligPVGGETLdcsfcGECIAVCPVGALSSSDFQYTSNAWEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 216 RETPSIAPHDCVGGNIFLHSRWQEFVPQREvmrAVPRENDEVNETWMSDRDRFGhFAVYHEsrlyqprIKKDGKweaiSW 295
Cdd:PRK08493 236 KKIPATCPHCSDCCLIYYDVKHSSILNQES---KIYRVSNDFYFNPLCGAGRFA-FDFQNE-------ADKDEK----AF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 296 EDALRIVKeKTQAIiekhgasqtgaLLSPSATIEEYFLFQKwLR---GLGSHNIDHRvRWQDFrdQNTFDAFPNL--GMP 370
Cdd:PRK08493 301 KEAVEAFK-EAKAI-----------KFNSFITNEEALILQR-LKkkfGLKLINEEAL-KFQQF--LKVFSEVSGKsySAN 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 371 ITELENLNAILLIGSNVRFEQPLLSHRMNKAYG-EGAKILAINPMDYPFV---------------------------FGI 422
Cdd:PRK08493 365 LEDIKTSDFVVVAGSALKTDNPLLRYAINNALKmNKASGLYFHPIKDNVIanlsknffcithevgaeeiilyfllkkFLE 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 423 NEKMIVSPSALIPALADVAKALAKEKSSEKAKVIAETLVSAE-------------------------------------- 464
Cdd:PRK08493 445 EEAILKSLEEFKQSIVKEAALSILEEIREKVLEQAEQGCENQeevkkevpkkvkkipevdtyllleelgineetyeklea 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 465 ---KAAIF---LGEHALHHPEAAKIREWAHFIAQQSGATVGLLTEGANSAGAWLAGALPHRRPGGQRLdspGLDAKAmlt 538
Cdd:PRK08493 525 llaKKNNFtlvVGEDLYAHKNAKNLAKLLGLIQKYTAFKVILIPPSTNTLGVALICDLSEEIEGGKTV---GYNEKG--- 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 539 tDplkayFLLNLEPEFDCAYPAqalhtLNQAEwvvafTTFTtptmeSYADILLPIAPFSESGGTYVNaegrwQWASAASV 618
Cdd:PRK08493 599 -D-----FTISSLEKGDLALPA-----LNQQE-----GTFT-----NIDKRVVPTNAALPFEGYDLN-----DIANALGF 652
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 619 PEKDAQPAWKVLRVLGNY----FD-LPSFdYKTIEEVTR--EINDMAHDKSRIEEGHSRSPIsveeKPIGENDEEALtrF 691
Cdd:PRK08493 653 DEEYTIDYTKKLPTEKGFkaieFDdLENY-YTNDGSNHRgyELETSSFEKSAKEETIECEPI----KPLKEKIGINI--Y 725
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1269139799 692 APWPMVRVDHLVRRSLPLQETLAkefktIRLNTKTAKKFNFNEGDQLTAIQGESRITLPLAIDDRL 757
Cdd:PRK08493 726 LANPITQFNNFTNKAENLNEKAG-----LYVSEAFLKKLNLKDGDNVTLKKEEEELTGSVYLDESL 786
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
220-633 |
1.44e-46 |
|
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: 170.52 E-value: 1.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 220 SIAPHDCVGGNIFLHSRwqefvpQREVMRAVPRENDEVNETWMSDRDRfghFAV----YHesRLYQPRIKKDGKWEAISW 295
Cdd:cd02773 2 SIDVLDAVGSNIRVDTR------GGEVMRILPRLNEDINEEWISDKTR---FAYdglkRQ--RLDKPYIRKNGKLKPATW 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 296 EDALRIVKEKTQAIiekhGASQTGALLSPSATIEEYFLFQKWLRGLGSHNIDHRvrwQDFRDQNT-FDAFPNLGMPITEL 374
Cdd:cd02773 71 EEALAAIAKALKGV----KPDEIAAIAGDLADVESMVALKDLLNKLGSENLACE---QDGPDLPAdLRSNYLFNTTIAGI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 375 ENLNAILLIGSNVRFEQPLLSHRMNKAY-GEGAKILAINP---MDYPFVFginekmivspsalipaLADVAKALAKEKSS 450
Cdd:cd02773 144 EEADAVLLVGTNPRFEAPVLNARIRKAWlHGGLKVGVIGPpvdLTYDYDH----------------LGTDAKTLQDIASG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 451 EKAkvIAETLVSAEKAAIFLGEHALHHPEAAKIREWAHFIAQQSGATVG------LLTEGANSAGAWLAGALPhrrpggq 524
Cdd:cd02773 208 KHP--FSKALKDAKKPMIIVGSGALARKDGAAILAAVAKLAKKNGVVREgwngfnVLHRAASRVGALDLGFVP------- 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 525 rldspglDAKAMLTTDPLKAYFLLNL-EPEFDCAYPA-----QALHTLNQAewvvafttfttptmeSYADILLPIAPFSE 598
Cdd:cd02773 279 -------GAGAIRKSGPPKVLYLLGAdEIDITPIPKDafvvyQGHHGDRGA---------------QIADVILPGAAYTE 336
|
410 420 430
....*....|....*....|....*....|....*
gi 1269139799 599 SGGTYVNAEGRWQWASAASVPEKDAQPAWKVLRVL 633
Cdd:cd02773 337 KSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRAL 371
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
18-201 |
6.53e-46 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 166.37 E-value: 6.53e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 18 SIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVEKSGKPLPACATPVTAGMKVFTQSKKALEAQRAVMEFLLINHPLD 97
Cdd:PTZ00305 86 NLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDAREGNVELILINHPND 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 98 CPICDQGGECELQDLAMGFGRAHSNYEDTKRAVFSDDIGPLIETEMTRCIQCTRCVRFGEEIAGLPELGVINRGEKEAIS 177
Cdd:PTZ00305 166 CPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTRVVLNRCIHCTRCVRFLNEHAQDFNLGMIGRGGLSEIS 245
|
170 180
....*....|....*....|....*
gi 1269139799 178 TYVKHF-MRSELSGNIIDICPVGAL 201
Cdd:PTZ00305 246 TFLDELeVKTDNNMPVSQLCPVGKL 270
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
2-204 |
7.95e-45 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 160.97 E-value: 7.95e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 2 VELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVEKSGKPLPACATPVTAGMKVFTQSKKALE 81
Cdd:PRK07569 4 KTLTIDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 82 AQRAVMEFLLI--NHPldCPICDQGGECELQDLAMGFGRAHSNYE--DTKRAVfsdDIG-PLIETEMTRCIQCTRCVRFG 156
Cdd:PRK07569 84 YRRMIVELLFAegNHV--CAVCVANGNCELQDLAIEVGMDHVRFPylFPRRPV---DIShPRFGIDHNRCVLCTRCVRVC 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1269139799 157 EEIAGLPELGVINRGEKEAISTYVKHFMRSELS----GNIIDICPVGALTDK 204
Cdd:PRK07569 159 DEIEGAHTWDVAGRGAKSRVITDLNQPWGTSETctscGKCVQACPTGAIFRK 210
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
278-636 |
8.56e-42 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 156.41 E-value: 8.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 278 RLYQPRIKK-DGKWEAISWEDALRIVKEKTQAIIEKHG--ASQTGALLSPSATIEEYFLFQKWLRGLGSHNIDHR----- 349
Cdd:pfam00384 1 RLKYPMVRRgDGKFVRVSWDEALDLIAKKLKRIIKKYGpdAIAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEdhngd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 350 -------VRWQDFRDQNTFdafpnlGMPITELENLNAILLIGSNVRFEQPLLSHRMNKAYGEG-AKILAINPmdyPFVFG 421
Cdd:pfam00384 81 lctaaaaAFGSDLRSNYLF------NSSIADIENADLILLIGTNPREEAPILNARIRKAALKGkAKVIVIGP---RLDLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 422 INEKMI-VSPSALIPALADVAKALAKEKSSEKAkviaetlvSAEKAAIFLGEHALHHPEAAKIR---------------- 484
Cdd:pfam00384 152 YADEHLgIKPGTDLALALAGAHVFIKELKKDKD--------FAPKPIIIVGAGVLQRQDGEAIFraianladltgnigrp 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 485 --EWAHF-IAQQSGATVGLLTEGANSagawlagalphrrpggqrlDSPGLDAKAMLTTDPLKAYFLLNLEPEFDCAYPAQ 561
Cdd:pfam00384 224 ggGWNGLnILQGAASPVGALDLGLVP-------------------GIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENR 284
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1269139799 562 ALHTLNQAEWVVAFTTFTTPTMESYADILLPIAPFSESGGTYVNAEGRWQWASAASVPEKDAQPAWKVLRVLGNY 636
Cdd:pfam00384 285 VVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
244-655 |
2.09e-40 |
|
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: 156.22 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 244 REVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKDGKWEAISWEDALRIVKEKTQAIIEKHGASQTGALLS 323
Cdd:cd02753 20 NKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDEALSLVASRLKEIKDKYGPDAIAFFGS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 324 PSATIEEYFLFQKWLR-GLGSHNIDHRVR----------WQDF---RDQNTFDafpnlgmpitELENLNAILLIGSNVRF 389
Cdd:cd02753 100 AKCTNEENYLFQKLARaVGGTNNVDHCARlchsptvaglAETLgsgAMTNSIA----------DIEEADVILVIGSNTTE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 390 EQPLLSHRMNKAYGEGAKILAINPMDYPFVFGINEKMIVSPS---ALIPALADV---------------------AKALA 445
Cdd:cd02753 170 AHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGtdvALLNAMAHViieeglydeefieertegfeeLKEIV 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 446 KEKSSEKAKVI-----------AETLVSAEKAAIFlgehalhhpeaakireWAHFIAQQSGAT--------VGLLT---- 502
Cdd:cd02753 250 EKYTPEYAERItgvpaedireaARMYATAKSAAIL----------------WGMGVTQHSHGTdnvmalsnLALLTgnig 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 503 -EGA---------NSAGAWLAGALPHRRPGGqrldspgldakamlttdpLKAYFLLNLEPEFDCAYPAQALHTLNQAEWV 572
Cdd:cd02753 314 rPGTgvnplrgqnNVQGACDMGALPNVLPGY------------------VKALYIMGENPALSDPNTNHVRKALESLEFL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 573 VAFTTFTTPTMEsYADILLPIAPFSESGGTYVNAEGRWQWASAASVPEKDAQPAWKVLRVLGNYFDLPSFdYKTIEEVTR 652
Cdd:cd02753 376 VVQDIFLTETAE-LADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGF-YSHPEEIFD 453
|
...
gi 1269139799 653 EIN 655
Cdd:cd02753 454 EIA 456
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
241-654 |
1.39e-26 |
|
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: 115.02 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 241 VPQREVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKKDG-KWEAISWEDALRIVKEKTQAIIEKHGASQTG 319
Cdd:cd02754 17 VKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGgELVPVSWDEALDLIAERFKAIQAEYGPDSVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 320 ALLSPSATIEEYFLFQKWLRG-LGSHNIdhrvrwqdfrDQNT----------------FDAFPNlgmPITELENLNAILL 382
Cdd:cd02754 97 FYGSGQLLTEEYYAANKLAKGgLGTNNI----------DTNSrlcmasavagykrsfgADGPPG---SYDDIEHADCFFL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 383 IGSNVRFEQPLLSHRM--NKAYGEGAKILAINP----------MDYPFVFG------------------INEKMIVSPSA 432
Cdd:cd02754 164 IGSNMAECHPILFRRLldRKKANPGAKIIVVDPrrtrtadiadLHLPIRPGtdlallngllhvlieeglIDRDFIDAHTE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 433 LIPALADVAKALAKEKSSEKAKVIAETLvsaEKAAIflgehALHHPEAAkIREWAHFIAQQS------------------ 494
Cdd:cd02754 244 GFEELKAFVADYTPEKVAEITGVPEADI---REAAR-----LFGEARKV-MSLWTMGVNQSTqgtaannaiinlhlatgk 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 495 ----GATVGLLTEGANSAGAWLAGALPHRRPGGQRLDSP----------GLDAKAMLTTDPLKAYFLLNL----EPEF-- 554
Cdd:cd02754 315 igrpGSGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPehraevakfwGVPEGTIPPKPGLHAVEMFEAiedgEIKAlw 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 555 -DCAYPAQAL-------HTLNQAEWVVAFTTF-TTPTMEsYADILLPIAPFSESGGTYVNAEGRWQWASAASVPEKDAQP 625
Cdd:cd02754 395 vMCTNPAVSLpnanrvrEALERLEFVVVQDAFaDTETAE-YADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARP 473
|
490 500 510
....*....|....*....|....*....|
gi 1269139799 626 AWKVLRVLGNYFDLPS-FDYKTIEEVTREI 654
Cdd:cd02754 474 DWWILADVARRLGFGElFPYTSPEEVFEEY 503
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
245-654 |
1.86e-26 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 115.33 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 245 EVMRAVPRENDEVNETWMSDRDRFGHFAVYHESRLYQPRIKK----DGKWEAISWEDALRIVKEKTQAIIEKHG----AS 316
Cdd:COG0243 45 RVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVgprgSGKFERISWDEALDLIAEKLKAIIDEYGpeavAF 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 317 QTGALLSPSATIEEYFLFQKWLRGLGSHNIDhrvrwqdfrDQNTFD------AFP------NLGMPITELENLNAILLIG 384
Cdd:COG0243 125 YTSGGSAGRLSNEAAYLAQRFARALGTNNLD---------DNSRLChesavaGLPrtfgsdKGTVSYEDLEHADLIVLWG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 385 SNVRFEQPLLSHRMNKAYGE-GAKILAINPMdypfvfginekmiVSPSAlipALAD------------VAKALAKEksse 451
Cdd:COG0243 196 SNPAENHPRLLRRLREAAKKrGAKIVVIDPR-------------RTETA---AIADewlpirpgtdaaLLLALAHV---- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 452 kakVIAETLVSAEkaaiFLGEH---------ALHH--PE---------AAKIREWAHFIAqQSGATVGLLTEGANSAG-- 509
Cdd:COG0243 256 ---LIEEGLYDRD----FLARHtvgfdelaaYVAAytPEwaaeitgvpAEDIRELAREFA-TAKPAVILWGMGLQQHSng 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 510 ---AWLAGALP-----HRRPGGQRLDSPGldaKAMLT--TDPLKAYFLLNLEPefdcaypaqALHTLNQAEW-------- 571
Cdd:COG0243 328 tqtVRAIANLAlltgnIGKPGGGPFSLTG---EAILDgkPYPIKALWVYGGNP---------AVSAPDTNRVrealrkld 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 572 -VVAFTTFTTPTMEsYADILLPIAPFSESGGTYVNAEGRWQWASAASV-PEKDAQPAWKVLRVLGNYFDLPS-FDY-KTI 647
Cdd:COG0243 396 fVVVIDTFLTETAR-YADIVLPATTWLERDDIVTNSEDRRVHLSRPAVePPGEARSDWEIFAELAKRLGFEEaFPWgRTE 474
|
....*..
gi 1269139799 648 EEVTREI 654
Cdd:COG0243 475 EDYLREL 481
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
2-109 |
4.77e-20 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 95.18 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 2 VELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKKLSVAANCRMCLVEVEKSGKPLPACATPVTAGMKVFTQSKKALE 81
Cdd:PRK12814 4 ISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETENAELHA 83
|
90 100
....*....|....*....|....*...
gi 1269139799 82 AQRAVMEFLLINHPLDCPicdqgGECEL 109
Cdd:PRK12814 84 MRRQSLERLIEQHCGDCL-----GPCEL 106
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
1-76 |
6.39e-19 |
|
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: 81.82 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 1 MVELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKK----LSVAANCRMCLVEVEKSGKpLPACATPVTAGMKVFTQS 76
Cdd:pfam13510 3 PVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRTQN 81
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
83-121 |
1.52e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 76.33 E-value: 1.52e-17
10 20 30
....*....|....*....|....*....|....*....
gi 1269139799 83 QRAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHS 121
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEV 39
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
83-123 |
3.50e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 75.31 E-value: 3.50e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1269139799 83 QRAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHSNY 123
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
265-641 |
3.13e-15 |
|
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: 78.88 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 265 RDRFGHFAVYHESRLYQPRI----KKDGKWEAISWEDALRIVKEKTQAIIEKHGAsQTGALLSPSATIEEYFLFqkWLRG 340
Cdd:cd02755 42 RGNAGIQLLYDPDRLKKPLIrvgeRGEGKFREASWDEALQYIASKLKEIKEQHGP-ESVLFGGHGGCYSPFFKH--FAAA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 341 LGSHNI----------DHRVRwqdfrdQNTFDAFPnlGMPITELENLNAILLIGSNvRFE--QPLLSHRMNKAYGEGAKI 408
Cdd:cd02755 119 FGSPNIfshestclasKNLAW------KLVIDSFG--GEVNPDFENARYIILFGRN-LAEaiIVVDARRLMKALENGAKV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 409 LAINP------------------MDYPFVFG-----INEKM---------IVSPSALipaladvaKALAKEKSSEKAKVI 456
Cdd:cd02755 190 VVVDPrfselaskadewipikpgTDLAFVLAlihvlISENLydaafvekyTNGFELL--------KAHVKPYTPEWAAQI 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 457 AEtlVSAEKAAIFLGEHALHHPEAAKIREWAHFIAQQS------GATVGLLTEGANSAGAWLAGALPhrRPGgqrldspg 530
Cdd:cd02755 262 TD--IPADTIRRIAREFAAAAPHAVVDPGWRGTFYSNSfqtrraIAIINALLGNIDKRGGLYYAGSA--KPY-------- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 531 ldakamlttdPLKAYFLLNLEPeFDCAYPAQAL-HTLNQAEWVVAFTTFTTPTMeSYADILLPIA-------PFSESGGT 602
Cdd:cd02755 330 ----------PIKALFIYRTNP-FHSMPDRARLiKALKNLDLVVAIDILPSDTA-LYADVILPEAtylerdePFSDKGGP 397
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1269139799 603 YVNAEGRWQWAsaasVPEKDAQPAWKVLRVLG---NYFDLPS 641
Cdd:cd02755 398 APAVATRQRAI----EPLYDTRPGWDILKELArrlGLFGTPS 435
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
273-655 |
3.94e-15 |
|
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: 79.37 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 273 VYHESRLYQP--RIKKDGKWEAISWEDAL----RIVKEKTQA-IIEKHGASQT-------GALLSPSATIEEYFLFQKWL 338
Cdd:cd02752 49 VHSPKRLKYPmyRAPGSGKWEEISWDEALdeiaRKMKDIRDAsFVEKNAAGVVvnrpdsiAFLGSAKLSNEECYLIRKFA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 339 RGLGSHNIDHRVRWQDFRD----QNTF--DAFPNlgmPITELENLNAILLIGSNVRFEQPL-LSHRMNKAYGEGAKILAI 411
Cdd:cd02752 129 RALGTNNLDHQARIUHSPTvaglANTFgrGAMTN---SWNDIKNADVILVMGGNPAEAHPVsFKWILEAKEKNGAKLIVV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 412 NP------------------MDYPFVFGINEKMI------VSPSALIPAlADVAKAlakekssekAKVIAETlVSAEKAA 467
Cdd:cd02752 206 DPrftrtaakadlyvpirsgTDIAFLGGMINYIIrytpeeVEDICGVPK-EDFLKV---------AEMFAAT-GRPDKPG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 468 IFLgeHAL----HHPEAAKIREWAhfIAQ-------QSGATVGLLTEGANSAGAWLAGALPHRRPG---GQRLDSPGLDA 533
Cdd:cd02752 275 TIL--YAMgwtqHTVGSQNIRAMC--ILQlllgnigVAGGGVNALRGHSNVQGATDLGLLSHNLPGylgGQNPNSSFPNA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 534 -KAMLTTDPLKayFLLNLEPeFDcaypaqalhTLNQAEWVVAFTTFTTPTMESYadiLLPIAPFSESGGTYVNAeGRW-Q 611
Cdd:cd02752 351 nKVRRALDKLD--WLVVIDP-FP---------TETAAFWKNPGMDPKSIQTEVF---LLPAACQYEKEGSITNS-GRWlQ 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1269139799 612 WASAASVPEKDAQPAWKVLRVL-----------GNYFDLPSFDYK-------TIEEVTREIN 655
Cdd:cd02752 415 WRYKVVEPPGEAKSDGDILVELakrlgflyekeGGAFPEPITKWNygygdepTPEEIAREIN 476
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
272-649 |
4.20e-15 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 78.50 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 272 AVYHESRLYQP--RI--KKDGKWEAISWEDALRIVKEKTQAIIEKHGASQTGALLSPSATIEEY--FLFQKWLRGLGSHN 345
Cdd:cd02759 48 IVYHPDRLLYPlkRVgeRGENKWERISWDEALDEIAEKLAEIKAEYGPESIATAVGTGRGTMWQdsLFWIRFVRLFGSPN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 346 IDHRVR--WQDFRDQNTFDAFPNLGMPITELENLNAILLIGSNvrfeqPLLS------HRMNKAYGEGAKILAINPMdyp 417
Cdd:cd02759 128 LFLSGEscYWPRDMAHALTTGFGLGYDEPDWENPECIVLWGKN-----PLNSnldlqgHWLVAAMKRGAKLIVVDPR--- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 418 fvfginekmiVSPSALIPAL-------ADVAKALA------KEKSSEKAKVIAETLVSAEkaaifLGEHALH-HPE---- 479
Cdd:cd02759 200 ----------LTWLAARADLwlpirpgTDAALALGmlnviiNEGLYDKDFVENWCYGFEE-----LAERVQEyTPEkvae 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 480 -----AAKIREWAHFIAQ--QSGATVGLLTEGANSAGAW---------LAGALPhrRPGGQRLDSPGLDAKAMLTTDPLK 543
Cdd:cd02759 265 itgvpAEKIRKAARLYATakPACIQWGLAIDQQKNGTQTsraiailraITGNLD--VPGGNLLIPYPVKMLIVFGTNPLA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 544 AYfllnlepefdcAYPAQALHTLNQAEWVVAFTTFTTPTMEsYADILLPIAPFSESGGTYVNAEGrWQWASA---ASVPE 620
Cdd:cd02759 343 SY-----------ADTAPVLEALKALDFIVVVDLFMTPTAM-LADIVLPVAMSLERPGLRGGFEA-ENFVQLrqkAVEPY 409
|
410 420
....*....|....*....|....*....
gi 1269139799 621 KDAQPAWKVLRVLGNYFDLPSFDYKTIEE 649
Cdd:cd02759 410 GEAKSDYEIVLELGKRLGPEEAEYYKYEK 438
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
219-411 |
3.62e-14 |
|
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: 74.71 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 219 PSIAPHDCVGGNIFLHSRwqefvpQREVMRAVPRENDEVNETWMSDRDRFgHFAVYHESRLYQPRIKKDG-KWEAISWED 297
Cdd:cd02774 1 ESIDVLDSLGSNIRVDIK------GNEILRILPKINDELNEEWISDKIRF-SYDSLKYQRIKTPLLKLSNnSFLEIGWKT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 298 ALRIVKEKtqaiIEKHGASQTGALLSPSATIEEYFLFQKWLRGLGSHNIdhrvrwqdfrdqNTFDAFPNLG--------- 368
Cdd:cd02774 74 AFKFLNKF----ILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNT------------NSNNFLENNNyfnldleny 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1269139799 369 ---MPITELENLNAILLIGSNVRFEQPLLSHRMNKAYGEGAKILAI 411
Cdd:cd02774 138 lfnNSLKNLDKSDLCLLIGSNLRVESPILNIRLRNRYNKGNKKIFV 183
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
273-634 |
6.77e-14 |
|
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: 74.98 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 273 VYHESRLYQPRIK---KDGKWEAISWEDALRIVKEKTQAIIEKHGA--------SQTGALLSPSAtieEYFLFqkwlRGL 341
Cdd:cd02766 50 VYSPDRLLTPLKRvgrKGGQWERISWDEALDTIAAKLKEIKAEYGPesilpysyAGTMGLLQRAA---RGRFF----HAL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 342 GSHNIDHRVRWQDFRDQNTFDAFPNLGMPITELENLNAILLIGSNVRFEQPLLSHRMNKAYGEGAKILAINPMDYPFVFG 421
Cdd:cd02766 123 GASELRGTICSGAGIEAQKYDFGASLGNDPEDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAAR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 422 INEKMIVSPSalipalADVAKALAkeksseKAKVI-AETLVSAEkaaiFLGEHALHHPE-AAKIREWA-HFIAQQSGATV 498
Cdd:cd02766 203 ADLHIQIRPG------TDGALALG------VAKVLfREGLYDRD----FLARHTEGFEElKAHLETYTpEWAAEITGVSA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 499 GLLTE-----GANSAGA-WLAGALPHRRPGGQ--RLdspgLDAKAMLTTDPLKA---YFLLNLEPEFDCAY-----P-AQ 561
Cdd:cd02766 267 EEIEElarlyGEAKPPSiRLGYGMQRYRNGGQnvRA----IDALPALTGNIGVPgggAFYSNSGPPVKALWvynsnPvAQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 562 A--LHTLNQA-----EWVVAFTTFTTPTMEsYADILLPIAPFSES-------GGTYVnaegrwQWASAASVPEKDAQPAW 627
Cdd:cd02766 343 ApdSNKVRKGlaredLFVVVHDQFMTDTAR-YADIVLPATTFLEHedvyasyWHYYL------QYNEPAIPPPGEARSNT 415
|
....*..
gi 1269139799 628 KVLRVLG 634
Cdd:cd02766 416 EIFRELA 422
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
275-414 |
1.36e-10 |
|
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239168 [Multi-domain] Cd Length: 574 Bit Score: 64.64 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 275 HESRLYQP--RIKKDGKWEAISWEDALRIVKEKTQAIIEKhgasQTGALLSPSATIEEYFLFQKWLRGLGSHNID----- 347
Cdd:cd02767 61 HLGRLTYPmrYDAGSDHYRPISWDEAFAEIAARLRALDPD----RAAFYTSGRASNEAAYLYQLFARAYGTNNLPdcsnm 136
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1269139799 348 -HrvrwqdfrdQNTFDAFPN-LGMP-----ITELENLNAILLIGSNVRFEQPLLSHRMNKAYGEGAKILAINPM 414
Cdd:cd02767 137 cH---------EPSSVGLKKsIGVGkgtvsLEDFEHTDLIFFIGQNPGTNHPRMLHYLREAKKRGGKIIVINPL 201
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
2-72 |
3.73e-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: 57.02 E-value: 3.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 2 VELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKklsvaaNCRMCLVEVEK----------------SGKPLPACATP 65
Cdd:cd00207 3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAG------ACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQTR 76
|
....*..
gi 1269139799 66 VTAGMKV 72
Cdd:cd00207 77 VTDGLVI 83
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
267-396 |
2.06e-07 |
|
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: 54.33 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 267 RFGHFAvYHESRLYQPRIKKDGKWEAISWEDALRIVKEKTQAIIEKHGASQTGALL-------SPSATIEEYFlfqkwLR 339
Cdd:cd02762 44 ALGDYQ-NDPDRLRTPMRRRGGSFEEIDWDEAFDEIAERLRAIRARHGGDAVGVYGgnpqahtHAGGAYSPAL-----LK 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269139799 340 GLGSHNidhrvrwqdFRDQNTFDAFP-----------NLGMPITELENLNAILLIGSNvrfeqPLLSH 396
Cdd:cd02762 118 ALGTSN---------YFSAATADQKPghfwsglmfghPGLHPVPDIDRTDYLLILGAN-----PLQSN 171
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
275-413 |
6.35e-07 |
|
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: 52.87 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 275 HESRLYQP-RIKK---------DGKWEAISWEDALRIVKEKTQAIIEKHGasqTGALLSPSATIEEYFLfqKWLR----G 340
Cdd:cd02765 46 HLQRVYSPdRLKYpmkrvgergEGKFERITWDEALDTIADKLTEAKREYG---GKSILWMSSSGDGAIL--SYLRlallG 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1269139799 341 LGSH-----NIDHRVRwQDFRDQNTFDAFPNlGMPITELENLNAILLIGSNVRFEQPLLSHRMNKAYGEGAKILAINP 413
Cdd:cd02765 121 GGLQdaltyGIDTGVG-QGFNRVTGGGFMPP-TNEITDWVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDP 196
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
269-649 |
1.05e-06 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 52.36 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 269 GHFAVYHESRLYQPRIKK----DGKWEAISWEDALRIVKEKTQAIIEKHGAsQTGALLSPSATIEeyflfqKWLRGLGsh 344
Cdd:PRK15488 89 GHSLLYDPQRIVKPLKRVgergEGKWQEISWDEAYQEIAAKLNAIKQQHGP-ESVAFSSKSGSLS------SHLFHLA-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 345 nidhrvrwQDFRDQNTFDAF----------------PNLGMpitELENLNAILLIGSNVrFEQPLLS--HRMNKAYGE-G 405
Cdd:PRK15488 160 --------TAFGSPNTFTHAstcpagyaiaakvmfgGKLKR---DLANSKYIINFGHNL-YEGINMSdtRGLMTAQMEkG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 406 AKIL-----------------AINP-MDYPFVFGINEKMI---VSPSALI-------PALADVAKALAKEKSSEKAKV-- 455
Cdd:PRK15488 228 AKLVvfeprfsvvaskadewhAIRPgTDLAVVLALCHVLIeenLYDKAFVerytsgfEELAASVKEYTPEWAEAISDVpa 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 456 -----IAETLVSAEKAAIF-LGEHALHHPEAAKIREwAHFIA--------QQSGATVGLLTEGANS-AGAWLAGAL---- 516
Cdd:PRK15488 308 ddirrIARELAAAAPHAIVdFGHRATFTPEEFDMRR-AIFAAnvllgnieRKGGLYFGKNASVYNKlAGEKVAPTLakpg 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 517 --PHRRPGGQRLDSPGLDAK--------------AMLTTDP--LKAYFLLNLEPEFDCAYPAQALHTLNQAEWVVAFTTF 578
Cdd:PRK15488 387 vkGMPKPTAKRIDLVGEQFKyiaagggvvqsiidATLTQKPyqIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVY 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 579 TTPTmESYADILLPiapfsESggTYVNAEGRWQWASAAS----------VPEKDAQPAWKVLRVLGNYFDLPS-FDYKTI 647
Cdd:PRK15488 467 LSES-AAYADVVLP-----ES--TYLERDEEISDKSGKNpayalrqrvvEPIGDTKPSWQIFKELGEKMGLGQyYPWQDM 538
|
..
gi 1269139799 648 EE 649
Cdd:PRK15488 539 ET 540
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
273-413 |
3.60e-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: 50.40 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 273 VYHESRLYQP--RIKK--DGKWEAISWEDALRIVKEKTQAIIEKHGASqtgALLSPSATIEEYFLFQK---WLRGLgshN 345
Cdd:cd02770 54 VYNPDRLKYPmkRVGKrgEGKFVRISWDEALDTIASELKRIIEKYGNE---AIYVNYGTGTYGGVPAGrgaIARLL---N 127
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1269139799 346 ID--HRVRWQDFRDQNTFDAFPNLGM------PITELENLNAILLIGSN---VRFEQPLLSHRMNKAYGEGAKILAINP 413
Cdd:cd02770 128 LTggYLNYYGTYSWAQITTATPYTYGaaasgsSLDDLKDSKLVVLFGHNpaeTRMGGGGSTYYYLQAKKAGAKFIVIDP 206
|
|
| MopB_CT_NDH-1_NuoG2-N7 |
cd02788 |
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ... |
690-767 |
6.56e-06 |
|
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant 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, 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 and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.
Pssm-ID: 239189 [Multi-domain] Cd Length: 96 Bit Score: 45.38 E-value: 6.56e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1269139799 690 RFAPWPMVR-VDHLVRRSLPLQETLAKEFktIRLNTKTAKKFNFNEGDQLTAIQGESRITLPLAIDDRLADNTVLLASG 767
Cdd:cd02788 2 QLVPYYHLFgSEELSQRSPVIAERAPAPY--ARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVGLPLG 78
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
223-327 |
1.33e-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: 48.76 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 223 PHDCVGGNIFLHsrwqefVPQREVMRAVPRENDEVNETWM--SDRDRfghfaVYHESRLYQPRIKK-------------- 286
Cdd:cd02751 1 PTACHWGPFKAH------VKDGVIVRVEPDDTDQPRPCPRgrSVRDR-----VYSPDRIKYPMKRVgwlgngpgsrelrg 69
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1269139799 287 DGKWEAISWEDALRIVKEKTQAIIEKHGASqtgALLSPSAT 327
Cdd:cd02751 70 EGEFVRISWDEALDLVASELKRIREKYGNE---AIFGGSYG 107
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
58-204 |
2.26e-05 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 47.71 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 58 PLPACATPVTAGMKVFTQSKKALEAQRAVMEFLLINHPLDCPICDQGGECELQDLAMGFGRAHSNYEDTKRAVFSDDIGP 137
Cdd:COG4624 5 LRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGP 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1269139799 138 LIETEMTRCIQCTRCVRFGEEIAGLPELGVINRGEKEAIStyvkhfmrselSGNIIDICPVGALTDK 204
Cdd:COG4624 85 SIIRDKEKCKNCYPCVRACPVKAIKVDDGKAEIDEEKCIS-----------CGQCVAVCPFGAITEK 140
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
4-67 |
5.10e-05 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 42.13 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 4 LEIDGKKTTAEEGA---SIIEAADEMGVYIPRFCYHkklsvaANCRMCLVEVEK----------------SGKPLPACAT 64
Cdd:pfam00111 1 VTINGKGVTIEVPDgetTLLDAAEEAGIDIPYSCRG------GGCGTCAVKVLEgedqsdqsfleddelaAGYVVLACQT 74
|
...
gi 1269139799 65 PVT 67
Cdd:pfam00111 75 YPK 77
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
271-630 |
2.89e-04 |
|
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: 44.40 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 271 FAVYHESRLYQP-RIKKDGKWEAISWEDALRIVKEKTQAIIEKHG-ASQTGALLSPS--ATIEEyflFQKWLRGLGSHNI 346
Cdd:cd02764 92 LSLYDPDRAQGPlRRGIDGAYVASDWADFDAKVAEQLKAVKDGGKlAVLSGNVNSPTteALIGD---FLKKYPGAKHVVY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 347 DH------RVRWQDfrdqntfdAFPNLGMPITELENLNAILLIGSNVrFEQPLLSHRMNKAYGEGAKILAINPMDYPFVF 420
Cdd:cd02764 169 DPlsaedvNEAWQA--------SFGKDVVPGYDFDKAEVIVSIDADF-LGSWISAIRHRHDFAAKRRLGAEEPMSRLVAA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 421 GIN---------EKMIVSPSALIPALADVAKALAKEKSSEKAKVIAETLVSAEKAAiflgehaLHHPEAAKIREWAHFIA 491
Cdd:cd02764 240 ESVytltganadVRLAIRPSQEKAFALGLAHKLIKKGAGSSLPDFFRALNLAFKPA-------KVAELTVDLDKALAALA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 492 QQSGA------TVGLLTEGANSAGAWLAG------------ALPHRRPGGQRLDSPGLDAKAM---LTTDPLKAYFLLNL 550
Cdd:cd02764 313 KALAAagkslvVAGSELSQTAGADTQVAVnalnsllgndgkTVDHARPIKGGELGNQQDLKALasrINAGKVSALLVYDV 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 551 EPEFDCAYPAQALHTLNQAEWVVAFTTFTTPTMESyADILLPIAPFSESGGTYVNAEGRWQWASAASVPEKDAQPAWKVL 630
Cdd:cd02764 393 NPVYDLPQGLGFAKALEKVPLSVSFGDRLDETAML-CDWVAPMSHGLESWGDAETPDGTYSICQPVIAPLFDTRSAQESL 471
|
|
| COG3894 |
COG3894 |
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ... |
2-100 |
8.91e-04 |
|
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown];
Pssm-ID: 443101 [Multi-domain] Cd Length: 621 Bit Score: 42.87 E-value: 8.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 2 VELEIDGKKTTAEEGASIIEAADEMGVYIPRFCYHKKLsvaanCRMCLVEVEkSGKPLP--------------------A 61
Cdd:COG3894 6 VTFLPSGKRVEVEAGTTLLDAAREAGVDIDAPCGGRGT-----CGKCKVKVE-EGEFSPvteeerrllspeelaegyrlA 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1269139799 62 CATPVTAGMKVFTQSKKALEAQRAVMEFLLINHPLDCPI 100
Cdd:COG3894 80 CQARVLGDLVVEVPPESRLDKQKILKEGLEREIELDPAV 118
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
274-347 |
1.02e-03 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 42.58 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1269139799 274 YHESRLYQP--RIK-----KDGKWEAISWEDALRIVKEKTQAIIEKHGASQTGALLSPSATIEEYFLFQKWLR-GLGSHN 345
Cdd:PRK13532 93 YGKDRLTQPllRMKdgkydKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKaGFRSNN 172
|
..
gi 1269139799 346 ID 347
Cdd:PRK13532 173 ID 174
|
|
| |
