|
Name |
Accession |
Description |
Interval |
E-value |
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
7-658 |
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: 707.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 7 IHVDGKEYEVDGADNLLHACLSLGLDIPYFCWHPALGSVGACRQCAVKQYqnaddTRGRLVMSCMTPAQDGTFISIDDEE 86
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVE-----KFPKPVASCATPVTDGMKISTNSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 87 AKKFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSVRKYRFTKRTHQNQELGPFVAHEMNRCIACYRCVRYYKD 166
Cdd:TIGR01973 76 VKKAREGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 167 YADGTDFGVYGAHDNVYFGRPESGTLESEFSGNLVEICPTGVFTDKTHSERYnRKWDMQFAPSVCQQCSVGCNISPGERY 246
Cdd:TIGR01973 156 VAGVEDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKA-RPWELKSTPSICVHDSVGCNIRVDERN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 247 GELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRR-GDDWLTINAEQAERAAADMLYHAKRTIGIGSPRASV 325
Cdd:TIGR01973 235 GEIMRILPRENDEINEEWLCDKGRFGYDGLNRQDRLTKPLLRNqEGNLLEVSWAEALAIAAEKLKASSRIGGIAGPRSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 326 ESNFALRELV---GAENFFSGLSAGEQHRLEMMLEILqqggiYTPSLREMENYDAVLVLGEDLTQTAARVALSVRQAVKG 402
Cdd:TIGR01973 315 EELFALKKLVrklGSENFDLRIRNYEFESADLRANYL-----FNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 403 KArEMAAAQKVADWQIAAIQNIGqrakyPLFVTAVDTTRLADVAalhynapvddqarlgfavaniidntapavtdlpadv 482
Cdd:TIGR01973 390 GG-AKVALIGIEKWNLTYPANTN-----LVFHPGLSPKKLDDIA------------------------------------ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 483 KAQAEMIAQALNGAKKPLIISGSN----PGSDALIQAAANVAWALKDKGID-AGLTFVGAEANSFGAAMTEAQPLDKAlA 557
Cdd:TIGR01973 428 SGAHSDIAAALKAAKKPLIIVGDSaishLDGAALISAAANIAKVIKVRRKEwNGLNILSSGANSVGLLDLGGESTGLD-A 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 558 LLADGSADTVVVMENDLYRHADKAAVDRALDAAANVIVLDHQRTDIMDKASLILSASSFAESDGTLINHEGRAQRFFQVY 637
Cdd:TIGR01973 507 ALNLGAADALFLLGADLERALDKTARDALSKADAFIIYQGHHGTETAEKADVILPGAAFTEKSGTYVNLEGRAQRFEQAV 586
|
650 660
....*....|....*....|.
gi 802097494 638 EPSFydksiIMHESWRWLTAL 658
Cdd:TIGR01973 587 KPPG-----EAREDWRILRAL 602
|
|
| 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 ... |
228-700 |
0e+00 |
|
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: 562.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 228 PSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRGDDWLTINAEQAERAAAD 307
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEALDVAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 308 MLYHAK-RTIGIGSPRASVESNFALRELVGAenfFSGLSAGEQHRLEMMLEILQQGGIYTPSLREMENYDAVLVLGEDLT 386
Cdd:cd02771 81 RLKEAKdKVGGIGSPRASNESNYALQKLVGA---VLGTNNVDHRARRLIAEILRNGPIYIPSLRDIESADAVLVLGEDLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 387 QTAARVALSVRQAVKGKAREMAAAQKVADWQIAAIQNIGQRAKYPLFVTAVDTTRLADVAALHYNAPVDDQARLGFAVAN 466
Cdd:cd02771 158 QTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDDIAAESIRASPGGQARLGAALAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 467 IIDNTAPAVTDLPADVKAQAemIAQALNGAKKPLIISGSNPGSDALIQAAANVAWALKDKGIDAGLTFVGAEANSFGAAM 546
Cdd:cd02771 238 AVDASAAGVSGLAPKEKAAR--IAARLTGAKKPLIVSGTLSGSLELIKAAANLAKALKRRGENAGLTLAVEEGNSPGLLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 547 TEAQP------LDKALALLADGSADTVVVMENDLYRHADKAAVDRALDAAANVIVLDHQRTDIMDKASLILSASSFAESD 620
Cdd:cd02771 316 LGGHVtepgldLDGALAALEDGSADALIVLGNDLYRSAPERRVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 621 GTLINHEGRAQRFFQVYEPSFYDksiiMHESWRWLTALYNDLNENTR--DWSQLDHVIDACIEQMPhlAGIKDAAPDAAF 698
Cdd:cd02771 396 GTFVNYEGRAQRFFKAYDDPAGD----ARSDWRWLHALAAKLGGKLVpsDAAILDEIIALVPGKAP--VGGHLYGGDPGV 469
|
..
gi 802097494 699 RI 700
Cdd:cd02771 470 TL 471
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
4-685 |
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: 549.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 4 MATIHVDGKEYEVDGADNLLHACLSLGLDIPYFCWHPALGSVGACRQCAVKQyqnadDTRGRLVMSCMTPAQDGTFISID 83
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEV-----EGAPKPVASCATPVTDGMVVKTD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 84 DEEAKKFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSVRKYRFTKRTHQNQELGPFVAHEMNRCIACYRCVRY 163
Cdd:COG1034 76 SPKVKKARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 164 YKDYADGTDFGVYGAHDNVYFGRPESGTLESEFSGNLVEICPTGVFTDKTHSErYNRKWDMQFAPSVCQQCSVGCNISPG 243
Cdd:COG1034 156 CDEIAGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRF-KARPWELKKTPSICPHCSVGCNIRVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 244 ERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRGDDWLTINAEQAERAAADmlyhakrtigigspra 323
Cdd:COG1034 235 VRGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELVEASWEEALAAAAE---------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 324 svesnfALRELVGAENffsglsageqhrlemmleilqqggiytpslremenydavlvlgedltqtaarvalsvrqavkgk 403
Cdd:COG1034 299 ------GLKALKKAEN---------------------------------------------------------------- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 404 aremaaaqkvadwqiaaiqnigqrakyplfvtavdttrladvaalhynapvddqaRLGFAVANIIDNTapavtdlpadvk 483
Cdd:COG1034 309 -------------------------------------------------------SVGAALLGALPDA------------ 321
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 484 aqAEMIAQALNGAKKPLIIsgsnpgsdaliqaaanvawalkdkgidagltfvgaeansfgaamteaqpldkalalladgs 563
Cdd:COG1034 322 --AAILEAAEAGKLKALVL------------------------------------------------------------- 338
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 564 adtvvvMENDLYRHADKAAvDRALDAAANVIVLDHQRTDIMDKASLILSASSFAESDGTLINHEGRAQRFFQVYEPSFYD 643
Cdd:COG1034 339 ------LGADPYDLDPAAA-LAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGRVQRFNAAVPPPGEA 411
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 802097494 644 KsiimhESWRWLTALYNDLNENTrDWSQLDHVIDACIEQMPH 685
Cdd:COG1034 412 R-----PDWRVLRALANALGAGL-PYDSLEEVRAELAAEAPA 447
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
4-905 |
1.52e-49 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 188.62 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 4 MATIHVDGKEYEVDGADNLLHACLSLGLDIPYFCWHPALGSVGACRQCAVkqyqnadDTRG--RLVMSCMTPAQDGTFI- 80
Cdd:PRK07860 4 LVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLV-------EVEGqrKPQASCTTTVTDGMVVk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 81 -SIDDEEAKKFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSVRKYRFTKRTHQNQ-ELGPFVAHEMNRCIACY 158
Cdd:PRK07860 77 tQLTSPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFPKPiNISTQVLLDRERCVLCA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 159 RCVRYYKDYAdGTDF---GVYGAHDNVyfGRPESGTLESEFSGNLVEICPTGVFTDKTHSERyNRKWDMQFAPSVCQQCS 235
Cdd:PRK07860 157 RCTRFSDQIA-GDPFidlQERGALQQV--GIYEGEPFQSYFSGNTVQICPVGALTGAAYRFR-ARPFDLVSTPSVCEHCA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 236 VGCNISPGERYGELRRienRYNG---TINHYFLCDKGRFGYGYVNRDDRPRQPQQRRGDDWL-TINAEQAERAAADMLYH 311
Cdd:PRK07860 233 SGCAQRTDHRRGKVLR---RLAGddpEVNEEWNCDKGRWAFTYATQPDRITTPLVRDEDGELePASWSEALAVAARGLAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 312 AKRTIGI---GspRASVE-----SNFAlRELVGAEN--FFS-GLSAGEQHRLEMMLEILQQGGIYTpslrEMENYDAVLV 380
Cdd:PRK07860 310 ARGRVGVlvgG--RLTVEdayayAKFA-RVALGTNDidFRArPHSAEEADFLAARVAGRGLGVTYA----DLEKAPAVLL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 381 LGEDLTQTAARVALSVRQAV-KGKAREMAaaqkVADWQIAAIQNIGQRakyplFVTAVDTTRLADVAALHYNAPVDDQA- 458
Cdd:PRK07860 383 VGFEPEEESPIVFLRLRKAArKHGLKVYS----IAPFATRGLEKMGGT-----LLRTAPGGEAAALDALATGAPDVAELl 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 459 -----------RLGF------AVANIIDNTAPAVTDLPADVKAQAEMIAQALngakkPLIISGSNPGSDALIQAAANVAW 521
Cdd:PRK07860 454 rtpgavilvgeRLATvpgalsAAARLADATGARLAWVPRRAGERGALEAGAL-----PTLLPGGRPVADPAARAEVAAAW 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 522 alkdkGIDAGLTFVGAEAnsfgAAMteaqpldkaLALLADGSADTVVVMENDLYRHADKAAVDRALDAAANVIVLDHQRT 601
Cdd:PRK07860 529 -----GVDELPAAPGRDT----AGI---------LAAAAAGELGALLVGGVEPADLPDPAAALAALDAAGFVVSLELRHS 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 602 DIMDKASLILSASSFAESDGTLINHEGRAqRFFqvyEPSFYDksiimheswrwlTALYNDLnentrdwsqldHVIDACIE 681
Cdd:PRK07860 591 AVTERADVVLPVAPVAEKAGTFLNWEGRL-RPF---EAALRT------------TGALSDL-----------RVLDALAD 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 682 QMphlaGIKDAAPDAAfRIRGQkLAREPhRYSGRTAMLANVSVHEQRQPQDKDTAFAfsmegnnspsaprqqipfawapG 761
Cdd:PRK07860 644 EM----GVDLGLPTVA-AARAE-LARLG-AWDGARAAAPAVPAAAPPQPGAGEAVLA----------------------T 694
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 762 WNspqawnkfQAEVGGHLRFGDPgvrlfsekdggmdyfstipaafapqqnvwtvapyyHLFGseelSQRAPViqermtds 841
Cdd:PRK07860 695 WR--------MLLDDGRLQDGEP-----------------------------------HLAG----TARPPV-------- 719
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802097494 842 yVMLNAQDAQQLNVAEGQILSVQLTDGALTLPVRIsTQLTAGQIGLPLGMPGIS-----PVLAGAVVNL 905
Cdd:PRK07860 720 -ARLSAATAAEIGVADGDAVTVSTERGSITLPLAI-TDMPDRVVWLPLNSPGSTvrrtlGATAGAVVRI 786
|
|
| 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 ... |
813-907 |
5.60e-32 |
|
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: 119.72 E-value: 5.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 813 WTVAPYYHLFGSEELSQRAPVIQERMTDSYVMLNAQDAQQLNVAEGQILSVQLTDGALTLPVRISTQLTAGQIGLPLGM- 891
Cdd:cd02788 1 WQLVPYYHLFGSEELSQRSPVIAERAPAPYARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVGLPLGAg 80
|
90
....*....|....*..
gi 802097494 892 -PGIsPVLAGAVVNLQE 907
Cdd:cd02788 81 fPGA-PVAEQTVVKLAA 96
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
91-131 |
3.74e-16 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 72.62 E-value: 3.74e-16
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 802097494 91 RESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSVRKY 131
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
91-126 |
1.73e-14 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 67.86 E-value: 1.73e-14
10 20 30
....*....|....*....|....*....|....*.
gi 802097494 91 RESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGH 126
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGV 36
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
7-658 |
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: 707.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 7 IHVDGKEYEVDGADNLLHACLSLGLDIPYFCWHPALGSVGACRQCAVKQYqnaddTRGRLVMSCMTPAQDGTFISIDDEE 86
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVE-----KFPKPVASCATPVTDGMKISTNSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 87 AKKFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSVRKYRFTKRTHQNQELGPFVAHEMNRCIACYRCVRYYKD 166
Cdd:TIGR01973 76 VKKAREGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 167 YADGTDFGVYGAHDNVYFGRPESGTLESEFSGNLVEICPTGVFTDKTHSERYnRKWDMQFAPSVCQQCSVGCNISPGERY 246
Cdd:TIGR01973 156 VAGVEDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKA-RPWELKSTPSICVHDSVGCNIRVDERN 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 247 GELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRR-GDDWLTINAEQAERAAADMLYHAKRTIGIGSPRASV 325
Cdd:TIGR01973 235 GEIMRILPRENDEINEEWLCDKGRFGYDGLNRQDRLTKPLLRNqEGNLLEVSWAEALAIAAEKLKASSRIGGIAGPRSSL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 326 ESNFALRELV---GAENFFSGLSAGEQHRLEMMLEILqqggiYTPSLREMENYDAVLVLGEDLTQTAARVALSVRQAVKG 402
Cdd:TIGR01973 315 EELFALKKLVrklGSENFDLRIRNYEFESADLRANYL-----FNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 403 KArEMAAAQKVADWQIAAIQNIGqrakyPLFVTAVDTTRLADVAalhynapvddqarlgfavaniidntapavtdlpadv 482
Cdd:TIGR01973 390 GG-AKVALIGIEKWNLTYPANTN-----LVFHPGLSPKKLDDIA------------------------------------ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 483 KAQAEMIAQALNGAKKPLIISGSN----PGSDALIQAAANVAWALKDKGID-AGLTFVGAEANSFGAAMTEAQPLDKAlA 557
Cdd:TIGR01973 428 SGAHSDIAAALKAAKKPLIIVGDSaishLDGAALISAAANIAKVIKVRRKEwNGLNILSSGANSVGLLDLGGESTGLD-A 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 558 LLADGSADTVVVMENDLYRHADKAAVDRALDAAANVIVLDHQRTDIMDKASLILSASSFAESDGTLINHEGRAQRFFQVY 637
Cdd:TIGR01973 507 ALNLGAADALFLLGADLERALDKTARDALSKADAFIIYQGHHGTETAEKADVILPGAAFTEKSGTYVNLEGRAQRFEQAV 586
|
650 660
....*....|....*....|.
gi 802097494 638 EPSFydksiIMHESWRWLTAL 658
Cdd:TIGR01973 587 KPPG-----EAREDWRILRAL 602
|
|
| 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 ... |
228-700 |
0e+00 |
|
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: 562.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 228 PSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRGDDWLTINAEQAERAAAD 307
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEALDVAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 308 MLYHAK-RTIGIGSPRASVESNFALRELVGAenfFSGLSAGEQHRLEMMLEILQQGGIYTPSLREMENYDAVLVLGEDLT 386
Cdd:cd02771 81 RLKEAKdKVGGIGSPRASNESNYALQKLVGA---VLGTNNVDHRARRLIAEILRNGPIYIPSLRDIESADAVLVLGEDLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 387 QTAARVALSVRQAVKGKAREMAAAQKVADWQIAAIQNIGQRAKYPLFVTAVDTTRLADVAALHYNAPVDDQARLGFAVAN 466
Cdd:cd02771 158 QTAPRIALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNALATRLDDIAAESIRASPGGQARLGAALAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 467 IIDNTAPAVTDLPADVKAQAemIAQALNGAKKPLIISGSNPGSDALIQAAANVAWALKDKGIDAGLTFVGAEANSFGAAM 546
Cdd:cd02771 238 AVDASAAGVSGLAPKEKAAR--IAARLTGAKKPLIVSGTLSGSLELIKAAANLAKALKRRGENAGLTLAVEEGNSPGLLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 547 TEAQP------LDKALALLADGSADTVVVMENDLYRHADKAAVDRALDAAANVIVLDHQRTDIMDKASLILSASSFAESD 620
Cdd:cd02771 316 LGGHVtepgldLDGALAALEDGSADALIVLGNDLYRSAPERRVEAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKS 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 621 GTLINHEGRAQRFFQVYEPSFYDksiiMHESWRWLTALYNDLNENTR--DWSQLDHVIDACIEQMPhlAGIKDAAPDAAF 698
Cdd:cd02771 396 GTFVNYEGRAQRFFKAYDDPAGD----ARSDWRWLHALAAKLGGKLVpsDAAILDEIIALVPGKAP--VGGHLYGGDPGV 469
|
..
gi 802097494 699 RI 700
Cdd:cd02771 470 TL 471
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
4-685 |
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: 549.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 4 MATIHVDGKEYEVDGADNLLHACLSLGLDIPYFCWHPALGSVGACRQCAVKQyqnadDTRGRLVMSCMTPAQDGTFISID 83
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEV-----EGAPKPVASCATPVTDGMVVKTD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 84 DEEAKKFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSVRKYRFTKRTHQNQELGPFVAHEMNRCIACYRCVRY 163
Cdd:COG1034 76 SPKVKKARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 164 YKDYADGTDFGVYGAHDNVYFGRPESGTLESEFSGNLVEICPTGVFTDKTHSErYNRKWDMQFAPSVCQQCSVGCNISPG 243
Cdd:COG1034 156 CDEIAGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRF-KARPWELKKTPSICPHCSVGCNIRVD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 244 ERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRGDDWLTINAEQAERAAADmlyhakrtigigspra 323
Cdd:COG1034 235 VRGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELVEASWEEALAAAAE---------------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 324 svesnfALRELVGAENffsglsageqhrlemmleilqqggiytpslremenydavlvlgedltqtaarvalsvrqavkgk 403
Cdd:COG1034 299 ------GLKALKKAEN---------------------------------------------------------------- 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 404 aremaaaqkvadwqiaaiqnigqrakyplfvtavdttrladvaalhynapvddqaRLGFAVANIIDNTapavtdlpadvk 483
Cdd:COG1034 309 -------------------------------------------------------SVGAALLGALPDA------------ 321
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 484 aqAEMIAQALNGAKKPLIIsgsnpgsdaliqaaanvawalkdkgidagltfvgaeansfgaamteaqpldkalalladgs 563
Cdd:COG1034 322 --AAILEAAEAGKLKALVL------------------------------------------------------------- 338
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 564 adtvvvMENDLYRHADKAAvDRALDAAANVIVLDHQRTDIMDKASLILSASSFAESDGTLINHEGRAQRFFQVYEPSFYD 643
Cdd:COG1034 339 ------LGADPYDLDPAAA-LAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGRVQRFNAAVPPPGEA 411
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 802097494 644 KsiimhESWRWLTALYNDLNENTrDWSQLDHVIDACIEQMPH 685
Cdd:COG1034 412 R-----PDWRVLRALANALGAGL-PYDSLEEVRAELAAEAPA 447
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
228-662 |
8.75e-109 |
|
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: 340.41 E-value: 8.75e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 228 PSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRGDDWLTINAEQAERAAAD 307
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVSWEEALKTVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 308 ML--YHAKRTIGIGSPRASVESNFALRELVGAEnffsGLSAGEQHRLEMMLEI---LQQGGIYTPSLREMENYDAVLVLG 382
Cdd:cd02768 81 GLkaVKGDKIGGIAGPRADLESLFLLKKLLNKL----GSNNIDHRLRQSDLPAdnrLRGNYLFNTSIAEIEEADAVLLIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 383 EDLTQTAARVALSVRQAVKGKaremaaaqkvadwqiaaiqnigqraKYPLFVTAVDTTRLadvaALHYNAPVDDqarLGF 462
Cdd:cd02768 157 SNLRKEAPLLNARLRKAVKKK-------------------------GAKIAVIGPKDTDL----IADLTYPVSP---LGA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 463 AVANIIDNTAPAVTDLpadvkaqaemIAQALNGAKKPLIISGS---NPGSDALIQAAANVAWALkdkGIDAGLTFVGAEA 539
Cdd:cd02768 205 SLATLLDIAEGKHLKP----------FAKSLKKAKKPLIILGSsalRKDGAAILKALANLAAKL---GTGAGLWNGLNVL 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 540 NSFGAAMTEAQpLDKALALLADGSADTVVVMENDLYRHADKAAVdrALDAAANVIVLDHQRTDIMDKASLILSASSFAES 619
Cdd:cd02768 272 NSVGARLGGAG-LDAGLALLEPGKAKLLLLGEDELDRSNPPAAV--ALAAADAFVVYQGHHGDTGAQADVILPAAAFTEK 348
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 802097494 620 DGTLINHEGRAQRFFQVYEPsFYDksiiMHESWRWLTALYNDL 662
Cdd:cd02768 349 SGTYVNTEGRVQRFKKAVSP-PGD----AREDWKILRALSNLL 386
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
4-905 |
1.52e-49 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 188.62 E-value: 1.52e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 4 MATIHVDGKEYEVDGADNLLHACLSLGLDIPYFCWHPALGSVGACRQCAVkqyqnadDTRG--RLVMSCMTPAQDGTFI- 80
Cdd:PRK07860 4 LVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLV-------EVEGqrKPQASCTTTVTDGMVVk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 81 -SIDDEEAKKFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSVRKYRFTKRTHQNQ-ELGPFVAHEMNRCIACY 158
Cdd:PRK07860 77 tQLTSPVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFPKPiNISTQVLLDRERCVLCA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 159 RCVRYYKDYAdGTDF---GVYGAHDNVyfGRPESGTLESEFSGNLVEICPTGVFTDKTHSERyNRKWDMQFAPSVCQQCS 235
Cdd:PRK07860 157 RCTRFSDQIA-GDPFidlQERGALQQV--GIYEGEPFQSYFSGNTVQICPVGALTGAAYRFR-ARPFDLVSTPSVCEHCA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 236 VGCNISPGERYGELRRienRYNG---TINHYFLCDKGRFGYGYVNRDDRPRQPQQRRGDDWL-TINAEQAERAAADMLYH 311
Cdd:PRK07860 233 SGCAQRTDHRRGKVLR---RLAGddpEVNEEWNCDKGRWAFTYATQPDRITTPLVRDEDGELePASWSEALAVAARGLAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 312 AKRTIGI---GspRASVE-----SNFAlRELVGAEN--FFS-GLSAGEQHRLEMMLEILQQGGIYTpslrEMENYDAVLV 380
Cdd:PRK07860 310 ARGRVGVlvgG--RLTVEdayayAKFA-RVALGTNDidFRArPHSAEEADFLAARVAGRGLGVTYA----DLEKAPAVLL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 381 LGEDLTQTAARVALSVRQAV-KGKAREMAaaqkVADWQIAAIQNIGQRakyplFVTAVDTTRLADVAALHYNAPVDDQA- 458
Cdd:PRK07860 383 VGFEPEEESPIVFLRLRKAArKHGLKVYS----IAPFATRGLEKMGGT-----LLRTAPGGEAAALDALATGAPDVAELl 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 459 -----------RLGF------AVANIIDNTAPAVTDLPADVKAQAEMIAQALngakkPLIISGSNPGSDALIQAAANVAW 521
Cdd:PRK07860 454 rtpgavilvgeRLATvpgalsAAARLADATGARLAWVPRRAGERGALEAGAL-----PTLLPGGRPVADPAARAEVAAAW 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 522 alkdkGIDAGLTFVGAEAnsfgAAMteaqpldkaLALLADGSADTVVVMENDLYRHADKAAVDRALDAAANVIVLDHQRT 601
Cdd:PRK07860 529 -----GVDELPAAPGRDT----AGI---------LAAAAAGELGALLVGGVEPADLPDPAAALAALDAAGFVVSLELRHS 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 602 DIMDKASLILSASSFAESDGTLINHEGRAqRFFqvyEPSFYDksiimheswrwlTALYNDLnentrdwsqldHVIDACIE 681
Cdd:PRK07860 591 AVTERADVVLPVAPVAEKAGTFLNWEGRL-RPF---EAALRT------------TGALSDL-----------RVLDALAD 643
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 682 QMphlaGIKDAAPDAAfRIRGQkLAREPhRYSGRTAMLANVSVHEQRQPQDKDTAFAfsmegnnspsaprqqipfawapG 761
Cdd:PRK07860 644 EM----GVDLGLPTVA-AARAE-LARLG-AWDGARAAAPAVPAAAPPQPGAGEAVLA----------------------T 694
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 762 WNspqawnkfQAEVGGHLRFGDPgvrlfsekdggmdyfstipaafapqqnvwtvapyyHLFGseelSQRAPViqermtds 841
Cdd:PRK07860 695 WR--------MLLDDGRLQDGEP-----------------------------------HLAG----TARPPV-------- 719
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802097494 842 yVMLNAQDAQQLNVAEGQILSVQLTDGALTLPVRIsTQLTAGQIGLPLGMPGIS-----PVLAGAVVNL 905
Cdd:PRK07860 720 -ARLSAATAAEIGVADGDAVTVSTERGSITLPLAI-TDMPDRVVWLPLNSPGSTvrrtlGATAGAVVRI 786
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
228-660 |
1.86e-49 |
|
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: 179.45 E-value: 1.86e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 228 PSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRG--DDWLTINAEQAERAA 305
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 306 ADML------YHAKRTIGIGSPRASVESNFALREL--------VGAENFFSGLSAGEQHRLEMmleilqqGGIYTPSLRE 371
Cdd:cd00368 81 AEKLkeirekYGPDAIAFYGGGGASNEEAYLLQKLlralgsnnVDSHARLCHASAVAALKAFG-------GGAPTNTLAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 372 MENYDAVLVLGEDLTQTAARVALSVRQAVKGKARemaaaqkvadwqiaaiqnigqrakypLFVTAVDTTRLADVAALHYn 451
Cdd:cd00368 154 IENADLILLWGSNPAETHPVLAARLRRAKKRGAK--------------------------LIVIDPRRTETAAKADEWL- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 452 apvddQARLGfavaniidntapavTDLpadvkaqaemiaqALNGAKKPLIISGSnpgSDALIQAAANVAWALKDKGIDAG 531
Cdd:cd00368 207 -----PIRPG--------------TDA-------------ALALAEWAAEITGV---PAETIRALAREFAAAKRAVILWG 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 532 LTFVGAEANSFGAAMTEAQPLDKALALLADGsadTVVVMENDLYRHADKAAVDRALDAAANVIVLDHQRTDIMDKASLIL 611
Cdd:cd00368 252 MGLTQHTNGTQNVRAIANLAALTGNIGRPGG---GLGPGGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAAYADVVL 328
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 802097494 612 SASSFAESDGTLINHEGRAQRFFQVYEPSFYDKSiimheSWRWLTALYN 660
Cdd:cd00368 329 PAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARS-----DWEILRELAK 372
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
228-662 |
2.46e-32 |
|
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: 130.55 E-value: 2.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 228 PSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRGDDWLTINAEQAERAAAD 307
Cdd:cd02772 1 KSVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEDRLTKPMIKKDGQWQEVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 308 ML-----YHAKRTIG-IGSPRASVESNFALREL---VGAENFfsglsageQHRLEMMLEILQQGGIYTP----SLREMEN 374
Cdd:cd02772 81 GLsaiikKHGADQIGaLASPHSTLEELYLLQKLargLGSDNI--------DHRLRQSDFRDDAKASGAPwlgmPIAEISE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 375 YDAVLVLGEDLTQTAARVALSVRQAVKGKAremaaaqkvadwQIAAIQNigqrAKYPlFVTAVDTTRLADVAALHYnapv 454
Cdd:cd02772 153 LDRVLVIGSNLRKEHPLLAQRLRQAVKKGA------------KLSAINP----ADDD-FLFPLSGKAIVAPSALAN---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 455 ddqARLGFAVAN-IIDNTAPAVTDLPADVKAQAEMIAQALNGAKKPLIISGS----NPGSDALIQAAANVAwalkdKGID 529
Cdd:cd02772 212 ---ALAQVAKALaEEKGLAVPDEDAKVEASEEARKIAASLVSAERAAVFLGNlaqnHPQAATLRALAQEIA-----KLTG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 530 AGLTFVGAEANSFGAAMTEAQPL--DKALALLADGSADTVVVMENDLYRHADKAAVDRALDAAANVIVLDHQRTDIM-DK 606
Cdd:cd02772 284 ATLGVLGEGANSVGAYLAGALPHggLNAAAMLEQPRKAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAALlDY 363
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 802097494 607 ASLILSASSFAESDGTLINHEGRAQRFFQVYEPsFYDKsiimHESWRWLTALYNDL 662
Cdd:cd02772 364 ADVLLPIAPFTETSGTFVNLEGRVQSFKGVVKP-LGEA----RPAWKVLRVLGNLL 414
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
20-207 |
3.19e-32 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 127.46 E-value: 3.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 20 DNLLHACLSLGLDIPYFCWHPALGSVGACRQCAVKqyqnADDTRGrLVMSCMTPAQDGTFISIDDEEAKKFRESVVEWLM 99
Cdd:PTZ00305 85 ENLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQ----VDGTQN-LVVSCATVALPGMSIITDSRLVRDAREGNVELIL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 100 TNHPHDCPVCEEGGNCHLQDMTVMTGHSVRKYRFTKRTHQNQELGPFVAHEMNRCIACYRCVRYYKDYADGTDFGVYGAH 179
Cdd:PTZ00305 160 INHPNDCPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTRVVLNRCIHCTRCVRFLNEHAQDFNLGMIGRG 239
|
170 180 190
....*....|....*....|....*....|....
gi 802097494 180 dnvyfGRPESGT----LESEFSGNL--VEICPTG 207
Cdd:PTZ00305 240 -----GLSEISTfldeLEVKTDNNMpvSQLCPVG 268
|
|
| 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 ... |
813-907 |
5.60e-32 |
|
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: 119.72 E-value: 5.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 813 WTVAPYYHLFGSEELSQRAPVIQERMTDSYVMLNAQDAQQLNVAEGQILSVQLTDGALTLPVRISTQLTAGQIGLPLGM- 891
Cdd:cd02788 1 WQLVPYYHLFGSEELSQRSPVIAERAPAPYARLSPADAARLGLADGDLVEFSLGDGTLTLPVQISKYLPAGVVGLPLGAg 80
|
90
....*....|....*..
gi 802097494 892 -PGIsPVLAGAVVNLQE 907
Cdd:cd02788 81 fPGA-PVAEQTVVKLAA 96
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
224-639 |
1.09e-30 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 129.23 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 224 MQFAPSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRGDDWLTINAEQAER 303
Cdd:COG3383 4 MKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVSWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 304 AAADMLYHAKRTIG------IGSPRASVESNFAL----RELVGAENFFSglsageQHRLEM------MLEILQQGGIyTP 367
Cdd:COG3383 84 LVAERLREIQAEHGpdavafYGSGQLTNEENYLLqklaRGVLGTNNIDN------NARLCMasavagLKQSFGSDAP-PN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 368 SLREMENYDAVLVLGEDLTQTAARVALSVRQAVKGKARemaaaqkvadwqiaaiqnigqrakypLFVtaVDT--TRLADV 445
Cdd:COG3383 157 SYDDIEEADVILVIGSNPAEAHPVLARRIKKAKKNGAK--------------------------LIV--VDPrrTETARL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 446 AALHYN-APVDDQARLGfAVAN-IIDN----------------------------TAPAVTDLPA-DVKAQAEMIAQaln 494
Cdd:COG3383 209 ADLHLQiKPGTDLALLN-GLLHvIIEEglvdedfiaertegfeelkasvakytpeRVAEITGVPAeDIREAARLIAE--- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 495 gAKKPLIISG-----SNPGSDAlIQAAANVAWALKDKGID-AGLTFVGAEANSFGAAMTEA--------QPLDKA----- 555
Cdd:COG3383 285 -AKRAMILWGmgvnqHTQGTDN-VNAIINLALATGNIGRPgTGPFPLTGQNNVQGGRDMGAlpnvlpgyRDVTDPehrak 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 556 ---------------------LALLADGSADTVVVM-ENDLYRHADKAAVDRALDAAANVIVLDHQRTDIMDKASLILSA 613
Cdd:COG3383 363 vadawgvpplpdkpgltavemFDAIADGEIKALWIIgENPAVSDPDANHVREALEKLEFLVVQDIFLTETAEYADVVLPA 442
|
490 500
....*....|....*....|....*.
gi 802097494 614 SSFAESDGTLINHEGRAQRFFQVYEP 639
Cdd:COG3383 443 ASWAEKDGTFTNTERRVQRVRKAVEP 468
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
4-401 |
5.95e-28 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 121.35 E-value: 5.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 4 MATIHVDGKEYEVDGADNLLHACLSLGLDIPYFCWHPALGSVGACRQCAVkqyqnadDTRGRLVMSCMTPAQDGTFISID 83
Cdd:PRK08493 1 MITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMV-------EADGKRVYSCNTKAKEGMNILTN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 84 DEEAKKFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSVRKYRfTKRTHQNQELGPFVAHEMNRCIACYRCVRY 163
Cdd:PRK08493 74 TPNLMDERNAIMQTYDVNHPLECGVCDKSGECELQNFTHEMGVNHQPYA-IKDTHKPHKHWGKINYDPSLCIVCERCVTV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 164 YKDY------------ADGTD-----------FGVYGAHDNVYFGRPESGTLESEFSGNLVEICPTGVFTDKTHSERYNr 220
Cdd:PRK08493 153 CKDKigesalktvprgLDAPDksfkesmpkdaYAVWSKKQKSLIGPVGGETLDCSFCGECIAVCPVGALSSSDFQYTSN- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 221 KWDMQFAPSVCQQCSVGCNIspgerYGELRR--IENR----YNGTINHYF--LCDKGRFGYGYVNRDDRPrqpqqrrgdd 292
Cdd:PRK08493 232 AWELKKIPATCPHCSDCCLI-----YYDVKHssILNQeskiYRVSNDFYFnpLCGAGRFAFDFQNEADKD---------- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 293 wltinaEQAERAAADMLYHAKrTIGIGSpRASVESNFALRELvgAENFFSGLSAGE----QHRLEMMLEIlqQGGIYTPS 368
Cdd:PRK08493 297 ------EKAFKEAVEAFKEAK-AIKFNS-FITNEEALILQRL--KKKFGLKLINEEalkfQQFLKVFSEV--SGKSYSAN 364
|
410 420 430
....*....|....*....|....*....|...
gi 802097494 369 LREMENYDAVLVLGEDLTQTAARVALSVRQAVK 401
Cdd:PRK08493 365 LEDIKTSDFVVVAGSALKTDNPLLRYAINNALK 397
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
6-207 |
5.88e-27 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 110.13 E-value: 5.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 6 TIHVDGKEYEVDGADNLLHACLSLGLDIPYFCWHPALGSVGACRQCAVK-QYQNaddtrgRLVMSCMTPAQDGTFISIDD 84
Cdd:PRK07569 5 TLTIDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEiEGSN------KLLPACVTPVAEGMVVQTNT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 85 EEAKKFRESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTG--HSVRKYRFTKRTHQnqelgpfVAHEM-----NRCIAC 157
Cdd:PRK07569 79 PRLQEYRRMIVELLFAEGNHVCAVCVANGNCELQDLAIEVGmdHVRFPYLFPRRPVD-------ISHPRfgidhNRCVLC 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 802097494 158 YRCVRYYkDYADGT---DFGVYGAHDNVYFG--RP--ESGTLESefSGNLVEICPTG 207
Cdd:PRK07569 152 TRCVRVC-DEIEGAhtwDVAGRGAKSRVITDlnQPwgTSETCTS--CGKCVQACPTG 205
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
228-639 |
1.89e-24 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 108.45 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 228 PSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRGDDWLTINAEQAERAAAD 307
Cdd:cd02753 1 KTVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDEALSLVAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 308 ML------YHAKRTIGIGSPRASVESNFAL----RELVGAENFfsglsageQH--RL------EMMLEILQQGGIyTPSL 369
Cdd:cd02753 81 RLkeikdkYGPDAIAFFGSAKCTNEENYLFqklaRAVGGTNNV--------DHcaRLchsptvAGLAETLGSGAM-TNSI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 370 REMENYDAVLVLGEDLTQTAARVALSVRQAVKGKARemaaaqkvadwqiaaiqnigqrakypLFVTAVDTTRLADVAALH 449
Cdd:cd02753 152 ADIEEADVILVIGSNTTEAHPVIARRIKRAKRNGAK--------------------------LIVADPRRTELARFADLH 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 450 Y-NAPVDDQARLGfAVANII--------------------------DNT---APAVTDLPA-DVKAQAEMIAQALNGAkk 498
Cdd:cd02753 206 LqLRPGTDVALLN-AMAHVIieeglydeefieertegfeelkeiveKYTpeyAERITGVPAeDIREAARMYATAKSAA-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 499 plIISG-----SNPGSDALIqAAANVAWALKDKGID-AGLTFVGAEANSFGAAMTEAQPLD-----KALalladgsadtV 567
Cdd:cd02753 283 --ILWGmgvtqHSHGTDNVM-ALSNLALLTGNIGRPgTGVNPLRGQNNVQGACDMGALPNVlpgyvKAL----------Y 349
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 802097494 568 VVMENDLYRHADKAAVDRALDAAANVIVLDHQRTDIMDKASLILSASSFAESDGTLINHEGRAQRFFQVYEP 639
Cdd:cd02753 350 IMGENPALSDPNTNHVRKALESLEFLVVQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEP 421
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
91-131 |
3.74e-16 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 72.62 E-value: 3.74e-16
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 802097494 91 RESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGHSVRKY 131
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
91-126 |
1.73e-14 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 67.86 E-value: 1.73e-14
10 20 30
....*....|....*....|....*....|....*.
gi 802097494 91 RESVVEWLMTNHPHDCPVCEEGGNCHLQDMTVMTGH 126
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGV 36
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
224-277 |
6.73e-14 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 66.89 E-value: 6.73e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 802097494 224 MQFAPSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVN 277
Cdd:smart00926 1 EKWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVY 54
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
224-278 |
7.27e-14 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 66.55 E-value: 7.27e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 802097494 224 MQFAPSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNR 278
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
281-641 |
9.35e-13 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 70.89 E-value: 9.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 281 RPRQPQQRRGDD-WLTINAEQAERAAADML-----YHAKRTIGIG---SPRASVESNFALREL--------VGAENFFSG 343
Cdd:pfam00384 1 RLKYPMVRRGDGkFVRVSWDEALDLIAKKLkriikKYGPDAIAINggsGGLTDVESLYALKKLlnrlgsknGNTEDHNGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 344 LSAGEQHRLEMMLeilQQGGIYTPSLREMENYDAVLVLGEDLTQTAARVALSVRQAVKGKAREMAAAQKVADWQIAaIQN 423
Cdd:pfam00384 81 LCTAAAAAFGSDL---RSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYA-DEH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 424 IGQRAKyplfvtavdttrlADVAalhynapvddqarLGFAVANIIdntapavtdlpadvkAQAEMIAQALngAKKPLIIS 503
Cdd:pfam00384 157 LGIKPG-------------TDLA-------------LALAGAHVF---------------IKELKKDKDF--APKPIIIV 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 504 GSN----PGSDALIQAAANVAWALKDKGIDAGLTF---VGAEANSFGAAMTEAQPLDKALALLADGSADTVVVM-----E 571
Cdd:pfam00384 194 GAGvlqrQDGEAIFRAIANLADLTGNIGRPGGGWNglnILQGAASPVGALDLGLVPGIKSVEMINAIKKGGIKVlyllgN 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 802097494 572 NDLYRHADKAAVDRALDAAANVIVLD-HQRTDIMDKASLILSASSFAESDGTLINHEGRAQRFFQVYEPSF 641
Cdd:pfam00384 274 NPFVTHADENRVVKALQKLDLFVVYDgHHGDKTAKYADVILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPG 344
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
236-632 |
1.27e-12 |
|
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: 70.37 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 236 VGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDdRPRQPQQRRGDDWLTINAEQAERAAADML--YHAK 313
Cdd:cd02773 9 VGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQ-RLDKPYIRKNGKLKPATWEEALAAIAKALkgVKPD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 314 RTIGIGSPRASVESNFALRELV---GAENffsglsageqhrlemmLEILQQGGIYTPSLREM----------ENYDAVLV 380
Cdd:cd02773 88 EIAAIAGDLADVESMVALKDLLnklGSEN----------------LACEQDGPDLPADLRSNylfnttiagiEEADAVLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 381 LGEDLTQTAARVALSVRQAVKGKaremaaaqkvaDWQIAaiqNIGQrakyplfvtAVDTTrladvaalhYnaPVDDqarL 460
Cdd:cd02773 152 VGTNPRFEAPVLNARIRKAWLHG-----------GLKVG---VIGP---------PVDLT---------Y--DYDH---L 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 461 GfavaniidNTAPAVTDLPADVKAqaemIAQALNGAKKPLIISGSN----PGSDALIQAAANVAWALKDKGID------- 529
Cdd:cd02773 195 G--------TDAKTLQDIASGKHP----FSKALKDAKKPMIIVGSGalarKDGAAILAAVAKLAKKNGVVREGwngfnvl 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 530 -------AGLTfVGAEANSfGAAMTEAQPldKALALL-------ADGSADTVVVmendlYR--HADKAAVdraldaaanv 593
Cdd:cd02773 263 hraasrvGALD-LGFVPGA-GAIRKSGPP--KVLYLLgadeidiTPIPKDAFVV-----YQghHGDRGAQ---------- 323
|
410 420 430
....*....|....*....|....*....|....*....
gi 802097494 594 ivldhqrtdimdKASLILSASSFAESDGTLINHEGRAQR 632
Cdd:cd02773 324 ------------IADVILPGAAYTEKSGTYVNTEGRVQQ 350
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
6-80 |
3.08e-12 |
|
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: 63.18 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 6 TIHVDGKEYEVDGADNLLHACLSLGLDIPYFCWHpalgsvGACRQCAVK----QYQN-------ADDTRGRLVMSCMTPA 74
Cdd:cd00207 4 NVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEvvegEVDQsdpslldEEEAEGGYVLACQTRV 77
|
....*.
gi 802097494 75 QDGTFI 80
Cdd:cd00207 78 TDGLVI 83
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
3-77 |
1.04e-10 |
|
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: 58.70 E-value: 1.04e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 802097494 3 TMATIHVDGKEYEVDGADNLLHACLSLGLDIPYFCWHPA----LGSVGACRQCAVKqyqnaDDTRGRlVMSCMTPAQDG 77
Cdd:pfam13510 2 RPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVE-----VDGVPN-VRACTTPVREG 74
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
4-110 |
5.91e-08 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 56.66 E-value: 5.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 4 MATIH--VDGKEYEVDGADNLLHACLSLGLDIPYFCWHPALGSVGACRQCAVKQyqnadDTRGRLVMSCMTPAQDGTFIS 81
Cdd:PRK12814 1 MNTISltINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEI-----KGKNRFVPACSTAVSEGMVIE 75
|
90 100 110
....*....|....*....|....*....|.
gi 802097494 82 IDDEEAKKFRESVVEWLMTNHPHDC--PvCE 110
Cdd:PRK12814 76 TENAELHAMRRQSLERLIEQHCGDClgP-CE 105
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
7-75 |
3.60e-07 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 48.29 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 7 IHVDGKEYEVDGADN---LLHACLSLGLDIPYFCWHpalgsvGACRQCAVK---------QYQNADDTR--GRLVMSCMT 72
Cdd:pfam00111 1 VTINGKGVTIEVPDGettLLDAAEEAGIDIPYSCRG------GGCGTCAVKvlegedqsdQSFLEDDELaaGYVVLACQT 74
|
...
gi 802097494 73 PAQ 75
Cdd:pfam00111 75 YPK 77
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
223-904 |
1.55e-06 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 52.15 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 223 DMQFAPSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRG----DDWLTINA 298
Cdd:COG0243 20 GTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGprgsGKFERISW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 299 EQA-ERAAADMlyhaKRTI-------------GIGSPRASVESNFALRELV---GAENFFSGLS---AGEQHRLEMMLei 358
Cdd:COG0243 100 DEAlDLIAEKL----KAIIdeygpeavafytsGGSAGRLSNEAAYLAQRFAralGTNNLDDNSRlchESAVAGLPRTF-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 359 lqQGGIYTPSLREMENYDAVLVLGEDLTQTAARVALSVRQAVKGKAremaaaqkvadwqiaaiqnigqrAKyplfVTAVD 438
Cdd:COG0243 174 --GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRG-----------------------AK----IVVID 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 439 T--TRLADVAALHYnaPV----D-----------------DQARL-----GF-AVANIIDNTAP----AVTDLPA-DVKA 484
Cdd:COG0243 225 PrrTETAAIADEWL--PIrpgtDaalllalahvlieeglyDRDFLarhtvGFdELAAYVAAYTPewaaEITGVPAeDIRE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 485 QAEMIAQalngAKKPLIISG------SNpGSDAlIQAAANVAWALkdkG-ID---AGLTFVGAEansfgaAMTEAQPLD- 553
Cdd:COG0243 303 LAREFAT----AKPAVILWGmglqqhSN-GTQT-VRAIANLALLT---GnIGkpgGGPFSLTGE------AILDGKPYPi 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 554 KALalladgsadtVVVMENDLYRHADKAAVDRALDAAANVIVLDHQRTDIMDKASLILSASSFAESDGTLINHE-GRAQR 632
Cdd:COG0243 368 KAL----------WVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 633 FFQVYEPsfydksiiMHES---WRWLTAL--------YNDLNENTRDWsqLDHVIDACIEQMPHLAGIKDAAPdaafrir 701
Cdd:COG0243 438 SRPAVEP--------PGEArsdWEIFAELakrlgfeeAFPWGRTEEDY--LRELLEATRGRGITFEELREKGP------- 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 702 gqklarephrysgrtamlanvsvheQRQPQDKDTAFafsmegnnspsapRQQIPFAWAPGwnspqawnKFqaevgghlrf 781
Cdd:COG0243 501 -------------------------VQLPVPPEPAF-------------RNDGPFPTPSG--------KA---------- 524
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 782 gdpgvRLFSEKdggmDYFSTIPAAFAPQQNVWTVA-----------PYYHLFGSeelSQRAPVIQERMTDSYVMLNAQDA 850
Cdd:COG0243 525 -----EFYSET----LALPPLPRYAPPYEGAEPLDaeyplrlitgrSRDQWHST---TYNNPRLREIGPRPVVEINPEDA 592
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*.
gi 802097494 851 QQLNVAEGQIlsVQLT--DGALTLPVRISTQLTAGQIGLPLGMPGISPVLAGAVVN 904
Cdd:COG0243 593 AALGIKDGDL--VRVEsdRGEVLARAKVTEGIRPGVVFAPHGWWYEPADDKGGNVN 646
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
231-382 |
5.41e-05 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 47.01 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 231 CQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKG-RFGYgYVNRDDRPRQPQQRRGDDWLTINAEQAERAAADML 309
Cdd:cd02762 4 CILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAaALGD-YQNDPDRLRTPMRRRGGSFEEIDWDEAFDEIAERL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 310 Y-----HAKRTIGI--GSPRASVESNFA----LRELVGAENFFSGLSAGEQ-HRLEMMLEILQQGGIYTPslrEMENYDA 377
Cdd:cd02762 83 RairarHGGDAVGVygGNPQAHTHAGGAyspaLLKALGTSNYFSAATADQKpGHFWSGLMFGHPGLHPVP---DIDRTDY 159
|
....*
gi 802097494 378 VLVLG 382
Cdd:cd02762 160 LLILG 164
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
228-309 |
4.44e-04 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 43.93 E-value: 4.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 228 PSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRG--DDWLTINAEQA-ERA 304
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPgsGKWEEISWDEAlDEI 80
|
....*
gi 802097494 305 AADML 309
Cdd:cd02752 81 ARKMK 85
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
280-619 |
9.27e-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: 42.86 E-value: 9.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 280 DRPRQPQQRRGD------DWLTINAEQAE--RAAADMLYHAKRTIGIGSPRASVESNFALRELVGAENFFsgLSAGEQhr 351
Cdd:cd02764 98 DRAQGPLRRGIDgayvasDWADFDAKVAEqlKAVKDGGKLAVLSGNVNSPTTEALIGDFLKKYPGAKHVV--YDPLSA-- 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 352 lEMMLEILQQ--GGIYTPSLReMENYDAVLVLGEDLTQTAARVALSVRQAVKGKaREMAAAQKVADWQIAAIQNI-GQRA 428
Cdd:cd02764 174 -EDVNEAWQAsfGKDVVPGYD-FDKAEVIVSIDADFLGSWISAIRHRHDFAAKR-RLGAEEPMSRLVAAESVYTLtGANA 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 429 KYPLFVTAVDTTRLAdVAALHYNAPVDDQARLG-FAVANIIDNTAPAVTDLPADVKAQAEMIAQALNGAKKPLIISGSNP 507
Cdd:cd02764 251 DVRLAIRPSQEKAFA-LGLAHKLIKKGAGSSLPdFFRALNLAFKPAKVAELTVDLDKALAALAKALAAAGKSLVVAGSEL 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 802097494 508 GSDALIQAAANVaWALKDKgIDAGLTFVGAEANSFGAAMTEAQPLDKALALLADGSADTVVVME-NDLYRHADKAAVDRA 586
Cdd:cd02764 330 SQTAGADTQVAV-NALNSL-LGNDGKTVDHARPIKGGELGNQQDLKALASRINAGKVSALLVYDvNPVYDLPQGLGFAKA 407
|
330 340 350
....*....|....*....|....*....|...
gi 802097494 587 LDAAANVIVLDHQRTDIMDKASLILSASSFAES 619
Cdd:cd02764 408 LEKVPLSVSFGDRLDETAMLCDWVAPMSHGLES 440
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
228-290 |
3.05e-03 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 41.27 E-value: 3.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 802097494 228 PSVCQQCSVGCNISPGERYGELRRIENRYNGTINHYFLCDKGRFGYGYVNRDDRPRQPQQRRG 290
Cdd:cd02757 3 PSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTN 65
|
|
| |
