|
Name |
Accession |
Description |
Interval |
E-value |
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
5-709 |
0e+00 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 978.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 5 SPLRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGKQLARArsDWE 84
Cdd:COG3383 2 NPMKKVKTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREV--SWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 85 SALEHAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYE 164
Cdd:COG3383 80 EALDLVAERLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGVLGTNNIDNNARLCMASAVAGLKQSFGSDAPPNSYD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 165 DLDCADCVLIAGSNMAFAHPVLFRRLEaaKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWI 244
Cdd:COG3383 160 DIEEADVILVIGSNPAEAHPVLARRIK--KAKKNGAKLIVVDPRRTETARLADLHLQIKPGTDLALLNGLLHVIIEEGLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 245 DRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATG 324
Cdd:COG3383 238 DEDFIAERTEGFEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIINLALATG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 325 KIGRAGCGPFSLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGVEQLPTSPGLSAIELFDAVHDGRIKALWI 404
Cdd:COG3383 318 NIGRPGTGPFPLTGQNNVQGGRDMGALPNVLPGYRDVTDPEHRAKVADAWGVPPLPDKPGLTAVEMFDAIADGEIKALWI 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 405 ACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDW 484
Cdd:COG3383 398 IGENPAVSDPDANHVREALEKLEFLVVQDIFL-TETAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDW 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 485 NIVCDFARRLEGHlrpakpglFAFADSRSLFDEYKLLTAgrdlDLSGLSYALLDRLGPQQWPFPTGAEQGTARLYADgRF 564
Cdd:COG3383 477 EIIAELARRLGYG--------FDYDSPEEVFDEIARLTP----DYSGISYERLEALGGVQWPCPSEDHPGTPRLFTG-RF 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 565 PTASGRAQLVAEPYRAAQEKRDARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLK 644
Cdd:COG3383 544 PTPDGKARFVPVEYRPPAELPDEEYPLVLTTGRLLDQWHTGTRTRRSPRLNKHAPEPFVEIHPEDAARLGIKDGDLVRVS 623
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596976 645 SRRGALVLPVSADDSVRPGQAFLPMHWGDrflkgLGCNVLTLPAFDPLSKQPELKHAGVQVESVE 709
Cdd:COG3383 624 SRRGEVVLRARVTDRVRPGTVFMPFHWGE-----GAANALTNDALDPVSKQPEYKACAVRVEKVA 683
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
11-581 |
0e+00 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. Members of the MopB_Nitrate-R-NapA CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239155 [Multi-domain] Cd Length: 565 Bit Score: 903.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 11 ASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRlGKQLARARSDWESALEHA 90
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLR-RNGGELVPVSWDEALDLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 91 AGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDCAD 170
Cdd:cd02754 80 AERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGGLGTNNIDTNSRLCMASAVAGYKRSFGADGPPGSYDDIEHAD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 171 CVLIAGSNMAFAHPVLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSFIA 250
Cdd:cd02754 160 CFFLIGSNMAECHPILFRRLLDRKKANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNGLLHVLIEEGLIDRDFID 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 251 EHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAG 330
Cdd:cd02754 240 AHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIINLHLATGKIGRPG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 331 CGPFSLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGV--EQLPTSPGLSAIELFDAVHDGRIKALWIACTN 408
Cdd:cd02754 320 SGPFSLTGQPNAMGGREVGGLANLLPGHRSVNNPEHRAEVAKFWGVpeGTIPPKPGLHAVEMFEAIEDGEIKALWVMCTN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 409 PAQSLPDQRKIHEALARCPFVVVQEAFAGTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVC 488
Cdd:cd02754 400 PAVSLPNANRVREALERLEFVVVQDAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWILA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 489 DFARRLEghlrpaKPGLFAFADSRSLFDEYKLLTAGRDLDLSGLSYALLDRlGPQQWPFPTGAEQGTARLYADGRFPTAS 568
Cdd:cd02754 480 DVARRLG------FGELFPYTSPEEVFEEYRRLSRGRGADLSGLSYERLRD-GGVQWPCPDGPPEGTRRLFEDGRFPTPD 552
|
570
....*....|...
gi 15596976 569 GRAQLVAEPYRAA 581
Cdd:cd02754 553 GRARFVAVPYRPP 565
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
3-709 |
0e+00 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 696.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 3 TDSPLRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGK----QLAR 78
Cdd:COG0243 17 EAAGTKTVKTTCPGCGVGCGLGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGPrgsgKFER 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 79 ArsDWESALEHAAGRFAETIREHGPDSVAFYISG----QLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVVGYKRSL 154
Cdd:COG0243 97 I--SWDEALDLIAEKLKAIIDEYGPEAVAFYTSGgsagRLSNEAAYLAQRFARAL-GTNNLDDNSRLCHESAVAGLPRTF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 155 GADAPPCSYEDLDCADCVLIAGSNMAFAHPVLFRRLEAAKAARPeMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGI 234
Cdd:COG0243 174 GSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAAKKRG-AKIVVIDPRRTETAAIADEWLPIRPGTDAALLLAL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 235 LHILLWEDWIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNS 314
Cdd:COG0243 253 AHVLIEEGLYDRDFLARHTVGFDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMGLQQHSNGTQTVR 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 315 ALINLHLATGKIGRAGCGPFSLTGqpnamggretgslanllpghreaadpghraevahywgveqlptspglsaielfDAV 394
Cdd:COG0243 333 AIANLALLTGNIGKPGGGPFSLTG-----------------------------------------------------EAI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 395 HDG---RIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSE-RRISHV 470
Cdd:COG0243 360 LDGkpyPIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVIDTFL-TETARYADIVLPATTWLERDDIVTNSEdRRVHLS 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 471 RRAVPPPGEARQDWNIVCDFARRLeghlrPAKPGLFAFADSRSLFDEYklLTAGRDldlSGLSYALLDRLGPQQWPFPTG 550
Cdd:COG0243 439 RPAVEPPGEARSDWEIFAELAKRL-----GFEEAFPWGRTEEDYLREL--LEATRG---RGITFEELREKGPVQLPVPPE 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 551 aeqgtARLYADGRFPTASGRAQL------------VAEPYRAAqEKRDARYPLTLNTGRLRDQWHGMSRtgTCARLFGHE 618
Cdd:COG0243 509 -----PAFRNDGPFPTPSGKAEFysetlalpplprYAPPYEGA-EPLDAEYPLRLITGRSRDQWHSTTY--NNPRLREIG 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 619 EEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPMHWGDRFL--KGLGCNVLTLPAFDPLSKQP 696
Cdd:COG0243 581 PRPVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWYEPAddKGGNVNVLTPDATDPLSGTP 660
|
730
....*....|...
gi 15596976 697 ELKHAGVQVESVE 709
Cdd:COG0243 661 AFKSVPVRVEKAA 673
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
12-705 |
0e+00 |
|
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate dehydrogenase alpha chains found mainly archaea but also in alpha and gamma proteobacteria and a small number of gram positive bacteria. The alpha chain contains domains for molybdopterin dinucleotide binding and molybdopterin oxidoreductase (pfam01568 and pfam00384, respectively). The holo-enzyme also contains beta and gamma subunits. The enzyme catalyzes the oxidation of formate (produced from pyruvate during anaerobic growth) to carbon dioxide with the concomitant release of two electrons and two protons. The enzyme's purpose is to allow growth on formate in some circumstances and, in the case of FdhH in gamma proteobacteria, to pass electrons to hydrogenase (by which process acid is neutralized). This model is well-defined, with only a single fragmentary sequence falling between trusted and noise. The alpha subunit of a version of nitrate reductase is closely related.
Pssm-ID: 130652 [Multi-domain] Cd Length: 671 Bit Score: 584.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKG--ASLHLTGdlQARALYPQLRLGKQLARArsDWESALEH 89
Cdd:TIGR01591 1 TVCPYCGVGCSLNLVVKDGKIVRVEPYQGHKANRGHLCVKGyfAWEFINS--KDRLTTPLIREGDKFREV--SWDEAISY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 90 AAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDCA 169
Cdd:TIGR01591 77 IAEKLKEIKEKYGPDSIGFIGSSRGTNEENYLLQKLARAVIGTNNVDNCARVCHGPSVAGLKQTVGIGAMSNTISEIENA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 170 DCVLIAGSNMAFAHPVLFRRLEAAKaaRPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSFI 249
Cdd:TIGR01591 157 DLIVIIGYNPAESHPVVAQYLKNAK--RNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEEGLYDKAFI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 250 AEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRA 329
Cdd:TIGR01591 235 EKRTEGFEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNIGKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 330 GCGPFSLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGVEQLPTSPGLSAIELFDAVHDGRIKALWIACTNP 409
Cdd:TIGR01591 315 GGGVNPLRGQNNVQGACDMGALPDFLPGYQPVSDEEVREKFAKAWGVVKLPAEPGLRIPEMIDAAADGDVKALYIMGEDP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 410 AQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVCD 489
Cdd:TIGR01591 395 LQSDPNTSKVRKALEKLELLVVQDIFM-TETAKYADVVLPAAAWLEKEGTFTNAERRIQRFFKAVEPKGESKPDWEIIQE 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 490 FARRLeghlrpakpGL-FAFADSRSLFDEYKLLTAgrdlDLSGLSYALLDRLGPQQWPFPTGAEQGTARLYADgRFPTAS 568
Cdd:TIGR01591 474 LANAL---------GLdWNYNHPQEIMDEIRELTP----LFAGLTYERLDELGSLQWPCNDSDASPTSYLYKD-KFATPD 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 569 GRAQLVAEPYRAAQEKRDARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRG 648
Cdd:TIGR01591 540 GKAKFIPLEWVAPIEEPDDEYPLILTTGRVLTHYNVGEMTRRVAGLRRLSPEPYVEINTEDAKKLGIKDGDLVKVKSRRG 619
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 15596976 649 ALVLPVSADDSVRPGQAFLPMHWGDRflkglGCNVLTLPAFDPLSKQPELKHAGVQV 705
Cdd:TIGR01591 620 EITLRAKVSDRVNKGAIYITMHFWDG-----AVNNLTTDDLDPISGTPEYKYTAVRI 671
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
12-580 |
9.70e-170 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. Members of the MopB_Formate-Dh-H CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239154 [Multi-domain] Cd Length: 512 Bit Score: 503.28 E-value: 9.70e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLH---LTGDlqaRALYPQLRLGKQLARArsDWESALE 88
Cdd:cd02753 2 TVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFdfvNSKD---RLTKPLIRKNGKFVEA--SWDEALS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 89 HAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDC 168
Cdd:cd02753 77 LVASRLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARAVGGTNNVDHCARLCHSPTVAGLAETLGSGAMTNSIADIEE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 169 ADCVLIAGSNMAFAHPVLFRRLEaaKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSF 248
Cdd:cd02753 157 ADVILVIGSNTTEAHPVIARRIK--RAKRNGAKLIVADPRRTELARFADLHLQLRPGTDVALLNAMAHVIIEEGLYDEEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 249 IAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGR 328
Cdd:cd02753 235 IEERTEGFEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDNVMALSNLALLTGNIGR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 329 AGCGPFSLTGQPNAMGGRETGSLANLLPGHreaadpghraevahywgveqlptspglsaielfdavhdgrIKALWIACTN 408
Cdd:cd02753 315 PGTGVNPLRGQNNVQGACDMGALPNVLPGY----------------------------------------VKALYIMGEN 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 409 PAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVC 488
Cdd:cd02753 355 PALSDPNTNHVRKALESLEFLVVQDIFL-TETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQ 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 489 DFARRLeGHlrpakPGlfAFADSRSLFDEYKLLTAgrdlDLSGLSYALLDRLGPQQWPFPTGAEQGTARLYADgRFPTAS 568
Cdd:cd02753 434 ELANRL-GY-----PG--FYSHPEEIFDEIARLTP----QYAGISYERLERPGGLQWPCPDEDHPGTPILHTE-RFATPD 500
|
570
....*....|..
gi 15596976 569 GRAQLVAEPYRA 580
Cdd:cd02753 501 GKARFMPVEYRP 512
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
14-708 |
6.04e-129 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 408.13 E-value: 6.04e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 14 CCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLhltgdlqARALYPQLRLGKQLARARS------------ 81
Cdd:PRK13532 47 CRFCGTGCGVLVGTKDGRVVATQGDPDAPVNRGLNCIKGYFL-------SKIMYGKDRLTQPLLRMKDgkydkegeftpv 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 82 DWESALEHAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPC 161
Cdd:PRK13532 120 SWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKAGFRSNNIDPNARHCMASAVVGFMRTFGIDEPMG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 162 SYEDLDCADCVLIAGSNMAFAHPVLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWE 241
Cdd:PRK13532 200 CYDDIEAADAFVLWGSNMAEMHPILWSRVTDRRLSNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQN 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 242 DWIDRSFIAEHTE----------------------------------GFADLKELVRDYTPAAVADICGIDRADLQRCAE 287
Cdd:PRK13532 280 NAVNWDFVNKHTNfrkgatdigyglrpthplekaaknpgtagksepiSFEEFKKFVAPYTLEKTAKMSGVPKEQLEQLAK 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 288 -WIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAMG-GRETGSLANLLPGHREAADPG 365
Cdd:PRK13532 360 lYADPNRKVVSFWTMGFNQHTRGVWANNLVYNIHLLTGKISTPGNGPFSLTGQPSACGtAREVGTFSHRLPADMVVTNPK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 366 HRAEVAHYWGVEQ--LPTSPGLSAIELFDAVHDGRIKALWIACTNPAQSLPDQRkiHEAL--ARCP--FVVVQEAFAGTe 439
Cdd:PRK13532 440 HREIAEKIWKLPEgtIPPKPGYHAVAQDRMLKDGKLNAYWVMCNNNMQAGPNIN--EERLpgWRNPdnFIVVSDPYPTV- 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 440 TCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQD-WNIVcDFARRLE------GHLRPAKPG-------- 504
Cdd:PRK13532 517 SALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV-EFSKRFKteevwpEELLAKKPEyrgktlyd 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 505 -LFA---------------FADSRS----------LFDEYKLLTAGRDLDLS---------GLSYALLDrlGPQ-QWPFP 548
Cdd:PRK13532 596 vLFAngqvdkfplselaegYLNDEAkhfgfyvqkgLFEEYASFGRGHGHDLApfdtyhkvrGLRWPVVD--GKEtLWRYR 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 549 TG----AEQGTA-RLYADgrfptASGRAQLVAEPYRAAQEKRDARYPLTLNTGRLRDQWHgmsrTGTCAR----LFGHEE 619
Cdd:PRK13532 674 EGydpyVKAGEGfKFYGK-----PDGKAVIFALPYEPPAESPDEEYDLWLSTGRVLEHWH----TGSMTRrvpeLYRAFP 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 620 EALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRP--GQAFLPmhWgdrFLKGLGCNVLTLPAFDPLSKQPE 697
Cdd:PRK13532 745 EAVCFMHPEDAKARGLRRGDEVKVVSRRGEVKSRVETRGRNKPprGLVFVP--F---FDAAQLINKLTLDATDPLSKQTD 819
|
810
....*....|.
gi 15596976 698 LKHAGVQVESV 708
Cdd:PRK13532 820 FKKCAVKIEKV 830
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
12-494 |
1.25e-120 |
|
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site.
Pssm-ID: 238218 [Multi-domain] Cd Length: 374 Bit Score: 370.89 E-value: 1.25e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGKQLARARSDWESALEHAA 91
Cdd:cd00368 2 SVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGGRGKFVPISWDEALDEIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 92 GRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVVGYKRsLGADAPPCSYEDLDCADC 171
Cdd:cd00368 82 EKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRAL-GSNNVDSHARLCHASAVAALKA-FGGGAPTNTLADIENADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 172 VLIAGSNMAFAHPVLFRRLeaAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGilhillwedwidrsfiae 251
Cdd:cd00368 160 ILLWGSNPAETHPVLAARL--RRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA------------------ 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 252 htegfadlkelvrdytpAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGC 331
Cdd:cd00368 220 -----------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 332 GPFSltgqpnamggretgslanllpghreaadpghraevahywgveqlptspglsaielfdavhdgrikalwiaCTNPAQ 411
Cdd:cd00368 283 GLGP----------------------------------------------------------------------GGNPLV 292
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 412 SLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVCDFA 491
Cdd:cd00368 293 SAPDANRVRAALKKLDFVVVIDIFM-TETAAYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELA 371
|
...
gi 15596976 492 RRL 494
Cdd:cd00368 372 KRL 374
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
64-493 |
2.84e-78 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 258.48 E-value: 2.84e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 64 RALYPQLRLGK-QLARArsDWESALEHAAGRFAETIREHGPDSVAF-YISGQLL-TEDYYAFNKLARALVGTN--NIDSN 138
Cdd:pfam00384 1 RLKYPMVRRGDgKFVRV--SWDEALDLIAKKLKRIIKKYGPDAIAInGGSGGLTdVESLYALKKLLNRLGSKNgnTEDHN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 139 SRLCMSSAVVgykrsLGADAPPC-----SYEDLDCADCVLIAGSNMAFAHPVLFRRLEAAkAARPEMRIVVIDPRRTDTc 213
Cdd:pfam00384 79 GDLCTAAAAA-----FGSDLRSNylfnsSIADIENADLILLIGTNPREEAPILNARIRKA-ALKGKAKVIVIGPRLDLT- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 214 eLADLHLALLPGTDVALFHGILHILLWEDWIDRSFiaehtegfadlkelvrdytpaavadicgidradlqrcaewigrSP 293
Cdd:pfam00384 152 -YADEHLGIKPGTDLALALAGAHVFIKELKKDKDF-------------------------------------------AP 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 294 RFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAmgGRETGSLAnllpghreaadpghraevahy 373
Cdd:pfam00384 188 KPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGWNGLNILQGA--ASPVGALD--------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 374 wgveqLPTSPGLSAIELFDAVHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAGTETCQYADLLLPAASW 453
Cdd:pfam00384 245 -----LGLVPGIKSVEMINAIKKGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHHGDKTAKYADVILPAAAY 319
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 15596976 454 GEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVCDFARR 493
Cdd:pfam00384 320 TEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
12-494 |
2.09e-77 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. Members of the MopB_Formate-Dh-Na-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239153 [Multi-domain] Cd Length: 649 Bit Score: 265.03 E-value: 2.09e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASL--HLTGDLqaRALYPQLRLGKQLARARSDWESALEH 89
Cdd:cd02752 2 TICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALrdFVHSPK--RLKYPMYRAPGSGKWEEISWDEALDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 90 AAGRFAEtIRE-------------HGPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVVGYKRSLGA 156
Cdd:cd02752 80 IARKMKD-IRDasfveknaagvvvNRPDSIAFLGSAKLSNEECYLIRKFARAL-GTNNLDHQARIUHSPTVAGLANTFGR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 157 DAPPCSYEDLDCADCVLIAGSNMAFAHPVLFRRLEAAKAARpEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILH 236
Cdd:cd02752 158 GAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKN-GAKLIVVDPRFTRTAAKADLYVPIRSGTDIAFLGGMIN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 237 illwedWIDRsfiaehtegfadlkelvrdYTPAAVADICGIDRADLQRCAEWI---GRSPRFLS-LWCMGLNQSSAGSAK 312
Cdd:cd02752 237 ------YIIR-------------------YTPEEVEDICGVPKEDFLKVAEMFaatGRPDKPGTiLYAMGWTQHTVGSQN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 313 NSALINLHLATGKIGRAGCGPFSLTGQPNAMGGRETGSLANLLPGHReaadPGHraevahywgveqlptspglsaielfd 392
Cdd:cd02752 292 IRAMCILQLLLGNIGVAGGGVNALRGHSNVQGATDLGLLSHNLPGYL----GGQ-------------------------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 393 avhdgrikalwiactNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYAD-------------LLLPAASWGEKEGS 459
Cdd:cd02752 342 ---------------NPNSSFPNANKVRRALDKLDWLVVIDPFP-TETAAFWKnpgmdpksiqtevFLLPAACQYEKEGS 405
|
490 500 510
....*....|....*....|....*....|....*
gi 15596976 460 VTNSERRISHVRRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02752 406 ITNSGRWLQWRYKVVEPPGEAKSDGDILVELAKRL 440
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
21-576 |
2.65e-74 |
|
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239167 [Multi-domain] Cd Length: 501 Bit Score: 252.55 E-value: 2.65e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 21 CGVLIEHDGERILGVQGDPRHPANFGRLCSKGAslHLTGDLQA--RALYPQLRLGKQLAR-ARSDWESALEHAAGRFAET 97
Cdd:cd02766 12 CSLLVTVEDGRIVRVEGDPAHPYTRGFICAKGA--RYVERVYSpdRLLTPLKRVGRKGGQwERISWDEALDTIAAKLKEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 98 IREHGPDSVAfYISGQ----LLTEDYYA--FNKL-ARALVGTnnidsnsrLCMSSAVVGYK----RSLGADAppcsyEDL 166
Cdd:cd02766 90 KAEYGPESIL-PYSYAgtmgLLQRAARGrfFHALgASELRGT--------ICSGAGIEAQKydfgASLGNDP-----EDM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 167 DCADCVLIAGSNMAFAHPVLFRRLEAAKAArpEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDR 246
Cdd:cd02766 156 VNADLIVIWGINPAATNIHLMRIIQEARKR--GAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYDR 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 247 SFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKI 326
Cdd:cd02766 234 DFLARHTEGFEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPPSIRLGYGMQRYRNGGQNVRAIDALPALTGNI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 327 GRAGCGPFSLTGQPNamggretgslanllpghreaadpghraevahywgveqlptspglsaielfdavhdgrIKALWIAC 406
Cdd:cd02766 314 GVPGGGAFYSNSGPP---------------------------------------------------------VKALWVYN 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 407 TNPAQSLPDQRKIHEALAR-CPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTnSE--RRISHVRRAVPPPGEARQD 483
Cdd:cd02766 337 SNPVAQAPDSNKVRKGLAReDLFVVVHDQFM-TDTARYADIVLPATTFLEHEDVYA-SYwhYYLQYNEPAIPPPGEARSN 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 484 WNIVCDFARRL--EGHLrpakpglfaFADSRSLFdeykLLTAGRDLDLSGLSYALLDRLGPQQWPFPtgaeqgtARLYAD 561
Cdd:cd02766 415 TEIFRELAKRLgfGEPP---------FEESDEEW----LDQALDGTGLPLEGIDLERLLGPRKAGFP-------LVAWED 474
|
570
....*....|....*
gi 15596976 562 GRFPTASGRAQLVAE 576
Cdd:cd02766 475 RGFPTPSGKFEFYSE 489
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
37-573 |
2.28e-70 |
|
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239168 [Multi-domain] Cd Length: 574 Bit Score: 243.75 E-value: 2.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 37 GDPRHPANFGRLCSKGA-----------------SLHLTGDLQARALYPQLRLGK----QLARARSD------WESALEH 89
Cdd:cd02767 10 GDPGQKLHGFEFCENGAkalawettpkrvtpeffALHSVSELRTWSDYELEHLGRltypMRYDAGSDhyrpisWDEAFAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 90 AAGRFaetiREHGPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDCA 169
Cdd:cd02767 90 IAARL----RALDPDRAAFYTSGRASNEAAYLYQLFARAY-GTNNLPDCSNMCHEPSSVGLKKSIGVGKGTVSLEDFEHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 170 DCVLIAGSNMAFAHPVLFRRLEAAKAArpEMRIVVIDPRR-----------------TDTCELADLHLALLPGTDVALFH 232
Cdd:cd02767 165 DLIFFIGQNPGTNHPRMLHYLREAKKR--GGKIIVINPLRepglerfanpqnpesmlTGGTKIADEYFQVRIGGDIALLN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 233 GIL-HILLWED----WIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSS 307
Cdd:cd02767 243 GMAkHLIERDDepgnVLDHDFIAEHTSGFEEYVAALRALSWDEIERASGLSREEIEAFAAMYAKSERVVFVWGMGITQHA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 308 AGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAMGGRETGSlanllpghREAADPGHRAEVAHYWGVEqLPTSPGLSA 387
Cdd:cd02767 323 HGVDNVRAIVNLALLRGNIGRPGAGLMPIRGHSNVQGDRTMGI--------TEKPFPEFLDALEEVFGFT-PPRDPGLDT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 388 IELFDAVHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQE-------AFAGTETcqyadLLLPAASWGEK---- 456
Cdd:cd02767 394 VEAIEAALEGKVKAFISLGGNFAEAMPDPAATEEALRRLDLTVHVAtklnrshLVHGEEA-----LILPCLGRTEIdmqa 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 457 ---------------EGSV----TNSERRISHV----RRAVPPPGEARQDWNIVCDFARRleghLRPAKPGLF--AFADs 511
Cdd:cd02767 469 ggaqavtvedsmsmtHTSRgrlkPASRVLLSEEaivaGIAGARLGEAKPEWEILVEDYDR----IRDEIAAVIyeGFAD- 543
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596976 512 rslFDEYKLLTAGRDLdlsglsyalldrlgpqqwpfPTGAeqgtarlyADGRFPTASGRAQL 573
Cdd:cd02767 544 ---FNQRGDQPGGFHL--------------------PNGA--------RERKFNTPSGKAQF 574
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
13-540 |
2.33e-66 |
|
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239163 [Multi-domain] Cd Length: 539 Bit Score: 231.90 E-value: 2.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 13 TCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLhltGDLQ---ARALYPQLRLGKQLARArsDWESALEH 89
Cdd:cd02762 3 ACILCEANCGLVVTVEDGRVASIRGDPDDPLSKGYICPKAAAL---GDYQndpDRLRTPMRRRGGSFEEI--DWDEAFDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 90 AAGRFAETIREHGPDSVAFYISG-QLLTEDYYAFNKLARALVGTNNIDSNSRLCMS----SAVVGYKRSLGADAPpcsye 164
Cdd:cd02762 78 IAERLRAIRARHGGDAVGVYGGNpQAHTHAGGAYSPALLKALGTSNYFSAATADQKpghfWSGLMFGHPGLHPVP----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 165 DLDCADCVLIAGSNMAFAH------PVLFRRLEAAKAarPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHIL 238
Cdd:cd02762 153 DIDRTDYLLILGANPLQSNgslrtaPDRVLRLKAAKD--RGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAAMLAVL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 239 LWEDWIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAkNSALIN 318
Cdd:cd02762 231 LAEGLTDRRFLAEHCDGLDEVRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSAAVYGRLGVQTQLFGTL-CSWLVK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 319 -LHLATGKIGRAGcgpfsltgqpnamGGRETGSLANLLPghreAADPGHRAEVAHYWGVEQLPTSPGL---SAI-ELFDA 393
Cdd:cd02762 310 lLNLLTGNLDRPG-------------GAMFTTPALDLVG----QTSGRTIGRGEWRSRVSGLPEIAGElpvNVLaEEILT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 394 VHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEaFAGTETCQYADLLLPAASWGEK-EGSVTNSE--RRISHV 470
Cdd:cd02762 373 DGPGRIRAMIVVAGNPVLSAPDGARLEAALGGLEFMVSVD-VYMTETTRHADYILPPASQLEKpHATFFNLEfpRNAFRY 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596976 471 RRA-VPPPGEARQDWNIVCDFARRLEGHLRPAKPGLFAFADsrSLFDeyKLLTAGRDLDLSGLSYALLDRL 540
Cdd:cd02762 452 RRPlFPPPPGTLPEWEILARLVEALDAVLRAGFYGERAGGT--LLLA--ALLERPSGVDLGPLTPRLWQRL 518
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
13-507 |
1.32e-64 |
|
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239160 [Multi-domain] Cd Length: 477 Bit Score: 225.26 E-value: 1.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 13 TCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGKQLARA--RSDWESALEHA 90
Cdd:cd02759 3 TCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTNKGRLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKweRISWDEALDEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 91 AGRFAETIREHGPDSVAFYI---SGQLL--TEDYYAFNKLARALVGTNNIDS--NSRLCMSSAVVGYkrslgadapPCSY 163
Cdd:cd02759 83 AEKLAEIKAEYGPESIATAVgtgRGTMWqdSLFWIRFVRLFGSPNLFLSGEScyWPRDMAHALTTGF---------GLGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 164 E--DLDCADCVLIAGSNMAFAHPVLFrrLEAAKAARPE-MRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLW 240
Cdd:cd02759 154 DepDWENPECIVLWGKNPLNSNLDLQ--GHWLVAAMKRgAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNVIIN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 241 EDWIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRS-PRFLSlWCMGLNQSSAGSAKNSALINL 319
Cdd:cd02759 232 EGLYDKDFVENWCYGFEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAkPACIQ-WGLAIDQQKNGTQTSRAIAIL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 320 HLATGKIGRAGcgpfsltgqpnamggretGSLanLLPghreaadpghraevahYwgveqlptspglsaielfdavhdgRI 399
Cdd:cd02759 311 RAITGNLDVPG------------------GNL--LIP----------------Y------------------------PV 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 400 KALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRIsHVR---RAVPP 476
Cdd:cd02759 331 KMLIVFGTNPLASYADTAPVLEALKALDFIVVVDLFM-TPTAMLADIVLPVAMSLERPGLRGGFEAEN-FVQlrqKAVEP 408
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 15596976 477 PGEARQDWNIVCDFARRL-----------EGHLRPAKPGLFA 507
Cdd:cd02759 409 YGEAKSDYEIVLELGKRLgpeeaeyykyeKGLLRPDGQPGFN 450
|
|
| arsenite_ox_L |
TIGR02693 |
arsenite oxidase, large subunit; This model represents the large subunit of an arsenite ... |
23-671 |
2.25e-59 |
|
arsenite oxidase, large subunit; This model represents the large subunit of an arsenite oxidase complex. The small subunit is a Rieske protein. Homologs to both large and small subunits that score in the gray zone between the set trusted and noise bit score cutoffs for the respective models are found in Aeropyrum pernix K1 and in Sulfolobus tokodaii str. 7. This enzyme acts in energy metabolim by arsenite oxidation, rather than detoxification by reduction of arsenate to arsenite prior to export. [Energy metabolism, Electron transport]
Pssm-ID: 274261 [Multi-domain] Cd Length: 806 Bit Score: 217.87 E-value: 2.25e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 23 VLIEHDGERI-LGVQGDPRHPANFGRLCSKGASLHLT-----GDLQARALYPQLRLGKQLARarSDWESALEHAAGRFAE 96
Cdd:TIGR02693 68 VVKQRDGRDVnVVIKPDKECVVNSGLGSVRGGRMAETsfsedRNTQDRLTYPLVWRGDQMQP--TSWDDALDLVARLTKK 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 97 TIREHGPDSVAFYI-----SGQLLtEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGyKRSLGADAPPCSYEDLDCADC 171
Cdd:TIGR02693 146 IVDEKGEDDIIVSAfdhggAGGGF-ENTWGTGKLYFEAMKVKNIRIHNRPAYNSEVHG-TREMGVGELNNCYEDAELADT 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 172 VLIAGSNMAFAHPVLF----------RRLEAAKAARPEM-----RIVVIDPRRTDTCELAD-------LHLALLPGTDVA 229
Cdd:TIGR02693 224 IVAVGTNAYETQTNYFlnhwlpnlrgETLGKKKQLFPGEphepgRIIIVDPRRTVSVNAAEqtaadrvLHLAINSGTDLA 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 230 LFHGILHILLWEDWIDRSFIAE--HTEGFADLKELVRdYTPAAVADICGIDRADLQRCAEWI------GRSPRFLSLWCM 301
Cdd:TIGR02693 304 LFNALFTYVADKGWVDRDFIDKsgHLSSFEDAVKGCR-MSIAEAARITGVSAAQIIKAAEWIgkpkagGKRRRTMFGYEK 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 302 GLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQ-------PNAMGGRETGSLANLLPGHReaadpghrAEVAHYW 374
Cdd:TIGR02693 383 GIIWGNDNYRTNGALVNLALATGNIGRPGTGCVRLGGHqegyvrpPDAHVGGPAAYVDQLLIGGK--------GGVHHIW 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 375 GVEQLPTSPGLSAI-ELFDAVHDGRIKALWIACTNPAQSLPDqrKIHEALARCP-FVVVQEAFAgTETCQYADLLLPAAS 452
Cdd:TIGR02693 455 GCDHYKTTLNAQEFrRVYKKRTDMVKDAMSAAPYGDREEMVN--AIVDAINQGGlFAVNVDIYP-TKIGEAAHLILPAAT 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 453 WGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIVCDFARRLEGHLRP-AKPGLF-------------AFADSrslFDEY 518
Cdd:TIGR02693 532 SGEMNLTSMNGERRMRLTEKFMDPPGQAMPDCLIAARLANTMERVYTAeGKVEYAkqfkgfdwkteedAFMDG---YNKN 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 519 KLLTAGRDLDLSG-----LSYALLDRLGPQ--QWP---FPTGAEQGTARLYADGRFPTASGRAQLVAEPYRAAQ----EK 584
Cdd:TIGR02693 609 RDNTVEDEAAHGGenykfVTYELLSAMGTNgfQEPatrFTDGKIEGTQRLYTDGVFSTDDGKARFMDAPWRGLPapgkQQ 688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 585 RDARYPLTLNTGRLRDQWHGmsrtgtcARLFGHEEE-------ALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSAD 657
Cdd:TIGR02693 689 QKDKHKFWINNGRANVVWQS-------AYHDQENDFvmdrfplPYIEMNPEDAAELGLKEGDLVEVYNDAGATQAMAYPT 761
|
730
....*....|....*
gi 15596976 658 DSVRPGQAFLPM-HW 671
Cdd:TIGR02693 762 PTAKPGETFMLFgFP 776
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
587-708 |
8.32e-56 |
|
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to nitrite. Monomeric Nas is located in the cytoplasm and participates in nitrogen assimilation. Dimeric Nap is located in the periplasm and is coupled to quinol oxidation via a membrane-anchored tetraheme cytochrome. This CD (MopB_CT_Nitrate-R-Nap) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs
Pssm-ID: 239192 [Multi-domain] Cd Length: 122 Bit Score: 188.17 E-value: 8.32e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 587 ARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAF 666
Cdd:cd02791 1 AEYPLWLNTGRVRDQWHTMTRTGRVPRLNAHVPEPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15596976 667 LPMHWGDRFLKGLGCNVLTLPAFDPLSKQPELKHAGVQVESV 708
Cdd:cd02791 81 VPMHWGDQFGRSGRVNALTLDATDPVSGQPEFKHCAVRIEKV 122
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
10-494 |
2.47e-50 |
|
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Members of the MopB_Thiosulfate-R-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239156 [Multi-domain] Cd Length: 454 Bit Score: 184.42 E-value: 2.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 10 TASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHLTgdlqaraLYPQLRLGKQLARA---------R 80
Cdd:cd02755 1 VPSICEMCSSRCGILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQL-------LYDPDRLKKPLIRVgergegkfrE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 81 SDWESALEHAAGRFAETIREHGPDSVAFYISGQLLtEDYyaFNKLARALvGTNNIDSNSRLCMSSAVVGYK---RSLGAD 157
Cdd:cd02755 74 ASWDEALQYIASKLKEIKEQHGPESVLFGGHGGCY-SPF--FKHFAAAF-GSPNIFSHESTCLASKNLAWKlviDSFGGE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 158 APPcsyeDLDCADCVLIAGSNMAFA-HPVLFRRLEAAKAARpeMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILH 236
Cdd:cd02755 150 VNP----DFENARYIILFGRNLAEAiIVVDARRLMKALENG--AKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIH 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 237 ILLWEDWIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCA-EWIGRSPR--FLSLWCMGLNQSSAGSAKN 313
Cdd:cd02755 224 VLISENLYDAAFVEKYTNGFELLKAHVKPYTPEWAAQITDIPADTIRRIArEFAAAAPHavVDPGWRGTFYSNSFQTRRA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 314 SALINlhLATGKIGRAGCGPFSLTGQPnamggretgslanllpghreaadpghraevahywgveqlptspglsaielfda 393
Cdd:cd02755 304 IAIIN--ALLGNIDKRGGLYYAGSAKP----------------------------------------------------- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 394 vhdGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEaFAGTETCQYADLLLPAASWGEKE--GSVTNSERRISHVR 471
Cdd:cd02755 329 ---YPIKALFIYRTNPFHSMPDRARLIKALKNLDLVVAID-ILPSDTALYADVILPEATYLERDepFSDKGGPAPAVATR 404
|
490 500
....*....|....*....|....
gi 15596976 472 -RAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02755 405 qRAIEPLYDTRPGWDILKELARRL 428
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
587-706 |
1.39e-48 |
|
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and other related proteins. Formate dehydrogenase H is a component of the anaerobic formate hydrogen lyase complex and catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. Formate dehydrogenase N (alpha subunit) is the major electron donor to the bacterial nitrate respiratory chain and nitrate reductases, Nap and Nas, catalyze the reduction of nitrate to nitrite. This CD (MopB_CT_Fdh-Nap-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 238282 [Multi-domain] Cd Length: 120 Bit Score: 167.68 E-value: 1.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 587 ARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAF 666
Cdd:cd00508 1 EEYPLVLTTGRLLEHWHTGTMTRRSPRLAALAPEPFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPGTVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15596976 667 LPMHWGDRFlKGLGCNVLTLPAFDPLSKQPELKHAGVQVE 706
Cdd:cd00508 81 MPFHWGGEV-SGGAANALTNDALDPVSGQPEFKACAVRIE 119
|
|
| MopB_NDH-1_NuoG2-N7 |
cd02771 |
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of ... |
12-502 |
5.56e-42 |
|
MopB_NDH-1_NuoG2-N7: The second domain of the NuoG subunit (with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239172 [Multi-domain] Cd Length: 472 Bit Score: 160.63 E-value: 5.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 12 STCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKG--ASLHLTGDlqARALYPQLRLGKQLARArsDWESALEH 89
Cdd:cd02771 2 SICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGrfGYGYVNSR--DRLTQPLIRRGGTLVPV--SWNEALDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 90 AAGRFAEtirehGPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVvgykRSLGADAPpcSYEDLDCA 169
Cdd:cd02771 78 AAARLKE-----AKDKVGGIGSPRASNESNYALQKLVGAVLGTNNVDHRARRLIAEIL----RNGPIYIP--SLRDIESA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 170 DCVLIAGSNMAFAHPVLFRRLEaaKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFH----GILHILLWEDWID 245
Cdd:cd02771 147 DAVLVLGEDLTQTAPRIALALR--QAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNalatRLDDIAAESIRAS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 246 RSFIAEHTEGFADLkelvrdyTPAAVADICGIDRADL-QRCAEWIGRSPRFLSLWcmGLNQSSAGSAKnsALINLHLATG 324
Cdd:cd02771 225 PGGQARLGAALARA-------VDASAAGVSGLAPKEKaARIAARLTGAKKPLIVS--GTLSGSLELIK--AAANLAKALK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 325 KIGRAGcgpfsltgqpNAMGGRETGSLANLLPGHREaadpghraevahywgveqlPTSPGLSAIELFDAVHDGRIKALWI 404
Cdd:cd02771 294 RRGENA----------GLTLAVEEGNSPGLLLLGGH-------------------VTEPGLDLDGALAALEDGSADALIV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 405 ACTNPAQSLPDqRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVP-PPGEARQD 483
Cdd:cd02771 345 LGNDLYRSAPE-RRVEAALDAAEFVVVLDHFL-TETAERADVVLPAASFAEKSGTFVNYEGRAQRFFKAYDdPAGDARSD 422
|
490
....*....|....*....
gi 15596976 484 WNIVCDFARRLEGHLRPAK 502
Cdd:cd02771 423 WRWLHALAAKLGGKLVPSD 441
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
9-494 |
7.11e-42 |
|
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. Members of the MopB_DMSOR-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239152 [Multi-domain] Cd Length: 609 Bit Score: 162.78 E-value: 7.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 9 TTASTCCYCGVgcgvlIEHDGeRILGVQGDPRHPAnfgRLCSKGASLHLTGDLQARALYPQLRLGK-------QLARARS 81
Cdd:cd02751 1 PTACHWGPFKA-----HVKDG-VIVRVEPDDTDQP---RPCPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsRELRGEG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 82 D-----WESALEHAAGRFAETIREHGPDSVaFYISGqllTEDYYAFNKLARALVG---------TNNIDSNSrlcMSSAV 147
Cdd:cd02751 72 EfvrisWDEALDLVASELKRIREKYGNEAI-FGGSY---GWASAGRLHHAQSLLHrflnliggyLGSYGTYS---TGAAQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 148 VGYKRSLGADAPPC---SYED-LDCADCVLIAGSNMA--------FAHPVLFRRLEAAKAARpeMRIVVIDPRRTDTCE- 214
Cdd:cd02751 145 VILPHVVGSDEVYEqgtSWDDiAEHSDLVVLFGANPLktrqggggGPDHGSYYYLKQAKDAG--VRFICIDPRYTDTAAv 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 215 LADLHLALLPGTDVALFHGILHILLWEDWIDRSFIAEHTEGFADLKelvrDY----------TPAAVADICGIDRADLQR 284
Cdd:cd02751 223 LAAEWIPIRPGTDVALMLAMAHTLITEDLHDQAFLARYTVGFDEFK----DYllgesdgvpkTPEWAAEITGVPAETIRA 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 285 CAEWIGRSPRFLSL-WcmGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAMGGRETGSLANLLPGHREAAD 363
Cdd:cd02751 299 LAREIASKRTMIAQgW--GLQRAHHGEQPAWMLVTLAAMLGQIGLPGGGFGFGYGYSNGGGPPRGGAGGPGLPQGKNPVK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 364 pghraevahywgvEQLPTSPGLSAIE----LFDA----VHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAF 435
Cdd:cd02751 377 -------------DSIPVARIADALLnpgkEFTAngklKTYPDIKMIYWAGGNPLHHHQDLNRLIKALRKDETIVVHDIF 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596976 436 AgTETCQYADLLLPAASWGEKE---GSVTNSERRISHVRRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02751 444 W-TASARYADIVLPATTSLERNdigLTGNYSNRYLIAMKQAVEPLGEARSDYEIFAELAKRL 504
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
47-494 |
4.19e-40 |
|
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under anaerobic conditions in the presence of nitrate, E. coli synthesizes the cytoplasmic membrane-bound quinol-nitrate oxidoreductase (NarGHI), which reduces nitrate to nitrite and forms part of a redox loop generating a proton-motive force. Found in prokaryotes and some archaea, NarGHI usually functions as a heterotrimer. The alpha chain contains the molybdenum cofactor-containing Mo-bisMGD catalytic subunit. Members of the MopB_Nitrate-R-NarG-like CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239151 [Multi-domain] Cd Length: 461 Bit Score: 154.78 E-value: 4.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 47 RLCSKGASLH--LTGDLqaRALYPQLRLGKQLAR--ARSDWESALEHAAGRFAETIREHGPDSVAFYI----SGQLLTED 118
Cdd:cd02750 49 RGCQRGASFSwyLYSPD--RVKYPLKRVGARGEGkwKRISWDEALELIADAIIDTIKKYGPDRVIGFSpipaMSMVSYAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 119 YYAFNKLARAlVGTNNIDSNSRLCMSSAVVGYKRSlgaDAPPCSyeDLDCADCVLIAGSNMAF-----AHPVLFRRLEAA 193
Cdd:cd02750 127 GSRFASLIGG-VSLSFYDWYGDLPPGSPQTWGEQT---DVPESA--DWYNADYIIMWGSNVPVtrtpdAHFLTEARYNGA 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 194 KaarpemrIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSFIAEHTegfaDLKELVrdYTPAAVAD 273
Cdd:cd02750 201 K-------VVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKEKLYDEDYLKEYT----DLPFLV--YTPAWQEA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 274 ICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQP-NAMGGRetgslA 352
Cdd:cd02750 268 ITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNEGKNGGGWAHYVGQPrVLFVWR-----G 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 353 NLLPGHREAAdpghraevahywgveqlptspglsaiELFDAVHDGrikalwiactnpaqslpdqrkihealaRCPFVVVQ 432
Cdd:cd02750 343 NLFGSSGKGH--------------------------EYFEDAPEG---------------------------KLDLIVDL 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596976 433 EaFAGTETCQYADLLLPAASWGEK-EGSVTNSERRISHVRRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02750 370 D-FRMDSTALYSDIVLPAATWYEKhDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKKV 431
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
13-571 |
1.09e-35 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 144.93 E-value: 1.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 13 TCCYCGVGCG-------------------------------------------VLIEHDGERILGVQ-GDPRHPANFGRL 48
Cdd:cd02756 16 TCHFCIVGCGyhvyvwpvgeeggpspgqnaigydlvdqvpplnlqwypktmhyVVVTQDGREVYIVIvPDKECPVNSGNY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 49 CSKGASLHLT------GDLQARALYPQLRLGKQLARarSDWESALEHAAGRFAETIREHGPDSVAFYI------SGQLLt 116
Cdd:cd02756 96 STRGGTNAERiwspdnRVGETRLTTPLVRRGGQLQP--TTWDDAIDLVARVIKGILDKDGNDDAVFASrfdhggGGGGF- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 117 EDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGyKRSLGADAPPCSYEDLDCADCVLIAGSN-------MAFAHpvLFRR 189
Cdd:cd02756 173 ENNWGVGKFFFMALQTPFVRIHNRPAYNSEVHA-TREMGVGELNNSYEDARLADTIVLWGNNpyetqtvYFLNH--WLPN 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 190 LEAAKAAR-----------PEMRIVVIDPRRTDTCELAD--------LHLALLPGTDVALFHGILHILlWEDWidRSFIA 250
Cdd:cd02756 250 LRGATVSEkqqwfppgepvPPGRIIVVDPRRTETVHAAEaaagkdrvLHLQVNPGTDTALANAIARYI-YESL--DEVLA 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 251 EhtegfadlkelvrdytpaaVADICGIDRADLQRCAEWI------GRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATG 324
Cdd:cd02756 327 E-------------------AEQITGVPRAQIEKAADWIakpkegGYRKRVMFEYEKGIIWGNDNYRPIYSLVNLAIITG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 325 KIGRAGCGPfsltgqpNAMGGRETGSLANLLPGHREAADPGHRA-----------EVAHYWGVEQLPTSPglSAIELFDA 393
Cdd:cd02756 388 NIGRPGTGC-------VRQGGHQEGYVRPPPPPPPWYPQYQYAPyidqllisgkgKVLWVIGCDPYKTTP--NAQRLRET 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 394 VHDgRIKALWIACTNPAQSLPDQRKIHEAL---ARCP---FVVVQEAFAgTETCQYADLLLPAASWGE-KEGSVTNSERR 466
Cdd:cd02756 459 INH-RSKLVTDAVEAALYAGTYDREAMVCLigdAIQPgglFIVVQDIYP-TKLAEDAHVILPAAANGEmNETSMNGHERR 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 467 ISHVRRAVPPPGEARQDWNIVCDFARRL------EGHLRPAKPGLFAF----------ADSRSLFDE------YKLLTAG 524
Cdd:cd02756 537 LRLYEKFMDPPGEAMPDWWIAAMIANRIyelyqeEGKGGSAQYQFFGFiwkteednfmDGSQEFADGgefsedYYVLGQE 616
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 15596976 525 RdldLSGLSYALLDRLGPQ--QWP---FPTGAEQGTARLYADGRFPTASGRA 571
Cdd:cd02756 617 R---YEGVTYNRLKAVGVNgiQLPvttDTVTKILVTNVLRTEGVFDTEDGKA 665
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
11-496 |
1.11e-35 |
|
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other related proteins. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239158 [Multi-domain] Cd Length: 523 Bit Score: 142.58 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 11 ASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGaslHLTgdLQA-----RALYPQLRLGKQLARA------ 79
Cdd:cd02757 3 PSTCQGCTAWCGLQAYVEDGRVTKVEGNPLHPGSRGRLCAKG---HLG--LQQvydpdRILYPMKRTNPRKGRDvdpkfv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 80 RSDWESALEHAAGRFAETIREHGPDSVAfYISGQLLTEDYYAFNKLARALVGTNNIdSNSRLCMSSAVVGYKRSLGADAP 159
Cdd:cd02757 78 PISWDEALDTIADKIRALRKENEPHKIM-LHRGRYGHNNSILYGRFTKMIGSPNNI-SHSSVCAESEKFGRYYTEGGWDY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 160 PcSYeDLDCADCVLIAGSN-MAFAHPV-LFRRLEAAKAARpeMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHI 237
Cdd:cd02757 156 N-SY-DYANAKYILFFGADpLESNRQNpHAQRIWGGKMDQ--AKVVVVDPRLSNTAAKADEWLPIKPGEDGALALAIAHV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 238 LLWE---------DWID-------------RSFIAEHTEGF-ADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPR 294
Cdd:cd02757 232 ILTEglwdkdfvgDFVDgknyfkagetvdeESFKEKSTEGLvKWWNLELKDYTPEWAAKISGIPAETIERVAREFATAAP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 295 FLSLW-----CMGLNQSSAGSAknsalinLHLATGkigragcgpfsLTGQPNAMGGretgslanllpghreaadpghrae 369
Cdd:cd02757 312 AAAAFtwrgaTMQNRGSYNSMA-------CHALNG-----------LVGSIDSKGG------------------------ 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 370 vahywgveqlpTSPGLSaielfdavhDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAGtETCQYADLLLP 449
Cdd:cd02757 350 -----------LCPNMG---------VPKIKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMS-ETTYFADIVLP 408
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 15596976 450 AASWGEKEG---SVTNSERRISHVRRAVPPPGEARQDWNIVCDFARRLEG 496
Cdd:cd02757 409 DGHHFERWDvmsQENNLHPWLSIRQPVVKSLGEVREETEILIELAKKLDP 458
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
12-486 |
1.16e-35 |
|
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone oxidoreductase (NADH-Q-OR)/respiratory complex I/NADH dehydrogenase-1 (NDH-1). The NADH-Q-OR is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The atomic structure of complex I is not known and the mechanisms of electron transfer and proton pumping are not established. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Escherichia coli, this subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The nad11 gene is nuclear-encoded in animals, plants, and fungi, but is still encoded in the mitochondrial genome of some protists. The Nad11/NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain family belongs to the molybdopterin_binding (MopB) superfamily of proteins. Bacterial type II NADH-quinone oxidoreductases and NQR-type sodium-motive NADH-quinone oxidoreductases are not homologs of this domain family.
Pssm-ID: 239169 [Multi-domain] Cd Length: 386 Bit Score: 139.73 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 12 STCCYCGVGCGVLIEHDGERILGVQgdPR-HPA-NFGRLCSKG--ASLHLTGDlqARALYPQLRLGKQLARArsDWESAL 87
Cdd:cd02768 2 SIDVHDALGSNIRVDVRGGEVMRIL--PReNEAiNEEWISDKGrfGYDGLNSR--QRLTQPLIKKGGKLVPV--SWEEAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 88 EHAAGRfaetIREHGPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVvgyKRSLGADAPPCSYEDLD 167
Cdd:cd02768 76 KTVAEG----LKAVKGDKIGGIAGPRADLESLFLLKKLLNKL-GSNNIDHRLRQSDLPAD---NRLRGNYLFNTSIAEIE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 168 CADCVLIAGSNMAFAHPVLFRRL-EAAKaaRPEMRIVVIDPRRTDTceladlhlallpgtdvalfhgilhillwedWIDR 246
Cdd:cd02768 148 EADAVLLIGSNLRKEAPLLNARLrKAVK--KKGAKIAVIGPKDTDL------------------------------IADL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 247 SFIAEHteGFADLKELVRDYTPAAVADICgidrADLQ---RCAEWIGrsprflslwcmglnqSSAGSAKNSALINlhlat 323
Cdd:cd02768 196 TYPVSP--LGASLATLLDIAEGKHLKPFA----KSLKkakKPLIILG---------------SSALRKDGAAILK----- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 324 gkigragcgpfsltgqpnamggretgSLANLlpghreAADPGHRAEVahyWGVEQLPTSPGLSAIEL-----FDAVHDGR 398
Cdd:cd02768 250 --------------------------ALANL------AAKLGTGAGL---WNGLNVLNSVGARLGGAgldagLALLEPGK 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 399 IKALWIACTNPAQSLPDQRKiheALARCPFVVVQEAFAGtETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPG 478
Cdd:cd02768 295 AKLLLLGEDELDRSNPPAAV---ALAAADAFVVYQGHHG-DTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPG 370
|
....*...
gi 15596976 479 EARQDWNI 486
Cdd:cd02768 371 DAREDWKI 378
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
10-693 |
1.09e-34 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 142.50 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 10 TASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLHltgdlqaRALYPQLRLGKQLARA--RSD----- 82
Cdd:PRK15488 44 TPSICEMCSTRCPIEARVVNGKNVFIQGNPKAKSFGTKVCARGGSGH-------SLLYDPQRIVKPLKRVgeRGEgkwqe 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 83 --WESALEHAAGRFAETIREHGPDSVAFYI-SGQLLTedyYAFNkLARALvGTNNIDSNSRLCMSSAVVGYKRSLGADAP 159
Cdd:PRK15488 117 isWDEAYQEIAAKLNAIKQQHGPESVAFSSkSGSLSS---HLFH-LATAF-GSPNTFTHASTCPAGYAIAAKVMFGGKLK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 160 pcsyEDLDCADCV------LIAGSNMAFAHPVlfrrleAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHG 233
Cdd:PRK15488 192 ----RDLANSKYIinfghnLYEGINMSDTRGL------MTAQMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 234 ILHILLWEDWIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCA-EWIGRSPRFLSLWCMGLNQSSAGSAK 312
Cdd:PRK15488 262 LCHVLIEENLYDKAFVERYTSGFEELAASVKEYTPEWAEAISDVPADDIRRIArELAAAAPHAIVDFGHRATFTPEEFDM 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 313 NSALINLHLATGKIGRAGcGPFSLTGQP--NAMGGRETG-SLANllPGHR----------EAADPGHrAEVAHYWGVEQL 379
Cdd:PRK15488 342 RRAIFAANVLLGNIERKG-GLYFGKNASvyNKLAGEKVApTLAK--PGVKgmpkptakriDLVGEQF-KYIAAGGGVVQS 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 380 PTSPGLSAIELfdavhdgRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGS 459
Cdd:PRK15488 418 IIDATLTQKPY-------QIKGWVMSRHNPMQTVTDRADVVKALKKLDLVVVCDVYL-SESAAYADVVLPESTYLERDEE 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 460 VTN-SERRISH-VR-RAVPPPGEARQDWNIVCDFARRLeghlrpAKPGLFAFADSRslfdEYKLLTAGRDLDLsglsYAL 536
Cdd:PRK15488 490 ISDkSGKNPAYaLRqRVVEPIGDTKPSWQIFKELGEKM------GLGQYYPWQDME----TLQLYQVNGDHAL----LKE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 537 LDRLGPQQW--P---------------FPTGAEQGTARLYADG-RFPTASGRAQLVAE------PYRAAQEKRDARY--- 589
Cdd:PRK15488 556 LKKKGYVSFgvPlllrepkmvakfvarYPNAKAVDEDGTYGSQlKFKTPSGKIELFSAklealaPGYGVPRYRDVALkke 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 590 -PLTLNTGRLrdQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRG-----ALVLPvsaddSVRPG 663
Cdd:PRK15488 636 dELYFIQGKV--AVHTNGATQNVPLLANLMSDNAVWIHPQTAGKLGIKNGDEIRLENSVGkekgkALVTP-----GIRPD 708
|
730 740 750
....*....|....*....|....*....|....*..
gi 15596976 664 QAFLPMHWGDR-------FLKGLGCNVLTLPAFDPLS 693
Cdd:PRK15488 709 TLFAYMGFGSKnkeltraTGKGIHCGNLLPHVTSPVS 745
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
12-576 |
5.36e-33 |
|
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239166 [Multi-domain] Cd Length: 567 Bit Score: 135.30 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 12 STCCY--CGVGCGVLIEHDGERILGVQgdPRHPAN--FGRLCSKGASlHLTGDLQA-RALYPQLRLGKqlaRA-----RS 81
Cdd:cd02765 1 YTACPpnCGGRCPLKCHVRDGKIVKVE--PNEWPDktYKRGCTRGLS-HLQRVYSPdRLKYPMKRVGE---RGegkfeRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 82 DWESALEHAAGRFAETIREHGPDSVAFYISgqllTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPC 161
Cdd:cd02765 75 TWDEALDTIADKLTEAKREYGGKSILWMSS----SGDGAILSYLRLALLGGGLQDALTYGIDTGVGQGFNRVTGGGFMPP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 162 SYE--DLDCADCVLIAGSNMAFAHpvlFRRLE-AAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHIL 238
Cdd:cd02765 151 TNEitDWVNAKTIIIWGSNILETQ---FQDAEfFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 239 LWEDWIDRSFIAEHT--------------------------------------------------------------EGF 256
Cdd:cd02765 228 LEHNWYDEAFLKSNTsapflvredngtllrqadvtatpaedgyvvwdtnsdspepvaatninpalegeytingvkvhTVL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 257 ADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPfsl 336
Cdd:cd02765 308 TALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKPSGIWGFGGVDRYYHSHVFGRTAAILAALTGNIGRVGGGV--- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 337 tgqpnamggretgslanllpghreaadpghraevahywgveqlptspglsaielfdavhdGRIKALWIACTNPAQSLPDQ 416
Cdd:cd02765 385 ------------------------------------------------------------GQIKFMYFMGSNFLGNQPDR 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 417 RKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERR--ISHVRRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02765 405 DRWLKVMKNLDFIVVVDIFH-TPTVRYADIVLPAAHWFEVEDLLVRYTTHphVLLQQKAIEPLFESKSDFEIEKGLAERL 483
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 495 E-GHLRPAKPG--LFAFADSRSLFdeykllTAGRDLDLSGLSYALLDRLGPQQwpfPTGAeqgtarlYADGRFPTASGRA 571
Cdd:cd02765 484 GlGDYFPKTPEdyVRAFMNSDDPA------LDGITWEALKEEGIIMRLATPED---PYVA-------YLDQKFGTPSGKL 547
|
....*
gi 15596976 572 QLVAE 576
Cdd:cd02765 548 EFYNE 552
|
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
587-706 |
3.42e-32 |
|
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 with the release of a proton and two electrons. It is a component of the anaerobic formate hydrogen lyase complex. The E. coli formate dehydrogenase H (Fdh-H) is a monomer composed of a single polypeptide chain with a Mo active site region and a [4Fe-4S] center. This CD (MopB_CT_Formate-Dh_H) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239191 [Multi-domain] Cd Length: 116 Bit Score: 121.19 E-value: 3.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 587 ARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAF 666
Cdd:cd02790 1 EEYPLVLTTGRVLYHYHTGTMTRRAEGLDAIAPEEYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRVPEGVVF 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15596976 667 LPMHWGDRflkglGCNVLTLPAFDPLSKQPELKHAGVQVE 706
Cdd:cd02790 81 MPFHFAEA-----AANLLTNAALDPVAKIPEFKVCAVRVE 115
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
591-701 |
5.97e-31 |
|
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - containing oxidoreductases and tungsten formylmethanofuran dehydrogenase subunit d (FwdD) and molybdenum formylmethanofuran dehydrogenase subunit (FmdD); where the domain constitutes almost the entire subunit. The formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and has a molybdopterin dinucleotide cofactor. This domain corresponds to the C-terminal domain IV in dimethyl sulfoxide (DMSO)reductase which interacts with the 2-amino pyrimidone ring of both molybdopterin guanine dinucleotide molecules.
Pssm-ID: 426328 [Multi-domain] Cd Length: 110 Bit Score: 117.37 E-value: 5.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 591 LTLNTGRLRDQWHGMSRTGTCARLFGHEEEAlVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPMH 670
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEV-VEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFG 79
|
90 100 110
....*....|....*....|....*....|.
gi 15596976 671 WGDRFlKGLGCNVLTLPAFDPLSKQPELKHA 701
Cdd:pfam01568 80 WWYEP-RGGNANALTDDATDPLSGGPEFKTC 109
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
17-494 |
2.81e-30 |
|
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239171 [Multi-domain] Cd Length: 617 Bit Score: 127.44 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 17 CGVGCG------VLIEhDGErILGVQGDPRHPANFG----RLCSKGASL--HLTG-DlqaRALYPQLRLGKqlaR----- 78
Cdd:cd02770 4 CTVNCGgrcplkAHVK-DGV-ITRIETDDTGDDDPGfhqiRACLRGRSQrkRVYNpD---RLKYPMKRVGK---Rgegkf 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 79 ARSDWESALEHAAGRFAETIREHGPDSVafYISGQllTEDYYAF----NKLAR--ALVG--TNNIDSNSRLCMSSAvvgY 150
Cdd:cd02770 76 VRISWDEALDTIASELKRIIEKYGNEAI--YVNYG--TGTYGGVpagrGAIARllNLTGgyLNYYGTYSWAQITTA---T 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 151 KRSLGADAPPCSYEDLDCADCVLIAGSN-----MAFAHPVLFrrLEAAKAARpeMRIVVIDPRRTDTCE-LADLHLALLP 224
Cdd:cd02770 149 PYTYGAAASGSSLDDLKDSKLVVLFGHNpaetrMGGGGSTYY--YLQAKKAG--AKFIVIDPRYTDTAVtLADEWIPIRP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 225 GTDVALFHGILHILLWEDWIDRSFIAEHTEGF--------ADLKELVRDY-----------TPAAVADICGIDRADLQRC 285
Cdd:cd02770 225 GTDAALVAAMAYVMITENLHDQAFLDRYCVGFdaehlpegAPPNESYKDYvlgtgydgtpkTPEWASEITGVPAETIRRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 286 AEWIG--RSPRFLSLWcmGLNQSSAGSAKNSALINLHLATGKIGRAGCGPfsltgqpnamGGRETGSLANLLPGhreaad 363
Cdd:cd02770 305 AREIAttKPAAILQGW--GPQRHANGEQAARAIMMLAAMTGNVGIPGGNT----------GARPGGSAYNGAGL------ 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 364 PGHRAEVAhywgvEQLPTSPGLSAIEL------FDAVHDGR------IKALW-IACTNPAQSLPDQRKIHEAL----ARC 426
Cdd:cd02770 367 PAGKNPVK-----TSIPCFMWTDAIERgeemtaDDGGVKGAdklksnIKMIWnYAGNTLINQHSDDNNTTRALlddeSKC 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596976 427 PFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISHV----RRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02770 442 EFIVVIDNFM-TPSARYADILLPDTTELEREDIVLTSNAGMMEYliysQKAIEPLYECKSDYEICAELAKRL 512
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
83-670 |
5.88e-30 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 127.37 E-value: 5.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 83 WESALEHAAGRFAETirehgPDSVAFYISGQLLTEDYYAFNKLARALVGTNNIDSNSRL-------CMSSAVVGYKRSLg 155
Cdd:PRK07860 296 WSEALAVAARGLAAA-----RGRVGVLVGGRLTVEDAYAYAKFARVALGTNDIDFRARPhsaeeadFLAARVAGRGLGV- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 156 adappcSYEDLDCADCVLIAGSNMAFAHPVLFRRLEaaKAARPE-MRIVVIDPRRTDTceLADLHLALL---PGTDVALf 231
Cdd:PRK07860 370 ------TYADLEKAPAVLLVGFEPEEESPIVFLRLR--KAARKHgLKVYSIAPFATRG--LEKMGGTLLrtaPGGEAAA- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 232 hgilhillwedwidrsfIAEHTEGFADLKELVRdyTPAAVAdICGidradlQRCAEwigrSPRFLSlwcmglnqssagsa 311
Cdd:PRK07860 439 -----------------LDALATGAPDVAELLR--TPGAVI-LVG------ERLAT----VPGALS-------------- 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 312 knsALINLHLATG-KIG----RAGcgpfsltgqpnAMGGRETGSLANLLPGHREAADPGHRAEVAHYWGVEQLPTSPGLS 386
Cdd:PRK07860 475 ---AAARLADATGaRLAwvprRAG-----------ERGALEAGALPTLLPGGRPVADPAARAEVAAAWGVDELPAAPGRD 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 387 AIELFDAVHDGRIKALWIACTNPAqSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERR 466
Cdd:PRK07860 541 TAGILAAAAAGELGALLVGGVEPA-DLPDPAAALAALDAAGFVVSLELRH-SAVTERADVVLPVAPVAEKAGTFLNWEGR 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 467 ISHVRRAVPPPGearqdwnivcdfarrleghlrpakpglfAFADSR---SLFDEyklltAGRDLDLSGLSYAL--LDRLG 541
Cdd:PRK07860 619 LRPFEAALRTTG----------------------------ALSDLRvldALADE-----MGVDLGLPTVAAARaeLARLG 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 542 PqqWpfpTGAEQGTARLYADGRFPTASGRAQLvaepyraaqekrdARYPLTLNTGRLRDqwhgmsrtGTCArLFGHEEEA 621
Cdd:PRK07860 666 A--W---DGARAAAPAVPAAAPPQPGAGEAVL-------------ATWRMLLDDGRLQD--------GEPH-LAGTARPP 718
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 15596976 622 LVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVrPGQAFLPMH 670
Cdd:PRK07860 719 VARLSAATAAEIGVADGDAVTVSTERGSITLPLAITDMP-DRVVWLPLN 766
|
|
| PRK09939 |
PRK09939 |
acid resistance putative oxidoreductase YdeP; |
83-430 |
1.04e-27 |
|
acid resistance putative oxidoreductase YdeP;
Pssm-ID: 182156 [Multi-domain] Cd Length: 759 Bit Score: 120.15 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 83 WESALEHAAGRFaETIREhgPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCS 162
Cdd:PRK09939 127 WQQAFDEIGARL-QSYSD--PNQVEFYTSGRTSNEAAFLYQLFAREY-GSNNFPDCSNMCHEPTSVGLAASIGVGKGTVL 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 163 YEDLDCADCVLIAGSNMAFAHPVLFRRLEAAkaARPEMRIVVIDPRRTDTCE------------------LADLHLALLP 224
Cdd:PRK09939 203 LEDFEKCDLVICIGHNPGTNHPRMLTSLRAL--VKRGAKMIAINPLQERGLErftapqnpfemltnsetqLASAYYNVRI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 225 GTDVALFHGILHILLWED----------WIDRSFIAEHTEGFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPR 294
Cdd:PRK09939 281 GGDMALLKGMMRLLIERDdaasaagrpsLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAER 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 295 FLSLWCMGLNQSSAGSAKNSALINLHLATGKIGRAGCGPFSLTGQPNAMGGRETGSlanllpghREAADPGHRAEVAHYW 374
Cdd:PRK09939 361 TIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGI--------TEKPSAEFLARLGERY 432
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 15596976 375 GVEQlPTSPGLSAIELFDAVHDGRIKALWIACTNPAQSLPDQRKIHEALARCPFVV 430
Cdd:PRK09939 433 GFTP-PHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAV 487
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
193-494 |
3.76e-27 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239170 [Multi-domain] Cd Length: 609 Bit Score: 117.75 E-value: 3.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 193 AKAARPEMRIVVIDPRRTDTCELADL-HLALLPGTDVALFHGILHILLWEDWIDRSFIAEHTEGFADLKELVR---D--- 265
Cdd:cd02769 202 KALKDRGIRFISISPLRDDTAAELGAeWIAIRPGTDVALMLALAHTLVTEGLHDKAFLARYTVGFDKFLPYLLgesDgvp 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 266 YTPAAVADICGIDRADLQRCAEWIGRSPRFLSL-WCMglNQSSAGSAKNSALINLHLATGKIGRAGCG-PFSLTGQPNAM 343
Cdd:cd02769 282 KTPEWAAAICGIPAETIRELARRFASKRTMIMAgWSL--QRAHHGEQPHWMAVTLAAMLGQIGLPGGGfGFGYHYSNGGG 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 344 GGRETGSLANLLPGHREAAD--PGHRAevahywgVEQLpTSPGlsaiELFDavHDGR------IKALWIACTNPAQSLPD 415
Cdd:cd02769 360 PPRGAAPPPALPQGRNPVSSfiPVARI-------ADML-LNPG----KPFD--YNGKkltypdIKLVYWAGGNPFHHHQD 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 416 QRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAASWGEKEG-SVTNSERRISHVRRAVPPPGEARQDWNIVCDFARRL 494
Cdd:cd02769 426 LNRLIRAWQKPETVIVHEPFW-TATARHADIVLPATTSLERNDiGGSGDNRYIVAMKQVVEPVGEARDDYDIFADLAERL 504
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
598-699 |
7.43e-27 |
|
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.
Pssm-ID: 239176 [Multi-domain] Cd Length: 101 Bit Score: 105.09 E-value: 7.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 598 LRDQWHGMSRTGtCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPMHWGDRFLK 677
Cdd:cd02775 1 LRDHFHSGTRTR-NPWLRELAPEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGGR 79
|
90 100
....*....|....*....|..
gi 15596976 678 GLGCNVLTLPAFDPLSKQPELK 699
Cdd:cd02775 80 GGNANVLTPDALDPPSGGPAYK 101
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
12-519 |
1.96e-25 |
|
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. These members belong to the molybdopterin_binding (MopB) superfamily of proteins
Pssm-ID: 239164 [Multi-domain] Cd Length: 679 Bit Score: 112.62 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 12 STCCYCGVGCGVLIE-HDGErILGVQGDPRHPANFGRLCSKGASLHLTGDLQARALYPQLRLGKQLARA--RSDWESALE 88
Cdd:cd02763 2 TTCYMCACRCGIRVHlRDGK-VRYIKGNPDHPLNKGVICAKGSSGIMKQYSPARLTKPLLRKGPRGSGQfeEIEWEEAFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 89 HAAGRFAEtIREHGPDSVAFYiSGQlltEDYYAFNKLARALVGTNNIDSNSRLCMSSAVVGYKRSLGADAPPCSYEDLDC 168
Cdd:cd02763 81 IATKRLKA-ARATDPKKFAFF-TGR---DQMQALTGWFAGQFGTPNYAAHGGFCSVNMAAGGLYSIGGSFWEFGGPDLEH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 169 ADCVLIAGSnmAFAHPVLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDWIDRSF 248
Cdd:cd02763 156 TKYFMMIGV--AEDHHSNPFKIGIQKLKRRGGKFVAVNPVRTGYAAIADEWVPIKPGTDGAFILALAHELLKAGLIDWEF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 249 IAEHTEGfadlKELVrDYTPAAVADICGIDRADLQRCA-------------------EWIGR-----SPRFLSLWCM-GL 303
Cdd:cd02763 234 LKRYTNA----AELV-DYTPEWVEKITGIPADTIRRIAkelgvtardqpielpiawtDVWGRkhekiTGRPVSFHAMrGI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 304 NQSSAGSAKNSALINLHLATGKIGRAGC----GPFSLTGQPnamGGRETGSLANLLPGHREA-------ADPGH------ 366
Cdd:cd02763 309 AAHSNGFQTIRALFVLMMLLGTIDRPGGfrhkPPYPRHIPP---LPKPPKIPSADKPFTPLYgpplgwpASPDDllvded 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 367 ----RAEVAHYWgveQLPTSP-GL--SAIELFDAVHDGRIKALWIACTNPA-QSLPDQRKIHEALA--------RCPFVV 430
Cdd:cd02763 386 gnplRIDKAYSW---EYPLAAhGCmqNVITNAWRGDPYPIDTLMIYMANMAwNSSMNTPEVREMLTdkdasgnyKIPFII 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 431 VQEAFAgTETCQYADLLLPAASWGEKEGSVTNSERRISH-------VRR-AVPPPGEARQDWNIVCDFARRLeghlrpak 502
Cdd:cd02763 463 VCDAFY-SEMVAFADLVLPDTTYLERHDAMSLLDRPISEadgpvdaIRVpIVEPKGDVKPFQEVLIELGTRL-------- 533
|
570
....*....|....*....
gi 15596976 503 pGLFAF--ADSRSLFDEYK 519
Cdd:cd02763 534 -GLPGFtnEDGTRKYRDYP 551
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
587-706 |
1.91e-23 |
|
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate respiration in bacteria such as in the E. coli formate dehydrogenase N (Fdh-N). Fdh-N is a membrane protein that is a complex of three different subunits and is the major electron donor to the nitrate respiratory chain. Also included in this CD is the Desulfovibrio gigas tungsten formate dehydrogenase, DgW-FDH. In contrast to Fdh-N, which is a functional heterotrimer, DgW-FDH is a heterodimer. The DgW-FDH complex is composed of a large subunit carrying the W active site and one [4Fe-4S] center, and a small subunit that harbors a series of three [4Fe-4S] clusters as well as a putative vacant binding site for a fourth cluster. The smaller subunit is not included in this alignment. This CD (MopB_CT_Formate-Dh-Na-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239193 [Multi-domain] Cd Length: 122 Bit Score: 96.14 E-value: 1.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 587 ARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAF 666
Cdd:cd02792 1 EEFPLVLTTGRLTEHFHGGNMTRNSPYLAELQPEMFVEISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15596976 667 LPMHWGDRFL-KGLGCNVLTLPAFDPLSKQPELKHAGVQVE 706
Cdd:cd02792 81 IPYHWGGMGLvIGDSANTLTPYVGDPNTQTPEYKAFLVNIE 121
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
17-708 |
1.81e-22 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 103.57 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 17 CGVGCGV---LIEH--DGErILGVQGDPRHPANFG-----RLCSKGASLHLTGDLQARALYPQLRLGK--QLARARSDWE 84
Cdd:PRK14990 63 CTVNCGSrcpLRMHvvDGE-IKYVETDNTGDDNYDglhqvRACLRGRSMRRRVYNPDRLKYPMKRVGArgEGKFERISWE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 85 SALEHAAGRFAETIREHGPDSVAF-YISGQL---LTEDYYAFNKLARALVGTNNIDSNSRLCMSSAVV--GYKRSLGADA 158
Cdd:PRK14990 142 EAYDIIATNMQRLIKEYGNESIYLnYGTGTLggtMTRSWPPGNTLVARLMNCCGGYLNHYGDYSSAQIaeGLNYTYGGWA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 159 PPCSYEDLDCADCVLIAGSN-----MAFAHPVLFrrLEAAKAaRPEMRIVVIDPRRTDT-CELADLHLALLPGTDVALFH 232
Cdd:PRK14990 222 DGNSPSDIENSKLVVLFGNNpgetrMSGGGVTYY--LEQARQ-KSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVN 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 233 GILHILLWEDWIDRSFIAEHTEGFaDLKEL---------VRDY-----------TPAAVADICGIDRADLQRCAEWIGRS 292
Cdd:PRK14990 299 GLAYVMITENLVDQPFLDKYCVGY-DEKTLpasapknghYKAYilgegpdgvakTPEWASQITGVPADKIIKLAREIGST 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 293 -PRFLSL-WcmGLNQSSAGSAKNSALINLHLATGKIGRAGcgpfsltgqpNAMGGREtGSLAnlLPGHREAA--DPGHRA 368
Cdd:PRK14990 378 kPAFISQgW--GPQRHANGEIATRAISMLAILTGNVGING----------GNSGARE-GSYS--LPFVRMPTleNPIQTS 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 369 EVAHYWgVEQLPTSPGLSAieLFDAVH-----DGRIKALWIACTNpaqSLPDQR----KIHEAL---ARCPFVVVQEAFA 436
Cdd:PRK14990 443 ISMFMW-TDAIERGPEMTA--LRDGVRgkdklDVPIKMIWNYAGN---CLINQHseinRTHEILqddKKCELIVVIDCHM 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 437 gTETCQYADLLLPAASWGEK-EGSVTNSERRISHV---RRAVPPPGEARQDWNIVCDFARRL------------EGHLRp 500
Cdd:PRK14990 517 -TSSAKYADILLPDCTASEQmDFALDASCGNMSYVifnDQVIKPRFECKTIYEMTSELAKRLgveqqftegrtqEEWMR- 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 501 akpglFAFADSRSL------FDEYKLLTAGRDLDLSG--LSYALLdRLGPQQWPF--PTGA----EQGTARLYADGRFPT 566
Cdd:PRK14990 595 -----HLYAQSREAipelptFEEFRKQGIFKKRDPQGhhVAYKAF-REDPQANPLttPSGKieiySQALADIAATWELPE 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 567 ASgraqlVAEP-------YRAAQEKRDARYPLTLNTGRLRDQWHGMSRTGTCARLFGHEEealVHLHPEELRRRQLLDGQ 639
Cdd:PRK14990 669 GD-----VIDPlpiytpgFESYQDPLNKQYPLQLTGFHYKSRVHSTYGNVDVLKAACRQE---MWINPLDAQKRGINNGD 740
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15596976 640 LVRLKSRRGALVLPVSADDSVRPGQAFL-PMHWGD----RFLKGLGCNVLTLPAFDPLSKQPELKHAGVQVESV 708
Cdd:PRK14990 741 KVRIFNDRGEVHIEAKVTPRMMPGVVALgEGAWYDpdakRVDKGGCINVLTTQRPSPLAKGNPSHTNLVQVEKV 814
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
82-486 |
1.29e-20 |
|
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1), found in beta- and gammaproteobacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239173 [Multi-domain] Cd Length: 414 Bit Score: 95.50 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 82 DWESALEHAAGRFAETIREHGPDSVAFYISGQLLTEDYYAFNKLARALvGTNNIDsnSRLCMSSAVVGYKRSlGADAPPC 161
Cdd:cd02772 70 DWETALEYVAEGLSAIIKKHGADQIGALASPHSTLEELYLLQKLARGL-GSDNID--HRLRQSDFRDDAKAS-GAPWLGM 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 162 SYEDLDCADCVLIAGSNMAFAHPVLFRRLEaaKAARPEMRIVVIDPrrtdtceLADLHLALLPGTDVALFHGILHILLwe 241
Cdd:cd02772 146 PIAEISELDRVLVIGSNLRKEHPLLAQRLR--QAVKKGAKLSAINP-------ADDDFLFPLSGKAIVAPSALANALA-- 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 242 dwiDRSFIAEHTEGFAdLKELVRDYTPAAVADICGIDRADLQRCAEWIGRsprflslwcMGLNQSSAGSAKNSALINLHL 321
Cdd:cd02772 215 ---QVAKALAEEKGLA-VPDEDAKVEASEEARKIAASLVSAERAAVFLGN---------LAQNHPQAATLRALAQEIAKL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 322 ATGKIGRagcgpfsLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVahYWGVEqlptsPGLsaielfdavhdgrika 401
Cdd:cd02772 282 TGATLGV-------LGEGANSVGAYLAGALPHGGLNAAAMLEQPRKAYL--LLNVE-----PEL---------------- 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 402 lwiACTNPAQSLpdqrkihEALARCPFVVVQEAFAGTETCQYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEAR 481
Cdd:cd02772 332 ---DCANPAQAL-------AALNQAEFVVALSAFASAALLDYADVLLPIAPFTETSGTFVNLEGRVQSFKGVVKPLGEAR 401
|
....*
gi 15596976 482 QDWNI 486
Cdd:cd02772 402 PAWKV 406
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
386-498 |
1.92e-20 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 95.29 E-value: 1.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 386 SAIELFDAVHDGRIKALWIACTNPAQSLPDQrkIHEALARCPFVVVQEAFaGTETCQYADLLLPAASWGEKEGSVTNSER 465
Cdd:COG1034 320 DAAAILEAAEAGKLKALVLLGADPYDLDPAA--ALAALAKADFVVVLDHF-GSATAERADVVLPAAAFAEKSGTFVNLEG 396
|
90 100 110
....*....|....*....|....*....|...
gi 15596976 466 RISHVRRAVPPPGEARQDWNIVCDFARRLEGHL 498
Cdd:COG1034 397 RVQRFNAAVPPPGEARPDWRVLRALANALGAGL 429
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
7-56 |
3.48e-19 |
|
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for which the structure is known. This first domain (residues 1 to 60) of PDB:1aa6 is an Fe4S4 cluster just below the protein surface.
Pssm-ID: 428168 [Multi-domain] Cd Length: 55 Bit Score: 81.96 E-value: 3.48e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15596976 7 LRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLH 56
Cdd:pfam04879 1 MKVVKTICPYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEGRLCVKGRFGY 50
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
7-56 |
8.61e-19 |
|
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is found in a number of reductase/dehydrogenase families, which include the periplasmic nitrate reductase precursor and the formate dehydrogenase alpha chain.
Pssm-ID: 197994 [Multi-domain] Cd Length: 55 Bit Score: 80.76 E-value: 8.61e-19
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15596976 7 LRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKGASLH 56
Cdd:smart00926 1 EKWVPTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGL 50
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
12-570 |
2.81e-17 |
|
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other related proteins. The Salmonella enterica tetrathionate reductase catalyses the reduction of trithionate but not sulfur or thiosulfate. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239159 [Multi-domain] Cd Length: 735 Bit Score: 86.63 E-value: 2.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 12 STCCYCGVGCG--VLIEHDGERILGVQGDPRHPANF---------------------------GRLCSKGASLhltgdlq 62
Cdd:cd02758 2 SSCLGCWTQCGirVRVDKETGKVLRIAGNPYHPLNTapslpyntplkeslylslvgenglkarATACARGNAG------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 63 ARALYPQLRLGKQLARA--RSD-------WESALEHAA--GRFAET--------IR-----------EHGPDSVAF-YIS 111
Cdd:cd02758 75 LQYLYDPYRVLQPLKRVgpRGSgkwkpisWEQLIEEVVegGDLFGEghveglkaIRdldtpidpdhpDLGPKANQLlYTF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 112 GQllTEDYYAFNK-LARALVGTNNIDSNSRLCMSSAVVGYKRSLG-ADAPPCSYEDLDCADCVLIAGSNMAFAHPVLFR- 188
Cdd:cd02758 155 GR--DEGRTPFIKrFANQAFGTVNFGGHGSYCGLSYRAGNGALMNdLDGYPHVKPDFDNAEFALFIGTSPAQAGNPFKRq 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 189 -RLEAAKAARPEMRIVVIDPR--RTDT-CELADLHLALLPGTDVALFHGILHILLWEDWIDRSFIAEHTE---------- 254
Cdd:cd02758 233 aRRLAEARTEGNFKYVVVDPVlpNTTSaAGENIRWVPIKPGGDGALAMAMIRWIIENERYNAEYLSIPSKeaakaageps 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 255 ---------------GFADLKELVRDYTPAAVADICGIDRADLQRCAEWIGRSPRFLSLWCMGLNQSSAGSAKNSALINL 319
Cdd:cd02758 313 wtnathlvitvrvksALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTSHGRAAAVVHHGGTMHSNGFYNAYAIRML 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 320 HLATGKIGRAGcGpFSLTGQPNAMGGRETGSLANLLPGH---------REAAD----PGHRAEVAH----Y-----Wgve 377
Cdd:cd02758 393 NALIGNLNWKG-G-LLMSGGGFADNSAGPRYDFKKFFGEvkpwgvpidRSKKAyektSEYKRKVAAgenpYpakrpW--- 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 378 qLPTSPGLSAiELFDAVHDG---RIKALWIACTNPAQSLPDQRKIHEAL----ARCPFVVVQEAFAGtETCQYADLLLPA 450
Cdd:cd02758 468 -YPLTPELYT-EVIASAAEGypyKLKALILWMANPVYGAPGLVKQVEEKlkdpKKLPLFIAIDAFIN-ETSAYADYIVPD 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 451 ASWGEKEGSVTN---SERRISHVRR-AVPPP------GEARQDWNIVCDFARRLE--GHLRPAKPGLFAFADSRSLFDEY 518
Cdd:cd02758 545 TTYYESWGFSTPwggVPTKASTARWpVIAPLtektanGHPVSMESFLIDLAKALGlpGFGPNAIKDGQGNKFPLNRAEDY 624
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596976 519 KLLTAG---------------RDLDLSGLSY---ALLDRLGPQQWPFptgaeqgTARLYA-DGRFPTASGR 570
Cdd:cd02758 625 YLRVAAniaydgkapvpdaseEELKLTGVNRpipALKRTLKPEEWRK-------VAYILArGGRFAPYEES 688
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
13-460 |
4.75e-15 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 78.35 E-value: 4.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 13 TCCYCGVGCGVL-IEHDGERILGVQgdprhpanfgRLCSKGASLHLTGDLQARALYPQLRlGKQlararSDWESALEHAA 91
Cdd:COG1029 9 VCPFCGCLCDDLeVEVEGGKIVVVK----------NACAIGAAKFERAVSDHRITSPRIR-GKE-----VSLEEAIDKAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 92 GRFAETIRehgPdsvAFYISGQLLTEDYYAFNKLARALVGTnnIDSNSRLCMSSAVVGYKRS------LGadappcsyED 165
Cdd:COG1029 73 EILANAKR---P---LIYGLSSTDCEAMRAGLALAERVGAV--VDNTASVCHGPSLLALQDVgwptctLG--------EV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 166 LDCADCVLIAGSNMAFAHP------VLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALfhgilhill 239
Cdd:COG1029 137 KNRADVIIYWGCNPVHAHPrhmsrySVFPRGFFTPKGRKDRTVIVVDPRPTDTAKVADLHLQVKPGRDYEV--------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 240 wedwidrsfiaehtegFADLKELVRDYTPAAvADICGIDRADLQRCAEWIgRSPRFLSL-WCMGLNQSSAGSAKNSALIN 318
Cdd:COG1029 208 ----------------LSALRALVRGKELSP-EEVAGIPVEDLEELAERL-KNAKYGVIfWGMGLTQSPGKHLNVDAAIE 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 319 LHLATGKIGRAGCGPfsltgqpnaMGGRE----TGSLANLLPGHREAAD--PGHraevAHYwgveqlptSPGLSAIElfD 392
Cdd:COG1029 270 LVRDLNRYTKFSILP---------LRGHYnvagANQVASWQTGYPFRVDfsRGY----PRY--------NPGETSAV--D 326
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15596976 393 AVHDGRIKALWIACTNPAQSLPdqRKIHEALARCPFVVVqeAFAGTETCQYADLLLPAASWG-EKEGSV 460
Cdd:COG1029 327 LLARGEVDALLWVASDPGAHFP--PDAVEHLAKIPTIVI--DPHGTPTTEVADVVIPVAIPGiEHGGTA 391
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
193-494 |
2.33e-14 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 77.40 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 193 AKAARPEMRIVVIDPRRTDT-----CEladlHLALLPGTDVALFHGILHILLWEDWIDRSFIAEHTEGFADL------KE 261
Cdd:PRK15102 248 EKVAKGEINVISIDPVVTKTqnylgCE----HLYVNPQTDVPLMLALAHTLYSENLYDKKFIDNYCLGFEQFlpyllgEK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 262 LVRDYTPAAVADICGIDRADLQRCAEWI--GRSpRFLSLWCMGLNQSSAGSAKNSALinlhLAT--GKIGRAGcGPFSLT 337
Cdd:PRK15102 324 DGVPKTPEWAEKICGIDAETIRELARQMakGRT-QIIAGWCIQRQQHGEQPYWMGAV----LAAmlGQIGLPG-GGISYG 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 338 GQPNAMGGRETGslANLLPGHREAADPGHRA--EVAHYWGV-EQLPTSPGLSAI----ELFDAvhDGR------IKALWI 404
Cdd:PRK15102 398 HHYSGIGVPSSG--GAIPGGFPGNLDTGQKPkhDNSDYKGYsSTIPVARFIDAIlepgKTINW--NGKkvtlppLKMMIF 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 405 ACTNPAQSLPDQRKIHEALARCPFVVVQEaFAGTETCQYADLLLPAASWGEKE-----GSVTNseRRISHVRRAVPPPGE 479
Cdd:PRK15102 474 SGTNPWHRHQDRNRMKEAFRKLETVVAID-NQWTATCRFADIVLPACTQFERNdidqyGSYSN--RGIIAMKKVVEPLFE 550
|
330
....*....|....*
gi 15596976 480 ARQDWNIVCDFARRL 494
Cdd:PRK15102 551 SRSDFDIFRELCRRF 565
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
10-458 |
5.52e-14 |
|
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like homologs (PHLH) of molybdopterin binding (MopB) proteins. This CD is of the PHLH region homologous to the catalytic molybdopterin-binding subunit of MopB homologs.
Pssm-ID: 239165 [Multi-domain] Cd Length: 524 Bit Score: 75.60 E-value: 5.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 10 TASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKG-ASLHLTGDlQARALYPqLRLGKQLARARSDWESALE 88
Cdd:cd02764 45 YATSLVPAGEGQGVLVKTVDGRPIKIEGNPDHPASLGGTSARAqASVLSLYD-PDRAQGP-LRRGIDGAYVASDWADFDA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 89 HAAGRFAETireHGPDSVAFyISGQLL---TEDYYAFnkLARALVGTNN--IDSNSRLCMSSAvvgYKRSLGADAPPcSY 163
Cdd:cd02764 123 KVAEQLKAV---KDGGKLAV-LSGNVNsptTEALIGD--FLKKYPGAKHvvYDPLSAEDVNEA---WQASFGKDVVP-GY 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 164 eDLDCADCVLIAGSNM--AFAHPVLFRRLEAAK----AARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHI 237
Cdd:cd02764 193 -DFDKAEVIVSIDADFlgSWISAIRHRHDFAAKrrlgAEEPMSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHK 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 238 LLwedwidRSFIAEHTEGFADLKELvrDYTPAAVADICGIDRADLQRCAEWIGRSPRflSLWCMGLNQSSAGSAKNSALI 317
Cdd:cd02764 272 LI------KKGAGSSLPDFFRALNL--AFKPAKVAELTVDLDKALAALAKALAAAGK--SLVVAGSELSQTAGADTQVAV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 318 N-LHLATGKIGRAgcgpfsltgqpnamggretgslanllpghreaadpghraeVAHYWGVEQLPTSPGLSAIELFDAVHD 396
Cdd:cd02764 342 NaLNSLLGNDGKT----------------------------------------VDHARPIKGGELGNQQDLKALASRINA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15596976 397 GRIKALWIACTNPAQSLPDQRKIHEALARCPFVVVQEAFAgTETCQYADLLLPAA----SWGEKEG 458
Cdd:cd02764 382 GKVSALLVYDVNPVYDLPQGLGFAKALEKVPLSVSFGDRL-DETAMLCDWVAPMShgleSWGDAET 446
|
|
| Bfd |
COG2906 |
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism]; |
854-900 |
5.59e-11 |
|
Bacterioferritin-associated ferredoxin [Inorganic ion transport and metabolism];
Pssm-ID: 442150 [Multi-domain] Cd Length: 54 Bit Score: 58.29 E-value: 5.59e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 15596976 854 CSCQNVSQQTVLGGIARGL-DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:COG2906 4 CLCNGVTDRQIRAAIAEGAtSLEELRAALGAGTQCGSCVPEARELLAE 51
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
601-708 |
3.26e-10 |
|
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239183 [Multi-domain] Cd Length: 129 Bit Score: 58.56 E-value: 3.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 601 QWHGMSRTGTcarlfgheeealVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPMHWGDRF----- 675
Cdd:cd02782 25 RLVKGRNRCT------------LRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDYpgvsg 92
|
90 100 110
....*....|....*....|....*....|....*..
gi 15596976 676 ---LKGLGCNVLTLPA-FDPLSKQPELKHAGVQVESV 708
Cdd:cd02782 93 agsRPGVNVNDLTDDTqRDPLSGNAAHNGVPVRLARV 129
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
442-487 |
3.25e-09 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 59.97 E-value: 3.25e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15596976 442 QYADLLLPAASWGEKEGSVTNSERRISHVRRAVPPPGEARQDWNIV 487
Cdd:cd02773 323 QIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKIL 368
|
|
| Fer2_BFD |
pfam04324 |
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved ... |
854-899 |
3.72e-09 |
|
BFD-like [2Fe-2S] binding domain; The two Fe ions are each coordinated by two conserved cysteine residues. This domain occurs alone in small proteins such as Bacterioferritin-associated ferredoxin (BFD). The function of BFD is not known, but it may may be a general redox and/or regulatory component involved in the iron storage or mobilization functions of bacterioferritin in bacteria. This domain is also found in nitrate reductase proteins in association with Nitrite and sulphite reductase 4Fe-4S domain (pfam01077), Nitrite/Sulfite reductase ferredoxin-like half domain (pfam03460) and Pyridine nucleotide-disulphide oxidoreductase (pfam00070). It is also found in NifU nitrogen fixation proteins, in association with NifU-like N terminal domain (pfam01592) and NifU-like domain (pfam01106).
Pssm-ID: 461261 [Multi-domain] Cd Length: 50 Bit Score: 53.30 E-value: 3.72e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 15596976 854 CSCQNVSQQTVLGGIARGL-DLDGLKREFGCGTGCGSCVPEIKRLLA 899
Cdd:pfam04324 3 CRCFGVTDGEIRDAIREGLtTVEEVKRRTKAGTGCGSCRPAIEEILA 49
|
|
| MopB_FmdB-FwdB |
cd02761 |
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, ... |
13-478 |
4.20e-09 |
|
The MopB_FmdB-FwdB CD contains the molybdenum/tungsten formylmethanofuran dehydrogenases, subunit B (FmdB/FwdB), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239162 [Multi-domain] Cd Length: 415 Bit Score: 59.65 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 13 TCCYCGVGCGVL-IEHDGERILGvqgdPRHpanfgrLCSKGASlHLTGdLQARALYPQLRlGKQlararSDWESALEHAA 91
Cdd:cd02761 3 VCPFCGLLCDDIeVEVEDNKITK----VRN------ACRIGAA-KFAR-YERRITTPRID-GKP-----VSLEEAIEKAA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 92 GRFAETIRehgPdsvAFYISGQLLTEDYYAFNKLARALVGTnnIDSNSRLCMSSAVVGYKRSlgaDAPPCSYEDL-DCAD 170
Cdd:cd02761 65 EILKEAKR---P---LFYGLGTTVCEAQRAGIELAEKLGAI--IDHAASVCHGPNLLALQDS---GWPTTTLGEVkNRAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 171 CVLIAGSNMAFAHP------VLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLHLALLPGTDVALFHGILHILLWEDwi 244
Cdd:cd02761 134 VIVYWGTNPMHAHPrhmsrySVFPRGFFREGGREDRTLIVVDPRKSDTAKLADIHLQIDPGSDYELLAALRALLRGAG-- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 245 drsfiaehtegfadlkeLVRDytpaavaDICGIDRADLQRCAEWIGRSpRFLSL-WCMGLnQSSAGSAKN-SALINLHLA 322
Cdd:cd02761 212 -----------------LVPD-------EVAGIPAETILELAERLKNA-KFGVIfWGLGL-LPSRGAHRNiEAAIRLVKA 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 323 TGKIGRAGCGPfsLTGQPNAMGGRETGSLANLLPGHREAADPGHRAEVAHYwgveqlptspglSAIELfdaVHDGRIKAL 402
Cdd:cd02761 266 LNEYTKFALLP--LRGHYNVRGFNQVLTWLTGYPFRVDFSRGYPRYNPGEF------------TAVDL---LAEGEADAL 328
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596976 403 WIACTNPAQSLPdqRKIHEALARCPFVVVqeAFAGTETCQYADLLLPAASWG-EKEGSVTNSERRISHVRRAVPPPG 478
Cdd:cd02761 329 LIIASDPPAHFP--QSAVKHLAEIPVIVI--DPPPTPTTRVADVVIPVAIPGiEAGGTAYRMDGVVVLPLKAVETER 401
|
|
| nitri_red_nirB |
TIGR02374 |
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ... |
783-900 |
1.53e-08 |
|
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]
Pssm-ID: 162827 [Multi-domain] Cd Length: 785 Bit Score: 58.69 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 783 YDDPRRAIGKRVRLEDGRIVAVRLAGETLARDWLKELWLTGRADSELRRwLLAPLGAAPGRPSQGAGG----KTLCSCQN 858
Cdd:TIGR02374 339 IYDEQKGIYKKLVLSDDKLLGAVLFGDTSDYGRLLDMVLKQADISEDPA-IIKPQISGPEAGGPGVEAmpdsEQICSCNT 417
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 15596976 859 VSQQTVLGGIARGL--DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:TIGR02374 418 VTKGAIIDAIHTGSctTVEELKACTKAGTSCGGCKPLVEQLLRA 461
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
589-685 |
5.48e-08 |
|
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239187 [Multi-domain] Cd Length: 116 Bit Score: 51.90 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 589 YPLTLNTGRLRdqwHGMSRT-GTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFL 667
Cdd:cd02786 1 YPLRLITPPAH---NFLNSTfANLPELRAKEGEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVA 77
|
90
....*....|....*....
gi 15596976 668 P-MHWGDRFLKGLGCNVLT 685
Cdd:cd02786 78 EgGWWREHSPDGRGVNALT 96
|
|
| NasA-like_Fer2_BFD-like |
cd19948 |
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of ... |
850-899 |
7.31e-07 |
|
bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit NasA and similar proteins; The BFD-like [2Fe-2S]-binding domain described in this family is found at the C-terminus of prokaryotic assimilatory nitrate reductase catalytic subunit (NasA) such as Rhodobacter capsulatus E1F1 NasA. Nitrate reductase catalyzes the reduction of nitrate to nitrite, the first step of nitrate assimilation. R. capsulatus E1F1 nitrate reductase is composed of this NasA subunit and a small diaphorase subunit with FAD. Note that this [2Fe-2S]-binding domain is not always present; for example, it is absent from the characterized haloaechean Haloferax mediterranei NasA; both, however, have an [4Fe-4S] binding domain at their N-terminus. The BFD-like [2Fe-2S]-binding domain is found in a variety of other proteins including bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381081 [Multi-domain] Cd Length: 53 Bit Score: 46.75 E-value: 7.31e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15596976 850 GKTLCSCQNVSQQTVLGGIA-RGL-DLDGLKREFGCGTGCGSCVPEIKRLLA 899
Cdd:cd19948 1 GRTVCACFSVGENTIRRAIAdNGLtSVAQVGTCLKAGTNCGSCVPEIQKLLS 52
|
|
| NirB_Fer2_BFD-like_1 |
cd19943 |
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large ... |
852-898 |
7.76e-06 |
|
first bacterioferritin-associated ferredoxin (BFD)-like [2Fe-2S]-binding domain of the large subunit of the NADH-dependent nitrite reductase; The NADH-dependent nitrite reductase (NirBD) complex comprises a large and a small subunit, and is also known as nitrite reductase (reduced nicotinamide adenine dinucleotide), NADH-nitrite oxidoreductase, and assimilatory nitrite reductase. NirBD uses NADH as electron donor, and FAD, iron-sulfur cluster, and siroheme cofactors, all embedded in the large subunit NirB to catalyze the 6-electron reduction of nitrite to ammonium. NirBD plays a role in regulating nitric oxide homeostasis in Streptomyces coelicolor. In addition to NirB, the BFD-like [2Fe-2S]-binding domain is found in a variety of proteins including bacterioferritin-associated ferredoxin (BFD) and Cu+ chaperone CopZ. It comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. For the class of proteins having a BFD-like [2Fe-2S]-binding domain, the Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport.
Pssm-ID: 381076 [Multi-domain] Cd Length: 53 Bit Score: 43.76 E-value: 7.76e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15596976 852 TLCSCQNVSQQTVLGGI-ARGL-DLDGLKREFGCGTGCGSCVPEIKRLL 898
Cdd:cd19943 5 EVCGCNGVSKGAIVQAIqEKGLtTLDEVKACTKASTSCGGCTPLVEQLL 53
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
407-494 |
2.01e-05 |
|
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), and other related proteins. The phenylacetyl-CoA:acceptor oxidoreductase has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. Members of this CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239161 [Multi-domain] Cd Length: 760 Bit Score: 48.43 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 407 TNPAQSLPDQRKIHEALARCPFvVVQEAFAGTETCQYADLLLPAASWGEKEGSVTN-----SERRISH----VRR-AVPP 476
Cdd:cd02760 522 TNPAISFWDTATLVDNIAKFPF-TVSFAYTEDETNWMADVLLPEATDLESLQMIKVggtkfVEQFWEHrgvvLRQpAVEP 600
|
90
....*....|....*...
gi 15596976 477 PGEARQDWNIVCDFARRL 494
Cdd:cd02760 601 QGEARDFTWISTELAKRT 618
|
|
| Fer2_BFD-like |
cd19942 |
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; ... |
851-897 |
4.05e-05 |
|
[2Fe-2S]-binding domain of bacterioferritin-associated ferredoxin (BFD) and related proteins; The BFD-like [2Fe-2S]-binding domain comprises a helix-turn-helix fold, and binds an [2Fe-2S] cluster via 4 highly-conserved Cys residues, found in loops between the alpha-helices. The Cys residues are organized in a unique C-X2-C-X31-35-C-X2-9-C-arrangement. [2Fe-2S] clusters are sulfide-linked diiron centers, a primary role for which is electron transport. BFD-like [2Fe-2S]-binding domains are found in proteins such as bacterioferritin-associated ferredoxin (BFD), the large subunit of NADH-dependent nitrite reductase, Cu+ chaperone CopZ, anaerobic glycerol 3-phosphate dehydrogenase subunit A, hydrogen cyanide synthase subunit B, nitrogen fixation protein NifU, prokaryotic assimilatory nitrate reductase catalytic subunit NasA, and archaeal proline dehydrogenase PDH1. This superfamily also includes uncharacterized proteins having an N-terminal BFD-like [2Fe-2S]-binding domain and a C-terminal domain belonging to the Ni,Fe-hydrogenase I small subunit family.
Pssm-ID: 381075 [Multi-domain] Cd Length: 49 Bit Score: 41.65 E-value: 4.05e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 15596976 851 KTLCSCQNVSQQTVLGGIARGLD--LDGLKREFGCGTGCGSCVPEIKRL 897
Cdd:cd19942 1 ALVCECFAVTEKELREAIRKGGLktVEELLTGTGAGGGCGVCHPHVAQL 49
|
|
| PRK14989 |
PRK14989 |
nitrite reductase subunit NirD; Provisional |
833-900 |
5.79e-05 |
|
nitrite reductase subunit NirD; Provisional
Pssm-ID: 184951 [Multi-domain] Cd Length: 847 Bit Score: 47.04 E-value: 5.79e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15596976 833 LLAPLGAAPGRPSQGAGG----KTLCSCQNVSQQTVLGGIARGL-DLDGLKREFGCGTGCGSCVPEIKRLLAA 900
Cdd:PRK14989 400 LILPAHAGSGKPSIGVDKlpdsAQICSCFDVTKGDLIAAINKGChTVAALKAETKAGTGCGGCIPLVTQVLNA 472
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
7-226 |
6.12e-05 |
|
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production and conversion]; NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440657 [Multi-domain] Cd Length: 453 Bit Score: 46.37 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 7 LRTTASTCCYCGVGCGVLIEHDGERILGVQGDPRHPANFGRLCSKG--ASLHLTGDlqARALYPQLRLGKQLARArsDWE 84
Cdd:COG1034 215 LKKTPSICPHCSVGCNIRVDVRGGKVYRVLPRENEAVNEEWLCDKGrfGYDGLNSP--DRLTRPLVRKDGELVEA--SWE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 85 SALEHAAGrfaetirehgpdsvafyisgqlltedyyAFNKLARAlvgtnnidSNSrlcMSSAVVGYKRSLGADAPPCSYE 164
Cdd:COG1034 291 EALAAAAE----------------------------GLKALKKA--------ENS---VGAALLGALPDAAAILEAAEAG 331
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596976 165 DLdcaDCVLIAGsnmafAHPVLFRRLEAAKAARPEMRIVVIDPRRTDTCELADLhlaLLPGT 226
Cdd:COG1034 332 KL---KALVLLG-----ADPYDLDPAAALAALAKADFVVVLDHFGSATAERADV---VLPAA 382
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
623-687 |
3.62e-04 |
|
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO. Also included in this group is the pyrogallol-phloroglucinol transhydroxylase from Pelobacter acidigallici. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239178 [Multi-domain] Cd Length: 127 Bit Score: 41.42 E-value: 3.62e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15596976 623 VHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPmH--WGD-RFLKGL---GC-NVLTLP 687
Cdd:cd02777 36 VWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVALP-EgaWYDpDDNGGLdkgGNpNVLTSD 106
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
588-671 |
8.45e-04 |
|
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. The acetylene hydratase of Pelobacter acetylenicus is a tungsten iron-sulfur protein involved in the fermentation of acetylene to ethanol and acetate. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239182 [Multi-domain] Cd Length: 130 Bit Score: 40.37 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596976 588 RYPLTLNTGRlRDQWHGMSRTGTCARLFGHEEEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFL 667
Cdd:cd02781 1 EYPLILTTGA-RSYYYFHSEHRQLPSLRELHPDPVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRA 79
|
....
gi 15596976 668 PMHW 671
Cdd:cd02781 80 EHGW 83
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
620-694 |
1.13e-03 |
|
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal molybdopterin-binding oxidoreductase-like domains with a putative N-terminal iron-sulfur [4Fe-4S] cluster binding site and molybdopterin cofactor binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239186 [Multi-domain] Cd Length: 124 Bit Score: 39.66 E-value: 1.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15596976 620 EALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPMHWGDRFLKGLGCNVLTLPAFDPLSK 694
Cdd:cd02785 31 EPRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAEQGWWSRYFQEGSLQDLTSPFVNPVHE 105
|
|
| MopB_CT_FmdC-FwdD |
cd02789 |
The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran ... |
593-669 |
1.34e-03 |
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The MopB_FmdC-FwdD CD includes the C-terminus of subunit C of molybdenum formylmethanofuran dehydrogenase (FmdC) and subunit D of tungsten formylmethanofuran dehydrogenase (FwdD), and other related proteins. Formylmethanofuran dehydrogenase catalyzes the first step in methane formation from CO2 in methanogenic archaea and some eubacteria. Members of this CD belong to the molybdopterin_binding superfamily of proteins. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239190 [Multi-domain] Cd Length: 106 Bit Score: 39.33 E-value: 1.34e-03
10 20 30 40 50 60 70
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gi 15596976 593 LNTGRLRDQwhgmSRTGTCARLFGHE--EEALVHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPGQAFLPM 669
Cdd:cd02789 5 LNSGRTIDQ----GRIIEGGNKLTYEvdACAYCEINPEDYKLLGKPEGDKVKVTSEFGEVVVFAKENEGVPEGMVFIPM 79
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| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
623-663 |
2.58e-03 |
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The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239194 [Multi-domain] Cd Length: 129 Bit Score: 38.77 E-value: 2.58e-03
10 20 30 40
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gi 15596976 623 VHLHPEELRRRQLLDGQLVRLKSRRGALVLPVSADDSVRPG 663
Cdd:cd02793 35 IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPG 75
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