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Conserved domains on  [gi|15596976|ref|NP_250470|]
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assimilatory nitrate reductase [Pseudomonas aeruginosa PAO1]

Protein Classification

nitrate reductase( domain architecture ID 10119795)

nitrate reductase catalyzes the reduction of nitrate into nitrite using a mononuclear molybdenum cofactor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
5-709 0e+00

Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];


:

Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 978.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   5 SPLRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGKQLARArsDWE 84
Cdd:COG3383   2 NPMKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREV--SWD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  85 SALEHAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYE 164
Cdd:COG3383  80 EALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPPNSYD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 165 DLDCADCVLIAGSNMAFAHPVLFRRLEaaKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWI 244
Cdd:COG3383 160 DIEEADVILVIGSNPAEAHPVLARRIK--KAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 245 DRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATG 324
Cdd:COG3383 238 DEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATG 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 325 KIGRAGCGPFSLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGVEQLPTSPGLSAIELFDAVHDGRIKALWI 404
Cdd:COG3383 318 NIGRPGTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPPLPDKPGLTAVEMFDAIADGEIKALWI 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 405 ACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDW 484
Cdd:COG3383 398 IGENPAVSDPDANHVREALEKLEFLVVQDIFL-TETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDW 476
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 485 NIVCDFARRLEGHlrpakpglFAFADSRSLFDEYKLLTAgrdlDLSGLSYALLDRLGPQQWPFPTGAEQGTARLYADgRF 564
Cdd:COG3383 477 EIIAELARRLGYG--------FDYDSPEEVFDEIARLTP----DYSGISYERLEALGGVQWPCPSEDHPGTPRLFTG-RF 543
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 565 PTASGRAQLVAEPYRAAQEKRDARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLK 644
Cdd:COG3383 544 PTPDGKARFVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVS 623
                       650       660       670       680       690       700
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596976 645 SRRGALVLPVSADDSVRPGQAFLPMHWGDrflkgLGCNVLTLPAFDPLSKQPELKHAGVQVESVE 709
Cdd:COG3383 624 SRRGEVVLRARVTDRVRPGTVFMPFHWGE-----GAANALTNDALDPVSKQPEYKACAVRVEKVA 683
Bfd COG2906
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
854-900 5.59e-11

Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];


:

Pssm-ID: 442150 [Multi-domain]  Cd Length: 54  Bit Score: 58.29  E-value: 5.59e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15596976 854 CSCQNVSQQTVLGGIARGL-DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:COG2906   4 CLCNGVTDRQIRAAIAEGAtSLEELRAALGAGTQCGSCVPEARELLAE 51
nitri_red_nirB super family cl31455
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
783-900 1.53e-08

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


The actual alignment was detected with superfamily member TIGR02374:

Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 58.69  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   783 YDDPRRAIGKRVRLEDGRIVAVRLAGETLARDWLKELWLTGRADSELRRwLLAPLGAAPGRPSQGAGG----KTLCSCQN 858
Cdd:TIGR02374 339 IYDEQKGIYKKLVLSDDKLLGAVLFGDTSDYGRLLDMVLKQADISEDPA-IIKPQISGPEAGGPGVEAmpdsEQICSCNT 417
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15596976   859 VSQQTVLGGIARGL--DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:TIGR02374 418 VTKGAIIDAIHTGSctTVEELKACTKAGTSCGGCKPLVEQLLRA 461
 
Name Accession Description Interval E-value
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
5-709 0e+00

Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];


Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 978.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   5 SPLRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGKQLARArsDWE 84
Cdd:COG3383   2 NPMKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREV--SWD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  85 SALEHAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYE 164
Cdd:COG3383  80 EALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPPNSYD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 165 DLDCADCVLIAGSNMAFAHPVLFRRLEaaKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWI 244
Cdd:COG3383 160 DIEEADVILVIGSNPAEAHPVLARRIK--KAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 245 DRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATG 324
Cdd:COG3383 238 DEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATG 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 325 KIGRAGCGPFSLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGVEQLPTSPGLSAIELFDAVHDGRIKALWI 404
Cdd:COG3383 318 NIGRPGTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPPLPDKPGLTAVEMFDAIADGEIKALWI 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 405 ACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDW 484
Cdd:COG3383 398 IGENPAVSDPDANHVREALEKLEFLVVQDIFL-TETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDW 476
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 485 NIVCDFARRLEGHlrpakpglFAFADSRSLFDEYKLLTAgrdlDLSGLSYALLDRLGPQQWPFPTGAEQGTARLYADgRF 564
Cdd:COG3383 477 EIIAELARRLGYG--------FDYDSPEEVFDEIARLTP----DYSGISYERLEALGGVQWPCPSEDHPGTPRLFTG-RF 543
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 565 PTASGRAQLVAEPYRAAQEKRDARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLK 644
Cdd:COG3383 544 PTPDGKARFVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVS 623
                       650       660       670       680       690       700
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596976 645 SRRGALVLPVSADDSVRPGQAFLPMHWGDrflkgLGCNVLTLPAFDPLSKQPELKHAGVQVESVE 709
Cdd:COG3383 624 SRRGEVVLRARVTDRVRPGTVFMPFHWGE-----GAANALTNDALDPVSKQPEYKACAVRVEKVA 683
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
11-581 0e+00

Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239155 [Multi-domain]  Cd Length: 565  Bit Score: 903.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  11 ASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRlGKQLARARSDWESALEHA 90
Cdd:cd02754   1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLR-RNGGELVPVSWDEALDLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  91 AGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDCAD 170
Cdd:cd02754  80 AERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGADGPPGSYDDIEHAD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 171 CVLIAGSNMAFAHPVLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSFIA 250
Cdd:cd02754 160 CFFLIGSNMAECHPILFRRLLDRKKANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDRDFID 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 251 EHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAG 330
Cdd:cd02754 240 AHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPG 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 331 CGPFSLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGV--EQLPTSPGLSAIELFDAVHDGRIKALWIACTN 408
Cdd:cd02754 320 SGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVpeGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTN 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 409 PAQSLPDQRKIHEALARCPFVVVQEAFAGTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVC 488
Cdd:cd02754 400 PAVSLPNANRVREALERLEFVVVQDAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILA 479
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 489 DFARRLEghlrpaKPGLFAFADSRSLFDEYKLLTAGRDLDLSGLSYALLDRlGPQQWPFPTGAEQGTARLYADGRFPTAS 568
Cdd:cd02754 480 DVARRLG------FGELFPYTSPEEVFEEYRRLSRGRGADLSGLSYERLRD-GGVQWPCPDGPPEGTRRLFEDGRFPTPD 552
                       570
                ....*....|...
gi 15596976 569 GRAQLVAEPYRAA 581
Cdd:cd02754 553 GRARFVAVPYRPP 565
Fdh-alpha TIGR01591
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ...
12-705 0e+00

formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.


Pssm-ID: 130652 [Multi-domain]  Cd Length: 671  Bit Score: 584.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976    12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKG--ASLHLTGdlQARALYPQLRLGKQLARArsDWESALEH 89
Cdd:TIGR01591   1 TVCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGyfAWEFINS--KDRLTTPLIREGDKFREV--SWDEAISY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976    90 AAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDCA 169
Cdd:TIGR01591  77 IAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEIENA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   170 DCVLIAGSNMAFAHPVLFRRLEAAKaaRPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSFI 249
Cdd:TIGR01591 157 DLIVIIGYNPAESHPVVAQYLKNAK--RNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAFI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   250 AEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRA 329
Cdd:TIGR01591 235 EKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   330 GCGPFSLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGVEQLPTSPGLSAIELFDAVHDGRIKALWIACTNP 409
Cdd:TIGR01591 315 GGGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGVVKLPAEPGLRIPEMIDAAADGDVKALYIMGEDP 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   410 AQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVCD 489
Cdd:TIGR01591 395 LQSDPNTSKVRKALEKLELLVVQDIFM-TETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQE 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   490 FARRLeghlrpakpGL-FAFADSRSLFDEYKLLTAgrdlDLSGLSYALLDRLGPQQWPFPTGAEQGTARLYADgRFPTAS 568
Cdd:TIGR01591 474 LANAL---------GLdWNYNHPQEIMDEIRELTP----LFAGLTYERLDELGSLQWPCNDSDASPTSYLYKD-KFATPD 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   569 GRAQLVAEPYRAAQEKRDARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRG 648
Cdd:TIGR01591 540 GKAKFIPLEWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRG 619
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596976   649 ALVLPVSADDSVRPGQAFLPMHWGDRflkglGCNVLTLPAFDPLSKQPELKHAGVQV 705
Cdd:TIGR01591 620 EITLRAKVSDRVNKGAIYITMHFWDG-----AVNNLTTDDLDPISGTPEYKYTAVRI 671
PRK13532 PRK13532
nitrate reductase catalytic subunit NapA;
14-708 6.04e-129

nitrate reductase catalytic subunit NapA;


Pssm-ID: 237416 [Multi-domain]  Cd Length: 830  Bit Score: 408.13  E-value: 6.04e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   14 CCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLhltgdlqARALYPQLRLGKQLARARS------------ 81
Cdd:PRK13532  47 CRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNCIKGYFL-------SKIMYGKDRLTQPLLRMKDgkydkegeftpv 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   82 DWESALEHAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPC 161
Cdd:PRK13532 120 SWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGIDEPMG 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  162 SYEDLDCADCVLIAGSNMAFAHPVLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWE 241
Cdd:PRK13532 200 CYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRLSNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQN 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  242 DWIDRSFIAEHTE----------------------------------GFADLKELVRDYTPAAVADICGIDRADLQRCAE 287
Cdd:PRK13532 280 NAVNWDFVNKHTNfrkgatdigyglrpthplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAK 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  288 -WIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAMG-GRETGSLANLLPGHREAADPG 365
Cdd:PRK13532 360 lYADPNRKVVSFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGtAREVGTFSHRLPADMVVTNPK 439
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  366 HRAEVAHYWGVEQ--LPTSPGLSAIELFDAVHDGRIKALWIACTNPAQSLPDQRkiHEAL--ARCP--FVVVQEAFAGTe 439
Cdd:PRK13532 440 HREIAEKIWKLPEgtIPPKPGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNIN--EERLpgWRNPdnFIVVSDPYPTV- 516
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  440 TCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQD-WNIVcDFARRLE------GHLRPAKPG-------- 504
Cdd:PRK13532 517 SALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV-EFSKRFKteevwpEELLAKKPEyrgktlyd 595
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  505 -LFA---------------FADSRS----------LFDEYKLLTAGRDLDLS---------GLSYALLDrlGPQ-QWPFP 548
Cdd:PRK13532 596 vLFAngqvdkfplselaegYLNDEAkhfgfyvqkgLFEEYASFGRGHGHDLApfdtyhkvrGLRWPVVD--GKEtLWRYR 673
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  549 TG----AEQGTA-RLYADgrfptASGRAQLVAEPYRAAQEKRDARYPLTLNTGRLRDQWHgmsrTGTCAR----LFGHEE 619
Cdd:PRK13532 674 EGydpyVKAGEGfKFYGK-----PDGKAVIFALPYEPPAESPDEEYDLWLSTGRVLEHWH----TGSMTRrvpeLYRAFP 744
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  620 EALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRP--GQAFLPmhWgdrFLKGLGCNVLTLPAFDPLSKQPE 697
Cdd:PRK13532 745 EAVCFMHPEDAKARGLRRGDEVKVVSRRGEVKSRVETRGRNKPprGLVFVP--F---FDAAQLINKLTLDATDPLSKQTD 819
                        810
                 ....*....|.
gi 15596976  698 LKHAGVQVESV 708
Cdd:PRK13532 820 FKKCAVKIEKV 830
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
64-493 2.84e-78

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 258.48  E-value: 2.84e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976    64 RALYPQLRLGK-QLARArsDWESALEHAAGRFAETIREHGPDSVAF-YISGQLL-TEDYYAFNKLARALVGTN--NIDSN 138
Cdd:pfam00384   1 RLKYPMVRRGDgKFVRV--SWDEALDLIAKKLKRIIKKYGPDAIAInGGSGGLTdVESLYALKKLLNRLGSKNgnTEDHN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   139 SRLCMSSAVVgykrsLGADAPPC-----SYEDLDCADCVLIAGSNMAFAHPVLFRRLEAAkAARPEMRIVVIDPRRTDTc 213
Cdd:pfam00384  79 GDLCTAAAAA-----FGSDLRSNylfnsSIADIENADLILLIGTNPREEAPILNARIRKA-ALKGKAKVIVIGPRLDLT- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   214 eLADLHLALLPGTDVALFHGILHILLWEDWIDRSFiaehtegfadlkelvrdytpaavadicgidradlqrcaewigrSP 293
Cdd:pfam00384 152 -YADEHLGIKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------AP 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   294 RFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAmgGRETGSLAnllpghreaadpghraevahy 373
Cdd:pfam00384 188 KPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGA--ASPVGALD--------------------- 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   374 wgveqLPTSPGLSAIELFDAVHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAGTETCQYADLLLPAASW 453
Cdd:pfam00384 245 -----LGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAY 319
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 15596976   454 GEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVCDFARR 493
Cdd:pfam00384 320 TEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
Molybdop_Fe4S4 smart00926
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ...
7-56 8.61e-19

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: 80.76  E-value: 8.61e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 15596976      7 LRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLH 56
Cdd:smart00926   1 EKWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGL 50
Bfd COG2906
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
854-900 5.59e-11

Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];


Pssm-ID: 442150 [Multi-domain]  Cd Length: 54  Bit Score: 58.29  E-value: 5.59e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15596976 854 CSCQNVSQQTVLGGIARGL-DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:COG2906   4 CLCNGVTDRQIRAAIAEGAtSLEELRAALGAGTQCGSCVPEARELLAE 51
Fer2_BFD pfam04324
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ...
854-899 3.72e-09

BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilization functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).


Pssm-ID: 461261 [Multi-domain]  Cd Length: 50  Bit Score: 53.30  E-value: 3.72e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15596976   854 CSCQNVSQQTVLGGIARGL-DLDGLKREFGCGTGCGSCVPEIKRLLA 899
Cdd:pfam04324   3 CRCFGVTDGEIRDAIREGLtTVEEVKRRTKAGTGCGSCRPAIEEILA 49
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
783-900 1.53e-08

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 58.69  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   783 YDDPRRAIGKRVRLEDGRIVAVRLAGETLARDWLKELWLTGRADSELRRwLLAPLGAAPGRPSQGAGG----KTLCSCQN 858
Cdd:TIGR02374 339 IYDEQKGIYKKLVLSDDKLLGAVLFGDTSDYGRLLDMVLKQADISEDPA-IIKPQISGPEAGGPGVEAmpdsEQICSCNT 417
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15596976   859 VSQQTVLGGIARGL--DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:TIGR02374 418 VTKGAIIDAIHTGSctTVEELKACTKAGTSCGGCKPLVEQLLRA 461
NasA-like_Fer2_BFD-like cd19948
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of ...
850-899 7.31e-07

bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit NasA and similar proteins; The BFD-like [2Fe-2S]-binding domain described in this family is found at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit (NasA) such as Rhodobacter capsulatus E1F1 NasA. Nitrate reductase catalyzes the reduction of nitrate to nitrite, the first step of nitrate assimilation. R. capsulatus E1F1 nitrate reductase is composed of this NasA subunit and a small diaphorase subunit with FAD. Note that this [2Fe-2S]-binding domain is not always present; for example, it is absent from the characterized haloaechean Haloferax mediterranei NasA; both, however, have an [4Fe-4S] binding domain at their N-terminus. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381081 [Multi-domain]  Cd Length: 53  Bit Score: 46.75  E-value: 7.31e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15596976 850 GKTLCSCQNVSQQTVLGGIA-RGL-DLDGLKREFGCGTGCGSCVPEIKRLLA 899
Cdd:cd19948   1 GRTVCACFSVGENTIRRAIAdNGLtSVAQVGTCLKAGTNCGSCVPEIQKLLS 52
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
833-900 5.79e-05

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 47.04  E-value: 5.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596976  833 LLAPLGAAPGRPSQGAGG----KTLCSCQNVSQQTVLGGIARGL-DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:PRK14989 400 LILPAHAGSGKPSIGVDKlpdsAQICSCFDVTKGDLIAAINKGChTVAALKAETKAGTGCGGCIPLVTQVLNA 472
 
Name Accession Description Interval E-value
YjgC COG3383
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
5-709 0e+00

Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];


Pssm-ID: 442610 [Multi-domain]  Cd Length: 684  Bit Score: 978.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   5 SPLRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGKQLARArsDWE 84
Cdd:COG3383   2 NPMKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREV--SWD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  85 SALEHAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYE 164
Cdd:COG3383  80 EALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPPNSYD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 165 DLDCADCVLIAGSNMAFAHPVLFRRLEaaKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWI 244
Cdd:COG3383 160 DIEEADVILVIGSNPAEAHPVLARRIK--KAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 245 DRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATG 324
Cdd:COG3383 238 DEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATG 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 325 KIGRAGCGPFSLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGVEQLPTSPGLSAIELFDAVHDGRIKALWI 404
Cdd:COG3383 318 NIGRPGTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPPLPDKPGLTAVEMFDAIADGEIKALWI 397
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 405 ACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDW 484
Cdd:COG3383 398 IGENPAVSDPDANHVREALEKLEFLVVQDIFL-TETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDW 476
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 485 NIVCDFARRLEGHlrpakpglFAFADSRSLFDEYKLLTAgrdlDLSGLSYALLDRLGPQQWPFPTGAEQGTARLYADgRF 564
Cdd:COG3383 477 EIIAELARRLGYG--------FDYDSPEEVFDEIARLTP----DYSGISYERLEALGGVQWPCPSEDHPGTPRLFTG-RF 543
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 565 PTASGRAQLVAEPYRAAQEKRDARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLK 644
Cdd:COG3383 544 PTPDGKARFVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVS 623
                       650       660       670       680       690       700
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596976 645 SRRGALVLPVSADDSVRPGQAFLPMHWGDrflkgLGCNVLTLPAFDPLSKQPELKHAGVQVESVE 709
Cdd:COG3383 624 SRRGEVVLRARVTDRVRPGTVFMPFHWGE-----GAANALTNDALDPVSKQPEYKACAVRVEKVA 683
MopB_Nitrate-R-NapA-like cd02754
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
11-581 0e+00

Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239155 [Multi-domain]  Cd Length: 565  Bit Score: 903.90  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  11 ASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRlGKQLARARSDWESALEHA 90
Cdd:cd02754   1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLR-RNGGELVPVSWDEALDLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  91 AGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDCAD 170
Cdd:cd02754  80 AERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGADGPPGSYDDIEHAD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 171 CVLIAGSNMAFAHPVLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSFIA 250
Cdd:cd02754 160 CFFLIGSNMAECHPILFRRLLDRKKANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDRDFID 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 251 EHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAG 330
Cdd:cd02754 240 AHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPG 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 331 CGPFSLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGV--EQLPTSPGLSAIELFDAVHDGRIKALWIACTN 408
Cdd:cd02754 320 SGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVpeGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTN 399
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 409 PAQSLPDQRKIHEALARCPFVVVQEAFAGTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVC 488
Cdd:cd02754 400 PAVSLPNANRVREALERLEFVVVQDAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILA 479
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 489 DFARRLEghlrpaKPGLFAFADSRSLFDEYKLLTAGRDLDLSGLSYALLDRlGPQQWPFPTGAEQGTARLYADGRFPTAS 568
Cdd:cd02754 480 DVARRLG------FGELFPYTSPEEVFEEYRRLSRGRGADLSGLSYERLRD-GGVQWPCPDGPPEGTRRLFEDGRFPTPD 552
                       570
                ....*....|...
gi 15596976 569 GRAQLVAEPYRAA 581
Cdd:cd02754 553 GRARFVAVPYRPP 565
BisC COG0243
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
3-709 0e+00

Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];


Pssm-ID: 440013 [Multi-domain]  Cd Length: 674  Bit Score: 696.21  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   3 TDSPLRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGK----QLAR 78
Cdd:COG0243  17 EAAGTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGPrgsgKFER 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  79 ArsDWESALEHAAGRFAETIREHGPDSVAFYISG----QLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVVGYKRSL 154
Cdd:COG0243  97 I--SWDEALDLIAEKLKAIIDEYGPEAVAFYTSGgsagRLSNEAAYLAQRFARAL-GTNNLDDNSRLCHESAVAGLPRTF 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 155 GADAPPCSYEDLDCADCVLIAGSNMAFAHPVLFRRLEAAKAARPeMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGI 234
Cdd:COG0243 174 GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRG-AKIVVIDPRRTETAAIADEWLPIRPGTDAALLLAL 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 235 LHILLWEDWIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNS 314
Cdd:COG0243 253 AHVLIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVR 332
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 315 ALINLHLATGKIGRAGCGPFSLTGqpnamggretgslanllpghreaadpghraevahywgveqlptspglsaielfDAV 394
Cdd:COG0243 333 AIANLALLTGNIGKPGGGPFSLTG-----------------------------------------------------EAI 359
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 395 HDG---RIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSE-RRISHV 470
Cdd:COG0243 360 LDGkpyPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFL-TETARYADIVLPATTWLERDDIVTNSEdRRVHLS 438
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 471 RRAVPPPGEARQDWNIVCDFARRLeghlrPAKPGLFAFADSRSLFDEYklLTAGRDldlSGLSYALLDRLGPQQWPFPTG 550
Cdd:COG0243 439 RPAVEPPGEARSDWEIFAELAKRL-----GFEEAFPWGRTEEDYLREL--LEATRG---RGITFEELREKGPVQLPVPPE 508
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 551 aeqgtARLYADGRFPTASGRAQL------------VAEPYRAAqEKRDARYPLTLNTGRLRDQWHGMSRtgTCARLFGHE 618
Cdd:COG0243 509 -----PAFRNDGPFPTPSGKAEFysetlalpplprYAPPYEGA-EPLDAEYPLRLITGRSRDQWHSTTY--NNPRLREIG 580
                       650       660       670       680       690       700       710       720
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 619 EEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPMHWGDRFL--KGLGCNVLTLPAFDPLSKQP 696
Cdd:COG0243 581 PRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWYEPAddKGGNVNVLTPDATDPLSGTP 660
                       730
                ....*....|...
gi 15596976 697 ELKHAGVQVESVE 709
Cdd:COG0243 661 AFKSVPVRVEKAA 673
Fdh-alpha TIGR01591
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ...
12-705 0e+00

formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.


Pssm-ID: 130652 [Multi-domain]  Cd Length: 671  Bit Score: 584.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976    12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKG--ASLHLTGdlQARALYPQLRLGKQLARArsDWESALEH 89
Cdd:TIGR01591   1 TVCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGyfAWEFINS--KDRLTTPLIREGDKFREV--SWDEAISY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976    90 AAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDCA 169
Cdd:TIGR01591  77 IAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEIENA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   170 DCVLIAGSNMAFAHPVLFRRLEAAKaaRPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSFI 249
Cdd:TIGR01591 157 DLIVIIGYNPAESHPVVAQYLKNAK--RNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAFI 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   250 AEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRA 329
Cdd:TIGR01591 235 EKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKP 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   330 GCGPFSLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGVEQLPTSPGLSAIELFDAVHDGRIKALWIACTNP 409
Cdd:TIGR01591 315 GGGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGVVKLPAEPGLRIPEMIDAAADGDVKALYIMGEDP 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   410 AQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVCD 489
Cdd:TIGR01591 395 LQSDPNTSKVRKALEKLELLVVQDIFM-TETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQE 473
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   490 FARRLeghlrpakpGL-FAFADSRSLFDEYKLLTAgrdlDLSGLSYALLDRLGPQQWPFPTGAEQGTARLYADgRFPTAS 568
Cdd:TIGR01591 474 LANAL---------GLdWNYNHPQEIMDEIRELTP----LFAGLTYERLDELGSLQWPCNDSDASPTSYLYKD-KFATPD 539
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   569 GRAQLVAEPYRAAQEKRDARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRG 648
Cdd:TIGR01591 540 GKAKFIPLEWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRG 619
                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15596976   649 ALVLPVSADDSVRPGQAFLPMHWGDRflkglGCNVLTLPAFDPLSKQPELKHAGVQV 705
Cdd:TIGR01591 620 EITLRAKVSDRVNKGAIYITMHFWDG-----AVNNLTTDDLDPISGTPEYKYTAVRI 671
MopB_Formate-Dh-H cd02753
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
12-580 9.70e-170

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: 503.28  E-value: 9.70e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLH---LTGDlqaRALYPQLRLGKQLARArsDWESALE 88
Cdd:cd02753   2 TVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFdfvNSKD---RLTKPLIRKNGKFVEA--SWDEALS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  89 HAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDC 168
Cdd:cd02753  77 LVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAMTNSIADIEE 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 169 ADCVLIAGSNMAFAHPVLFRRLEaaKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSF 248
Cdd:cd02753 157 ADVILVIGSNTTEAHPVIARRIK--RAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEF 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 249 IAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGR 328
Cdd:cd02753 235 IEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGR 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 329 AGCGPFSLTGQPNAMGGRETGSLANLLPGHreaadpghraevahywgveqlptspglsaielfdavhdgrIKALWIACTN 408
Cdd:cd02753 315 PGTGVNPLRGQNNVQGACDMGALPNVLPGY----------------------------------------VKALYIMGEN 354
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 409 PAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVC 488
Cdd:cd02753 355 PALSDPNTNHVRKALESLEFLVVQDIFL-TETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQ 433
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 489 DFARRLeGHlrpakPGlfAFADSRSLFDEYKLLTAgrdlDLSGLSYALLDRLGPQQWPFPTGAEQGTARLYADgRFPTAS 568
Cdd:cd02753 434 ELANRL-GY-----PG--FYSHPEEIFDEIARLTP----QYAGISYERLERPGGLQWPCPDEDHPGTPILHTE-RFATPD 500
                       570
                ....*....|..
gi 15596976 569 GRAQLVAEPYRA 580
Cdd:cd02753 501 GKARFMPVEYRP 512
PRK13532 PRK13532
nitrate reductase catalytic subunit NapA;
14-708 6.04e-129

nitrate reductase catalytic subunit NapA;


Pssm-ID: 237416 [Multi-domain]  Cd Length: 830  Bit Score: 408.13  E-value: 6.04e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   14 CCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLhltgdlqARALYPQLRLGKQLARARS------------ 81
Cdd:PRK13532  47 CRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNCIKGYFL-------SKIMYGKDRLTQPLLRMKDgkydkegeftpv 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   82 DWESALEHAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPC 161
Cdd:PRK13532 120 SWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGIDEPMG 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  162 SYEDLDCADCVLIAGSNMAFAHPVLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWE 241
Cdd:PRK13532 200 CYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRLSNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQN 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  242 DWIDRSFIAEHTE----------------------------------GFADLKELVRDYTPAAVADICGIDRADLQRCAE 287
Cdd:PRK13532 280 NAVNWDFVNKHTNfrkgatdigyglrpthplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAK 359
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  288 -WIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAMG-GRETGSLANLLPGHREAADPG 365
Cdd:PRK13532 360 lYADPNRKVVSFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGtAREVGTFSHRLPADMVVTNPK 439
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  366 HRAEVAHYWGVEQ--LPTSPGLSAIELFDAVHDGRIKALWIACTNPAQSLPDQRkiHEAL--ARCP--FVVVQEAFAGTe 439
Cdd:PRK13532 440 HREIAEKIWKLPEgtIPPKPGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNIN--EERLpgWRNPdnFIVVSDPYPTV- 516
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  440 TCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQD-WNIVcDFARRLE------GHLRPAKPG-------- 504
Cdd:PRK13532 517 SALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV-EFSKRFKteevwpEELLAKKPEyrgktlyd 595
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  505 -LFA---------------FADSRS----------LFDEYKLLTAGRDLDLS---------GLSYALLDrlGPQ-QWPFP 548
Cdd:PRK13532 596 vLFAngqvdkfplselaegYLNDEAkhfgfyvqkgLFEEYASFGRGHGHDLApfdtyhkvrGLRWPVVD--GKEtLWRYR 673
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  549 TG----AEQGTA-RLYADgrfptASGRAQLVAEPYRAAQEKRDARYPLTLNTGRLRDQWHgmsrTGTCAR----LFGHEE 619
Cdd:PRK13532 674 EGydpyVKAGEGfKFYGK-----PDGKAVIFALPYEPPAESPDEEYDLWLSTGRVLEHWH----TGSMTRrvpeLYRAFP 744
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  620 EALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRP--GQAFLPmhWgdrFLKGLGCNVLTLPAFDPLSKQPE 697
Cdd:PRK13532 745 EAVCFMHPEDAKARGLRRGDEVKVVSRRGEVKSRVETRGRNKPprGLVFVP--F---FDAAQLINKLTLDATDPLSKQTD 819
                        810
                 ....*....|.
gi 15596976  698 LKHAGVQVESV 708
Cdd:PRK13532 820 FKKCAVKIEKV 830
Molybdopterin-Binding cd00368
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ...
12-494 1.25e-120

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: 370.89  E-value: 1.25e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGKQLARARSDWESALEHAA 91
Cdd:cd00368   2 SVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGKFVPISWDEALDEIA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  92 GRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVVGYKRsLGADAPPCSYEDLDCADC 171
Cdd:cd00368  82 EKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRAL-GSNNVDSHARLCHASAVAALKA-FGGGAPTNTLADIENADL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 172 VLIAGSNMAFAHPVLFRRLeaAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGilhillwedwidrsfiae 251
Cdd:cd00368 160 ILLWGSNPAETHPVLAARL--RRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA------------------ 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 252 htegfadlkelvrdytpAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGC 331
Cdd:cd00368 220 -----------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGG 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 332 GPFSltgqpnamggretgslanllpghreaadpghraevahywgveqlptspglsaielfdavhdgrikalwiaCTNPAQ 411
Cdd:cd00368 283 GLGP----------------------------------------------------------------------GGNPLV 292
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 412 SLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVCDFA 491
Cdd:cd00368 293 SAPDANRVRAALKKLDFVVVIDIFM-TETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELA 371

                ...
gi 15596976 492 RRL 494
Cdd:cd00368 372 KRL 374
Molybdopterin pfam00384
Molybdopterin oxidoreductase;
64-493 2.84e-78

Molybdopterin oxidoreductase;


Pssm-ID: 395308 [Multi-domain]  Cd Length: 359  Bit Score: 258.48  E-value: 2.84e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976    64 RALYPQLRLGK-QLARArsDWESALEHAAGRFAETIREHGPDSVAF-YISGQLL-TEDYYAFNKLARALVGTN--NIDSN 138
Cdd:pfam00384   1 RLKYPMVRRGDgKFVRV--SWDEALDLIAKKLKRIIKKYGPDAIAInGGSGGLTdVESLYALKKLLNRLGSKNgnTEDHN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   139 SRLCMSSAVVgykrsLGADAPPC-----SYEDLDCADCVLIAGSNMAFAHPVLFRRLEAAkAARPEMRIVVIDPRRTDTc 213
Cdd:pfam00384  79 GDLCTAAAAA-----FGSDLRSNylfnsSIADIENADLILLIGTNPREEAPILNARIRKA-ALKGKAKVIVIGPRLDLT- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   214 eLADLHLALLPGTDVALFHGILHILLWEDWIDRSFiaehtegfadlkelvrdytpaavadicgidradlqrcaewigrSP 293
Cdd:pfam00384 152 -YADEHLGIKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------AP 187
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   294 RFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAmgGRETGSLAnllpghreaadpghraevahy 373
Cdd:pfam00384 188 KPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGA--ASPVGALD--------------------- 244
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   374 wgveqLPTSPGLSAIELFDAVHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAGTETCQYADLLLPAASW 453
Cdd:pfam00384 245 -----LGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAY 319
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 15596976   454 GEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVCDFARR 493
Cdd:pfam00384 320 TEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
MopB_Formate-Dh-Na-like cd02752
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ...
12-494 2.09e-77

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: 265.03  E-value: 2.09e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASL--HLTGDLqaRALYPQLRLGKQLARARSDWESALEH 89
Cdd:cd02752   2 TICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALrdFVHSPK--RLKYPMYRAPGSGKWEEISWDEALDE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  90 AAGRFAEtIRE-------------HGPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVVGYKRSLGA 156
Cdd:cd02752  80 IARKMKD-IRDasfveknaagvvvNRPDSIAFLGSAKLSNEECYLIRKFARAL-GTNNLDHQARIUHSPTVAGLANTFGR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 157 DAPPCSYEDLDCADCVLIAGSNMAFAHPVLFRRLEAAKAARpEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILH 236
Cdd:cd02752 158 GAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKN-GAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMIN 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 237 illwedWIDRsfiaehtegfadlkelvrdYTPAAVADICGIDRADLQRCAEWI---GRSPRFLS-LWCMGLNQSSAGSAK 312
Cdd:cd02752 237 ------YIIR-------------------YTPEEVEDICGVPKEDFLKVAEMFaatGRPDKPGTiLYAMGWTQHTVGSQN 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 313 NSALINLHLATGKIGRAGCGPFSLTGQPNAMGGRETGSLANLLPGHReaadPGHraevahywgveqlptspglsaielfd 392
Cdd:cd02752 292 IRAMCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPGYL----GGQ-------------------------- 341
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 393 avhdgrikalwiactNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYAD-------------LLLPAASWGEKEGS 459
Cdd:cd02752 342 ---------------NPNSSFPNANKVRRALDKLDWLVVIDPFP-TETAAFWKnpgmdpksiqtevFLLPAACQYEKEGS 405
                       490       500       510
                ....*....|....*....|....*....|....*
gi 15596976 460 VTNSERRISHVRRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02752 406 ITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRL 440
MopB_3 cd02766
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ...
21-576 2.65e-74

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: 252.55  E-value: 2.65e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  21 CGVLIEHDGERILGVQGDPRHPANFGRLCSKGAslHLTGDLQA--RALYPQLRLGKQLAR-ARSDWESALEHAAGRFAET 97
Cdd:cd02766  12 CSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGA--RYVERVYSpdRLLTPLKRVGRKGGQwERISWDEALDTIAAKLKEI 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  98 IREHGPDSVAfYISGQ----LLTEDYYA--FNKL-ARALVGTnnidsnsrLCMSSAVVGYK----RSLGADAppcsyEDL 166
Cdd:cd02766  90 KAEYGPESIL-PYSYAgtmgLLQRAARGrfFHALgASELRGT--------ICSGAGIEAQKydfgASLGNDP-----EDM 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 167 DCADCVLIAGSNMAFAHPVLFRRLEAAKAArpEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDR 246
Cdd:cd02766 156 VNADLIVIWGINPAATNIHLMRIIQEARKR--GAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDR 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 247 SFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKI 326
Cdd:cd02766 234 DFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNI 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 327 GRAGCGPFSLTGQPNamggretgslanllpghreaadpghraevahywgveqlptspglsaielfdavhdgrIKALWIAC 406
Cdd:cd02766 314 GVPGGGAFYSNSGPP---------------------------------------------------------VKALWVYN 336
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 407 TNPAQSLPDQRKIHEALAR-CPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTnSE--RRISHVRRAVPPPGEARQD 483
Cdd:cd02766 337 SNPVAQAPDSNKVRKGLAReDLFVVVHDQFM-TDTARYADIVLPATTFLEHEDVYA-SYwhYYLQYNEPAIPPPGEARSN 414
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 484 WNIVCDFARRL--EGHLrpakpglfaFADSRSLFdeykLLTAGRDLDLSGLSYALLDRLGPQQWPFPtgaeqgtARLYAD 561
Cdd:cd02766 415 TEIFRELAKRLgfGEPP---------FEESDEEW----LDQALDGTGLPLEGIDLERLLGPRKAGFP-------LVAWED 474
                       570
                ....*....|....*
gi 15596976 562 GRFPTASGRAQLVAE 576
Cdd:cd02766 475 RGFPTPSGKFEFYSE 489
MopB_ydeP cd02767
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
37-573 2.28e-70

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: 243.75  E-value: 2.28e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  37 GDPRHPANFGRLCSKGA-----------------SLHLTGDLQARALYPQLRLGK----QLARARSD------WESALEH 89
Cdd:cd02767  10 GDPGQKLHGFEFCENGAkalawettpkrvtpeffALHSVSELRTWSDYELEHLGRltypMRYDAGSDhyrpisWDEAFAE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  90 AAGRFaetiREHGPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDCA 169
Cdd:cd02767  90 IAARL----RALDPDRAAFYTSGRASNEAAYLYQLFARAY-GTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHT 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 170 DCVLIAGSNMAFAHPVLFRRLEAAKAArpEMRIVVIDPRR-----------------TDTCELADLHLALLPGTDVALFH 232
Cdd:cd02767 165 DLIFFIGQNPGTNHPRMLHYLREAKKR--GGKIIVINPLRepglerfanpqnpesmlTGGTKIADEYFQVRIGGDIALLN 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 233 GIL-HILLWED----WIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSS 307
Cdd:cd02767 243 GMAkHLIERDDepgnVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVWGMGITQHA 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 308 AGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAMGGRETGSlanllpghREAADPGHRAEVAHYWGVEqLPTSPGLSA 387
Cdd:cd02767 323 HGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGI--------TEKPFPEFLDALEEVFGFT-PPRDPGLDT 393
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 388 IELFDAVHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQE-------AFAGTETcqyadLLLPAASWGEK---- 456
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVAtklnrshLVHGEEA-----LILPCLGRTEIdmqa 468
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 457 ---------------EGSV----TNSERRISHV----RRAVPPPGEARQDWNIVCDFARRleghLRPAKPGLF--AFADs 511
Cdd:cd02767 469 ggaqavtvedsmsmtHTSRgrlkPASRVLLSEEaivaGIAGARLGEAKPEWEILVEDYDR----IRDEIAAVIyeGFAD- 543
                       570       580       590       600       610       620
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596976 512 rslFDEYKLLTAGRDLdlsglsyalldrlgpqqwpfPTGAeqgtarlyADGRFPTASGRAQL 573
Cdd:cd02767 544 ---FNQRGDQPGGFHL--------------------PNGA--------RERKFNTPSGKAQF 574
MopB_1 cd02762
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
13-540 2.33e-66

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: 231.90  E-value: 2.33e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  13 TCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLhltGDLQ---ARALYPQLRLGKQLARArsDWESALEH 89
Cdd:cd02762   3 ACILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAAL---GDYQndpDRLRTPMRRRGGSFEEI--DWDEAFDE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  90 AAGRFAETIREHGPDSVAFYISG-QLLTEDYYAFNKLARALVGTNNIDSNSRLCMS----SAVVGYKRSLGADAPpcsye 164
Cdd:cd02762  78 IAERLRAIRARHGGDAVGVYGGNpQAHTHAGGAYSPALLKALGTSNYFSAATADQKpghfWSGLMFGHPGLHPVP----- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 165 DLDCADCVLIAGSNMAFAH------PVLFRRLEAAKAarPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHIL 238
Cdd:cd02762 153 DIDRTDYLLILGANPLQSNgslrtaPDRVLRLKAAKD--RGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 239 LWEDWIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAkNSALIN 318
Cdd:cd02762 231 LAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTL-CSWLVK 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 319 -LHLATGKIGRAGcgpfsltgqpnamGGRETGSLANLLPghreAADPGHRAEVAHYWGVEQLPTSPGL---SAI-ELFDA 393
Cdd:cd02762 310 lLNLLTGNLDRPG-------------GAMFTTPALDLVG----QTSGRTIGRGEWRSRVSGLPEIAGElpvNVLaEEILT 372
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 394 VHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEaFAGTETCQYADLLLPAASWGEK-EGSVTNSE--RRISHV 470
Cdd:cd02762 373 DGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVD-VYMTETTRHADYILPPASQLEKpHATFFNLEfpRNAFRY 451
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596976 471 RRA-VPPPGEARQDWNIVCDFARRLEGHLRPAKPGLFAFADsrSLFDeyKLLTAGRDLDLSGLSYALLDRL 540
Cdd:cd02762 452 RRPlFPPPPGTLPEWEILARLVEALDAVLRAGFYGERAGGT--LLLA--ALLERPSGVDLGPLTPRLWQRL 518
MopB_Acetylene-hydratase cd02759
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ...
13-507 1.32e-64

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: 225.26  E-value: 1.32e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  13 TCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGKQLARA--RSDWESALEHA 90
Cdd:cd02759   3 TCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKweRISWDEALDEI 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  91 AGRFAETIREHGPDSVAFYI---SGQLL--TEDYYAFNKLARALVGTNNIDS--NSRLCMSSAVVGYkrslgadapPCSY 163
Cdd:cd02759  83 AEKLAEIKAEYGPESIATAVgtgRGTMWqdSLFWIRFVRLFGSPNLFLSGEScyWPRDMAHALTTGF---------GLGY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 164 E--DLDCADCVLIAGSNMAFAHPVLFrrLEAAKAARPE-MRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLW 240
Cdd:cd02759 154 DepDWENPECIVLWGKNPLNSNLDLQ--GHWLVAAMKRgAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIIN 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 241 EDWIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRS-PRFLSlWCMGLNQSSAGSAKNSALINL 319
Cdd:cd02759 232 EGLYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAkPACIQ-WGLAIDQQKNGTQTSRAIAIL 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 320 HLATGKIGRAGcgpfsltgqpnamggretGSLanLLPghreaadpghraevahYwgveqlptspglsaielfdavhdgRI 399
Cdd:cd02759 311 RAITGNLDVPG------------------GNL--LIP----------------Y------------------------PV 330
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 400 KALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRIsHVR---RAVPP 476
Cdd:cd02759 331 KMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFM-TPTAMLADIVLPVAMSLERPGLRGGFEAEN-FVQlrqKAVEP 408
                       490       500       510       520
                ....*....|....*....|....*....|....*....|..
gi 15596976 477 PGEARQDWNIVCDFARRL-----------EGHLRPAKPGLFA 507
Cdd:cd02759 409 YGEAKSDYEIVLELGKRLgpeeaeyykyeKGLLRPDGQPGFN 450
arsenite_ox_L TIGR02693
arsenite oxidase, large subunit; This model represents the large subunit of an arsenite ...
23-671 2.25e-59

arsenite oxidase, large subunit; This model represents the large subunit of an arsenite oxidase complex. The small subunit is a Rieske protein. Homologs to both large and small subunits that score in the gray zone between the set trusted and noise bit score cutoffs for the respective models are found in Aeropyrum pernix K1 and in Sulfolobus tokodaii str. 7. This enzyme acts in energy metabolim by arsenite oxidation, rather than detoxification by reduction of arsenate to arsenite prior to export. [Energy metabolism, Electron transport]


Pssm-ID: 274261 [Multi-domain]  Cd Length: 806  Bit Score: 217.87  E-value: 2.25e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976    23 VLIEHDGERI-LGVQGDPRHPANFGRLCSKGASLHLT-----GDLQARALYPQLRLGKQLARarSDWESALEHAAGRFAE 96
Cdd:TIGR02693  68 VVKQRDGRDVnVVIKPDKECVVNSGLGSVRGGRMAETsfsedRNTQDRLTYPLVWRGDQMQP--TSWDDALDLVARLTKK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976    97 TIREHGPDSVAFYI-----SGQLLtEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGyKRSLGADAPPCSYEDLDCADC 171
Cdd:TIGR02693 146 IVDEKGEDDIIVSAfdhggAGGGF-ENTWGTGKLYFEAMKVKNIRIHNRPAYNSEVHG-TREMGVGELNNCYEDAELADT 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   172 VLIAGSNMAFAHPVLF----------RRLEAAKAARPEM-----RIVVIDPRRTDTCELAD-------LHLALLPGTDVA 229
Cdd:TIGR02693 224 IVAVGTNAYETQTNYFlnhwlpnlrgETLGKKKQLFPGEphepgRIIIVDPRRTVSVNAAEqtaadrvLHLAINSGTDLA 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   230 LFHGILHILLWEDWIDRSFIAE--HTEGFADLKELVRdYTPAAVADICGIDRADLQRCAEWI------GRSPRFLSLWCM 301
Cdd:TIGR02693 304 LFNALFTYVADKGWVDRDFIDKsgHLSSFEDAVKGCR-MSIAEAARITGVSAAQIIKAAEWIgkpkagGKRRRTMFGYEK 382
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   302 GLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQ-------PNAMGGRETGSLANLLPGHReaadpghrAEVAHYW 374
Cdd:TIGR02693 383 GIIWGNDNYRTNGALVNLALATGNIGRPGTGCVRLGGHqegyvrpPDAHVGGPAAYVDQLLIGGK--------GGVHHIW 454
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   375 GVEQLPTSPGLSAI-ELFDAVHDGRIKALWIACTNPAQSLPDqrKIHEALARCP-FVVVQEAFAgTETCQYADLLLPAAS 452
Cdd:TIGR02693 455 GCDHYKTTLNAQEFrRVYKKRTDMVKDAMSAAPYGDREEMVN--AIVDAINQGGlFAVNVDIYP-TKIGEAAHLILPAAT 531
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   453 WGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVCDFARRLEGHLRP-AKPGLF-------------AFADSrslFDEY 518
Cdd:TIGR02693 532 SGEMNLTSMNGERRMRLTEKFMDPPGQAMPDCLIAARLANTMERVYTAeGKVEYAkqfkgfdwkteedAFMDG---YNKN 608
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   519 KLLTAGRDLDLSG-----LSYALLDRLGPQ--QWP---FPTGAEQGTARLYADGRFPTASGRAQLVAEPYRAAQ----EK 584
Cdd:TIGR02693 609 RDNTVEDEAAHGGenykfVTYELLSAMGTNgfQEPatrFTDGKIEGTQRLYTDGVFSTDDGKARFMDAPWRGLPapgkQQ 688
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   585 RDARYPLTLNTGRLRDQWHGmsrtgtcARLFGHEEE-------ALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSAD 657
Cdd:TIGR02693 689 QKDKHKFWINNGRANVVWQS-------AYHDQENDFvmdrfplPYIEMNPEDAAELGLKEGDLVEVYNDAGATQAMAYPT 761
                         730
                  ....*....|....*
gi 15596976   658 DSVRPGQAFLPM-HW 671
Cdd:TIGR02693 762 PTAKPGETFMLFgFP 776
MopB_CT_Nitrate-R-NapA-like cd02791
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ...
587-708 8.32e-56

Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs


Pssm-ID: 239192 [Multi-domain]  Cd Length: 122  Bit Score: 188.17  E-value: 8.32e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 587 ARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAF 666
Cdd:cd02791   1 AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVF 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15596976 667 LPMHWGDRFLKGLGCNVLTLPAFDPLSKQPELKHAGVQVESV 708
Cdd:cd02791  81 VPMHWGDQFGRSGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
MopB_Thiosulfate-R-like cd02755
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ...
10-494 2.47e-50

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: 184.42  E-value: 2.47e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  10 TASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTgdlqaraLYPQLRLGKQLARA---------R 80
Cdd:cd02755   1 VPSICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQL-------LYDPDRLKKPLIRVgergegkfrE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  81 SDWESALEHAAGRFAETIREHGPDSVAFYISGQLLtEDYyaFNKLARALvGTNNIDSNSRLCMSSAVVGYK---RSLGAD 157
Cdd:cd02755  74 ASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCY-SPF--FKHFAAAF-GSPNIFSHESTCLASKNLAWKlviDSFGGE 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 158 APPcsyeDLDCADCVLIAGSNMAFA-HPVLFRRLEAAKAARpeMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILH 236
Cdd:cd02755 150 VNP----DFENARYIILFGRNLAEAiIVVDARRLMKALENG--AKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIH 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 237 ILLWEDWIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCA-EWIGRSPR--FLSLWCMGLNQSSAGSAKN 313
Cdd:cd02755 224 VLISENLYDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIArEFAAAAPHavVDPGWRGTFYSNSFQTRRA 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 314 SALINlhLATGKIGRAGCGPFSLTGQPnamggretgslanllpghreaadpghraevahywgveqlptspglsaielfda 393
Cdd:cd02755 304 IAIIN--ALLGNIDKRGGLYYAGSAKP----------------------------------------------------- 328
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 394 vhdGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEaFAGTETCQYADLLLPAASWGEKE--GSVTNSERRISHVR 471
Cdd:cd02755 329 ---YPIKALFIYRTNPFHSMPDRARLIKALKNLDLVVAID-ILPSDTALYADVILPEATYLERDepFSDKGGPAPAVATR 404
                       490       500
                ....*....|....*....|....
gi 15596976 472 -RAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02755 405 qRAIEPLYDTRPGWDILKELARRL 428
MopB_CT_Fdh-Nap-like cd00508
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ...
587-706 1.39e-48

This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 238282 [Multi-domain]  Cd Length: 120  Bit Score: 167.68  E-value: 1.39e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 587 ARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAF 666
Cdd:cd00508   1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVF 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15596976 667 LPMHWGDRFlKGLGCNVLTLPAFDPLSKQPELKHAGVQVE 706
Cdd:cd00508  81 MPFHWGGEV-SGGAANALTNDALDPVSGQPEFKACAVRIE 119
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 ...
12-502 5.56e-42

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: 160.63  E-value: 5.56e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKG--ASLHLTGDlqARALYPQLRLGKQLARArsDWESALEH 89
Cdd:cd02771   2 SICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGrfGYGYVNSR--DRLTQPLIRRGGTLVPV--SWNEALDV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  90 AAGRFAEtirehGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVvgykRSLGADAPpcSYEDLDCA 169
Cdd:cd02771  78 AAARLKE-----AKDKVGGIGSPRASNESNYALQKLVGAVLGTNNVDHRARRLIAEIL----RNGPIYIP--SLRDIESA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 170 DCVLIAGSNMAFAHPVLFRRLEaaKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFH----GILHILLWEDWID 245
Cdd:cd02771 147 DAVLVLGEDLTQTAPRIALALR--QAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNalatRLDDIAAESIRAS 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 246 RSFIAEHTEGFADLkelvrdyTPAAVADICGIDRADL-QRCAEWIGRSPRFLSLWcmGLNQSSAGSAKnsALINLHLATG 324
Cdd:cd02771 225 PGGQARLGAALARA-------VDASAAGVSGLAPKEKaARIAARLTGAKKPLIVS--GTLSGSLELIK--AAANLAKALK 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 325 KIGRAGcgpfsltgqpNAMGGRETGSLANLLPGHREaadpghraevahywgveqlPTSPGLSAIELFDAVHDGRIKALWI 404
Cdd:cd02771 294 RRGENA----------GLTLAVEEGNSPGLLLLGGH-------------------VTEPGLDLDGALAALEDGSADALIV 344
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 405 ACTNPAQSLPDqRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVP-PPGEARQD 483
Cdd:cd02771 345 LGNDLYRSAPE-RRVEAALDAAEFVVVLDHFL-TETAERADVVLPAASFAEKSGTFVNYEGRAQRFFKAYDdPAGDARSD 422
                       490
                ....*....|....*....
gi 15596976 484 WNIVCDFARRLEGHLRPAK 502
Cdd:cd02771 423 WRWLHALAAKLGGKLVPSD 441
MopB_DMSOR-like cd02751
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
9-494 7.11e-42

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: 162.78  E-value: 7.11e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   9 TTASTCCYCGVgcgvlIEHDGeRILGVQGDPRHPAnfgRLCSKGASLHLTGDLQARALYPQLRLGK-------QLARARS 81
Cdd:cd02751   1 PTACHWGPFKA-----HVKDG-VIVRVEPDDTDQP---RPCPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsRELRGEG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  82 D-----WESALEHAAGRFAETIREHGPDSVaFYISGqllTEDYYAFNKLARALVG---------TNNIDSNSrlcMSSAV 147
Cdd:cd02751  72 EfvrisWDEALDLVASELKRIREKYGNEAI-FGGSY---GWASAGRLHHAQSLLHrflnliggyLGSYGTYS---TGAAQ 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 148 VGYKRSLGADAPPC---SYED-LDCADCVLIAGSNMA--------FAHPVLFRRLEAAKAARpeMRIVVIDPRRTDTCE- 214
Cdd:cd02751 145 VILPHVVGSDEVYEqgtSWDDiAEHSDLVVLFGANPLktrqggggGPDHGSYYYLKQAKDAG--VRFICIDPRYTDTAAv 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 215 LADLHLALLPGTDVALFHGILHILLWEDWIDRSFIAEHTEGFADLKelvrDY----------TPAAVADICGIDRADLQR 284
Cdd:cd02751 223 LAAEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFK----DYllgesdgvpkTPEWAAEITGVPAETIRA 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 285 CAEWIGRSPRFLSL-WcmGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAMGGRETGSLANLLPGHREAAD 363
Cdd:cd02751 299 LAREIASKRTMIAQgW--GLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGAGGPGLPQGKNPVK 376
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 364 pghraevahywgvEQLPTSPGLSAIE----LFDA----VHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAF 435
Cdd:cd02751 377 -------------DSIPVARIADALLnpgkEFTAngklKTYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIF 443
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596976 436 AgTETCQYADLLLPAASWGEKE---GSVTNSERRISHVRRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02751 444 W-TASARYADIVLPATTSLERNdigLTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRL 504
MopB_Nitrate-R-NarG-like cd02750
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ...
47-494 4.19e-40

Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239151 [Multi-domain]  Cd Length: 461  Bit Score: 154.78  E-value: 4.19e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  47 RLCSKGASLH--LTGDLqaRALYPQLRLGKQLAR--ARSDWESALEHAAGRFAETIREHGPDSVAFYI----SGQLLTED 118
Cdd:cd02750  49 RGCQRGASFSwyLYSPD--RVKYPLKRVGARGEGkwKRISWDEALELIADAIIDTIKKYGPDRVIGFSpipaMSMVSYAA 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 119 YYAFNKLARAlVGTNNIDSNSRLCMSSAVVGYKRSlgaDAPPCSyeDLDCADCVLIAGSNMAF-----AHPVLFRRLEAA 193
Cdd:cd02750 127 GSRFASLIGG-VSLSFYDWYGDLPPGSPQTWGEQT---DVPESA--DWYNADYIIMWGSNVPVtrtpdAHFLTEARYNGA 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 194 KaarpemrIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSFIAEHTegfaDLKELVrdYTPAAVAD 273
Cdd:cd02750 201 K-------VVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYT----DLPFLV--YTPAWQEA 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 274 ICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQP-NAMGGRetgslA 352
Cdd:cd02750 268 ITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVGQPrVLFVWR-----G 342
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 353 NLLPGHREAAdpghraevahywgveqlptspglsaiELFDAVHDGrikalwiactnpaqslpdqrkihealaRCPFVVVQ 432
Cdd:cd02750 343 NLFGSSGKGH--------------------------EYFEDAPEG---------------------------KLDLIVDL 369
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596976 433 EaFAGTETCQYADLLLPAASWGEK-EGSVTNSERRISHVRRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02750 370 D-FRMDSTALYSDIVLPAATWYEKhDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKV 431
MopB_Arsenite-Ox cd02756
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ...
13-571 1.09e-35

Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239157 [Multi-domain]  Cd Length: 676  Bit Score: 144.93  E-value: 1.09e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  13 TCCYCGVGCG-------------------------------------------VLIEHDGERILGVQ-GDPRHPANFGRL 48
Cdd:cd02756  16 TCHFCIVGCGyhvyvwpvgeeggpspgqnaigydlvdqvpplnlqwypktmhyVVVTQDGREVYIVIvPDKECPVNSGNY 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  49 CSKGASLHLT------GDLQARALYPQLRLGKQLARarSDWESALEHAAGRFAETIREHGPDSVAFYI------SGQLLt 116
Cdd:cd02756  96 STRGGTNAERiwspdnRVGETRLTTPLVRRGGQLQP--TTWDDAIDLVARVIKGILDKDGNDDAVFASrfdhggGGGGF- 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 117 EDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGyKRSLGADAPPCSYEDLDCADCVLIAGSN-------MAFAHpvLFRR 189
Cdd:cd02756 173 ENNWGVGKFFFMALQTPFVRIHNRPAYNSEVHA-TREMGVGELNNSYEDARLADTIVLWGNNpyetqtvYFLNH--WLPN 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 190 LEAAKAAR-----------PEMRIVVIDPRRTDTCELAD--------LHLALLPGTDVALFHGILHILlWEDWidRSFIA 250
Cdd:cd02756 250 LRGATVSEkqqwfppgepvPPGRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDTALANAIARYI-YESL--DEVLA 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 251 EhtegfadlkelvrdytpaaVADICGIDRADLQRCAEWI------GRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATG 324
Cdd:cd02756 327 E-------------------AEQITGVPRAQIEKAADWIakpkegGYRKRVMFEYEKGIIWGNDNYRPIYSLVNLAIITG 387
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 325 KIGRAGCGPfsltgqpNAMGGRETGSLANLLPGHREAADPGHRA-----------EVAHYWGVEQLPTSPglSAIELFDA 393
Cdd:cd02756 388 NIGRPGTGC-------VRQGGHQEGYVRPPPPPPPWYPQYQYAPyidqllisgkgKVLWVIGCDPYKTTP--NAQRLRET 458
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 394 VHDgRIKALWIACTNPAQSLPDQRKIHEAL---ARCP---FVVVQEAFAgTETCQYADLLLPAASWGE-KEGSVTNSERR 466
Cdd:cd02756 459 INH-RSKLVTDAVEAALYAGTYDREAMVCLigdAIQPgglFIVVQDIYP-TKLAEDAHVILPAAANGEmNETSMNGHERR 536
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 467 ISHVRRAVPPPGEARQDWNIVCDFARRL------EGHLRPAKPGLFAF----------ADSRSLFDE------YKLLTAG 524
Cdd:cd02756 537 LRLYEKFMDPPGEAMPDWWIAAMIANRIyelyqeEGKGGSAQYQFFGFiwkteednfmDGSQEFADGgefsedYYVLGQE 616
                       650       660       670       680       690
                ....*....|....*....|....*....|....*....|....*....|..
gi 15596976 525 RdldLSGLSYALLDRLGPQ--QWP---FPTGAEQGTARLYADGRFPTASGRA 571
Cdd:cd02756 617 R---YEGVTYNRLKAVGVNgiQLPvttDTVTKILVTNVLRTEGVFDTEDGKA 665
MopB_Arsenate-R cd02757
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ...
11-496 1.11e-35

This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239158 [Multi-domain]  Cd Length: 523  Bit Score: 142.58  E-value: 1.11e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  11 ASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGaslHLTgdLQA-----RALYPQLRLGKQLARA------ 79
Cdd:cd02757   3 PSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKG---HLG--LQQvydpdRILYPMKRTNPRKGRDvdpkfv 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  80 RSDWESALEHAAGRFAETIREHGPDSVAfYISGQLLTEDYYAFNKLARALVGTNNIdSNSRLCMSSAVVGYKRSLGADAP 159
Cdd:cd02757  78 PISWDEALDTIADKIRALRKENEPHKIM-LHRGRYGHNNSILYGRFTKMIGSPNNI-SHSSVCAESEKFGRYYTEGGWDY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 160 PcSYeDLDCADCVLIAGSN-MAFAHPV-LFRRLEAAKAARpeMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHI 237
Cdd:cd02757 156 N-SY-DYANAKYILFFGADpLESNRQNpHAQRIWGGKMDQ--AKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHV 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 238 LLWE---------DWID-------------RSFIAEHTEGF-ADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPR 294
Cdd:cd02757 232 ILTEglwdkdfvgDFVDgknyfkagetvdeESFKEKSTEGLvKWWNLELKDYTPEWAAKISGIPAETIERVAREFATAAP 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 295 FLSLW-----CMGLNQSSAGSAknsalinLHLATGkigragcgpfsLTGQPNAMGGretgslanllpghreaadpghrae 369
Cdd:cd02757 312 AAAAFtwrgaTMQNRGSYNSMA-------CHALNG-----------LVGSIDSKGG------------------------ 349
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 370 vahywgveqlpTSPGLSaielfdavhDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAGtETCQYADLLLP 449
Cdd:cd02757 350 -----------LCPNMG---------VPKIKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMS-ETTYFADIVLP 408
                       490       500       510       520       530
                ....*....|....*....|....*....|....*....|....*....|
gi 15596976 450 AASWGEKEG---SVTNSERRISHVRRAVPPPGEARQDWNIVCDFARRLEG 496
Cdd:cd02757 409 DGHHFERWDvmsQENNLHPWLSIRQPVVKSLGEVREETEILIELAKKLDP 458
MopB_NADH-Q-OR-NuoG2 cd02768
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ...
12-486 1.16e-35

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: 139.73  E-value: 1.16e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  12 STCCYCGVGCGVLIEHDGERILGVQgdPR-HPA-NFGRLCSKG--ASLHLTGDlqARALYPQLRLGKQLARArsDWESAL 87
Cdd:cd02768   2 SIDVHDALGSNIRVDVRGGEVMRIL--PReNEAiNEEWISDKGrfGYDGLNSR--QRLTQPLIKKGGKLVPV--SWEEAL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  88 EHAAGRfaetIREHGPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVvgyKRSLGADAPPCSYEDLD 167
Cdd:cd02768  76 KTVAEG----LKAVKGDKIGGIAGPRADLESLFLLKKLLNKL-GSNNIDHRLRQSDLPAD---NRLRGNYLFNTSIAEIE 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 168 CADCVLIAGSNMAFAHPVLFRRL-EAAKaaRPEMRIVVIDPRRTDTceladlhlallpgtdvalfhgilhillwedWIDR 246
Cdd:cd02768 148 EADAVLLIGSNLRKEAPLLNARLrKAVK--KKGAKIAVIGPKDTDL------------------------------IADL 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 247 SFIAEHteGFADLKELVRDYTPAAVADICgidrADLQ---RCAEWIGrsprflslwcmglnqSSAGSAKNSALINlhlat 323
Cdd:cd02768 196 TYPVSP--LGASLATLLDIAEGKHLKPFA----KSLKkakKPLIILG---------------SSALRKDGAAILK----- 249
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 324 gkigragcgpfsltgqpnamggretgSLANLlpghreAADPGHRAEVahyWGVEQLPTSPGLSAIEL-----FDAVHDGR 398
Cdd:cd02768 250 --------------------------ALANL------AAKLGTGAGL---WNGLNVLNSVGARLGGAgldagLALLEPGK 294
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 399 IKALWIACTNPAQSLPDQRKiheALARCPFVVVQEAFAGtETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPG 478
Cdd:cd02768 295 AKLLLLGEDELDRSNPPAAV---ALAAADAFVVYQGHHG-DTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPG 370

                ....*...
gi 15596976 479 EARQDWNI 486
Cdd:cd02768 371 DAREDWKI 378
PRK15488 PRK15488
thiosulfate reductase PhsA; Provisional
10-693 1.09e-34

thiosulfate reductase PhsA; Provisional


Pssm-ID: 237973 [Multi-domain]  Cd Length: 759  Bit Score: 142.50  E-value: 1.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   10 TASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHltgdlqaRALYPQLRLGKQLARA--RSD----- 82
Cdd:PRK15488  44 TPSICEMCSTRCPIEARVVNGKNVFIQGNPKAKSFGTKVCARGGSGH-------SLLYDPQRIVKPLKRVgeRGEgkwqe 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   83 --WESALEHAAGRFAETIREHGPDSVAFYI-SGQLLTedyYAFNkLARALvGTNNIDSNSRLCMSSAVVGYKRSLGADAP 159
Cdd:PRK15488 117 isWDEAYQEIAAKLNAIKQQHGPESVAFSSkSGSLSS---HLFH-LATAF-GSPNTFTHASTCPAGYAIAAKVMFGGKLK 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  160 pcsyEDLDCADCV------LIAGSNMAFAHPVlfrrleAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHG 233
Cdd:PRK15488 192 ----RDLANSKYIinfghnLYEGINMSDTRGL------MTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLA 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  234 ILHILLWEDWIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCA-EWIGRSPRFLSLWCMGLNQSSAGSAK 312
Cdd:PRK15488 262 LCHVLIEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIArELAAAAPHAIVDFGHRATFTPEEFDM 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  313 NSALINLHLATGKIGRAGcGPFSLTGQP--NAMGGRETG-SLANllPGHR----------EAADPGHrAEVAHYWGVEQL 379
Cdd:PRK15488 342 RRAIFAANVLLGNIERKG-GLYFGKNASvyNKLAGEKVApTLAK--PGVKgmpkptakriDLVGEQF-KYIAAGGGVVQS 417
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  380 PTSPGLSAIELfdavhdgRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGS 459
Cdd:PRK15488 418 IIDATLTQKPY-------QIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYL-SESAAYADVVLPESTYLERDEE 489
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  460 VTN-SERRISH-VR-RAVPPPGEARQDWNIVCDFARRLeghlrpAKPGLFAFADSRslfdEYKLLTAGRDLDLsglsYAL 536
Cdd:PRK15488 490 ISDkSGKNPAYaLRqRVVEPIGDTKPSWQIFKELGEKM------GLGQYYPWQDME----TLQLYQVNGDHAL----LKE 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  537 LDRLGPQQW--P---------------FPTGAEQGTARLYADG-RFPTASGRAQLVAE------PYRAAQEKRDARY--- 589
Cdd:PRK15488 556 LKKKGYVSFgvPlllrepkmvakfvarYPNAKAVDEDGTYGSQlKFKTPSGKIELFSAklealaPGYGVPRYRDVALkke 635
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  590 -PLTLNTGRLrdQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRG-----ALVLPvsaddSVRPG 663
Cdd:PRK15488 636 dELYFIQGKV--AVHTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGkekgkALVTP-----GIRPD 708
                        730       740       750
                 ....*....|....*....|....*....|....*..
gi 15596976  664 QAFLPMHWGDR-------FLKGLGCNVLTLPAFDPLS 693
Cdd:PRK15488 709 TLFAYMGFGSKnkeltraTGKGIHCGNLLPHVTSPVS 745
MopB_4 cd02765
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ...
12-576 5.36e-33

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: 135.30  E-value: 5.36e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  12 STCCY--CGVGCGVLIEHDGERILGVQgdPRHPAN--FGRLCSKGASlHLTGDLQA-RALYPQLRLGKqlaRA-----RS 81
Cdd:cd02765   1 YTACPpnCGGRCPLKCHVRDGKIVKVE--PNEWPDktYKRGCTRGLS-HLQRVYSPdRLKYPMKRVGE---RGegkfeRI 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  82 DWESALEHAAGRFAETIREHGPDSVAFYISgqllTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPC 161
Cdd:cd02765  75 TWDEALDTIADKLTEAKREYGGKSILWMSS----SGDGAILSYLRLALLGGGLQDALTYGIDTGVGQGFNRVTGGGFMPP 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 162 SYE--DLDCADCVLIAGSNMAFAHpvlFRRLE-AAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHIL 238
Cdd:cd02765 151 TNEitDWVNAKTIIIWGSNILETQ---FQDAEfFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYI 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 239 LWEDWIDRSFIAEHT--------------------------------------------------------------EGF 256
Cdd:cd02765 228 LEHNWYDEAFLKSNTsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeytingvkvhTVL 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 257 ADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPfsl 336
Cdd:cd02765 308 TALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGV--- 384
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 337 tgqpnamggretgslanllpghreaadpghraevahywgveqlptspglsaielfdavhdGRIKALWIACTNPAQSLPDQ 416
Cdd:cd02765 385 ------------------------------------------------------------GQIKFMYFMGSNFLGNQPDR 404
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 417 RKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERR--ISHVRRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02765 405 DRWLKVMKNLDFIVVVDIFH-TPTVRYADIVLPAAHWFEVEDLLVRYTTHphVLLQQKAIEPLFESKSDFEIEKGLAERL 483
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 495 E-GHLRPAKPG--LFAFADSRSLFdeykllTAGRDLDLSGLSYALLDRLGPQQwpfPTGAeqgtarlYADGRFPTASGRA 571
Cdd:cd02765 484 GlGDYFPKTPEdyVRAFMNSDDPA------LDGITWEALKEEGIIMRLATPED---PYVA-------YLDQKFGTPSGKL 547

                ....*
gi 15596976 572 QLVAE 576
Cdd:cd02765 548 EFYNE 552
MopB_CT_Formate-Dh_H cd02790
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ...
587-706 3.42e-32

Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239191 [Multi-domain]  Cd Length: 116  Bit Score: 121.19  E-value: 3.42e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 587 ARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAF 666
Cdd:cd02790   1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVF 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15596976 667 LPMHWGDRflkglGCNVLTLPAFDPLSKQPELKHAGVQVE 706
Cdd:cd02790  81 MPFHFAEA-----AANLLTNAALDPVAKIPEFKVCAVRVE 115
Molydop_binding pfam01568
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ...
591-701 5.97e-31

Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.


Pssm-ID: 426328 [Multi-domain]  Cd Length: 110  Bit Score: 117.37  E-value: 5.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   591 LTLNTGRLRDQWHGMSRTGTCARLFGHEEEAlVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPMH 670
Cdd:pfam01568   1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEV-VEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 15596976   671 WGDRFlKGLGCNVLTLPAFDPLSKQPELKHA 701
Cdd:pfam01568  80 WWYEP-RGGNANALTDDATDPLSGGPEFKTC 109
MopB_DmsA-EC cd02770
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ...
17-494 2.81e-30

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: 127.44  E-value: 2.81e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  17 CGVGCG------VLIEhDGErILGVQGDPRHPANFG----RLCSKGASL--HLTG-DlqaRALYPQLRLGKqlaR----- 78
Cdd:cd02770   4 CTVNCGgrcplkAHVK-DGV-ITRIETDDTGDDDPGfhqiRACLRGRSQrkRVYNpD---RLKYPMKRVGK---Rgegkf 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  79 ARSDWESALEHAAGRFAETIREHGPDSVafYISGQllTEDYYAF----NKLAR--ALVG--TNNIDSNSRLCMSSAvvgY 150
Cdd:cd02770  76 VRISWDEALDTIASELKRIIEKYGNEAI--YVNYG--TGTYGGVpagrGAIARllNLTGgyLNYYGTYSWAQITTA---T 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 151 KRSLGADAPPCSYEDLDCADCVLIAGSN-----MAFAHPVLFrrLEAAKAARpeMRIVVIDPRRTDTCE-LADLHLALLP 224
Cdd:cd02770 149 PYTYGAAASGSSLDDLKDSKLVVLFGHNpaetrMGGGGSTYY--YLQAKKAG--AKFIVIDPRYTDTAVtLADEWIPIRP 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 225 GTDVALFHGILHILLWEDWIDRSFIAEHTEGF--------ADLKELVRDY-----------TPAAVADICGIDRADLQRC 285
Cdd:cd02770 225 GTDAALVAAMAYVMITENLHDQAFLDRYCVGFdaehlpegAPPNESYKDYvlgtgydgtpkTPEWASEITGVPAETIRRL 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 286 AEWIG--RSPRFLSLWcmGLNQSSAGSAKNSALINLHLATGKIGRAGCGPfsltgqpnamGGRETGSLANLLPGhreaad 363
Cdd:cd02770 305 AREIAttKPAAILQGW--GPQRHANGEQAARAIMMLAAMTGNVGIPGGNT----------GARPGGSAYNGAGL------ 366
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 364 PGHRAEVAhywgvEQLPTSPGLSAIEL------FDAVHDGR------IKALW-IACTNPAQSLPDQRKIHEAL----ARC 426
Cdd:cd02770 367 PAGKNPVK-----TSIPCFMWTDAIERgeemtaDDGGVKGAdklksnIKMIWnYAGNTLINQHSDDNNTTRALlddeSKC 441
                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596976 427 PFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHV----RRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02770 442 EFIVVIDNFM-TPSARYADILLPDTTELEREDIVLTSNAGMMEYliysQKAIEPLYECKSDYEICAELAKRL 512
PRK07860 PRK07860
NADH dehydrogenase subunit G; Validated
83-670 5.88e-30

NADH dehydrogenase subunit G; Validated


Pssm-ID: 236118 [Multi-domain]  Cd Length: 797  Bit Score: 127.37  E-value: 5.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   83 WESALEHAAGRFAETirehgPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRL-------CMSSAVVGYKRSLg 155
Cdd:PRK07860 296 WSEALAVAARGLAAA-----RGRVGVLVGGRLTVEDAYAYAKFARVALGTNDIDFRARPhsaeeadFLAARVAGRGLGV- 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  156 adappcSYEDLDCADCVLIAGSNMAFAHPVLFRRLEaaKAARPE-MRIVVIDPRRTDTceLADLHLALL---PGTDVALf 231
Cdd:PRK07860 370 ------TYADLEKAPAVLLVGFEPEEESPIVFLRLR--KAARKHgLKVYSIAPFATRG--LEKMGGTLLrtaPGGEAAA- 438
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  232 hgilhillwedwidrsfIAEHTEGFADLKELVRdyTPAAVAdICGidradlQRCAEwigrSPRFLSlwcmglnqssagsa 311
Cdd:PRK07860 439 -----------------LDALATGAPDVAELLR--TPGAVI-LVG------ERLAT----VPGALS-------------- 474
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  312 knsALINLHLATG-KIG----RAGcgpfsltgqpnAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGVEQLPTSPGLS 386
Cdd:PRK07860 475 ---AAARLADATGaRLAwvprRAG-----------ERGALEAGALPTLLPGGRPVADPAARAEVAAAWGVDELPAAPGRD 540
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  387 AIELFDAVHDGRIKALWIACTNPAqSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERR 466
Cdd:PRK07860 541 TAGILAAAAAGELGALLVGGVEPA-DLPDPAAALAALDAAGFVVSLELRH-SAVTERADVVLPVAPVAEKAGTFLNWEGR 618
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  467 ISHVRRAVPPPGearqdwnivcdfarrleghlrpakpglfAFADSR---SLFDEyklltAGRDLDLSGLSYAL--LDRLG 541
Cdd:PRK07860 619 LRPFEAALRTTG----------------------------ALSDLRvldALADE-----MGVDLGLPTVAAARaeLARLG 665
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  542 PqqWpfpTGAEQGTARLYADGRFPTASGRAQLvaepyraaqekrdARYPLTLNTGRLRDqwhgmsrtGTCArLFGHEEEA 621
Cdd:PRK07860 666 A--W---DGARAAAPAVPAAAPPQPGAGEAVL-------------ATWRMLLDDGRLQD--------GEPH-LAGTARPP 718
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*....
gi 15596976  622 LVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVrPGQAFLPMH 670
Cdd:PRK07860 719 VARLSAATAAEIGVADGDAVTVSTERGSITLPLAITDMP-DRVVWLPLN 766
PRK09939 PRK09939
acid resistance putative oxidoreductase YdeP;
83-430 1.04e-27

acid resistance putative oxidoreductase YdeP;


Pssm-ID: 182156 [Multi-domain]  Cd Length: 759  Bit Score: 120.15  E-value: 1.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   83 WESALEHAAGRFaETIREhgPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCS 162
Cdd:PRK09939 127 WQQAFDEIGARL-QSYSD--PNQVEFYTSGRTSNEAAFLYQLFAREY-GSNNFPDCSNMCHEPTSVGLAASIGVGKGTVL 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  163 YEDLDCADCVLIAGSNMAFAHPVLFRRLEAAkaARPEMRIVVIDPRRTDTCE------------------LADLHLALLP 224
Cdd:PRK09939 203 LEDFEKCDLVICIGHNPGTNHPRMLTSLRAL--VKRGAKMIAINPLQERGLErftapqnpfemltnsetqLASAYYNVRI 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  225 GTDVALFHGILHILLWED----------WIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPR 294
Cdd:PRK09939 281 GGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAER 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  295 FLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAMGGRETGSlanllpghREAADPGHRAEVAHYW 374
Cdd:PRK09939 361 TIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGI--------TEKPSAEFLARLGERY 432
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15596976  375 GVEQlPTSPGLSAIELFDAVHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVV 430
Cdd:PRK09939 433 GFTP-PHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAV 487
MopB_DMSOR-BSOR-TMAOR cd02769
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
193-494 3.76e-27

The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239170 [Multi-domain]  Cd Length: 609  Bit Score: 117.75  E-value: 3.76e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 193 AKAARPEMRIVVIDPRRTDTCELADL-HLALLPGTDVALFHGILHILLWEDWIDRSFIAEHTEGFADLKELVR---D--- 265
Cdd:cd02769 202 KALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLgesDgvp 281
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 266 YTPAAVADICGIDRADLQRCAEWIGRSPRFLSL-WCMglNQSSAGSAKNSALINLHLATGKIGRAGCG-PFSLTGQPNAM 343
Cdd:cd02769 282 KTPEWAAAICGIPAETIRELARRFASKRTMIMAgWSL--QRAHHGEQPHWMAVTLAAMLGQIGLPGGGfGFGYHYSNGGG 359
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 344 GGRETGSLANLLPGHREAAD--PGHRAevahywgVEQLpTSPGlsaiELFDavHDGR------IKALWIACTNPAQSLPD 415
Cdd:cd02769 360 PPRGAAPPPALPQGRNPVSSfiPVARI-------ADML-LNPG----KPFD--YNGKkltypdIKLVYWAGGNPFHHHQD 425
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 416 QRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEG-SVTNSERRISHVRRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02769 426 LNRLIRAWQKPETVIVHEPFW-TATARHADIVLPATTSLERNDiGGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERL 504
MopB_CT cd02775
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ...
598-699 7.43e-27

Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.


Pssm-ID: 239176 [Multi-domain]  Cd Length: 101  Bit Score: 105.09  E-value: 7.43e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 598 LRDQWHGMSRTGtCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPMHWGDRFLK 677
Cdd:cd02775   1 LRDHFHSGTRTR-NPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGGR 79
                        90       100
                ....*....|....*....|..
gi 15596976 678 GLGCNVLTLPAFDPLSKQPELK 699
Cdd:cd02775  80 GGNANVLTPDALDPPSGGPAYK 101
MopB_2 cd02763
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
12-519 1.96e-25

The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins


Pssm-ID: 239164 [Multi-domain]  Cd Length: 679  Bit Score: 112.62  E-value: 1.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  12 STCCYCGVGCGVLIE-HDGErILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGKQLARA--RSDWESALE 88
Cdd:cd02763   2 TTCYMCACRCGIRVHlRDGK-VRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPRGSGQfeEIEWEEAFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  89 HAAGRFAEtIREHGPDSVAFYiSGQlltEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDC 168
Cdd:cd02763  81 IATKRLKA-ARATDPKKFAFF-TGR---DQMQALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLYSIGGSFWEFGGPDLEH 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 169 ADCVLIAGSnmAFAHPVLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSF 248
Cdd:cd02763 156 TKYFMMIGV--AEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLIDWEF 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 249 IAEHTEGfadlKELVrDYTPAAVADICGIDRADLQRCA-------------------EWIGR-----SPRFLSLWCM-GL 303
Cdd:cd02763 234 LKRYTNA----AELV-DYTPEWVEKITGIPADTIRRIAkelgvtardqpielpiawtDVWGRkhekiTGRPVSFHAMrGI 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 304 NQSSAGSAKNSALINLHLATGKIGRAGC----GPFSLTGQPnamGGRETGSLANLLPGHREA-------ADPGH------ 366
Cdd:cd02763 309 AAHSNGFQTIRALFVLMMLLGTIDRPGGfrhkPPYPRHIPP---LPKPPKIPSADKPFTPLYgpplgwpASPDDllvded 385
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 367 ----RAEVAHYWgveQLPTSP-GL--SAIELFDAVHDGRIKALWIACTNPA-QSLPDQRKIHEALA--------RCPFVV 430
Cdd:cd02763 386 gnplRIDKAYSW---EYPLAAhGCmqNVITNAWRGDPYPIDTLMIYMANMAwNSSMNTPEVREMLTdkdasgnyKIPFII 462
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 431 VQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISH-------VRR-AVPPPGEARQDWNIVCDFARRLeghlrpak 502
Cdd:cd02763 463 VCDAFY-SEMVAFADLVLPDTTYLERHDAMSLLDRPISEadgpvdaIRVpIVEPKGDVKPFQEVLIELGTRL-------- 533
                       570
                ....*....|....*....
gi 15596976 503 pGLFAF--ADSRSLFDEYK 519
Cdd:cd02763 534 -GLPGFtnEDGTRKYRDYP 551
MopB_CT_Formate-Dh-Na-like cd02792
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ...
587-706 1.91e-23

Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239193 [Multi-domain]  Cd Length: 122  Bit Score: 96.14  E-value: 1.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 587 ARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAF 666
Cdd:cd02792   1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVG 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15596976 667 LPMHWGDRFL-KGLGCNVLTLPAFDPLSKQPELKHAGVQVE 706
Cdd:cd02792  81 IPYHWGGMGLvIGDSANTLTPYVGDPNTQTPEYKAFLVNIE 121
PRK14990 PRK14990
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
17-708 1.81e-22

anaerobic dimethyl sulfoxide reductase subunit A; Provisional


Pssm-ID: 184952 [Multi-domain]  Cd Length: 814  Bit Score: 103.57  E-value: 1.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   17 CGVGCGV---LIEH--DGErILGVQGDPRHPANFG-----RLCSKGASLHLTGDLQARALYPQLRLGK--QLARARSDWE 84
Cdd:PRK14990  63 CTVNCGSrcpLRMHvvDGE-IKYVETDNTGDDNYDglhqvRACLRGRSMRRRVYNPDRLKYPMKRVGArgEGKFERISWE 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   85 SALEHAAGRFAETIREHGPDSVAF-YISGQL---LTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVV--GYKRSLGADA 158
Cdd:PRK14990 142 EAYDIIATNMQRLIKEYGNESIYLnYGTGTLggtMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIaeGLNYTYGGWA 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  159 PPCSYEDLDCADCVLIAGSN-----MAFAHPVLFrrLEAAKAaRPEMRIVVIDPRRTDT-CELADLHLALLPGTDVALFH 232
Cdd:PRK14990 222 DGNSPSDIENSKLVVLFGNNpgetrMSGGGVTYY--LEQARQ-KSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVN 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  233 GILHILLWEDWIDRSFIAEHTEGFaDLKEL---------VRDY-----------TPAAVADICGIDRADLQRCAEWIGRS 292
Cdd:PRK14990 299 GLAYVMITENLVDQPFLDKYCVGY-DEKTLpasapknghYKAYilgegpdgvakTPEWASQITGVPADKIIKLAREIGST 377
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  293 -PRFLSL-WcmGLNQSSAGSAKNSALINLHLATGKIGRAGcgpfsltgqpNAMGGREtGSLAnlLPGHREAA--DPGHRA 368
Cdd:PRK14990 378 kPAFISQgW--GPQRHANGEIATRAISMLAILTGNVGING----------GNSGARE-GSYS--LPFVRMPTleNPIQTS 442
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  369 EVAHYWgVEQLPTSPGLSAieLFDAVH-----DGRIKALWIACTNpaqSLPDQR----KIHEAL---ARCPFVVVQEAFA 436
Cdd:PRK14990 443 ISMFMW-TDAIERGPEMTA--LRDGVRgkdklDVPIKMIWNYAGN---CLINQHseinRTHEILqddKKCELIVVIDCHM 516
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  437 gTETCQYADLLLPAASWGEK-EGSVTNSERRISHV---RRAVPPPGEARQDWNIVCDFARRL------------EGHLRp 500
Cdd:PRK14990 517 -TSSAKYADILLPDCTASEQmDFALDASCGNMSYVifnDQVIKPRFECKTIYEMTSELAKRLgveqqftegrtqEEWMR- 594
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  501 akpglFAFADSRSL------FDEYKLLTAGRDLDLSG--LSYALLdRLGPQQWPF--PTGA----EQGTARLYADGRFPT 566
Cdd:PRK14990 595 -----HLYAQSREAipelptFEEFRKQGIFKKRDPQGhhVAYKAF-REDPQANPLttPSGKieiySQALADIAATWELPE 668
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  567 ASgraqlVAEP-------YRAAQEKRDARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEealVHLHPEELRRRQLLDGQ 639
Cdd:PRK14990 669 GD-----VIDPlpiytpgFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAACRQE---MWINPLDAQKRGINNGD 740
                        730       740       750       760       770       780       790
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596976  640 LVRLKSRRGALVLPVSADDSVRPGQAFL-PMHWGD----RFLKGLGCNVLTLPAFDPLSKQPELKHAGVQVESV 708
Cdd:PRK14990 741 KVRIFNDRGEVHIEAKVTPRMMPGVVALgEGAWYDpdakRVDKGGCINVLTTQRPSPLAKGNPSHTNLVQVEKV 814
MopB_NDH-1_NuoG2 cd02772
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ...
82-486 1.29e-20

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: 95.50  E-value: 1.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  82 DWESALEHAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDsnSRLCMSSAVVGYKRSlGADAPPC 161
Cdd:cd02772  70 DWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLARGL-GSDNID--HRLRQSDFRDDAKAS-GAPWLGM 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 162 SYEDLDCADCVLIAGSNMAFAHPVLFRRLEaaKAARPEMRIVVIDPrrtdtceLADLHLALLPGTDVALFHGILHILLwe 241
Cdd:cd02772 146 PIAEISELDRVLVIGSNLRKEHPLLAQRLR--QAVKKGAKLSAINP-------ADDDFLFPLSGKAIVAPSALANALA-- 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 242 dwiDRSFIAEHTEGFAdLKELVRDYTPAAVADICGIDRADLQRCAEWIGRsprflslwcMGLNQSSAGSAKNSALINLHL 321
Cdd:cd02772 215 ---QVAKALAEEKGLA-VPDEDAKVEASEEARKIAASLVSAERAAVFLGN---------LAQNHPQAATLRALAQEIAKL 281
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 322 ATGKIGRagcgpfsLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVahYWGVEqlptsPGLsaielfdavhdgrika 401
Cdd:cd02772 282 TGATLGV-------LGEGANSVGAYLAGALPHGGLNAAAMLEQPRKAYL--LLNVE-----PEL---------------- 331
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 402 lwiACTNPAQSLpdqrkihEALARCPFVVVQEAFAGTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEAR 481
Cdd:cd02772 332 ---DCANPAQAL-------AALNQAEFVVALSAFASAALLDYADVLLPIAPFTETSGTFVNLEGRVQSFKGVVKPLGEAR 401

                ....*
gi 15596976 482 QDWNI 486
Cdd:cd02772 402 PAWKV 406
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
386-498 1.92e-20

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: 95.29  E-value: 1.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 386 SAIELFDAVHDGRIKALWIACTNPAQSLPDQrkIHEALARCPFVVVQEAFaGTETCQYADLLLPAASWGEKEGSVTNSER 465
Cdd:COG1034 320 DAAAILEAAEAGKLKALVLLGADPYDLDPAA--ALAALAKADFVVVLDHF-GSATAERADVVLPAAAFAEKSGTFVNLEG 396
                        90       100       110
                ....*....|....*....|....*....|...
gi 15596976 466 RISHVRRAVPPPGEARQDWNIVCDFARRLEGHL 498
Cdd:COG1034 397 RVQRFNAAVPPPGEARPDWRVLRALANALGAGL 429
Molybdop_Fe4S4 pfam04879
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ...
7-56 3.48e-19

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: 81.96  E-value: 3.48e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15596976     7 LRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLH 56
Cdd:pfam04879   1 MKVVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGY 50
Molybdop_Fe4S4 smart00926
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ...
7-56 8.61e-19

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: 80.76  E-value: 8.61e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 15596976      7 LRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLH 56
Cdd:smart00926   1 EKWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGL 50
MopB_Tetrathionate-Ra cd02758
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ...
12-570 2.81e-17

The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239159 [Multi-domain]  Cd Length: 735  Bit Score: 86.63  E-value: 2.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  12 STCCYCGVGCG--VLIEHDGERILGVQGDPRHPANF---------------------------GRLCSKGASLhltgdlq 62
Cdd:cd02758   2 SSCLGCWTQCGirVRVDKETGKVLRIAGNPYHPLNTapslpyntplkeslylslvgenglkarATACARGNAG------- 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  63 ARALYPQLRLGKQLARA--RSD-------WESALEHAA--GRFAET--------IR-----------EHGPDSVAF-YIS 111
Cdd:cd02758  75 LQYLYDPYRVLQPLKRVgpRGSgkwkpisWEQLIEEVVegGDLFGEghveglkaIRdldtpidpdhpDLGPKANQLlYTF 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 112 GQllTEDYYAFNK-LARALVGTNNIDSNSRLCMSSAVVGYKRSLG-ADAPPCSYEDLDCADCVLIAGSNMAFAHPVLFR- 188
Cdd:cd02758 155 GR--DEGRTPFIKrFANQAFGTVNFGGHGSYCGLSYRAGNGALMNdLDGYPHVKPDFDNAEFALFIGTSPAQAGNPFKRq 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 189 -RLEAAKAARPEMRIVVIDPR--RTDT-CELADLHLALLPGTDVALFHGILHILLWEDWIDRSFIAEHTE---------- 254
Cdd:cd02758 233 aRRLAEARTEGNFKYVVVDPVlpNTTSaAGENIRWVPIKPGGDGALAMAMIRWIIENERYNAEYLSIPSKeaakaageps 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 255 ---------------GFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINL 319
Cdd:cd02758 313 wtnathlvitvrvksALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTMHSNGFYNAYAIRML 392
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 320 HLATGKIGRAGcGpFSLTGQPNAMGGRETGSLANLLPGH---------REAAD----PGHRAEVAH----Y-----Wgve 377
Cdd:cd02758 393 NALIGNLNWKG-G-LLMSGGGFADNSAGPRYDFKKFFGEvkpwgvpidRSKKAyektSEYKRKVAAgenpYpakrpW--- 467
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 378 qLPTSPGLSAiELFDAVHDG---RIKALWIACTNPAQSLPDQRKIHEAL----ARCPFVVVQEAFAGtETCQYADLLLPA 450
Cdd:cd02758 468 -YPLTPELYT-EVIASAAEGypyKLKALILWMANPVYGAPGLVKQVEEKlkdpKKLPLFIAIDAFIN-ETSAYADYIVPD 544
                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 451 ASWGEKEGSVTN---SERRISHVRR-AVPPP------GEARQDWNIVCDFARRLE--GHLRPAKPGLFAFADSRSLFDEY 518
Cdd:cd02758 545 TTYYESWGFSTPwggVPTKASTARWpVIAPLtektanGHPVSMESFLIDLAKALGlpGFGPNAIKDGQGNKFPLNRAEDY 624
                       650       660       670       680       690       700       710
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596976 519 KLLTAG---------------RDLDLSGLSY---ALLDRLGPQQWPFptgaeqgTARLYA-DGRFPTASGR 570
Cdd:cd02758 625 YLRVAAniaydgkapvpdaseEELKLTGVNRpipALKRTLKPEEWRK-------VAYILArGGRFAPYEES 688
FwdB COG1029
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
13-460 4.75e-15

Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];


Pssm-ID: 440652 [Multi-domain]  Cd Length: 428  Bit Score: 78.35  E-value: 4.75e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  13 TCCYCGVGCGVL-IEHDGERILGVQgdprhpanfgRLCSKGASLHLTGDLQARALYPQLRlGKQlararSDWESALEHAA 91
Cdd:COG1029   9 VCPFCGCLCDDLeVEVEGGKIVVVK----------NACAIGAAKFERAVSDHRITSPRIR-GKE-----VSLEEAIDKAA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  92 GRFAETIRehgPdsvAFYISGQLLTEDYYAFNKLARALVGTnnIDSNSRLCMSSAVVGYKRS------LGadappcsyED 165
Cdd:COG1029  73 EILANAKR---P---LIYGLSSTDCEAMRAGLALAERVGAV--VDNTASVCHGPSLLALQDVgwptctLG--------EV 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 166 LDCADCVLIAGSNMAFAHP------VLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALfhgilhill 239
Cdd:COG1029 137 KNRADVIIYWGCNPVHAHPrhmsrySVFPRGFFTPKGRKDRTVIVVDPRPTDTAKVADLHLQVKPGRDYEV--------- 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 240 wedwidrsfiaehtegFADLKELVRDYTPAAvADICGIDRADLQRCAEWIgRSPRFLSL-WCMGLNQSSAGSAKNSALIN 318
Cdd:COG1029 208 ----------------LSALRALVRGKELSP-EEVAGIPVEDLEELAERL-KNAKYGVIfWGMGLTQSPGKHLNVDAAIE 269
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 319 LHLATGKIGRAGCGPfsltgqpnaMGGRE----TGSLANLLPGHREAAD--PGHraevAHYwgveqlptSPGLSAIElfD 392
Cdd:COG1029 270 LVRDLNRYTKFSILP---------LRGHYnvagANQVASWQTGYPFRVDfsRGY----PRY--------NPGETSAV--D 326
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596976 393 AVHDGRIKALWIACTNPAQSLPdqRKIHEALARCPFVVVqeAFAGTETCQYADLLLPAASWG-EKEGSV 460
Cdd:COG1029 327 LLARGEVDALLWVASDPGAHFP--PDAVEHLAKIPTIVI--DPHGTPTTEVADVVIPVAIPGiEHGGTA 391
PRK15102 PRK15102
trimethylamine-N-oxide reductase TorA;
193-494 2.33e-14

trimethylamine-N-oxide reductase TorA;


Pssm-ID: 237909 [Multi-domain]  Cd Length: 825  Bit Score: 77.40  E-value: 2.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  193 AKAARPEMRIVVIDPRRTDT-----CEladlHLALLPGTDVALFHGILHILLWEDWIDRSFIAEHTEGFADL------KE 261
Cdd:PRK15102 248 EKVAKGEINVISIDPVVTKTqnylgCE----HLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFlpyllgEK 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  262 LVRDYTPAAVADICGIDRADLQRCAEWI--GRSpRFLSLWCMGLNQSSAGSAKNSALinlhLAT--GKIGRAGcGPFSLT 337
Cdd:PRK15102 324 DGVPKTPEWAEKICGIDAETIRELARQMakGRT-QIIAGWCIQRQQHGEQPYWMGAV----LAAmlGQIGLPG-GGISYG 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  338 GQPNAMGGRETGslANLLPGHREAADPGHRA--EVAHYWGV-EQLPTSPGLSAI----ELFDAvhDGR------IKALWI 404
Cdd:PRK15102 398 HHYSGIGVPSSG--GAIPGGFPGNLDTGQKPkhDNSDYKGYsSTIPVARFIDAIlepgKTINW--NGKkvtlppLKMMIF 473
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  405 ACTNPAQSLPDQRKIHEALARCPFVVVQEaFAGTETCQYADLLLPAASWGEKE-----GSVTNseRRISHVRRAVPPPGE 479
Cdd:PRK15102 474 SGTNPWHRHQDRNRMKEAFRKLETVVAID-NQWTATCRFADIVLPACTQFERNdidqyGSYSN--RGIIAMKKVVEPLFE 550
                        330
                 ....*....|....*
gi 15596976  480 ARQDWNIVCDFARRL 494
Cdd:PRK15102 551 SRSDFDIFRELCRRF 565
MopB_PHLH cd02764
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ...
10-458 5.52e-14

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: 75.60  E-value: 5.52e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  10 TASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKG-ASLHLTGDlQARALYPqLRLGKQLARARSDWESALE 88
Cdd:cd02764  45 YATSLVPAGEGQGVLVKTVDGRPIKIEGNPDHPASLGGTSARAqASVLSLYD-PDRAQGP-LRRGIDGAYVASDWADFDA 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  89 HAAGRFAETireHGPDSVAFyISGQLL---TEDYYAFnkLARALVGTNN--IDSNSRLCMSSAvvgYKRSLGADAPPcSY 163
Cdd:cd02764 123 KVAEQLKAV---KDGGKLAV-LSGNVNsptTEALIGD--FLKKYPGAKHvvYDPLSAEDVNEA---WQASFGKDVVP-GY 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 164 eDLDCADCVLIAGSNM--AFAHPVLFRRLEAAK----AARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHI 237
Cdd:cd02764 193 -DFDKAEVIVSIDADFlgSWISAIRHRHDFAAKrrlgAEEPMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHK 271
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 238 LLwedwidRSFIAEHTEGFADLKELvrDYTPAAVADICGIDRADLQRCAEWIGRSPRflSLWCMGLNQSSAGSAKNSALI 317
Cdd:cd02764 272 LI------KKGAGSSLPDFFRALNL--AFKPAKVAELTVDLDKALAALAKALAAAGK--SLVVAGSELSQTAGADTQVAV 341
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 318 N-LHLATGKIGRAgcgpfsltgqpnamggretgslanllpghreaadpghraeVAHYWGVEQLPTSPGLSAIELFDAVHD 396
Cdd:cd02764 342 NaLNSLLGNDGKT----------------------------------------VDHARPIKGGELGNQQDLKALASRINA 381
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596976 397 GRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAA----SWGEKEG 458
Cdd:cd02764 382 GKVSALLVYDVNPVYDLPQGLGFAKALEKVPLSVSFGDRL-DETAMLCDWVAPMShgleSWGDAET 446
Bfd COG2906
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
854-900 5.59e-11

Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];


Pssm-ID: 442150 [Multi-domain]  Cd Length: 54  Bit Score: 58.29  E-value: 5.59e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 15596976 854 CSCQNVSQQTVLGGIARGL-DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:COG2906   4 CLCNGVTDRQIRAAIAEGAtSLEELRAALGAGTQCGSCVPEARELLAE 51
MopB_CT_1 cd02782
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
601-708 3.26e-10

The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239183 [Multi-domain]  Cd Length: 129  Bit Score: 58.56  E-value: 3.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 601 QWHGMSRTGTcarlfgheeealVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPMHWGDRF----- 675
Cdd:cd02782  25 RLVKGRNRCT------------LRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYpgvsg 92
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15596976 676 ---LKGLGCNVLTLPA-FDPLSKQPELKHAGVQVESV 708
Cdd:cd02782  93 agsRPGVNVNDLTDDTqRDPLSGNAAHNGVPVRLARV 129
MopB_Res-Cmplx1_Nad11 cd02773
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ...
442-487 3.25e-09

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: 59.97  E-value: 3.25e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15596976 442 QYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIV 487
Cdd:cd02773 323 QIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKIL 368
Fer2_BFD pfam04324
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ...
854-899 3.72e-09

BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilization functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).


Pssm-ID: 461261 [Multi-domain]  Cd Length: 50  Bit Score: 53.30  E-value: 3.72e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 15596976   854 CSCQNVSQQTVLGGIARGL-DLDGLKREFGCGTGCGSCVPEIKRLLA 899
Cdd:pfam04324   3 CRCFGVTDGEIRDAIREGLtTVEEVKRRTKAGTGCGSCRPAIEEILA 49
MopB_FmdB-FwdB cd02761
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ...
13-478 4.20e-09

The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239162 [Multi-domain]  Cd Length: 415  Bit Score: 59.65  E-value: 4.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  13 TCCYCGVGCGVL-IEHDGERILGvqgdPRHpanfgrLCSKGASlHLTGdLQARALYPQLRlGKQlararSDWESALEHAA 91
Cdd:cd02761   3 VCPFCGLLCDDIeVEVEDNKITK----VRN------ACRIGAA-KFAR-YERRITTPRID-GKP-----VSLEEAIEKAA 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  92 GRFAETIRehgPdsvAFYISGQLLTEDYYAFNKLARALVGTnnIDSNSRLCMSSAVVGYKRSlgaDAPPCSYEDL-DCAD 170
Cdd:cd02761  65 EILKEAKR---P---LFYGLGTTVCEAQRAGIELAEKLGAI--IDHAASVCHGPNLLALQDS---GWPTTTLGEVkNRAD 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 171 CVLIAGSNMAFAHP------VLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDwi 244
Cdd:cd02761 134 VIVYWGTNPMHAHPrhmsrySVFPRGFFREGGREDRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRALLRGAG-- 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 245 drsfiaehtegfadlkeLVRDytpaavaDICGIDRADLQRCAEWIGRSpRFLSL-WCMGLnQSSAGSAKN-SALINLHLA 322
Cdd:cd02761 212 -----------------LVPD-------EVAGIPAETILELAERLKNA-KFGVIfWGLGL-LPSRGAHRNiEAAIRLVKA 265
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 323 TGKIGRAGCGPfsLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYwgveqlptspglSAIELfdaVHDGRIKAL 402
Cdd:cd02761 266 LNEYTKFALLP--LRGHYNVRGFNQVLTWLTGYPFRVDFSRGYPRYNPGEF------------TAVDL---LAEGEADAL 328
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596976 403 WIACTNPAQSLPdqRKIHEALARCPFVVVqeAFAGTETCQYADLLLPAASWG-EKEGSVTNSERRISHVRRAVPPPG 478
Cdd:cd02761 329 LIIASDPPAHFP--QSAVKHLAEIPVIVI--DPPPTPTTRVADVVIPVAIPGiEAGGTAYRMDGVVVLPLKAVETER 401
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
783-900 1.53e-08

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 58.69  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   783 YDDPRRAIGKRVRLEDGRIVAVRLAGETLARDWLKELWLTGRADSELRRwLLAPLGAAPGRPSQGAGG----KTLCSCQN 858
Cdd:TIGR02374 339 IYDEQKGIYKKLVLSDDKLLGAVLFGDTSDYGRLLDMVLKQADISEDPA-IIKPQISGPEAGGPGVEAmpdsEQICSCNT 417
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 15596976   859 VSQQTVLGGIARGL--DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:TIGR02374 418 VTKGAIIDAIHTGSctTVEELKACTKAGTSCGGCKPLVEQLLRA 461
MopB_CT_3 cd02786
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ...
589-685 5.48e-08

The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239187 [Multi-domain]  Cd Length: 116  Bit Score: 51.90  E-value: 5.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 589 YPLTLNTGRLRdqwHGMSRT-GTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFL 667
Cdd:cd02786   1 YPLRLITPPAH---NFLNSTfANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVA 77
                        90
                ....*....|....*....
gi 15596976 668 P-MHWGDRFLKGLGCNVLT 685
Cdd:cd02786  78 EgGWWREHSPDGRGVNALT 96
NasA-like_Fer2_BFD-like cd19948
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of ...
850-899 7.31e-07

bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit NasA and similar proteins; The BFD-like [2Fe-2S]-binding domain described in this family is found at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit (NasA) such as Rhodobacter capsulatus E1F1 NasA. Nitrate reductase catalyzes the reduction of nitrate to nitrite, the first step of nitrate assimilation. R. capsulatus E1F1 nitrate reductase is composed of this NasA subunit and a small diaphorase subunit with FAD. Note that this [2Fe-2S]-binding domain is not always present; for example, it is absent from the characterized haloaechean Haloferax mediterranei NasA; both, however, have an [4Fe-4S] binding domain at their N-terminus. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381081 [Multi-domain]  Cd Length: 53  Bit Score: 46.75  E-value: 7.31e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15596976 850 GKTLCSCQNVSQQTVLGGIA-RGL-DLDGLKREFGCGTGCGSCVPEIKRLLA 899
Cdd:cd19948   1 GRTVCACFSVGENTIRRAIAdNGLtSVAQVGTCLKAGTNCGSCVPEIQKLLS 52
NirB_Fer2_BFD-like_1 cd19943
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ...
852-898 7.76e-06

first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large subunit of the NADH-dependent nitrite reductase; The NADH-dependent nitrite reductase (NirBD) complex comprises a large and a small subunit, and is also known as nitrite reductase (reduced nicotinamide adenine dinucleotide), NADH-nitrite oxidoreductase, and assimilatory nitrite reductase. NirBD uses NADH as electron donor, and FAD, iron-sulfur cluster, and siroheme cofactors, all embedded in the large subunit NirB to catalyze the 6-electron reduction of nitrite to ammonium. NirBD plays a role in regulating nitric oxide homeostasis in Streptomyces coelicolor. In addition to NirB, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins including bacterioferritin-associated ferredoxin (BFD) and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.


Pssm-ID: 381076 [Multi-domain]  Cd Length: 53  Bit Score: 43.76  E-value: 7.76e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15596976 852 TLCSCQNVSQQTVLGGI-ARGL-DLDGLKREFGCGTGCGSCVPEIKRLL 898
Cdd:cd19943   5 EVCGCNGVSKGAIVQAIqEKGLtTLDEVKACTKASTSCGGCTPLVEQLL 53
MopB_Phenylacetyl-CoA-OR cd02760
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ...
407-494 2.01e-05

The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.


Pssm-ID: 239161 [Multi-domain]  Cd Length: 760  Bit Score: 48.43  E-value: 2.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 407 TNPAQSLPDQRKIHEALARCPFvVVQEAFAGTETCQYADLLLPAASWGEKEGSVTN-----SERRISH----VRR-AVPP 476
Cdd:cd02760 522 TNPAISFWDTATLVDNIAKFPF-TVSFAYTEDETNWMADVLLPEATDLESLQMIKVggtkfVEQFWEHrgvvLRQpAVEP 600
                        90
                ....*....|....*...
gi 15596976 477 PGEARQDWNIVCDFARRL 494
Cdd:cd02760 601 QGEARDFTWISTELAKRT 618
Fer2_BFD-like cd19942
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ...
851-897 4.05e-05

[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; The BFD-like [2Fe-2S]-binding domain comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. The Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1. This superfamily also includes uncharacterized proteins having an N-terminal BFD-like [2Fe-2S]-binding domain and a C-terminal domain belonging to the Ni,Fe-hydrogenase I small subunit family.


Pssm-ID: 381075 [Multi-domain]  Cd Length: 49  Bit Score: 41.65  E-value: 4.05e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15596976 851 KTLCSCQNVSQQTVLGGIARGLD--LDGLKREFGCGTGCGSCVPEIKRL 897
Cdd:cd19942   1 ALVCECFAVTEKELREAIRKGGLktVEELLTGTGAGGGCGVCHPHVAQL 49
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
833-900 5.79e-05

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 47.04  E-value: 5.79e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596976  833 LLAPLGAAPGRPSQGAGG----KTLCSCQNVSQQTVLGGIARGL-DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:PRK14989 400 LILPAHAGSGKPSIGVDKlpdsAQICSCFDVTKGDLIAAINKGChTVAALKAETKAGTGCGGCIPLVTQVLNA 472
NuoG COG1034
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ...
7-226 6.12e-05

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: 46.37  E-value: 6.12e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976   7 LRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKG--ASLHLTGDlqARALYPQLRLGKQLARArsDWE 84
Cdd:COG1034 215 LKKTPSICPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKGrfGYDGLNSP--DRLTRPLVRKDGELVEA--SWE 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976  85 SALEHAAGrfaetirehgpdsvafyisgqlltedyyAFNKLARAlvgtnnidSNSrlcMSSAVVGYKRSLGADAPPCSYE 164
Cdd:COG1034 291 EALAAAAE----------------------------GLKALKKA--------ENS---VGAALLGALPDAAAILEAAEAG 331
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596976 165 DLdcaDCVLIAGsnmafAHPVLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLhlaLLPGT 226
Cdd:COG1034 332 KL---KALVLLG-----ADPYDLDPAAALAALAKADFVVVLDHFGSATAERADV---VLPAA 382
MopB_CT_DMSOR-like cd02777
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
623-687 3.62e-04

The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239178 [Multi-domain]  Cd Length: 127  Bit Score: 41.42  E-value: 3.62e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596976 623 VHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPmH--WGD-RFLKGL---GC-NVLTLP 687
Cdd:cd02777  36 VWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALP-EgaWYDpDDNGGLdkgGNpNVLTSD 106
MopB_CT_Acetylene-hydratase cd02781
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ...
588-671 8.45e-04

The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239182 [Multi-domain]  Cd Length: 130  Bit Score: 40.37  E-value: 8.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 588 RYPLTLNTGRlRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFL 667
Cdd:cd02781   1 EYPLILTTGA-RSYYYFHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRA 79

                ....
gi 15596976 668 PMHW 671
Cdd:cd02781  80 EHGW 83
MopB_CT_4 cd02785
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ...
620-694 1.13e-03

The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239186 [Multi-domain]  Cd Length: 124  Bit Score: 39.66  E-value: 1.13e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596976 620 EALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPMHWGDRFLKGLGCNVLTLPAFDPLSK 694
Cdd:cd02785  31 EPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQGWWSRYFQEGSLQDLTSPFVNPVHE 105
MopB_CT_FmdC-FwdD cd02789
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ...
593-669 1.34e-03

The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239190 [Multi-domain]  Cd Length: 106  Bit Score: 39.33  E-value: 1.34e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596976 593 LNTGRLRDQwhgmSRTGTCARLFGHE--EEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPM 669
Cdd:cd02789   5 LNSGRTIDQ----GRIIEGGNKLTYEvdACAYCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPM 79
MopB_CT_DMSOR-BSOR-TMAOR cd02793
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ...
623-663 2.58e-03

The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.


Pssm-ID: 239194 [Multi-domain]  Cd Length: 129  Bit Score: 38.77  E-value: 2.58e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 15596976 623 VHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPG 663
Cdd:cd02793  35 IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPG 75
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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