|
Name |
Accession |
Description |
Interval |
E-value |
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
53-710 |
0e+00 |
|
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: 642.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 53 KYVRTTCSPNCTLACGIRAMVVDGQIKALLPSNDYPE-----PEYGPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGE 127
Cdd:cd02750 2 KVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPEtppdlPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVGARGEGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 128 FREVSWEEALDYTAKRLKEIAAKYGPESIGFIFQVGGTGHVQKGAWIALATMAGWSLIHPYDQNGDLPMFWPQTFGVQTE 207
Cdd:cd02750 82 WKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAAGSRFASLIGGVSLSFYDWYGDLPPGSPQTWGEQTD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 208 ELEPLEWLNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEE 287
Cdd:cd02750 162 VPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 288 KLYDEAFIKTYSDMPLLVrldngrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeievelkd 367
Cdd:cd02750 242 KLYDEDYLKEYTDLPFLV-------------------------------------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 368 grlvrvkpvfqllkehlasYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNI 447
Cdd:cd02750 260 -------------------YTPAWQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 448 GKPGAGISTYAGQykirfnvkewwfpgsprwlpwlyilhgptpgmkarwpkngVKALIFGWGNPFDQHNMADRLRQMAIK 527
Cdd:cd02750 321 GKNGGGWAHYVGQ----------------------------------------PRVLFVWRGNLFGSSGKGHEYFEDAPE 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 528 GELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIRPLYEARSELWMAKELAKRldpgfakhff 607
Cdd:cd02750 361 GKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKK---------- 430
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 608 peldentaaekavelllatggppvagitleqlkkgpvrlksevpgnrqIPFyeqvqfkkpfppvsrpaaieataqFVKSG 687
Cdd:cd02750 431 ------------------------------------------------VPW------------------------RTLTG 438
|
650 660
....*....|....*....|...
gi 1731597526 688 RIEFYKDEDAFIALGETLPVHKP 710
Cdd:cd02750 439 RQQFYLDHDWFLELGETLPTYKP 461
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
33-857 |
1.52e-169 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 507.07 E-value: 1.52e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 33 ATRYFIPKAGAENTSPLKEVKYVRTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPEPEyGpRGCLRGLSFINLIYGPDR 112
Cdd:COG0243 2 SLRDFKAAGAGAAALEAAGTKTVKTTC-PGCGVGCGLGVKVEDGRVVRVRGDPDHPVNR-G-RLCAKGAALDERLYSPDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 113 IKKPLIRTGERGAGEFREVSWEEALDYTAKRLKEIAAKYGPESIGFIFQVGGTGHVQ-KGAWIA--LATMAGWSLihpYD 189
Cdd:COG0243 79 LTYPMKRVGPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSnEAAYLAqrFARALGTNN---LD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 190 QNGDL-----PMFWPQTFGVQTEELEPLEWLNSRYTAIFGSNIMVTRLIDADFLIKA-RNNGTKVVVFDPNYSPTAAKAD 263
Cdd:COG0243 156 DNSRLchesaVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 264 EWVQLKPSSDAALALGMARVIIEEKLYDEAFIKTYSDMpllvrldngrrlkadevkglarpdglppyreafvayngklla 343
Cdd:COG0243 236 EWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVG------------------------------------------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 344 vhpeklelppdvilegeievelkdgrlvrvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGAS 423
Cdd:COG0243 274 ---------------------------------FDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 424 NYQWYHGDLKGRALALLPVLTGNIGKPGAGIstyagqykirfnvkewwFPGSPRWLpwlyilhgpTPGMKARwpkngVKA 503
Cdd:COG0243 321 LQQHSNGTQTVRAIANLALLTGNIGKPGGGP-----------------FSLTGEAI---------LDGKPYP-----IKA 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 504 LIFGWGNPFDQHNMADRLRQmAIKGeLEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIRPLYE 583
Cdd:COG0243 370 LWVYGGNPAVSAPDTNRVRE-ALRK-LDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVEPPGE 447
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 584 ARSELWMAKELAKRLdpGFAKHFfpelDENTAAEKAVELLLATGGPpvAGITLEQLK-KGPVRLksevPGNRQIPFYEQV 662
Cdd:COG0243 448 ARSDWEIFAELAKRL--GFEEAF----PWGRTEEDYLRELLEATRG--RGITFEELReKGPVQL----PVPPEPAFRNDG 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 663 QFKKPfppvsrpaaieataqfvkSGRIEFYKDEDAFialgETLPVHKPPFEDSEyalnpEIKGKYQFAYITRNSLYRVHS 742
Cdd:COG0243 516 PFPTP------------------SGKAEFYSETLAL----PPLPRYAPPYEGAE-----PLDAEYPLRLITGRSRDQWHS 568
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 743 THSNNLWMNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWWSRYLNGD--SYNS 820
Cdd:COG0243 569 TTYNNPRLREIGPR-PVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWYEPADDKggNVNV 647
|
810 820 830
....*....|....*....|....*....|....*..
gi 1731597526 821 LTYPFIKPThevyfvpgiwAPNTAWNEALCDVRKAGE 857
Cdd:COG0243 648 LTPDATDPL----------SGTPAFKSVPVRVEKAAA 674
|
|
| MopB_4 |
cd02765 |
The MopB_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
57-711 |
4.65e-120 |
|
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: 375.28 E-value: 4.65e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 57 TTCSPNCTLACGIRAMVVDGQIKALLPsNDYPEPEYgPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEA 136
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEP-NEWPDKTY-KRGCTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITWDEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 137 LDYTAKRLKEIAAKYGPESIGFIFqvgGTGHVQKGAWIALATMAGW---SLIHPYDQNGDLPMFWPQTFGVQTEELEPLE 213
Cdd:cd02765 80 LDTIADKLTEAKREYGGKSILWMS---SSGDGAILSYLRLALLGGGlqdALTYGIDTGVGQGFNRVTGGGFMPPTNEITD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 214 WLNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYDEA 293
Cdd:cd02765 157 WVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 294 FIKTYSDMPLLVRLDNGRRLKADEVkglarpdGLPPYREAFVAYNGKLLAVHP-EKLELPPDviLEGEIEVelkDGrlVR 372
Cdd:cd02765 237 FLKSNTSAPFLVREDNGTLLRQADV-------TATPAEDGYVVWDTNSDSPEPvAATNINPA--LEGEYTI---NG--VK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 373 VKPVFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPlHVIYGASNYQ-WYHGDLKGRALALLPVLTGNIGKPG 451
Cdd:cd02765 303 VHTVLTALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKP-SGIWGFGGVDrYYHSHVFGRTAAILAALTGNIGRVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 452 AGIStyagqykirfNVKEWWFPGSprwlpwlyilhgptpgmkarwpkngvkalifgwgnpfDQHNM-ADRLRQMAIKGEL 530
Cdd:cd02765 382 GGVG----------QIKFMYFMGS-------------------------------------NFLGNqPDRDRWLKVMKNL 414
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 531 EFIAGLDFSLTTSCRYSDVVFPAATWYE-KTELVTTPLHPYMQLQQPAIRPLYEARSELWMAKELAKRLdpGFAkHFFPE 609
Cdd:cd02765 415 DFIVVVDIFHTPTVRYADIVLPAAHWFEvEDLLVRYTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERL--GLG-DYFPK 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 610 LDENTaaekaVELLLATGGPPVAGITLEQLKKGPVRLKSEVPGNRQIPFYEQVqFKKPfppvsrpaaieataqfvkSGRI 689
Cdd:cd02765 492 TPEDY-----VRAFMNSDDPALDGITWEALKEEGIIMRLATPEDPYVAYLDQK-FGTP------------------SGKL 547
|
650 660
....*....|....*....|..
gi 1731597526 690 EFYkdEDAFIALGETLPVHKPP 711
Cdd:cd02765 548 EFY--NEAAPELEEALPLPEEP 567
|
|
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
12-830 |
6.85e-103 |
|
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family include known and probable dimethyl sulfoxide reductase (DMSO reductase) A chains. In E. coli, dmsA encodes the canonical anaerobic DMSO reductase A chain. The paralog ynfE, as part of ynfFGH expressed from a multicopy plasmid, could complement a dmsABC deletion, suggesting a similar function and some overlap in specificity, although YnfE could not substitute for DmsA in a mixed complex.
Pssm-ID: 274006 [Multi-domain] Cd Length: 797 Bit Score: 336.74 E-value: 6.85e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 12 LSRRQFLKASAATAVLAGTAGA-TRYFIPKAGAENTSPLKEVKYVRTTCSPNCTLACGIRAMVVDGQIKALLPSNDYpEP 90
Cdd:TIGR02166 1 ISRRHFLKTSAALGGLAAASGAlSLPFSVNAAAEATPTGPDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTG-DD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 91 EYGP---RGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEALDYTAKRLKEIAAKYGPESIGFIFQVGGTGH 167
Cdd:TIGR02166 80 EYGNhqvRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTTGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 168 VQKGAWIALATMAGWSLIHPY-DQNGDLPM-----FWPQTFGVQTEELEPLEWLNSRYTAIFGSNIMVTRL----IDADF 237
Cdd:TIGR02166 160 TMSRSWPPTAVARLLNLCGGYlNQYGSYSTaqineAMPYTYGISADGSSLDDIENSKLVVMFGNNPAETRMsgggQTYYF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 238 LIKARNNGTKVVVFDPNYSPTAA-KADEWVQLKPSSDAALALGMARVIIEEKLYDEAFIKTYSdmpllVRLDNgrrlkad 316
Cdd:TIGR02166 240 LQALEKSNARVIVIDPRYTDTVAgREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYC-----VGFDE------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 317 evKGLarPDGLPPyREAFVAYngkllavhpeklelppdVILEGEIEVElkdgrlvrvkpvfqllkehlasYTPAYVEQET 396
Cdd:TIGR02166 308 --KTL--PASAPK-NGSYKDY-----------------ILGEGADGTP----------------------KTPEWASKIT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 397 GVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNIGKPGAGISTYAGQYKIRFNVkewwFPGSP 476
Cdd:TIGR02166 344 GIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKGGNNGAREGNYSLPFAR----MPELP 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 477 R-------WLPWL-YILHGPTpgMKARwpKNGVKA-------LIFGW---GNPF-DQH---NMADRLRQMAIKgeLEFIA 534
Cdd:TIGR02166 420 NpvktsisCFLWTdAIDRGTE--MTAI--KDGVRGkdkldsnIKFLWnyaGNCLiNQHsdiNRTHKILQDESK--CEMIV 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 535 GLDFSLTTSCRYSDVVFPAATWYEKTELV---TTPLHPYMQLQQPAIRPLYEARSELWMAKELAKRLDpgfakhFFPELD 611
Cdd:TIGR02166 494 VIDNHMTSSAKYADILLPDTTTLEQNDFIedsYASNMSYLIFMQKAIEPLFECKPIYDMLSEVAKRLG------VEAEFT 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 612 ENTAAEKAVELLLAtggppvagitlEQLKKGPvrlksevpgnrQIPFYEQVQ----FKKPFPPVSRPA------AIEATA 681
Cdd:TIGR02166 568 EGRTQEEWLEHLYA-----------QTRAADP-----------ALPSFAELRkqgiYKAKSAPGPFVAfedfrrDPEANP 625
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 682 QFVKSGRIEFYKDEDAFIA----LGE-----TLPVHKPPFEDSEYALNPEikgkYQFAYITRNSLYRVHSTHSNNLWMNE 752
Cdd:TIGR02166 626 LKTPSGKIEIYSERLAQIAhtweLPEgdvitPLPEYVPTFEGPDDPLRKD----FPLQLTGFHYKGRTHSTYGNVDWLRE 701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 753 LQDNkpKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQG-WWSRYLN----GDSYNSLTY---- 823
Cdd:TIGR02166 702 AAPQ--ELWINPIDAQKRGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGaWYQPDKNgidvGGCINTLTTqrps 779
|
....*....
gi 1731597526 824 PFIK--PTH 830
Cdd:TIGR02166 780 PLAKgnPQH 788
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
56-706 |
1.90e-98 |
|
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: 316.11 E-value: 1.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 56 RTTCSPNCTLACGIRAMVVDGQIKALLPSNDYPepeYgPRG--CLRGLSFINLIYGPDRIKKPLIRTGeRGAGEFREVSW 133
Cdd:cd02766 1 RSVCPLDCPDTCSLLVTVEDGRIVRVEGDPAHP---Y-TRGfiCAKGARYVERVYSPDRLLTPLKRVG-RKGGQWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 134 EEALDYTAKRLKEIAAKYGPESIGFIFQVGGTGHVQKGAWIALATMAGWSLIH--PYDQNGDLPmfWPQTFGvQTEELEP 211
Cdd:cd02766 76 DEALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHALGASELRgtICSGAGIEA--QKYDFG-ASLGNDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 212 LEWLNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYD 291
Cdd:cd02766 153 EDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 292 EAFIKTYSDMpllvrldngrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeievelkdgrlv 371
Cdd:cd02766 233 RDFLARHTEG---------------------------------------------------------------------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 372 rvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKP--LHVIYGASNYqwYHGDLKGRALALLPVLTGNIGK 449
Cdd:cd02766 243 -----FEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPpsIRLGYGMQRY--RNGGQNVRAIDALPALTGNIGV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 450 PGAGIstyagqykirfnvkewwfpgsprwlpwLYILHGPTpgmkarwpkngVKALIFGWGNPFDQHNMADRLRQMAIKgE 529
Cdd:cd02766 316 PGGGA---------------------------FYSNSGPP-----------VKALWVYNSNPVAQAPDSNKVRKGLAR-E 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 530 LEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIRPLYEARSELWMAKELAKRLdpGFAKHFFpE 609
Cdd:cd02766 357 DLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYNEPAIPPPGEARSNTEIFRELAKRL--GFGEPPF-E 433
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 610 LDENTAAEKAvellLATGGPPVAGITLEQLKKGPVRLKSEVPgnrqipfYEQVQFKKPfppvsrpaaieataqfvkSGRI 689
Cdd:cd02766 434 ESDEEWLDQA----LDGTGLPLEGIDLERLLGPRKAGFPLVA-------WEDRGFPTP------------------SGKF 484
|
650
....*....|....*..
gi 1731597526 690 EFYKdEDAFIALGETLP 706
Cdd:cd02766 485 EFYS-ERAAKRGLPPLP 500
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
63-600 |
6.42e-93 |
|
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: 299.98 E-value: 6.42e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 63 CTLACGIRAMVVDGQIKALLPsndYPE-PEYGPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEALDYTA 141
Cdd:cd02755 8 CSSRCGILARVEDGRVVKIDG---NPLsPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGKFREASWDEALQYIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 142 KRLKEIAAKYGPESIGFifqvGGTGHVQKGAWIALATMAGWSLIHPYDQNGDLP--MFWPQTFGVQTEELEPlEWLNSRY 219
Cdd:cd02755 85 SKLKEIKEQHGPESVLF----GGHGGCYSPFFKHFAAAFGSPNIFSHESTCLASknLAWKLVIDSFGGEVNP-DFENARY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 220 TAIFGSN----IMVTRLIDadfLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYDEAFI 295
Cdd:cd02755 160 IILFGRNlaeaIIVVDARR---LMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAAFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 296 KTYSdmpllvrldNGrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeievelkdgrlvrvkp 375
Cdd:cd02755 237 EKYT---------NG----------------------------------------------------------------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 376 vFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLK-GRALALLPVLTGNIGKPGAgi 454
Cdd:cd02755 243 -FELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRGTFYSNSFQtRRAIAIINALLGNIDKRGG-- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 455 styagqykirfnvkeWWFPGSPRwlpwlyilhgPTPgmkarwpkngVKALIFGWGNPFdqHNMADRLR-QMAIKgELEFI 533
Cdd:cd02755 320 ---------------LYYAGSAK----------PYP----------IKALFIYRTNPF--HSMPDRARlIKALK-NLDLV 361
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731597526 534 AGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQ--LQQPAIRPLYEARSELWMAKELAKRLDP 600
Cdd:cd02755 362 VAIDILPSDTALYADVILPEATYLERDEPFSDKGGPAPAvaTRQRAIEPLYDTRPGWDILKELARRLGL 430
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
52-804 |
6.60e-90 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 299.11 E-value: 6.60e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 52 VKYVRTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPePEYGpRGCLRGLSFINLIYGPDRIKKPLIRTGergaGEFREV 131
Cdd:COG3383 4 MKKVKTVC-PYCGVGCGIDLEVKDGKIVKVEGDPDHP-VNRG-RLCVKGRFGFEFVNSPDRLTTPLIRRG----GEFREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 132 SWEEALDYTAKRLKEIAAKYGPESIGFIfqvgGTGH--------VQKGAWIALATmagwsliHPYDQNGDLPMFwP---- 199
Cdd:COG3383 77 SWDEALDLVAERLREIQAEHGPDAVAFY----GSGQltneenylLQKLARGVLGT-------NNIDNNARLCMA-Savag 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 200 --QTFGVQT-----EELEplewlNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSS 272
Cdd:COG3383 145 lkQSFGSDAppnsyDDIE-----EADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 273 DAALALGMARVIIEEKLYDEAFIKtysdmpllvrldngrrlkadevkglARPDGlppyreafvayngkllavhpeklelp 352
Cdd:COG3383 220 DLALLNGLLHVIIEEGLVDEDFIA-------------------------ERTEG-------------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 353 pdvilegeievelkdgrlvrvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDL 432
Cdd:COG3383 249 ------------------------FEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTD 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 433 KGRALALLPVLTGNIGKPGAGISTYAGQykirFNV-----------------------------KEWWFPGSPRWlPWLy 483
Cdd:COG3383 305 NVNAIINLALATGNIGRPGTGPFPLTGQ----NNVqggrdmgalpnvlpgyrdvtdpehrakvaDAWGVPPLPDK-PGL- 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 484 ilhgPTPGMKARWPKNGVKAL-IFGwGNPFDQHNMADRLRQmAIKgELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTEL 562
Cdd:COG3383 379 ----TAVEMFDAIADGEIKALwIIG-ENPAVSDPDANHVRE-ALE-KLEFLVVQDIFLTETAEYADVVLPAASWAEKDGT 451
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 563 VTTpLHPYMQLQQPAIRPLYEARSELWMAKELAKRLDPGFakhffpelDENTAAEKAVELLLATggPPVAGITLEQLKK- 641
Cdd:COG3383 452 FTN-TERRVQRVRKAVEPPGEARPDWEIIAELARRLGYGF--------DYDSPEEVFDEIARLT--PDYSGISYERLEAl 520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 642 GPVR---LKSEVPGNRqipfyeqVQFKKPFPPVSRPAAIEATAqfvksgriefykdedafialgetlpvHKPPFEdseya 718
Cdd:COG3383 521 GGVQwpcPSEDHPGTP-------RLFTGRFPTPDGKARFVPVE--------------------------YRPPAE----- 562
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 719 lnpEIKGKYQFAYITRNSLYRVHS----THSNNLwmNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALD 794
Cdd:COG3383 563 ---LPDEEYPLVLTTGRLLDQWHTgtrtRRSPRL--NKHAPE-PFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVT 636
|
810
....*....|
gi 1731597526 795 PGLgRKIVVF 804
Cdd:COG3383 637 DRV-RPGTVF 645
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
56-598 |
1.50e-89 |
|
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: 288.46 E-value: 1.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 56 RTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPEPEygPRGCLRGLSFINLIYGPDRIKKPLIRTGERGagEFREVSWEE 135
Cdd:cd00368 1 PSVC-PFCGVGCGILVYVKDGKVVRIEGDPNHPVNE--GRLCDKGRAGLDGLYSPDRLKYPLIRVGGRG--KFVPISWDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 136 ALDYTAKRLKEIAAKYGPESIGFIFQvGGTGHVQKGAWIALATMAGWSLIHPYDQNGDLPMFWPQT-FGVQTEELEPLEW 214
Cdd:cd00368 76 ALDEIAEKLKEIREKYGPDAIAFYGG-GGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKaFGGGAPTNTLADI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 215 LNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGmarviieeklydeaf 294
Cdd:cd00368 155 ENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA--------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 295 iktysdmpllvrldngrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeievelkdgrlvrvk 374
Cdd:cd00368 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 375 pvfqllkehlasytpAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNIGKPGAGI 454
Cdd:cd00368 220 ---------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGL 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 455 styagqykirfnvkewwFPGsprwlpwlyilhgptpgmkarwpkngvkalifgwGNPFDQHNMADRLRQMAikGELEFIA 534
Cdd:cd00368 285 -----------------GPG----------------------------------GNPLVSAPDANRVRAAL--KKLDFVV 311
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731597526 535 GLDFSLTTSCRYSDVVFPAATWYEKTELVTTpLHPYMQLQQPAIRPLYEARSELWMAKELAKRL 598
Cdd:cd00368 312 VIDIFMTETAAYADVVLPAATYLEKEGTYTN-TEGRVQLFRQAVEPPGEARSDWEILRELAKRL 374
|
|
| MopB_DmsA-EC |
cd02770 |
This CD (MopB_DmsA-EC) includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
57-692 |
6.69e-87 |
|
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: 289.22 E-value: 6.69e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 57 TTCSPNCTLACGIRAMVVDGQIKALLPSNDYPEPEYGP--RGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWE 134
Cdd:cd02770 2 SACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHqiRACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 135 EALDYTAKRLKEIAAKYGPESIGFIFQVGGTGHV--QKGAWI-ALATMAGWSLIHPYDQNGDLPMFWPQTFGVQTEELEP 211
Cdd:cd02770 82 EALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVpaGRGAIArLLNLTGGYLNYYGTYSWAQITTATPYTYGAAASGSSL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 212 LEWLNSRYTAIFGSNIMVTRLIDAD---FLIKARNNGTKVVVFDPNYSPTAA-KADEWVQLKPSSDAALALGMARVIIEE 287
Cdd:cd02770 162 DDLKDSKLVVLFGHNPAETRMGGGGstyYYLQAKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMITE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 288 KLYDEAFIKTYSdmpllVRLDngrrlkADEVkglarPDGLPPyREAFVAYngkllavhpeklelppdVILEGEIEVElkd 367
Cdd:cd02770 242 NLHDQAFLDRYC-----VGFD------AEHL-----PEGAPP-NESYKDY-----------------VLGTGYDGTP--- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 368 grlvrvkpvfqllkehlasYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNI 447
Cdd:cd02770 285 -------------------KTPEWASEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGNV 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 448 GKPGAGISTYAGQYKIRFNvkeWWFPGS-------PRWLPWLYILHGP--TPGMKARWPKNGVKA---LIFGWGNPF--- 512
Cdd:cd02770 346 GIPGGNTGARPGGSAYNGA---GLPAGKnpvktsiPCFMWTDAIERGEemTADDGGVKGADKLKSnikMIWNYAGNTlin 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 513 ---DQHNMADRLRQMAIKgeLEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTT---PLHPYMQLQQPAIRPLYEARS 586
Cdd:cd02770 423 qhsDDNNTTRALLDDESK--CEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTsnaGMMEYLIYSQKAIEPLYECKS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 587 ELWMAKELAKRLdpGFAKHFFPELDENTAAEKAVELLLATGGPPvagITLEQL-KKGPVRLKSEVPgnrQIPFYEQVQFK 665
Cdd:cd02770 501 DYEICAELAKRL--GVEDQFTEGKTEQEWLEELYGQTRAKEPGL---PTYEEFrEKGIYRVPRALP---FVAFEDFREDP 572
|
650 660
....*....|....*....|....*....
gi 1731597526 666 --KPFPpvsrpaaieaTAqfvkSGRIEFY 692
Cdd:cd02770 573 enNPLK----------TP----SGKIEIY 587
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
11-804 |
3.21e-80 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 274.62 E-value: 3.21e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 11 KLSRRQFLK-ASAATAVLAGTAgatryFIPKA-GAENTSPLK-EVKYVRTTCSpNCTLACGIRAMVVDGqiKALLPSNDY 87
Cdd:PRK15488 2 SLSRRDFLKgAGAGCAACALGS-----LLPGAlAANEIAQLKgKTKLTPSICE-MCSTRCPIEARVVNG--KNVFIQGNP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 88 PEPEYGPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEALDYTAKRLKEIAAKYGPESIGFIFQVGGTgh 167
Cdd:PRK15488 74 KAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKSGSL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 168 vqKGAWIALATMAGWSLI--HPYDQNGDLPMFWPQTFGvqtEELEpLEWLNSRYTAIFGSNI-------MVTRLIDAdfl 238
Cdd:PRK15488 152 --SSHLFHLATAFGSPNTftHASTCPAGYAIAAKVMFG---GKLK-RDLANSKYIINFGHNLyeginmsDTRGLMTA--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 239 ikARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYDEAFIKTYsdmpllvrldngrrlkadeV 318
Cdd:PRK15488 223 --QMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERY-------------------T 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 319 KGlarpdglppyreafvayngkllavhpeklelppdvilegeievelkdgrlvrvkpvFQLLKEHLASYTPAYVEQETGV 398
Cdd:PRK15488 282 SG--------------------------------------------------------FEELAASVKEYTPEWAEAISDV 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 399 PGDTVVRLAREMATTKPlHVIygasnYQWYHG--------DLKgRALALLPVLTGNI--------GKPGAGISTYAGQYK 462
Cdd:PRK15488 306 PADDIRRIARELAAAAP-HAI-----VDFGHRatftpeefDMR-RAIFAANVLLGNIerkgglyfGKNASVYNKLAGEKV 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 463 I----RFNVKEWWFPGSPRwlpwlyiLHGPTPGMKARWPKNGVKALIF------------GW----GNPFdqHNMADRLR 522
Cdd:PRK15488 379 AptlaKPGVKGMPKPTAKR-------IDLVGEQFKYIAAGGGVVQSIIdatltqkpyqikGWvmsrHNPM--QTVTDRAD 449
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 523 -QMAIKgELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVT--TPLHPYMQLQQPAIRPLYEARSELWMAKELAKRLD 599
Cdd:PRK15488 450 vVKALK-KLDLVVVCDVYLSESAAYADVVLPESTYLERDEEISdkSGKNPAYALRQRVVEPIGDTKPSWQIFKELGEKMG 528
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 600 PGfakHFFPELDENTaaekaVELLLATGGPPVagitLEQLKK-GPVRLKseVPGNRQIPFYEQvQFKKPFP---PVSRPA 675
Cdd:PRK15488 529 LG---QYYPWQDMET-----LQLYQVNGDHAL----LKELKKkGYVSFG--VPLLLREPKMVA-KFVARYPnakAVDEDG 593
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 676 AIEATAQF-VKSGRIEFYKDEDAFIALGETLPVHKP--PFEDSEYALnpeIKGKYQfayitrnslyrVHS---THsNNLW 749
Cdd:PRK15488 594 TYGSQLKFkTPSGKIELFSAKLEALAPGYGVPRYRDvaLKKEDELYF---IQGKVA-----------VHTngaTQ-NVPL 658
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1731597526 750 MNELQDNKPkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLgRKIVVF 804
Cdd:PRK15488 659 LANLMSDNA-VWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGI-RPDTLF 711
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
11-830 |
4.12e-77 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 267.28 E-value: 4.12e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 11 KLSRRQFLKASAATAVLAGTAGATRYFIPKAGAENT-SPLKEV-KYVRTTCSPNCTLACGIRAMVVDGQIKALLPSN--- 85
Cdd:PRK14990 13 EVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSaIPTKSDeKVIWSACTVNCGSRCPLRMHVVDGEIKYVETDNtgd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 86 DYPEPEYGPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEALDYTAKRLKEIAAKYGPESIGFIFQVGGT 165
Cdd:PRK14990 93 DNYDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 166 GHVQKGAW------IA-LATMAGWSLIHPYD-QNGDLPMFWPQTFGVQTEELEPLEWLNSRYTAIFGSNIMVTRLIDAD- 236
Cdd:PRK14990 173 GGTMTRSWppgntlVArLMNCCGGYLNHYGDySSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGGv 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 237 --FLIKAR-NNGTKVVVFDPNYSPT-AAKADEWVQLKPSSDAALALGMARVIIEEKLYDEAFIKTYSdmpllvrldngrr 312
Cdd:PRK14990 253 tyYLEQARqKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYC------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 313 lkadevkglarpdglppyreafVAYNGKLL-AVHPEKLELPPDVILEGeievelKDGrlvrvkpvfqllkehlASYTPAY 391
Cdd:PRK14990 320 ----------------------VGYDEKTLpASAPKNGHYKAYILGEG------PDG----------------VAKTPEW 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 392 VEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNIGKPGAGISTYAGQYKI---RFNVK 468
Cdd:PRK14990 356 ASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREGSYSLpfvRMPTL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 469 EWWFPGSPRWLPWL-YILHGPTpgMKARwpKNGVKA---------LIFGW-GNPF-DQHNMADRLRQ-MAIKGELEFIAG 535
Cdd:PRK14990 436 ENPIQTSISMFMWTdAIERGPE--MTAL--RDGVRGkdkldvpikMIWNYaGNCLiNQHSEINRTHEiLQDDKKCELIVV 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 536 LDFSLTTSCRYSDVVFPAATWYEKTEL---VTTPLHPYMQLQQPAIRPLYEARSELWMAKELAKRLdpGFAKHFfpelDE 612
Cdd:PRK14990 512 IDCHMTSSAKYADILLPDCTASEQMDFaldASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRL--GVEQQF----TE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 613 NTAAEKAVELLLATGGPPVAGI-TLEQLKKGPVrLKSEVPGNRQIPfYEQVQFKKPFPPVSRPaaieataqfvkSGRIEF 691
Cdd:PRK14990 586 GRTQEEWMRHLYAQSREAIPELpTFEEFRKQGI-FKKRDPQGHHVA-YKAFREDPQANPLTTP-----------SGKIEI 652
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 692 YKDEDAFIALG---------ETLPVHKPPFEDseyaLNPEIKGKYQFAYITRNSLYRVHSTHSNnlwMNELQDN-KPKVF 761
Cdd:PRK14990 653 YSQALADIAATwelpegdviDPLPIYTPGFES----YQDPLNKQYPLQLTGFHYKSRVHSTYGN---VDVLKAAcRQEMW 725
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 762 LNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWW-----SRYLNGDSYNSLTY----PFIK--PTH 830
Cdd:PRK14990 726 INPLDAQKRGINNGDKVRIFNDRGEVHIEAKVTPRMMPGVVALGEGAWydpdaKRVDKGGCINVLTTqrpsPLAKgnPSH 805
|
|
| NarG |
COG5013 |
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and ... |
53-787 |
9.46e-77 |
|
Nitrate reductase alpha subunit [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 444037 [Multi-domain] Cd Length: 1231 Bit Score: 272.08 E-value: 9.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 53 KYVRTTCSPNCTLACGIRAMVVDGQIKALLPSNDYPE-----PEYGPRGCLRGLSFINLIYGPDRIKKPLIR-------- 119
Cdd:COG5013 47 KVVRSTHGVNCTGSCSWKVYVKDGIITWETQQTDYPRtgpdlPNYEPRGCPRGASFSWYTYSPTRVKYPYVRgvllelwr 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 120 --------------------------TGERGAGEFREVSWEEALD-------YTAKrlkeiaaKYGPESI-GF------- 158
Cdd:COG5013 127 eararhgdpveawasivedpekrrryKSARGKGGFVRATWDEANEiiaaanvYTIK-------KYGPDRVaGFspipams 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 159 -IFQVGGTGHVQkgawialatMAGWSLIHPYDQNGDLPMFWPQTFGVQTEELEPLEWLNSRYTAIFGSNIMVTRLIDADF 237
Cdd:COG5013 200 mVSYAAGARFLS---------LIGGVMLSFYDWYADLPPASPQVWGEQTDVPESADWYNSGYLIMWGSNVPQTRTPDAHF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 238 LIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYD---EAFI---KTYSDMPLLVRLDN-- 309
Cdd:COG5013 271 MTEARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKEFHVDrqvPYFTdyaRRYTDLPFLVTLEErd 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 310 -----GRRLKADEVKGLARPDGLPPYR--------EAFVAYNGKL--------------------LAVHP---------- 346
Cdd:COG5013 351 ggyvpGRFLRASDLGGALGESNNPEWKtvvldeatGEPVVPNGSIgfrwgesegkwnlelkdatgADVDPalsllddhde 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 347 -EKLELP--------PDVILEG--EIEVELKDGRlVRVKPVFQLLKEHL-----------------ASYTPAYVEQETGV 398
Cdd:COG5013 431 vVEVAFPyfggetggGGVLRRGvpVRRVTLADGE-VLVTTVFDLMLANYgvdrglpgnwptgydddVPYTPAWQEKITGV 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 399 PGDTVVRLAREMATT------KPLhVIYGASNYQWYHGDLKGRALALLPVLTGNIGKPGAGISTYAGQYKIR-------- 464
Cdd:COG5013 510 PREQVIRVAREFAQNaektrgRSM-IIMGAGTNHWYHSDMIYRAILNLLMLCGCQGVNGGGWAHYVGQEKLRpqtgwqpl 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 465 --------------------FNVKEW-------------WFPGSPR---------------WLPwlyilHGPT------- 489
Cdd:COG5013 589 afaldwsrpprqmngtsffyAHTDQWryetlsadellspLADGKFWgghladynvraarlgWLP-----SYPQfnrnpld 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 490 -------------------------------PGMKARWPKNgvkalIFGW----------GNPF--------DQHNMADR 520
Cdd:COG5013 664 ladeaeaagmepadyvvdqlksgelkfacedPDNPENFPRN-----LFVWrsnllgssgkGHEYflkhllgtDNGVQGEE 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 521 L-----------RQMAIKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIRPLYEARSELW 589
Cdd:COG5013 739 LgpglrprevvwRDEAPEGKLDLLVTLDFRMTSTCLYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPPWEARSDWD 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 590 MAKELAKRLDPGFAKHFFPELD-------ENTAAEKA-----VELLLATGGPPVAGITLEQL-----------KK----G 642
Cdd:COG5013 819 IFKGIAKKFSELAAGHLGVRKDvvatplqHDTPGELAqpfgdVKDWKKGECEPIPGKTMPKLvvverdypaiyEKftslG 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 643 PvrLKSEVP-GNRQIPFY--EQVQF--------KKPFPPVSRPA------AIEA-------------------------- 679
Cdd:COG5013 899 P--LLEKLGnGGKGITWDteEEVEElgklngvvREEGVAKGRPRldtdidAAEAilalspetnghvavkawkalekrtgr 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 680 -------------------TAQFVK---------------------------------SGRIEFYKDEDAFIALGETLPV 707
Cdd:COG5013 977 dlahlaagreeekirfrdiQAQPRKvitsptwsgsesggrrysafttnveelipwrtlTGRQHFYLDHDWMREFGEGLPV 1056
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 708 HKPPFEDSEYALNPEIK--GKYQFA--YITRNSLYRVHSTHSNNLWMNELQDNKPKVFLNPQDAAAKGIKEGDLVEVYND 783
Cdd:COG5013 1057 YRPPLDMKTLFGEPGIGpnGNPEIVlrYLTPHQKWGIHSTYQDNLLMLTLSRGGPTVWMSEEDAAKIGIKDNDWIEAFNR 1136
|
....
gi 1731597526 784 RGRV 787
Cdd:COG5013 1137 NGVV 1140
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
61-692 |
2.31e-75 |
|
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: 257.54 E-value: 2.31e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 61 PNCTLACGIRAMVVDGQIKALLPsndypEPEYGPRGCLRGLSFINLIYGPDRIKKPLIRTGE----------RGAGEFRE 130
Cdd:cd02751 1 PTACHWGPFKAHVKDGVIVRVEP-----DDTDQPRPCPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsrelRGEGEFVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 131 VSWEEALDYTAKRLKEIAAKYGPESIgFI-----FQVGGTGHVQKGAWIALATMAGWSLIHPYDQNGDLPMFWPQTFGVQ 205
Cdd:cd02751 76 ISWDEALDLVASELKRIREKYGNEAI-FGgsygwASAGRLHHAQSLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 206 TEELEPLEWL----NSRYTAIFGSNIMVTRLIDA--------DFLIKARNNGTKVVVFDPNYSPTAA-KADEWVQLKPSS 272
Cdd:cd02751 155 EVYEQGTSWDdiaeHSDLVVLFGANPLKTRQGGGggpdhgsyYYLKQAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 273 DAALALGMARVIIEEKLYDEAFIKTYSDmpllvrldngrrlkadevkGLarpdglppyrEAFVAYngkllavhpeklelp 352
Cdd:cd02751 235 DVALMLAMAHTLITEDLHDQAFLARYTV-------------------GF----------DEFKDY--------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 353 pdviLEGEievelKDGrlvRVKpvfqllkehlasyTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQwYHGDL 432
Cdd:cd02751 271 ----LLGE-----SDG---VPK-------------TPEWAAEITGVPAETIRALAREIASKRTMIAQGWGLQRA-HHGEQ 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 433 KGRALALLPVLTGNIGKPGAGISTYAGQYKirfNVKEWWFPGSPRWLPWLY---------------ILHGPTP----GMK 493
Cdd:cd02751 325 PAWMLVTLAAMLGQIGLPGGGFGFGYGYSN---GGGPPRGGAGGPGLPQGKnpvkdsipvariadaLLNPGKEftanGKL 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 494 ARWPKngVKALIFGWGNPFdqHNMADRLRQMAIKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPL--HPYM 571
Cdd:cd02751 402 KTYPD--IKMIYWAGGNPL--HHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTGNysNRYL 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 572 QLQQPAIRPLYEARSELWMAKELAKRLdpGFAKHFFPELDE----NTAAEKAVElllATGGPPVAGITLEQL-KKGPVRL 646
Cdd:cd02751 478 IAMKQAVEPLGEARSDYEIFAELAKRL--GVEEEFTEGRDEmewlEHLYEETRA---KAAGPGPELPSFEEFwEKGIVRV 552
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1731597526 647 KSevPGNRQIPFYEQVQFKKPFpPVSRPaaieataqfvkSGRIEFY 692
Cdd:cd02751 553 PA--APKPFVAFADFREDPEAN-PLGTP-----------SGKIEIY 584
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
57-785 |
2.03e-72 |
|
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: 251.23 E-value: 2.03e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 57 TTCsPNCTLACGIRAMVVDGQIKALLPSNDYPePEYGpRGCLRGLSFINLIYGPDRIKKPLIRTGergaGEFREVSWEEA 136
Cdd:TIGR01591 1 TVC-PYCGVGCSLNLVVKDGKIVRVEPYQGHK-ANRG-HLCVKGYFAWEFINSKDRLTTPLIREG----DKFREVSWDEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 137 LDYTAKRLKEIAAKYGPESIGFIFQVGGTGH----VQKGAWIALATmagwsliHPYDQ-----NGDLPMFWPQTFGVQTE 207
Cdd:TIGR01591 74 ISYIAEKLKEIKEKYGPDSIGFIGSSRGTNEenylLQKLARAVIGT-------NNVDNcarvcHGPSVAGLKQTVGIGAM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 208 ELEPLEWLNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEE 287
Cdd:TIGR01591 147 SNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 288 KLYDEAFIKTysdmpllvRLDNgrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeievelkd 367
Cdd:TIGR01591 227 GLYDKAFIEK--------RTEG---------------------------------------------------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 368 grlvrvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNI 447
Cdd:TIGR01591 241 ---------FEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNI 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 448 GKPGAGISTYAGQ-------YKIRFNV------------------KEWWFPGSPRwLPWLYIlhgptPGMKARWPKNGVK 502
Cdd:TIGR01591 312 GKPGGGVNPLRGQnnvqgacDMGALPDflpgyqpvsdeevrekfaKAWGVVKLPA-EPGLRI-----PEMIDAAADGDVK 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 503 ALIFGWGNPFdqhnMADRLRQMAIKG--ELEFIAGLDFSLTTSCRYSDVVFPAATWYEKtELVTTPLHPYMQLQQPAIRP 580
Cdd:TIGR01591 386 ALYIMGEDPL----QSDPNTSKVRKAleKLELLVVQDIFMTETAKYADVVLPAAAWLEK-EGTFTNAERRIQRFFKAVEP 460
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 581 LYEARSELWMAKELAKRLDpgfakhffpeLDENTAAEKAVELLLATGGPPVAGITLEQLkkgpvrlksEVPGNRQIPfye 660
Cdd:TIGR01591 461 KGESKPDWEIIQELANALG----------LDWNYNHPQEIMDEIRELTPLFAGLTYERL---------DELGSLQWP--- 518
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 661 qvqfkkPFPPVSRPAAIEATAQFV-KSGRIEFYKDEdafialgETLPVHKPPfEDSEYALNpeiKGKYQFAYITRNSLYR 739
Cdd:TIGR01591 519 ------CNDSDASPTSYLYKDKFAtPDGKAKFIPLE-------WVAPIEEPD-DEYPLILT---TGRVLTHYNVGEMTRR 581
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1731597526 740 VHSthsnnlWMNELQDnkPKVFLNPQDAAAKGIKEGDLVEVYNDRG 785
Cdd:TIGR01591 582 VAG------LRRLSPE--PYVEINTEDAKKLGIKDGDLVKVKSRRG 619
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
57-631 |
7.00e-72 |
|
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: 244.52 E-value: 7.00e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 57 TTCSPNCTLACGIRAMVVDGQIKALLPSNDYPEPeyGPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEA 136
Cdd:cd02759 1 KGTCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTN--KGRLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKWERISWDEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 137 LDYTAKRLKEIAAKYGPESIGFIFQVG-GTGHVQKGAWIALA--------TMAGWSLIHPYDQNGDLPMFWPQTFGVqte 207
Cdd:cd02759 79 LDEIAEKLAEIKAEYGPESIATAVGTGrGTMWQDSLFWIRFVrlfgspnlFLSGESCYWPRDMAHALTTGFGLGYDE--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 208 elepLEWLNSRYTAIFGSNIMVTrliDADF----LIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARV 283
Cdd:cd02759 156 ----PDWENPECIVLWGKNPLNS---NLDLqghwLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 284 IIEEKLYDEAFIKTYSdmpllvrldNGrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeiev 363
Cdd:cd02759 229 IINEGLYDKDFVENWC---------YG----------------------------------------------------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 364 elkdgrlvrvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKP-LHVIYGASNYQwYHGDLKGRALALLPV 442
Cdd:cd02759 247 -------------FEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPaCIQWGLAIDQQ-KNGTQTSRAIAILRA 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 443 LTGNIGKPGAGIstyagqykirfnvkewWFPgsprwlpwlyilhgptpgmkarWPkngVKALIFGWGNPFDQHNMADRLR 522
Cdd:cd02759 313 ITGNLDVPGGNL----------------LIP----------------------YP---VKMLIVFGTNPLASYADTAPVL 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 523 QmAIKgELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLH-PYMQLQQPAIRPLYEARSELWMAKELAKRLDPG 601
Cdd:cd02759 352 E-ALK-ALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAeNFVQLRQKAVEPYGEAKSDYEIVLELGKRLGPE 429
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1731597526 602 FAKHF---FPELDE------NTAA---EKAVELLLATGGPPV 631
Cdd:cd02759 430 EAEYYkyeKGLLRPdgqpgfNTPTgkvELYSTMLEELGYDPL 471
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
56-641 |
1.15e-71 |
|
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: 244.82 E-value: 1.15e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 56 RTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPepeyGPRG--CLRGLSFINLIYGPDRIKKPLIRTGergaGEFREVSW 133
Cdd:cd02753 1 KTVC-PYCGVGCGLELWVKDNKIVGVEPVKGHP----VNRGklCVKGRFGFDFVNSKDRLTKPLIRKN----GKFVEASW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 134 EEALDYTAKRLKEIAAKYGPESIGFI------------FQ-----VGGTGHVQKGAWIALA-TMAGWSlihpydqngdlp 195
Cdd:cd02753 72 DEALSLVASRLKEIKDKYGPDAIAFFgsakctneenylFQklaraVGGTNNVDHCARLCHSpTVAGLA------------ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 196 mfwpQTFG--VQTEELEPLEwlNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSD 273
Cdd:cd02753 140 ----ETLGsgAMTNSIADIE--EADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLRPGTD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 274 AALALGMARVIIEEKLYDEAFIKtysdmpllvrldngrrlkadevkglARPDGlppyreafvayngkllavhpeklelpp 353
Cdd:cd02753 214 VALLNAMAHVIIEEGLYDEEFIE-------------------------ERTEG--------------------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 354 dvilegeievelkdgrlvrvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLK 433
Cdd:cd02753 242 -----------------------FEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSHGTDN 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 434 GRALALLPVLTGNIGKPGAGISTYAGQYkirfNVKewwfpGS------PRWLPwlyilhgptpgmkarwpkNGVKAL-IF 506
Cdd:cd02753 299 VMALSNLALLTGNIGRPGTGVNPLRGQN----NVQ-----GAcdmgalPNVLP------------------GYVKALyIM 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 507 GwGNPF----DQHNMADRLRQmaikgeLEFIAGLDFSLTTSCRYSDVVFPAATWYEKtELVTTPLHPYMQLQQPAIRPLY 582
Cdd:cd02753 352 G-ENPAlsdpNTNHVRKALES------LEFLVVQDIFLTETAELADVVLPAASFAEK-DGTFTNTERRVQRVRKAVEPPG 423
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731597526 583 EARSELWMAKELAKRL-DPGFAKHffPE--LDEntaaekavellLATGGPPVAGITLEQLKK 641
Cdd:cd02753 424 EARPDWEIIQELANRLgYPGFYSH--PEeiFDE-----------IARLTPQYAGISYERLER 472
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
56-645 |
1.19e-62 |
|
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: 221.33 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 56 RTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPepeyGPRG--CLRGLSFINLIYGPDRIKKPLIRTGErgaGEFREVSW 133
Cdd:cd02754 1 KTTC-PYCGVGCGVEIGVKDGKVVAVRGDPEHP----VNRGrlCIKGLNLHKTLNGPERLTRPLLRRNG---GELVPVSW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 134 EEALDYTAKRLKEIAAKYGPESIGFIfqvgGTGHVQKGAWIALATMA-GWSLIHPYDQNGDLPMF-----WPQTFG--VQ 205
Cdd:cd02754 73 DEALDLIAERFKAIQAEYGPDSVAFY----GSGQLLTEEYYAANKLAkGGLGTNNIDTNSRLCMAsavagYKRSFGadGP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 206 TEELEPLEwlNSRYTAIFGSN------IMVTRLIDAdfliKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALG 279
Cdd:cd02754 149 PGSYDDIE--HADCFFLIGSNmaechpILFRRLLDR----KKANPGAKIIVVDPRRTRTADIADLHLPIRPGTDLALLNG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 280 MARVIIEEKLYDEAFIKTYSdmpllvrldngrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilEG 359
Cdd:cd02754 223 LLHVLIEEGLIDRDFIDAHT----------------------------------------------------------EG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 360 EIEvelkdgrlvrvkpvfqlLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALAL 439
Cdd:cd02754 245 FEE-----------------LKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGTAANNAIIN 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 440 LPVLTGNIGKPGAGISTYAGQ------------------YKI------RFNVKEWWfpGSPrwlpwlYILHGPTPGMKA- 494
Cdd:cd02754 308 LHLATGKIGRPGSGPFSLTGQpnamggrevgglanllpgHRSvnnpehRAEVAKFW--GVP------EGTIPPKPGLHAv 379
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 495 ---RWPKNG-VKALIFGWGNPFdqHNMADRLRQMAIKGELEFIAGLD-FSLTTSCRYSDVVFPAATWYEKTELVT----T 565
Cdd:cd02754 380 emfEAIEDGeIKALWVMCTNPA--VSLPNANRVREALERLEFVVVQDaFADTETAEYADLVLPAASWGEKEGTMTnserR 457
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 566 plhpyMQLQQPAIRPLYEARSELWMAKELAKRLDpgfakhFFPELDENTAAEKAVELLLATGGPP--VAGITLEQLKKGP 643
Cdd:cd02754 458 -----VSLLRAAVEPPGEARPDWWILADVARRLG------FGELFPYTSPEEVFEEYRRLSRGRGadLSGLSYERLRDGG 526
|
..
gi 1731597526 644 VR 645
Cdd:cd02754 527 VQ 528
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
726-855 |
1.29e-62 |
|
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: 206.45 E-value: 1.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 726 KYQFAYITRNSLYRVHSTHSNNLWMNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFE 805
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQFSNVPWLLELQPE-PRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1731597526 806 QGWWSRYLNGDSYNSLTYPFIKPTHEvyfvpGIWAPNTAWNEALCDVRKA 855
Cdd:cd02785 80 QGWWSRYFQEGSLQDLTSPFVNPVHE-----YIYGPNSAFYDTLVEVRKA 124
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
55-617 |
6.40e-56 |
|
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: 201.51 E-value: 6.40e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 55 VRTTCSpNCTLACGIRAMVVDGQIKALLPSNDYPepeyGPRG--CLRGLSFINLIYGPDRIKKPLIRTGERGA----GEF 128
Cdd:cd02757 2 VPSTCQ-GCTAWCGLQAYVEDGRVTKVEGNPLHP----GSRGrlCAKGHLGLQQVYDPDRILYPMKRTNPRKGrdvdPKF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 129 REVSWEEALDYTAKRLK---------EIAAKYG-PESIGFIF------QVGGTGHVQKGAWIALATMAGwslihpydqng 192
Cdd:cd02757 77 VPISWDEALDTIADKIRalrkenephKIMLHRGrYGHNNSILygrftkMIGSPNNISHSSVCAESEKFG----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 193 dlPMFWPQTFGVQTEELEplewlNSRYTAIFGSNIMVT--RLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKP 270
Cdd:cd02757 146 --RYYTEGGWDYNSYDYA-----NAKYILFFGADPLESnrQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 271 SSDAALALGMARVIIEEKLYDEAFIKTYSDMPllVRLDNGRRLKADEVKglarpdglPPYREAFVAYngkllavhpekle 350
Cdd:cd02757 219 GEDGALALAIAHVILTEGLWDKDFVGDFVDGK--NYFKAGETVDEESFK--------EKSTEGLVKW------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 351 lppdvilegeievelkdgrlvrvkpvfqlLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKP---LHVIYGAS--NY 425
Cdd:cd02757 276 -----------------------------WNLELKDYTPEWAAKISGIPAETIERVAREFATAAPaaaAFTWRGATmqNR 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 426 QWYhgdlKGRALALLPVLTGNIGKPGaGISTYAGQYKI-----RFNVKEWWFPGSPRWLpwlyilhgptpgmkarwpkng 500
Cdd:cd02757 327 GSY----NSMACHALNGLVGSIDSKG-GLCPNMGVPKIkvyftYLDNPVFSNPDGMSWE--------------------- 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 501 vKALifgwgnpfdqhnmadrlrqmaikGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTP--LHPYMQLQQPAI 578
Cdd:cd02757 381 -EAL-----------------------AKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQEnnLHPWLSIRQPVV 436
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 1731597526 579 RPLYEARSELWMAKELAKRLDP----GFAKHFF-----PELDENTAAE 617
Cdd:cd02757 437 KSLGEVREETEILIELAKKLDPkgsdGMKRYAPgqfkdPETGKNNRWE 484
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
112-597 |
9.40e-44 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 162.57 E-value: 9.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 112 RIKKPLIRtgeRGAGEFREVSWEEALDYTAKRLKEIAAKYGPESIGFIFQVGGTGHVqkGAWIALATMA---GWSLIHPY 188
Cdd:pfam00384 1 RLKYPMVR---RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSGGLTDV--ESLYALKKLLnrlGSKNGNTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 189 DQNGDLPMFWPQTFG-------VQTEELEPLEwlNSRYTAIFGSNIMVTRLIDADFLIKA-RNNGTKVVVFDPNYSPTaa 260
Cdd:pfam00384 76 DHNGDLCTAAAAAFGsdlrsnyLFNSSIADIE--NADLILLIGTNPREEAPILNARIRKAaLKGKAKVIVIGPRLDLT-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 261 KADEWVQLKPSSDAALALGMARVIIEEKLYDEAFiktysdmpllvrldngrrlkadevkglarpdglppyreafvayngk 340
Cdd:pfam00384 152 YADEHLGIKPGTDLALALAGAHVFIKELKKDKDF---------------------------------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 341 llavhpeklelppdvilegeievelkdgrlvrvkpvfqllkehlasytpayveqetgvpgdtvvrlaremaTTKPLhVIY 420
Cdd:pfam00384 186 -----------------------------------------------------------------------APKPI-IIV 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 421 GASNYQWYHGDLKGRALALLPVLTGNIGKPGAG------ISTYA---GQYKIRFnvkewwFPGsprwlpwlyilhGPTPG 491
Cdd:pfam00384 194 GAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGwnglniLQGAAspvGALDLGL------VPG------------IKSVE 255
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 492 MKARWPKNGVKALIFGWGNPFDQHnmADRLRQMAIKGELEFIAGLDFSL-TTSCRYSDVVFPAATWYEKTELVTTPLHPy 570
Cdd:pfam00384 256 MINAIKKGGIKVLYLLGNNPFVTH--ADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGTYVNTEGR- 332
|
490 500
....*....|....*....|....*..
gi 1731597526 571 MQLQQPAIRPLYEARSELWMAKELAKR 597
Cdd:pfam00384 333 VQSTKQAVPPPGEAREDWKILRALSEV 359
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
69-606 |
4.15e-43 |
|
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: 166.28 E-value: 4.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 69 IRAMVVDGQIKALLP--SNDYPEPeygprgclRGLSFINLIYGPDRIKKPLIR-----------TGERGAGEFREVSWEE 135
Cdd:cd02769 9 FRARVKDGRIVGVRPfeEDPDPSP--------LLDGVPDAVYSPTRIKYPMVRrgwlekgpgsdRSLRGKEEFVRVSWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 136 ALDYTAKRLKEIAAKYGPESI-----GFiFQVGGTGHVQKGAWIALATMAGW-SLIHPYdQNGDLPMFWPQTFGvqteel 209
Cdd:cd02769 81 ALDLVAAELKRVRKTYGNEAIfggsyGW-SSAGRFHHAQSLLHRFLNLAGGYvGSVGDY-STGAAQVILPHVVG------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 210 ePLEWLNSRYTA------------IFGSNIMVTRLIDA---------DFLIKARNNGTKVVVFDPNYSPTAAKAD-EWVQ 267
Cdd:cd02769 153 -SMEVYTEQQTSwpviaehtelvvAFGADPLKNAQIAWggipdhqaySYLKALKDRGIRFISISPLRDDTAAELGaEWIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 268 LKPSSDAALALGMARVIIEEKLYDEAFIKTYSDmpllvrldngrrlkadevkGLARpdglppyreaFVAYngkllavhpe 347
Cdd:cd02769 232 IRPGTDVALMLALAHTLVTEGLHDKAFLARYTV-------------------GFDK----------FLPY---------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 348 klelppdviLEGEievelKDGrlvrvkpvfqllkehlASYTPAYVEQETGVPGDTVVRLAREMATTKPLhVIYGASNYQW 427
Cdd:cd02769 273 ---------LLGE-----SDG----------------VPKTPEWAAAICGIPAETIRELARRFASKRTM-IMAGWSLQRA 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 428 YHGDLKGRALALLPVLTGNIGKPGAGIST---YAGQYKIRFNvkewwfPGSPRWLPWLY---------------ILHGPT 489
Cdd:cd02769 322 HHGEQPHWMAVTLAAMLGQIGLPGGGFGFgyhYSNGGGPPRG------AAPPPALPQGRnpvssfipvariadmLLNPGK 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 490 P----GMKARWPKngVKALIFGWGNPFDQHNMADRLRQMAIKGELeFIAGlDFSLTTSCRYSDVVFPAATWYEKTELVTT 565
Cdd:cd02769 396 PfdynGKKLTYPD--IKLVYWAGGNPFHHHQDLNRLIRAWQKPET-VIVH-EPFWTATARHADIVLPATTSLERNDIGGS 471
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1731597526 566 PLHPYMQLQQPAIRPLYEARSELWMAKELAKRLdpGFAKHF 606
Cdd:cd02769 472 GDNRYIVAMKQVVEPVGEARDDYDIFADLAERL--GVEEQF 510
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
12-822 |
8.82e-42 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 164.46 E-value: 8.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 12 LSRRQFLKASAATAvlAGTAGATRYFIP-KAGAENTSPLKEVKYVRTTCSPnctlACGIRAMVVDGQIKALLP--SNDYP 88
Cdd:PRK15102 1 ASRRRFLKGLGGLS--AAGMLGPSLLTPrSALAAQAAAAETTKEWILTGSH----WGAFRAKVKNGRFVEAKPfeLDKYP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 89 EPeygprgCLRGLSfiNLIYGPDRIKKPLIR-----------TGERGAGEFREVSWEEALDYTAKRLKEIAAKYGPESIg 157
Cdd:PRK15102 75 TK------MINGIK--GHVYNPSRIRYPMVRldwlrkrhksdTSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSAL- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 158 FIFQVG---------GTGHVQKGawIAL-----------ATMAG-------------------WSLIHpydQNGDLPMFW 198
Cdd:PRK15102 146 HTGQTGwqstgqfhsATGHMQRA--IGMhgnsvgtvgdySTGAGqvilpyvlgstevyeqgtsWPLIL---ENSKTIVLW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 199 P------QTFGVQTEELEPLEWLnsrytaifgsnimvtrlidADFLIKARNNGTKVVVFDPNYSPTAAKAD-EWVQLKPS 271
Cdd:PRK15102 221 GsdpvknLQVGWNCETHESYAYL-------------------AQLKEKVAKGEINVISIDPVVTKTQNYLGcEHLYVNPQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 272 SDAALALGMARVIIEEKLYDEAFIKTYSdmpllvrldngrrLKADEvkglarpdglppyreaFVAYngkllavhpeklel 351
Cdd:PRK15102 282 TDVPLMLALAHTLYSENLYDKKFIDNYC-------------LGFEQ----------------FLPY-------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 352 ppdviLEGEievelKDGrlvrvkpvfqllkehlASYTPAYVEQETGVPGDTVVRLAREMATTKPlHVIYGASNYQWYHGD 431
Cdd:PRK15102 319 -----LLGE-----KDG----------------VPKTPEWAEKICGIDAETIRELARQMAKGRT-QIIAGWCIQRQQHGE 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 432 LKGRALALLPVLTGNIGKPGAGIStYAGQY------------------------KIRFNVKEwwFPGSPRWLP---WL-Y 483
Cdd:PRK15102 372 QPYWMGAVLAAMLGQIGLPGGGIS-YGHHYsgigvpssggaipggfpgnldtgqKPKHDNSD--YKGYSSTIPvarFIdA 448
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 484 ILHgptPGMKARWpkNG-------VKALIFGWGNPFDQHNMADRLRQMAIKgeLEFIAGLDFSLTTSCRYSDVVFPAATW 556
Cdd:PRK15102 449 ILE---PGKTINW--NGkkvtlppLKMMIFSGTNPWHRHQDRNRMKEAFRK--LETVVAIDNQWTATCRFADIVLPACTQ 521
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 557 YEKTELVTTPLHP---YMQLQQpAIRPLYEARSELWMAKELAKRLdpGFAKHFFPELDENTAAEKAVELLLATGGPPVAG 633
Cdd:PRK15102 522 FERNDIDQYGSYSnrgIIAMKK-VVEPLFESRSDFDIFRELCRRF--GREKEYTRGMDEMGWLKRLYQECKQQNKGKFHM 598
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 634 ITLEQL-KKGPVRLKSEVPGNRQIPFYEQVQFKkpfpPVSRPaaieataqfvkSGRIEFYKDEDAfiALG-ETLPVHKPP 711
Cdd:PRK15102 599 PEFDEFwKKGYVEFGEGQPWVRHADFREDPELN----PLGTP-----------SGLIEIYSRKIA--DMGyDDCQGHPMW 661
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 712 FEDSEYALNPEIKGKYQFAYITRNSLYRVHSTHSNNLWMNE---LQDNKPkVFLNPQDAAAKGIKEGDLVEVYNDRGRVR 788
Cdd:PRK15102 662 FEKIERSHGGPGSDKYPLWLQSVHPDKRLHSQLCESEELREtytVQGREP-VYINPQDAKARGIKDGDVVRVFNDRGQVL 740
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1731597526 789 GYAALDPGLGRKIVVFEQG-WWSRYLNG-----DSY---NSLT 822
Cdd:PRK15102 741 AGAVVSDRYPPGVIRIHEGaWYGPDKGGeigalCTYgdpNTLT 783
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
57-629 |
2.55e-41 |
|
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: 159.87 E-value: 2.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 57 TTCsPNCTLACGIRAMVVDGQIKALLPSNDYPepeyGPRG--CLRGLSFINLIYGPDRIKKPLIRTGergaGEFREVSWE 134
Cdd:cd02762 2 RAC-ILCEANCGLVVTVEDGRVASIRGDPDDP----LSKGyiCPKAAALGDYQNDPDRLRTPMRRRG----GSFEEIDWD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 135 EALDYTAKRLKEIAAKYGPESIGFiFQVGGTGHVQKGAWIALATMAG------------------WSLIHPYDQNGDLPm 196
Cdd:cd02762 73 EAFDEIAERLRAIRARHGGDAVGV-YGGNPQAHTHAGGAYSPALLKAlgtsnyfsaatadqkpghFWSGLMFGHPGLHP- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 197 fwpqtfgvqTEELEplewlNSRYTAIFGSNIMVTR-----LIDADFLIKA-RNNGTKVVVFDPNYSPTAAKADEWVQLKP 270
Cdd:cd02762 151 ---------VPDID-----RTDYLLILGANPLQSNgslrtAPDRVLRLKAaKDRGGSLVVIDPRRTETAKLADEHLFVRP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 271 SSDAALALGMARVIIEEKLYDEAFIktysdmpllvrldngrrlkADEVKGLARpdglppyreafvayngkllavhpekle 350
Cdd:cd02762 217 GTDAWLLAAMLAVLLAEGLTDRRFL-------------------AEHCDGLDE--------------------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 351 lppdvilegeievelkdgrlvrvkpvfqlLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLhVIY---GASnyQW 427
Cdd:cd02762 251 -----------------------------VRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSA-AVYgrlGVQ--TQ 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 428 YHGDLKGRALALLPVLTGNIGKPGAGIST-----YAGQYKIR-FNVKEWWFPGSPrwlpwLYILHGPTPG------MKAR 495
Cdd:cd02762 299 LFGTLCSWLVKLLNLLTGNLDRPGGAMFTtpaldLVGQTSGRtIGRGEWRSRVSG-----LPEIAGELPVnvlaeeILTD 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 496 WPKNgVKALIFGWGNPFdqHNMADRLRQMAIKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELvtTPLHP-----Y 570
Cdd:cd02762 374 GPGR-IRAMIVVAGNPV--LSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPHA--TFFNLefprnA 448
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1731597526 571 MQLQQPAIRPLYEARSELWMAKELAKRLDPGFAKHFFpelDENTAAEKAVELLLATGGP 629
Cdd:cd02762 449 FRYRRPLFPPPPGTLPEWEILARLVEALDAVLRAGFY---GERAGGTLLLAALLERPSG 504
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
57-598 |
1.34e-39 |
|
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: 157.44 E-value: 1.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 57 TTCSpNCTLACGIRAM-VVDGQIKALLPSNDYPEPEYGP-RGCLRGLSFINLIYGPDRIKKPLIRTG-ERGAGE---FRE 130
Cdd:cd02760 2 TYCY-NCVAGPDFMAVkVVDGVATEIEPNFAAEDIHPARgRVCVKAYGLVQKTYNPNRVLQPMKRTNpKKGRNEdpgFVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 131 VSWEEALDYTAKRLKEIAAKYGPESIGFI-----FQVGGTGHVQKGAWIALatMAGWSLIHPYDQNGDLPM--------- 196
Cdd:cd02760 81 ISWDEALDLVAAKLRRVREKGLLDEKGLPrlaatFGHGGTPAMYMGTFPAF--LAAWGPIDFSFGSGQGVKcvhsehlyg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 197 -FWPQTFGVQTEElePLewlnSRYTAIFGSNI-------MVTRLIDAdflikaRNNGTKVVVFDPNYSPTAAKADEWVQL 268
Cdd:cd02760 159 eFWHRAFTVAADT--PL----ANYVISFGSNVeasggpcAVTRHADA------RVRGYKRVQVEPHLSVTGACSAEWVPI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 269 KPSSDAALALGMARVIIEEK---LYDEAFIKTYSDMPLLVRLD--------NGRRLKADEVKGLARPDGLPPYREAFVAy 337
Cdd:cd02760 227 RPKTDPAFMFAMIHVMVHEQglgKLDVPFLRDRTSSPYLVGPDglylrdaaTGKPLVWDERSGRAVPFDTRGAVPAVAG- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 338 ngkllavhpeklelppDVILEGEIEVELKDGRL----VRVKPVFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATT 413
Cdd:cd02760 306 ----------------DFAVDGAVSVDADDETAihqgVEGTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIAREFLEN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 414 ----------------KPLHVIYG-ASNYQWyhGDLKG-RALALLPVLTGNIGKPGAGIST---------------YAGQ 460
Cdd:cd02760 370 asigstievdgvtlpyRPVAVTLGkSVNNGW--GAFECcWARTLLATLVGALEVPGGTLGTtvrlnrphddrlasvKPGE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 461 -----------YKIRFNVKEWW---------FPGSPRW--------LPWLYILHGPTP-GMKARWP--------KNGVKA 503
Cdd:cd02760 448 dgfmaqgfnptDKEHWVVKPTGrnahrtlvpIVGNSAWsqalgptqLAWMFLREVPLDwKFELPTLpdvwfnyrTNPAIS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 504 LifgWGNPFDQHNMAdrlrqmaikgELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTP---------LHPYMQLQ 574
Cdd:cd02760 528 F---WDTATLVDNIA----------KFPFTVSFAYTEDETNWMADVLLPEATDLESLQMIKVGgtkfveqfwEHRGVVLR 594
|
650 660
....*....|....*....|....
gi 1731597526 575 QPAIRPLYEARSELWMAKELAKRL 598
Cdd:cd02760 595 QPAVEPQGEARDFTWISTELAKRT 618
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
56-632 |
1.13e-33 |
|
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: 138.30 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 56 RTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPEPeygpRG--CLRGLSFINLIYGPDRIKKPLIRTGerGAGEFREVSW 133
Cdd:cd02752 1 RTIC-PYCSVGCGLIAYVQNGVWVHQEGDPDHPVN----RGslCPKGAALRDFVHSPKRLKYPMYRAP--GSGKWEEISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 134 EEALDYTAKRLKEI---------AAKY---GPESIGFIfqvGGTGHVQKGAWIALATMAGWSLIHPYDQ---------NG 192
Cdd:cd02752 74 DEALDEIARKMKDIrdasfveknAAGVvvnRPDSIAFL---GSAKLSNEECYLIRKFARALGTNNLDHQariuhsptvAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 193 DLPMFwpqTFGVQTEELEPLEwlNSRYTAIFGSNIMVTRLIDADFLIKAR-NNGTKVVVFDPNYSPTAAKADEWVQLKPS 271
Cdd:cd02752 151 LANTF---GRGAMTNSWNDIK--NADVILVMGGNPAEAHPVSFKWILEAKeKNGAKLIVVDPRFTRTAAKADLYVPIRSG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 272 SDAALALGMARVIIEeklydeafiktysdmpllvrldngrrlkadevkglarpdglppyreafvayngkllavhpeklel 351
Cdd:cd02752 226 TDIAFLGGMINYIIR----------------------------------------------------------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 352 ppdvilegeievelkdgrlvrvkpvfqllkehlasYTPAYVEQETGVPGDTVVRLAREMATT----KPLHVIYGASNYQW 427
Cdd:cd02752 241 -----------------------------------YTPEEVEDICGVPKEDFLKVAEMFAATgrpdKPGTILYAMGWTQH 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 428 YHGDLKGRALALLPVLTGNIGKPGAGISTYAGQYkirfNVKewwfpGS------PRWLPWLYILHGPTPGmkARWPKNGV 501
Cdd:cd02752 286 TVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHS----NVQ-----GAtdlgllSHNLPGYLGGQNPNSS--FPNANKVR 354
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 502 KALI-FGW---GNPFDqhNMADRLRQMaikgelefiAGLDfslTTSCRYSDVVFPAATWYEKTELVTTPlHPYMQLQQPA 577
Cdd:cd02752 355 RALDkLDWlvvIDPFP--TETAAFWKN---------PGMD---PKSIQTEVFLLPAACQYEKEGSITNS-GRWLQWRYKV 419
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1731597526 578 IRPLYEARSELWMAKELAKRLdpgfakHFFPELDENTAAEKAVELLLATGGPPVA 632
Cdd:cd02752 420 VEPPGEAKSDGDILVELAKRL------GFLYEKEGGAFPEPITKWNYGYGDEPTP 468
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
57-451 |
5.36e-29 |
|
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: 123.79 E-value: 5.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 57 TTCSpNCTLACGIRAMVVDGQIKALLPSNDYPEPeygpRG--CLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWE 134
Cdd:cd02763 2 TTCY-MCACRCGIRVHLRDGKVRYIKGNPDHPLN----KGviCAKGSSGIMKQYSPARLTKPLLRKGPRGSGQFEEIEWE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 135 EALDYTAKRLKEIAAKyGPESIGFIF--------------QVGGTGHVQKGAWIAlATMAGWSLihpYDQNGDlpmFWpq 200
Cdd:cd02763 77 EAFSIATKRLKAARAT-DPKKFAFFTgrdqmqaltgwfagQFGTPNYAAHGGFCS-VNMAAGGL---YSIGGS---FW-- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 201 TFGvqteelEPlEWLNSRYTAIFG------SNIMVTRLIDadflIKARnnGTKVVVFDPNYSPTAAKADEWVQLKPSSDA 274
Cdd:cd02763 147 EFG------GP-DLEHTKYFMMIGvaedhhSNPFKIGIQK----LKRR--GGKFVAVNPVRTGYAAIADEWVPIKPGTDG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 275 ALALGMARVIIEEKLYDEAFIKTYSDMPLLVrldngrrlkadevkglarpdglppyreafvayngkllavhpeklelppd 354
Cdd:cd02763 214 AFILALAHELLKAGLIDWEFLKRYTNAAELV------------------------------------------------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 355 vilegeievelkdgrlvrvkpvfqllkehlaSYTPAYVEQETGVPGDTVVRLAREMATT--------------------- 413
Cdd:cd02763 245 -------------------------------DYTPEWVEKITGIPADTIRRIAKELGVTardqpielpiawtdvwgrkhe 293
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1731597526 414 ----KP--LHVIYG-ASNYQWYHgdlKGRALALLPVLTGNIGKPG 451
Cdd:cd02763 294 kitgRPvsFHAMRGiAAHSNGFQ---TIRALFVLMMLLGTIDRPG 335
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
57-640 |
5.93e-25 |
|
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: 111.28 E-value: 5.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 57 TTCSpNCTLACGIRAMVVD--GQIK-------ALL---PSNDYPEP---------------EYGPRGCLRGLSFINLIYG 109
Cdd:cd02758 2 SSCL-GCWTQCGIRVRVDKetGKVLriagnpyHPLntaPSLPYNTPlkeslylslvgenglKARATACARGNAGLQYLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 110 PDRIKKPLIRTGERGAGEFREVSWEEALdytakrlKEIAAKygpesiGFIFqvgGTGHVQKGAWIALATmagwSLIHPyd 189
Cdd:cd02758 81 PYRVLQPLKRVGPRGSGKWKPISWEQLI-------EEVVEG------GDLF---GEGHVEGLKAIRDLD----TPIDP-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 190 QNGDL------------------PM---FWPQTFG----------------------VQTEELEPL---EWLNSRY---- 219
Cdd:cd02758 139 DHPDLgpkanqllytfgrdegrtPFikrFANQAFGtvnfgghgsycglsyragngalMNDLDGYPHvkpDFDNAEFalfi 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 220 -TAIFGSNIMVTRLidADFLIKAR-NNGTKVVVFDP---NYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYDEAF 294
Cdd:cd02758 219 gTSPAQAGNPFKRQ--ARRLAEARtEGNFKYVVVDPvlpNTTSAAGENIRWVPIKPGGDGALAMAMIRWIIENERYNAEY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 295 iktysdmpllvrldngrrlkadevkgLARPDGLPPYREAFVAYNGkllAVHPeklelppdVIlegeievelkdgrLVRVK 374
Cdd:cd02758 297 --------------------------LSIPSKEAAKAAGEPSWTN---ATHL--------VI-------------TVRVK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 375 PVFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMAT--TKPLHVIYGASNYQwyHGDLKGRALALLPVLTGNIGKPGa 452
Cdd:cd02758 327 SALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTShgRAAAVVHHGGTMHS--NGFYNAYAIRMLNALIGNLNWKG- 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 453 GISTYAGQYK-----IRFN-------VKEWWFP-----------------------GSPRWLPWlYILHGPT-----PGM 492
Cdd:cd02758 404 GLLMSGGGFAdnsagPRYDfkkffgeVKPWGVPidrskkayektseykrkvaagenPYPAKRPW-YPLTPELyteviASA 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 493 KARWPKnGVKALIFGWGNP-----FDQHNMADRLRQmaiKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPL 567
Cdd:cd02758 483 AEGYPY-KLKALILWMANPvygapGLVKQVEEKLKD---PKKLPLFIAIDAFINETSAYADYIVPDTTYYESWGFSTPWG 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 568 H-PYMQ--LQQPAIRPLYEARSE-----LW-MAKELAKRLD-PGFAKHFFPELDE-----NTAAE---KAVELLLATGGP 629
Cdd:cd02758 559 GvPTKAstARWPVIAPLTEKTANghpvsMEsFLIDLAKALGlPGFGPNAIKDGQGnkfplNRAEDyylRVAANIAYDGKA 638
|
730
....*....|.
gi 1731597526 630 PVAGITLEQLK 640
Cdd:cd02758 639 PVPDASEEELK 649
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
729-830 |
7.03e-24 |
|
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: 96.96 E-value: 7.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 729 FAYITRNSLYRVHSTHSNNLWMNELQDNKPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGW 808
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100
....*....|....*....|..
gi 1731597526 809 WSRYLNGdSYNSLTYPFIKPTH 830
Cdd:pfam01568 81 WYEPRGG-NANALTDDATDPLS 101
|
|
| MopB_CT |
cd02775 |
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ... |
736-829 |
2.84e-23 |
|
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: 95.08 E-value: 2.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 736 SLYRVHS-THSNNLWMNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWWSRYLN 814
Cdd:cd02775 1 LRDHFHSgTRTRNPWLRELAPE-PVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGGR 79
|
90
....*....|....*
gi 1731597526 815 GDSYNSLTYPFIKPT 829
Cdd:cd02775 80 GGNANVLTPDALDPP 94
|
|
| MopB_CT_Nitrate-R-NarG-like |
cd02776 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
729-832 |
4.27e-22 |
|
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. This CD (MopB_CT_Nitrate-R-NarG-like) is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239177 [Multi-domain] Cd Length: 141 Bit Score: 93.21 E-value: 4.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 729 FAYITRNSLYRVHSTHSNNLWMNELQDNKPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGW 808
Cdd:cd02776 2 LNYLTPHGKWSIHSTYRDNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHAQ 81
|
90 100 110
....*....|....*....|....*....|...
gi 1731597526 809 ---------WSRYLNGDSYNSLTYPFIKPTHEV 832
Cdd:cd02776 82 erhvnvpgsKLTGKRGGIHNSVTRVRIKPTHLV 114
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
11-813 |
4.84e-22 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 102.38 E-value: 4.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 11 KLSRRQFLKASAATA-------------------VLAGTAG-ATR-----------YFIPKAGAENTSPLKEVKYvrTTC 59
Cdd:PRK14991 2 DKTRRQLLKGGLAAGglaafaagysdtakraakgLLNGTSGkPTRdrihgnsltpeYRVDAQGQLQPNPQQRVAN--TQC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 60 SpNCTLACGIRAMV--VDGQIKALL-----P-SNDYPEP--------------EYGPRG----CLRGLSFINLIYGPDRI 113
Cdd:PRK14991 80 L-GCWTQCGVRVRVdnATNKILRIAgnpyhPlSTDHHIDmstpvkeafeslsgESGLEGrstaCARGNAMLEQLDSPYRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 114 KKPLIRTGERGAGEFREVSWEEALDYTAKR-----------LKEI----------AAKYGPESIG--------------- 157
Cdd:PRK14991 159 LQPLKRVGKRGSGKWQRISFEQLVEEVVEGgdlfgeghvdgLRAIrdldtpidakNPEYGPKANQllvtnasdegrdafi 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 158 --FIFQVGGT----GHvqkGAWIALATMAGWSLIHpydqnGDLPmfwpqtfgvQTEELEPlEWLNSRYtAIFgsniMVT- 230
Cdd:PRK14991 239 krFAFNSFGTrnfgNH---GSYCGLAYRAGSGALM-----GDLD---------KNPHVKP-DWDNVEF-ALF----IGTs 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 231 ---------RliDADFLIKARNNGT-KVVVFDP---NYSPTAA-KADEWVQLKPSSDAALALGMARVIIEEKLYDEAFI- 295
Cdd:PRK14991 296 paqsgnpfkR--QARQLANARTRGNfEYVVVAPalpLSSSLAAgDNNRWLPIRPGTDSALAMGMIRWIIDNQRYNADYLa 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 296 ------------KTYSDMPLLVRLD-----NGRRLKA----DEVKGLARPDGLPPYreaFVAYNGKLLAVHPEKLELPPD 354
Cdd:PRK14991 374 qpgvaamqaageASWTNATHLVIADpghprYGQFLRAsdlgLPFEGEARGDGEDTL---VVDAADGELVPATQAQPARLF 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 355 VilegEIEVELKDGRLVRVKPVFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMAT--TKPLHVIYG---ASN--YQW 427
Cdd:PRK14991 451 V----EQYVTLADGQRVRVKSSLQLLKEAARKLSLAEYSEQCGVPEAQIIALAEEFTShgRKAAVISHGgtmSGNgfYNA 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 428 YhgdlkgrALALLPVLTGNIGKPGaGISTYAGQYKI-----RFNVKEwwFPGS--------------------------- 475
Cdd:PRK14991 527 W-------AIMMLNALIGNLNLKG-GVVVGGGKFPGfgdgpRYNLAS--FAGKvkpkgvslsrskfpyeksseyrrkvea 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 476 -----PRWLPWlYILHGPT-----PGMKARWPKnGVKALIFGWGNPFD-----QHNMADRLRQMAIkgeLEFIAGLDFSL 540
Cdd:PRK14991 597 gqspyPAKAPW-YPFVAGLltemlTAALEGYPY-PLKAWINHMSNPIYgvpglRAVIEEKLKDPKK---LPLFISIDAFI 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 541 TTSCRYSDVVFPAATWYEKTElVTTPLHPYMQLQQPAIRPLYEARselwMAK--------------ELAKRLD-PGFAKH 605
Cdd:PRK14991 672 NETTALADYIVPDTHTYESWG-FTAPWGGVPTKASTARWPVVEPR----TAKtadgqpvcmesfliAVAKRLQlPGFGDN 746
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 606 FFPELDENT-AAEKAVELLLA-------TGGPPVAGITLEQLKKGPV---------RLKSE---------VPGNRQIPFY 659
Cdd:PRK14991 747 AIKDAQGNThPLNRAEDFYLRgaaniayLGKTPVADASDEDIALTGVsrilpalqaTLKPDevrrvafiyARGGRFAPAE 826
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 660 EQVQFKKPFPPVSRPAAI----EATAQFVKSGriEFYKD-----EDAFI---ALGETLPVHKPPFEDSEYalnpeiKGKY 727
Cdd:PRK14991 827 SAYDEERMGNRWKKPLQIwnedVAAARHSMTG--ERYSGcptwyPPRLAdgtPLREQFPESQWPLLLISF------KSNL 898
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 728 QFAYitRNSLYRVHSTHSNNLwmnelqdnkpkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQG 807
Cdd:PRK14991 899 MSSM--SIASPRLRQVKPANP-----------VALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAIEHG 965
|
....*.
gi 1731597526 808 WWSRYL 813
Cdd:PRK14991 966 YGHREL 971
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
11-296 |
9.22e-17 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 84.95 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 11 KLSRRQFLKASAATAVlAGTAGATryfIP-KAGAENTSPLKEVKYVRTTCSpNCTLACGIRAMVVDGQIKAllpSNDYPE 89
Cdd:PRK13532 2 KLSRRDFMKANAAAAA-AAAAGLS---LPaVANAVVGSAQTAIKWDKAPCR-FCGTGCGVLVGTKDGRVVA---TQGDPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 90 PEYGpRG--CLRG--LSFInlIYGPDRIKKPLIRTgERGA----GEFREVSWEEALDYTAKRLKEIAAKYGPESIGfIFq 161
Cdd:PRK13532 74 APVN-RGlnCIKGyfLSKI--MYGKDRLTQPLLRM-KDGKydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVG-MF- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 162 vgGTGH--VQKGaWIALATM-AGWsLIHPYDQNGDLPM------FWpQTFGVQteelEP------LEwlNSRYTAIFGSN 226
Cdd:PRK13532 148 --GSGQwtIWEG-YAASKLMkAGF-RSNNIDPNARHCMasavvgFM-RTFGID----EPmgcyddIE--AADAFVLWGSN 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731597526 227 ------IMVTRLIDAdfliKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYDEAFIK 296
Cdd:PRK13532 217 maemhpILWSRVTDR----RLSNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVN 288
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
727-822 |
1.14e-16 |
|
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: 76.55 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 727 YQFAYITRNSLYRVHSTHSNNLWMNELQdNKPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQ 806
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELRAKE-GEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEG 79
|
90
....*....|....*..
gi 1731597526 807 GWWSR-YLNGDSYNSLT 822
Cdd:cd02786 80 GWWREhSPDGRGVNALT 96
|
|
| MopB_CT_DMSOR-like |
cd02777 |
The MopB_CT_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
727-809 |
1.26e-16 |
|
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: 76.85 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 727 YQFAYITRNSLYRVHSTHSNNLWMNELQDNKPK--VFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVF 804
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREAYKVKGRepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
....*
gi 1731597526 805 EQGWW 809
Cdd:cd02777 81 PEGAW 85
|
|
| MopB_CT_DmsA-EC |
cd02794 |
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic ... |
727-854 |
1.47e-16 |
|
The MopB_CT_DmsA-EC CD includes the DmsA enzyme of the dmsABC operon encoding the anaerobic dimethylsulfoxide reductase (DMSOR) of Escherichia coli and other related DMSOR-like enzymes. Unlike other DMSOR-like enzymes, this group has a predicted N-terminal iron-sulfur [4Fe-4S] cluster binding site. This CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239195 [Multi-domain] Cd Length: 121 Bit Score: 76.56 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 727 YQFAYITRNSLYRVHSTHSNNLWMNELQDNKpkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQ 806
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNVPWLREAFPQE--VWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1731597526 807 GWWSRYLN-----GDSYNSLTYPFIKPThevyfvpgiwAPNTAWNEALCDVRK 854
Cdd:cd02794 79 GAWYEPDAngidkGGCINTLTGLRPSPL----------AKGNPQHTNLVQVEK 121
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
736-809 |
2.62e-14 |
|
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: 70.41 E-value: 2.62e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731597526 736 SLYRVHSTHSNNLWMNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWW 809
Cdd:cd02781 12 SYYYFHSEHRQLPSLRELHPD-PVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEHGWW 84
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
14-288 |
2.17e-11 |
|
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: 67.13 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 14 RRQFLKASAAtAVLAGTAGATRYFIPKAG-----AENTSPLKEVKYVRTTCSPNctLACGIRAMVVDGQIKALLPSNDYP 88
Cdd:cd02764 1 RRGFLKLMGA-SLAMASAAACRYPVEKIVpyviwPENIVPGETVYYATSLVPAG--EGQGVLVKTVDGRPIKIEGNPDHP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 89 EPEYGPRGclRGLSFINLIYGPDRIKKPLIRTGErgaGEFREVSWEEALDYTAKRLKeiAAKYGPESIGFIFQVGG-TGH 167
Cdd:cd02764 78 ASLGGTSA--RAQASVLSLYDPDRAQGPLRRGID---GAYVASDWADFDAKVAEQLK--AVKDGGKLAVLSGNVNSpTTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 168 VQKGAWIALATMAGWSLIHPYDqNGDLPMFWPQTFG---VQTEELEPlewlnsrytaifgSNIMVTrlIDADFL------ 238
Cdd:cd02764 151 ALIGDFLKKYPGAKHVVYDPLS-AEDVNEAWQASFGkdvVPGYDFDK-------------AEVIVS--IDADFLgswisa 214
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731597526 239 -------IKARNNG-----TKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEK 288
Cdd:cd02764 215 irhrhdfAAKRRLGaeepmSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIKKG 276
|
|
| MopB_CT_Thiosulfate-R-like |
cd02778 |
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, ... |
728-854 |
2.98e-11 |
|
The MopB_CT_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and other related proteins. Thiosulfate reductase catalyzes the cleavage of sulfur-sulfur bonds in thiosulfate. Polysulfide reductase is a membrane-bound enzyme that catalyzes the reduction of polysulfide using either hydrogen or formate as the electron donor. Also included in this CD is the phenylacetyl-CoA:acceptor oxidoreductase, large subunit (PadB2), which has been characterized as a membrane-bound molybdenum-iron-sulfur enzyme involved in anaerobic metabolism of phenylalanine in the denitrifying bacterium Thauera aromatica. The MopB_CT_Thiosulfate-R-like CD is of the conserved molybdopterin_binding C-terminal (MopB_CT) region present in many, but not all, MopB homologs.
Pssm-ID: 239179 [Multi-domain] Cd Length: 123 Bit Score: 61.52 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 728 QFAYITRNSLYRVHSTHSNNLWMNELQDNKpKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQG 807
Cdd:cd02778 1 EFRLIYGKSPVHTHGHTANNPLLHELTPEN-TLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1731597526 808 W-------WSRYLNGDSYNSLTYPFIKPThevyfvpgiwAPNTAWNEALCDVRK 854
Cdd:cd02778 80 FghwapalSRAYGGGVNDNNLLPGSTEPV----------SGGAGLQEFTVTVRK 123
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
51-263 |
1.03e-10 |
|
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: 64.86 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 51 EVKYVRTTCsPNCTLACGIRAMVVDGQIKALLPSNDypEPEYGPRGCLRG-LSFiNLIYGPDRIKKPLIRTGergaGEFR 129
Cdd:COG1034 214 ELKKTPSIC-PHCSVGCNIRVDVRGGKVYRVLPREN--EAVNEEWLCDKGrFGY-DGLNSPDRLTRPLVRKD----GELV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 130 EVSWEEALDYTAKRLKEIAAKYGpesigfifqvggtghvQKGAWIAlatmagwslihpydqnGDLPMFwpqtfgvqTEEL 209
Cdd:COG1034 286 EASWEEALAAAAEGLKALKKAEN----------------SVGAALL----------------GALPDA--------AAIL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1731597526 210 EPLEWLNSRYTAIFGSNImvtRLIDADFLIKARNNGTKVVVFDPNYSPTAAKAD 263
Cdd:COG1034 326 EAAEAGKLKALVLLGADP---YDLDPAAALAALAKADFVVVLDHFGSATAERAD 376
|
|
| MopB_CT_DMSOR-BSOR-TMAOR |
cd02793 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
727-809 |
1.26e-10 |
|
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide reductase (BSOR), trimethylamine N-oxide reductase (TMAOR) and other related proteins. DMSOR always catalyzes the reduction of DMSO to dimethylsulfide, but its cellular location and oligomerization state are organism-dependent. For example, in Rhodobacter sphaeriodes and Rhodobacter capsulatus, it is an 82-kDa monomeric soluble protein found in the periplasmic space; in E. coli, it is membrane-bound and exists as a heterotrimer. BSOR catalyzes the reduction of biotin sulfixode to biotin, and is unique among Mo enzymes because no additional auxiliary proteins or cofactors are required. TMAOR is similar to DMSOR, but its only natural substrate is TMAO.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: 59.96 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 727 YQFAYITRNSLYRVHS-----THSNNlwmNELQDNKPkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKI 801
Cdd:cd02793 1 YPLHLLSNQPATRLHSqldhgSLSRA---YKVQGREP-IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGV 76
|
....*...
gi 1731597526 802 VVFEQGWW 809
Cdd:cd02793 77 VQLPTGAW 84
|
|
| Molybdop_Fe4S4 |
pfam04879 |
Molybdopterin oxidoreductase Fe4S4 domain; This domain is found in formate dehydrogenase H for ... |
53-109 |
2.76e-09 |
|
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: 53.45 E-value: 2.76e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1731597526 53 KYVRTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPEPEYgpRGCLRGLSFINLIYG 109
Cdd:pfam04879 2 KVVKTIC-PYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEG--RLCVKGRFGYERVYN 55
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
107-159 |
3.86e-09 |
|
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: 59.67 E-value: 3.86e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1731597526 107 IYGPDRIKKPLIRTGergaGEFREVSWEEALDYTAKRLKEIAAKYGPESIGFI 159
Cdd:cd02772 49 LNSEDRLTKPMIKKD----GQWQEVDWETALEYVAEGLSAIIKKHGADQIGAL 97
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
58-325 |
9.90e-09 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 58.32 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 58 TCsPNCTLACG-IRAMVVDGQIKALLpsndypepeygpRGCLRGLSFINLIYGPDRIKKPLIRtgergageFREVSWEEA 136
Cdd:COG1029 9 VC-PFCGCLCDdLEVEVEGGKIVVVK------------NACAIGAAKFERAVSDHRITSPRIR--------GKEVSLEEA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 137 LDYTAKRLKEiaAKYgPesigFIFQVGGT-GHVQKGAwIALATMAGWSLIHPYD----------QNG------------- 192
Cdd:COG1029 68 IDKAAEILAN--AKR-P----LIYGLSSTdCEAMRAG-LALAERVGAVVDNTASvchgpsllalQDVgwptctlgevknr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 193 -DLPMFWpqtfGVQTEELEPLEWlnSRYTaifgsnimvtrlIDAD--FLIKARnNGTKVVVFDPNYSPTAAKADEWVQLK 269
Cdd:COG1029 140 aDVIIYW----GCNPVHAHPRHM--SRYS------------VFPRgfFTPKGR-KDRTVIVVDPRPTDTAKVADLHLQVK 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1731597526 270 PSSDAALALGMaRVIIeeklydeafiktysdmpllvrldNGRRLKADEVKGLARPD 325
Cdd:COG1029 201 PGRDYEVLSAL-RALV-----------------------RGKELSPEEVAGIPVED 232
|
|
| MopB_CT_Tetrathionate_Arsenate-R |
cd02780 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate ... |
727-807 |
2.07e-08 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of tetrathionate reductase, subunit A, (TtrA); respiratory arsenate As(V) reductase, catalytic subunit (ArrA); and other related proteins.
Pssm-ID: 239181 [Multi-domain] Cd Length: 143 Bit Score: 53.84 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 727 YQFAYITRNSLYRVHSThSNNLWMNELQDNKPkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQ 806
Cdd:cd02780 1 YPFILVTFKSNLNSHRS-ANAPWLKEIKPENP-VWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIEH 78
|
.
gi 1731597526 807 G 807
Cdd:cd02780 79 G 79
|
|
| MopB_CT_Arsenite-Ox |
cd02779 |
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase ... |
758-840 |
2.56e-08 |
|
This CD contains the molybdopterin_binding C-terminal (MopB_CT) region of Arsenite oxidase (Arsenite-Ox) and related proteins. Arsenite oxidase oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin.
Pssm-ID: 239180 [Multi-domain] Cd Length: 115 Bit Score: 52.85 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 758 PKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWWSrylngDSYNSLTYPFIKPTHEVYFVPG 837
Cdd:cd02779 33 PYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHPR-----PGANGLVTPYVDPETIIPYYKG 107
|
...
gi 1731597526 838 IWA 840
Cdd:cd02779 108 TWA 110
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
749-822 |
6.84e-08 |
|
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: 51.74 E-value: 6.84e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731597526 749 WMNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKiVVFEQGWWSRYLNGDSYNSLT 822
Cdd:cd00508 27 RLAALAPE-PFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPG-TVFMPFHWGGEVSGGAANALT 98
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
52-108 |
6.87e-08 |
|
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: 49.56 E-value: 6.87e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1731597526 52 VKYVRTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPEPEYgpRGCLRGLSFINLIY 108
Cdd:smart00926 1 EKWVPTVC-PLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRG--RLCPKGRAGLEQVY 54
|
|
| MopB_CT_Nitrate-R-NapA-like |
cd02791 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
757-828 |
1.08e-07 |
|
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: 51.03 E-value: 1.08e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1731597526 757 KPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWWSRYLNGDSYNSLTYPFIKP 828
Cdd:cd02791 34 EPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFVPMHWGDQFGRSGRVNALTLDATDP 105
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
112-455 |
1.54e-07 |
|
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: 55.01 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 112 RIKKPLIRtgERGAGEFREVSWEEALDYTAKRLKEI----AAKY----GPESIGFIFQ----VGGTGHVQKGAWIALATm 179
Cdd:cd02767 64 RLTYPMRY--DAGSDHYRPISWDEAFAEIAARLRALdpdrAAFYtsgrASNEAAYLYQlfarAYGTNNLPDCSNMCHEP- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 180 AGWSLihpydqngdlpmfwPQTFGV--QTEELEplEWLNSRYTAIFGSN------IMVTrlidadFLIKARNNGTKVVVF 251
Cdd:cd02767 141 SSVGL--------------KKSIGVgkGTVSLE--DFEHTDLIFFIGQNpgtnhpRMLH------YLREAKKRGGKIIVI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 252 DP-------NY-SPTAAK---------ADEWVQLKPSSDAALALGMARVIIEEK-----LYDEAFIKTYSdmpllvrldn 309
Cdd:cd02767 199 NPlrepgleRFaNPQNPEsmltggtkiADEYFQVRIGGDIALLNGMAKHLIERDdepgnVLDHDFIAEHT---------- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 310 grrlkadevkglarpdglppyreafvayNGkllavhpeklelppdvilegeievelkdgrlvrvkpvFQLLKEHLASYTP 389
Cdd:cd02767 269 ----------------------------SG-------------------------------------FEEYVAALRALSW 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731597526 390 AYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNIGKPGAGIS 455
Cdd:cd02767 284 DEIERASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLM 349
|
|
| MopB_CT_Formate-Dh-Na-like |
cd02792 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
746-854 |
2.49e-07 |
|
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: 50.30 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 746 NNLWMNELQdnkPKVF--LNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVV--FEQGWWSrYLNGDSYNSL 821
Cdd:cd02792 24 NSPYLAELQ---PEMFveISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGipYHWGGMG-LVIGDSANTL 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 1731597526 822 TypfikpthevyfvPGIWAPNT---AWNEALCDVRK 854
Cdd:cd02792 100 T-------------PYVGDPNTqtpEYKAFLVNIEK 122
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
107-278 |
2.66e-07 |
|
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: 53.83 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 107 IYGPDRIKKPLIRTGergaGEFREVSWEEALDYTAKRLKEIAakygPESIGFIfqvgGTGHVQKGAWIALATMAGWSLIH 186
Cdd:cd02768 49 LNSRQRLTQPLIKKG----GKLVPVSWEEALKTVAEGLKAVK----GDKIGGI----AGPRADLESLFLLKKLLNKLGSN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 187 PYDQNGDLPMFWPQTFgvqteeLEPLEWLNSRYTAI--------FGSN------IMVTRLIDAdflikARNNGTKVVVFD 252
Cdd:cd02768 117 NIDHRLRQSDLPADNR------LRGNYLFNTSIAEIeeadavllIGSNlrkeapLLNARLRKA-----VKKKGAKIAVIG 185
|
170 180
....*....|....*....|....*.
gi 1731597526 253 PnySPTAAKADEWVQLKPSSDAALAL 278
Cdd:cd02768 186 P--KDTDLIADLTYPVSPLGASLATL 209
|
|
| 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 ... |
57-632 |
7.97e-07 |
|
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: 52.39 E-value: 7.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 57 TTCsPNCTLACGIRAMVVDGQIKALlpSNDYPEPEYGPRGCLRG---LSFINliyGPDRIKKPLIRTGergaGEFREVSW 133
Cdd:cd02771 2 SIC-HHCSVGCNISLGERYGELRRV--ENRYNGAVNHYFLCDRGrfgYGYVN---SRDRLTQPLIRRG----GTLVPVSW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 134 EEALDYTAKRLKEIAAKygpeSIGFifqvgGTGHVQKGAWIALATMAGWSLihpydqngdlpmfwpqtfgvqteeleple 213
Cdd:cd02771 72 NEALDVAAARLKEAKDK----VGGI-----GSPRASNESNYALQKLVGAVL----------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 214 wlnsrytaifGSNimvtrliDADFliKARNNGTKVVVFDPNYSPTAAKADewvqlkpSSDAALALGmarviieEKLYDEA 293
Cdd:cd02771 114 ----------GTN-------NVDH--RARRLIAEILRNGPIYIPSLRDIE-------SADAVLVLG-------EDLTQTA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 294 FIktysdMPLLVRLDNGRRLKADEVKGLARPDGLPPYREAFVAYNGKLLAVHPEklelpPDVILEGeievelkDGRLVRV 373
Cdd:cd02771 161 PR-----IALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNAL-----ATRLDDI-------AAESIRA 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 374 KPVFQL-LKEHLASYTPAYVE-QETGVPGDTVVRLARE-MATTKPLHVIYGASnyqwyHGDLKGRALALLPVLTGNIGKP 450
Cdd:cd02771 224 SPGGQArLGAALARAVDASAAgVSGLAPKEKAARIAARlTGAKKPLIVSGTLS-----GSLELIKAAANLAKALKRRGEN 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 451 GAgistyagqykirfnvkeWWFPGSPRWLPWLYILHGP-------TPGMKARWPKNGVKALIFGWGNPFDqhnMADRLRQ 523
Cdd:cd02771 299 AG-----------------LTLAVEEGNSPGLLLLGGHvtepgldLDGALAALEDGSADALIVLGNDLYR---SAPERRV 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 524 MAIKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIRPLYEARSELWMAKELAKRLDPGFA 603
Cdd:cd02771 359 EAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAQRFFKAYDDPAGDARSDWRWLHALAAKLGGKLV 438
|
570 580 590
....*....|....*....|....*....|.
gi 1731597526 604 KHFFPELDENTA--AEKAVELLLATGGPPVA 632
Cdd:cd02771 439 PSDAAILDEIIAlvPGKAPVGGHLYGGDPGV 469
|
|
| TAT_signal |
pfam10518 |
TAT (twin-arginine translocation) pathway signal sequence; |
11-34 |
1.72e-05 |
|
TAT (twin-arginine translocation) pathway signal sequence;
Pssm-ID: 463131 [Multi-domain] Cd Length: 26 Bit Score: 41.98 E-value: 1.72e-05
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
726-804 |
1.03e-04 |
|
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: 42.61 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 726 KYQFAYITRNSLYRVHS-THSNNLW-MNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLgRKIVV 803
Cdd:cd02790 2 EYPLVLTTGRVLYHYHTgTMTRRAEgLDAIAPE-EYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRV-PEGVV 79
|
.
gi 1731597526 804 F 804
Cdd:cd02790 80 F 80
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
109-146 |
2.18e-03 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 41.86 E-value: 2.18e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1731597526 109 GPDRIKKPLIRTGErgaGEFREVSWEEALDYTAKRLKE 146
Cdd:PRK07860 275 QPDRITTPLVRDED---GELEPASWSEALAVAARGLAA 309
|
|
| TAT_signal_seq |
TIGR01409 |
Tat (twin-arginine translocation) pathway signal sequence; Proteins assembled with various ... |
12-43 |
2.22e-03 |
|
Tat (twin-arginine translocation) pathway signal sequence; Proteins assembled with various cofactors or by means of cytosolic molecular chaperones are poor candidates for translocation across the bacterial inner membrane by the standard general secretory (Sec) pathway. This model describes a family of predicted long, non-Sec signal sequences and signal-anchor sequences (uncleaved signal sequences). All contain an absolutely conserved pair of arginine residues, in a motif approximated by (S/T)-R-R-X-F-L-K, followed by a membrane-spanning hydrophobic region. Members with small amino acid side chains at the -1 and -3 positions from the C-terminus of the model should be predicted to be cleaved as are Sec pathway signal sequences. Members are almost exclusively bacterial, although archaeal sequences are also found. A large fraction of the members of this family may have bound redox-active cofactors. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273604 Cd Length: 29 Bit Score: 36.34 E-value: 2.22e-03
10 20 30
....*....|....*....|....*....|..
gi 1731597526 12 LSRRQFLKASAATAVLAGTAGatrYFIPKAGA 43
Cdd:TIGR01409 1 LSRRDFLKGAAAAGAAAGLGA---LLPSPARA 29
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
489-628 |
4.23e-03 |
|
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: 40.59 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731597526 489 TPGMKARWPKNGVKALIFGWGNPFDqhnmADRLRQMAIKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTplh 568
Cdd:COG1034 321 AAAILEAAEAGKLKALVLLGADPYD----LDPAAALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVN--- 393
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731597526 569 pyM----QLQQPAIRPLYEARsELWM-AKELAKRLDPGFAkhfFPELDENTAA-EKAVELLLATGG 628
Cdd:COG1034 394 --LegrvQRFNAAVPPPGEAR-PDWRvLRALANALGAGLP---YDSLEEVRAElAAEAPATVSAEG 453
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
739-812 |
4.92e-03 |
|
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: 38.14 E-value: 4.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731597526 739 RVHSThSNNLWMNELQ-----DNKPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWWSRY 812
Cdd:cd02782 10 RRHLR-SNNSWLHNDPrlvkgRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDY 87
|
|
| |
