|
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: 640.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 53 KYVRTTCSPNCTLACGIRAMVVDGQIKALLPSNDYPE-----PEYGPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGE 127
Cdd:cd02750 2 KVVRSTHGVNCTGSCSWNVYVKNGIVTREEQATDYPEtppdlPDYNPRGCQRGASFSWYLYSPDRVKYPLKRVGARGEGK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 128 FREVSWEEALDYTAKRLKEIAARYGPESIGFIFQVGGTGHVQKGAWIALATMVGWSLIHPYDQNGDLPMFWPQTFGVQTE 207
Cdd:cd02750 82 WKRISWDEALELIADAIIDTIKKYGPDRVIGFSPIPAMSMVSYAAGSRFASLIGGVSLSFYDWYGDLPPGSPQTWGEQTD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 208 ELEPLEWLNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEE 287
Cdd:cd02750 162 VPESADWYNADYIIMWGSNVPVTRTPDAHFLTEARYNGAKVVVVSPDYSPSAKHADLWVPIKPGTDAALALAMAHVIIKE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 288 KLYDEAFIKTYSDMPLLVrldngrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeievelkd 367
Cdd:cd02750 242 KLYDEDYLKEYTDLPFLV-------------------------------------------------------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 368 grlvrvkpvfqllkehlasYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNI 447
Cdd:cd02750 260 -------------------YTPAWQEAITGVPRETVIRLAREFATNGRSMIIVGAGINHWYHGDLCYRALILLLALTGNE 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 448 GKPGAGISTYAGQykirfnvkewwfpgsprwlpwlyilhgptpgmkarwpkngIKALIFGWGNPFDQHNMADRLRQMAIK 527
Cdd:cd02750 321 GKNGGGWAHYVGQ----------------------------------------PRVLFVWRGNLFGSSGKGHEYFEDAPE 360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 528 GELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIKPLYEARSELWMARELAKRldpgfakhff 607
Cdd:cd02750 361 GKLDLIVDLDFRMDSTALYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPLWEAKSDWEIFKALAKK---------- 430
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 608 peldentaaekavelllatggppvagitleqlkkgpvrlksevpgnrqIPFyeqvqfkkpfppvsrpaaieataqFVKSG 687
Cdd:cd02750 431 ------------------------------------------------VPW------------------------RTLTG 438
|
650 660
....*....|....*....|...
gi 1731596781 688 RIEFYKDEDAFIALGETLPVHKP 710
Cdd:cd02750 439 RQQFYLDHDWFLELGETLPTYKP 461
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
33-857 |
5.71e-171 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 510.54 E-value: 5.71e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 33 ATRYFIPKAGAENTSPLKEVKYVRTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPEPEyGpRGCLRGLSFINLIYGPDR 112
Cdd:COG0243 2 SLRDFKAAGAGAAALEAAGTKTVKTTC-PGCGVGCGLGVKVEDGRVVRVRGDPDHPVNR-G-RLCAKGAALDERLYSPDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 113 IKKPLIRTGERGAGEFREVSWEEALDYTAKRLKEIAARYGPESIGFIFQVGGTGHVQ-KGAWIA--LATMVGWSLihpYD 189
Cdd:COG0243 79 LTYPMKRVGPRGSGKFERISWDEALDLIAEKLKAIIDEYGPEAVAFYTSGGSAGRLSnEAAYLAqrFARALGTNN---LD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 190 QNGDL-----PMFWPQTFGVQTEELEPLEWLNSRYTAIFGSNIMVTRLIDADFLIKA-RNNGTKVVVFDPNYSPTAAKAD 263
Cdd:COG0243 156 DNSRLchesaVAGLPRTFGSDKGTVSYEDLEHADLIVLWGSNPAENHPRLLRRLREAaKKRGAKIVVIDPRRTETAAIAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 264 EWVQLKPSSDAALALGMARVIIEEKLYDEAFIKTYSDMpllvrldngrrlkadevkglarpdglppyreafvayngklla 343
Cdd:COG0243 236 EWLPIRPGTDAALLLALAHVLIEEGLYDRDFLARHTVG------------------------------------------ 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 344 vhpeklelppdvilegeievelkdgrlvrvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGAS 423
Cdd:COG0243 274 ---------------------------------FDELAAYVAAYTPEWAAEITGVPAEDIRELAREFATAKPAVILWGMG 320
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 424 NYQWYHGDLKGRALALLPVLTGNIGKPGAGIstyagqykirfnvkewwFPGSPRWLpwlyilhgpTPGMKARwpkngIKA 503
Cdd:COG0243 321 LQQHSNGTQTVRAIANLALLTGNIGKPGGGP-----------------FSLTGEAI---------LDGKPYP-----IKA 369
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 504 LIFGWGNPFDQHNMADRLRQmAIKGeLEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIKPLYE 583
Cdd:COG0243 370 LWVYGGNPAVSAPDTNRVRE-ALRK-LDFVVVIDTFLTETARYADIVLPATTWLERDDIVTNSEDRRVHLSRPAVEPPGE 447
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 584 ARSELWMARELAKRLdpGFAKHFfpelDENTAAEKAVELLLATGGPpvAGITLEQLK-KGPVRLksevPGNRQIPFYEQV 662
Cdd:COG0243 448 ARSDWEIFAELAKRL--GFEEAF----PWGRTEEDYLRELLEATRG--RGITFEELReKGPVQL----PVPPEPAFRNDG 515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 663 QFKKPfppvsrpaaieataqfvkSGRIEFYKDEDAFialgETLPVHKPPFEDSEyalnpEIKGKYQFAYITRNSLYRVHS 742
Cdd:COG0243 516 PFPTP------------------SGKAEFYSETLAL----PPLPRYAPPYEGAE-----PLDAEYPLRLITGRSRDQWHS 568
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 743 THSNNLWMNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWWSRYLNGD--SYNS 820
Cdd:COG0243 569 TTYNNPRLREIGPR-PVVEINPEDAAALGIKDGDLVRVESDRGEVLARAKVTEGIRPGVVFAPHGWWYEPADDKggNVNV 647
|
810 820 830
....*....|....*....|....*....|....*..
gi 1731596781 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 |
6.97e-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: 374.89 E-value: 6.97e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 57 TTCSPNCTLACGIRAMVVDGQIKALLPsNDYPEPEYgPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEA 136
Cdd:cd02765 2 TACPPNCGGRCPLKCHVRDGKIVKVEP-NEWPDKTY-KRGCTRGLSHLQRVYSPDRLKYPMKRVGERGEGKFERITWDEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 137 LDYTAKRLKEIAARYGPESIGFIFqvgGTGHVQKGAWIALATMVGW---SLIHPYDQNGDLPMFWPQTFGVQTEELEPLE 213
Cdd:cd02765 80 LDTIADKLTEAKREYGGKSILWMS---SSGDGAILSYLRLALLGGGlqdALTYGIDTGVGQGFNRVTGGGFMPPTNEITD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 214 WLNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYDEA 293
Cdd:cd02765 157 WVNAKTIIIWGSNILETQFQDAEFFLDARENGAKIVVIDPVYSTTAAKADQWVPIRPGTDPALALGMINYILEHNWYDEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 294 FIKTYSDMPLLVRLDNGRRLKADEVkglarpdGLPPYREAFVAYNGKLLAVHP-EKLELPPDviLEGEIEVelkDGrlVR 372
Cdd:cd02765 237 FLKSNTSAPFLVREDNGTLLRQADV-------TATPAEDGYVVWDTNSDSPEPvAATNINPA--LEGEYTI---NG--VK 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 373 VKPVFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPlHVIYGASNYQ-WYHGDLKGRALALLPVLTGNIGKPG 451
Cdd:cd02765 303 VHTVLTALREQAASYPPKAAAEICGLEEAIIETLAEWYATGKP-SGIWGFGGVDrYYHSHVFGRTAAILAALTGNIGRVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 452 AGistyAGQykirfnvkewwfpgsprwlpwlyilhgptpgmkarwpkngIKALIFGwGNPFdQHNMADRLRQMAIKGELE 531
Cdd:cd02765 382 GG----VGQ----------------------------------------IKFMYFM-GSNF-LGNQPDRDRWLKVMKNLD 415
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 532 FIAGLDFSLTTSCRYSDVVFPAATWYE-KTELVTTPLHPYMQLQQPAIKPLYEARSELWMARELAKRLdpGFAkHFFPEL 610
Cdd:cd02765 416 FIVVVDIFHTPTVRYADIVLPAAHWFEvEDLLVRYTTHPHVLLQQKAIEPLFESKSDFEIEKGLAERL--GLG-DYFPKT 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 611 DENTaaekaVELLLATGGPPVAGITLEQLKKGPVRLKSEVPGNRQIPFYEQVqFKKPfppvsrpaaieataqfvkSGRIE 690
Cdd:cd02765 493 PEDY-----VRAFMNSDDPALDGITWEALKEEGIIMRLATPEDPYVAYLDQK-FGTP------------------SGKLE 548
|
650 660
....*....|....*....|.
gi 1731596781 691 FYkdEDAFIALGETLPVHKPP 711
Cdd:cd02765 549 FY--NEAAPELEEALPLPEEP 567
|
|
| dmsA_ynfE |
TIGR02166 |
anaerobic dimethyl sulfoxide reductase, A subunit, DmsA/YnfE family; Members of this family ... |
12-830 |
2.89e-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: 337.90 E-value: 2.89e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 12 LSRRQFLKASAATAVLAGTAGA-TRYFIPKAGAENTSPLKEVKYVRTTCSPNCTLACGIRAMVVDGQIKALLPSNDYpEP 90
Cdd:TIGR02166 1 ISRRHFLKTSAALGGLAAASGAlSLPFSVNAAAEATPTGPDEKVVWSACTVNCGSRCPLRVHVKDGEITRIETDNTG-DD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 91 EYGP---RGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEALDYTAKRLKEIAARYGPESIGFIFQVGGTGH 167
Cdd:TIGR02166 80 EYGNhqvRACLRGRSMRRRVYNPDRLKYPMKRVGKRGEGKFERISWDEATDTIADNLKRIIEKYGNEAIYVNYGTGTTGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 168 VQKGAWIALATMVGWSLIHPY-DQNGDLPM-----FWPQTFGVQTEELEPLEWLNSRYTAIFGSNIMVTRL----IDADF 237
Cdd:TIGR02166 160 TMSRSWPPTAVARLLNLCGGYlNQYGSYSTaqineAMPYTYGISADGSSLDDIENSKLVVMFGNNPAETRMsgggQTYYF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 238 LIKARNNGTKVVVFDPNYSPTAA-KADEWVQLKPSSDAALALGMARVIIEEKLYDEAFIKTYSdmpllVRLDNgrrlkad 316
Cdd:TIGR02166 240 LQALEKSNARVIVIDPRYTDTVAgREDEWIPIRPGTDAALVAAIAYVMISENLHDQAFLDRYC-----VGFDE------- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 317 evKGLarPDGLPPyREAFVAYngkllavhpeklelppdVILEGEIEVElkdgrlvrvkpvfqllkehlasYTPAYVEQET 396
Cdd:TIGR02166 308 --KTL--PASAPK-NGSYKDY-----------------ILGEGADGTP----------------------KTPEWASKIT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 397 GVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNIGKPGAGISTYAGQYKIRFNVkewwFPGSP 476
Cdd:TIGR02166 344 GIPADTIIKLAREIGNAKPAFISQGWGPQRHANGEQAARAIMMLALLTGNVGIKGGNNGAREGNYSLPFAR----MPELP 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 477 R-------WLPWL-YILHGPTpgMKARwpKNGIKA-------LIFGW---GNPF-DQH---NMADRLRQMAIKgeLEFIA 534
Cdd:TIGR02166 420 NpvktsisCFLWTdAIDRGTE--MTAI--KDGVRGkdkldsnIKFLWnyaGNCLiNQHsdiNRTHKILQDESK--CEMIV 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 535 GLDFSLTTSCRYSDVVFPAATWYEKTELV---TTPLHPYMQLQQPAIKPLYEARSELWMARELAKRLDpgfakhFFPELD 611
Cdd:TIGR02166 494 VIDNHMTSSAKYADILLPDTTTLEQNDFIedsYASNMSYLIFMQKAIEPLFECKPIYDMLSEVAKRLG------VEAEFT 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 612 ENTAAEKAVELLLAtggppvagitlEQLKKGPvrlksevpgnrQIPFYEQVQ----FKKPFPPVSRPA------AIEATA 681
Cdd:TIGR02166 568 EGRTQEEWLEHLYA-----------QTRAADP-----------ALPSFAELRkqgiYKAKSAPGPFVAfedfrrDPEANP 625
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 682 QFVKSGRIEFYKDEDAFIA----LGE-----TLPVHKPPFEDSEYALNPEikgkYQFAYITRNSLYRVHSTHSNNLWMNE 752
Cdd:TIGR02166 626 LKTPSGKIEIYSERLAQIAhtweLPEgdvitPLPEYVPTFEGPDDPLRKD----FPLQLTGFHYKGRTHSTYGNVDWLRE 701
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 753 LQDNkpKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQG-WWSRYLN----GDSYNSLTY---- 823
Cdd:TIGR02166 702 AAPQ--ELWINPIDAQKRGITNGDMVRIFNSRGEVEIPAKVTPRIMPGVVALGQGaWYQPDKNgidvGGCINTLTTqrps 779
|
....*....
gi 1731596781 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 |
3.66e-99 |
|
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: 318.04 E-value: 3.66e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 56 RTTCSPNCTLACGIRAMVVDGQIKALLPSNDYPepeYgPRG--CLRGLSFINLIYGPDRIKKPLIRTGeRGAGEFREVSW 133
Cdd:cd02766 1 RSVCPLDCPDTCSLLVTVEDGRIVRVEGDPAHP---Y-TRGfiCAKGARYVERVYSPDRLLTPLKRVG-RKGGQWERISW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 134 EEALDYTAKRLKEIAARYGPESIGFIFQVGGTGHVQKGAWIALATMVGWSLIH--PYDQNGDLPmfWPQTFGvQTEELEP 211
Cdd:cd02766 76 DEALDTIAAKLKEIKAEYGPESILPYSYAGTMGLLQRAARGRFFHALGASELRgtICSGAGIEA--QKYDFG-ASLGNDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 212 LEWLNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYD 291
Cdd:cd02766 153 EDMVNADLIVIWGINPAATNIHLMRIIQEARKRGAKVVVIDPYRTATAARADLHIQIRPGTDGALALGVAKVLFREGLYD 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 292 EAFIKTYSDMpllvrldngrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeievelkdgrlv 371
Cdd:cd02766 233 RDFLARHTEG---------------------------------------------------------------------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 372 rvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKP--LHVIYGASNYqwYHGDLKGRALALLPVLTGNIGK 449
Cdd:cd02766 243 -----FEELKAHLETYTPEWAAEITGVSAEEIEELARLYGEAKPpsIRLGYGMQRY--RNGGQNVRAIDALPALTGNIGV 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 450 PGAGIstyagqykirfnvkewwfpgsprwlpwLYILHGPTpgmkarwpkngIKALIFGWGNPFDQHNMADRLRQMAIKgE 529
Cdd:cd02766 316 PGGGA---------------------------FYSNSGPP-----------VKALWVYNSNPVAQAPDSNKVRKGLAR-E 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 530 LEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIKPLYEARSELWMARELAKRLdpGFAKHFFpE 609
Cdd:cd02766 357 DLFVVVHDQFMTDTARYADIVLPATTFLEHEDVYASYWHYYLQYNEPAIPPPGEARSNTEIFRELAKRL--GFGEPPF-E 433
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 610 LDENTAAEKAvellLATGGPPVAGITLEQLKKGPVRLKSEVPgnrqipfYEQVQFKKPfppvsrpaaieataqfvkSGRI 689
Cdd:cd02766 434 ESDEEWLDQA----LDGTGLPLEGIDLERLLGPRKAGFPLVA-------WEDRGFPTP------------------SGKF 484
|
650
....*....|....*..
gi 1731596781 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 1731596781 63 CTLACGIRAMVVDGQIKALLPsndYPE-PEYGPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEALDYTA 141
Cdd:cd02755 8 CSSRCGILARVEDGRVVKIDG---NPLsPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGERGEGKFREASWDEALQYIA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 142 KRLKEIAARYGPESIGFifqvGGTGHVQKGAWIALATMVGWSLIHPYDQNGDLP--MFWPQTFGVQTEELEPlEWLNSRY 219
Cdd:cd02755 85 SKLKEIKEQHGPESVLF----GGHGGCYSPFFKHFAAAFGSPNIFSHESTCLASknLAWKLVIDSFGGEVNP-DFENARY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 220 TAIFGSN----IMVTRLIDadfLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYDEAFI 295
Cdd:cd02755 160 IILFGRNlaeaIIVVDARR---LMKALENGAKVVVVDPRFSELASKADEWIPIKPGTDLAFVLALIHVLISENLYDAAFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 296 KTYSdmpllvrldNGrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeievelkdgrlvrvkp 375
Cdd:cd02755 237 EKYT---------NG----------------------------------------------------------------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 376 vFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLK-GRALALLPVLTGNIGKPGAgi 454
Cdd:cd02755 243 -FELLKAHVKPYTPEWAAQITDIPADTIRRIAREFAAAAPHAVVDPGWRGTFYSNSFQtRRAIAIINALLGNIDKRGG-- 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 455 styagqykirfnvkeWWFPGSPRwlpwlyilhgPTPgmkarwpkngIKALIFGWGNPFdqHNMADRLR-QMAIKgELEFI 533
Cdd:cd02755 320 ---------------LYYAGSAK----------PYP----------IKALFIYRTNPF--HSMPDRARlIKALK-NLDLV 361
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731596781 534 AGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQ--LQQPAIKPLYEARSELWMARELAKRLDP 600
Cdd:cd02755 362 VAIDILPSDTALYADVILPEATYLERDEPFSDKGGPAPAvaTRQRAIEPLYDTRPGWDILKELARRLGL 430
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
52-804 |
3.70e-90 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 299.49 E-value: 3.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 52 VKYVRTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPePEYGpRGCLRGLSFINLIYGPDRIKKPLIRTGergaGEFREV 131
Cdd:COG3383 4 MKKVKTVC-PYCGVGCGIDLEVKDGKIVKVEGDPDHP-VNRG-RLCVKGRFGFEFVNSPDRLTTPLIRRG----GEFREV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 132 SWEEALDYTAKRLKEIAARYGPESIGFIfqvgGTGH--------VQKGAWIALATmvgwsliHPYDQNGDLPMFwP---- 199
Cdd:COG3383 77 SWDEALDLVAERLREIQAEHGPDAVAFY----GSGQltneenylLQKLARGVLGT-------NNIDNNARLCMA-Savag 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 200 --QTFGVQT-----EELEplewlNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSS 272
Cdd:COG3383 145 lkQSFGSDAppnsyDDIE-----EADVILVIGSNPAEAHPVLARRIKKAKKNGAKLIVVDPRRTETARLADLHLQIKPGT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 273 DAALALGMARVIIEEKLYDEAFIKtysdmpllvrldngrrlkadevkglARPDGlppyreafvayngkllavhpeklelp 352
Cdd:COG3383 220 DLALLNGLLHVIIEEGLVDEDFIA-------------------------ERTEG-------------------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 353 pdvilegeievelkdgrlvrvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDL 432
Cdd:COG3383 249 ------------------------FEELKASVAKYTPERVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTD 304
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 433 KGRALALLPVLTGNIGKPGAGISTYAGQykirFNV-----------------------------KEWWFPGSPRWlPWLy 483
Cdd:COG3383 305 NVNAIINLALATGNIGRPGTGPFPLTGQ----NNVqggrdmgalpnvlpgyrdvtdpehrakvaDAWGVPPLPDK-PGL- 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 484 ilhgPTPGMKARWPKNGIKAL-IFGwGNPFDQHNMADRLRQmAIKgELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTEL 562
Cdd:COG3383 379 ----TAVEMFDAIADGEIKALwIIG-ENPAVSDPDANHVRE-ALE-KLEFLVVQDIFLTETAEYADVVLPAASWAEKDGT 451
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 563 VTTpLHPYMQLQQPAIKPLYEARSELWMARELAKRLDPGFakhffpelDENTAAEKAVELLLATggPPVAGITLEQLKK- 641
Cdd:COG3383 452 FTN-TERRVQRVRKAVEPPGEARPDWEIIAELARRLGYGF--------DYDSPEEVFDEIARLT--PDYSGISYERLEAl 520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 642 GPVR---LKSEVPGNRqipfyeqVQFKKPFPPVSRPAAIEATAqfvksgriefykdedafialgetlpvHKPPFEdseya 718
Cdd:COG3383 521 GGVQwpcPSEDHPGTP-------RLFTGRFPTPDGKARFVPVE--------------------------YRPPAE----- 562
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 719 lnpEIKGKYQFAYITRNSLYRVHS----THSNNLwmNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALD 794
Cdd:COG3383 563 ---LPDEEYPLVLTTGRLLDQWHTgtrtRRSPRL--NKHAPE-PFVEIHPEDAARLGIKDGDLVRVSSRRGEVVLRARVT 636
|
810
....*....|
gi 1731596781 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 |
7.29e-90 |
|
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: 289.23 E-value: 7.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 56 RTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPEPEygPRGCLRGLSFINLIYGPDRIKKPLIRTGERGagEFREVSWEE 135
Cdd:cd00368 1 PSVC-PFCGVGCGILVYVKDGKVVRIEGDPNHPVNE--GRLCDKGRAGLDGLYSPDRLKYPLIRVGGRG--KFVPISWDE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 136 ALDYTAKRLKEIAARYGPESIGFIFQvGGTGHVQKGAWIALATMVGWSLIHPYDQNGDLPMFWPQT-FGVQTEELEPLEW 214
Cdd:cd00368 76 ALDEIAEKLKEIREKYGPDAIAFYGG-GGASNEEAYLLQKLLRALGSNNVDSHARLCHASAVAALKaFGGGAPTNTLADI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 215 LNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGmarviieeklydeaf 294
Cdd:cd00368 155 ENADLILLWGSNPAETHPVLAARLRRAKKRGAKLIVIDPRRTETAAKADEWLPIRPGTDAALALA--------------- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 295 iktysdmpllvrldngrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeievelkdgrlvrvk 374
Cdd:cd00368 --------------------------------------------------------------------------------
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 375 pvfqllkehlasytpAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNIGKPGAGI 454
Cdd:cd00368 220 ---------------EWAAEITGVPAETIRALAREFAAAKRAVILWGMGLTQHTNGTQNVRAIANLAALTGNIGRPGGGL 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 455 styagqykirfnvkewwFPGsprwlpwlyilhgptpgmkarwpkngikalifgwGNPFDQHNMADRLRQMAikGELEFIA 534
Cdd:cd00368 285 -----------------GPG----------------------------------GNPLVSAPDANRVRAAL--KKLDFVV 311
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731596781 535 GLDFSLTTSCRYSDVVFPAATWYEKTELVTTpLHPYMQLQQPAIKPLYEARSELWMARELAKRL 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 |
6.03e-88 |
|
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: 291.92 E-value: 6.03e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 57 TTCSPNCTLACGIRAMVVDGQIKALLPSNDYPEPEYGP--RGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWE 134
Cdd:cd02770 2 SACTVNCGGRCPLKAHVKDGVITRIETDDTGDDDPGFHqiRACLRGRSQRKRVYNPDRLKYPMKRVGKRGEGKFVRISWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 135 EALDYTAKRLKEIAARYGPESIGFIFQVGGTGHV--QKGAWIALATMVGWSLIHpYD--QNGDLPMFWPQTFGVQTEELE 210
Cdd:cd02770 82 EALDTIASELKRIIEKYGNEAIYVNYGTGTYGGVpaGRGAIARLLNLTGGYLNY-YGtySWAQITTATPYTYGAAASGSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 211 PLEWLNSRYTAIFGSNIMVTRLIDAD---FLIKARNNGTKVVVFDPNYSPTAA-KADEWVQLKPSSDAALALGMARVIIE 286
Cdd:cd02770 161 LDDLKDSKLVVLFGHNPAETRMGGGGstyYYLQAKKAGAKFIVIDPRYTDTAVtLADEWIPIRPGTDAALVAAMAYVMIT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 287 EKLYDEAFIKTYSdmpllVRLDngrrlkADEVkglarPDGLPPyREAFVAYngkllavhpeklelppdVILEGEIEVElk 366
Cdd:cd02770 241 ENLHDQAFLDRYC-----VGFD------AEHL-----PEGAPP-NESYKDY-----------------VLGTGYDGTP-- 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 367 dgrlvrvkpvfqllkehlasYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGN 446
Cdd:cd02770 285 --------------------KTPEWASEITGVPAETIRRLAREIATTKPAAILQGWGPQRHANGEQAARAIMMLAAMTGN 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 447 IGKPGAGISTYAGQYKIRFNvkeWWFPGS-------PRWLPWLYILHGP--TPGMKARWPKNGIKA---LIFGWGNPF-- 512
Cdd:cd02770 345 VGIPGGNTGARPGGSAYNGA---GLPAGKnpvktsiPCFMWTDAIERGEemTADDGGVKGADKLKSnikMIWNYAGNTli 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 513 ----DQHNMADRLRQMAIKgeLEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTT---PLHPYMQLQQPAIKPLYEAR 585
Cdd:cd02770 422 nqhsDDNNTTRALLDDESK--CEFIVVIDNFMTPSARYADILLPDTTELEREDIVLTsnaGMMEYLIYSQKAIEPLYECK 499
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 586 SELWMARELAKRLdpGFAKHFFPELDENTAAEKAVELLLATGGPPvagITLEQL-KKGPVRLKSEVPgnrQIPFYEQVQF 664
Cdd:cd02770 500 SDYEICAELAKRL--GVEDQFTEGKTEQEWLEELYGQTRAKEPGL---PTYEEFrEKGIYRVPRALP---FVAFEDFRED 571
|
650 660 670
....*....|....*....|....*....|
gi 1731596781 665 K--KPFPpvsrpaaieaTAqfvkSGRIEFY 692
Cdd:cd02770 572 PenNPLK----------TP----SGKIEIY 587
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
11-804 |
4.13e-80 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 274.24 E-value: 4.13e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 11 KLSRRQFLK-ASAATAVLAGTAgatryFIPKA-GAENTSPLK-EVKYVRTTCSpNCTLACGIRAMVVDGqiKALLPSNDY 87
Cdd:PRK15488 2 SLSRRDFLKgAGAGCAACALGS-----LLPGAlAANEIAQLKgKTKLTPSICE-MCSTRCPIEARVVNG--KNVFIQGNP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 88 PEPEYGPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEALDYTAKRLKEIAARYGPESIGFIFQVGGTgh 167
Cdd:PRK15488 74 KAKSFGTKVCARGGSGHSLLYDPQRIVKPLKRVGERGEGKWQEISWDEAYQEIAAKLNAIKQQHGPESVAFSSKSGSL-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 168 vqKGAWIALATMVG-------WSLIhPydqnGDLPMFWPQTFGvqtEELEpLEWLNSRYTAIFGSNI-------MVTRLI 233
Cdd:PRK15488 152 --SSHLFHLATAFGspntfthASTC-P----AGYAIAAKVMFG---GKLK-RDLANSKYIINFGHNLyeginmsDTRGLM 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 234 DAdflikARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYDEAFIKTYsdmpllvrldngrrl 313
Cdd:PRK15488 221 TA-----QMEKGAKLVVFEPRFSVVASKADEWHAIRPGTDLAVVLALCHVLIEENLYDKAFVERY--------------- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 314 kadeVKGlarpdglppyreafvayngkllavhpeklelppdvilegeievelkdgrlvrvkpvFQLLKEHLASYTPAYVE 393
Cdd:PRK15488 281 ----TSG--------------------------------------------------------FEELAASVKEYTPEWAE 300
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 394 QETGVPGDTVVRLAREMATTKPlHVIygasnYQWYHG--------DLKgRALALLPVLTGNI--------GKPGAGISTY 457
Cdd:PRK15488 301 AISDVPADDIRRIARELAAAAP-HAI-----VDFGHRatftpeefDMR-RAIFAANVLLGNIerkgglyfGKNASVYNKL 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 458 AGQYKI----RFNVKEWWFPGSPRwlpwlyiLHGPTPGMKARWPKNGIKALIF------------GW----GNPFdqHNM 517
Cdd:PRK15488 374 AGEKVAptlaKPGVKGMPKPTAKR-------IDLVGEQFKYIAAGGGVVQSIIdatltqkpyqikGWvmsrHNPM--QTV 444
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 518 ADRLR-QMAIKgELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVT--TPLHPYMQLQQPAIKPLYEARSELWMAREL 594
Cdd:PRK15488 445 TDRADvVKALK-KLDLVVVCDVYLSESAAYADVVLPESTYLERDEEISdkSGKNPAYALRQRVVEPIGDTKPSWQIFKEL 523
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 595 AKRLDPGfakHFFPELDENTaaekaVELLLATGGPPVagitLEQLKK-GPVRLKseVPGNRQIPFYEQvQFKKPFP---P 670
Cdd:PRK15488 524 GEKMGLG---QYYPWQDMET-----LQLYQVNGDHAL----LKELKKkGYVSFG--VPLLLREPKMVA-KFVARYPnakA 588
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 671 VSRPAAIEATAQF-VKSGRIEFYKDEDAFIALGETLPVHKP--PFEDSEYALnpeIKGKYQfayitrnslyrVHS---TH 744
Cdd:PRK15488 589 VDEDGTYGSQLKFkTPSGKIELFSAKLEALAPGYGVPRYRDvaLKKEDELYF---IQGKVA-----------VHTngaTQ 654
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 745 sNNLWMNELQDNKPkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLgRKIVVF 804
Cdd:PRK15488 655 -NVPLLANLMSDNA-VWIHPQTAGKLGIKNGDEIRLENSVGKEKGKALVTPGI-RPDTLF 711
|
|
| PRK14990 |
PRK14990 |
anaerobic dimethyl sulfoxide reductase subunit A; Provisional |
11-830 |
2.02e-77 |
|
anaerobic dimethyl sulfoxide reductase subunit A; Provisional
Pssm-ID: 184952 [Multi-domain] Cd Length: 814 Bit Score: 268.05 E-value: 2.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 11 KLSRRQFLKASAATAVLAGTAGATRYFIPKAGAENT-SPLKEV-KYVRTTCSPNCTLACGIRAMVVDGQIKALLPSN--- 85
Cdd:PRK14990 13 EVSRRGLVKTTAIGGLAMASSALTLPFSRIAHAVDSaIPTKSDeKVIWSACTVNCGSRCPLRMHVVDGEIKYVETDNtgd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 86 DYPEPEYGPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEALDYTAKRLKEIAARYGPESIGFIFQVGGT 165
Cdd:PRK14990 93 DNYDGLHQVRACLRGRSMRRRVYNPDRLKYPMKRVGARGEGKFERISWEEAYDIIATNMQRLIKEYGNESIYLNYGTGTL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 166 GHVQKGAWIALATMV-------GWSLIHPYD-QNGDLPMFWPQTFGVQTEELEPLEWLNSRYTAIFGSNIMVTRLIDAD- 236
Cdd:PRK14990 173 GGTMTRSWPPGNTLVarlmnccGGYLNHYGDySSAQIAEGLNYTYGGWADGNSPSDIENSKLVVLFGNNPGETRMSGGGv 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 237 --FLIKAR-NNGTKVVVFDPNYSPT-AAKADEWVQLKPSSDAALALGMARVIIEEKLYDEAFIKTYSdmpllvrldngrr 312
Cdd:PRK14990 253 tyYLEQARqKSNARMIIIDPRYTDTgAGREDEWIPIRPGTDAALVNGLAYVMITENLVDQPFLDKYC------------- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 313 lkadevkglarpdglppyreafVAYNGKLL-AVHPEKLELPPDVILEGeievelKDGrlvrvkpvfqllkehlASYTPAY 391
Cdd:PRK14990 320 ----------------------VGYDEKTLpASAPKNGHYKAYILGEG------PDG----------------VAKTPEW 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 392 VEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNIGKPGAGISTYAGQYKI---RFNVK 468
Cdd:PRK14990 356 ASQITGVPADKIIKLAREIGSTKPAFISQGWGPQRHANGEIATRAISMLAILTGNVGINGGNSGAREGSYSLpfvRMPTL 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 469 EWWFPGSPRWLPWL-YILHGPTpgMKARwpKNGIKA---------LIFGW-GNPF-DQHNMADRLRQ-MAIKGELEFIAG 535
Cdd:PRK14990 436 ENPIQTSISMFMWTdAIERGPE--MTAL--RDGVRGkdkldvpikMIWNYaGNCLiNQHSEINRTHEiLQDDKKCELIVV 511
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 536 LDFSLTTSCRYSDVVFPAATWYEKTEL---VTTPLHPYMQLQQPAIKPLYEARSELWMARELAKRLdpGFAKHFfpelDE 612
Cdd:PRK14990 512 IDCHMTSSAKYADILLPDCTASEQMDFaldASCGNMSYVIFNDQVIKPRFECKTIYEMTSELAKRL--GVEQQF----TE 585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 613 NTAAEKAVELLLATGGPPVAGI-TLEQLKKGPVrLKSEVPGNRQIPfYEQVQFKKPFPPVSRPaaieataqfvkSGRIEF 691
Cdd:PRK14990 586 GRTQEEWMRHLYAQSREAIPELpTFEEFRKQGI-FKKRDPQGHHVA-YKAFREDPQANPLTTP-----------SGKIEI 652
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 692 YKDEDAFIALG---------ETLPVHKPPFEDseyaLNPEIKGKYQFAYITRNSLYRVHSTHSNnlwMNELQDN-KPKVF 761
Cdd:PRK14990 653 YSQALADIAATwelpegdviDPLPIYTPGFES----YQDPLNKQYPLQLTGFHYKSRVHSTYGN---VDVLKAAcRQEMW 725
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 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 |
7.52e-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: 7.52e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 53 KYVRTTCSPNCTLACGIRAMVVDGQIKALLPSNDYPE-----PEYGPRGCLRGLSFINLIYGPDRIKKPLIR-------- 119
Cdd:COG5013 47 KVVRSTHGVNCTGSCSWKVYVKDGIITWETQQTDYPRtgpdlPNYEPRGCPRGASFSWYTYSPTRVKYPYVRgvllelwr 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 120 --------------------------TGERGAGEFREVSWEEALD-------YTAKRlkeiaarYGPESI-GF------- 158
Cdd:COG5013 127 eararhgdpveawasivedpekrrryKSARGKGGFVRATWDEANEiiaaanvYTIKK-------YGPDRVaGFspipams 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 159 -IFQVGGTGHVQkgawialatMVGWSLIHPYDQNGDLPMFWPQTFGVQTEELEPLEWLNSRYTAIFGSNIMVTRLIDADF 237
Cdd:COG5013 200 mVSYAAGARFLS---------LIGGVMLSFYDWYADLPPASPQVWGEQTDVPESADWYNSGYLIMWGSNVPQTRTPDAHF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 238 LIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYD---EAFI---KTYSDMPLLVRLDN-- 309
Cdd:COG5013 271 MTEARYKGTKVVVVSPDYAENTKFADEWLPPKQGTDAALAMAMGHVILKEFHVDrqvPYFTdyaRRYTDLPFLVTLEErd 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 310 -----GRRLKADEVKGLARPDGLPPYR--------EAFVAYNGKL--------------------LAVHP---------- 346
Cdd:COG5013 351 ggyvpGRFLRASDLGGALGESNNPEWKtvvldeatGEPVVPNGSIgfrwgesegkwnlelkdatgADVDPalsllddhde 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 347 -EKLELP--------PDVILEG--EIEVELKDGRlVRVKPVFQLLKEHL-----------------ASYTPAYVEQETGV 398
Cdd:COG5013 431 vVEVAFPyfggetggGGVLRRGvpVRRVTLADGE-VLVTTVFDLMLANYgvdrglpgnwptgydddVPYTPAWQEKITGV 509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 399 PGDTVVRLAREMATT------KPLhVIYGASNYQWYHGDLKGRALALLPVLTGNIGKPGAGISTYAGQYKIR-------- 464
Cdd:COG5013 510 PREQVIRVAREFAQNaektrgRSM-IIMGAGTNHWYHSDMIYRAILNLLMLCGCQGVNGGGWAHYVGQEKLRpqtgwqpl 588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 465 --------------------FNVKEW-------------WFPGSPR---------------WLPwlyilHGPT------- 489
Cdd:COG5013 589 afaldwsrpprqmngtsffyAHTDQWryetlsadellspLADGKFWgghladynvraarlgWLP-----SYPQfnrnpld 663
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 490 -------------------------------PGMKARWPKNgikalIFGW----------GNPF--------DQHNMADR 520
Cdd:COG5013 664 ladeaeaagmepadyvvdqlksgelkfacedPDNPENFPRN-----LFVWrsnllgssgkGHEYflkhllgtDNGVQGEE 738
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 521 L-----------RQMAIKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIKPLYEARSELW 589
Cdd:COG5013 739 LgpglrprevvwRDEAPEGKLDLLVTLDFRMTSTCLYSDIVLPAATWYEKHDLSTTDMHPFIHPFSPAVDPPWEARSDWD 818
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 590 MARELAKRLDPGFAKHFFPELD-------ENTAAEKA-----VELLLATGGPPVAGITLEQL-----------KK----G 642
Cdd:COG5013 819 IFKGIAKKFSELAAGHLGVRKDvvatplqHDTPGELAqpfgdVKDWKKGECEPIPGKTMPKLvvverdypaiyEKftslG 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 643 PvrLKSEVP-GNRQIPFY--EQVQF--------KKPFPPVSRPA------AIEA-------------------------- 679
Cdd:COG5013 899 P--LLEKLGnGGKGITWDteEEVEElgklngvvREEGVAKGRPRldtdidAAEAilalspetnghvavkawkalekrtgr 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 680 -------------------TAQFVK---------------------------------SGRIEFYKDEDAFIALGETLPV 707
Cdd:COG5013 977 dlahlaagreeekirfrdiQAQPRKvitsptwsgsesggrrysafttnveelipwrtlTGRQHFYLDHDWMREFGEGLPV 1056
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 708 HKPPFEDSEYALNPEIK--GKYQFA--YITRNSLYRVHSTHSNNLWMNELQDNKPKVFLNPQDAAAKGIKEGDLVEVYND 783
Cdd:COG5013 1057 YRPPLDMKTLFGEPGIGpnGNPEIVlrYLTPHQKWGIHSTYQDNLLMLTLSRGGPTVWMSEEDAAKIGIKDNDWIEAFNR 1136
|
....
gi 1731596781 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 |
9.07e-77 |
|
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: 261.39 E-value: 9.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 61 PNCTLACGIRAMVVDGQIKALLPsndypEPEYGPRGCLRGLSFINLIYGPDRIKKPLIRTGE----------RGAGEFRE 130
Cdd:cd02751 1 PTACHWGPFKAHVKDGVIVRVEP-----DDTDQPRPCPRGRSVRDRVYSPDRIKYPMKRVGWlgngpgsrelRGEGEFVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 131 VSWEEALDYTAKRLKEIAARYGPESIgFI-----FQVGGTGHVQKGAWIALATMVGWSLIHPYDQNGDLPMFWPQTFGVQ 205
Cdd:cd02751 76 ISWDEALDLVASELKRIREKYGNEAI-FGgsygwASAGRLHHAQSLLHRFLNLIGGYLGSYGTYSTGAAQVILPHVVGSD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 206 TEELEPLEWL----NSRYTAIFGSNIMVTRLIDA--------DFLIKARNNGTKVVVFDPNYSPTAA-KADEWVQLKPSS 272
Cdd:cd02751 155 EVYEQGTSWDdiaeHSDLVVLFGANPLKTRQGGGggpdhgsyYYLKQAKDAGVRFICIDPRYTDTAAvLAAEWIPIRPGT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 273 DAALALGMARVIIEEKLYDEAFIKTYSDmpllvrldngrrlkadevkglarpdGLppyrEAFVAYngkllavhpeklelp 352
Cdd:cd02751 235 DVALMLAMAHTLITEDLHDQAFLARYTV-------------------------GF----DEFKDY--------------- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 353 pdviLEGEievelKDGRlvrVKpvfqllkehlasyTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQwYHGDL 432
Cdd:cd02751 271 ----LLGE-----SDGV---PK-------------TPEWAAEITGVPAETIRALAREIASKRTMIAQGWGLQRA-HHGEQ 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 433 KGRALALLPVLTGNIGKPGAGISTYAGQYKirfNVKEWWFPGSPRWLPWLY---------------ILHGPTP----GMK 493
Cdd:cd02751 325 PAWMLVTLAAMLGQIGLPGGGFGFGYGYSN---GGGPPRGGAGGPGLPQGKnpvkdsipvariadaLLNPGKEftanGKL 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 494 ARWPKngIKALIFGWGNPFdqHNMADRLRQMAIKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPL--HPYM 571
Cdd:cd02751 402 KTYPD--IKMIYWAGGNPL--HHHQDLNRLIKALRKDETIVVHDIFWTASARYADIVLPATTSLERNDIGLTGNysNRYL 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 572 QLQQPAIKPLYEARSELWMARELAKRLdpGFAKHFFPELDE----NTAAEKAVElllATGGPPVAGITLEQL-KKGPVRL 646
Cdd:cd02751 478 IAMKQAVEPLGEARSDYEIFAELAKRL--GVEEEFTEGRDEmewlEHLYEETRA---KAAGPGPELPSFEEFwEKGIVRV 552
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 1731596781 647 KSevPGNRQIPFYEQVQFKKPFpPVSRPaaieataqfvkSGRIEFY 692
Cdd:cd02751 553 PA--APKPFVAFADFREDPEAN-PLGTP-----------SGKIEIY 584
|
|
| MopB_Acetylene-hydratase |
cd02759 |
The MopB_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related proteins. ... |
57-631 |
2.37e-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: 245.68 E-value: 2.37e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 57 TTCSPNCTLACGIRAMVVDGQIKALLPSNDYPEPeyGPRGCLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWEEA 136
Cdd:cd02759 1 KGTCPGCHSGCGVLVYVKDGKLVKVEGDPNHPTN--KGRLCMRGLAAPEIVYHPDRLLYPLKRVGERGENKWERISWDEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 137 LDYTAKRLKEIAARYGPESIGFIFqvgGTGHvqkGAWIALaTMVGWSLIHPYDQ-NGDLPMF---WPQTFGVQTEELEPL 212
Cdd:cd02759 79 LDEIAEKLAEIKAEYGPESIATAV---GTGR---GTMWQD-SLFWIRFVRLFGSpNLFLSGEscyWPRDMAHALTTGFGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 213 -----EWLNSRYTAIFGSNIMVTrliDADF----LIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARV 283
Cdd:cd02759 152 gydepDWENPECIVLWGKNPLNS---NLDLqghwLVAAMKRGAKLIVVDPRLTWLAARADLWLPIRPGTDAALALGMLNV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 284 IIEEKLYDEAFIKTYSdmpllvrldNGrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeiev 363
Cdd:cd02759 229 IINEGLYDKDFVENWC---------YG----------------------------------------------------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 364 elkdgrlvrvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKP-LHVIYGASNYQwYHGDLKGRALALLPV 442
Cdd:cd02759 247 -------------FEELAERVQEYTPEKVAEITGVPAEKIRKAARLYATAKPaCIQWGLAIDQQ-KNGTQTSRAIAILRA 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 443 LTGNIGKPGAGIstyagqykirfnvkewWFPgsprwlpwlyilhgptpgmkarWPkngIKALIFGWGNPFDQHNMADRLR 522
Cdd:cd02759 313 ITGNLDVPGGNL----------------LIP----------------------YP---VKMLIVFGTNPLASYADTAPVL 351
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 523 QmAIKgELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLH-PYMQLQQPAIKPLYEARSELWMARELAKRLDPG 601
Cdd:cd02759 352 E-ALK-ALDFIVVVDLFMTPTAMLADIVLPVAMSLERPGLRGGFEAeNFVQLRQKAVEPYGEAKSDYEIVLELGKRLGPE 429
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1731596781 602 FAKHF---FPELDE------NTAA---EKAVELLLATGGPPV 631
Cdd:cd02759 430 EAEYYkyeKGLLRPdgqpgfNTPTgkvELYSTMLEELGYDPL 471
|
|
| Fdh-alpha |
TIGR01591 |
formate dehydrogenase, alpha subunit, archaeal-type; This model describes a subset of formate ... |
57-785 |
6.71e-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: 249.69 E-value: 6.71e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 57 TTCsPNCTLACGIRAMVVDGQIKALLPSNDYPePEYGpRGCLRGLSFINLIYGPDRIKKPLIRTGergaGEFREVSWEEA 136
Cdd:TIGR01591 1 TVC-PYCGVGCSLNLVVKDGKIVRVEPYQGHK-ANRG-HLCVKGYFAWEFINSKDRLTTPLIREG----DKFREVSWDEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 137 LDYTAKRLKEIAARYGPESIGFIFQVGGTGH----VQKGAWIALATmvgwsliHPYDQ-----NGDLPMFWPQTFGVQTE 207
Cdd:TIGR01591 74 ISYIAEKLKEIKEKYGPDSIGFIGSSRGTNEenylLQKLARAVIGT-------NNVDNcarvcHGPSVAGLKQTVGIGAM 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 208 ELEPLEWLNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEE 287
Cdd:TIGR01591 147 SNTISEIENADLIVIIGYNPAESHPVVAQYLKNAKRNGAKIIVIDPRKTETAKIADLHIPLKPGTDIALLNAMANVIIEE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 288 KLYDEAFIKTysdmpllvRLDNgrrlkadevkglarpdglppyreafvayngkllavhpeklelppdvilegeievelkd 367
Cdd:TIGR01591 227 GLYDKAFIEK--------RTEG---------------------------------------------------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 368 grlvrvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNI 447
Cdd:TIGR01591 241 ---------FEEFREIVKGYTPEYVEDITGVPADLIREAARMYAKAGSAAILWGMGVTQHSQGVETVMALINLAMLTGNI 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 448 GKPGAGISTYAGQ-------YKIRFNV------------------KEWWFPGSPRwLPWLYIlhgptPGMKARWPKNGIK 502
Cdd:TIGR01591 312 GKPGGGVNPLRGQnnvqgacDMGALPDflpgyqpvsdeevrekfaKAWGVVKLPA-EPGLRI-----PEMIDAAADGDVK 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 503 ALIFGWGNPFdqhnMADRLRQMAIKG--ELEFIAGLDFSLTTSCRYSDVVFPAATWYEKtELVTTPLHPYMQLQQPAIKP 580
Cdd:TIGR01591 386 ALYIMGEDPL----QSDPNTSKVRKAleKLELLVVQDIFMTETAKYADVVLPAAAWLEK-EGTFTNAERRIQRFFKAVEP 460
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 581 LYEARSELWMARELAKRLDpgfakhffpeLDENTAAEKAVELLLATGGPPVAGITLEQLkkgpvrlksEVPGNRQIPfye 660
Cdd:TIGR01591 461 KGESKPDWEIIQELANALG----------LDWNYNHPQEIMDEIRELTPLFAGLTYERL---------DELGSLQWP--- 518
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 661 qvqfkkPFPPVSRPAAIEATAQFV-KSGRIEFYKDEdafialgETLPVHKPPfEDSEYALNpeiKGKYQFAYITRNSLYR 739
Cdd:TIGR01591 519 ------CNDSDASPTSYLYKDKFAtPDGKAKFIPLE-------WVAPIEEPD-DEYPLILT---TGRVLTHYNVGEMTRR 581
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1731596781 740 VHSthsnnlWMNELQDnkPKVFLNPQDAAAKGIKEGDLVEVYNDRG 785
Cdd:TIGR01591 582 VAG------LRRLSPE--PYVEINTEDAKKLGIKDGDLVKVKSRRG 619
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
56-641 |
8.45e-72 |
|
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: 245.20 E-value: 8.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 56 RTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPepeyGPRG--CLRGLSFINLIYGPDRIKKPLIRTGergaGEFREVSW 133
Cdd:cd02753 1 KTVC-PYCGVGCGLELWVKDNKIVGVEPVKGHP----VNRGklCVKGRFGFDFVNSKDRLTKPLIRKN----GKFVEASW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 134 EEALDYTAKRLKEIAARYGPESIGFI------------FQ-----VGGTGHVQKGAWI-------ALATMVGwslihpyd 189
Cdd:cd02753 72 DEALSLVASRLKEIKDKYGPDAIAFFgsakctneenylFQklaraVGGTNNVDHCARLchsptvaGLAETLG-------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 190 qngdlpmfwpqtFGVQTEELEPLEwlNSRYTAIFGSNIMVTRLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLK 269
Cdd:cd02753 144 ------------SGAMTNSIADIE--EADVILVIGSNTTEAHPVIARRIKRAKRNGAKLIVADPRRTELARFADLHLQLR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 270 PSSDAALALGMARVIIEEKLYDEAFIKtysdmpllvrldngrrlkadevkglARPDGlppyreafvayngkllavhpekl 349
Cdd:cd02753 210 PGTDVALLNAMAHVIIEEGLYDEEFIE-------------------------ERTEG----------------------- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 350 elppdvilegeievelkdgrlvrvkpvFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYH 429
Cdd:cd02753 242 ---------------------------FEELKEIVEKYTPEYAERITGVPAEDIREAARMYATAKSAAILWGMGVTQHSH 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 430 GDLKGRALALLPVLTGNIGKPGAGISTYAGQYkirfNVKewwfpGS------PRWLPwlyilhgptpgmkarwpkNGIKA 503
Cdd:cd02753 295 GTDNVMALSNLALLTGNIGRPGTGVNPLRGQN----NVQ-----GAcdmgalPNVLP------------------GYVKA 347
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 504 L-IFGwGNPF----DQHNMADRLRQmaikgeLEFIAGLDFSLTTSCRYSDVVFPAATWYEKtELVTTPLHPYMQLQQPAI 578
Cdd:cd02753 348 LyIMG-ENPAlsdpNTNHVRKALES------LEFLVVQDIFLTETAELADVVLPAASFAEK-DGTFTNTERRVQRVRKAV 419
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731596781 579 KPLYEARSELWMARELAKRL-DPGFAKHffPE--LDEntaaekavellLATGGPPVAGITLEQLKK 641
Cdd:cd02753 420 EPPGEARPDWEIIQELANRLgYPGFYSH--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 |
1.40e-63 |
|
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: 224.03 E-value: 1.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 56 RTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPepeyGPRG--CLRGLSFINLIYGPDRIKKPLIRTGErgaGEFREVSW 133
Cdd:cd02754 1 KTTC-PYCGVGCGVEIGVKDGKVVAVRGDPEHP----VNRGrlCIKGLNLHKTLNGPERLTRPLLRRNG---GELVPVSW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 134 EEALDYTAKRLKEIAARYGPESIGFIfqVGGT---------GHVQKGAwialatmVGwslIHPYDQNGDLPMF-----WP 199
Cdd:cd02754 73 DEALDLIAERFKAIQAEYGPDSVAFY--GSGQllteeyyaaNKLAKGG-------LG---TNNIDTNSRLCMAsavagYK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 200 QTFG--VQTEELEPLEwlNSRYTAIFGSN------IMVTRLIDAdfliKARNNGTKVVVFDPNYSPTAAKADEWVQLKPS 271
Cdd:cd02754 141 RSFGadGPPGSYDDIE--HADCFFLIGSNmaechpILFRRLLDR----KKANPGAKIIVVDPRRTRTADIADLHLPIRPG 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 272 SDAALALGMARVIIEEKLYDEAFIKTYSdmpllvrldngrrlkadevkglarpdglppyreafvayngkllavhpeklel 351
Cdd:cd02754 215 TDLALLNGLLHVLIEEGLIDRDFIDAHT---------------------------------------------------- 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 352 ppdvilEGEIEvelkdgrlvrvkpvfqlLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGD 431
Cdd:cd02754 243 ------EGFEE-----------------LKAFVADYTPEKVAEITGVPEADIREAARLFGEARKVMSLWTMGVNQSTQGT 299
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 432 LKGRALALLPVLTGNIGKPGAGISTYAGQ------------------YKI------RFNVKEWWfpGSPrwlpwlYILHG 487
Cdd:cd02754 300 AANNAIINLHLATGKIGRPGSGPFSLTGQpnamggrevgglanllpgHRSvnnpehRAEVAKFW--GVP------EGTIP 371
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 488 PTPGMKA----RWPKNG-IKALIFGWGNPFdqHNMADRLRQMAIKGELEFIAGLD-FSLTTSCRYSDVVFPAATWYEKTE 561
Cdd:cd02754 372 PKPGLHAvemfEAIEDGeIKALWVMCTNPA--VSLPNANRVREALERLEFVVVQDaFADTETAEYADLVLPAASWGEKEG 449
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 562 LVT----TplhpyMQLQQPAIKPLYEARSELWMARELAKRLDpgfakhFFPELDENTAAEKAVELLLATGGPP--VAGIT 635
Cdd:cd02754 450 TMTnserR-----VSLLRAAVEPPGEARPDWWILADVARRLG------FGELFPYTSPEEVFEEYRRLSRGRGadLSGLS 518
|
650
....*....|
gi 1731596781 636 LEQLKKGPVR 645
Cdd:cd02754 519 YERLRDGGVQ 528
|
|
| MopB_CT_4 |
cd02785 |
The MopB_CT_4 CD includes a group of related uncharacterized bacterial and archaeal ... |
726-855 |
1.36e-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: 1.36e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 726 KYQFAYITRNSLYRVHSTHSNNLWMNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFE 805
Cdd:cd02785 1 KYPLACIQRHSRFRVHSQFSNVPWLLELQPE-PRVKINPIDAAARGIAHGDLVEVYNDRGSVVCKAKVDDGIQPGVVTAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1731596781 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 |
1.68e-57 |
|
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: 206.14 E-value: 1.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 55 VRTTCSpNCTLACGIRAMVVDGQIKALLPSNDYPepeyGPRG--CLRGLSFINLIYGPDRIKKPLIRTGERGA----GEF 128
Cdd:cd02757 2 VPSTCQ-GCTAWCGLQAYVEDGRVTKVEGNPLHP----GSRGrlCAKGHLGLQQVYDPDRILYPMKRTNPRKGrdvdPKF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 129 REVSWEEALDYTAKRLkeIAARYGPESIGFIFQVGGTGHVQKGAWIALATMVG-------WSLIHPYDQNGdlPMFWPQT 201
Cdd:cd02757 77 VPISWDEALDTIADKI--RALRKENEPHKIMLHRGRYGHNNSILYGRFTKMIGspnnishSSVCAESEKFG--RYYTEGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 202 FGVQTEELEplewlNSRYTAIFGSNIMVT--RLIDADFLIKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALG 279
Cdd:cd02757 153 WDYNSYDYA-----NAKYILFFGADPLESnrQNPHAQRIWGGKMDQAKVVVVDPRLSNTAAKADEWLPIKPGEDGALALA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 280 MARVIIEEKLYDEAFIKTYSDMPllVRLDNGRRLKADEVKglarpdglPPYREAFVAYngkllavhpeklelppdvileg 359
Cdd:cd02757 228 IAHVILTEGLWDKDFVGDFVDGK--NYFKAGETVDEESFK--------EKSTEGLVKW---------------------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 360 eievelkdgrlvrvkpvfqlLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKP---LHVIYGAS--NYQWYhgdlKG 434
Cdd:cd02757 276 --------------------WNLELKDYTPEWAAKISGIPAETIERVAREFATAAPaaaAFTWRGATmqNRGSY----NS 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 435 RALALLPVLTGNIGKPGaGISTYAGQYKI-----RFNVKEWWFPGSPRWlpwlyilhgptpgmkarwpkngIKALifgwg 509
Cdd:cd02757 332 MACHALNGLVGSIDSKG-GLCPNMGVPKIkvyftYLDNPVFSNPDGMSW----------------------EEAL----- 383
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 510 npfdqhnmadrlrqmaikGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTP--LHPYMQLQQPAIKPLYEARSE 587
Cdd:cd02757 384 ------------------AKIPFHVHLSPFMSETTYFADIVLPDGHHFERWDVMSQEnnLHPWLSIRQPVVKSLGEVREE 445
|
570 580 590
....*....|....*....|....*....|....*....
gi 1731596781 588 LWMARELAKRLDP----GFAKHFF-----PELDENTAAE 617
Cdd:cd02757 446 TEILIELAKKLDPkgsdGMKRYAPgqfkdPETGKNNRWE 484
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
112-597 |
3.19e-44 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 163.73 E-value: 3.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 112 RIKKPLIRtgeRGAGEFREVSWEEALDYTAKRLKEIAARYGPESIGFIFQVGGTGHVqkGAWIALATM---VGWSLIHPY 188
Cdd:pfam00384 1 RLKYPMVR---RGDGKFVRVSWDEALDLIAKKLKRIIKKYGPDAIAINGGSGGLTDV--ESLYALKKLlnrLGSKNGNTE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 189 DQNGDLPMFWPQTFG-------VQTEELEPLEwlNSRYTAIFGSNIMVTRLIDADFLIKA-RNNGTKVVVFDPNYSPTaa 260
Cdd:pfam00384 76 DHNGDLCTAAAAAFGsdlrsnyLFNSSIADIE--NADLILLIGTNPREEAPILNARIRKAaLKGKAKVIVIGPRLDLT-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 261 KADEWVQLKPSSDAALALGMARVIIEEKLYDEAFiktysdmpllvrldngrrlkadevkglarpdglppyreafvayngk 340
Cdd:pfam00384 152 YADEHLGIKPGTDLALALAGAHVFIKELKKDKDF---------------------------------------------- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 341 llavhpeklelppdvilegeievelkdgrlvrvkpvfqllkehlasytpayveqetgvpgdtvvrlaremaTTKPLhVIY 420
Cdd:pfam00384 186 -----------------------------------------------------------------------APKPI-IIV 193
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 421 GASNYQWYHGDLKGRALALLPVLTGNIGKPGAG------ISTYA---GQYKIRFnvkewwFPGsprwlpwlyilhGPTPG 491
Cdd:pfam00384 194 GAGVLQRQDGEAIFRAIANLADLTGNIGRPGGGwnglniLQGAAspvGALDLGL------VPG------------IKSVE 255
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 492 MKARWPKNGIKALIFGWGNPFDQHnmADRLRQMAIKGELEFIAGLDFSL-TTSCRYSDVVFPAATWYEKTELVTTPLHPy 570
Cdd:pfam00384 256 MINAIKKGGIKVLYLLGNNPFVTH--ADENRVVKALQKLDLFVVYDGHHgDKTAKYADVILPAAAYTEKNGTYVNTEGR- 332
|
490 500
....*....|....*....|....*..
gi 1731596781 571 MQLQQPAIKPLYEARSELWMARELAKR 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 |
4.55e-44 |
|
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: 168.98 E-value: 4.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 69 IRAMVVDGQIKALLP--SNDYPEPeygprgclRGLSFINLIYGPDRIKKPLIR-----------TGERGAGEFREVSWEE 135
Cdd:cd02769 9 FRARVKDGRIVGVRPfeEDPDPSP--------LLDGVPDAVYSPTRIKYPMVRrgwlekgpgsdRSLRGKEEFVRVSWDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 136 ALDYTAKRLKEIAARYGPESI-----GFiFQVGGTGHVQKGAWIALATMVGW-SLIHPYdQNGDLPMFWPQTFGvqteel 209
Cdd:cd02769 81 ALDLVAAELKRVRKTYGNEAIfggsyGW-SSAGRFHHAQSLLHRFLNLAGGYvGSVGDY-STGAAQVILPHVVG------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 210 ePLEWLNSRYTA------------IFGSNIMVTRLIDA---------DFLIKARNNGTKVVVFDPNYSPTAAKAD-EWVQ 267
Cdd:cd02769 153 -SMEVYTEQQTSwpviaehtelvvAFGADPLKNAQIAWggipdhqaySYLKALKDRGIRFISISPLRDDTAAELGaEWIA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 268 LKPSSDAALALGMARVIIEEKLYDEAFIKTYSDmpllvrldngrrlkadevkGLARpdglppyreaFVAYngkllavhpe 347
Cdd:cd02769 232 IRPGTDVALMLALAHTLVTEGLHDKAFLARYTV-------------------GFDK----------FLPY---------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 348 klelppdviLEGEievelKDGrlvrvkpvfqllkehlASYTPAYVEQETGVPGDTVVRLAREMATTKPLhVIYGASNYQW 427
Cdd:cd02769 273 ---------LLGE-----SDG----------------VPKTPEWAAAICGIPAETIRELARRFASKRTM-IMAGWSLQRA 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 428 YHGDLKGRALALLPVLTGNIGKPGAGIST---YAGQYKIRFNvkewwfPGSPRWLPWLY---------------ILHGPT 489
Cdd:cd02769 322 HHGEQPHWMAVTLAAMLGQIGLPGGGFGFgyhYSNGGGPPRG------AAPPPALPQGRnpvssfipvariadmLLNPGK 395
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 490 P----GMKARWPKngIKALIFGWGNPFDQHNMADRLRQMAIKGELeFIAGlDFSLTTSCRYSDVVFPAATWYEKTELVTT 565
Cdd:cd02769 396 PfdynGKKLTYPD--IKLVYWAGGNPFHHHQDLNRLIRAWQKPET-VIVH-EPFWTATARHADIVLPATTSLERNDIGGS 471
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1731596781 566 PLHPYMQLQQPAIKPLYEARSELWMARELAKRLdpGFAKHF 606
Cdd:cd02769 472 GDNRYIVAMKQVVEPVGEARDDYDIFADLAERL--GVEEQF 510
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
57-629 |
6.32e-42 |
|
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: 161.41 E-value: 6.32e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 57 TTCsPNCTLACGIRAMVVDGQIKALLPSNDYPepeyGPRG--CLRGLSFINLIYGPDRIKKPLIRTGergaGEFREVSWE 134
Cdd:cd02762 2 RAC-ILCEANCGLVVTVEDGRVASIRGDPDDP----LSKGyiCPKAAALGDYQNDPDRLRTPMRRRG----GSFEEIDWD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 135 EALDYTAKRLKEIAARYGPESIGFiFQVGGTGHVQKGAwIALATMVGWSLIHPYDQNG---DLP-MFWP-QTFGVQ---- 205
Cdd:cd02762 73 EAFDEIAERLRAIRARHGGDAVGV-YGGNPQAHTHAGG-AYSPALLKALGTSNYFSAAtadQKPgHFWSgLMFGHPglhp 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 206 TEELEplewlNSRYTAIFGSNIMVTR-----LIDADFLIKA-RNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALG 279
Cdd:cd02762 151 VPDID-----RTDYLLILGANPLQSNgslrtAPDRVLRLKAaKDRGGSLVVIDPRRTETAKLADEHLFVRPGTDAWLLAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 280 MARVIIEEKLYDEAFIktysdmpllvrldngrrlkADEVKGLARpdglppyreafvayngkllavhpeklelppdvileg 359
Cdd:cd02762 226 MLAVLLAEGLTDRRFL-------------------AEHCDGLDE------------------------------------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 360 eievelkdgrlvrvkpvfqlLKEHLASYTPAYVEQETGVPGDTVVRLAREMATTKPLhVIY---GASnyQWYHGDLKGRA 436
Cdd:cd02762 251 --------------------VRAALAEFTPEAYAPRCGVPAETIRRLAREFAAAPSA-AVYgrlGVQ--TQLFGTLCSWL 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 437 LALLPVLTGNIGKPGAGIST-----YAGQYKIR-FNVKEWWFPGSPrwlpwLYILHGPTPG------MKARWPKNgIKAL 504
Cdd:cd02762 308 VKLLNLLTGNLDRPGGAMFTtpaldLVGQTSGRtIGRGEWRSRVSG-----LPEIAGELPVnvlaeeILTDGPGR-IRAM 381
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 505 IFGWGNPFdqHNMADRLRQMAIKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELvtTPLHP-----YMQLQQPAIK 579
Cdd:cd02762 382 IVVAGNPV--LSAPDGARLEAALGGLEFMVSVDVYMTETTRHADYILPPASQLEKPHA--TFFNLefprnAFRYRRPLFP 457
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1731596781 580 PLYEARSELWMARELAKRLDPGFAKHFFpelDENTAAEKAVELLLATGGP 629
Cdd:cd02762 458 PPPGTLPEWEILARLVEALDAVLRAGFY---GERAGGTLLLAALLERPSG 504
|
|
| PRK15102 |
PRK15102 |
trimethylamine-N-oxide reductase TorA; |
12-822 |
8.07e-42 |
|
trimethylamine-N-oxide reductase TorA;
Pssm-ID: 237909 [Multi-domain] Cd Length: 825 Bit Score: 164.84 E-value: 8.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 12 LSRRQFLKASAATAvlAGTAGATRYFIP-KAGAENTSPLKEVKYVRTTCSPnctlACGIRAMVVDGQIKALLP--SNDYP 88
Cdd:PRK15102 1 ASRRRFLKGLGGLS--AAGMLGPSLLTPrSALAAQAAAAETTKEWILTGSH----WGAFRAKVKNGRFVEAKPfeLDKYP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 89 EPeygprgCLRGLSfiNLIYGPDRIKKPLIR-----------TGERGAGEFREVSWEEALDYTAKRLKEIAARYGPESIg 157
Cdd:PRK15102 75 TK------MINGIK--GHVYNPSRIRYPMVRldwlrkrhksdTSQRGDNRFVRVSWDEALDLFYEELERVQKTYGPSAL- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 158 FIFQVG---------GTGHVQK-----------------GA------WIALATMV-----GWSLIHpydQNGDLPMFWP- 199
Cdd:PRK15102 146 HTGQTGwqstgqfhsATGHMQRaigmhgnsvgtvgdystGAgqvilpYVLGSTEVyeqgtSWPLIL---ENSKTIVLWGs 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 200 -----QTFGVQTEELEPLEWLnsrytaifgsnimvtrlidADFLIKARNNGTKVVVFDPNYSPTAAKAD-EWVQLKPSSD 273
Cdd:PRK15102 223 dpvknLQVGWNCETHESYAYL-------------------AQLKEKVAKGEINVISIDPVVTKTQNYLGcEHLYVNPQTD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 274 AALALGMARVIIEEKLYDEAFIKTYSdmpllvrldngrrLKADEvkglarpdglppyreaFVAYngkllavhpeklelpp 353
Cdd:PRK15102 284 VPLMLALAHTLYSENLYDKKFIDNYC-------------LGFEQ----------------FLPY---------------- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 354 dviLEGEievelKDGrlvrvkpvfqllkehlASYTPAYVEQETGVPGDTVVRLAREMATTKPlHVIYGASNYQWYHGDLK 433
Cdd:PRK15102 319 ---LLGE-----KDG----------------VPKTPEWAEKICGIDAETIRELARQMAKGRT-QIIAGWCIQRQQHGEQP 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 434 GRALALLPVLTGNIGKPGAGIStYAGQY------------------------KIRFNVKEwwFPGSPRWLP---WL-YIL 485
Cdd:PRK15102 374 YWMGAVLAAMLGQIGLPGGGIS-YGHHYsgigvpssggaipggfpgnldtgqKPKHDNSD--YKGYSSTIPvarFIdAIL 450
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 486 HgptPGMKARWpkNG-------IKALIFGWGNPFDQHNMADRLRQMAIKgeLEFIAGLDFSLTTSCRYSDVVFPAATWYE 558
Cdd:PRK15102 451 E---PGKTINW--NGkkvtlppLKMMIFSGTNPWHRHQDRNRMKEAFRK--LETVVAIDNQWTATCRFADIVLPACTQFE 523
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 559 KTELVTTPLHP---YMQLQQpAIKPLYEARSELWMARELAKRLdpGFAKHFFPELDENTAAEKAVELLLATGGPPVAGIT 635
Cdd:PRK15102 524 RNDIDQYGSYSnrgIIAMKK-VVEPLFESRSDFDIFRELCRRF--GREKEYTRGMDEMGWLKRLYQECKQQNKGKFHMPE 600
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 636 LEQL-KKGPVRLKSEVPGNRQIPFYEQVQFKkpfpPVSRPaaieataqfvkSGRIEFYKDEDAfiALG-ETLPVHKPPFE 713
Cdd:PRK15102 601 FDEFwKKGYVEFGEGQPWVRHADFREDPELN----PLGTP-----------SGLIEIYSRKIA--DMGyDDCQGHPMWFE 663
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 714 DSEYALNPEIKGKYQFAYITRNSLYRVHSTHSNNLWMNE---LQDNKPkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGY 790
Cdd:PRK15102 664 KIERSHGGPGSDKYPLWLQSVHPDKRLHSQLCESEELREtytVQGREP-VYINPQDAKARGIKDGDVVRVFNDRGQVLAG 742
|
890 900 910 920
....*....|....*....|....*....|....*....|.
gi 1731596781 791 AALDPGLGRKIVVFEQG-WWSRYLNG-----DSY---NSLT 822
Cdd:PRK15102 743 AVVSDRYPPGVIRIHEGaWYGPDKGGeigalCTYgdpNTLT 783
|
|
| MopB_Phenylacetyl-CoA-OR |
cd02760 |
The MopB_Phenylacetyl-CoA-OR CD contains the phenylacetyl-CoA:acceptor oxidoreductase, large ... |
57-598 |
9.79e-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: 154.74 E-value: 9.79e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 57 TTCSpNCTLACGIRAM-VVDGQIKALLPSNDYPEPEYGP-RGCLRGLSFINLIYGPDRIKKPLIRTG-ERGAGE---FRE 130
Cdd:cd02760 2 TYCY-NCVAGPDFMAVkVVDGVATEIEPNFAAEDIHPARgRVCVKAYGLVQKTYNPNRVLQPMKRTNpKKGRNEdpgFVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 131 VSWEEALDYTAKRLKEIAA-----RYGPESIGFIFQVGGTGHVQKGAWIALatMVGWSLIHPYDQNGDLPM--------- 196
Cdd:cd02760 81 ISWDEALDLVAAKLRRVREkglldEKGLPRLAATFGHGGTPAMYMGTFPAF--LAAWGPIDFSFGSGQGVKcvhsehlyg 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 197 -FWPQTFGVQTEElePLewlnSRYTAIFGSNI-------MVTRLIDAdflikaRNNGTKVVVFDPNYSPTAAKADEWVQL 268
Cdd:cd02760 159 eFWHRAFTVAADT--PL----ANYVISFGSNVeasggpcAVTRHADA------RVRGYKRVQVEPHLSVTGACSAEWVPI 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 269 KPSSDAALALGMARVIIEEK---LYDEAFIKTYSDMPLLVRLD--------NGRRLKADEVKGLARPDGLPPYREAFVAy 337
Cdd:cd02760 227 RPKTDPAFMFAMIHVMVHEQglgKLDVPFLRDRTSSPYLVGPDglylrdaaTGKPLVWDERSGRAVPFDTRGAVPAVAG- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 338 ngkllavhpeklelppDVILEGEIEVELKDGRL----VRVKPVFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMATT 413
Cdd:cd02760 306 ----------------DFAVDGAVSVDADDETAihqgVEGTTAFTMLVEHMRKYTPEWAESICDVPAATIRRIAREFLEN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 414 ----------------KPLHVIYG-ASNYQWyhGDLKG-RALALLPVLTGNIGKPGAGIST---------------YAGQ 460
Cdd:cd02760 370 asigstievdgvtlpyRPVAVTLGkSVNNGW--GAFECcWARTLLATLVGALEVPGGTLGTtvrlnrphddrlasvKPGE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 461 -----------YKIRFNVKEWW---------FPGSPRW--------LPWLYILHGPTP-GMKARWP--------KNGIKA 503
Cdd:cd02760 448 dgfmaqgfnptDKEHWVVKPTGrnahrtlvpIVGNSAWsqalgptqLAWMFLREVPLDwKFELPTLpdvwfnyrTNPAIS 527
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 504 LifgWGNPFDQHNMAdrlrqmaikgELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTP---------LHPYMQLQ 574
Cdd:cd02760 528 F---WDTATLVDNIA----------KFPFTVSFAYTEDETNWMADVLLPEATDLESLQMIKVGgtkfveqfwEHRGVVLR 594
|
650 660
....*....|....*....|....
gi 1731596781 575 QPAIKPLYEARSELWMARELAKRL 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 |
1.16e-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: 137.92 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 56 RTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPEPeygpRG--CLRGLSFINLIYGPDRIKKPLIRTGerGAGEFREVSW 133
Cdd:cd02752 1 RTIC-PYCSVGCGLIAYVQNGVWVHQEGDPDHPVN----RGslCPKGAALRDFVHSPKRLKYPMYRAP--GSGKWEEISW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 134 EEALDYTAKRLKEI---------AARY---GPESIGFIfqvGGTGHVQKGAWIALATMVGWSLIHPYDQ---------NG 192
Cdd:cd02752 74 DEALDEIARKMKDIrdasfveknAAGVvvnRPDSIAFL---GSAKLSNEECYLIRKFARALGTNNLDHQariuhsptvAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 193 DLPMFwpqTFGVQTEELEPLEwlNSRYTAIFGSNIMVTRLIDADFLIKAR-NNGTKVVVFDPNYSPTAAKADEWVQLKPS 271
Cdd:cd02752 151 LANTF---GRGAMTNSWNDIK--NADVILVMGGNPAEAHPVSFKWILEAKeKNGAKLIVVDPRFTRTAAKADLYVPIRSG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 272 SDAALALGMARVIIEeklydeafiktysdmpllvrldngrrlkadevkglarpdglppyreafvayngkllavhpeklel 351
Cdd:cd02752 226 TDIAFLGGMINYIIR----------------------------------------------------------------- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 352 ppdvilegeievelkdgrlvrvkpvfqllkehlasYTPAYVEQETGVPGDTVVRLAREMATT----KPLHVIYGASNYQW 427
Cdd:cd02752 241 -----------------------------------YTPEEVEDICGVPKEDFLKVAEMFAATgrpdKPGTILYAMGWTQH 285
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 428 YHGDLKGRALALLPVLTGNIGKPGAGISTYAGQYkirfNVKewwfpGS------PRWLPWLYILHGP---TP-GMKARWP 497
Cdd:cd02752 286 TVGSQNIRAMCILQLLLGNIGVAGGGVNALRGHS----NVQ-----GAtdlgllSHNLPGYLGGQNPnssFPnANKVRRA 356
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 498 KNGIKALIFgwGNPFDqhNMADRLRQMaikgelefiAGLDfslTTSCRYSDVVFPAATWYEKTELVTTPlHPYMQLQQPA 577
Cdd:cd02752 357 LDKLDWLVV--IDPFP--TETAAFWKN---------PGMD---PKSIQTEVFLLPAACQYEKEGSITNS-GRWLQWRYKV 419
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 1731596781 578 IKPLYEARSELWMARELAKRLdpgfakHFFPELDENTAAEKAVELLLATGGPPVA 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 |
5.29e-28 |
|
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: 120.71 E-value: 5.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 57 TTCSpNCTLACGIRAMVVDGQIKALLPSNDYPEPeygpRG--CLRGLSFINLIYGPDRIKKPLIRTGERGAGEFREVSWE 134
Cdd:cd02763 2 TTCY-MCACRCGIRVHLRDGKVRYIKGNPDHPLN----KGviCAKGSSGIMKQYSPARLTKPLLRKGPRGSGQFEEIEWE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 135 EALDYTAKRLKEIAARyGPESIGFIfqvggTGHVQKGA---WIA-------LATMVGWSLIHP-----YDQNGDlpmFWp 199
Cdd:cd02763 77 EAFSIATKRLKAARAT-DPKKFAFF-----TGRDQMQAltgWFAgqfgtpnYAAHGGFCSVNMaagglYSIGGS---FW- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 200 qTFGvqteelEPlEWLNSRYTAIFG------SNIMVTRLIDadflIKARnnGTKVVVFDPNYSPTAAKADEWVQLKPSSD 273
Cdd:cd02763 147 -EFG------GP-DLEHTKYFMMIGvaedhhSNPFKIGIQK----LKRR--GGKFVAVNPVRTGYAAIADEWVPIKPGTD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 274 AALALGMARVIIEEKLYDEAFIKTYSDMPLLVrldngrrlkadevkglarpdglppyreafvayngkllavhpeklelpp 353
Cdd:cd02763 213 GAFILALAHELLKAGLIDWEFLKRYTNAAELV------------------------------------------------ 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 354 dvilegeievelkdgrlvrvkpvfqllkehlaSYTPAYVEQETGVPGDTVVRLAREMATT-------------------- 413
Cdd:cd02763 245 --------------------------------DYTPEWVEKITGIPADTIRRIAKELGVTardqpielpiawtdvwgrkh 292
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1731596781 414 -----KP--LHVIYG-ASNYQWYHgdlKGRALALLPVLTGNIGKPG 451
Cdd:cd02763 293 ekitgRPvsFHAMRGiAAHSNGFQ---TIRALFVLMMLLGTIDRPG 335
|
|
| MopB_Tetrathionate-Ra |
cd02758 |
The MopB_Tetrathionate-Ra CD contains tetrathionate reductase, subunit A, (TtrA) and other ... |
57-640 |
2.03e-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: 112.82 E-value: 2.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 57 TTCSpNCTLACGIRAMVVD--GQIK-------ALL---PSNDYPEP---------------EYGPRGCLRGLSFINLIYG 109
Cdd:cd02758 2 SSCL-GCWTQCGIRVRVDKetGKVLriagnpyHPLntaPSLPYNTPlkeslylslvgenglKARATACARGNAGLQYLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 110 PDRIKKPLIRTGERGAGEFREVSWEEALdytakrlKEIAarygpeSIGFIFqvgGTGHVQKGAWIALATmvgwSLIHPyd 189
Cdd:cd02758 81 PYRVLQPLKRVGPRGSGKWKPISWEQLI-------EEVV------EGGDLF---GEGHVEGLKAIRDLD----TPIDP-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 190 QNGDL------------------PM---FWPQTFG----------------------VQTEELEPL---EWLNSRY---- 219
Cdd:cd02758 139 DHPDLgpkanqllytfgrdegrtPFikrFANQAFGtvnfgghgsycglsyragngalMNDLDGYPHvkpDFDNAEFalfi 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 220 -TAIFGSNIMVTRLidADFLIKAR-NNGTKVVVFDP---NYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYDEAF 294
Cdd:cd02758 219 gTSPAQAGNPFKRQ--ARRLAEARtEGNFKYVVVDPvlpNTTSAAGENIRWVPIKPGGDGALAMAMIRWIIENERYNAEY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 295 iktysdmpllvrldngrrlkadevkgLARPDGLPPYREAFVAYNGkllAVHPeklelppdVIlegeievelkdgrLVRVK 374
Cdd:cd02758 297 --------------------------LSIPSKEAAKAAGEPSWTN---ATHL--------VI-------------TVRVK 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 375 PVFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMAT--TKPLHVIYGASNYQwyHGDLKGRALALLPVLTGNIGKPGa 452
Cdd:cd02758 327 SALQLLKEEAFSYSLEEYAEICGVPEAKIIELAKEFTShgRAAAVVHHGGTMHS--NGFYNAYAIRMLNALIGNLNWKG- 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 453 GISTYAGQYK-----IRFN-------VKEWWFP-----------------------GSPRWLPWlYILHGPT-----PGM 492
Cdd:cd02758 404 GLLMSGGGFAdnsagPRYDfkkffgeVKPWGVPidrskkayektseykrkvaagenPYPAKRPW-YPLTPELyteviASA 482
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 493 KARWPKnGIKALIFGWGNP-----FDQHNMADRLRQmaiKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPL 567
Cdd:cd02758 483 AEGYPY-KLKALILWMANPvygapGLVKQVEEKLKD---PKKLPLFIAIDAFINETSAYADYIVPDTTYYESWGFSTPWG 558
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 568 H-PYMQ--LQQPAIKPLYEARSE-----LW-MARELAKRLD-PGFAKHFFPELDE-----NTAAE---KAVELLLATGGP 629
Cdd:cd02758 559 GvPTKAstARWPVIAPLTEKTANghpvsMEsFLIDLAKALGlPGFGPNAIKDGQGnkfplNRAEDyylRVAANIAYDGKA 638
|
730
....*....|.
gi 1731596781 630 PVAGITLEQLK 640
Cdd:cd02758 639 PVPDASEEELK 649
|
|
| Molydop_binding |
pfam01568 |
Molydopterin dinucleotide binding domain; This domain is found in various molybdopterin - ... |
729-830 |
7.31e-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: 7.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 729 FAYITRNSLYRVHSTHSNNLWMNELQDNKPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGW 808
Cdd:pfam01568 1 LYLITGRVLGQYHSQTRTRRVLRLAKPEPEVVEIHPEDAAALGIKDGDLVEVTSRRGSVVVRAKVTDRVRPGVVFMPFGW 80
|
90 100
....*....|....*....|..
gi 1731596781 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 |
3.01e-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: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 736 SLYRVHS-THSNNLWMNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWWSRYLN 814
Cdd:cd02775 1 LRDHFHSgTRTRNPWLRELAPE-PVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVTDGVPPGVVFLPHGWGHRGGR 79
|
90
....*....|....*
gi 1731596781 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 1731596781 729 FAYITRNSLYRVHSTHSNNLWMNELQDNKPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGW 808
Cdd:cd02776 2 LNYLTPHGKWSIHSTYRDNLLMLRLQRGGPVVWMNPKDAAELGIKDNDWVEVFNDNGVVVARAKVSPRIPRGTVFMYHAQ 81
|
90 100 110
....*....|....*....|....*....|...
gi 1731596781 809 ---------WSRYLNGDSYNSLTYPFIKPTHEV 832
Cdd:cd02776 82 erhvnvpgsKLTGKRGGIHNSVTRVRIKPTHLV 114
|
|
| PRK14991 |
PRK14991 |
tetrathionate reductase subunit TtrA; |
11-813 |
2.12e-21 |
|
tetrathionate reductase subunit TtrA;
Pssm-ID: 237883 [Multi-domain] Cd Length: 1031 Bit Score: 100.46 E-value: 2.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 11 KLSRRQFLKASAATA-------------------VLAGTAG-ATR-----------YFIPKAGAENTSPLKEVKYvrTTC 59
Cdd:PRK14991 2 DKTRRQLLKGGLAAGglaafaagysdtakraakgLLNGTSGkPTRdrihgnsltpeYRVDAQGQLQPNPQQRVAN--TQC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 60 SpNCTLACGIRAMV--VDGQIKALL-----P-SNDYPEP--------------EYGPRG----CLRGLSFINLIYGPDRI 113
Cdd:PRK14991 80 L-GCWTQCGVRVRVdnATNKILRIAgnpyhPlSTDHHIDmstpvkeafeslsgESGLEGrstaCARGNAMLEQLDSPYRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 114 KKPLIRTGERGAGEFREVSWEEALdytakrlKEIAAryGpesiGFIFqvgGTGHVQkgawiALATMvgWSLIHPYDQN-- 191
Cdd:PRK14991 159 LQPLKRVGKRGSGKWQRISFEQLV-------EEVVE--G----GDLF---GEGHVD-----GLRAI--RDLDTPIDAKnp 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 192 -----------------GDLPM---FWPQTFGV--------------------------QTEELEPlEWLNSRYtAIFgs 225
Cdd:PRK14991 216 eygpkanqllvtnasdeGRDAFikrFAFNSFGTrnfgnhgsycglayragsgalmgdldKNPHVKP-DWDNVEF-ALF-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 226 niMVT----------RliDADFLIKARNNGT-KVVVFDP---NYSPTAA-KADEWVQLKPSSDAALALGMARVIIEEKLY 290
Cdd:PRK14991 292 --IGTspaqsgnpfkR--QARQLANARTRGNfEYVVVAPalpLSSSLAAgDNNRWLPIRPGTDSALAMGMIRWIIDNQRY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 291 DEAFI-------------KTYSDMPLLVRLD-----NGRRLKA----DEVKGLARPDGLPPYreaFVAYNGKLLAVHPEK 348
Cdd:PRK14991 368 NADYLaqpgvaamqaageASWTNATHLVIADpghprYGQFLRAsdlgLPFEGEARGDGEDTL---VVDAADGELVPATQA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 349 LELPPDVilegEIEVELKDGRLVRVKPVFQLLKEHLASYTPAYVEQETGVPGDTVVRLAREMAT--TKPLHVIYG---AS 423
Cdd:PRK14991 445 QPARLFV----EQYVTLADGQRVRVKSSLQLLKEAARKLSLAEYSEQCGVPEAQIIALAEEFTShgRKAAVISHGgtmSG 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 424 N--YQWYhgdlkgrALALLPVLTGNIGKPGaGISTYAGQYKI-----RFNVKEwwFPGS--------------------- 475
Cdd:PRK14991 521 NgfYNAW-------AIMMLNALIGNLNLKG-GVVVGGGKFPGfgdgpRYNLAS--FAGKvkpkgvslsrskfpyekssey 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 476 -----------PRWLPWlYILHGPT-----PGMKARWPKnGIKALIFGWGNPFD-----QHNMADRLRQMAIkgeLEFIA 534
Cdd:PRK14991 591 rrkveagqspyPAKAPW-YPFVAGLltemlTAALEGYPY-PLKAWINHMSNPIYgvpglRAVIEEKLKDPKK---LPLFI 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 535 GLDFSLTTSCRYSDVVFPAATWYEKTElVTTPLHPYMQLQQPAIKPLYEARSELwMAR-----------ELAKRLD-PGF 602
Cdd:PRK14991 666 SIDAFINETTALADYIVPDTHTYESWG-FTAPWGGVPTKASTARWPVVEPRTAK-TADgqpvcmesfliAVAKRLQlPGF 743
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 603 AKHFFPELDENT-AAEKAVELLLA-------TGGPPVAGITLEQLKKGPV---------RLKSE---------VPGNRQI 656
Cdd:PRK14991 744 GDNAIKDAQGNThPLNRAEDFYLRgaaniayLGKTPVADASDEDIALTGVsrilpalqaTLKPDevrrvafiyARGGRFA 823
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 657 PFYEQVQFKKPFPPVSRPAAI----EATAQFVKSGriEFYKD-----EDAFI---ALGETLPVHKPPFEDSEYalnpeiK 724
Cdd:PRK14991 824 PAESAYDEERMGNRWKKPLQIwnedVAAARHSMTG--ERYSGcptwyPPRLAdgtPLREQFPESQWPLLLISF------K 895
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 725 GKYQFAYitRNSLYRVHSTHSNNLwmnelqdnkpkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVF 804
Cdd:PRK14991 896 SNLMSSM--SIASPRLRQVKPANP-----------VALNPQDAARLGIQHGDRVRISTPGGSVVAQASVLNGVMPGVIAI 962
|
....*....
gi 1731596781 805 EQGWWSRYL 813
Cdd:PRK14991 963 EHGYGHREL 971
|
|
| MopB_CT_3 |
cd02786 |
The MopB_CT_3 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
727-822 |
1.16e-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: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 727 YQFAYITRNSLYRVHSTHSNNLWMNELQdNKPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQ 806
Cdd:cd02786 1 YPLRLITPPAHNFLNSTFANLPELRAKE-GEPTLLIHPADAAARGIADGDLVVVFNDRGSVTLRAKVTDDVPPGVVVAEG 79
|
90
....*....|....*..
gi 1731596781 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 |
1.33e-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: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 727 YQFAYITRNSLYRVHSTHSNNLWMNELQDNKPK--VFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVF 804
Cdd:cd02777 1 YPLQLISPHPKRRLHSQLDNVPWLREAYKVKGRepVWINPLDAAARGIKDGDIVRVFNDRGAVLAGARVTDRIMPGVVAL 80
|
....*
gi 1731596781 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 |
1.53e-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: 1.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 727 YQFAYITRNSLYRVHSTHSNNLWMNELQDNKpkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQ 806
Cdd:cd02794 1 YPLQLIGWHYKRRTHSTFDNVPWLREAFPQE--VWINPLDAAARGIKDGDRVLVFNDRGKVIRPVKVTERIMPGVVALPQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1731596781 807 GWWSRYLN-----GDSYNSLTYPFIKPThevyfvpgiwAPNTAWNEALCDVRK 854
Cdd:cd02794 79 GAWYEPDAngidkGGCINTLTGLRPSPL----------AKGNPQHTNLVQVEK 121
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
11-296 |
7.87e-16 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 82.25 E-value: 7.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 11 KLSRRQFLKASAATAVlAGTAGATryfIP-KAGAENTSPLKEVKYVRTTCSpNCTLACGIRAMVVDGQIKAllpSNDYPE 89
Cdd:PRK13532 2 KLSRRDFMKANAAAAA-AAAAGLS---LPaVANAVVGSAQTAIKWDKAPCR-FCGTGCGVLVGTKDGRVVA---TQGDPD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 90 PEYGpRG--CLRG--LSFInlIYGPDRIKKPLIRTgERGA----GEFREVSWEEALDYTAKRLKEIAARYGPESIGfIFq 161
Cdd:PRK13532 74 APVN-RGlnCIKGyfLSKI--MYGKDRLTQPLLRM-KDGKydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVG-MF- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 162 vgGTGH--VQKGaWIALATMVGWSLIHPYDQNGDLPM------FWpQTFGVQteelEP------LEwlNSRYTAIFGSN- 226
Cdd:PRK13532 148 --GSGQwtIWEG-YAASKLMKAGFRSNNIDPNARHCMasavvgFM-RTFGID----EPmgcyddIE--AADAFVLWGSNm 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731596781 227 -----IMVTRLIDAdfliKARNNGTKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEKLYDEAFIK 296
Cdd:PRK13532 218 aemhpILWSRVTDR----RLSNPDVKVAVLSTFEHRSFELADNGIIFTPQTDLAILNYIANYIIQNNAVNWDFVN 288
|
|
| MopB_CT_Acetylene-hydratase |
cd02781 |
The MopB_CT_Acetylene-hydratase CD contains acetylene hydratase (Ahy) and other related ... |
736-809 |
2.65e-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: 2.65e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731596781 736 SLYRVHSTHSNNLWMNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWW 809
Cdd:cd02781 12 SYYYFHSEHRQLPSLRELHPD-PVAEINPETAAKLGIADGDWVWVETPRGRARQKARLTPGIRPGVVRAEHGWW 84
|
|
| 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 1731596781 728 QFAYITRNSLYRVHSTHSNNLWMNELQDNKpKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQG 807
Cdd:cd02778 1 EFRLIYGKSPVHTHGHTANNPLLHELTPEN-TLWINPETAARLGIKDGDRVEVSSARGKVTGKARLTEGIRPDTVFMPHG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1731596781 808 W-------WSRYLNGDSYNSLTYPFIKPThevyfvpgiwAPNTAWNEALCDVRK 854
Cdd:cd02778 80 FghwapalSRAYGGGVNDNNLLPGSTEPV----------SGGAGLQEFTVTVRK 123
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
14-288 |
5.83e-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: 65.97 E-value: 5.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 14 RRQFLKASAAtAVLAGTAGATRYFIPKAG-----AENTSPLKEVKYVRTTCSPNctLACGIRAMVVDGQIKALLPSNDYP 88
Cdd:cd02764 1 RRGFLKLMGA-SLAMASAAACRYPVEKIVpyviwPENIVPGETVYYATSLVPAG--EGQGVLVKTVDGRPIKIEGNPDHP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 89 EPEYGPRGclRGLSFINLIYGPDRIKKPLIRTGErgaGEFREVSWEEALDYTAKRLKEIAaryGPESIGFIF-QVGG-TG 166
Cdd:cd02764 78 ASLGGTSA--RAQASVLSLYDPDRAQGPLRRGID---GAYVASDWADFDAKVAEQLKAVK---DGGKLAVLSgNVNSpTT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 167 HVQKGAWialATMVGWSLIHPYDQNGDLPMF--WPQTFG---VQTEELEPlewlnsrytaifgSNIMVTrlIDADFL--- 238
Cdd:cd02764 150 EALIGDF---LKKYPGAKHVVYDPLSAEDVNeaWQASFGkdvVPGYDFDK-------------AEVIVS--IDADFLgsw 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1731596781 239 ----------IKARNNG-----TKVVVFDPNYSPTAAKADEWVQLKPSSDAALALGMARVIIEEK 288
Cdd:cd02764 212 isairhrhdfAAKRRLGaeepmSRLVAAESVYTLTGANADVRLAIRPSQEKAFALGLAHKLIKKG 276
|
|
| 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 1731596781 727 YQFAYITRNSLYRVHS-----THSNNlwmNELQDNKPkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKI 801
Cdd:cd02793 1 YPLHLLSNQPATRLHSqldhgSLSRA---YKVQGREP-IRINPADAAARGIADGDIVRVFNDRGACLAGAVVTDGIMPGV 76
|
....*...
gi 1731596781 802 VVFEQGWW 809
Cdd:cd02793 77 VQLPTGAW 84
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
51-263 |
1.46e-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: 64.48 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 51 EVKYVRTTCsPNCTLACGIRAMVVDGQIKALLPSNDypEPEYGPRGCLRG-LSFiNLIYGPDRIKKPLIRTGergaGEFR 129
Cdd:COG1034 214 ELKKTPSIC-PHCSVGCNIRVDVRGGKVYRVLPREN--EAVNEEWLCDKGrFGY-DGLNSPDRLTRPLVRKD----GELV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 130 EVSWEEALDYTAKRLKEIAAryGPESIgfifqvggtghvqkGAWIAlatmvgwslihpydqnGDLPMFwpqtfgvqTEEL 209
Cdd:COG1034 286 EASWEEALAAAAEGLKALKK--AENSV--------------GAALL----------------GALPDA--------AAIL 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1731596781 210 EPLEWLNSRYTAIFGSNImvtRLIDADFLIKARNNGTKVVVFDPNYSPTAAKAD 263
Cdd:COG1034 326 EAAEAGKLKALVLLGADP---YDLDPAAALAALAKADFVVVLDHFGSATAERAD 376
|
|
| 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 1731596781 53 KYVRTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPEPEYgpRGCLRGLSFINLIYG 109
Cdd:pfam04879 2 KVVKTIC-PYCGVGCGLEVHVKDGKIVKVEGDPDHPVNEG--RLCVKGRFGYERVYN 55
|
|
| FwdB |
COG1029 |
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion]; |
58-325 |
6.92e-09 |
|
Formylmethanofuran dehydrogenase subunit B [Energy production and conversion];
Pssm-ID: 440652 [Multi-domain] Cd Length: 428 Bit Score: 59.09 E-value: 6.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 58 TCsPNCTLACG-IRAMVVDGQIKALLpsndypepeygpRGCLRGLSFINLIYGPDRIKKPLIRtgergageFREVSWEEA 136
Cdd:COG1029 9 VC-PFCGCLCDdLEVEVEGGKIVVVK------------NACAIGAAKFERAVSDHRITSPRIR--------GKEVSLEEA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 137 LDYTAKRLKEiaARYgPesigFIFQVGGT-GHVQKGAwIALATMVGWSLIHPYD----------QNG------------- 192
Cdd:COG1029 68 IDKAAEILAN--AKR-P----LIYGLSSTdCEAMRAG-LALAERVGAVVDNTASvchgpsllalQDVgwptctlgevknr 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 193 -DLPMFWpqtfGVQTEELEPLEWlnSRYTaifgsnimvtrlIDAD--FLIKARnNGTKVVVFDPNYSPTAAKADEWVQLK 269
Cdd:COG1029 140 aDVIIYW----GCNPVHAHPRHM--SRYS------------VFPRgfFTPKGR-KDRTVIVVDPRPTDTAKVADLHLQVK 200
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1731596781 270 PSSDAALALGMaRVIIeeklydeafiktysdmpllvrldNGRRLKADEVKGLARPD 325
Cdd:COG1029 201 PGRDYEVLSAL-RALV-----------------------RGKELSPEEVAGIPVED 232
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
107-159 |
1.13e-08 |
|
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: 58.13 E-value: 1.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1731596781 107 IYGPDRIKKPLIRTGergaGEFREVSWEEALDYTAKRLKEIAARYGPESIGFI 159
Cdd:cd02772 49 LNSEDRLTKPMIKKD----GQWQEVDWETALEYVAEGLSAIIKKHGADQIGAL 97
|
|
| 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 1731596781 727 YQFAYITRNSLYRVHSThSNNLWMNELQDNKPkVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQ 806
Cdd:cd02780 1 YPFILVTFKSNLNSHRS-ANAPWLKEIKPENP-VWINPEDAAKLGIKTGDRVRVVTPGGSVVGKAKVTEGVRPGVVAIEH 78
|
.
gi 1731596781 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 |
2.61e-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: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 758 PKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWWSrylngDSYNSLTYPFIKPTHEVYFVPG 837
Cdd:cd02779 33 PYIEVNPEDAKREGLKNGDLVEVYNDYGSTTAMAYVTNTVKPGQTFMLMAHPR-----PGANGLVTPYVDPETIIPYYKG 107
|
...
gi 1731596781 838 IWA 840
Cdd:cd02779 108 TWA 110
|
|
| MopB_ydeP |
cd02767 |
The MopB_ydeP CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
112-455 |
4.86e-08 |
|
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: 56.55 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 112 RIKKPLIRtgERGAGEFREVSWEEALDYTAKRLKEI----AARY----GPESIGFIFQ----VGGTGHVQKGAWIA-LAT 178
Cdd:cd02767 64 RLTYPMRY--DAGSDHYRPISWDEAFAEIAARLRALdpdrAAFYtsgrASNEAAYLYQlfarAYGTNNLPDCSNMChEPS 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 179 MVGWslihpydqngdlpmfwPQTFGV--QTEELEplEWLNSRYTAIFGSN------IMVTrlidadFLIKARNNGTKVVV 250
Cdd:cd02767 142 SVGL----------------KKSIGVgkGTVSLE--DFEHTDLIFFIGQNpgtnhpRMLH------YLREAKKRGGKIIV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 251 FDP-------NY-SPTAAK---------ADEWVQLKPSSDAALALGMARVIIEEK-----LYDEAFIKTYSdmpllvrld 308
Cdd:cd02767 198 INPlrepgleRFaNPQNPEsmltggtkiADEYFQVRIGGDIALLNGMAKHLIERDdepgnVLDHDFIAEHT--------- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 309 ngrrlkadevkglarpdglppyreafvayNGkllavhpeklelppdvilegeievelkdgrlvrvkpvFQLLKEHLASYT 388
Cdd:cd02767 269 -----------------------------SG-------------------------------------FEEYVAALRALS 282
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731596781 389 PAYVEQETGVPGDTVVRLAREMATTKPLHVIYGASNYQWYHGDLKGRALALLPVLTGNIGKPGAGIS 455
Cdd:cd02767 283 WDEIERASGLSREEIEAFAAMYAKSERVVFVWGMGITQHAHGVDNVRAIVNLALLRGNIGRPGAGLM 349
|
|
| 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 1731596781 52 VKYVRTTCsPNCTLACGIRAMVVDGQIKALLPSNDYPEPEYgpRGCLRGLSFINLIY 108
Cdd:smart00926 1 EKWVPTVC-PLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRG--RLCPKGRAGLEQVY 54
|
|
| MopB_CT_Fdh-Nap-like |
cd00508 |
This CD includes formate dehydrogenases (Fdh) H and N; nitrate reductases, Nap and Nas; and ... |
749-822 |
7.04e-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: 7.04e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1731596781 749 WMNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKiVVFEQGWWSRYLNGDSYNSLT 822
Cdd:cd00508 27 RLAALAPE-PFVEIHPEDAARLGIKDGDLVRVSSRRGSVVVRARVTDRVRPG-TVFMPFHWGGEVSGGAANALT 98
|
|
| 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 1731596781 757 KPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWWSRYLNGDSYNSLTYPFIKP 828
Cdd:cd02791 34 EPYVEIHPEDAARLGLKEGDLVRVTSRRGEVVLRVRVTDRVRPGEVFVPMHWGDQFGRSGRVNALTLDATDP 105
|
|
| 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 |
1.59e-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: 54.60 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 107 IYGPDRIKKPLIRTGergaGEFREVSWEEALDYTAKRLKEIAarygPESIGFIfqvgGTGHVQKGAWIALATMVGWSLIH 186
Cdd:cd02768 49 LNSRQRLTQPLIKKG----GKLVPVSWEEALKTVAEGLKAVK----GDKIGGI----AGPRADLESLFLLKKLLNKLGSN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 187 PYDQNGDLPMFWPQTFgvqteeLEPLEWLNSRYTAI--------FGSN------IMVTRLIDAdflikARNNGTKVVVFD 252
Cdd:cd02768 117 NIDHRLRQSDLPADNR------LRGNYLFNTSIAEIeeadavllIGSNlrkeapLLNARLRKA-----VKKKGAKIAVIG 185
|
170 180
....*....|....*....|....*.
gi 1731596781 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 |
2.37e-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: 54.32 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 57 TTCsPNCTLACGIRAMVVDGQIKALlpSNDYPEPEYGPRGCLRG---LSFINliyGPDRIKKPLIRTGergaGEFREVSW 133
Cdd:cd02771 2 SIC-HHCSVGCNISLGERYGELRRV--ENRYNGAVNHYFLCDRGrfgYGYVN---SRDRLTQPLIRRG----GTLVPVSW 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 134 EEALDYTAKRLKEIAARygpeSIGFifqvgGTGHVQKGAWIALATMVGWSLihpydqngdlpmfwpqtfgvqteeleple 213
Cdd:cd02771 72 NEALDVAAARLKEAKDK----VGGI-----GSPRASNESNYALQKLVGAVL----------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 214 wlnsrytaifGSNimvtrliDADFliKARNNGTKVVVFDPNYSPTAAKADewvqlkpSSDAALALGmarviieEKLYDEA 293
Cdd:cd02771 114 ----------GTN-------NVDH--RARRLIAEILRNGPIYIPSLRDIE-------SADAVLVLG-------EDLTQTA 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 294 FIktysdMPLLVRLDNGRRLKADEVKGLARPDGLPPYREAFVAYNGKLLAVHPEklelpPDVILEGeievelkDGRLVRV 373
Cdd:cd02771 161 PR-----IALALRQAARRKAVELAALSGIPKWQDAAVRNIAQGAKSPLFIVNAL-----ATRLDDI-------AAESIRA 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 374 KPVFQL-LKEHLASYTPAYVE-QETGVPGDTVVRLARE-MATTKPLHVIYGASnyqwyHGDLKGRALALLPVLTGNIGKP 450
Cdd:cd02771 224 SPGGQArLGAALARAVDASAAgVSGLAPKEKAARIAARlTGAKKPLIVSGTLS-----GSLELIKAAANLAKALKRRGEN 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 451 GAgistyagqykirfnvkeWWFPGSPRWLPWLYILHGP-------TPGMKARWPKNGIKALIFGWGNPFDqhnMADRLRQ 523
Cdd:cd02771 299 AG-----------------LTLAVEEGNSPGLLLLGGHvtepgldLDGALAALEDGSADALIVLGNDLYR---SAPERRV 358
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 524 MAIKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIKPLYEARSELWMARELAKRLDPGFA 603
Cdd:cd02771 359 EAALDAAEFVVVLDHFLTETAERADVVLPAASFAEKSGTFVNYEGRAQRFFKAYDDPAGDARSDWRWLHALAAKLGGKLV 438
|
570 580 590
....*....|....*....|....*....|.
gi 1731596781 604 KHFFPELDENTA--AEKAVELLLATGGPPVA 632
Cdd:cd02771 439 PSDAAILDEIIAlvPGKAPVGGHLYGGDPGV 469
|
|
| 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 1731596781 746 NNLWMNELQdnkPKVF--LNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVV--FEQGWWSrYLNGDSYNSL 821
Cdd:cd02792 24 NSPYLAELQ---PEMFveISPELAAERGIKNGDMVWVSSPRGKIKVKALVTDRVKPHEVGipYHWGGMG-LVIGDSANTL 99
|
90 100 110
....*....|....*....|....*....|....*.
gi 1731596781 822 TypfikpthevyfvPGIWAPNT---AWNEALCDVRK 854
Cdd:cd02792 100 T-------------PYVGDPNTqtpEYKAFLVNIEK 122
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
109-598 |
8.24e-06 |
|
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the electrons obtained from the oxidation of arsenite towards the soluble periplasmic electron carriers cytochrome c and/or amicyanin. Arsenite oxidase is a heterodimeric enzyme containing a large and a small subunit. The large catalytic subunit harbors the molybdopterin cofactor and the [3Fe-4S] cluster; and the small subunit belongs to the structural class of the Rieske proteins. The small subunit is not included in this alignment. Members of MopB_Arsenite-Ox CD belong to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239157 [Multi-domain] Cd Length: 676 Bit Score: 49.40 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 109 GPDRIKKPLIRTGergaGEFREVSWEEALDYTAKRLKEIAARYGPESIGF--IFQVGGTGHVQKGAWIA-----LATMVG 181
Cdd:cd02756 114 GETRLTTPLVRRG----GQLQPTTWDDAIDLVARVIKGILDKDGNDDAVFasRFDHGGGGGGFENNWGVgkfffMALQTP 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 182 WSLIHpydqngDLPMFWPQTFGvqTEELEPLEwLNSRYTAI--------FGSNIMVTRLIdadFLIK------------- 240
Cdd:cd02756 190 FVRIH------NRPAYNSEVHA--TREMGVGE-LNNSYEDArladtivlWGNNPYETQTV---YFLNhwlpnlrgatvse 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 241 ---ARNNGTKV-----VVFDPNYSPTAAKADE--------WVQLKPSSDAALALGMARVIIEeklydeafikTYSDMpll 304
Cdd:cd02756 258 kqqWFPPGEPVppgriIVVDPRRTETVHAAEAaagkdrvlHLQVNPGTDTALANAIARYIYE----------SLDEV--- 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 305 vrLDngrrlKADEVKGLARpdglppyreafvayngkllavhpEKLELPPDVIlegeieVELKDGRlvrvkpvfqllkehl 384
Cdd:cd02756 325 --LA-----EAEQITGVPR-----------------------AQIEKAADWI------AKPKEGG--------------- 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 385 aSYTPAYVEQETGvpgdtvvrlaremattkplhVIYGASNYQWYHgdlkgrALALLPVLTGNIGKPGAGISTYAGQYkir 464
Cdd:cd02756 354 -YRKRVMFEYEKG--------------------IIWGNDNYRPIY------SLVNLAIITGNIGRPGTGCVRQGGHQ--- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 465 fnvKEWWFPGSPrwlpwlyilhGPTPGMKARWPKNGIKALIFGWG--------NPFDQHNMADRLRQM----------AI 526
Cdd:cd02756 404 ---EGYVRPPPP----------PPPWYPQYQYAPYIDQLLISGKGkvlwvigcDPYKTTPNAQRLRETinhrsklvtdAV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 527 KGELE----------------------FIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTPLHPYMQLQQPAIKPLYEA 584
Cdd:cd02756 471 EAALYagtydreamvcligdaiqpgglFIVVQDIYPTKLAEDAHVILPAAANGEMNETSMNGHERRLRLYEKFMDPPGEA 550
|
570
....*....|....
gi 1731596781 585 RSELWMARELAKRL 598
Cdd:cd02756 551 MPDWWIAAMIANRI 564
|
|
| TAT_signal |
pfam10518 |
TAT (twin-arginine translocation) pathway signal sequence; |
11-34 |
1.65e-05 |
|
TAT (twin-arginine translocation) pathway signal sequence;
Pssm-ID: 463131 [Multi-domain] Cd Length: 26 Bit Score: 41.98 E-value: 1.65e-05
|
| MopB_CT_Formate-Dh_H |
cd02790 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
726-804 |
1.04e-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: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 726 KYQFAYITRNSLYRVHS-THSNNLW-MNELQDNkPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLgRKIVV 803
Cdd:cd02790 2 EYPLVLTTGRVLYHYHTgTMTRRAEgLDAIAPE-EYVEINPEDAKRLGIEDGEKVRVSSRRGSVEVRARVTDRV-PEGVV 79
|
.
gi 1731596781 804 F 804
Cdd:cd02790 80 F 80
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
489-628 |
3.32e-04 |
|
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: 44.06 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731596781 489 TPGMKARWPKNGIKALIFGWGNPFDqhnmADRLRQMAIKGELEFIAGLDFSLTTSCRYSDVVFPAATWYEKTELVTTplh 568
Cdd:COG1034 321 AAAILEAAEAGKLKALVLLGADPYD----LDPAAALAALAKADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVN--- 393
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1731596781 569 pyM----QLQQPAIKPLYEARsELWM-ARELAKRLDPGFAkhfFPELDENTAA-EKAVELLLATGG 628
Cdd:COG1034 394 --LegrvQRFNAAVPPPGEAR-PDWRvLRALANALGAGLP---YDSLEEVRAElAAEAPATVSAEG 453
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
109-152 |
6.44e-04 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 43.40 E-value: 6.44e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1731596781 109 GPDRIKKPLIRTGErgaGEFREVSWEEALDYTAKRLKEIAARYG 152
Cdd:PRK07860 275 QPDRITTPLVRDED---GELEPASWSEALAVAARGLAAARGRVG 315
|
|
| TAT_signal_seq |
TIGR01409 |
Tat (twin-arginine translocation) pathway signal sequence; Proteins assembled with various ... |
12-43 |
2.11e-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: 2.11e-03
10 20 30
....*....|....*....|....*....|..
gi 1731596781 12 LSRRQFLKASAATAVLAGTAGatrYFIPKAGA 43
Cdd:TIGR01409 1 LSRRDFLKGAAAAGAAAGLGA---LLPSPARA 29
|
|
| MopB_CT_1 |
cd02782 |
The MopB_CT_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
739-812 |
5.07e-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: 5.07e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1731596781 739 RVHSThSNNLWMNELQ-----DNKPKVFLNPQDAAAKGIKEGDLVEVYNDRGRVRGYAALDPGLGRKIVVFEQGWWSRY 812
Cdd:cd02782 10 RRHLR-SNNSWLHNDPrlvkgRNRCTLRIHPDDAAALGLADGDKVRVTSAAGSVEAEVEVTDDMMPGVVSLPHGWGHDY 87
|
|
| |
