|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
17-824 |
0e+00 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 1847.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 17 GLPILVRAsNLVTEADVTSLVWNKAPCRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTR 96
Cdd:PRK13532 22 GLSLPAVA-NAVVGSAQTAIKWDKAPCRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNCIKGYFLSKIMYGKDRLTQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 97 PLLRMKDGKFDKQGEFQPISWEQAFDIMAEKFKAALKAKGPESVGMFGSGQWTVWEGYAANKLFKAGLRSNNIDPNARHC 176
Cdd:PRK13532 101 PLLRMKDGKYDKEGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNIDPNARHC 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 177 MASAVMGFMRSFGMDEPMGCYDDIEATDSFVLWGSNMAEMHPVLWSRVTDRRLSAPQVKVAVLSTFEHRSFELADLPMVF 256
Cdd:PRK13532 181 MASAVVGFMRTFGIDEPMGCYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRLSNPDVKVAVLSTFEHRSFELADNGIIF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 257 KPQTDLIILNYIANHIIESGAVNRDFVERHVRFAHGAEDIGYGLRPDDPLEKKAKNADKANTWSDIDFKAFAEFVKPYTL 336
Cdd:PRK13532 261 TPQTDLAILNYIANYIIQNNAVNWDFVNKHTNFRKGATDIGYGLRPTHPLEKAAKNPGTAGKSEPISFEEFKKFVAPYTL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 337 ERTARESGVPAERLKALAELYADPKRKVVSFWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPFSLTGQPSACGTAR 416
Cdd:PRK13532 341 EKTAKMSGVPKEQLEQLAKLYADPNRKVVSFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGTAR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 417 EVGTFSHRLPADLVVTNPKHRETAEKIWKVPAGTIQEKVGFHAVQQSRMLKDGVLNVYWTQVSNNMQAGPNVMQEVLPGW 496
Cdd:PRK13532 421 EVGTFSHRLPADMVVTNPKHREIAEKIWKLPEGTIPPKPGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNINEERLPGW 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 497 RNPDNFVIVSDVYPTVSAQAADLILPSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDLWQLVEFSKRFTTDEVWPAE 576
Cdd:PRK13532 501 RNPDNFIVVSDPYPTVSALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDLWQLVEFSKRFKTEEVWPEE 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 577 LLAKAPELKGKTLYDVLFRNGQVDRFPASDLAKGYANDEVDAFGFYIQKGLFEEYAAFGRGHGHDLAPFDAYHEARGLRW 656
Cdd:PRK13532 581 LLAKKPEYRGKTLYDVLFANGQVDKFPLSELAEGYLNDEAKHFGFYVQKGLFEEYASFGRGHGHDLAPFDTYHKVRGLRW 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 657 PVVDGKETRWRYREGYDPYVSKGSGVQFYGYPDKKAIVFALPYEPPAEAPDQDYPFWLATGRVLEHWHTGSMTARVPELY 736
Cdd:PRK13532 661 PVVDGKETLWRYREGYDPYVKAGEGFKFYGKPDGKAVIFALPYEPPAESPDEEYDLWLSTGRVLEHWHTGSMTRRVPELY 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 737 KAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRNKPPQGLVFVPFFDANKLINKVTLDATDPISKQTDY 816
Cdd:PRK13532 741 RAFPEAVCFMHPEDAKARGLRRGDEVKVVSRRGEVKSRVETRGRNKPPRGLVFVPFFDAAQLINKLTLDATDPLSKQTDF 820
|
....*...
gi 15596371 817 KKCAVRIE 824
Cdd:PRK13532 821 KKCAVKIE 828
|
|
| NAPA |
TIGR01706 |
periplasmic nitrate reductase, large subunit; This model represents the large subunit of a ... |
17-824 |
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: 1574.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 17 GLPILVRASNLVTEADVTSLVWNKAPCRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTR 96
Cdd:TIGR01706 21 GLSLPAQAANMVGGQEETAIKWDKAPCRFCGTGCGVMVGVKDGRVVATQGDPAAPVNRGLNCIKGYFLSKIMYGQDRLTQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 97 PLLRMKDGKFDKQGEFQPISWEQAFDIMAEKFKAALKAKGPESVGMFGSGQWTVWEGYAANKLFKAGLRSNNIDPNARHC 176
Cdd:TIGR01706 101 PLLRMKDGKYDKDGEFTPVSWDQAFDEMEEQFKRALKEKGPTAIGMFGSGQWTIWEGYAALKLMKAGFRSNNIDPNARHC 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 177 MASAVMGFMRSFGMDEPMGCYDDIEATDSFVLWGSNMAEMHPVLWSRVTDRRLSAPQVKVAVLSTFEHRSFELADLPMVF 256
Cdd:TIGR01706 181 MASAVVGFMRTFGMDEPMGCYDDFEAADAFVLWGSNMAEMHPILWTRVTDRRLSHPKVKVVVLSTFTHRSFDLADIGIIF 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 257 KPQTDLIILNYIANHIIESGAVNRDFVERHVRFAHGAEDIGYGLRPDDPLEKKAKNADKANTWSDIDFKAFAEFVKPYTL 336
Cdd:TIGR01706 261 KPQTDLAILNYIANYIIQNNAVNMDFVNKHTVFKTGATDIGYGLRPDHPLEKAAKNADDPAATSLSTFEEFKKFVAPYTL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 337 ERTARESGVPAERLKALAELYADPKRKVVSFWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPFSLTGQPSACGTAR 416
Cdd:TIGR01706 341 EKTSELSGVPKAKLEQLAELYADPNRKVMSLWTMGFNQHTRGVWANNMVYNLHLLTGKIATPGNSPFSLTGQPSACGTAR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 417 EVGTFSHRLPADLVVTNPKHRETAEKIWKVPAGTIQEKVGFHAVQQSRMLKDGVLNVYWTQVSNNMQAGPNVMQEVLPGW 496
Cdd:TIGR01706 421 EVGTFSHRLPADMVVTNPKHREIAEKIWKIPAGTIPEKPGLHAVAQDRALKDGKLNFYWVQVNNNMQAGPNINEERLPGY 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 497 RNPDNFVIVSDVYPTVSAQAADLILPSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDLWQLVEFSKRFTTDEVWPAE 576
Cdd:TIGR01706 501 RNPDNFIVVSDAYPTVTALAADLILPSAMWVEKEGAYGNAERRTQVWHQQVLAPGEARSDLWQLVEFSKRFKTEEVWPEE 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 577 LLAKAPELKGKTLYDVLFRNGQVDRFPASDLAKGYANDEVDAFGFYIQKGLFEEYAAFGRGHGHDLAPFDAYHEARGLRW 656
Cdd:TIGR01706 581 LLAKKPEYRGKTLYDVLFANGEVDKFPLSEANAKSLNAESTAFGFYVQKGLFEEYAKFGRGHGHDLAPFDTYHKVRGLRW 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 657 PVVDGKETRWRYREGYDPYVSKGSGVQFYGYPDKKAIVFALPYEPPAEAPDQDYPFWLATGRVLEHWHTGSMTARVPELY 736
Cdd:TIGR01706 661 PVVNGKETQWRYREGSDPYVKAGAGFQFYGNPDGKAVIFALPYEPPAERPDEEYPLWLVTGRVLEHWHSGSMTRRVPELY 740
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 737 KAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRNKPPQGLVFVPFFDANKLINKVTLDATDPISKQTDY 816
Cdd:TIGR01706 741 RAFPEALCFMHPEDAKALGLRRGDEVWVVSRRGEVRSRVETRGRNKPPRGLVFVPWFDASQLINKVTLDATDPLSKQTDF 820
|
....*...
gi 15596371 817 KKCAVRIE 824
Cdd:TIGR01706 821 KKCAVKIY 828
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
40-702 |
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: 772.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 40 KAPCRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRMKDGkfdkqgEFQPISWEQ 119
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRRNGG------ELVPVSWDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 120 AFDIMAEKFKAALKAKGPESVGMFGSGQWTVWEGYAANKLFKAGLRSNNIDPNARHCMASAVMGFMRSFGMDEPMGCYDD 199
Cdd:cd02754 75 ALDLIAERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGADGPPGSYDD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 200 IEATDSFVLWGSNMAEMHPVLWSRVTDRRLSAPQVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIANHIIESGAVN 279
Cdd:cd02754 155 IEHADCFFLIGSNMAECHPILFRRLLDRKKANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLID 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 280 RDFVERHVRFahgaedigyglrpddplekkaknadkantwsdidFKAFAEFVKPYTLERTARESGVPAERLKALAELYAD 359
Cdd:cd02754 235 RDFIDAHTEG----------------------------------FEELKAFVADYTPEKVAEITGVPEADIREAARLFGE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 360 PkRKVVSFWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPFSLTGQPSAcGTAREVGTFSHRLPADLVVTNPKHRET 439
Cdd:cd02754 281 A-RKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPGSGPFSLTGQPNA-MGGREVGGLANLLPGHRSVNNPEHRAE 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 440 AEKIWKVPAGTIQEKVGFHAVQQSRMLKDGVLNVYWTQVSNNMQAGPNVMQEVLpgWRNPDNFVIVSDVYP-TVSAQAAD 518
Cdd:cd02754 359 VAKFWGVPEGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTNPAVSLPNANRVRE--ALERLEFVVVQDAFAdTETAEYAD 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 519 LILPSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDLWQLVEFSKRFTTDEvwpaellakapelkgktlydvlfrngq 598
Cdd:cd02754 437 LVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILADVARRLGFGE--------------------------- 489
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 599 vdrfpasdlakgyandevdAFGFYIQKGLFEEYAAFGRGHGHDLAPFDaYHEAR--GLRWPVVDG-KETRWRYREGYdpy 675
Cdd:cd02754 490 -------------------LFPYTSPEEVFEEYRRLSRGRGADLSGLS-YERLRdgGVQWPCPDGpPEGTRRLFEDG--- 546
|
650 660
....*....|....*....|....*..
gi 15596371 676 vskgsgvqFYGYPDKKAIVFALPYEPP 702
Cdd:cd02754 547 --------RFPTPDGRARFVAVPYRPP 565
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
43-824 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 628.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRmkdgkfdKQGEFQPISWEQAFD 122
Cdd:COG3383 11 CPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIR-------RGGEFREVSWDEALD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 123 IMAEKFKAALKAKGPESVGMFGSGQWTVWEGYAANKLFKAGLRSNNIDPNARHCMASAVMGFMRSFGMDEPMGCYDDIEA 202
Cdd:COG3383 84 LVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPPNSYDDIEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 203 TDSFVLWGSNMAEMHPVLWSRVTDRRlsAPQVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIANHIIESGAVNRDF 282
Cdd:COG3383 164 ADVILVIGSNPAEAHPVLARRIKKAK--KNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLVDEDF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 283 VERHVRfahgaedigyglrpddplekkaknadkantwsdiDFKAFAEFVKPYTLERTARESGVPAERLKALAELYADPKR 362
Cdd:COG3383 242 IAERTE----------------------------------GFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 363 kVVSFWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPFSLTGQPSACGtAREVGTFSHRLPADLVVTNPKHRETAEK 442
Cdd:COG3383 288 -AMILWGMGVNQHTQGTDNVNAIINLALATGNIGRPGTGPFPLTGQNNVQG-GRDMGALPNVLPGYRDVTDPEHRAKVAD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 443 IWKVPAgtIQEKVGFHAVQQSRMLKDGVLNVYWTQVSNNMQAGPNVmQEVLPGWRNPDnFVIVSDVYPTVSAQAADLILP 522
Cdd:COG3383 366 AWGVPP--LPDKPGLTAVEMFDAIADGEIKALWIIGENPAVSDPDA-NHVREALEKLE-FLVVQDIFLTETAEYADVVLP 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 523 SAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDLWQLVEFSKRF-------TTDEVWpAELLAKAPELKGKTlydvlfr 595
Cdd:COG3383 442 AASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARRLgygfdydSPEEVF-DEIARLTPDYSGIS------- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 596 ngqvdrfpasdlakgyandevdafgfyiqkglfeeyaafgrghghdlapFDAYHEARGLRWPV--VDGKETRWRYREGyd 673
Cdd:COG3383 514 -------------------------------------------------YERLEALGGVQWPCpsEDHPGTPRLFTGR-- 542
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 674 pyvskgsgvqFYgYPDKKAIVFALPYEPPAEAPDQDYPFWLATGRVLEHWHTGSMTARVPELYKAVPDALVYMHPEDARQ 753
Cdd:COG3383 543 ----------FP-TPDGKARFVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAAR 611
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596371 754 LKLRRGSEVKVVSRRGEIRARVETRGRNKPpqGLVFVPFFDANKLINKVTLDATDPISKQTDYKKCAVRIE 824
Cdd:COG3383 612 LGIKDGDLVRVSSRRGEVVLRARVTDRVRP--GTVFMPFHWGEGAANALTNDALDPVSKQPEYKACAVRVE 680
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
38-824 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 579.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 38 WNKAPCRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRM-KDGKfdkqGEFQPIS 116
Cdd:COG0243 23 TVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVgPRGS----GKFERIS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 117 WEQAFDIMAEKFKAALKAKGPESVGMFGSG----QWTVWEGYAANKLFKAgLRSNNIDPNARHCMASAVMGFMRSFGMDE 192
Cdd:COG0243 99 WDEALDLIAEKLKAIIDEYGPEAVAFYTSGgsagRLSNEAAYLAQRFARA-LGTNNLDDNSRLCHESAVAGLPRTFGSDK 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 193 PMGCYDDIEATDSFVLWGSNMAEMHPVLWSRVTDRRlSAPQVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIANHI 272
Cdd:COG0243 178 GTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAA-KKRGAKIVVIDPRRTETAAIADEWLPIRPGTDAALLLALAHVL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 273 IESGAVNRDFVERHVrfaHGaedigyglrpddplekkaknadkantwsdidFKAFAEFVKPYTLERTARESGVPAERLKA 352
Cdd:COG0243 257 IEEGLYDRDFLARHT---VG-------------------------------FDELAAYVAAYTPEWAAEITGVPAEDIRE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 353 LAELYAdPKRKVVSFWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPFSLTGqpsacgtarevgtfshrlpadlvvt 432
Cdd:COG0243 303 LAREFA-TAKPAVILWGMGLQQHSNGTQTVRAIANLALLTGNIGKPGGGPFSLTG------------------------- 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 433 npkhretaekiwkvpagtiqekvgfhavqqsRMLKDGV---LNVYWTQVSNNMQAGPNvMQEVLPGWRNPDnFVIVSDVY 509
Cdd:COG0243 357 -------------------------------EAILDGKpypIKALWVYGGNPAVSAPD-TNRVREALRKLD-FVVVIDTF 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 510 PTVSAQAADLILPSAMWVEKEGAFGNAE-RRTQFWHQLVKAPGEAKSDLWQLVEFSKRFTTDEVWPAEllakapelkgkt 588
Cdd:COG0243 404 LTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPWG------------ 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 589 lydvlfrngqvdrfpasdlakgyandevdafgfYIQKGLFEEYAAFGRGHGhdlAPFDAYHEARGLRWPVVDGKetrwRY 668
Cdd:COG0243 472 ---------------------------------RTEEDYLRELLEATRGRG---ITFEELREKGPVQLPVPPEP----AF 511
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 669 REgyDPYVSKGSG-VQFygYPDKKAIVFALPYEPPAE---APDQDYPFWLATGRVLEHWHtgSMTARVPELYKAVPDALV 744
Cdd:COG0243 512 RN--DGPFPTPSGkAEF--YSETLALPPLPRYAPPYEgaePLDAEYPLRLITGRSRDQWH--STTYNNPRLREIGPRPVV 585
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 745 YMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRnkPPQGLVFVPFF-------DANKLINKVTLDATDPISKQTDYK 817
Cdd:COG0243 586 EINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEG--IRPGVVFAPHGwwyepadDKGGNVNVLTPDATDPLSGTPAFK 663
|
....*..
gi 15596371 818 KCAVRIE 824
Cdd:COG0243 664 SVPVRVE 670
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
43-823 |
1.75e-136 |
|
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: 420.72 E-value: 1.75e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRMKDgkfdkqgEFQPISWEQAFD 122
Cdd:TIGR01591 3 CPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGYFAWEFINSKDRLTTPLIREGD-------KFREVSWDEAIS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 123 IMAEKFKAALKAKGPESVGMFGSGQWTVWEGYAANKLFKAGLRSNNIDPNARHCMASAVMGFMRSFGMDEPMGCYDDIEA 202
Cdd:TIGR01591 76 YIAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEIEN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 203 TDSFVLWGSNMAEMHPVLWSRVTDRRLSApqVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIANHIIESGAVNRDF 282
Cdd:TIGR01591 156 ADLIVIIGYNPAESHPVVAQYLKNAKRNG--AKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 283 VERHVRfahgaedigyglrpddplekkaknadkantwsdiDFKAFAEFVKPYTLERTARESGVPAERLKALAELYADPKR 362
Cdd:TIGR01591 234 IEKRTE----------------------------------GFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGS 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 363 KVVSfWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPFSLTGQPSACGTArEVGTFSHRLPADLVVTNPKHRETAEK 442
Cdd:TIGR01591 280 AAIL-WGMGVTQHSQGVETVMALINLAMLTGNIGKPGGGVNPLRGQNNVQGAC-DMGALPDFLPGYQPVSDEEVREKFAK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 443 IW-KVPAGTiqeKVGFHAVQQSRMLKDGVLNVYWTQVSNNMQAGPNVMQeVLPGWRNPDnFVIVSDVYPTVSAQAADLIL 521
Cdd:TIGR01591 358 AWgVVKLPA---EPGLRIPEMIDAAADGDVKALYIMGEDPLQSDPNTSK-VRKALEKLE-LLVVQDIFMTETAKYADVVL 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 522 PSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDLWQLVEFSKRFTTDevW----PAELLAKAPELkgktlydvlfrng 597
Cdd:TIGR01591 433 PAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQELANALGLD--WnynhPQEIMDEIREL------------- 497
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 598 qvdrFPasdLAKGYANDEVDAFGFyiqkglfeeyaafgrghghdlapfdayheargLRWPVV--DGKETRWRYREGYDpy 675
Cdd:TIGR01591 498 ----TP---LFAGLTYERLDELGS--------------------------------LQWPCNdsDASPTSYLYKDKFA-- 536
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 676 vskgsgvqfygYPDKKAIVFALPYEPPAEAPDQDYPFWLATGRVLEHWHTGSMTARVPELYKAVPDALVYMHPEDARQLK 755
Cdd:TIGR01591 537 -----------TPDGKAKFIPLEWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLG 605
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 756 LRRGSEVKVVSRRGEI--RARVEtrgrNKPPQGLVFVPFFDANKLINKVTLDATDPISKQTDYKKCAVRI 823
Cdd:TIGR01591 606 IKDGDLVKVKSRRGEItlRAKVS----DRVNKGAIYITMHFWDGAVNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
43-628 |
1.04e-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: 311.07 E-value: 1.04e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRmkdgkfdKQGEFQPISWEQAFD 122
Cdd:cd02753 4 CPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIR-------KNGKFVEASWDEALS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 123 IMAEKFKAALKAKGPESVGMFGSGQWTVWEGYAANKLFKAGLRSNNIDPNARHCMASAVMGFMRSFGMDEPMGCYDDIEA 202
Cdd:cd02753 77 LVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAMTNSIADIEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 203 TDSFVLWGSNMAEMHPVLWSRVTDRRLSApqVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIANHIIESGAVNRDF 282
Cdd:cd02753 157 ADVILVIGSNTTEAHPVIARRIKRAKRNG--AKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 283 VERHVRFahgaedigyglrpddplekkaknadkantwsdidFKAFAEFVKPYTLERTARESGVPAERLKALAELYADpKR 362
Cdd:cd02753 235 IEERTEG----------------------------------FEELKEIVEKYTPEYAERITGVPAEDIREAARMYAT-AK 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 363 KVVSFWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPFSLTGQPSACGtAREVGTFSHRLPadlvvtnpkhretaek 442
Cdd:cd02753 280 SAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGRPGTGVNPLRGQNNVQG-ACDMGALPNVLP---------------- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 443 iwkvpagtiqekvgfhavqqsrmlkdGVLNVYWTQVSNNMQAGPNVmQEVLPGWRNPDnFVIVSDVYPTVSAQAADLILP 522
Cdd:cd02753 343 --------------------------GYVKALYIMGENPALSDPNT-NHVRKALESLE-FLVVQDIFLTETAELADVVLP 394
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 523 SAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDLWQLVEFSKR-------FTTDEVWpAELLAKAPELKGKTlYDVLFR 595
Cdd:cd02753 395 AASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRlgypgfySHPEEIF-DEIARLTPQYAGIS-YERLER 472
|
570 580 590
....*....|....*....|....*....|....
gi 15596371 596 NGQVdRFPASDLA-KGYANDEVDAFGFYIQKGLF 628
Cdd:cd02753 473 PGGL-QWPCPDEDhPGTPILHTERFATPDGKARF 505
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
43-567 |
1.80e-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: 298.09 E-value: 1.80e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRMKDGkfdkqGEFQPISWEQAFD 122
Cdd:cd00368 4 CPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGR-----GKFVPISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 123 IMAEKFKAALKAKGPESVGMFGSGQWTVWEGYAANKLFkAGLRSNNIDPNARHCMASAVMGfMRSFGMDEPMGCYDDIEA 202
Cdd:cd00368 79 EIAEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLL-RALGSNNVDSHARLCHASAVAA-LKAFGGGAPTNTLADIEN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 203 TDSFVLWGSNMAEMHPVLWSRVTDRRlsAPQVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNyianhiiesgavnrdf 282
Cdd:cd00368 157 ADLILLWGSNPAETHPVLAARLRRAK--KRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALAL---------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 283 verhvrfahgaedigyglrpddplekkaknadkantwsdidfkafaefvkpytLERTARESGVPAERLKALAELYADPKR 362
Cdd:cd00368 219 -----------------------------------------------------AEWAAEITGVPAETIRALAREFAAAKR 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 363 kVVSFWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPFSltgqpsacgtarevgtfshrlpadlvvtnpkhretaek 442
Cdd:cd00368 246 -AVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGLGP-------------------------------------- 286
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 443 iwkvpagtiqekvgfhavqqsrmlkdgvlnvywtqVSNNMQAGPNVmQEVLPGWRNPDnFVIVSDVYPTVSAQAADLILP 522
Cdd:cd00368 287 -----------------------------------GGNPLVSAPDA-NRVRAALKKLD-FVVVIDIFMTETAAYADVVLP 329
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 15596371 523 SAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDLWQLVEFSKRF 567
Cdd:cd00368 330 AATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
93-566 |
3.45e-71 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 238.07 E-value: 3.45e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 93 RLTRPLLRMKDGKFdkqgefQPISWEQAFDIMAEKFKAALKAKGPESVGM-FGSGQWT-VWEGYAANKLFKA--GLRSNN 168
Cdd:pfam00384 1 RLKYPMVRRGDGKF------VRVSWDEALDLIAKKLKRIIKKYGPDAIAInGGSGGLTdVESLYALKKLLNRlgSKNGNT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 169 IDPNARHCMASAVmgfmrSFGMDEPMG-----CYDDIEATDSFVLWGSNMAEMHPVLWSRvTDRRLSAPQVKVAVLSTFE 243
Cdd:pfam00384 75 EDHNGDLCTAAAA-----AFGSDLRSNylfnsSIADIENADLILLIGTNPREEAPILNAR-IRKAALKGKAKVIVIGPRL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 244 HRSFELADLPmvFKPQTDLIILNYIANHIIESGAVNRDFverhvrfahgaedigyglrpddplekkaknadkantwsdid 323
Cdd:pfam00384 149 DLTYADEHLG--IKPGTDLALALAGAHVFIKELKKDKDF----------------------------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 324 fkafaefvkpytlertaresgvpaerlkalaelyadpKRKVVSFWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPF 403
Cdd:pfam00384 186 -------------------------------------APKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWN 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 404 SLTgqpSACGTAREVGtfshrlpadlvvtnpkhretaekiwkvpAGTIQEKVGFHAVQQSRMLKDGVLNVYWTQVSNNMQ 483
Cdd:pfam00384 229 GLN---ILQGAASPVG----------------------------ALDLGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFV 277
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 484 AGPNVMqEVLPGWRNPDNFVIVSDVYPTVSAQAADLILPSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDLWQLVEF 563
Cdd:pfam00384 278 THADEN-RVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRAL 356
|
...
gi 15596371 564 SKR 566
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 ... |
709-824 |
3.07e-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: 3.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 709 DYPFWLATGRVLEHWHTGSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRnkPPQGLV 788
Cdd:cd02791 2 EYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDR--VRPGEV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15596371 789 FVPFFDAN-----KLINKVTLDATDPISKQTDYKKCAVRIE 824
Cdd:cd02791 80 FVPMHWGDqfgrsGRVNALTLDATDPVSGQPEFKHCAVRIE 120
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
709-824 |
1.70e-47 |
|
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: 164.60 E-value: 1.70e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 709 DYPFWLATGRVLEHWHTGSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRNKPpqGLV 788
Cdd:cd00508 2 EYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRP--GTV 79
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15596371 789 FVPFFDANK----LINKVTLDATDPISKQTDYKKCAVRIE 824
Cdd:cd00508 80 FMPFHWGGEvsggAANALTNDALDPVSGQPEFKACAVRIE 119
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
50-644 |
2.20e-45 |
|
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: 170.51 E-value: 2.20e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 50 CSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRmkDGKfdKQGEFQPISWEQAFDIMAEKFK 129
Cdd:cd02766 12 CSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKR--VGR--KGGQWERISWDEALDTIAAKLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 130 AALKAKGPESVGM-FGSGQWTVWEGYAANKLFKAGLRSNNIDP---NARHCMASAVMGfmRSFGMDEpmgcyDDIEATDS 205
Cdd:cd02766 88 EIKAEYGPESILPySYAGTMGLLQRAARGRFFHALGASELRGTicsGAGIEAQKYDFG--ASLGNDP-----EDMVNADL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 206 FVLWGSNMAEMHPVLWSRVTDRRLSApqVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIANHIIESGAVNRDFVER 285
Cdd:cd02766 161 IVIWGINPAATNIHLMRIIQEARKRG--AKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDRDFLAR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 286 HVrfahgaedigyglrpddplekkaknadkantwsdIDFKAFAEFVKPYTLERTARESGVPAERLKALAELYADPKRkvV 365
Cdd:cd02766 239 HT----------------------------------EGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKP--P 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 366 SFWT-MGFNQHTRGvwANNL--IYNIHLLTGKISEPGNSPFSLTGQPsacgtarevgtfshrlpadlvvtnpkhretaek 442
Cdd:cd02766 283 SIRLgYGMQRYRNG--GQNVraIDALPALTGNIGVPGGGAFYSNSGP--------------------------------- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 443 iwkvpagtiqekvgfhavqQSRMLkdgvlnvyWTQVSNNMQAGPNVmQEVLPGWRNPDNFVIVSDVYPTVSAQAADLILP 522
Cdd:cd02766 328 -------------------PVKAL--------WVYNSNPVAQAPDS-NKVRKGLAREDLFVVVHDQFMTDTARYADIVLP 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 523 SAMWVEKEGAFGNaerrtqFWH-------QLVKAPGEAKSDLWQLVEFSKRFT--------TDEVWPAELLAK-APELKG 586
Cdd:cd02766 380 ATTFLEHEDVYAS------YWHyylqynePAIPPPGEARSNTEIFRELAKRLGfgeppfeeSDEEWLDQALDGtGLPLEG 453
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596371 587 KTLYDvLFRNGQVDRFPASDLAKGYANDEvdafgfyiqkGLFEEYAAFGRGHGHDLAP 644
Cdd:cd02766 454 IDLER-LLGPRKAGFPLVAWEDRGFPTPS----------GKFEFYSERAAKRGLPPLP 500
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
43-657 |
9.63e-42 |
|
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: 162.57 E-value: 9.63e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRMkdgkfDKQGEFQPISWEQAFD 122
Cdd:cd02752 4 CPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRA-----PGSGKWEEISWDEALD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 123 IMAEKFKAALKA------------KGPESVGMFGSGQWTVWEGYAANKlFKAGLRSNNIDPNARHCMASAVMGFMRSFGM 190
Cdd:cd02752 79 EIARKMKDIRDAsfveknaagvvvNRPDSIAFLGSAKLSNEECYLIRK-FARALGTNNLDHQARIUHSPTVAGLANTFGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 191 DEPMGCYDDIEATDSFVLWGSNMAEMHPVLWSRVtdrrLSAPQVKVAVLSTFE---HRSFELADLPMVFKPQTDLIILNY 267
Cdd:cd02752 158 GAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWI----LEAKEKNGAKLIVVDprfTRTAAKADLYVPIRSGTDIAFLGG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 268 IANHIIesgavnrdfverhvrfahgaedigyglrpddplekkaknadkantwsdidfkafaefvkPYTLERTARESGVPA 347
Cdd:cd02752 234 MINYII-----------------------------------------------------------RYTPEEVEDICGVPK 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 348 ERLKALAELYA---DPKRKVVSFWTMGFNQHTRGVwANNLIYNI-HLLTGKISEPGNSPFSLTGQPSACGtAREVGTFSH 423
Cdd:cd02752 255 EDFLKVAEMFAatgRPDKPGTILYAMGWTQHTVGS-QNIRAMCIlQLLLGNIGVAGGGVNALRGHSNVQG-ATDLGLLSH 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 424 RLPADLVVTNPkhretaekiwkvpagtiqeKVGFhavQQSRMLKDGVLNVYWTQVSNNMqagpnvMQEVLPGWRNPDNfv 503
Cdd:cd02752 333 NLPGYLGGQNP-------------------NSSF---PNANKVRRALDKLDWLVVIDPF------PTETAAFWKNPGM-- 382
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 504 ivsdvyPTVSAQAADLILPSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDLWQLVEFSKRF---------------- 567
Cdd:cd02752 383 ------DPKSIQTEVFLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRLgflyekeggafpepit 456
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 568 -----TTDEVWPAELlakAPELKGKTLYDVLFRNGQVDRFPASDLAKGYA---NDEVDAFGFYIQKGLFEEYAAFGRGHG 639
Cdd:cd02752 457 kwnygYGDEPTPEEI---AREINGGALTDGYTGQSPERLKAHGQNVHTFDtlrDDGSTACGCWIYSGSYTEEGRMARRDT 533
|
650
....*....|....*...
gi 15596371 640 HDLAPFDAYHearGLRWP 657
Cdd:cd02752 534 SDPDGLGLYP---GWPWP 548
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
43-650 |
1.05e-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: 159.39 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRM-KDGKfdkqGEFQPISWEQAF 121
Cdd:cd02759 4 CPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVgERGE----NKWERISWDEAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 122 DIMAEKFKAALKAKGPESVGM-FGSGQWTVWEGYAANKLFKAGLRSNNIDPNARHC-----MASA-VMGFMRsfGMDEPm 194
Cdd:cd02759 80 DEIAEKLAEIKAEYGPESIATaVGTGRGTMWQDSLFWIRFVRLFGSPNLFLSGESCywprdMAHAlTTGFGL--GYDEP- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 195 gcydDIEATDSFVLWGSNMAEMHPVLWSrVTDRRLSAPQVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIANHIIE 274
Cdd:cd02759 157 ----DWENPECIVLWGKNPLNSNLDLQG-HWLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIIN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 275 SGAVNRDFVERHVrfahgaedigYGlrpddplekkaknadkantwsdidFKAFAEFVKPYTLERTARESGVPAERLKALA 354
Cdd:cd02759 232 EGLYDKDFVENWC----------YG------------------------FEELAERVQEYTPEKVAEITGVPAEKIRKAA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 355 ELYADPKRKVVSfWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGnspfsltgqpsacgtarevgtfshrlpADLVVTNP 434
Cdd:cd02759 278 RLYATAKPACIQ-WGLAIDQQKNGTQTSRAIAILRAITGNLDVPG---------------------------GNLLIPYP 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 435 khretaekiwkvpagtiqekvgfhavqqSRMLkdgvlnvyWTQvSNNMQAGPNVMQEVLPGWRNPDnFVIVSDVYPTVSA 514
Cdd:cd02759 330 ----------------------------VKML--------IVF-GTNPLASYADTAPVLEALKALD-FIVVVDLFMTPTA 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 515 QAADLILPSAMWVEKEGAFGNAERRTQFW--HQLVKAPGEAKSDLWQLVEFSKRFTTDEvwpaellakAPELKGKTLYdv 592
Cdd:cd02759 372 MLADIVLPVAMSLERPGLRGGFEAENFVQlrQKAVEPYGEAKSDYEIVLELGKRLGPEE---------AEYYKYEKGL-- 440
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596371 593 LFRNGQVdrfpasdlakgyandevdafGFYIQKGLFEEYAAFGRGHGHDlaPFDAYHE 650
Cdd:cd02759 441 LRPDGQP--------------------GFNTPTGKVELYSTMLEELGYD--PLPYYRE 476
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
43-566 |
1.02e-38 |
|
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: 150.14 E-value: 1.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRM-KDGKfdkqGEFQPISWEQAF 121
Cdd:cd02755 5 CEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVgERGE----GKFREASWDEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 122 DIMAEKFKAALKAKGPESVGMFGSGQWTVWEgyaaNKLFKAGLRSNNIDPNARHCMAS--AVMGFMRSFGMDEPMgcyDD 199
Cdd:cd02755 81 QYIASKLKEIKEQHGPESVLFGGHGGCYSPF----FKHFAAAFGSPNIFSHESTCLASknLAWKLVIDSFGGEVN---PD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 200 IEATDSFVLWGSNMAE-MHPvlwsrVTDRRLSAPQVKVAVLSTFEHRSFEL---ADLPMVFKPQTDLIILNYIANHIIES 275
Cdd:cd02755 154 FENARYIILFGRNLAEaIIV-----VDARRLMKALENGAKVVVVDPRFSELaskADEWIPIKPGTDLAFVLALIHVLISE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 276 GAVNRDFVERHVrfahgaedigyglrpddplekkakNAdkantwsdidFKAFAEFVKPYTLERTARESGVPAERLKALA- 354
Cdd:cd02755 229 NLYDAAFVEKYT------------------------NG----------FELLKAHVKPYTPEWAAQITDIPADTIRRIAr 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 355 ELYADPKRKVVSFWTMG-FNQHTRGVWANNLIYNIhlLTGKISEPGNSPFSLTGQPsacgtAREVGTFSHRlpadlvvTN 433
Cdd:cd02755 275 EFAAAAPHAVVDPGWRGtFYSNSFQTRRAIAIINA--LLGNIDKRGGLYYAGSAKP-----YPIKALFIYR-------TN 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 434 PKHRETAEKIWKvpagtiqekvgfhavqqsRMLKdgvlnvywtqvsnNMqagpnvmqevlpgwrnpdNFVIVSDVYPTVS 513
Cdd:cd02755 341 PFHSMPDRARLI------------------KALK-------------NL------------------DLVVAIDILPSDT 371
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596371 514 AQAADLILPSAMWVEKEGAFGNAERRTQFWHQLVKAP---GEAKSDLWQLVEFSKR 566
Cdd:cd02755 372 ALYADVILPEATYLERDEPFSDKGGPAPAVATRQRAIeplYDTRPGWDILKELARR 427
|
|
| arsenite_ox_L |
TIGR02693 |
arsenite oxidase, large subunit; This model represents the large subunit of an arsenite ... |
72-814 |
1.11e-36 |
|
arsenite oxidase, large subunit; This model represents the large subunit of an arsenite oxidase complex. The small subunit is a Rieske protein. Homologs to both large and small subunits that score in the gray zone between the set trusted and noise bit score cutoffs for the respective models are found in Aeropyrum pernix K1 and in Sulfolobus tokodaii str. 7. This enzyme acts in energy metabolim by arsenite oxidation, rather than detoxification by reduction of arsenate to arsenite prior to export. [Energy metabolism, Electron transport]
Pssm-ID: 274261 [Multi-domain] Cd Length: 806 Bit Score: 148.53 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 72 VNRGINCVKGYFLSKIMYGSDRLTRPllRMKDGKFDKQGEFQPISWEQAFDIMAEKFKAALKAKGPES--VGMF---GSG 146
Cdd:TIGR02693 89 VNSGLGSVRGGRMAETSFSEDRNTQD--RLTYPLVWRGDQMQPTSWDDALDLVARLTKKIVDEKGEDDiiVSAFdhgGAG 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 147 QwTVWEGYAANKLFKAGLRSNNIDPNARHCMASAVMGfMRSFGMDEPMGCYDDIEATDSFVLWGSNMAEMHPVLW----- 221
Cdd:TIGR02693 167 G-GFENTWGTGKLYFEAMKVKNIRIHNRPAYNSEVHG-TREMGVGELNNCYEDAELADTIVAVGTNAYETQTNYFlnhwl 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 222 -----SRVTDRRLSAPQ--VKVAVLSTFEHR---SFELAD-------LPMVFKPQTDLIILNYIANHIIESGAVNRDFVE 284
Cdd:TIGR02693 245 pnlrgETLGKKKQLFPGepHEPGRIIIVDPRrtvSVNAAEqtaadrvLHLAINSGTDLALFNALFTYVADKGWVDRDFID 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 285 RHVRFAhGAEDIGYGLRpddplekkaknadkantwsdidfkafaefvkpYTLERTARESGVPAERLKALAELYADPK--- 361
Cdd:TIGR02693 325 KSGHLS-SFEDAVKGCR--------------------------------MSIAEAARITGVSAAQIIKAAEWIGKPKagg 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 362 --RKVVSFWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPFSLTG------QPSACGTAREV-----------GTFS 422
Cdd:TIGR02693 372 krRRTMFGYEKGIIWGNDNYRTNGALVNLALATGNIGRPGTGCVRLGGhqegyvRPPDAHVGGPAayvdqlliggkGGVH 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 423 HRLPADLVVTNPKHRETAEKIWKvpagtiqekvgfhavqQSRMLKDGvlnvywtqvsnnMQAGP-----NVMQEVLPGWR 497
Cdd:TIGR02693 452 HIWGCDHYKTTLNAQEFRRVYKK----------------RTDMVKDA------------MSAAPygdreEMVNAIVDAIN 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 498 NPDNFVIVSDVYPTVSAQAADLILPSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDLwqlvefskrfttdevwpaeL 577
Cdd:TIGR02693 504 QGGLFAVNVDIYPTKIGEAAHLILPAATSGEMNLTSMNGERRMRLTEKFMDPPGQAMPDC-------------------L 564
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 578 LAKAPELKGKTLYDVLFRNGQVDRFPASDlakgYANDEvDAF--GFYIQKGLFEEYAAFGRGHGHDLAPFDAYHEA--RG 653
Cdd:TIGR02693 565 IAARLANTMERVYTAEGKVEYAKQFKGFD----WKTEE-DAFmdGYNKNRDNTVEDEAAHGGENYKFVTYELLSAMgtNG 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 654 LRWPVV---DGK--ETRWRYREGYdpyvskgsgvqfYGYPDKKAIVFALPYE----PPAEAPDQDYPFWLATGRVLEHWH 724
Cdd:TIGR02693 640 FQEPATrftDGKieGTQRLYTDGV------------FSTDDGKARFMDAPWRglpaPGKQQQKDKHKFWINNGRANVVWQ 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 725 TGSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRNKPpqGLVFVPFFDANKLINKVTL 804
Cdd:TIGR02693 708 SAYHDQENDFVMDRFPLPYIEMNPEDAAELGLKEGDLVEVYNDAGATQAMAYPTPTAKP--GETFMLFGFPTGVQGNVTT 785
|
810
....*....|....
gi 15596371 805 DATD----PISKQT 814
Cdd:TIGR02693 786 AGTDeliiPNYKGT 799
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
709-824 |
2.26e-36 |
|
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: 132.75 E-value: 2.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 709 DYPFWLATGRVLEHWHTGSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVetRGRNKPPQGLV 788
Cdd:cd02790 2 EYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRA--RVTDRVPEGVV 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 15596371 789 FVPFFDANKLINKVTLDATDPISKQTDYKKCAVRIE 824
Cdd:cd02790 80 FMPFHFAEAAANLLTNAALDPVAKIPEFKVCAVRVE 115
|
|
| formate-DH-alph |
TIGR01553 |
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase ... |
19-824 |
3.16e-33 |
|
formate dehydrogenase-N alpha subunit; This model describes a subset of formate dehydrogenase alpha chains found mainly in proteobacteria but also in Aquifex. 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 of 32 and 20 kDa. 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 electrons are utilized mainly in the nitrate respiration by nitrate reductase. In E. coli and Salmonella, there are two forms of the formate dehydrogenase, one induced by nitrate which is strictly anaerobic (fdn), and one incuced during the transition from aerobic to anaerobic growth (fdo). This subunit is one of only three proteins in E. coli which contain selenocysteine. This model is well-defined, with a large, unpopulated trusted/noise gap. [Energy metabolism, Anaerobic, Energy metabolism, Electron transport]
Pssm-ID: 273689 [Multi-domain] Cd Length: 1009 Bit Score: 138.12 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 19 PILVRASNL-VTEADVTslvwnKAPCRFCGTGCSVMVATRDG-------QVVATHGDIKAEVNRGINCVKGYFLSKIMYG 90
Cdd:TIGR01553 29 PAKAQARALkTVDAKQT-----TSVCCYCSVSCGLLVYSSSHtgdnktnRAIHVEGDPDHPINRGSLCPKGASTWDLVNN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 91 SDRLTRPLLRMKDGKfdkqgEFQPISWEQAFDIMAEKFKAALKA-------KGP-----ESVGMFGSGQWTVWEGYAANK 158
Cdd:TIGR01553 104 ERRPANPLYRAPGSD-----QWEEISWDWAIDTIARRVKDTRDAtfvtkdaKGQvvnrcDGIASVGSSAMDNEECWLYQK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 159 LFKAgLRSNNIDPNARHCMASAVMGFMRSFGMDEPMGCYDDIEATDSFVLWGSNMAEMHPVLWSRVTDRRLSApqVKVAV 238
Cdd:TIGR01553 179 WLRS-LGLFYIEHQARIUHSPTVASLAPSFGRGAMTNNWVDIKNSDLILVMGGNPAENHPIGFKWAIRAKKKG--AKIIH 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 239 LSTFEHRSFELADLPMVFKPQTDLIILNYIANHIIESGAVNRDFVERHVrfaHGAEDIGYGLRPDDPL----EKKAKNAD 314
Cdd:TIGR01553 256 IDPRFNRTATVADLYAPIRSGSDIAFLNGMIKYILEKELYQKEYVVNYT---NASFIVGEGFAFEDGLfagyNKETRKYD 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 315 K--------ANTWSDID---------FKAFAEFVKPYTLERTARESGVPAERLKALAELYAD---PKRKVVSFWTMGFNQ 374
Cdd:TIGR01553 333 KskwgyefdENGNPKRDetlkhprcvFNILKEHYSRYTPEKVSAICGTPKELFLKVYEEYCKtgkPNKAMTILYALGWTQ 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 375 HTRGVWANNLIYNIHLLTGKISEPGNSPFSLTGQPSACGTArEVGTFSHRLPADLVVTNPKHRETAEKIWK------VP- 447
Cdd:TIGR01553 413 HSVGTQNIRAMSINQLLLGNIGVPGGGINALRGHSNVQGST-DHGLLMHILPGYLGTPRASIPTYEQYTKKftpvskDPq 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 448 ----------------------AGTIQEKVGFHAVQQSRMLKD-----------GVLNVYWTQVSNNMQAGPN------- 487
Cdd:TIGR01553 492 sanywsnfpkffasyiksmwgdAATNENGWAYDYLPKGEDGYDswltlfddmfqGKIKGFFAWGQNPLNSGPNsnktrea 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 488 ------------VMQEVLPGWRNPDnfvivsdVYPTvSAQAADLILPSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKS 555
Cdd:TIGR01553 572 ltklkwmvvmdpFDNETGSFWRGPG-------MDPK-EIKTEVFFLPTAVFIEKEGSISNSGRWMQWRYKGPDPPGNAIP 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 556 DLWQLVEFSKRFTtdevwpaELLAKAPELKGKTLYDVLFRNGQVDRFPASDLAK---GYANDEVDAFGFYIQKGlfEEYA 632
Cdd:TIGR01553 644 DGDIIVELAKRVQ-------ELYAKEGGKLAEPVTKLKWDYWVPDHPDAHEIAKeinGYALKDFKVGDVEYKKG--QQIA 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 633 AFGR-------------------GHGHDLAPFDAYHEAR-------GLRWPV------------VDGKE-------TRWR 667
Cdd:TIGR01553 715 TFGHlrddgsttsgcwlytgsytEKGNMAARRDKSDPAGlglypgwTWAWPAnrrvlynrasvdLNGKPwdperalVEWN 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 668 YRE--------GYDPYVSKGSGVQ-FYGYPDKKAIVFAL-------------PYEPPAE-----------------APDQ 708
Cdd:TIGR01553 795 AAEkkwvgdipDYPPTAPPEKGKGaFIMKPEGYGRLFAPgkredgplpehyePMESPVItnpfhpnvlhnptalhyKTDE 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 709 D-------YPFWLATGRVLEHWHTgsMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRN 781
Cdd:TIGR01553 875 KavgdpkrYPFVATTYRLTEHWHT--WTRNTPWLLEAEPQMFCEISEELATEKGIQNGDKVILESVRGKIWAKAIVTKRI 952
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596371 782 KP--PQG----LVFVPF-----FDANK--LINKVTLDATDPISKQTDYKKCAVRIE 824
Cdd:TIGR01553 953 KPlaIQGqqvhMIGIPIhwgwsFLKNGgdATNILTPSVGDPNTGTPETKAFLVNIE 1008
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
43-560 |
1.34e-32 |
|
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: 133.29 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRmkdgkfdKQGEFQPISWEQAFD 122
Cdd:cd02762 4 CILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAALGDYQNDPDRLRTPMRR-------RGGSFEEIDWDEAFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 123 IMAEKFKAALKAKGPESVGMF-GSGQWTVWEGYAANKLFKAGLRSNNIDPNAR-----HCMASAVMgFMRSFGMDEPmgc 196
Cdd:cd02762 77 EIAERLRAIRARHGGDAVGVYgGNPQAHTHAGGAYSPALLKALGTSNYFSAATadqkpGHFWSGLM-FGHPGLHPVP--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 197 ydDIEATDSFVLWGSNMAEMHPVLWSrVTDRR-----LSAPQVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIANH 271
Cdd:cd02762 153 --DIDRTDYLLILGANPLQSNGSLRT-APDRVlrlkaAKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 272 IIESGAVNRDFVERHVrfaHGAEDigygLRPddplekkaknadkantwsdidfkAFAEFvkpyTLERTARESGVPAERLK 351
Cdd:cd02762 230 LLAEGLTDRRFLAEHC---DGLDE----VRA-----------------------ALAEF----TPEAYAPRCGVPAETIR 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 352 ALA-ELYADPkrKVVSFWTMGFNQHTRGV---WANNLIYnihLLTGKISEPGnspfsltgqpsacgtarevGTFSHRLPA 427
Cdd:cd02762 276 RLArEFAAAP--SAAVYGRLGVQTQLFGTlcsWLVKLLN---LLTGNLDRPG-------------------GAMFTTPAL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 428 DLVVtNPKHRETAEKIWKVPAGTIQEKVGFH--AVQQSRMLKDGVLNV--YWTQVSNNMQAGPN--VMQEVLPGWrnpdN 501
Cdd:cd02762 332 DLVG-QTSGRTIGRGEWRSRVSGLPEIAGELpvNVLAEEILTDGPGRIraMIVVAGNPVLSAPDgaRLEAALGGL----E 406
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596371 502 FVIVSDVYPTVSAQAADLILPSAMWVEKEGA-FGNAE---RRTQFWHQLVKAPGEAKSDlWQL 560
Cdd:cd02762 407 FMVSVDVYMTETTRHADYILPPASQLEKPHAtFFNLEfprNAFRYRRPLFPPPPGTLPE-WEI 468
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
38-609 |
3.78e-29 |
|
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: 122.55 E-value: 3.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 38 WNKAPCRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRM-KDGKFDKQGEFQPIS 116
Cdd:cd02757 1 WVPSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKGHLGLQQVYDPDRILYPMKRTnPRKGRDVDPKFVPIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 117 WEQAFDIMAEKFKAALKAKGPESVgMFGSGQWTVWEGYAANKLFKAGLRSNNIDpnarHcmaSAVMGFMRSFGMDEPMGC 196
Cdd:cd02757 81 WDEALDTIADKIRALRKENEPHKI-MLHRGRYGHNNSILYGRFTKMIGSPNNIS----H---SSVCAESEKFGRYYTEGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 197 YD----DIEATDSFVLWGSN-MAEMHPV-LWSRVTDRrlSAPQVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIAN 270
Cdd:cd02757 153 WDynsyDYANAKYILFFGADpLESNRQNpHAQRIWGG--KMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 271 HIIESGAVNRDFVErhvRFAHGAEDIGYGlRPDDPlekkaknADKANTWSDIDFKAFAEFVKPYTLERTARESGVPAERL 350
Cdd:cd02757 231 VILTEGLWDKDFVG---DFVDGKNYFKAG-ETVDE-------ESFKEKSTEGLVKWWNLELKDYTPEWAAKISGIPAETI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 351 KALAELYADPKRKVVSFWTMGFNQHTRGVWANNLIYNIHLLTGKISEPGnspfsltgqpsacgtarevGTFSHRlpadlv 430
Cdd:cd02757 300 ERVAREFATAAPAAAAFTWRGATMQNRGSYNSMACHALNGLVGSIDSKG-------------------GLCPNM------ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 431 vtnpkhretaekiwkvpagtiqekvgfhavqqsrmlKDGVLNVYWTQVSNnmqagpnvmqevlPGWRNPDNFV------- 503
Cdd:cd02757 355 ------------------------------------GVPKIKVYFTYLDN-------------PVFSNPDGMSweealak 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 504 --IVSDVYPTVSAQA--ADLILPSAMWVEKEG---AFGNAERRTQFWHQLVKAPGEAKSD---LWQLVE----------- 562
Cdd:cd02757 386 ipFHVHLSPFMSETTyfADIVLPDGHHFERWDvmsQENNLHPWLSIRQPVVKSLGEVREEteiLIELAKkldpkgsdgmk 465
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596371 563 ---FSKRFTTDE----VWPAELLAKAP----ELKGKTLYDVLFRNGQVDRFPASDLAK 609
Cdd:cd02757 466 ryaPGQFKDPETgknnRWEFENVFPTEtgkfEFYSETLKKYLQNHADKKKVSWDEVME 523
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
80-399 |
9.33e-27 |
|
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: 115.87 E-value: 9.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 80 KGYFLSKImygsDRLTRPLLRmkDGKFDKqgeFQPISWEQAFDIMAEKfkaaLKAKGPESVGMFGSGQwTVWEGYAANKL 159
Cdd:cd02767 55 SDYELEHL----GRLTYPMRY--DAGSDH---YRPISWDEAFAEIAAR----LRALDPDRAAFYTSGR-ASNEAAYLYQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 160 FKAGLRSNNIDPNARHCMASAVMGFMRSFGMDEPMGCYDDIEATDSFVLWGSNMAEMHPVLWSRVtdRRLSAPQVKVAVL 239
Cdd:cd02767 121 FARAYGTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHTDLIFFIGQNPGTNHPRMLHYL--REAKKRGGKIIVI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 240 STFEHRSFE-----------------LADlpMVFKPQT--DLIILNYIANHIIES-----GAVNRDFVERHvrfAHGAED 295
Cdd:cd02767 199 NPLREPGLErfanpqnpesmltggtkIAD--EYFQVRIggDIALLNGMAKHLIERddepgNVLDHDFIAEH---TSGFEE 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 296 igyglrpddpLEKKAKNADkantWSDIDfkafaefvkpytlertaRESGVPAERLKALAELYADPKRKVVSfWTMGFNQH 375
Cdd:cd02767 274 ----------YVAALRALS----WDEIE-----------------RASGLSREEIEAFAAMYAKSERVVFV-WGMGITQH 321
|
330 340
....*....|....*....|....
gi 15596371 376 TRGVWANNLIYNIHLLTGKISEPG 399
Cdd:cd02767 322 AHGVDNVRAIVNLALLRGNIGRPG 345
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
712-820 |
1.87e-26 |
|
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: 104.28 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 712 FWLATGRVLEHWHTGSMTARVPELYKAVPDAlVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRnkPPQGLVFVP 791
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEV-VEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDR--VRPGVVFMP 77
|
90 100 110
....*....|....*....|....*....|...
gi 15596371 792 FFDANKL----INKVTLDATDPISKQTDYKKCA 820
Cdd:pfam01568 78 FGWWYEPrggnANALTDDATDPLSGGPEFKTCA 110
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
709-824 |
9.78e-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: 99.99 E-value: 9.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 709 DYPFWLATGRVLEHWHTGSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRNKPPQglV 788
Cdd:cd02792 2 EFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHE--V 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15596371 789 FVPF-FDANKL-----INKVTLDATDPISKQTDYKKCAVRIE 824
Cdd:cd02792 80 GIPYhWGGMGLvigdsANTLTPYVGDPNTQTPEYKAFLVNIE 121
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
46-604 |
2.70e-24 |
|
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: 108.47 E-value: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 46 CGTGCSVMVATRDGQVVATHGDIKAEVNrgiNCVKGYFLSKIMYGSDRLTRPLLRM-KDGKFDK------QGEFQPISWE 118
Cdd:cd02751 3 ACHWGPFKAHVKDGVIVRVEPDDTDQPR---PCPRGRSVRDRVYSPDRIKYPMKRVgWLGNGPGsrelrgEGEFVRISWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 119 QAFDIMAEKFKAALKAKGPESVgMFGSGQWTVWEGY-AANKLFK-----AG--LRSNNIDPNArhcmASAVmGFMRSFGM 190
Cdd:cd02751 80 EALDLVASELKRIREKYGNEAI-FGGSYGWASAGRLhHAQSLLHrflnlIGgyLGSYGTYSTG----AAQV-ILPHVVGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 191 DEPMGCY---DDI-EATDSFVLWGSNMAEMHPVLWS----RVTDRRLSAPQVKVAVLSTFEHRS---FELAD--LPMvfK 257
Cdd:cd02751 154 DEVYEQGtswDDIaEHSDLVVLFGANPLKTRQGGGGgpdhGSYYYLKQAKDAGVRFICIDPRYTdtaAVLAAewIPI--R 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 258 PQTDLIILNYIANHIIESGAVNRDFVERHvrfAHG-AEDIGYGLRPDDPLEKkaknadkantwsdidfkafaefvkpyTL 336
Cdd:cd02751 232 PGTDVALMLAMAHTLITEDLHDQAFLARY---TVGfDEFKDYLLGESDGVPK--------------------------TP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 337 ERTARESGVPAERLKALAELYADPKRKVVSFWtmGFNQHTRG---VWAnnlIYNIHLLTGKISEPG-NSPFSLTGQPSAC 412
Cdd:cd02751 283 EWAAEITGVPAETIRALAREIASKRTMIAQGW--GLQRAHHGeqpAWM---LVTLAAMLGQIGLPGgGFGFGYGYSNGGG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 413 GTAREVGtfshrLPADLVVTNPkhreTAEKIwkvPAGTIQEkvgfhAVQQ--SRMLKDGVLNVY------WTQVSN---N 481
Cdd:cd02751 358 PPRGGAG-----GPGLPQGKNP----VKDSI---PVARIAD-----ALLNpgKEFTANGKLKTYpdikmiYWAGGNplhH 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 482 MQAGPNVMQevlpGWRNPDnFVIVSDVYPTVSAQAADLILPSAMWVEKE--GAFGNAERRTQF-WHQLVKAPGEAKSDLW 558
Cdd:cd02751 421 HQDLNRLIK----ALRKDE-TIVVHDIFWTASARYADIVLPATTSLERNdiGLTGNYSNRYLIaMKQAVEPLGEARSDYE 495
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 559 QLVEFSKRFTTDEV------------WPAELLAKAPELKGKTL--YDVLFRNGQVDRFPA 604
Cdd:cd02751 496 IFAELAKRLGVEEEftegrdemewleHLYEETRAKAAGPGPELpsFEEFWEKGIVRVPAA 555
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
43-556 |
6.95e-24 |
|
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: 104.67 E-value: 6.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRmkdgkfdKQGEFQPISWEQAFD 122
Cdd:cd02768 4 DVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIK-------KGGKLVPVSWEEALK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 123 IMAEKfkaaLKAKGPESVGMFGSGQWTVWEGYAANKLFKaGLRSNNIDPNARHCMASAVMGFMRSFGMDEPmgcYDDIEA 202
Cdd:cd02768 77 TVAEG----LKAVKGDKIGGIAGPRADLESLFLLKKLLN-KLGSNNIDHRLRQSDLPADNRLRGNYLFNTS---IAEIEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 203 TDSFVLWGSNMAEMHPVLWSRVTdRRLSAPQVKVAVLSTFEHRSfeLADLPMVFKPQTDLIilNYIANhiIESGAVNRDF 282
Cdd:cd02768 149 ADAVLLIGSNLRKEAPLLNARLR-KAVKKKGAKIAVIGPKDTDL--IADLTYPVSPLGASL--ATLLD--IAEGKHLKPF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 283 VERhvrfahgaedigyglrpddplEKKAKNAdkANTWSDIDFKAFAEFVkpytlertaresgvpaerLKALAELYADPKr 362
Cdd:cd02768 222 AKS---------------------LKKAKKP--LIILGSSALRKDGAAI------------------LKALANLAAKLG- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 363 KVVSFWTMGFNQHTRGVWANNLIYNIHLltgKISEPGNSPFSLTGQPsacgtarevgtfshrlpaDLVVTNPkhretaek 442
Cdd:cd02768 260 TGAGLWNGLNVLNSVGARLGGAGLDAGL---ALLEPGKAKLLLLGED------------------ELDRSNP-------- 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 443 iwkvpagtiqekvgfhavQQSRMLKdgvlnvywtqvsnnmqagpnvmqevlpgwrNPDNFVIVSDVYPTVSAQaADLILP 522
Cdd:cd02768 311 ------------------PAAVALA------------------------------AADAFVVYQGHHGDTGAQ-ADVILP 341
|
490 500 510
....*....|....*....|....*....|....
gi 15596371 523 SAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSD 556
Cdd:cd02768 342 AAAFTEKSGTYVNTEGRVQRFKKAVSPPGDARED 375
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
46-574 |
1.53e-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: 106.02 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 46 CGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRMKDGKfdkQGEFQPISWEQAFDIMA 125
Cdd:cd02765 8 CGGRCPLKCHVRDGKIVKVEPNEWPDKTYKRGCTRGLSHLQRVYSPDRLKYPMKRVGERG---EGKFERITWDEALDTIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 126 EKFKAALKAKGPESVG-MFGSGQWTVWeGYAANKLFKAGLRSN---NIDPNARHCMaSAVMGFMRSFGMDEPmgcyDDIE 201
Cdd:cd02765 85 DKLTEAKREYGGKSILwMSSSGDGAIL-SYLRLALLGGGLQDAltyGIDTGVGQGF-NRVTGGGFMPPTNEI----TDWV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 202 ATDSFVLWGSNMAEMHpvlwsrVTDRR--LSAPQ--VKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIANHIIESGA 277
Cdd:cd02765 159 NAKTIIIWGSNILETQ------FQDAEffLDAREngAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNW 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 278 VNRDFVERH------VRfahgaEDIGYGLRPDDPLEKKAK--------NADKANTWSD--IDFKAFAEF------VKP-- 333
Cdd:cd02765 233 YDEAFLKSNtsapflVR-----EDNGTLLRQADVTATPAEdgyvvwdtNSDSPEPVAAtnINPALEGEYtingvkVHTvl 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 334 ---------YTLERTARESGVPAERLKALAELYAdpKRKVVSFWTMG-----FNQHTRGVWANNLIynihLLTGKISEPG 399
Cdd:cd02765 308 talreqaasYPPKAAAEICGLEEAIIETLAEWYA--TGKPSGIWGFGgvdryYHSHVFGRTAAILA----ALTGNIGRVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 400 nspfsltgqpsacgtarevgtfshrlpadlvvtnpkhretaekiwkvpagtiqekvGFHAvqqsrMLKdgvlnVYWTQVS 479
Cdd:cd02765 382 --------------------------------------------------------GGVG-----QIK-----FMYFMGS 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 480 N--NMQAGPNVMQEVLPgwrNPDnFVIVSDVYPTVSAQAADLILPSAMWVEKEGAFGNAERRTqfwHQLVKAP-----GE 552
Cdd:cd02765 396 NflGNQPDRDRWLKVMK---NLD-FIVVVDIFHTPTVRYADIVLPAAHWFEVEDLLVRYTTHP---HVLLQQKaieplFE 468
|
570 580
....*....|....*....|..
gi 15596371 553 AKSDLWQLVEFSKRFTTDEVWP 574
Cdd:cd02765 469 SKSDFEIEKGLAERLGLGDYFP 490
|
|
| 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 ... |
43-224 |
1.69e-23 |
|
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: 104.78 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRmkdgkfdKQGEFQPISWEQAFD 122
Cdd:cd02771 4 CHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIR-------RGGTLVPVSWNEALD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 123 IMAEKFKAALKAkgpesVGMFGSGQWTVWEGYAANKLFKAGLRSNNIDPNARHCMASavmgFMRSFGmdEPMGCYDDIEA 202
Cdd:cd02771 77 VAAARLKEAKDK-----VGGIGSPRASNESNYALQKLVGAVLGTNNVDHRARRLIAE----ILRNGP--IYIPSLRDIES 145
|
170 180
....*....|....*....|..
gi 15596371 203 TDSFVLWGSNMAEMHPVLWSRV 224
Cdd:cd02771 146 ADAVLVLGEDLTQTAPRIALAL 167
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
46-571 |
8.54e-23 |
|
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: 103.94 E-value: 8.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 46 CGTGCSVMVATRDGQVV-----ATHGDIKAEVN-RGinCVKGYFLSKIMYGSDRLTRPLLRMkdGKfDKQGEFQPISWEQ 119
Cdd:cd02770 8 CGGRCPLKAHVKDGVITrietdDTGDDDPGFHQiRA--CLRGRSQRKRVYNPDRLKYPMKRV--GK-RGEGKFVRISWDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 120 AFDIMAEKFKAALKAKGPES----VGMFGSGQWTVWEGYAANKLFKAGLRSNNIDPNARHCMASAVMGFmrsFGMDEPMG 195
Cdd:cd02770 83 ALDTIASELKRIIEKYGNEAiyvnYGTGTYGGVPAGRGAIARLLNLTGGYLNYYGTYSWAQITTATPYT---YGAAASGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 196 CYDDIEATDSFVLWGSNMAEM-----HPVLWSRVTDRRlsapQVKVAVLSTFEHRSFE-LAD--LPMvfKPQTDLIILNY 267
Cdd:cd02770 160 SLDDLKDSKLVVLFGHNPAETrmgggGSTYYYLQAKKA----GAKFIVIDPRYTDTAVtLADewIPI--RPGTDAALVAA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 268 IANHIIESGAVNRDFVERHVrfahgaedIGYGlrpDDPLEkkaKNADKANTWSDIDFKAFAEFVkPYTLERTARESGVPA 347
Cdd:cd02770 234 MAYVMITENLHDQAFLDRYC--------VGFD---AEHLP---EGAPPNESYKDYVLGTGYDGT-PKTPEWASEITGVPA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 348 ERLKALAELYADPKRK-VVSFWtmGFNQHTRGVWANNLIYNIHLLTGKISEPGNSPFSLTGQPSACGTArevgtfshrLP 426
Cdd:cd02770 299 ETIRRLAREIATTKPAaILQGW--GPQRHANGEQAARAIMMLAAMTGNVGIPGGNTGARPGGSAYNGAG---------LP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 427 AdlvVTNPkhreTAEKIwkvPAGTIQEkvgfhAVQQSRML---KDGVLNV---------YWTQVSN---NMQAGPNVMQE 491
Cdd:cd02770 368 A---GKNP----VKTSI---PCFMWTD-----AIERGEEMtadDGGVKGAdklksnikmIWNYAGNtliNQHSDDNNTTR 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 492 VLPGWRNPDNFVIVSDVYPTVSAQAADLILPSAMWVEKEG--AFGNAERRTQFWH--QLVKAPGEAKSDLWQLVEFSKRF 567
Cdd:cd02770 433 ALLDDESKCEFIVVIDNFMTPSARYADILLPDTTELEREDivLTSNAGMMEYLIYsqKAIEPLYECKSDYEICAELAKRL 512
|
....
gi 15596371 568 TTDE 571
Cdd:cd02770 513 GVED 516
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
43-774 |
7.18e-22 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 101.28 E-value: 7.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRM-KDGkfdkQGEFQPISWEQAF 121
Cdd:PRK15488 48 CEMCSTRCPIEARVVNGKNVFIQGNPKAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVgERG----EGKWQEISWDEAY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 122 DIMAEKFkAALKAK-GPESVGMFGSGQWTvwEGYAANklFKAGLRSNNIDPNARHCMASAVMGFMRSFGMDEPMgcydDI 200
Cdd:PRK15488 124 QEIAAKL-NAIKQQhGPESVAFSSKSGSL--SSHLFH--LATAFGSPNTFTHASTCPAGYAIAAKVMFGGKLKR----DL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 201 EATDSFVLWGSN------MAEMHPVlwsrvtdrrLSAPQVKVAVLSTFEHRsFEL----ADLPMVFKPQTDLIILNYIAN 270
Cdd:PRK15488 195 ANSKYIINFGHNlyeginMSDTRGL---------MTAQMEKGAKLVVFEPR-FSVvaskADEWHAIRPGTDLAVVLALCH 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 271 HIIESGAVNRDFVERHVrfahgaedigyglrpddplekkaknadkantwsdIDFKAFAEFVKPYTLERTARESGVPAERL 350
Cdd:PRK15488 265 VLIEENLYDKAFVERYT----------------------------------SGFEELAASVKEYTPEWAEAISDVPADDI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 351 KALA-ELYADPKRKVVSF-----WTMGFNQHTRGVW-ANNLIYNIH----LLTGKISEPGNspfSLTGQPSACGTAREvg 419
Cdd:PRK15488 311 RRIArELAAAAPHAIVDFghratFTPEEFDMRRAIFaANVLLGNIErkggLYFGKNASVYN---KLAGEKVAPTLAKP-- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 420 tfshRLPADLVVTNPKHRETAEK---IWK-------VPAGTIQEK-VGFHAVQQSRmlkdgvlnvywtqvSNNMQ--AGP 486
Cdd:PRK15488 386 ----GVKGMPKPTAKRIDLVGEQfkyIAAgggvvqsIIDATLTQKpYQIKGWVMSR--------------HNPMQtvTDR 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 487 NVMQEVLPGWrnpdNFVIVSDVYPTVSAQAADLILPSAMWVEKEGAFGNAERRTQFW---HQLVKAPGEAKSDlWQLV-E 562
Cdd:PRK15488 448 ADVVKALKKL----DLVVVCDVYLSESAAYADVVLPESTYLERDEEISDKSGKNPAYalrQRVVEPIGDTKPS-WQIFkE 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 563 FSKRFTTDEVWPAELLAkapELKgktLYDVlfrNGQVDRFPASdLAKGYAndevdAFGFYIqkgLFEEYAafgrghghDL 642
Cdd:PRK15488 523 LGEKMGLGQYYPWQDME---TLQ---LYQV---NGDHALLKEL-KKKGYV-----SFGVPL---LLREPK--------MV 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 643 APF-DAYHEARGLRWPVVDGKETRWRYREG----YDPYVSKgsgvQFYGYPdkkaivfALPYEPPAEApdQDYPFWLATG 717
Cdd:PRK15488 577 AKFvARYPNAKAVDEDGTYGSQLKFKTPSGkielFSAKLEA----LAPGYG-------VPRYRDVALK--KEDELYFIQG 643
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596371 718 RVLEhwHTGSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRAR 774
Cdd:PRK15488 644 KVAV--HTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGKEKGK 698
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
54-566 |
7.66e-22 |
|
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: 101.02 E-value: 7.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 54 VATRDGQ--VVATHGDIKAEVNRGINCVKGYFLSKIMY------GSDRLTRPLLRmkdgkfdKQGEFQPISWEQAFDIMA 125
Cdd:cd02756 70 VVTQDGRevYIVIVPDKECPVNSGNYSTRGGTNAERIWspdnrvGETRLTTPLVR-------RGGQLQPTTWDDAIDLVA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 126 EKFKAALKAKGPESVGMF------GSGQWTVwEGYAANKLFKAGLRSNNIDPNARHCMASAVMGfMRSFGMDEPMGCYDD 199
Cdd:cd02756 143 RVIKGILDKDGNDDAVFAsrfdhgGGGGGFE-NNWGVGKFFFMALQTPFVRIHNRPAYNSEVHA-TREMGVGELNNSYED 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 200 IEATDSFVLWGSNMAEMHPVLW-------------SRVTDRRLSAPQVKVAVLSTFEHRSFE-------LADLPMVF--- 256
Cdd:cd02756 221 ARLADTIVLWGNNPYETQTVYFlnhwlpnlrgatvSEKQQWFPPGEPVPPGRIIVVDPRRTEtvhaaeaAAGKDRVLhlq 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 257 -KPQTDLIILNYIANHIIESgavNRDFVERhvrfahgAEDIgyglrpddplekkaknadkantwsdidfkafaefvkpyt 335
Cdd:cd02756 301 vNPGTDTALANAIARYIYES---LDEVLAE-------AEQI--------------------------------------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 336 lertareSGVPAERLKALAELYADPK-----RKVVSFWTMGF---NQHTRGVWAnnlIYNIHLLTGKISEPGnspfsltg 407
Cdd:cd02756 332 -------TGVPRAQIEKAADWIAKPKeggyrKRVMFEYEKGIiwgNDNYRPIYS---LVNLAIITGNIGRPG-------- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 408 qpsaCGTAREVGtfshrlpadlvvtnpkHRETAEKIWKVPAGTIQEkvGFHAVQQSRMLKDGVLNVYWTQVSNNMQAGPN 487
Cdd:cd02756 394 ----TGCVRQGG----------------HQEGYVRPPPPPPPWYPQ--YQYAPYIDQLLISGKGKVLWVIGCDPYKTTPN 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 488 -------------------------------VMQEVLPGWRNPDN-FVIVSDVYPTVSAQAADLILPSAMWVE-KEGAFG 534
Cdd:cd02756 452 aqrlretinhrsklvtdaveaalyagtydreAMVCLIGDAIQPGGlFIVVQDIYPTKLAEDAHVILPAAANGEmNETSMN 531
|
570 580 590
....*....|....*....|....*....|..
gi 15596371 535 NAERRTQFWHQLVKAPGEAKSDLWQLVEFSKR 566
Cdd:cd02756 532 GHERRLRLYEKFMDPPGEAMPDWWIAAMIANR 563
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
719-817 |
3.36e-21 |
|
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: 88.92 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 719 VLEHWHTGSMTaRVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRnkPPQGLVFVPF-----F 793
Cdd:cd02775 1 LRDHFHSGTRT-RNPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDG--VPPGVVFLPHgwghrG 77
|
90 100
....*....|....*....|....
gi 15596371 794 DANKLINKVTLDATDPISKQTDYK 817
Cdd:cd02775 78 GRGGNANVLTPDALDPPSGGPAYK 101
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
36-824 |
3.49e-19 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 92.78 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 36 LVWNKAPCRfCGTGCSVMVATRDGQVVATHGDIKAEVN-RGIN----CVKGYFLSKIMYGSDRLTRPLLRMkdGKfDKQG 110
Cdd:PRK14990 58 VIWSACTVN-CGSRCPLRMHVVDGEIKYVETDNTGDDNyDGLHqvraCLRGRSMRRRVYNPDRLKYPMKRV--GA-RGEG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 111 EFQPISWEQAFDIMAEKFKAALKAKGPESVGM-FGSGQW--TVWEGYAANKLFKAGLRS---NNIDPNARHCMASAVMGF 184
Cdd:PRK14990 134 KFERISWEEAYDIIATNMQRLIKEYGNESIYLnYGTGTLggTMTRSWPPGNTLVARLMNccgGYLNHYGDYSSAQIAEGL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 185 MRSFGMDEPMGCYDDIEATDSFVLWGSNMAEMHpVLWSRVTDRRLSAPQVKVAVLSTFEHRSFELA----DLPMVFKPQT 260
Cdd:PRK14990 214 NYTYGGWADGNSPSDIENSKLVVLFGNNPGETR-MSGGGVTYYLEQARQKSNARMIIIDPRYTDTGagreDEWIPIRPGT 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 261 DLIILNYIANHIIESGAVNRDFVERHVrfahgaedIGYGlrpddplEKKAKNADKANTwsdiDFKAFAEFVKPYTLERT- 339
Cdd:PRK14990 293 DAALVNGLAYVMITENLVDQPFLDKYC--------VGYD-------EKTLPASAPKNG----HYKAYILGEGPDGVAKTp 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 340 ---ARESGVPAERLKALAELYADPKRKVVS-FWtmGFNQHTRGVWANNLIYNIHLLTGKIS-EPGNSpfsltgqpsacgT 414
Cdd:PRK14990 354 ewaSQITGVPADKIIKLAREIGSTKPAFISqGW--GPQRHANGEIATRAISMLAILTGNVGiNGGNS------------G 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 415 AREvGTFS---HRLPadlVVTNPKHRETAEKIWkvpAGTIQEKVGFHAVQQSRMLKDGV---LNVYWTQVSN---NMQAG 485
Cdd:PRK14990 420 ARE-GSYSlpfVRMP---TLENPIQTSISMFMW---TDAIERGPEMTALRDGVRGKDKLdvpIKMIWNYAGNcliNQHSE 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 486 PNVMQEVLPGWRNPDnFVIVSDVYPTVSAQAADLILPSAMWVEK-----EGAFGNAErRTQFWHQLVKAPGEAKSDLWQL 560
Cdd:PRK14990 493 INRTHEILQDDKKCE-LIVVIDCHMTSSAKYADILLPDCTASEQmdfalDASCGNMS-YVIFNDQVIKPRFECKTIYEMT 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 561 VEFSKRFTTDEVWPaellakapelKGKTLYDVLFRNGQVDRFPASDLAKgyandevdaFGFYIQKGLFEEYAAfgrgHGH 640
Cdd:PRK14990 571 SELAKRLGVEQQFT----------EGRTQEEWMRHLYAQSREAIPELPT---------FEEFRKQGIFKKRDP----QGH 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 641 DLApFDAYHE---ARGLRWPvvDGK-----------ETRWRYREG--YDPYVSKGSGVQFYGYPDKKaivfalpyeppae 704
Cdd:PRK14990 628 HVA-YKAFREdpqANPLTTP--SGKieiysqaladiAATWELPEGdvIDPLPIYTPGFESYQDPLNK------------- 691
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 705 apdqDYPFWLaTGrvlehWHtgsMTARVPELY------KAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETR 778
Cdd:PRK14990 692 ----QYPLQL-TG-----FH---YKSRVHSTYgnvdvlKAACRQEMWINPLDAQKRGINNGDKVRIFNDRGEVHIEAKVT 758
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596371 779 GRNKP-----PQGLVFVPffDANKL-----INKVTLDATDPISKQTDYKKCAVRIE 824
Cdd:PRK14990 759 PRMMPgvvalGEGAWYDP--DAKRVdkggcINVLTTQRPSPLAKGNPSHTNLVQVE 812
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
40-411 |
4.52e-19 |
|
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: 92.20 E-value: 4.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 40 KAPCRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYflSKIM--YGSDRLTRPLLRMKDgkfDKQGEFQPISW 117
Cdd:cd02763 1 TTTCYMCACRCGIRVHLRDGKVRYIKGNPDHPLNKGVICAKGS--SGIMkqYSPARLTKPLLRKGP---RGSGQFEEIEW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 118 EQAFDIMAEKFKaALKAKGPESVGMF-GSGQWTvwegyAANKLFKAGLRSNNIDPNARHCMASAVMGFMRSFG-----MD 191
Cdd:cd02763 76 EEAFSIATKRLK-AARATDPKKFAFFtGRDQMQ-----ALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLYSIGgsfweFG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 192 EPmgcydDIEATDSFVLWGSnmAEMHPVLWSRVTDRRLSAPQVKVAVLSTFEHRSFELADLPMVFKPQTDLIILNYIANH 271
Cdd:cd02763 150 GP-----DLEHTKYFMMIGV--AEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 272 IIESGAVNRDFVerhVRFAHGAEDIGYGlrPDDPLEKKAKNADkantwsdidfkafaefvkpyTLERTARESGV------ 345
Cdd:cd02763 223 LLKAGLIDWEFL---KRYTNAAELVDYT--PEWVEKITGIPAD--------------------TIRRIAKELGVtardqp 277
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596371 346 ---PAERLKALAELYADPKRKVVSFWTM-GFNQHTRGVWANNLIYNIHLLTGKISEPG----NSPFSLTGQPSA 411
Cdd:cd02763 278 ielPIAWTDVWGRKHEKITGRPVSFHAMrGIAAHSNGFQTIRALFVLMMLLGTIDRPGgfrhKPPYPRHIPPLP 351
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
38-90 |
1.34e-18 |
|
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: 80.03 E-value: 1.34e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15596371 38 WNKAPCRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYG 90
Cdd:pfam04879 3 VVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGYERVYN 55
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
46-567 |
4.89e-17 |
|
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: 84.68 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 46 CGTGCSVMVATRDGQVV---------ATHGDIKAEVNRGinCVKGYFLSKIMYGSDRLTRPLLRM-KDGKfdkqGEFQPI 115
Cdd:cd02750 12 CTGSCSWNVYVKNGIVTreeqatdypETPPDLPDYNPRG--CQRGASFSWYLYSPDRVKYPLKRVgARGE----GKWKRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 116 SWEQAFDIMAEKFKAALKAKGPESVGMFGSGQWTVWEGYAanklfkAGLRsnnidpnarhcMASAVMGFMRSFgmdepmg 195
Cdd:cd02750 86 SWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYA------AGSR-----------FASLIGGVSLSF------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 196 cYDDI------------EATDSF-----------VLWGSNMAEMHPVLWSRVTDRRLSApqVKVAVLSTFEHRSFELADL 252
Cdd:cd02750 142 -YDWYgdlppgspqtwgEQTDVPesadwynadyiIMWGSNVPVTRTPDAHFLTEARYNG--AKVVVVSPDYSPSAKHADL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 253 PMVFKPQTDLIILNYIANHIIESGAVNRDFVERHVrfahgaedigyglrpDDPLekkaknadkantwsdidfkafaeFVk 332
Cdd:cd02750 219 WVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYT---------------DLPF-----------------------LV- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 333 pYTLERTARESGVPAERLKALAELYADPKRKVVsfwTMGF--NQHTRGVWANNLIYNIHLLTGKISEPGNSPFSLTGQPS 410
Cdd:cd02750 260 -YTPAWQEAITGVPRETVIRLAREFATNGRSMI---IVGAgiNHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVGQPR 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 411 acgtarevgtfshrlpadlvvtnpkhretaekiwkvpagtiqekvgfhavqqsrmlkdgVLNVYWtqvsNNMQAGPNVMQ 490
Cdd:cd02750 336 -----------------------------------------------------------VLFVWR----GNLFGSSGKGH 352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 491 EVLPGWRNPD-NFVIVSDVYPTVSAQAADLILPSAMWVEKegafgnAERRT-------QFWHQLVKAPGEAKSDLWQLVE 562
Cdd:cd02750 353 EYFEDAPEGKlDLIVDLDFRMDSTALYSDIVLPAATWYEK------HDLSTtdmhpfiHPFSPAVDPLWEAKSDWEIFKA 426
|
....*
gi 15596371 563 FSKRF 567
Cdd:cd02750 427 LAKKV 431
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
37-142 |
5.22e-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: 81.42 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 37 VW--NKAP--CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRmkdgkfdKQGEF 112
Cdd:COG1034 212 PWelKKTPsiCPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVR-------KDGEL 284
|
90 100 110
....*....|....*....|....*....|
gi 15596371 113 QPISWEQAFDIMAEKFKAALKAKGpeSVGM 142
Cdd:COG1034 285 VEASWEEALAAAAEGLKALKKAEN--SVGA 312
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
36-240 |
4.52e-14 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 76.14 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 36 LVWNKAPCRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMYGSDRLTRPLLRmkdgkfDKQGEFQPI 115
Cdd:PRK07860 221 LVSTPSVCEHCASGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTYATQPDRITTPLVR------DEDGELEPA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 116 SWEQAFDIMAEKFKAALkakgpESVGMFGSGQWTVWEGYAANKLFKAGLRSNNIDPNAR-------HCMASAVMGfmRSF 188
Cdd:PRK07860 295 SWSEALAVAARGLAAAR-----GRVGVLVGGRLTVEDAYAYAKFARVALGTNDIDFRARphsaeeaDFLAARVAG--RGL 367
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 15596371 189 GMDepmgcYDDIEATDSFVLWGSNMAEMHPVLWSRVtdrRLSAPQVKVAVLS 240
Cdd:PRK07860 368 GVT-----YADLEKAPAVLLVGFEPEEESPIVFLRL---RKAARKHGLKVYS 411
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
93-419 |
4.51e-13 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 73.16 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 93 RLTRPLlrmkdgKFDKQGE-FQPISWEQAFDIMAEKFKAalkAKGPESVGMFGSGQwTVWEGYAANKLFKAGLRSNNIDP 171
Cdd:PRK09939 108 RLTQPL------KYDAVSDcYKPLSWQQAFDEIGARLQS---YSDPNQVEFYTSGR-TSNEAAFLYQLFAREYGSNNFPD 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 172 NARHCMASAVMGFMRSFGMDEPMGCYDDIEATDSFVLWGSNMAEMHPVLWSRVtdRRLSAPQVKVAVLSTFEHRSFELAD 251
Cdd:PRK09939 178 CSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSL--RALVKRGAKMIAINPLQERGLERFT 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 252 LP-----MVFKPQTDLIILNY---IANHIIESGAVNRDFVERHvrfaHGAEDIGYGLRPDDPLEKK------AKNADKAN 317
Cdd:PRK09939 256 APqnpfeMLTNSETQLASAYYnvrIGGDMALLKGMMRLLIERD----DAASAAGRPSLLDDEFIQThtvgfdELRRDVLN 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 318 T-WSDIDfkafaefvkpytlertaRESGVPAERLKALAELYADPKRKVVSFwTMGFNQHTRGVWANNLIYNIHLLTGKIS 396
Cdd:PRK09939 332 SeWKDIE-----------------RISGLSQTQIAELADAYAAAERTIICY-GMGITQHEHGTQNVQQLVNLLLMKGNIG 393
|
330 340
....*....|....*....|...
gi 15596371 397 EPGNSPFSLTGQPSACGTaREVG 419
Cdd:PRK09939 394 KPGAGICPLRGHSNVQGD-RTVG 415
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
710-823 |
4.32e-12 |
|
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: 63.63 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 710 YPFWLATGRVLEHWHTGSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRNKPpqGLVF 789
Cdd:cd02779 1 YKYWVNNGRANIIWQTAYHDQNNSEIAERVPLPYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKP--GQTF 78
|
90 100 110
....*....|....*....|....*....|....
gi 15596371 790 VPFFDANKLINKVTLDATDPISKQTDYKKCAVRI 823
Cdd:cd02779 79 MLMAHPRPGANGLVTPYVDPETIIPYYKGTWANI 112
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
88-224 |
5.81e-12 |
|
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: 68.53 E-value: 5.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 88 MYGSDRLTRPLLRmkdgkfdKQGEFQPISWEQAFDIMAEKFKAALKAKGPESVGMFGSGQWTVWEGYAANKLFkAGLRSN 167
Cdd:cd02772 49 LNSEDRLTKPMIK-------KDGQWQEVDWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLA-RGLGSD 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596371 168 NIDPNARHCMASAVMgfmrSFGMDEPMGC-YDDIEATDSFVLWGSNMAEMHPVLWSRV 224
Cdd:cd02772 121 NIDHRLRQSDFRDDA----KASGAPWLGMpIAEISELDRVLVIGSNLRKEHPLLAQRL 174
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
43-89 |
7.34e-12 |
|
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: 60.73 E-value: 7.34e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15596371 43 CRFCGTGCSVMVATRDGQVVATHGDIKAEVNRGINCVKGYFLSKIMY 89
Cdd:smart00926 8 CPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVY 54
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
498-582 |
1.45e-11 |
|
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: 67.56 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 498 NPDNFVIVSDVYPTVSAQAADLILPSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDlWQLV-----EFSKRF---TT 569
Cdd:COG1034 356 AKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPD-WRVLralanALGAGLpydSL 434
|
90
....*....|...
gi 15596371 570 DEVWpAELLAKAP 582
Cdd:COG1034 435 EEVR-AELAAEAP 446
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
88-572 |
6.80e-10 |
|
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: 62.67 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 88 MYGSDRLTRPLLR---MKDGKFDK-----QGEFQPISWEQAFDIMAEKFKAALKAKGPESV----------GMFGSGQWT 149
Cdd:cd02769 41 VYSPTRIKYPMVRrgwLEKGPGSDrslrgKEEFVRVSWDEALDLVAAELKRVRKTYGNEAIfggsygwssaGRFHHAQSL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 150 VWE------GYAAnklfkaglRSNNIDPNARHCMASAVMGFMRSFgmDEPMGCYDDI-EATDSFVLWGSNMAEMHPVLWS 222
Cdd:cd02769 121 LHRflnlagGYVG--------SVGDYSTGAAQVILPHVVGSMEVY--TEQQTSWPVIaEHTELVVAFGADPLKNAQIAWG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 223 RVTD-------RRLSAPQVKVAVLSTFEHRSFELAD---LPMVfkPQTDLIILNYIANHIIESGAVNRDFVERH-VRFAH 291
Cdd:cd02769 191 GIPDhqaysylKALKDRGIRFISISPLRDDTAAELGaewIAIR--PGTDVALMLALAHTLVTEGLHDKAFLARYtVGFDK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 292 GAEdigYGLRPDDpleKKAKNADKAntwsdidfkafaefvkpytlertARESGVPAERLKALAELYADPKRKVVSFWTMG 371
Cdd:cd02769 269 FLP---YLLGESD---GVPKTPEWA-----------------------AAICGIPAETIRELARRFASKRTMIMAGWSLQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 372 FNQHtrG---VWAnnlIYNIHLLTGKISEPGNSpFSLTGQPSACGTAREVGTFSHRL-----PADLVVtnPKHReTAEKI 443
Cdd:cd02769 320 RAHH--GeqpHWM---AVTLAAMLGQIGLPGGG-FGFGYHYSNGGGPPRGAAPPPALpqgrnPVSSFI--PVAR-IADML 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 444 WKvPAGTIQekvgFHAvqQSRMLKDGVLnVYWtqvsnnmqAGPNV------MQEVLPGWRNPDNfVIVSDVYPTVSAQAA 517
Cdd:cd02769 391 LN-PGKPFD----YNG--KKLTYPDIKL-VYW--------AGGNPfhhhqdLNRLIRAWQKPET-VIVHEPFWTATARHA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596371 518 DLILPSAMWVEKEG-AFGNAERRTQFWHQLVKAPGEAKSDLWQLVEFSKRFTTDEV 572
Cdd:cd02769 454 DIVLPATTSLERNDiGGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERLGVEEQ 509
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
711-792 |
7.27e-09 |
|
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: 54.59 E-value: 7.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 711 PFWLATGRVLehWHTGSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRG--EIRARVETRGRNkppqGLV 788
Cdd:cd02778 1 EFRLIYGKSP--VHTHGHTANNPLLHELTPENTLWINPETAARLGIKDGDRVEVSSARGkvTGKARLTEGIRP----DTV 74
|
....
gi 15596371 789 FVPF 792
Cdd:cd02778 75 FMPH 78
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
709-774 |
1.60e-08 |
|
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: 53.85 E-value: 1.60e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596371 709 DYPFWLATG-RVLEHWHtgSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRAR 774
Cdd:cd02781 1 EYPLILTTGaRSYYYFH--SEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQK 65
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
43-146 |
1.93e-08 |
|
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: 58.06 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 43 CRFCGTGCSVM-VATRDGQVVATHGDIKAE---VNRGINCVKGYFLSKIMYGSDRLTRPLLRM--KDGKFDKQGeFQPIS 116
Cdd:cd02760 4 CYNCVAGPDFMaVKVVDGVATEIEPNFAAEdihPARGRVCVKAYGLVQKTYNPNRVLQPMKRTnpKKGRNEDPG-FVPIS 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 15596371 117 WEQAFDIMAEKFKaALKAKG-------PESVGMFGSG 146
Cdd:cd02760 83 WDEALDLVAAKLR-RVREKGlldekglPRLAATFGHG 118
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
73-393 |
2.63e-08 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 57.74 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 73 NRGINCVKGYFLSKIMYGSDRLTRPLLRmkDGKfDKQGEFQPISWEQAFDIMAEK---FKA-------ALKAK------- 135
Cdd:cd02758 63 ARATACARGNAGLQYLYDPYRVLQPLKR--VGP-RGSGKWKPISWEQLIEEVVEGgdlFGEghveglkAIRDLdtpidpd 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 136 ----GPES---VGMFGSGQwtvweG--YAANKLFKAGLRSNNIDPNARHC----MASAVMGFMRSFGMDEPMGCYDDIEa 202
Cdd:cd02758 140 hpdlGPKAnqlLYTFGRDE-----GrtPFIKRFANQAFGTVNFGGHGSYCglsyRAGNGALMNDLDGYPHVKPDFDNAE- 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 203 tdsFVL-WGSNMAEMHPVLWS---RVTDRRLSaPQVKVAVLSTFEHRSFELAD-----LPMvfKPQTDLIILNYIANHII 273
Cdd:cd02758 214 ---FALfIGTSPAQAGNPFKRqarRLAEARTE-GNFKYVVVDPVLPNTTSAAGenirwVPI--KPGGDGALAMAMIRWII 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 274 ESGAVNRDFVErhvrfahgaedigyglRPDdpleKKAKNADKANTWSD-----IDFKA------FAEFVKPYTLERTARE 342
Cdd:cd02758 288 ENERYNAEYLS----------------IPS----KEAAKAAGEPSWTNathlvITVRVksalqlLKEEAFSYSLEEYAEI 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 15596371 343 SGVPAERLKALAELYADPKRKVVSFwTMGFNQHTRG---VWA----NNLIYNIHLLTG 393
Cdd:cd02758 348 CGVPEAKIIELAKEFTSHGRAAAVV-HHGGTMHSNGfynAYAirmlNALIGNLNWKGG 404
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
498-561 |
8.14e-07 |
|
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: 52.27 E-value: 8.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596371 498 NPDNFVIVSDVYPTVSAQAADLILPSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSDlWQLV 561
Cdd:cd02773 306 PKDAFVVYQGHHGDRGAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDARED-WKIL 368
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
709-776 |
1.71e-06 |
|
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: 47.77 E-value: 1.71e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596371 709 DYPFWLATGRvlEHWHTG-SMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVE 776
Cdd:cd02782 1 DYPFLLLIGR--RHLRSNnSWLHNDPRLVKGRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVE 67
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
37-225 |
1.80e-06 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 51.39 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 37 VWNKAPCRFCGTGCsvmvatrDGQVVATHGDIKAEVNRGinCVKGyfLSKIMY--GSDRLTRPLLRMKdgkfdkqgefqP 114
Cdd:COG1029 4 VVKNVVCPFCGCLC-------DDLEVEVEGGKIVVVKNA--CAIG--AAKFERavSDHRITSPRIRGK-----------E 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 115 ISWEQAFDIMAEKFKAAlkaKGPeSVGMFGSgqwTVWEGY-AANKLfkAGLRSNNIDPNARHCMASAVMGFMRSfGMdep 193
Cdd:COG1029 62 VSLEEAIDKAAEILANA---KRP-LIYGLSS---TDCEAMrAGLAL--AERVGAVVDNTASVCHGPSLLALQDV-GW--- 128
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15596371 194 MGCyddieaT--------DSFVLWGSNMAEMHPVLWSRVT 225
Cdd:COG1029 129 PTC------TlgevknraDVIIYWGCNPVHAHPRHMSRYS 162
|
|
| MopB_CT_ydeP |
cd02787 |
The MopB_CT_ydeP CD includes a group of related uncharacterized bacterial ... |
744-823 |
5.44e-06 |
|
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: 46.11 E-value: 5.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 744 VYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRNKP---PQGLVFVPFFDANKLInkvTLDATDPISKQTDYKKCA 820
Cdd:cd02787 33 VFMNPDDIARLGLKAGDRVDLESAFGDGQGRIVRGFRVVEydiPRGCLAAYYPEGNVLV---PLDHRDPQSKTPAYKSVP 109
|
...
gi 15596371 821 VRI 823
Cdd:cd02787 110 VRL 112
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
710-824 |
5.96e-06 |
|
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: 46.13 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 710 YPFWLATgrvlehWHTG----SMTARVPELYKAVPDAlVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRNKP-- 783
Cdd:cd02794 1 YPLQLIG------WHYKrrthSTFDNVPWLREAFPQE-VWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPgv 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15596371 784 ---PQGLVFVPffDANKL-----INKVTLDATDPISKQTDYKKCAVRIE 824
Cdd:cd02794 74 valPQGAWYEP--DANGIdkggcINTLTGLRPSPLAKGNPQHTNLVQVE 120
|
|
| FwdD |
COG1153 |
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion]; |
742-824 |
1.13e-05 |
|
Formylmethanofuran dehydrogenase subunit D [Energy production and conversion];
Pssm-ID: 440767 [Multi-domain] Cd Length: 127 Bit Score: 45.61 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 742 ALVYMHPEDARQLKLRRGSEVKVVSRRGEI--RArVETRGrnkPPQGLVFVPFFD-ANKLINKVTLDATDPiskqtDYKK 818
Cdd:COG1153 31 AVCELNPEDMKKLGIKEGDKVKVTSEYGEVvvKA-KESED---LHPGLVFIPMGPwANAVVPPETHSTGMP-----DFKG 101
|
....*.
gi 15596371 819 CAVRIE 824
Cdd:COG1153 102 VPVEVE 107
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
710-775 |
4.79e-05 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 44.21 E-value: 4.79e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596371 710 YPFWLATGRVLEHWHtgsMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARV 775
Cdd:cd02780 1 YPFILVTFKSNLNSH---RSANAPWLKEIKPENPVWINPEDAAKLGIKTGDRVRVVTPGGSVVGKA 63
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
645-778 |
9.90e-05 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 46.14 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 645 FDAYHEARglrwpvvDGKETRWRYREG---YDPYVSKG----SGVQFYGYPDkkaivfalpYEPPAEA---------PDQ 708
Cdd:PRK14991 822 FAPAESAY-------DEERMGNRWKKPlqiWNEDVAAArhsmTGERYSGCPT---------WYPPRLAdgtplreqfPES 885
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 709 DYPFWLATGRvlEHWHTgSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETR 778
Cdd:PRK14991 886 QWPLLLISFK--SNLMS-SMSIASPRLRQVKPANPVALNPQDAARLGIQHGDRVRISTPGGSVVAQASVL 952
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
742-812 |
1.51e-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: 1.51e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596371 742 ALVYMHPEDARQLKLRRGSEVKVVSRRGEIRARVETRGRNkpPQGLVFVPFFD-ANKLINKVTLDATDPISK 812
Cdd:cd02789 31 AYCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGV--PEGMVFIPMGPwANVVVDPYTDSTGSPIFK 100
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
710-809 |
2.49e-04 |
|
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: 41.50 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596371 710 YPFWLATGRVleHWHTGSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEI--RARVETRgrnkPPQGL 787
Cdd:cd02786 1 YPLRLITPPA--HNFLNSTFANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVtlRAKVTDD----VPPGV 74
|
90 100
....*....|....*....|....*....
gi 15596371 788 VFVP------FFDANKLINKVTLDA-TDP 809
Cdd:cd02786 75 VVAEggwwreHSPDGRGVNALTSARlTDL 103
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
710-775 |
2.66e-04 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 41.42 E-value: 2.66e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596371 710 YPFWLATgrvlehWHTG----SMTARVPELYKAVPDAL---VYMHPEDARQLKLRRGSEVKVVSRRGEIRARV 775
Cdd:cd02777 1 YPLQLIS------PHPKrrlhSQLDNVPWLREAYKVKGrepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGA 67
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
710-774 |
4.87e-04 |
|
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: 40.81 E-value: 4.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596371 710 YPFWLATGRVLehWHTGSMTARVPELYKAVPDALVYMHPEDARQLKLRRGSEVKVVSRRGEIRAR 774
Cdd:cd02785 2 YPLACIQRHSR--FRVHSQFSNVPWLLELQPEPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCK 64
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
498-556 |
3.02e-03 |
|
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex I, the second domain of the Nad11/75-kDa subunit of some protists. NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH-quinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. The Nad11 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239175 [Multi-domain] Cd Length: 366 Bit Score: 40.81 E-value: 3.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 15596371 498 NPDNFVIVSDVYPTVSAQAADLILPSAMWVEKEGAFGNAERRTQFWHQLVKAPGEAKSD 556
Cdd:cd02774 297 NKNNFVIYQGHHFLNLANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSD 355
|
|
| |
