|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
1-829 |
0e+00 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 1923.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 1 MKLSRRDFMKANAVAAAAAVAGVSAPTlAANLITSTDKTAIHWDKAPCRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRG 80
Cdd:PRK13532 1 MKLSRRDFMKANAAAAAAAAAGLSLPA-VANAVVGSAQTAIKWDKAPCRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 81 LNCIKGYFLSKIMYGQDRLTQPMLRMKNGQFDKDGDFAPISWDQAFDIMAEKFKATLKEKGPTAVGMFGSGQWTVWEGYA 160
Cdd:PRK13532 80 LNCIKGYFLSKIMYGKDRLTQPLLRMKDGKYDKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 161 AAKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGSNMAEMHPILWSRMSDRRLSNPDVQ 240
Cdd:PRK13532 160 ASKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRLSNPDVK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 241 VHVLSTFEHRSFELADNGMVFTPQTDLAILNYVANYIIQNDKVNWDFVNKHTVFKKGVTDIGYGLRPTDPLQQKAKNP-D 319
Cdd:PRK13532 240 VAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVNKHTNFRKGATDIGYGLRPTHPLEKAAKNPgT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 320 SGDATPMTFEEFAKFVADYDVESVSKLSGVSKEKLEKLAKLYADPSKKVVSYWTMGFNQHTRGVWANNLCYNIHLLTGKI 399
Cdd:PRK13532 320 AGKSEPISFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAKLYADPNRKVVSFWTMGFNQHTRGVWANNLVYNIHLLTGKI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 400 SEPGNGPFSLTGQPSACGTAREVGTFAHRLPADMVVTEPKHRAIAEQIWKLPEGTIPDKVGFHAVLQDRMLKDGKLNAYW 479
Cdd:PRK13532 400 STPGNGPFSLTGQPSACGTAREVGTFSHRLPADMVVTNPKHREIAEKIWKLPEGTIPPKPGYHAVAQDRMLKDGKLNAYW 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 480 VMCNNNMQAGPNMNTDRLPGYRDPRNFIVVSDPYPTVTAQAADLILPTAMWVEKEGAYGNAERRTQFWHQQVKAPEGAKS 559
Cdd:PRK13532 480 VMCNNNMQAGPNINEERLPGWRNPDNFIVVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKS 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 560 DLWQLMEFSKRFKVEEVWPAELIAKMPEVKGKTLFDVLYANGQVNQFP-KEQSKGMLNDEAEHFGFYVQKGLFEEYATFG 638
Cdd:PRK13532 560 DLWQLVEFSKRFKTEEVWPEELLAKKPEYRGKTLYDVLFANGQVDKFPlSELAEGYLNDEAKHFGFYVQKGLFEEYASFG 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 639 RGHGHDLAPFDQYHEARGLRWPVVDGKETLWRYREGFDPYVKAGEGVRFYGKPDGKAVIFALPFEPAAESPDKEYDLWLS 718
Cdd:PRK13532 640 RGHGHDLAPFDTYHKVRGLRWPVVDGKETLWRYREGYDPYVKAGEGFKFYGKPDGKAVIFALPYEPPAESPDEEYDLWLS 719
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 719 TGRVLEHWHTGTMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPPKGLVFMPFFDA 798
Cdd:PRK13532 720 TGRVLEHWHTGSMTRRVPELYRAFPEAVCFMHPEDAKARGLRRGDEVKVVSRRGEVKSRVETRGRNKPPRGLVFVPFFDA 799
|
810 820 830
....*....|....*....|....*....|.
gi 835291226 799 SQLVNKLTLDATDPLSKETDYKKCAVKVMKA 829
Cdd:PRK13532 800 AQLINKLTLDATDPLSKQTDFKKCAVKIEKV 830
|
|
| NAPA |
TIGR01706 |
periplasmic nitrate reductase, large subunit; This model represents the large subunit of a ... |
2-829 |
0e+00 |
|
periplasmic nitrate reductase, large subunit; This model represents the large subunit of a family of nitrate reductases found in proteobacteria which are localized to the periplasm. This subunit binds molybdopterin and contains a twin-arginine motif at the N-terminus. The protein associates with NapB, a soluble heme-containing protein and NapC, a membrane-bound cytochrome c. The periplasmic nitrate reductases are not involved in the assimilation of nitrogen, and are not directly involved in the formation of electrochemical gradients (i.e. respiration) either. Rather, the purpose of this enzyme is either dissimilatory (i.e. to dispose of excess reductive equivalents) or indirectly respiratory by virtue of the consumption of electrons derived from NADH via the proton translocating NADH dehydrogenase. The enzymes from Alicagenes eutrophus and Paracoccus pantotrophus have been characterized. In E. coli (as well as other organisms) this gene is part of a large nitrate reduction operon (napFDAGHBC). [Energy metabolism, Aerobic, Energy metabolism, Electron transport, Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 273766 [Multi-domain] Cd Length: 830 Bit Score: 1658.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 2 KLSRRDFMKANAVAAAAAVAGVSAPTLAANLITSTDKTAIHWDKAPCRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGL 81
Cdd:TIGR01706 1 KISRRDFIKATAIASAASVAGLSLPAQAANMVGGQEETAIKWDKAPCRFCGTGCGVMVGVKDGRVVATQGDPAAPVNRGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 82 NCIKGYFLSKIMYGQDRLTQPMLRMKNGQFDKDGDFAPISWDQAFDIMAEKFKATLKEKGPTAVGMFGSGQWTVWEGYAA 161
Cdd:TIGR01706 81 NCIKGYFLSKIMYGQDRLTQPLLRMKDGKYDKDGEFTPVSWDQAFDEMEEQFKRALKEKGPTAIGMFGSGQWTIWEGYAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 162 AKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGSNMAEMHPILWSRMSDRRLSNPDVQV 241
Cdd:TIGR01706 161 LKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDFEAADAFVLWGSNMAEMHPILWTRVTDRRLSHPKVKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 242 HVLSTFEHRSFELADNGMVFTPQTDLAILNYVANYIIQNDKVNWDFVNKHTVFKKGVTDIGYGLRPTDPLQQKAKNPDSG 321
Cdd:TIGR01706 241 VVLSTFTHRSFDLADIGIIFKPQTDLAILNYIANYIIQNNAVNMDFVNKHTVFKTGATDIGYGLRPDHPLEKAAKNADDP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 322 DATPM-TFEEFAKFVADYDVESVSKLSGVSKEKLEKLAKLYADPSKKVVSYWTMGFNQHTRGVWANNLCYNIHLLTGKIS 400
Cdd:TIGR01706 321 AATSLsTFEEFKKFVAPYTLEKTSELSGVPKAKLEQLAELYADPNRKVMSLWTMGFNQHTRGVWANNMVYNLHLLTGKIA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 401 EPGNGPFSLTGQPSACGTAREVGTFAHRLPADMVVTEPKHRAIAEQIWKLPEGTIPDKVGFHAVLQDRMLKDGKLNAYWV 480
Cdd:TIGR01706 401 TPGNSPFSLTGQPSACGTAREVGTFSHRLPADMVVTNPKHREIAEKIWKIPAGTIPEKPGLHAVAQDRALKDGKLNFYWV 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 481 MCNNNMQAGPNMNTDRLPGYRDPRNFIVVSDPYPTVTAQAADLILPTAMWVEKEGAYGNAERRTQFWHQQVKAPEGAKSD 560
Cdd:TIGR01706 481 QVNNNMQAGPNINEERLPGYRNPDNFIVVSDAYPTVTALAADLILPSAMWVEKEGAYGNAERRTQVWHQQVLAPGEARSD 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 561 LWQLMEFSKRFKVEEVWPAELIAKMPEVKGKTLFDVLYANGQVNQFP-KEQSKGMLNDEAEHFGFYVQKGLFEEYATFGR 639
Cdd:TIGR01706 561 LWQLVEFSKRFKTEEVWPEELLAKKPEYRGKTLYDVLFANGEVDKFPlSEANAKSLNAESTAFGFYVQKGLFEEYAKFGR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 640 GHGHDLAPFDQYHEARGLRWPVVDGKETLWRYREGFDPYVKAGEGVRFYGKPDGKAVIFALPFEPAAESPDKEYDLWLST 719
Cdd:TIGR01706 641 GHGHDLAPFDTYHKVRGLRWPVVNGKETQWRYREGSDPYVKAGAGFQFYGNPDGKAVIFALPYEPPAERPDEEYPLWLVT 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 720 GRVLEHWHTGTMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPPKGLVFMPFFDAS 799
Cdd:TIGR01706 721 GRVLEHWHSGSMTRRVPELYRAFPEALCFMHPEDAKALGLRRGDEVWVVSRRGEVRSRVETRGRNKPPRGLVFVPWFDAS 800
|
810 820 830
....*....|....*....|....*....|
gi 835291226 800 QLVNKLTLDATDPLSKETDYKKCAVKVMKA 829
Cdd:TIGR01706 801 QLINKVTLDATDPLSKQTDFKKCAVKIYKV 830
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
45-705 |
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: 801.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 45 KAPCRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRMKngqfdkDGDFAPISWDQ 124
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRN------GGELVPVSWDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 125 AFDIMAEKFKATLKEKGPTAVGMFGSGQWTVWEGYAAAKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDD 204
Cdd:cd02754 75 ALDLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGADGPPGSYDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 205 IEQADAFVLWGSNMAEMHPILWSRMSDRRLSNPDVQVHVLSTFEHRSFELADNGMVFTPQTDLAILNYVANYIIQNDKVN 284
Cdd:cd02754 155 IEHADCFFLIGSNMAECHPILFRRLLDRKKANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLID 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 285 WDFVNKHTVFkkgvtdigyglrptdplqqkaknpdsgdatpmtFEEFAKFVADYDVESVSKLSGVSKEKLEKLAKLYADp 364
Cdd:cd02754 235 RDFIDAHTEG---------------------------------FEELKAFVADYTPEKVAEITGVPEADIREAARLFGE- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 365 SKKVVSYWTMGFNQHTRGVWANNLCYNIHLLTGKISEPGNGPFSLTGQPSAcGTAREVGTFAHRLPADMVVTEPKHRAIA 444
Cdd:cd02754 281 ARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNA-MGGREVGGLANLLPGHRSVNNPEHRAEV 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 445 EQIWKLPEGTIPDKVGFHAVLQDRMLKDGKLNAYWVMCNNNMQAGPNMNTDRLpgYRDPRNFIVVSDPYP-TVTAQAADL 523
Cdd:cd02754 360 AKFWGVPEGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVRE--ALERLEFVVVQDAFAdTETAEYADL 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 524 ILPTAMWVEKEGAYGNAERRTQFWHQQVKAPEGAKSDLWQLMEFSKRFKVEEVwpaeliakmpevkgktlfdvlyangqv 603
Cdd:cd02754 438 VLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILADVARRLGFGEL--------------------------- 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 604 nqfpkeqskgmlndeaehFGFYVQKGLFEEYATFGRGHGHDLAPFDqYHEAR--GLRWPVVDG-KETLWRYREGFdpyvk 680
Cdd:cd02754 491 ------------------FPYTSPEEVFEEYRRLSRGRGADLSGLS-YERLRdgGVQWPCPDGpPEGTRRLFEDG----- 546
|
650 660
....*....|....*....|....*
gi 835291226 681 agegvrFYGKPDGKAVIFALPFEPA 705
Cdd:cd02754 547 ------RFPTPDGRARFVAVPYRPP 565
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
40-829 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 646.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 40 AIHWDKAPCRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRmkngqfdKDGDFAP 119
Cdd:COG3383 3 PMKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIR-------RGGEFRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 120 ISWDQAFDIMAEKFKATLKEKGPTAVGMFGSGQWTVWEGYAAAKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPM 199
Cdd:COG3383 76 VSWDEALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 200 GCYDDIEQADAFVLWGSNMAEMHPILWSRMSDRRlsNPDVQVHVLSTFEHRSFELADNGMVFTPQTDLAILNYVANYIIQ 279
Cdd:COG3383 156 NSYDDIEEADVILVIGSNPAEAHPVLARRIKKAK--KNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 280 NDKVNWDFVNKHTvfkkgvtdigyglrptdplqqkaknpdSGdatpmtFEEFAKFVADYDVESVSKLSGVSKEKLEKLAK 359
Cdd:COG3383 234 EGLVDEDFIAERT---------------------------EG------FEELKASVAKYTPERVAEITGVPAEDIREAAR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 360 LYADpSKKVVSYWTMGFNQHTRGVWANNLCYNIHLLTGKISEPGNGPFSLTGQPSACGtAREVGTFAHRLPADMVVTEPK 439
Cdd:COG3383 281 LIAE-AKRAMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQG-GRDMGALPNVLPGYRDVTDPE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 440 HRAIAEQIWKLPEgtIPDKVGFHAVLQDRMLKDGKLNAYWVMCNNNMQAGPNMNT-----DRLPgyrdprnFIVVSDPYP 514
Cdd:COG3383 359 HRAKVADAWGVPP--LPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDANHvrealEKLE-------FLVVQDIFL 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 515 TVTAQAADLILPTAMWVEKEGAYGNAERRTQFWHQQVKAPEGAKSDLWQLMEFSKRF-------KVEEVWpAELIAKMPE 587
Cdd:COG3383 430 TETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARRLgygfdydSPEEVF-DEIARLTPD 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 588 VKGKTlfdvlyangqvnqfpkeqskgmlndeaehfgfyvqkglfeeyatfgrghghdlapFDQYHEARGLRWPV--VDGK 665
Cdd:COG3383 509 YSGIS-------------------------------------------------------YERLEALGGVQWPCpsEDHP 533
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 666 ETLWRYREGFDPyvkagegvrfygkPDGKAVIFALPFEPAAESPDKEYDLWLSTGRVLEHWHTGTMTRRVPELYRAFPDA 745
Cdd:COG3383 534 GTPRLFTGRFPT-------------PDGKARFVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEP 600
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 746 VLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVetRGRNRPPKGLVFMPFFDASQLVNKLTLDATDPLSKETDYKKCAVK 825
Cdd:COG3383 601 FVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRA--RVTDRVRPGTVFMPFHWGEGAANALTNDALDPVSKQPEYKACAVR 678
|
....
gi 835291226 826 VMKA 829
Cdd:COG3383 679 VEKV 682
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
29-829 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 608.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 29 AANLITSTDKTAIHWDKAPCRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRMKN 108
Cdd:COG0243 9 AGAGAAALEAAGTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 109 gqfDKDGDFAPISWDQAFDIMAEKFKATLKEKGPTAVGMFGSG----QWTVWEGYAAAKLMKAgFRSNNIDPNARHCMAS 184
Cdd:COG0243 89 ---RGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGgsagRLSNEAAYLAQRFARA-LGTNNLDDNSRLCHES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 185 AVVGFMRTFGMDEPMGCYDDIEQADAFVLWGSNMAEMHPILWSRMSDRRlSNPDVQVHVLSTFEHRSFELADNGMVFTPQ 264
Cdd:COG0243 165 AVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAA-KKRGAKIVVIDPRRTETAAIADEWLPIRPG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 265 TDLAILNYVANYIIQNDKVNWDFVNKHTVfkkGvtdigyglrptdplqqkaknpdsgdatpmtFEEFAKFVADYDVESVS 344
Cdd:COG0243 244 TDAALLLALAHVLIEEGLYDRDFLARHTV---G------------------------------FDELAAYVAAYTPEWAA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 345 KLSGVSKEKLEKLAKLYAdPSKKVVSYWTMGFNQHTRGVWANNLCYNIHLLTGKISEPGNGPFSLTGqpsacgtarevgt 424
Cdd:COG0243 291 EITGVPAEDIRELAREFA-TAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 425 fahrlpadmvvtepkhRAIAEQiwklpegtipdkvgfhavlqdrmlKDGKLNAYWVMCNNNMQAGPNMN-TDRlpGYRDP 503
Cdd:COG0243 357 ----------------EAILDG------------------------KPYPIKALWVYGGNPAVSAPDTNrVRE--ALRKL 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 504 rNFIVVSDPYPTVTAQAADLILPTAMWVEKEGAYGNAE-RRTQFWHQQVKAPEGAKSDLWQLMEFSKRFKVEEVWPAEli 582
Cdd:COG0243 395 -DFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWG-- 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 583 akmpevkgktlfdvlyangqvnqfpkeqskgmlNDEAEhfgfyvqkgLFEEYATFGRGHGhdlAPFDQYHEARGLRWPVV 662
Cdd:COG0243 472 ---------------------------------RTEED---------YLRELLEATRGRG---ITFEELREKGPVQLPVP 506
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 663 DgkETLWRYREGFdpyvkagegvrfyGKPDGKAVIF--ALPFEP---------AAESPDKEYDLWLSTGRVLEHWHtgTM 731
Cdd:COG0243 507 P--EPAFRNDGPF-------------PTPSGKAEFYseTLALPPlpryappyeGAEPLDAEYPLRLITGRSRDQWH--ST 569
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 732 TRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPpkGLVFMPFF-------DASQLVNK 804
Cdd:COG0243 570 TYNNPRLREIGPRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRP--GVVFAPHGwwyepadDKGGNVNV 647
|
810 820
....*....|....*....|....*
gi 835291226 805 LTLDATDPLSKETDYKKCAVKVMKA 829
Cdd:COG0243 648 LTPDATDPLSGTPAFKSVPVRVEKA 672
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
48-826 |
1.06e-137 |
|
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: 423.80 E-value: 1.06e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRMKngqfdkdGDFAPISWDQAFD 127
Cdd:TIGR01591 3 CPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREG-------DKFREVSWDEAIS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 128 IMAEKFKATLKEKGPTAVGMFGSGQWTVWEGYAAAKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQ 207
Cdd:TIGR01591 76 YIAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEIEN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 208 ADAFVLWGSNMAEMHPILWSRMSdRRLSNpDVQVHVLSTFEHRSFELADNGMVFTPQTDLAILNYVANYIIQNDKVNWDF 287
Cdd:TIGR01591 156 ADLIVIIGYNPAESHPVVAQYLK-NAKRN-GAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 288 VNKHTVfkkgvtdigyglrptdplqqkaknpdsgdatpmTFEEFAKFVADYDVESVSKLSGVSKEKLEKLAKLYADpSKK 367
Cdd:TIGR01591 234 IEKRTE---------------------------------GFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAK-AGS 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 368 VVSYWTMGFNQHTRGVWANNLCYNIHLLTGKISEPGNGPFSLTGQPSACGTArEVGTFAHRLPADMVVTEPKHRAIAEQI 447
Cdd:TIGR01591 280 AAILWGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGAC-DMGALPDFLPGYQPVSDEEVREKFAKA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 448 W---KLPEGT---IPDKvgFHAVLqdrmlkDGKLNAYWVMCNNNMQAGPnmNTDRLPGYRDPRNFIVVSDPYPTVTAQAA 521
Cdd:TIGR01591 359 WgvvKLPAEPglrIPEM--IDAAA------DGDVKALYIMGEDPLQSDP--NTSKVRKALEKLELLVVQDIFMTETAKYA 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 522 DLILPTAMWVEKEGAYGNAERRTQFWHQQVKAPEGAKSDLWQLMEFSKRfkveevwpaeliakmpevkgktlfdvLYANG 601
Cdd:TIGR01591 429 DVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQELANA--------------------------LGLDW 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 602 QVNQfPKEqskgmLNDEAEHfgfyvqkgLFEEYATfgrghghdlAPFDQYHEARGLRWPVV--DGKETLWRYREGFDpyv 679
Cdd:TIGR01591 483 NYNH-PQE-----IMDEIRE--------LTPLFAG---------LTYERLDELGSLQWPCNdsDASPTSYLYKDKFA--- 536
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 680 kagegvrfygKPDGKAVIFALPFEPAAESPDKEYDLWLSTGRVLEHWHTGTMTRRVPELYRAFPDAVLFMHPDDAKARGV 759
Cdd:TIGR01591 537 ----------TPDGKAKFIPLEWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGI 606
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835291226 760 RRGEEVIVSSRRGEVKTRveTRGRNRPPKGLVFMPFFDASQLVNKLTLDATDPLSKETDYKKCAVKV 826
Cdd:TIGR01591 607 KDGDLVKVKSRRGEITLR--AKVSDRVNKGAIYITMHFWDGAVNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
48-631 |
8.77e-96 |
|
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: 308.76 E-value: 8.77e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRmkngqfdKDGDFAPISWDQAFD 127
Cdd:cd02753 4 CPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIR-------KNGKFVEASWDEALS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 128 IMAEKFKATLKEKGPTAVGMFGSGQWTVWEGYAAAKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQ 207
Cdd:cd02753 77 LVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAMTNSIADIEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 208 ADAFVLWGSNMAEMHPILWSRMSDRRLSnpDVQVHVLSTFEHRSFELADNGMVFTPQTDLAILNYVANYIIQNDKVNWDF 287
Cdd:cd02753 157 ADVILVIGSNTTEAHPVIARRIKRAKRN--GAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 288 VNKHTvfkKGvtdigyglrptdplqqkaknpdsgdatpmtFEEFAKFVADYDVESVSKLSGVSKEKLEKLAKLYADpSKK 367
Cdd:cd02753 235 IEERT---EG------------------------------FEELKEIVEKYTPEYAERITGVPAEDIREAARMYAT-AKS 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 368 VVSYWTMGFNQHTRGVwANNLCY-NIHLLTGKISEPGNGPFSLTGQPSACGtAREVGTFAHRLPadmvvtepkhraiaeq 446
Cdd:cd02753 281 AAILWGMGVTQHSHGT-DNVMALsNLALLTGNIGRPGTGVNPLRGQNNVQG-ACDMGALPNVLP---------------- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 447 iwklpegtipdkvgfhavlqdrmlkdGKLNAYWVMCNNNMQAGPNMNTDRlpgyRDPRN--FIVVSDPYPTVTAQAADLI 524
Cdd:cd02753 343 --------------------------GYVKALYIMGENPALSDPNTNHVR----KALESleFLVVQDIFLTETAELADVV 392
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 525 LPTAMWVEKEGAYGNAERRTQFWHQQVKAPEGAKSDLWQLMEFSKR-------FKVEEVWpAELIAKMPEVKGKTlFDVL 597
Cdd:cd02753 393 LPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRlgypgfySHPEEIF-DEIARLTPQYAGIS-YERL 470
|
570 580 590
....*....|....*....|....*....|....*.
gi 835291226 598 YANGQVnQFPK--EQSKGMLNDEAEHFGFYVQKGLF 631
Cdd:cd02753 471 ERPGGL-QWPCpdEDHPGTPILHTERFATPDGKARF 505
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
48-571 |
3.54e-93 |
|
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: 297.32 E-value: 3.54e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRMkngqfDKDGDFAPISWDQAFD 127
Cdd:cd00368 4 CPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRV-----GGRGKFVPISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 128 IMAEKFKATLKEKGPTAVGMFGSGQWTVWEGYAAAKLMkAGFRSNNIDPNARHCMASAVVGfMRTFGMDEPMGCYDDIEQ 207
Cdd:cd00368 79 EIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL-RALGSNNVDSHARLCHASAVAA-LKAFGGGAPTNTLADIEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 208 ADAFVLWGSNMAEMHPILWSRMSDRRLsnPDVQVHVLSTFEHRSFELADNGMVFTPQTDLAILNyvanyiiqndkvnwdf 287
Cdd:cd00368 157 ADLILLWGSNPAETHPVLAARLRRAKK--RGAKLIVIDPRRTETAAKADEWLPIRPGTDAALAL---------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 288 vnkhtvfkkgvtdigyglrptdplqqkaknpdsgdatpmtfeefakfvadydVESVSKLSGVSKEKLEKLAKLYADpSKK 367
Cdd:cd00368 219 ----------------------------------------------------AEWAAEITGVPAETIRALAREFAA-AKR 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 368 VVSYWTMGFNQHTRGVWANNLCYNIHLLTGKISEPGNGPFSltgqpsacgtarevgtfahrlpadmvvtepkhraiaeqi 447
Cdd:cd00368 246 AVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP--------------------------------------- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 448 wklpegtipdkvgfhavlqdrmlkdgklnaywvmCNNNMQAGPNMNTDRLPGYRDPrnFIVVSDPYPTVTAQAADLILPT 527
Cdd:cd00368 287 ----------------------------------GGNPLVSAPDANRVRAALKKLD--FVVVIDIFMTETAAYADVVLPA 330
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 835291226 528 AMWVEKEGAYGNAERRTQFWHQQVKAPEGAKSDLWQLMEFSKRF 571
Cdd:cd00368 331 ATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
98-570 |
8.42e-70 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 234.60 E-value: 8.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 98 RLTQPMLRmkngqfDKDGDFAPISWDQAFDIMAEKFKATLKEKGPTAVGM-FGSGQWT-VWEGYAAAKLMKAGFRSN--N 173
Cdd:pfam00384 1 RLKYPMVR------RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAInGGSGGLTdVESLYALKKLLNRLGSKNgnT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 174 IDPNARHCMASAVvgfmrTFGMDEPMG-----CYDDIEQADAFVLWGSNMAEMHPILWSRmSDRRLSNPDVQVHVLSTFE 248
Cdd:pfam00384 75 EDHNGDLCTAAAA-----AFGSDLRSNylfnsSIADIENADLILLIGTNPREEAPILNAR-IRKAALKGKAKVIVIGPRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 249 HRSFELADNGmvFTPQTDLAILNYVANYIIQNDKVNWDFVNKhtvfkkgvtdigyglrptdplqqkaknpdsgdatPMTF 328
Cdd:pfam00384 149 DLTYADEHLG--IKPGTDLALALAGAHVFIKELKKDKDFAPK----------------------------------PIII 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 329 eefakfvadydvesvsklsgvskekleklaklyadpskkvvsyWTMGFNQHTRGVWANNLCYNIHLLTGKISEPGNGPFS 408
Cdd:pfam00384 193 -------------------------------------------VGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNG 229
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 409 LTgqpSACGTAREVGTFahrlpadmvvtepkhraiaeqiwklpegTIPDKVGFHAVLQDRMLKDGKLNAYWVMCNNNMQA 488
Cdd:pfam00384 230 LN---ILQGAASPVGAL----------------------------DLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVT 278
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 489 GPnmNTDRLPGYRDPRNFIVVSDPYP-TVTAQAADLILPTAMWVEKEGAYGNAERRTQFWHQQVKAPEGAKSDLWQLMEF 567
Cdd:pfam00384 279 HA--DENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRAL 356
|
...
gi 835291226 568 SKR 570
Cdd:pfam00384 357 SEV 359
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
712-829 |
3.33e-53 |
|
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: 180.46 E-value: 3.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 712 EYDLWLSTGRVLEHWHTGTMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPpkGLV 791
Cdd:cd02791 2 EYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRP--GEV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 835291226 792 FMPFFDA-----SQLVNKLTLDATDPLSKETDYKKCAVKVMKA 829
Cdd:cd02791 80 FVPMHWGdqfgrSGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
711-828 |
5.68e-50 |
|
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: 171.15 E-value: 5.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 711 KEYDLWLSTGRVLEHWHTGTMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPpkGL 790
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRP--GT 78
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 835291226 791 VFMPFFDA----SQLVNKLTLDATDPLSKETDYKKCAVKVMK 828
Cdd:cd00508 79 VFMPFHWGgevsGGAANALTNDALDPVSGQPEFKACAVRIEK 120
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
48-572 |
1.10e-47 |
|
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: 180.29 E-value: 1.10e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRmKNGQfdkdGDFAPISWDQAFD 127
Cdd:cd02752 4 CPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYR-APGS----GKWEEISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 128 IMAEKFK----ATLKEK--------GPTAVGMFGSGQWTVWEGYAAAKLMKAgFRSNNIDPNARHCMASAVVGFMRTFGM 195
Cdd:cd02752 79 EIARKMKdirdASFVEKnaagvvvnRPDSIAFLGSAKLSNEECYLIRKFARA-LGTNNLDHQARIUHSPTVAGLANTFGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 196 DEPMGCYDDIEQADAFVLWGSNMAEMHPILWSRMSDRRLSNPDVQVHVLSTFEhRSFELADNGMVFTPQTDLAILNYVAN 275
Cdd:cd02752 158 GAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVVDPRFT-RTAAKADLYVPIRSGTDIAFLGGMIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 276 YIIQndkvnwdfvnkhtvfkkgvtdigyglrptdplqqkaknpdsgdatpmtfeefakfvadYDVESVSKLSGVSKEKLE 355
Cdd:cd02752 237 YIIR----------------------------------------------------------YTPEEVEDICGVPKEDFL 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 356 KLAKLYA---DPSKKVVSYWTMGFNQHTRGVwANNLCYNI-HLLTGKISEPGNGPFSLTGQPSACGtAREVGTFAHRLPa 431
Cdd:cd02752 259 KVAEMFAatgRPDKPGTILYAMGWTQHTVGS-QNIRAMCIlQLLLGNIGVAGGGVNALRGHSNVQG-ATDLGLLSHNLP- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 432 dmvvtepkhraiaeqiwklpegtipdkvgfhavlqdrmlkdgklnAYWVMCN-NNMQAGPNMNTDRLpgyrDPRNFIVVS 510
Cdd:cd02752 336 ---------------------------------------------GYLGGQNpNSSFPNANKVRRAL----DKLDWLVVI 366
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835291226 511 DPYPTVTAQAAD-------------LILPTAMWVEKEGAYGNAERRTQFWHQQVKAPEGAKSDLWQLMEFSKRFK 572
Cdd:cd02752 367 DPFPTETAAFWKnpgmdpksiqtevFLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLG 441
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
55-575 |
1.64e-44 |
|
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: 168.20 E-value: 1.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 55 CSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRmkngQFDKDGDFAPISWDQAFDIMAEKFK 134
Cdd:cd02766 12 CSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKR----VGRKGGQWERISWDEALDTIAAKLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 135 ATLKEKGPTAVGM-FGSGQWTVWEGYAAAKLMKAGfRSNNID--PNARHCMASAVVGFMRTFGMDEpmgcyDDIEQADAF 211
Cdd:cd02766 88 EIKAEYGPESILPySYAGTMGLLQRAARGRFFHAL-GASELRgtICSGAGIEAQKYDFGASLGNDP-----EDMVNADLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 212 VLWGSNMAEMHPILWSRMSDRRlsNPDVQVHVLSTFEHRSFELADNGMVFTPQTDLAILNYVANYIIQNDKVNWDFVNKH 291
Cdd:cd02766 162 VIWGINPAATNIHLMRIIQEAR--KRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRDFLARH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 292 TVFkkgvtdigyglrptdplqqkaknpdsgdatpmtFEEFAKFVADYDVESVSKLSGVSKEKLEKLAKLYADpSKKVVSY 371
Cdd:cd02766 240 TEG---------------------------------FEELKAHLETYTPEWAAEITGVSAEEIEELARLYGE-AKPPSIR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 372 WTMGFNQHTRGvwANNL----CynIHLLTGKISEPGNGPFSLTGQPsacgtarevgtfahrlPADMVvtepkhraiaeqi 447
Cdd:cd02766 286 LGYGMQRYRNG--GQNVraidA--LPALTGNIGVPGGGAFYSNSGP----------------PVKAL------------- 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 448 wklpegtipdkvgfhavlqdrmlkdgklnayWVMCNNNMQAGPNMNTDRlPGYRDPRNFIVVSDPYPTVTAQAADLILPT 527
Cdd:cd02766 333 -------------------------------WVYNSNPVAQAPDSNKVR-KGLAREDLFVVVHDQFMTDTARYADIVLPA 380
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 835291226 528 AMWVEKEGAYGNaerrtqFWH------QQVKAPEG-AKSDLWQLMEFSKRFKVEE 575
Cdd:cd02766 381 TTFLEHEDVYAS------YWHyylqynEPAIPPPGeARSNTEIFRELAKRLGFGE 429
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
48-575 |
1.46e-41 |
|
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: 159.01 E-value: 1.46e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRM-KNGqfdkDGDFAPISWDQAF 126
Cdd:cd02759 4 CPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgERG----ENKWERISWDEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 127 DIMAEKFKATLKEKGPTAVGM-FGSGQWTVWEGYAAAKLMKAGFRSNNIDPNARHC-----MASA-VVGFMRtfGMDEPm 199
Cdd:cd02759 80 DEIAEKLAEIKAEYGPESIATaVGTGRGTMWQDSLFWIRFVRLFGSPNLFLSGESCywprdMAHAlTTGFGL--GYDEP- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 200 gcydDIEQADAFVLWGSNMAEmhpilwsrmsdrrlSNPDVQVHVLSTFEHRSFEL-------------ADNGMVFTPQTD 266
Cdd:cd02759 157 ----DWENPECIVLWGKNPLN--------------SNLDLQGHWLVAAMKRGAKLivvdprltwlaarADLWLPIRPGTD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 267 LAILNYVANYIIQNDKVNWDFVNKHTvfkkgvtdigYGlrptdplqqkaknpdsgdatpmtFEEFAKFVADYDVESVSKL 346
Cdd:cd02759 219 AALALGMLNVIINEGLYDKDFVENWC----------YG-----------------------FEELAERVQEYTPEKVAEI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 347 SGVSKEKLEKLAKLYADpSKKVVSYWTMGFNQHTRGVWANNLCYNIHLLTGKISEPGngpfsltgqpsacgtarevgtfa 426
Cdd:cd02759 266 TGVPAEKIRKAARLYAT-AKPACIQWGLAIDQQKNGTQTSRAIAILRAITGNLDVPG----------------------- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 427 hrlpadmvvtepkhraiaEQIWklpegtIPDKVgfhavlqdRMLkdgklnayWVMCNN--NMQAGPNmntdrlPGYRDPR 504
Cdd:cd02759 322 ------------------GNLL------IPYPV--------KML--------IVFGTNplASYADTA------PVLEALK 355
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835291226 505 N--FIVVSDPYPTVTAQAADLILPTAMWVEKEGAYGNAERRTQFW-HQQVKAPEG-AKSDLWQLMEFSKRFKVEE 575
Cdd:cd02759 356 AldFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAENFVQlRQKAVEPYGeAKSDYEIVLELGKRLGPEE 430
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
711-828 |
3.02e-39 |
|
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: 140.84 E-value: 3.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 711 KEYDLWLSTGRVLEHWHTGTMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVetRGRNRPPKGL 790
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRA--RVTDRVPEGV 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 835291226 791 VFMPFFDASQLVNKLTLDATDPLSKETDYKKCAVKVMK 828
Cdd:cd02790 79 VFMPFHFAEAAANLLTNAALDPVAKIPEFKVCAVRVEK 116
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
48-585 |
1.80e-38 |
|
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: 151.01 E-value: 1.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRmkngqfdKDGDFAPISWDQAFD 127
Cdd:cd02762 4 CILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRR-------RGGSFEEIDWDEAFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 128 IMAEKFKATLKEKGPTAVGMFGSG------QWTVWEGYAAAKLMKAGFRSNN-IDPNARHcmasAVVGFMRTFGMDEPMG 200
Cdd:cd02762 77 EIAERLRAIRARHGGDAVGVYGGNpqahthAGGAYSPALLKALGTSNYFSAAtADQKPGH----FWSGLMFGHPGLHPVP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 201 cydDIEQADAFVLWGSNMAEMHPILWSrMSDRRLSNPDVQ-----VHVLSTFEHRSFELADNGMVFTPQTDLAILNYVAn 275
Cdd:cd02762 153 ---DIDRTDYLLILGANPLQSNGSLRT-APDRVLRLKAAKdrggsLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAML- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 276 yiiqndkvnwdfvnkHTVFKKGVTDIGyGLRPTdplqqkaknpDSGdatpmtFEEFAKFVADYDVESVSKLSGVSKEKLE 355
Cdd:cd02762 228 ---------------AVLLAEGLTDRR-FLAEH----------CDG------LDEVRAALAEFTPEAYAPRCGVPAETIR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 356 KLAKLYAdPSKKVVSYWTMGFNQHTRGV---WANNLcynIHLLTGKISEPGngpfsltgqpsacgtarevGTFAHRLPAD 432
Cdd:cd02762 276 RLAREFA-AAPSAAVYGRLGVQTQLFGTlcsWLVKL---LNLLTGNLDRPG-------------------GAMFTTPALD 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 433 mVVTEPKHRAIAEQIWKLPEGTIPDKVGFH--AVLQDRMLKDG--KLNAYWVMCNNNMQAGPnmNTDRLPGYRDPRNFIV 508
Cdd:cd02762 333 -LVGQTSGRTIGRGEWRSRVSGLPEIAGELpvNVLAEEILTDGpgRIRAMIVVAGNPVLSAP--DGARLEAALGGLEFMV 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 509 VSDPYPTVTAQAADLILPTAMWVEKEGA-YGNAE---RRTQFWHQQVKAPEGAKSDlWqlmefskrfkveEVWpAELIAK 584
Cdd:cd02762 410 SVDVYMTETTRHADYILPPASQLEKPHAtFFNLEfprNAFRYRRPLFPPPPGTLPE-W------------EIL-ARLVEA 475
|
.
gi 835291226 585 M 585
Cdd:cd02762 476 L 476
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
48-570 |
9.39e-36 |
|
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: 141.28 E-value: 9.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRMknGQfDKDGDFAPISWDQAFD 127
Cdd:cd02755 5 CEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRV--GE-RGEGKFREASWDEALQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 128 IMAEKFKATLKEKGPTAVGMFGSGQWTVWEgyaaAKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGcYDDIEQ 207
Cdd:cd02755 82 YIASKLKEIKEQHGPESVLFGGHGGCYSPF----FKHFAAAFGSPNIFSHESTCLASKNLAWKLVIDSFGGEV-NPDFEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 208 ADAFVLWGSNMAE------MHPILWSRMSDRRLSNPDVQVHVLSTFehrsfelADNGMVFTPQTDLAILNYVANYIIQND 281
Cdd:cd02755 157 ARYIILFGRNLAEaiivvdARRLMKALENGAKVVVVDPRFSELASK-------ADEWIPIKPGTDLAFVLALIHVLISEN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 282 KVNWDFVNKHTvfkkgvtdigYGlrptdplqqkaknpdsgdatpmtFEEFAKFVADYDVESVSKLSGVSKEKLEKLAKLY 361
Cdd:cd02755 230 LYDAAFVEKYT----------NG-----------------------FELLKAHVKPYTPEWAAQITDIPADTIRRIAREF 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 362 ADPSKKVVSY--WTMGFNQHTRGVWANNLCYNIhlLTGKISEPGNGPFSLTGQPsacgtarevgtfahrlpadmvvtepk 439
Cdd:cd02755 277 AAAAPHAVVDpgWRGTFYSNSFQTRRAIAIINA--LLGNIDKRGGLYYAGSAKP-------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 440 hraiaeqiwklpegtipdkvgfhavlqdrmlkdGKLNAYWVMCNNNMQAGPnmNTDRLPGYRDPRNFIVVSDPYPTVTAQ 519
Cdd:cd02755 329 ---------------------------------YPIKALFIYRTNPFHSMP--DRARLIKALKNLDLVVAIDILPSDTAL 373
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 835291226 520 AADLILPTAMWVEKEGAYGNAERRTQFWHQQVKAPE---GAKSDLWQLMEFSKR 570
Cdd:cd02755 374 YADVILPEATYLERDEPFSDKGGPAPAVATRQRAIEplyDTRPGWDILKELARR 427
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
85-490 |
6.85e-33 |
|
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: 134.74 E-value: 6.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 85 KGYFLSKimygQDRLTQPMLRmkngqfDKDGD-FAPISWDQAFDIMAEKFKATLkekgPTAVGMFGSGQWTVWEGYAAAK 163
Cdd:cd02767 55 SDYELEH----LGRLTYPMRY------DAGSDhYRPISWDEAFAEIAARLRALD----PDRAAFYTSGRASNEAAYLYQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 164 LMKAgFRSNNIDPNARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGSNMAEMHPILWSRM---SDR-------- 232
Cdd:cd02767 121 FARA-YGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYLreaKKRggkiivin 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 233 --------RLSNPDVQVHVLStfehRSFELADngMVFTPQT--DLAILNYVANYIIQNDK-----VNWDFVNKHTvfkkg 297
Cdd:cd02767 200 plrepgleRFANPQNPESMLT----GGTKIAD--EYFQVRIggDIALLNGMAKHLIERDDepgnvLDHDFIAEHT----- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 298 vtdigyglrptdplqqkaknpdSGdatpmtFEEFAKFVADYDVESVSKLSGVSKEKLEKLAKLYADpSKKVVSYWTMGFN 377
Cdd:cd02767 269 ----------------------SG------FEEYVAALRALSWDEIERASGLSREEIEAFAAMYAK-SERVVFVWGMGIT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 378 QHTRGVwannlcYNIH------LLTGKISEPGNGPFSLTGQPSACGtAREVGtfahrlpadmvVTEPKHRAIAEQIWKLP 451
Cdd:cd02767 320 QHAHGV------DNVRaivnlaLLRGNIGRPGAGLMPIRGHSNVQG-DRTMG-----------ITEKPFPEFLDALEEVF 381
|
410 420 430
....*....|....*....|....*....|....*....
gi 835291226 452 EGTIPDKVGFHAVLQDRMLKDGKLNAYWVMCNNNMQAGP 490
Cdd:cd02767 382 GFTPPRDPGLDTVEAIEAALEGKVKAFISLGGNFAEAMP 420
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
715-823 |
1.19e-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: 119.30 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 715 LWLSTGRVLEHWHTGTMTRRVPELYRAFPDAVLfMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPpkGLVFMP 794
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEVVE-IHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRP--GVVFMP 77
|
90 100 110
....*....|....*....|....*....|...
gi 835291226 795 F----FDASQLVNKLTLDATDPLSKETDYKKCA 823
Cdd:pfam01568 78 FgwwyEPRGGNANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
51-575 |
1.25e-31 |
|
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: 131.20 E-value: 1.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 51 CGTGCSVLVGSQDGRVVATQGDPDAPVNrglNCIKGYFLSKIMYGQDRLTQPMLR-------MKNGQFDKDGDFAPISWD 123
Cdd:cd02751 3 ACHWGPFKAHVKDGVIVRVEPDDTDQPR---PCPRGRSVRDRVYSPDRIKYPMKRvgwlgngPGSRELRGEGEFVRISWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 124 QAFDIMAEKFKATLKEKGPTAVgMFGSGQWTVWEGY-AAAKLMK-----AGFRSNNIDPnarHCMASAVVGFMRTFGMDE 197
Cdd:cd02751 80 EALDLVASELKRIREKYGNEAI-FGGSYGWASAGRLhHAQSLLHrflnlIGGYLGSYGT---YSTGAAQVILPHVVGSDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 198 PMGCY---DDI-EQADAFVLWGSNMAEMHPILWsrMSDRRLSNPDVQ------VHVLSTFEHRS---FELADNGMVFTPQ 264
Cdd:cd02751 156 VYEQGtswDDIaEHSDLVVLFGANPLKTRQGGG--GGPDHGSYYYLKqakdagVRFICIDPRYTdtaAVLAAEWIPIRPG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 265 TDLAILNYVANYIIQNDKVNWDFVNKHTV-FKKgvtDIGYGLRPTDplqQKAKNPdsgdatpmtfeEFAkfvadydvesv 343
Cdd:cd02751 234 TDVALMLAMAHTLITEDLHDQAFLARYTVgFDE---FKDYLLGESD---GVPKTP-----------EWA----------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 344 SKLSGVSKEKLEKLAKLYADPSKKVVSYWtmGFNQHTRG---VWAnnlCYNIHLLTGKISEPGNGpFSLTGQPSACGTAR 420
Cdd:cd02751 286 AEITGVPAETIRALAREIASKRTMIAQGW--GLQRAHHGeqpAWM---LVTLAAMLGQIGLPGGG-FGFGYGYSNGGGPP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 421 EVGTFAHRLPADmvvtepkHRAIAEQIwklPEGTIPDkvgfhAVLQD--RMLKDGKLN-------AYWVMCNN--NMQAG 489
Cdd:cd02751 360 RGGAGGPGLPQG-------KNPVKDSI---PVARIAD-----ALLNPgkEFTANGKLKtypdikmIYWAGGNPlhHHQDL 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 490 PNMntdrLPGYRDPRnFIVVSDPYPTVTAQAADLILPTAMWVEKE--GAYGNAERRTQFWHQQVKAPEG-AKSDLWQLME 566
Cdd:cd02751 425 NRL----IKALRKDE-TIVVHDIFWTASARYADIVLPATTSLERNdiGLTGNYSNRYLIAMKQAVEPLGeARSDYEIFAE 499
|
....*....
gi 835291226 567 FSKRFKVEE 575
Cdd:cd02751 500 LAKRLGVEE 508
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
43-403 |
2.36e-30 |
|
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: 126.40 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 43 WDKAPCRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRM-KNGQFDKDGDFAPIS 121
Cdd:cd02757 1 WVPSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnPRKGRDVDPKFVPIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 122 WDQAFDIMAEKFKATLKEKGPTAVgMFGSGQWTVWEGYAAAKLMKAGFRSNNIDpnarHcmaSAVVGFMRTFGMDEPMGC 201
Cdd:cd02757 81 WDEALDTIADKIRALRKENEPHKI-MLHRGRYGHNNSILYGRFTKMIGSPNNIS----H---SSVCAESEKFGRYYTEGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 202 YD----DIEQADAFVLWGSN-MAEMHPI-----LWSRMSDR--------RLSNpdvqvhvlstfehrSFELADNGMVFTP 263
Cdd:cd02757 153 WDynsyDYANAKYILFFGADpLESNRQNphaqrIWGGKMDQakvvvvdpRLSN--------------TAAKADEWLPIKP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 264 QTDLAILNYVANYIIQNDKVN----WDFVNKHTVFKKGVTDigyglrptdplqqkaknpDSGDATPMTFEEFAKF----V 335
Cdd:cd02757 219 GEDGALALAIAHVILTEGLWDkdfvGDFVDGKNYFKAGETV------------------DEESFKEKSTEGLVKWwnleL 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 835291226 336 ADYDVESVSKLSGVSKEKLEKLAKLYADPSKKVVSYWTMGFNQHTRGVWANNLCYNIHLLTGKISEPG 403
Cdd:cd02757 281 KDYTPEWAAKISGIPAETIERVAREFATAAPAAAAFTWRGATMQNRGSYNSMACHALNGLVGSIDSKG 348
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
1-775 |
2.15e-29 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 125.16 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 1 MKLSRRDFMKANAVAAAAAVAGVSAP-TLAANLIT----STDKTAihwdkAPCRFCGTGCSVLVGSQDGRVVATQGDPDA 75
Cdd:PRK15488 1 MSLSRRDFLKGAGAGCAACALGSLLPgALAANEIAqlkgKTKLTP-----SICEMCSTRCPIEARVVNGKNVFIQGNPKA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 76 PVNRGLNCIKGYFLSKIMYGQDRLTQPMLRM-KNGqfdkDGDFAPISWDQAFDIMAEKFKATLKEKGPTAVgMFG--SGQ 152
Cdd:PRK15488 76 KSFGTKVCARGGSGHSLLYDPQRIVKPLKRVgERG----EGKWQEISWDEAYQEIAAKLNAIKQQHGPESV-AFSskSGS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 153 WTVWegyaAAKLMKAgFRSNNIDPNARHCMASAVVGFMRTFGMDEPMgcydDIEQADAFVLWGSNMAEMHPILWSRMSDR 232
Cdd:PRK15488 151 LSSH----LFHLATA-FGSPNTFTHASTCPAGYAIAAKVMFGGKLKR----DLANSKYIINFGHNLYEGINMSDTRGLMT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 233 RLSNPDVQvhvLSTFEHRsFEL----ADNGMVFTPQTDLAILNYVANYIIQNDKVNWDFVNKHTVfkkgvtdigyglrpt 308
Cdd:PRK15488 222 AQMEKGAK---LVVFEPR-FSVvaskADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERYTS--------------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 309 dplqqkaknpdsgdatpmTFEEFAKFVADYDVESVSKLSGVSKEKLEKLAKLYADPSKKVVSYW--TMGFNQH----TRG 382
Cdd:PRK15488 283 ------------------GFEELAASVKEYTPEWAEAISDVPADDIRRIARELAAAAPHAIVDFghRATFTPEefdmRRA 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 383 VW-ANNLCYNIH----LLTGKISEPGNgpfSLTGQPSAcgtarevGTFAHRLPADM-VVTEPKHRAIAEQ---IWKlpEG 453
Cdd:PRK15488 345 IFaANVLLGNIErkggLYFGKNASVYN---KLAGEKVA-------PTLAKPGVKGMpKPTAKRIDLVGEQfkyIAA--GG 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 454 ----TIPDkvgfhAVLQDrmlKDGKLNAyWVMCNNN-MQagpNM-NTDRLPGYRDPRNFIVVSDPYPTVTAQAADLILPT 527
Cdd:PRK15488 413 gvvqSIID-----ATLTQ---KPYQIKG-WVMSRHNpMQ---TVtDRADVVKALKKLDLVVVCDVYLSESAAYADVVLPE 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 528 AMWVE----------KEGAYGnaerrtqfWHQQVKAPEGAKSDLWQ-LMEFSKRFKVEEVWPAELIAKmpevkgktlFDV 596
Cdd:PRK15488 481 STYLErdeeisdksgKNPAYA--------LRQRVVEPIGDTKPSWQiFKELGEKMGLGQYYPWQDMET---------LQL 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 597 LYANGQVNQFPKEQSKGmlndeaehfgfYVQKG---LFEEYAtfgrghghDLAPF-DQYHEARglrwpVVDGKETLwryr 672
Cdd:PRK15488 544 YQVNGDHALLKELKKKG-----------YVSFGvplLLREPK--------MVAKFvARYPNAK-----AVDEDGTY---- 595
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 673 egfdpyvkaGEGVRFyGKPDGKAVIF------------ALPFEPAAESpdKEYDLWLSTGRVLEhwHTGTMTRRVPELYR 740
Cdd:PRK15488 596 ---------GSQLKF-KTPSGKIELFsaklealapgygVPRYRDVALK--KEDELYFIQGKVAV--HTNGATQNVPLLAN 661
|
810 820 830
....*....|....*....|....*....|....*
gi 835291226 741 AFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVK 775
Cdd:PRK15488 662 LMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEK 696
|
|
| 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 ... |
48-594 |
4.83e-28 |
|
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: 118.65 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRmkngqfdKDGDFAPISWDQAFD 127
Cdd:cd02771 4 CHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR-------RGGTLVPVSWNEALD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 128 IMAEKFKatlkeKGPTAVGMFGSGQWTVWEGYAAAKLMKAGFRSNNIDPNARhcmaSAVVGFMRTFGmdEPMGCYDDIEQ 207
Cdd:cd02771 77 VAAARLK-----EAKDKVGGIGSPRASNESNYALQKLVGAVLGTNNVDHRAR----RLIAEILRNGP--IYIPSLRDIES 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 208 ADAFVLWGSNMAEMHPI--LWSRMSDRRlsnpdvqvhvlstfehRSFELADNGMVFTPQtDLAILNYVAN-----YIIQN 280
Cdd:cd02771 146 ADAVLVLGEDLTQTAPRiaLALRQAARR----------------KAVELAALSGIPKWQ-DAAVRNIAQGaksplFIVNA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 281 DKVNWDFVNKHTVFkkgvTDIGYGLRPTDPLQQKAKNpDSGDATPMTFEEFAKFVADYDVES-----VSKLSGVSKEKLE 355
Cdd:cd02771 209 LATRLDDIAAESIR----ASPGGQARLGAALARAVDA-SAAGVSGLAPKEKAARIAARLTGAkkpliVSGTLSGSLELIK 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 356 KLAKLyadpskkvvsYWTMGFNQHTRGVwannlcyniHLLTGKISEPGNGPfsLTGQPSACGTAREvgtfahrlpadmvv 435
Cdd:cd02771 284 AAANL----------AKALKRRGENAGL---------TLAVEEGNSPGLLL--LGGHVTEPGLDLD-------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 436 tepkhraiaeqiwklpegtipdkvgfhAVLQDrmLKDGKLNAYWVMCNNNMQAGPNMNTDRLpgyRDPRNFIVVSDPYPT 515
Cdd:cd02771 329 ---------------------------GALAA--LEDGSADALIVLGNDLYRSAPERRVEAA---LDAAEFVVVLDHFLT 376
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 516 VTAQAADLILPTAMWVEKEGAYGNAERRTQFWHQQVKAPEG-AKSDLWQLMEFSKRFKVEEV---WP--AELIAKMPEVK 589
Cdd:cd02771 377 ETAERADVVLPAASFAEKSGTFVNYEGRAQRFFKAYDDPAGdARSDWRWLHALAAKLGGKLVpsdAAilDEIIALVPGKA 456
|
....*
gi 835291226 590 GKTLF 594
Cdd:cd02771 457 PVGGH 461
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
711-828 |
2.22e-25 |
|
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: 101.53 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 711 KEYDLWLSTGRVLEHWHTGTMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPPkgL 790
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPH--E 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 835291226 791 VFMPF-FDASQLV-----NKLTLDATDPLSKETDYKKCAVKVMK 828
Cdd:cd02792 79 VGIPYhWGGMGLVigdsaNTLTPYVGDPNTQTPEYKAFLVNIEK 122
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
51-603 |
4.95e-25 |
|
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: 110.88 E-value: 4.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 51 CGTGCSVLVGSQDGRVV------ATQGDPDAPVNRGlnCIKGYFLSKIMYGQDRLTQPMLRM-KNGQfdkdGDFAPISWD 123
Cdd:cd02770 8 CGGRCPLKAHVKDGVITrietddTGDDDPGFHQIRA--CLRGRSQRKRVYNPDRLKYPMKRVgKRGE----GKFVRISWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 124 QAFDIMAEKFKATLKEKGPTA----VGMFGSGQWTVWEGyAAAKLMKA--GFrsnnIDPNARHCMASAVVGFMRTFGMDE 197
Cdd:cd02770 82 EALDTIASELKRIIEKYGNEAiyvnYGTGTYGGVPAGRG-AIARLLNLtgGY----LNYYGTYSWAQITTATPYTYGAAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 198 PMGCYDDIEQADAFVLWGSNMAEmhpilwSRMSD-------RRLSNPDVQVHVLSTFEHRSFE-LADNGMVFTPQTDLAI 269
Cdd:cd02770 157 SGSSLDDLKDSKLVVLFGHNPAE------TRMGGggstyyyLQAKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 270 LNYVANYIIQNDKVNWDFVNKHTVfkkgvtdiGYG---LRPTDPLQQKAKN------PDSGDATPmtfeEFAkfvadydv 340
Cdd:cd02770 231 VAAMAYVMITENLHDQAFLDRYCV--------GFDaehLPEGAPPNESYKDyvlgtgYDGTPKTP----EWA-------- 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 341 esvSKLSGVSKEKLEKLAKLYAdpSKK---VVSYWtmGFNQHTRGVWANNLCYNIHLLTGKISEPGNGPFSLTGQPSACG 417
Cdd:cd02770 291 ---SEITGVPAETIRRLAREIA--TTKpaaILQGW--GPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 418 TArevgtfahrLPAdmvVTEPkhraIAEQIwklPEGTIPDKV-GFHAVLQDRMLKDG--KLNAYWVM-----CNN--NMQ 487
Cdd:cd02770 364 AG---------LPA---GKNP----VKTSI---PCFMWTDAIeRGEEMTADDGGVKGadKLKSNIKMiwnyaGNTliNQH 424
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 488 AGPNMNTDRLPGYRDPRNFIVVSDPYPTVTAQAADLILPTAMWVEKEG--AYGNAERRTQFWH-QQVKAPEG-AKSDLWQ 563
Cdd:cd02770 425 SDDNNTTRALLDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDivLTSNAGMMEYLIYsQKAIEPLYeCKSDYEI 504
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 835291226 564 LMEFSKR---------FKVEEVWPAELI----AKMP------EVKGKTLFDVLYANGQV 603
Cdd:cd02770 505 CAELAKRlgvedqfteGKTEQEWLEELYgqtrAKEPglptyeEFREKGIYRVPRALPFV 563
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
722-820 |
3.88e-24 |
|
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: 97.39 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 722 VLEHWHTGTMTRrVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPpkGLVFMPF-----F 796
Cdd:cd02775 1 LRDHFHSGTRTR-NPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPP--GVVFLPHgwghrG 77
|
90 100
....*....|....*....|....
gi 835291226 797 DASQLVNKLTLDATDPLSKETDYK 820
Cdd:cd02775 78 GRGGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
51-578 |
1.73e-23 |
|
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: 105.64 E-value: 1.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 51 CGTGCSVLVGSQDGRVVA-TQGD-PDAPVNRGlnCIKGYFLSKIMYGQDRLTQPMLRMKNGqfdKDGDFAPISWDQAFDI 128
Cdd:cd02765 8 CGGRCPLKCHVRDGKIVKvEPNEwPDKTYKRG--CTRGLSHLQRVYSPDRLKYPMKRVGER---GEGKFERITWDEALDT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 129 MAEKFKATLKEKGPTAVG-MFGSGQW--TVWEGYAAAKLMKAGFRSNNIDPNARHCMaSAVVGFMRTFGMDEPmgcyDDI 205
Cdd:cd02765 83 IADKLTEAKREYGGKSILwMSSSGDGaiLSYLRLALLGGGLQDALTYGIDTGVGQGF-NRVTGGGFMPPTNEI----TDW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 206 EQADAFVLWGSNMAEMHP-----ILWSRMSDRRLSNPDvqvHVLSTfehrSFELADNGMVFTPQTDLAILNYVANYIIQN 280
Cdd:cd02765 158 VNAKTIIIWGSNILETQFqdaefFLDARENGAKIVVID---PVYST----TAAKADQWVPIRPGTDPALALGMINYILEH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 281 DKVNWDFVNKHTVFKKGV-TDIGYGLRPTDPLQQKAKNP------DSG-----DATPMTFEEFAKF-------------- 334
Cdd:cd02765 231 NWYDEAFLKSNTSAPFLVrEDNGTLLRQADVTATPAEDGyvvwdtNSDspepvAATNINPALEGEYtingvkvhtvltal 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 335 ---VADYDVESVSKLSGVSKEKLEKLAKLYAdpSKKVVSYWTMG-----FNQHTRGVWANNLCynihLLTGKISEPGNGP 406
Cdd:cd02765 311 reqAASYPPKAAAEICGLEEAIIETLAEWYA--TGKPSGIWGFGgvdryYHSHVFGRTAAILA----ALTGNIGRVGGGV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 407 fsltgqpsacgtarevgtfahrlpadmvvtepkhraiaeqiwklpegtipdkvgfhavlqdrmlkdGKLNAYWVMCNNNM 486
Cdd:cd02765 385 ------------------------------------------------------------------GQIKFMYFMGSNFL 398
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 487 QAGPNMNT-----DRLPgyrdprnFIVVSDPYPTVTAQAADLILPTAMWVEKEGAYGNAERRTQFWHQQvKAPEG---AK 558
Cdd:cd02765 399 GNQPDRDRwlkvmKNLD-------FIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHPHVLLQQ-KAIEPlfeSK 470
|
570 580
....*....|....*....|
gi 835291226 559 SDLWQLMEFSKRFKVEEVWP 578
Cdd:cd02765 471 SDFEIEKGLAERLGLGDYFP 490
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
41-95 |
4.56e-22 |
|
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: 90.04 E-value: 4.56e-22
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 835291226 41 IHWDKAPCRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYG 95
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
51-828 |
7.60e-22 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 101.26 E-value: 7.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 51 CGTGCSVLVGSQDGRVVATQGDPDAPVN-RGLN----CIKGYFLSKIMYGQDRLTQPMLRM-KNGQfdkdGDFAPISWDQ 124
Cdd:PRK14990 67 CGSRCPLRMHVVDGEIKYVETDNTGDDNyDGLHqvraCLRGRSMRRRVYNPDRLKYPMKRVgARGE----GKFERISWEE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 125 AFDIMAEKFKATLKEKGPTAV------GMFGSGQWTVWE--GYAAAKLMK--AGFRSNNIDpnarHCMASAVVGFMRTFG 194
Cdd:PRK14990 143 AYDIIATNMQRLIKEYGNESIylnygtGTLGGTMTRSWPpgNTLVARLMNccGGYLNHYGD----YSSAQIAEGLNYTYG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 195 MDEPMGCYDDIEQADAFVLWGSNMAEmhpilwSRMSD----------RRLSNPDVQVhVLSTFEHRSFELADNGMVFTPQ 264
Cdd:PRK14990 219 GWADGNSPSDIENSKLVVLFGNNPGE------TRMSGggvtyyleqaRQKSNARMII-IDPRYTDTGAGREDEWIPIRPG 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 265 TDLAILNYVANYIIQNDKVNWDFVNKHTVfkkgvtdiGYglrptDPLQQKAKNPDSGDATPMTFEEFAKFVADYDvESVS 344
Cdd:PRK14990 292 TDAALVNGLAYVMITENLVDQPFLDKYCV--------GY-----DEKTLPASAPKNGHYKAYILGEGPDGVAKTP-EWAS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 345 KLSGVSKEKLEKLAKLYADPSKKVVSY-WtmGFNQHTRGVWANNLCYNIHLLTGKIsepgngpfSLTGQPSAcgtAREvG 423
Cdd:PRK14990 358 QITGVPADKIIKLAREIGSTKPAFISQgW--GPQRHANGEIATRAISMLAILTGNV--------GINGGNSG---ARE-G 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 424 TFA---HRLPadmVVTEPKHRAIAEQIWKLPEGTIPDKVGFHAVLQDRMLKDGKLNAYWVMCNN---NMQAGPNMNTDRL 497
Cdd:PRK14990 424 SYSlpfVRMP---TLENPIQTSISMFMWTDAIERGPEMTALRDGVRGKDKLDVPIKMIWNYAGNcliNQHSEINRTHEIL 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 498 pgyRDPRN--FIVVSDPYPTVTAQAADLILPTAMWVEK-----EGAYGNAErRTQFWHQQVKAPEGAKSDLWQLMEFSKR 570
Cdd:PRK14990 501 ---QDDKKceLIVVIDCHMTSSAKYADILLPDCTASEQmdfalDASCGNMS-YVIFNDQVIKPRFECKTIYEMTSELAKR 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 571 FKVEEVWpaeliakmpeVKGKTLFDVLyangqvnQFPKEQSKGMLNDEAEhFGFYVQKGLFEEYATfgRGHGHDLAPFDQ 650
Cdd:PRK14990 577 LGVEQQF----------TEGRTQEEWM-------RHLYAQSREAIPELPT-FEEFRKQGIFKKRDP--QGHHVAYKAFRE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 651 YHEARGLRWPvvDGKETLwrYREGFDPYVKAGEgvrfygKPDGKaVIFALP-----FEPAAESPDKEYDLWLSTGRVLEH 725
Cdd:PRK14990 637 DPQANPLTTP--SGKIEI--YSQALADIAATWE------LPEGD-VIDPLPiytpgFESYQDPLNKQYPLQLTGFHYKSR 705
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 726 WHTgtmTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRP-----PKGLVFMPffDASQ 800
Cdd:PRK14990 706 VHS---TYGNVDVLKAACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPgvvalGEGAWYDP--DAKR 780
|
810 820 830
....*....|....*....|....*....|...
gi 835291226 801 L-----VNKLTLDATDPLSKETDYKKCAVKVMK 828
Cdd:PRK14990 781 VdkggcINVLTTQRPSPLAKGNPSHTNLVQVEK 813
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
59-602 |
1.50e-21 |
|
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: 100.25 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 59 VGSQDGR--VVATQGDPDAPVNRGLNCIKGYFLSKIMY------GQDRLTQPMLRmkngqfdKDGDFAPISWDQAFDIMA 130
Cdd:cd02756 70 VVTQDGRevYIVIVPDKECPVNSGNYSTRGGTNAERIWspdnrvGETRLTTPLVR-------RGGQLQPTTWDDAIDLVA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 131 EKFKATLKEKGPTAVGMF------GSGQWTVwEGYAAAKLMKAGFRSNNIDPNARHCMASAVVGfMRTFGMDEPMGCYDD 204
Cdd:cd02756 143 RVIKGILDKDGNDDAVFAsrfdhgGGGGGFE-NNWGVGKFFFMALQTPFVRIHNRPAYNSEVHA-TREMGVGELNNSYED 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 205 IEQADAFVLWGSNMAE---------MHPILW----SRMSDRRLSNPDVQVHVLSTFEHRSFELA---------DNGMVF- 261
Cdd:cd02756 221 ARLADTIVLWGNNPYEtqtvyflnhWLPNLRgatvSEKQQWFPPGEPVPPGRIIVVDPRRTETVhaaeaaagkDRVLHLq 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 262 -TPQTDLAILNYVANYIIqndkvnwdfvnkhtvfkkgvtdigYGLRptdplqqkaknpdsgdatpMTFEEfakfvadydv 340
Cdd:cd02756 301 vNPGTDTALANAIARYIY------------------------ESLD-------------------EVLAE---------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 341 esVSKLSGVSKEKLEKLAKLYADPskKVVSYWTMGFNQHTRGVWANNLCY-------NIHLLTGKISEPGNGpfsltgqp 413
Cdd:cd02756 328 --AEQITGVPRAQIEKAADWIAKP--KEGGYRKRVMFEYEKGIIWGNDNYrpiyslvNLAIITGNIGRPGTG-------- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 414 saCGTArevgtFAHRLPAdmvvTEPkhraiaeqiwkLPEGTIPDKVGFHAVLQDRMLKDGKLNAYWVMCNNNMQAGPN-- 491
Cdd:cd02756 396 --CVRQ-----GGHQEGY----VRP-----------PPPPPPWYPQYQYAPYIDQLLISGKGKVLWVIGCDPYKTTPNaq 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 492 ----------------MNTDRLPGYRDPRN--------------FIVVSDPYPTVTAQAADLILPTAMWVE-KEGAYGNA 540
Cdd:cd02756 454 rlretinhrsklvtdaVEAALYAGTYDREAmvcligdaiqpgglFIVVQDIYPTKLAEDAHVILPAAANGEmNETSMNGH 533
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835291226 541 ERRTQFWHQQVKAPEGAKSDLWQLMEFSKRfkVEEVWPAELIAKMPEVKG-----KTLFDVLYANGQ 602
Cdd:cd02756 534 ERRLRLYEKFMDPPGEAMPDWWIAAMIANR--IYELYQEEGKGGSAQYQFfgfiwKTEEDNFMDGSQ 598
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
48-229 |
4.29e-21 |
|
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: 96.20 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRmkngqfdKDGDFAPISWDQAFD 127
Cdd:cd02768 4 DVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIK-------KGGKLVPVSWEEALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 128 IMAEKFKATLKEKgptaVGMFGSGQWTVWEGYAAAKLMKaGFRSNNIDPNARHCMASAVVGFMRTFGMDEPmgcYDDIEQ 207
Cdd:cd02768 77 TVAEGLKAVKGDK----IGGIAGPRADLESLFLLKKLLN-KLGSNNIDHRLRQSDLPADNRLRGNYLFNTS---IAEIEE 148
|
170 180
....*....|....*....|..
gi 835291226 208 ADAFVLWGSNMAEMHPILWSRM 229
Cdd:cd02768 149 ADAVLLIGSNLRKEAPLLNARL 170
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
45-533 |
2.07e-18 |
|
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: 89.89 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 45 KAPCRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYflSKIM--YGQDRLTQPMLRMKNgqfDKDGDFAPISW 122
Cdd:cd02763 1 TTTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGS--SGIMkqYSPARLTKPLLRKGP---RGSGQFEEIEW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 123 DQAFDIMAEKFKAtLKEKGPTAVGMF-GSGQWTVWEGYAAAKlmkagFRSNNIDPNARHCMASAVVGFMRTFG-----MD 196
Cdd:cd02763 76 EEAFSIATKRLKA-ARATDPKKFAFFtGRDQMQALTGWFAGQ-----FGTPNYAAHGGFCSVNMAAGGLYSIGgsfweFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 197 EPmgcydDIEQADAFVLWGSnmAEMH---PILWSRMSDRRLSNPDVQVHVLSTFEHrsfELADNGMVFTPQTDLAILNYV 273
Cdd:cd02763 150 GP-----DLEHTKYFMMIGV--AEDHhsnPFKIGIQKLKRRGGKFVAVNPVRTGYA---AIADEWVPIKPGTDGAFILAL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 274 ANYIIQNDKVNWDFVNKHTVfkkgvtdigyglrptdplqqkaknpdsgdatpmtfeefAKFVADYDVESVSKLSGVSKEK 353
Cdd:cd02763 220 AHELLKAGLIDWEFLKRYTN--------------------------------------AAELVDYTPEWVEKITGIPADT 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 354 LEKLAK-------------------LYADPSKKV----VSYWTM-GFNQHTRGVWANNLCYNIHLLTGKISEPG----NG 405
Cdd:cd02763 262 IRRIAKelgvtardqpielpiawtdVWGRKHEKItgrpVSFHAMrGIAAHSNGFQTIRALFVLMMLLGTIDRPGgfrhKP 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 406 PFSLTGQPSACGTAREVGTFAHRLPADM---VVTEPKHRAIAEQ----------IWKLPegtipdkVGFHAVLQDRMLKD 472
Cdd:cd02763 342 PYPRHIPPLPKPPKIPSADKPFTPLYGPplgWPASPDDLLVDEDgnplridkaySWEYP-------LAAHGCMQNVITNA 414
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835291226 473 GKLNAY----WVMCNNNMQAGPNMNT----------DRLPGYRDPrnFIVVSDPYPTVTAQAADLILPTAMWVEK 533
Cdd:cd02763 415 WRGDPYpidtLMIYMANMAWNSSMNTpevremltdkDASGNYKIP--FIIVCDAFYSEMVAFADLVLPDTTYLER 487
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
93-229 |
7.86e-17 |
|
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: 83.56 E-value: 7.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 93 MYGQDRLTQPMLRmkngqfdKDGDFAPISWDQAFDIMAEKFKATLKEKGPTAVGMFGSGQWTVWEGYAAAKLMkAGFRSN 172
Cdd:cd02772 49 LNSEDRLTKPMIK-------KDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLA-RGLGSD 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 835291226 173 NIDPNARHCMASAVVgfmrTFGMDEPMGC-YDDIEQADAFVLWGSNMAEMHPILWSRM 229
Cdd:cd02772 121 NIDHRLRQSDFRDDA----KASGAPWLGMpIAEISELDRVLVIGSNLRKEHPLLAQRL 174
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
43-149 |
4.00e-16 |
|
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: 81.81 E-value: 4.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 43 WD--KAP--CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRmkngqfdKDGDFA 118
Cdd:COG1034 213 WElkKTPsiCPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVR-------KDGELV 285
|
90 100 110
....*....|....*....|....*....|.
gi 835291226 119 PISWDQAFDIMAEKFKATLKEKGPTAVGMFG 149
Cdd:COG1034 286 EASWEEALAAAAEGLKALKKAENSVGAALLG 316
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
98-444 |
1.01e-15 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 81.63 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 98 RLTQPMlrmkngQFDKDGD-FAPISWDQAFDIMAEKFKATlkeKGPTAVGMFGSGQwTVWEGYAAAKLMKAGFRSNNIDP 176
Cdd:PRK09939 108 RLTQPL------KYDAVSDcYKPLSWQQAFDEIGARLQSY---SDPNQVEFYTSGR-TSNEAAFLYQLFAREYGSNNFPD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 177 NARHCMASAVVGFMRTFGMDEPMGCYDDIEQADAFVLWGSNMAEMHPILWSRMsdRRLSNPDVQVHVLSTFEHRSFELad 256
Cdd:PRK09939 178 CSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSL--RALVKRGAKMIAINPLQERGLER-- 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 257 ngmvFT-PQTDLAILNyvaNYIIQNDKVNWDF-VNKHTVFKKGVTDIgygLRPTDPLQQKAKNPDSGD-----ATPMTFE 329
Cdd:PRK09939 254 ----FTaPQNPFEMLT---NSETQLASAYYNVrIGGDMALLKGMMRL---LIERDDAASAAGRPSLLDdefiqTHTVGFD 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 330 EFAKFVADYDVESVSKLSGVSKEKLEKLAKLYADPSKKVVSYwTMGFNQHTRGVWANNLCYNIHLLTGKISEPGNGPFSL 409
Cdd:PRK09939 324 ELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICY-GMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPL 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 835291226 410 TGQPSACG------TAREVGTFAHRLPADMVVTEPK---HRAIA 444
Cdd:PRK09939 403 RGHSNVQGdrtvgiTEKPSAEFLARLGERYGFTPPHapgHAAIA 446
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
48-94 |
1.30e-15 |
|
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: 71.51 E-value: 1.30e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMY 94
Cdd:smart00926 8 CPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVY 54
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
48-253 |
1.43e-14 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 78.06 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRmkngqfDKDGDFAPISWDQAFD 127
Cdd:PRK07860 228 CEHCASGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTYATQPDRITTPLVR------DEDGELEPASWSEALA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 128 IMAEKFKATLkekgpTAVGMFGSGQWTVWEGYAAAKLMKAGFRSNNIDPNAR-------HCMASAVVGfmRTFGMDepmg 200
Cdd:PRK07860 302 VAARGLAAAR-----GRVGVLVGGRLTVEDAYAYAKFARVALGTNDIDFRARphsaeeaDFLAARVAG--RGLGVT---- 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 835291226 201 cYDDIEQADAFVLWGSNMAEMHPILWSRMSDRRLSNpDVQVHVLSTFEHRSFE 253
Cdd:PRK07860 371 -YADLEKAPAVLLVGFEPEEESPIVFLRLRKAARKH-GLKVYSIAPFATRGLE 421
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
62-576 |
8.19e-12 |
|
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: 68.83 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 62 QDGRVVATQGDPDAPVNRGLncIKGYFLSkiMYGQDRLTQPMLR---MKNGQFDK-----DGDFAPISWDQAFDIMAEKF 133
Cdd:cd02769 14 KDGRIVGVRPFEEDPDPSPL--LDGVPDA--VYSPTRIKYPMVRrgwLEKGPGSDrslrgKEEFVRVSWDEALDLVAAEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 134 KATLKEKGPTAV----------GMFGSGQWTVWEGYAAAklmkAGF--RSNNIDPNARHCMASAVVGFMRTFgmDEPMGC 201
Cdd:cd02769 90 KRVRKTYGNEAIfggsygwssaGRFHHAQSLLHRFLNLA----GGYvgSVGDYSTGAAQVILPHVVGSMEVY--TEQQTS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 202 YDDI-EQADAFVLWGSNmaemhpilwsrmsdrRLSNpdVQVHVLSTFEHRSF----ELADNGMVFT-------------- 262
Cdd:cd02769 164 WPVIaEHTELVVAFGAD---------------PLKN--AQIAWGGIPDHQAYsylkALKDRGIRFIsisplrddtaaelg 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 263 -------PQTDLAILNYVANYIIQNDKVNWDFVNKHTV-FKK------GVTDigyGLrptdplqqkAKNPdsgdatpmtf 328
Cdd:cd02769 227 aewiairPGTDVALMLALAHTLVTEGLHDKAFLARYTVgFDKflpyllGESD---GV---------PKTP---------- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 329 eEFAkfvadydvesvSKLSGVSKEKLEKLAKLYADPSKKVVSYWTMGFNQHtrG---VW-ANNLCYNIhlltGKISEPGN 404
Cdd:cd02769 285 -EWA-----------AAICGIPAETIRELARRFASKRTMIMAGWSLQRAHH--GeqpHWmAVTLAAML----GQIGLPGG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 405 GpFSLTGQPSACGTAREVGTFAHRL-----PADMVVtePKHRaIAEQIWKlPEGTIpDKVGfhavlQDRMLKDGKLnAYW 479
Cdd:cd02769 347 G-FGFGYHYSNGGGPPRGAAPPPALpqgrnPVSSFI--PVAR-IADMLLN-PGKPF-DYNG-----KKLTYPDIKL-VYW 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 480 vmcnnnmqAGPN-----MNTDRL-PGYRDPRNFIvVSDPYPTVTAQAADLILPTAMWVEKE--GAYGNaeRRTQFWHQQV 551
Cdd:cd02769 415 --------AGGNpfhhhQDLNRLiRAWQKPETVI-VHEPFWTATARHADIVLPATTSLERNdiGGSGD--NRYIVAMKQV 483
|
570 580
....*....|....*....|....*.
gi 835291226 552 KAPEG-AKSDLWQLMEFSKRFKVEEV 576
Cdd:cd02769 484 VEPVGeARDDYDIFADLAERLGVEEQ 509
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
713-828 |
3.84e-11 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase 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.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 60.94 E-value: 3.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 713 YDLWLSTGRVLEHWHTGTMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPpkGLVF 792
Cdd:cd02779 1 YKYWVNNGRANIIWQTAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKP--GQTF 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 835291226 793 MPFFDASQLVNKLTLDATDPLSKETDYKKCAVKVMK 828
Cdd:cd02779 79 MLMAHPRPGANGLVTPYVDPETIIPYYKGTWANIRK 114
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
48-143 |
4.21e-11 |
|
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: 66.53 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 48 CRFCGTGCSVL-VGSQDGRVVATQGDPDAP---VNRGLNCIKGYFLSKIMYGQDRLTQPMLRM--KNGQfDKDGDFAPIS 121
Cdd:cd02760 4 CYNCVAGPDFMaVKVVDGVATEIEPNFAAEdihPARGRVCVKAYGLVQKTYNPNRVLQPMKRTnpKKGR-NEDPGFVPIS 82
|
90 100
....*....|....*....|..
gi 835291226 122 WDQAFDIMAEKFKATlKEKGPT 143
Cdd:cd02760 83 WDEALDLVAAKLRRV-REKGLL 103
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
51-571 |
4.06e-10 |
|
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: 63.11 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 51 CGTGCSVLVGSQDGRVVA--TQGD-PDAPVN------RGlnCIKGYFLSKIMYGQDRLTQPMLRM-KNGQfdkdGDFAPI 120
Cdd:cd02750 12 CTGSCSWNVYVKNGIVTReeQATDyPETPPDlpdynpRG--CQRGASFSWYLYSPDRVKYPLKRVgARGE----GKWKRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 121 SWDQAFDIMAEKFKATLKEKGPTAVGMF----GSGQWTVWEGYAAAKLMKAGFRSNNiDPNARHCMASAvvgfmRTFG-- 194
Cdd:cd02750 86 SWDEALELIADAIIDTIKKYGPDRVIGFspipAMSMVSYAAGSRFASLIGGVSLSFY-DWYGDLPPGSP-----QTWGeq 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 195 MDEPMgcYDDIEQADAFVLWGSNMAEMHPILWSRMSDRRLSNpdVQVHVLSTFEHRSFELADNGMVFTPQTDLAILNYVA 274
Cdd:cd02750 160 TDVPE--SADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNG--AKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 275 NYIIQNDKVNWDFVNKHTVFkkgvtdigyglrptdPLqqkaknpdsgdatpmtfeefakFVadYDVESVSKLSGVSKEKL 354
Cdd:cd02750 236 HVIIKEKLYDEDYLKEYTDL---------------PF----------------------LV--YTPAWQEAITGVPRETV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 355 EKLAKLYADpSKKVVSYWTMGFNQHTRGvwanNLCY----NIHLLTGKISEPGNGPFSLTGQPSACGTARevgtfahrlp 430
Cdd:cd02750 277 IRLAREFAT-NGRSMIIVGAGINHWYHG----DLCYraliLLLALTGNEGKNGGGWAHYVGQPRVLFVWR---------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 431 ADMVVTEPK-HRAIAEQIWklpegtipdkvgfhavlqdrmlkdGKLnaywvmcnnnmqagpnmntdrlpgyrdprNFIVV 509
Cdd:cd02750 342 GNLFGSSGKgHEYFEDAPE------------------------GKL-----------------------------DLIVD 368
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835291226 510 SDPYPTVTAQAADLILPTAMWVEKegaygnAERRT-------QFWHQQVKAPEGAKSDLWQLMEFSKRF 571
Cdd:cd02750 369 LDFRMDSTALYSDIVLPAATWYEK------HDLSTtdmhpfiHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
712-777 |
5.01e-10 |
|
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: 58.09 E-value: 5.01e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835291226 712 EYDLWLSTG-RVLEHWHTgtMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTR 777
Cdd:cd02781 1 EYPLILTTGaRSYYYFHS--EHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQK 65
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
715-795 |
1.53e-08 |
|
The MopB_CT_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. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 53.43 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 715 LWLSTGRVLehWHTGTMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPpkGLVFMP 794
Cdd:cd02778 2 FRLIYGKSP--VHTHGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRP--DTVFMP 77
|
.
gi 835291226 795 F 795
Cdd:cd02778 78 H 78
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
745-794 |
1.19e-07 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 51.00 E-value: 1.19e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 835291226 745 AVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTR-VETRGrnrPPKGLVFMP 794
Cdd:COG1153 31 AVCELNPEDMKKLGIKEGDKVKVTSEYGEVVVKaKESED---LHPGLVFIP 78
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
730-814 |
1.65e-07 |
|
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: 50.85 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 730 TMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPpkGLVFMPF-------------F 796
Cdd:cd02782 18 SWLHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMP--GVVSLPHgwghdypgvsgagS 95
|
90
....*....|....*....
gi 835291226 797 DASQLVNKLTLDA-TDPLS 814
Cdd:cd02782 96 RPGVNVNDLTDDTqRDPLS 114
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
726-828 |
2.94e-07 |
|
The MopB_CT_DmsA-EC CD 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. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 49.98 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 726 WHTGtmtRR-------VPELYRAFPDAVlFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRPpkGLVFMPF--- 795
Cdd:cd02794 8 WHYK---RRthstfdnVPWLREAFPQEV-WINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMP--GVVALPQgaw 81
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 835291226 796 -------FDASQLVNKLTLDATDPLSKETDYKKCAVKVMK 828
Cdd:cd02794 82 yepdangIDKGGCINTLTGLRPSPLAKGNPQHTNLVQVEK 121
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
746-826 |
3.22e-07 |
|
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative 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: 239188 [Multi-domain] Cd Length: 112 Bit Score: 49.58 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 746 VLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNRP---PKGLVFMPFFDASQLVnklTLDATDPLSKETDYKKC 822
Cdd:cd02787 32 VVFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEydiPRGCLAAYYPEGNVLV---PLDHRDPQSKTPAYKSV 108
|
....
gi 835291226 823 AVKV 826
Cdd:cd02787 109 PVRL 112
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
735-812 |
4.30e-06 |
|
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: 46.51 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 735 VPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVetRGRNRPPKGLVFMP------FFDASQLVNKLTLD 808
Cdd:cd02786 21 LPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRA--KVTDDVPPGVVVAEggwwreHSPDGRGVNALTSA 98
|
....*
gi 835291226 809 A-TDP 812
Cdd:cd02786 99 RlTDL 103
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
726-777 |
5.62e-05 |
|
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: 43.51 E-value: 5.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 835291226 726 WHTGTMTRRVPELYRAFPDAVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTR 777
Cdd:cd02785 13 FRVHSQFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCK 64
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| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
518-562 |
1.26e-04 |
|
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: 45.33 E-value: 1.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 835291226 518 AQAADLILPTAMWVEKEGAYGNAERRTQFWHQQVKAPEGAKSDlW 562
Cdd:cd02773 322 AQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDARED-W 365
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| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
745-794 |
1.41e-04 |
|
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: 41.64 E-value: 1.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 835291226 745 AVLFMHPDDAKARGVRRGEEVIVSSRRGEVKTRVETRGRNrpPKGLVFMP 794
Cdd:cd02789 31 AYCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGV--PEGMVFIP 78
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| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
713-774 |
1.77e-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: 42.19 E-value: 1.77e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835291226 713 YDLWLSTgrvlehWHTGtmtRR-------VPELYRAFPDA---VLFMHPDDAKARGVRRGEEVIVSSRRGEV 774
Cdd:cd02777 1 YPLQLIS------PHPK---RRlhsqldnVPWLREAYKVKgrePVWINPLDAAARGIKDGDIVRVFNDRGAV 63
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| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
47-230 |
5.16e-04 |
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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: 43.48 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 47 PCRFCGTGCSVL-VGSQDGRVVATQGdpdapvnrglNCIKGYflSKIMYGQDRLTQPMLRMKngqfdkdgdfaPISWDQA 125
Cdd:cd02761 3 VCPFCGLLCDDIeVEVEDNKITKVRN----------ACRIGA--AKFARYERRITTPRIDGK-----------PVSLEEA 59
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 126 FDIMAEkfkaTLKEKGPTAVGMFGSgqwTVWEGYAAA-KL-MKAGfrsNNIDPNARHCMASAVVGFMRTfgmDEPMGCYD 203
Cdd:cd02761 60 IEKAAE----ILKEAKRPLFYGLGT---TVCEAQRAGiELaEKLG---AIIDHAASVCHGPNLLALQDS---GWPTTTLG 126
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170 180
....*....|....*....|....*...
gi 835291226 204 DIE-QADAFVLWGSNMAEMHPILWSRMS 230
Cdd:cd02761 127 EVKnRADVIVYWGTNPMHAHPRHMSRYS 154
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| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
50-189 |
2.06e-03 |
|
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: 41.71 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 50 FCGTGCSVLVGSQDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGQDRLTQPMLRMKNGQfdkdgdFAPISWDQAFDIM 129
Cdd:cd02764 51 PAGEGQGVLVKTVDGRPIKIEGNPDHPASLGGTSARAQASVLSLYDPDRAQGPLRRGIDGA------YVASDWADFDAKV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835291226 130 AEKFKA----------TLKEKGPT---AVGMF----GSGQWTVW---EGYAAAKLMKAGFrSNNIDPNARHCMASAVVGF 189
Cdd:cd02764 125 AEQLKAvkdggklavlSGNVNSPTteaLIGDFlkkyPGAKHVVYdplSAEDVNEAWQASF-GKDVVPGYDFDKAEVIVSI 203
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| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
747-774 |
4.28e-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: 38.00 E-value: 4.28e-03
10 20
....*....|....*....|....*...
gi 835291226 747 LFMHPDDAKARGVRRGEEVIVSSRRGEV 774
Cdd:cd02793 35 IRINPADAAARGIADGDIVRVFNDRGAC 62
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