|
Name |
Accession |
Description |
Interval |
E-value |
| NuoG |
TIGR01973 |
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of ... |
4-623 |
0e+00 |
|
NADH-quinone oxidoreductase, chain G; This model represents the G subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria while translocating protons, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes related subunits from formate dehydrogenase complexes. [Energy metabolism, Electron transport]
Pssm-ID: 273904 [Multi-domain] Cd Length: 602 Bit Score: 686.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 4 IELDGKKVGIAEGSTVMHAAEKAGTYIPHFCYHKKLSIAANCRMCLVDIEKMPKPMPACATSVTQGMVVRTKTDKAVKAQ 83
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 84 QSVMEFLLINHPLDCPICDQGGECQLQDLAVGYGGVKSRYEEEKRVVKVKDVGPLIsMQEMTRCIHCTRCVRFGQEIAGV 163
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLI-KTEMTRCIHCTRCVRFANEVAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 164 MELGMSQRGEHSEIEAFVGQTVDSELSGNMIDICPVGALTSKPFRYSARTWELSRRKSISPHDSTGANLIVQVKNNRVMR 243
Cdd:TIGR01973 160 EDLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEIMR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 244 VVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIK-QGGQWNEVDWKTALEYVAHGLRNIksehgaSAVGALVSPHST 322
Cdd:TIGR01973 240 ILPRENDEINEEWLCDKGRFGYDGLNRQDRLTKPLLRnQEGNLLEVSWAEALAIAAEKLKAS------SRIGGIAGPRSS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 323 IEELYLTGALVRGLGSENIDYRLRNAEFDRTQPGARWL-GMPIAGLSTLQSVLVVGSSLRKDHPLFAQRIRQAARNGCAV 401
Cdd:TIGR01973 314 LEELFALKKLVRKLGSENFDLRIRNYEFESADLRANYLfNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 402 HAVASaAPQW--AMPLASATVLPATEWVACLASIAAAvgqekgvaapqsavvtdAALIAAQSLLAGEHKAVLLGNGAAHH 479
Cdd:TIGR01973 394 VALIG-IEKWnlTYPANTNLVFHPGLSPKKLDDIASG-----------------AHSDIAAALKAAKKPLIIVGDSAISH 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 480 PLAAQLLALANWIGEQCG------ASVGYLTEAANTVGAQLVGALPglGGLNAGQMLaGGLKATILLNTEPQWDAAAgVA 553
Cdd:TIGR01973 456 LDGAALISAAANIAKVIKvrrkewNGLNILSSGANSVGLLDLGGES--TGLDAALNL-GAADALFLLGADLERALDK-TA 531
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1101172364 554 TLDALGQSEMVVSL-TPFKTNMAFSDVLLPIAPFTETSGSFVNAEGRLQSFHAVVKPLGETRPAWKVLRAL 623
Cdd:TIGR01973 532 RDALSKADAFIIYQgHHGTETAEKADVILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
1-655 |
0e+00 |
|
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: 639.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 1 MIEIELDGKKVGIAEGSTVMHAAEKAGTYIPHFCYHKKLSIAANCRMCLVDIEKMPKPMPACATSVTQGMVVRTKTDKAV 80
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 81 KAQQSVMEFLLINHPLDCPICDQGGECQLQDLAVGYGGVKSRYEEEKRVVKVKDVGPLISMqEMTRCIHCTRCVRFGQEI 160
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILL-DMNRCILCTRCVRFCDEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 161 AGVMELGMSQRGEHSEIEAFVGQTVDSELSGNMIDICPVGALTSKPFRYSARTWELSRRKSISPHDSTGANLIVQVKNNR 240
Cdd:COG1034 160 AGDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVRGGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 241 VMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQGGQWNEVDWktaleyvahglrniksehgasavgalvsph 320
Cdd:COG1034 240 VYRVLPRENEAVNEEWLCDKGRFGYDGLNSPDRLTRPLVRKDGELVEASW------------------------------ 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 321 stieelyltgalvrglgsenidyrlrnaefdrtqpgarwlgmpiaglstlqsvlvvgsslrkdhplfaqrirqaarngca 400
Cdd:COG1034 --------------------------------------------------------------------------------
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 401 vhavasaapqwamplasatvlpatewvaclasiaaavgqekgvaapqsavvtDAALIAAQSLLAgehkavllgngaahhp 480
Cdd:COG1034 290 ----------------------------------------------------EEALAAAAEGLK---------------- 301
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 481 laaqllalanwigeqcgasvgYLTEAANTVGAQLVGALPGLGGLNAGqMLAGGLKATILLNTEPqwDAAAGVATLDALGQ 560
Cdd:COG1034 302 ---------------------ALKKAENSVGAALLGALPDAAAILEA-AEAGKLKALVLLGADP--YDLDPAAALAALAK 357
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 561 SEMVVSLTPFKT-NMAFSDVLLPIAPFTETSGSFVNAEGRLQSFHAVVKPLGETRPAWKVLRALADILGlPGFGFDSSLE 639
Cdd:COG1034 358 ADFVVVLDHFGSaTAERADVVLPAAAFAEKSGTFVNLEGRVQRFNAAVPPPGEARPDWRVLRALANALG-AGLPYDSLEE 436
|
650
....*....|....*.
gi 1101172364 640 VLGRALDLPPgATVAA 655
Cdd:COG1034 437 VRAELAAEAP-ATVSA 451
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
220-627 |
0e+00 |
|
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: 580.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 220 KSISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQGGQWNEVDWKTALEYVAH 299
Cdd:cd02772 1 KSVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEDRLTKPMIKKDGQWQEVDWETALEYVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 300 GLRNIKSEHGASAVGALVSPHSTIEELYLTGALVRGLGSENIDYRLRNAEF--DRTQPGARWLGMPIAGLSTLQSVLVVG 377
Cdd:cd02772 81 GLSAIIKKHGADQIGALASPHSTLEELYLLQKLARGLGSDNIDHRLRQSDFrdDAKASGAPWLGMPIAEISELDRVLVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 378 SSLRKDHPLFAQRIRQAARNGCAVHAVASAAPQWAMPLASATVLPATEWVACLASIAAAVGQEKGVAAP---QSAVVTDA 454
Cdd:cd02772 161 SNLRKEHPLLAQRLRQAVKKGAKLSAINPADDDFLFPLSGKAIVAPSALANALAQVAKALAEEKGLAVPdedAKVEASEE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 455 ALIAAQSLLAGEHKAVLLGNGAAHHPLAAQLLALANWIGEQCGASVGYLTEAANTVGAQLVGALPGlGGLNAGQMLAGGL 534
Cdd:cd02772 241 ARKIAASLVSAERAAVFLGNLAQNHPQAATLRALAQEIAKLTGATLGVLGEGANSVGAYLAGALPH-GGLNAAAMLEQPR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 535 KATILLNTEPQWDAAAGVATLDALGQSEMVVSLTPFKTN--MAFSDVLLPIAPFTETSGSFVNAEGRLQSFHAVVKPLGE 612
Cdd:cd02772 320 KAYLLLNVEPELDCANPAQALAALNQAEFVVALSAFASAalLDYADVLLPIAPFTETSGTFVNLEGRVQSFKGVVKPLGE 399
|
410
....*....|....*
gi 1101172364 613 TRPAWKVLRALADIL 627
Cdd:cd02772 400 ARPAWKVLRVLGNLL 414
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
220-627 |
1.40e-135 |
|
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: 404.36 E-value: 1.40e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 220 KSISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQGGQWNEVDWKTALEYVAH 299
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNSRQRLTQPLIKKGGKLVPVSWEEALKTVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 300 GLRNIKsehgASAVGALVSPHSTIEELYLTGALVRGLGSENIDYRLRN--AEFDRTQPGARWLGMPIAGLSTLQSVLVVG 377
Cdd:cd02768 81 GLKAVK----GDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLRQsdLPADNRLRGNYLFNTSIAEIEEADAVLLIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 378 SSLRKDHPLFAQRIRQAARNGCAVHAVASAAPQWAMPLASATVLPATEWVACLASIAAAvgqekgvaapqsavvtDAALI 457
Cdd:cd02768 157 SNLRKEAPLLNARLRKAVKKKGAKIAVIGPKDTDLIADLTYPVSPLGASLATLLDIAEG----------------KHLKP 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 458 AAQSLLAGEHKAVLLGNGAAHHPLAAQLLALANWIGEQC-GASVGYLTEAANTVGAQLVGAlpglgGLNAGQMLAGGLKA 536
Cdd:cd02768 221 FAKSLKKAKKPLIILGSSALRKDGAAILKALANLAAKLGtGAGLWNGLNVLNSVGARLGGA-----GLDAGLALLEPGKA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 537 TILLNTEPQWDAAAGVATLdALGQSEMVVSLTPFKT-NMAFSDVLLPIAPFTETSGSFVNAEGRLQSFHAVVKPLGETRP 615
Cdd:cd02768 296 KLLLLGEDELDRSNPPAAV-ALAAADAFVVYQGHHGdTGAQADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDARE 374
|
410
....*....|..
gi 1101172364 616 AWKVLRALADIL 627
Cdd:cd02768 375 DWKILRALSNLL 386
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
1-630 |
5.26e-114 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 361.96 E-value: 5.26e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 1 MIEIELDGKKVGIAEGSTVMHAAEKAGTYIPHFCYHKKLSIAANCRMCLVDIEKMPKPMPACATSVTQGMVVRTKTDKAV 80
Cdd:PRK07860 4 LVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTQLTSPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 81 --KAQQSVMEFLLINHPLDCPICDQGGECQLQDLAVGYGGVKSRYEEEKRVVKvkdvGPL-ISMQ---EMTRCIHCTRCV 154
Cdd:PRK07860 84 adKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFP----KPInISTQvllDRERCVLCARCT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 155 RFGQEIAGVMELGMSQRGEHSEIEAFVGQTVDSELSGNMIDICPVGALTSKPFRYSARTWELSRRKSISPHDSTGANLIV 234
Cdd:PRK07860 160 RFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHCASGCAQRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 235 QVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIK-QGGQWNEVDWKTALEYVAHGLRnikseHGASAV 313
Cdd:PRK07860 240 DHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTYATQPDRITTPLVRdEDGELEPASWSEALAVAARGLA-----AARGRV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 314 GALVSPHSTIEELYLTGALVR-GLGSENIDYRLR-----NAEFDRTQPGARWLGMPIAGLSTLQSVLVVGSSLRKDHPLF 387
Cdd:PRK07860 315 GVLVGGRLTVEDAYAYAKFARvALGTNDIDFRARphsaeEADFLAARVAGRGLGVTYADLEKAPAVLLVGFEPEEESPIV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 388 AQRIRQAAR-NGCAVHAVAsaapqwamPLAS-------ATVLPA-----TEWVACLASIAAAVGQekgvaapqsAVVTDA 454
Cdd:PRK07860 395 FLRLRKAARkHGLKVYSIA--------PFATrglekmgGTLLRTapggeAAALDALATGAPDVAE---------LLRTPG 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 455 ALIaaqslLAGEHKAVLLGNGAAHHPLAAQLLALANWI----GEQCGASVGYL----------TEAANTVGAQL---VGA 517
Cdd:PRK07860 458 AVI-----LVGERLATVPGALSAAARLADATGARLAWVprraGERGALEAGALptllpggrpvADPAARAEVAAawgVDE 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 518 LPGLGGLNAGQMLA----GGLKATILLNTEPQ--WDAAAGVATLDALGqseMVVSLTPFKTN-MAFSDVLLPIAPFTETS 590
Cdd:PRK07860 533 LPAAPGRDTAGILAaaaaGELGALLVGGVEPAdlPDPAAALAALDAAG---FVVSLELRHSAvTERADVVLPVAPVAEKA 609
|
650 660 670 680
....*....|....*....|....*....|....*....|
gi 1101172364 591 GSFVNAEGRLQSFHAVVKPLGETrPAWKVLRALADILGLP 630
Cdd:PRK07860 610 GTFLNWEGRLRPFEAALRTTGAL-SDLRVLDALADEMGVD 648
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
220-627 |
3.57e-76 |
|
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: 249.55 E-value: 3.57e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 220 KSISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQG--GQWNEVDWKTALEYV 297
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYSPDRLKYPLIRVGgrGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 298 AHGLRNIKSEHGASAVGALVSPHSTIEELYLTGALVRGLGSENIDYRLR----NAEFDRTQPGARWLGMPIAGLSTLQSV 373
Cdd:cd00368 81 AEKLKEIREKYGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARlchaSAVAALKAFGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 374 LVVGSSLRKDHPLFAQRIRQAARNGCAVhAVASaapqwamPLASATVLPATEWVACL-ASIAAAVGQEKgvAAPQSAVvt 452
Cdd:cd00368 161 LLWGSNPAETHPVLAARLRRAKKRGAKL-IVID-------PRRTETAAKADEWLPIRpGTDAALALAEW--AAEITGV-- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 453 DAALIAAQSLLAGEHKAVLL--GNGAAHHplaaqllalanwigeqcgasvgylteAANTVGAQLVGALPGLGGLNagqml 530
Cdd:cd00368 229 PAETIRALAREFAAAKRAVIlwGMGLTQH--------------------------TNGTQNVRAIANLAALTGNI----- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 531 aGGLKATILLNTEPQWDAAAGVATLDALGQSEMVVSLTPFKTNMA-FSDVLLPIAPFTETSGSFVNAEGRLQSFHAVVKP 609
Cdd:cd00368 278 -GRPGGGLGPGGNPLVSAPDANRVRAALKKLDFVVVIDIFMTETAaYADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEP 356
|
410
....*....|....*...
gi 1101172364 610 LGETRPAWKVLRALADIL 627
Cdd:cd00368 357 PGEARSDWEILRELAKRL 374
|
|
| 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 ... |
220-630 |
2.57e-57 |
|
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: 201.85 E-value: 2.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 220 KSISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQGGQWNEVDWKTALEYVAH 299
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNSRDRLTQPLIRRGGTLVPVSWNEALDVAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 300 GLRNIKsehgaSAVGALVSPHSTIEELYLTGALVRG-LGSENIDYRLRN--AEFDRTQPGARwlgMPIAGLSTLQSVLVV 376
Cdd:cd02771 81 RLKEAK-----DKVGGIGSPRASNESNYALQKLVGAvLGTNNVDHRARRliAEILRNGPIYI---PSLRDIESADAVLVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 377 GSSLRKDHPLFAQRIRQAARNGCAVHAVASAAPQWAM------------PLASATVLPAT--------------EWVACL 430
Cdd:cd02771 153 GEDLTQTAPRIALALRQAARRKAVELAALSGIPKWQDaavrniaqgaksPLFIVNALATRlddiaaesiraspgGQARLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 431 ASIAAAVGQEKGVAAPQSAvvTDAALIAAQSLLAGEHKAVLLGnGAAHHPLAAQLLALANW----IGEQCGasVGYLTEA 506
Cdd:cd02771 233 AALARAVDASAAGVSGLAP--KEKAARIAARLTGAKKPLIVSG-TLSGSLELIKAAANLAKalkrRGENAG--LTLAVEE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 507 ANTVGAQLVGALPGLGGLNAGQMLA----GGLKATILLNTEPqWDAAAGVATLDALGQSEMVVSLTPFKTN-MAFSDVLL 581
Cdd:cd02771 308 GNSPGLLLLGGHVTEPGLDLDGALAaledGSADALIVLGNDL-YRSAPERRVEAALDAAEFVVVLDHFLTEtAERADVVL 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1101172364 582 PIAPFTETSGSFVNAEGRLQSFHAVV-KPLGETRPAWKVLRALADILGLP 630
Cdd:cd02771 387 PAASFAEKSGTFVNYEGRAQRFFKAYdDPAGDARSDWRWLHALAAKLGGK 436
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
220-640 |
2.11e-55 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 201.27 E-value: 2.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 220 KSISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQGGQWNEVDWKTALEYVAH 299
Cdd:COG3383 8 KTVCPYCGVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVNSPDRLTTPLIRRGGEFREVSWDEALDLVAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 300 GLRNIKSEHGASAVGALVSPHSTIEELYLTGALVRG-LGSENIDY--RLRNAefdRTQPG-ARWLGM-----PIAGLSTL 370
Cdd:COG3383 88 RLREIQAEHGPDAVAFYGSGQLTNEENYLLQKLARGvLGTNNIDNnaRLCMA---SAVAGlKQSFGSdappnSYDDIEEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 371 QSVLVVGSSLRKDHPLFAQRIRQAARNGCAV-------HAVASAAPQWampLAsatVLPATEwVACLASIAAAVGQEKGV 443
Cdd:COG3383 165 DVILVIGSNPAEAHPVLARRIKKAKKNGAKLivvdprrTETARLADLH---LQ---IKPGTD-LALLNGLLHVIIEEGLV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 444 --------------------------AAPQSAVVTDAALIAAQSLLAGEHKAVLLGNGAAHHPLAAQLLALAN------- 490
Cdd:COG3383 238 dedfiaertegfeelkasvakytperVAEITGVPAEDIREAARLIAEAKRAMILWGMGVNQHTQGTDNVNAIInlalatg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 491 WIGEQcGASVGYLTEAANTVGAQLVGALPGL----------------------------GGLNAGQML----AGGLKATI 538
Cdd:COG3383 318 NIGRP-GTGPFPLTGQNNVQGGRDMGALPNVlpgyrdvtdpehrakvadawgvpplpdkPGLTAVEMFdaiaDGEIKALW 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 539 LLNTEP-QWDAAAGvATLDALGQSEMVVSLTPFKTNMA-FSDVLLPIAPFTETSGSFVNAEGRLQSFHAVVKPLGETRPA 616
Cdd:COG3383 397 IIGENPaVSDPDAN-HVREALEKLEFLVVQDIFLTETAeYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPD 475
|
490 500
....*....|....*....|....
gi 1101172364 617 WKVLRALADILGLPgFGFDSSLEV 640
Cdd:COG3383 476 WEIIAELARRLGYG-FDYDSPEEV 498
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
273-625 |
4.13e-47 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 170.66 E-value: 4.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 273 RLTKPMIKQG-GQWNEVDWKTALEYVAHGLRNIKSEHG--ASAVGALVSPHSTIEELYLTGALVRGLGSENIDYRLRN-- 347
Cdd:pfam00384 1 RLKYPMVRRGdGKFVRVSWDEALDLIAKKLKRIIKKYGpdAIAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDHNgd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 348 ------AEFDRTQPGARWLGMPIAGLSTLQSVLVVGSSLRKDHPLFAQRIRQAARNGCAvhAVASAAPQWAMPLASA--T 419
Cdd:pfam00384 81 lctaaaAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKA--KVIVIGPRLDLTYADEhlG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 420 VLPATEwVACLASIAAAVGQEKGVAAPQSavvTDAALIAAQSLLAGEHkavllgnGAAHHPLAAQLLALANWIGEQCG-- 497
Cdd:pfam00384 159 IKPGTD-LALALAGAHVFIKELKKDKDFA---PKPIIIVGAGVLQRQD-------GEAIFRAIANLADLTGNIGRPGGgw 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 498 ASVGYLTEAANTVGAQLVGALPGLGGLNAGQMLA-GGLKATILLNTEPQWDAAAGVATLDALGQSEMVVSLTPF-KTNMA 575
Cdd:pfam00384 228 NGLNILQGAASPVGALDLGLVPGIKSVEMINAIKkGGIKVLYLLGNNPFVTHADENRVVKALQKLDLFVVYDGHhGDKTA 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1101172364 576 -FSDVLLPIAPFTETSGSFVNAEGRLQSFHAVVKPLGETRPAWKVLRALAD 625
Cdd:pfam00384 308 kYADVILPAAAYTEKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
221-627 |
6.83e-46 |
|
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone oxidoreductase/respiratory complex I/NADH dehydrogenase-1(NDH-1) of eukaryotes and the Nqo3/G subunit of alphaproteobacteria NDH-1. The NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chains of many prokaryotes and eukaryotes. Mitochondrial complex I and its bacterial counterpart, NDH-1, function as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75 kDa) subunit of the mitochondrial NADH:ubiquinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. In Paracoccus denitrificans, this subunit is encoded by the nqo3 gene, and is part of the 14 distinct subunits constituting the 'minimal' functional enzyme. The Nad11/Nqo3 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239174 [Multi-domain] Cd Length: 375 Bit Score: 167.83 E-value: 6.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 221 SISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNAdDRLTKPMIKQGGQWNEVDWKTALEYVAHG 300
Cdd:cd02773 2 SIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKR-QRLDKPYIRKNGKLKPATWEEALAAIAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 301 LRNIKSEHGASAVGALVSphstIEELYLTGALVRGLGSENIDYRLRNAEFDRTQPGARWLGMPIAGLSTLQSVLVVGSSL 380
Cdd:cd02773 81 LKGVKPDEIAAIAGDLAD----VESMVALKDLLNKLGSENLACEQDGPDLPADLRSNYLFNTTIAGIEEADAVLLVGTNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 381 RKDHPLFAQRIRQAARNGCAVhaVASAAPQWAMplasatvlpaTEWVACLASIAAAVgqeKGVAA---PQSAVVTDA--- 454
Cdd:cd02773 157 RFEAPVLNARIRKAWLHGGLK--VGVIGPPVDL----------TYDYDHLGTDAKTL---QDIASgkhPFSKALKDAkkp 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 455 ALIAAQSLLAGEHKAVLLgnGAAHHPLAAQLLALANWIGeqcgasVGYLTEAANTVGAQLVGALPGLGGLNAgqmlAGGL 534
Cdd:cd02773 222 MIIVGSGALARKDGAAIL--AAVAKLAKKNGVVREGWNG------FNVLHRAASRVGALDLGFVPGAGAIRK----SGPP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 535 KATILLNtepqwdaaAGVATLDALGQSEMVVSLTPFKTNMA-FSDVLLPIAPFTETSGSFVNAEGRLQSFHAVVKPLGET 613
Cdd:cd02773 290 KVLYLLG--------ADEIDITPIPKDAFVVYQGHHGDRGAqIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDA 361
|
410
....*....|....
gi 1101172364 614 RPAWKVLRALADIL 627
Cdd:cd02773 362 REDWKILRALSEVL 375
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
13-202 |
3.92e-44 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 160.59 E-value: 3.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 13 IAEGSTVMHAAEKAGTYIPHFCYHKKLSIAANCRMCLVDIEKMPKPMPACATSVTQGMVVRTKTDKAVKAQQSVMEFLLI 92
Cdd:PTZ00305 81 IPQEENLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVVSCATVALPGMSIITDSRLVRDAREGNVELILI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 93 NHPLDCPICDQGGECQLQDLAVGYGGVKSRYEEEKRVVKVKDVGPLISMQeMTRCIHCTRCVRFGQEIAGVMELGMSQRG 172
Cdd:PTZ00305 161 NHPNDCPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTRVV-LNRCIHCTRCVRFLNEHAQDFNLGMIGRG 239
|
170 180 190
....*....|....*....|....*....|..
gi 1101172364 173 EHSEIEAFVGQtVDSELSGNM--IDICPVGAL 202
Cdd:PTZ00305 240 GLSEISTFLDE-LEVKTDNNMpvSQLCPVGKL 270
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
1-394 |
1.05e-41 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 162.95 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 1 MIEIELDGKKVGIAEGSTVMHAAEKAGTYIPHFCYHKKLSIAANCRMCLVDIEKmpKPMPACATSVTQGMVVRTKTDKAV 80
Cdd:PRK08493 1 MITITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEADG--KRVYSCNTKAKEGMNILTNTPNLM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 81 KAQQSVMEFLLINHPLDCPICDQGGECQLQDLAvgyggVKSRYEEEKRVVK-----VKDVGpLISMQEmTRCIHCTRCVR 155
Cdd:PRK08493 79 DERNAIMQTYDVNHPLECGVCDKSGECELQNFT-----HEMGVNHQPYAIKdthkpHKHWG-KINYDP-SLCIVCERCVT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 156 FGQEIAGVMELGMSQRGEHSEIEAF-----------------------VGQTVDSELSGNMIDICPVGALTSKPFRYSAR 212
Cdd:PRK08493 152 VCKDKIGESALKTVPRGLDAPDKSFkesmpkdayavwskkqksligpvGGETLDCSFCGECIAVCPVGALSSSDFQYTSN 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 213 TWELSRRKSISPHDSTGANLIVQVKNN-------RVMRVvpfENEaVNECWIADRDRFSYEALNADDRltkpmikqggqw 285
Cdd:PRK08493 232 AWELKKIPATCPHCSDCCLIYYDVKHSsilnqesKIYRV---SND-FYFNPLCGAGRFAFDFQNEADK------------ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 286 NEVDWKTALEyvahGLRNIKsehgASAVGALVsphsTIEELYLTGALvrglgSENIDYRLRNAEFDRTQPGARWLGmPIA 365
Cdd:PRK08493 296 DEKAFKEAVE----AFKEAK----AIKFNSFI----TNEEALILQRL-----KKKFGLKLINEEALKFQQFLKVFS-EVS 357
|
410 420 430
....*....|....*....|....*....|....*...
gi 1101172364 366 GLSTL---------QSVLVVGSSLRKDHPLFAQRIRQA 394
Cdd:PRK08493 358 GKSYSanlediktsDFVVVAGSALKTDNPLLRYAINNA 395
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
220-637 |
1.37e-41 |
|
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: 158.92 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 220 KSISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQGGQWNEVDWKTALEYVAH 299
Cdd:cd02753 1 KTVCPYCGVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNSKDRLTKPLIRKNGKFVEASWDEALSLVAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 300 GLRNIKSEHGASAVGALVSPHSTIEELYLTGALVR-GLGSENIDY--RLRNAEfdrTQPG-ARWLGM-----PIAGLSTL 370
Cdd:cd02753 81 RLKEIKDKYGPDAIAFFGSAKCTNEENYLFQKLARaVGGTNNVDHcaRLCHSP---TVAGlAETLGSgamtnSIADIEEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 371 QSVLVVGSSLRKDHPLFAQRIRQAARNGCAV-------HAVASAAPQW---------AMPLASATVL------------P 422
Cdd:cd02753 158 DVILVIGSNTTEAHPVIARRIKRAKRNGAKLivadprrTELARFADLHlqlrpgtdvALLNAMAHVIieeglydeefieE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 423 ATEWVACLASIAAAVGQEK-----GVAAPQsavVTDAALIAAQsllaGEHKAVLLGNGAAHHplaaqllalanwigeqcg 497
Cdd:cd02753 238 RTEGFEELKEIVEKYTPEYaeritGVPAED---IREAARMYAT----AKSAAILWGMGVTQH------------------ 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 498 aSVGYLTEAANTVGAQLVGAL--PGlGGLN--AGQ--------------MLAGGLKATILLNTEP-QWDAAAGVATlDAL 558
Cdd:cd02753 293 -SHGTDNVMALSNLALLTGNIgrPG-TGVNplRGQnnvqgacdmgalpnVLPGYVKALYIMGENPaLSDPNTNHVR-KAL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 559 GQSEMVVSLTPFKTNMA-FSDVLLPIAPFTETSGSFVNAEGRLQSFHAVVKPLGETRPAWKVLRALADILGLPGFGFDSS 637
Cdd:cd02753 370 ESLEFLVVQDIFLTETAeLADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSHPE 449
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
6-229 |
3.51e-41 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 150.19 E-value: 3.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 6 LDGKKVGIAEGSTVMHAAEKAGTYIPHFCYHKKLSIAANCRMCLVDIEKMPKPMPACATSVTQGMVVRTKTDKAVKAQQS 85
Cdd:PRK07569 8 IDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQEYRRM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 86 VMEFLLI--NHPldCPICDQGGECQLQDLAVGYGGVKSRYEEEKRVVKVKDVGPLISMqEMTRCIHCTRCVRFGQEIAGV 163
Cdd:PRK07569 88 IVELLFAegNHV--CAVCVANGNCELQDLAIEVGMDHVRFPYLFPRRPVDISHPRFGI-DHNRCVLCTRCVRVCDEIEGA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 164 MELGMSQRGEHSEIEAFVGQ---TVDSELS-GNMIDICPVGALtskpFRYSARTWELSRRKSISPHDSTG 229
Cdd:PRK07569 165 HTWDVAGRGAKSRVITDLNQpwgTSETCTScGKCVQACPTGAI----FRKGSTVGEMEKDRDKLEFLVTA 230
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
232-639 |
6.10e-27 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 116.48 E-value: 6.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 232 LIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQG----GQWNEVDWKTALEYVAHGLRNIKSE 307
Cdd:COG0243 37 LGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLYSPDRLTYPMKRVGprgsGKFERISWDEALDLIAEKLKAIIDE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 308 HGASAVGALVS----PHSTIEELYLTGALVRGLGSENIDyrlRNAEFDRtqpGARWLGMPIA-GLSTLQS---------- 372
Cdd:COG0243 117 YGPEAVAFYTSggsaGRLSNEAAYLAQRFARALGTNNLD---DNSRLCH---ESAVAGLPRTfGSDKGTVsyedlehadl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 373 VLVVGSSLRKDHPLFAQRIRQAAR-NGCAVHAVAsaapqwamPLASATVLPATEW--------VACLASIAAAVGQEKGV 443
Cdd:COG0243 191 IVLWGSNPAENHPRLLRRLREAAKkRGAKIVVID--------PRRTETAAIADEWlpirpgtdAALLLALAHVLIEEGLY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 444 --------------------------AAPQSAVvtDAALI--AAQSLLAGEHKAVLLGNGAAHHPLaaqllalanwiGEQ 495
Cdd:COG0243 263 drdflarhtvgfdelaayvaaytpewAAEITGV--PAEDIreLAREFATAKPAVILWGMGLQQHSN-----------GTQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 496 CGAsvgylteAANTVGAqLVGAL--PGlGGLNA--GQMLAGG----LKATILLNTEPQWDAAAGVATLDALGQSEMVVSL 567
Cdd:COG0243 330 TVR-------AIANLAL-LTGNIgkPG-GGPFSltGEAILDGkpypIKALWVYGGNPAVSAPDTNRVREALRKLDFVVVI 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1101172364 568 TPFKTNMA-FSDVLLPIAPFTETSGSFVNAE-GRLQSFHAVVKPLGETRPAWKVLRALADILGLP-GFGFDSSLE 639
Cdd:COG0243 401 DTFLTETArYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEeAFPWGRTEE 475
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
220-647 |
4.31e-23 |
|
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: 103.84 E-value: 4.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 220 KSISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIK-QGGQWNEVDWKTALEYVA 298
Cdd:cd02754 1 KTTCPYCGVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKGLNLHKTLNGPERLTRPLLRrNGGELVPVSWDEALDLIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 299 HGLRNIKSEHGASAVGALVSPHSTIEELYLTGALVRG-LGSENIDY--RL----------RNAEFDRtQPGarwlgmPIA 365
Cdd:cd02754 81 ERFKAIQAEYGPDSVAFYGSGQLLTEEYYAANKLAKGgLGTNNIDTnsRLcmasavagykRSFGADG-PPG------SYD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 366 GLSTLQSVLVVGSSLRKDHPLFAQRIRQAARNGCAV---------HAVASAA-------PQWAMPLAS--ATVLPATEWV 427
Cdd:cd02754 154 DIEHADCFFLIGSNMAECHPILFRRLLDRKKANPGAkiivvdprrTRTADIAdlhlpirPGTDLALLNglLHVLIEEGLI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 428 --ACLAsiAAAVGQEKGVAAPQSAVVTDAALIAAQSLLAGEHKAVLLGNGAA-----------HHPLAAQLLALANW--- 491
Cdd:cd02754 234 drDFID--AHTEGFEELKAFVADYTPEKVAEITGVPEADIREAARLFGEARKvmslwtmgvnqSTQGTAANNAIINLhla 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 492 ---IGEQcGASVGYLTEAANTVGAQLVGAL-PGLG-----------------------------GLNAGQM----LAGGL 534
Cdd:cd02754 312 tgkIGRP-GSGPFSLTGQPNAMGGREVGGLaNLLPghrsvnnpehraevakfwgvpegtippkpGLHAVEMfeaiEDGEI 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 535 KATILLNTEPqwdaAAGVATLD----ALGQSEMVVSLTPFKTN--MAFSDVLLPIAPFTETSGSFVNAEGRLQSFHAVVK 608
Cdd:cd02754 391 KALWVMCTNP----AVSLPNANrvreALERLEFVVVQDAFADTetAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVE 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1101172364 609 PLGETRPAWKVLRALADILGL-PGFGFDSSLEVL--------GRALDL 647
Cdd:cd02754 467 PPGEARPDWWILADVARRLGFgELFPYTSPEEVFeeyrrlsrGRGADL 514
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
1-76 |
2.07e-16 |
|
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.
Pssm-ID: 433268 [Multi-domain] Cd Length: 82 Bit Score: 74.50 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 1 MIEIELDGKKVGIAEGSTVMHAAEKAGTYIPHFCYHKK----LSIAANCRMCLVDIEKMPKpMPACATSVTQGMVVRTKT 76
Cdd:pfam13510 3 PVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRTQN 81
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
83-123 |
7.33e-16 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 71.46 E-value: 7.33e-16
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1101172364 83 QQSVMEFLLINHPLDCPICDQGGECQLQDLAVGYGGVKSRY 123
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
83-117 |
9.03e-16 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 71.33 E-value: 9.03e-16
10 20 30
....*....|....*....|....*....|....*
gi 1101172364 83 QQSVMEFLLINHPLDCPICDQGGECQLQDLAVGYG 117
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELG 35
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
2-109 |
1.06e-15 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 80.93 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 2 IEIELDGKKVGIAEGSTVMHAAEKAGTYIPHFCYHKKLSIAANCRMCLVDIEKMPKPMPACATSVTQGMVVRTKTDKAVK 81
Cdd:PRK12814 4 ISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETENAELHA 83
|
90 100
....*....|....*....|....*...
gi 1101172364 82 AQQSVMEFLLINHPLDCPicdqgGECQL 109
Cdd:PRK12814 84 MRRQSLERLIEQHCGDCL-----GPCEL 106
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
220-398 |
5.85e-15 |
|
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex I, the second domain of the Nad11/75-kDa subunit of some protists. NADH-quinone oxidoreductase is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. The nad11 gene codes for the largest (75-kDa) subunit of the mitochondrial NADH-quinone oxidoreductase, it constitutes the electron input part of the enzyme, or the so-called NADH dehydrogenase fragment. The Nad11 subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain (this CD), is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Although only vestigial sequence evidence remains of a molybdopterin binding site, this protein domain belongs to the molybdopterin_binding (MopB) superfamily of proteins.
Pssm-ID: 239175 [Multi-domain] Cd Length: 366 Bit Score: 77.02 E-value: 5.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 220 KSISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNAdDRLTKPMIK-QGGQWNEVDWKTALEYVA 298
Cdd:cd02774 1 ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKY-QRIKTPLLKlSNNSFLEIGWKTAFKFLN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 299 HGLRNIKSehgaSAVGALVSPHSTIEELYLTGALVRGLGSENIDYRLRNAEFDRTQPGARWL--GMPIAGLSTLQSVLVV 376
Cdd:cd02774 80 KFILLKKF----SKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFLENNNYFNLDLENYlfNNSLKNLDKSDLCLLI 155
|
170 180
....*....|....*....|..
gi 1101172364 377 GSSLRKDHPLFAQRIRQAARNG 398
Cdd:cd02774 156 GSNLRVESPILNIRLRNRYNKG 177
|
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
232-671 |
1.43e-13 |
|
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: 73.97 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 232 LIVQVKNNRVMRVVPFENEAVNECWIADRD-RFSYeALNADDRLTKPMIKQGGQWNEVDWKTALEYVAHGLRNIKSEHGA 310
Cdd:cd02762 13 LVVTVEDGRVASIRGDPDDPLSKGYICPKAaALGD-YQNDPDRLRTPMRRRGGSFEEIDWDEAFDEIAERLRAIRARHGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 311 SAVGALV---SPHSTIEELYLtGALVRGLGSENidyRLRNA-------EFDRTQPGARWLGMPIAGLSTLQSVLVVG--- 377
Cdd:cd02762 92 DAVGVYGgnpQAHTHAGGAYS-PALLKALGTSN---YFSAAtadqkpgHFWSGLMFGHPGLHPVPDIDRTDYLLILGanp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 378 ----SSLRKdHPLFAQRIRQAARNGCAVHAVAsaapqwamPLASATVLPATEWVA--------CLASIAAAVGQE----- 440
Cdd:cd02762 168 lqsnGSLRT-APDRVLRLKAAKDRGGSLVVID--------PRRTETAKLADEHLFvrpgtdawLLAAMLAVLLAEgltdr 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 441 -------KGVAAPQSAV--VTDAAL-----IAAQSL--LAGEH----KAVLLGN-GAAHHPLaaqllalanwigeqcGAS 499
Cdd:cd02762 239 rflaehcDGLDEVRAALaeFTPEAYaprcgVPAETIrrLAREFaaapSAAVYGRlGVQTQLF---------------GTL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 500 VGYLTEAANTV-------GAQL-------------------------VGALPGLGGLNAGQMLA--------GGLKATIL 539
Cdd:cd02762 304 CSWLVKLLNLLtgnldrpGGAMfttpaldlvgqtsgrtigrgewrsrVSGLPEIAGELPVNVLAeeiltdgpGRIRAMIV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 540 LNTEPQWDAAAGVATLDALGQSEMVVSLTPFKTNMA-FSDVLLP-IAPFTETSGSFVNAEGRLQSFH---AVVKPLGETR 614
Cdd:cd02762 384 VAGNPVLSAPDGARLEAALGGLEFMVSVDVYMTETTrHADYILPpASQLEKPHATFFNLEFPRNAFRyrrPLFPPPPGTL 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1101172364 615 PAWKVL----RALADILGLPGFGFDSSLEVLGRALDLPPGATVAAVDTGCLSNANATGDAD 671
Cdd:cd02762 464 PEWEILarlvEALDAVLRAGFYGERAGGTLLLAALLERPSGVDLGPLTPRLWQRLRTPDGR 524
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
220-628 |
1.97e-13 |
|
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: 73.59 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 220 KSISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQGG--QWNEVDWKTALEYV 297
Cdd:cd02752 1 RTICPYCSVGCGLIAYVQNGVWVHQEGDPDHPVNRGSLCPKGAALRDFVHSPKRLKYPMYRAPGsgKWEEISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 298 AHGLRNIKSEH------------GASAVGALVSPHSTIEELYLTGALVRGLGSENIDYRLR----------NAEFDRtqp 355
Cdd:cd02752 81 ARKMKDIRDASfveknaagvvvnRPDSIAFLGSAKLSNEECYLIRKFARALGTNNLDHQARiuhsptvaglANTFGR--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 356 GA---RWLGMPIAglstlQSVLVVGSSLRKDHPLFAQRIRQA-ARNGCAVHAV-------ASAAPQWAmPLASATVLPAT 424
Cdd:cd02752 158 GAmtnSWNDIKNA-----DVILVMGGNPAEAHPVSFKWILEAkEKNGAKLIVVdprftrtAAKADLYV-PIRSGTDIAFL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 425 EWVA--CLASIAAAVGQEKGVaaPQSAVVTDAALIAAQSlLAGEHKAVLLGNGAAHHplaaqllalanwigeqcgasvgy 502
Cdd:cd02752 232 GGMInyIIRYTPEEVEDICGV--PKEDFLKVAEMFAATG-RPDKPGTILYAMGWTQH----------------------- 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 503 lteaanTVGAQLVGALPGL-----------GGLNAgqmLAG----------GLKATIL------LNtePQWDAAAGVATL 555
Cdd:cd02752 286 ------TVGSQNIRAMCILqlllgnigvagGGVNA---LRGhsnvqgatdlGLLSHNLpgylggQN--PNSSFPNANKVR 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 556 DALGQSEMVVSLTPFKT------NMAFSDV--------LLPIAPFTETSGSFVNAEGRLQSFHAVVKPLGETRPAWKVLR 621
Cdd:cd02752 355 RALDKLDWLVVIDPFPTetaafwKNPGMDPksiqtevfLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAKSDGDILV 434
|
....*..
gi 1101172364 622 ALADILG 628
Cdd:cd02752 435 ELAKRLG 441
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
232-629 |
2.22e-13 |
|
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: 72.72 E-value: 2.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 232 LIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQG----GQWNEVDWKTALEYVAHGLRNIKSE 307
Cdd:cd02755 14 ILARVEDGRVVKIDGNPLSPLSRGKLCARGNAGIQLLYDPDRLKKPLIRVGergeGKFREASWDEALQYIASKLKEIKEQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 308 HGASAVgaLVSPHSTIEELYLTgALVRGLGSENID------YRLRNAEFDRTQPGARwlGMPIAGLSTLQSVLVVGSSLR 381
Cdd:cd02755 94 HGPESV--LFGGHGGCYSPFFK-HFAAAFGSPNIFshestcLASKNLAWKLVIDSFG--GEVNPDFENARYIILFGRNLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 382 KD-HPLFAQRIRQAARNGCAVHAV-------ASAAPQW---------AMPLASATVLPA-----TEWVA--CLASIAAAV 437
Cdd:cd02755 169 EAiIVVDARRLMKALENGAKVVVVdprfselASKADEWipikpgtdlAFVLALIHVLISenlydAAFVEkyTNGFELLKA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 438 GQEKGVAApQSAVVTDaalIAAQSL------LAGEHKAVLLGNGaaHHplaaqllalanwigeqcGASVGYLTE---AAN 508
Cdd:cd02755 249 HVKPYTPE-WAAQITD---IPADTIrriareFAAAAPHAVVDPG--WR-----------------GTFYSNSFQtrrAIA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 509 TVGAqLVGALPGLGGLNAGQMLA-GGLKATILLNTEP---QWDAAAGVATLDALgqsEMVVSLTPFKTNMA-FSDVLLPI 583
Cdd:cd02755 306 IINA-LLGNIDKRGGLYYAGSAKpYPIKALFIYRTNPfhsMPDRARLIKALKNL---DLVVAIDILPSDTAlYADVILPE 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1101172364 584 APFTETSgSFVNAEGRLQSFHA----VVKPLGETRPAWKVLRALADILGL 629
Cdd:cd02755 382 ATYLERD-EPFSDKGGPAPAVAtrqrAIEPLYDTRPGWDILKELARRLGL 430
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
232-646 |
3.51e-12 |
|
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: 69.20 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 232 LIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALNADDRLTKPMIKQG---GQWNEVDWKTALEYVAHGLRNIKSEH 308
Cdd:cd02766 14 LLVTVEDGRIVRVEGDPAHPYTRGFICAKGARYVERVYSPDRLLTPLKRVGrkgGQWERISWDEALDTIAAKLKEIKAEY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 309 GASAVgalvsphstieeLYLTGALVRGLGSENIDYRLRNA----EFDRTQP------------GARWLGMPiagLSTLQS 372
Cdd:cd02766 94 GPESI------------LPYSYAGTMGLLQRAARGRFFHAlgasELRGTICsgagieaqkydfGASLGNDP---EDMVNA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 373 VLVV--GSSLRKDHPLFAQRIRQAARNGCAV-----HAVASAApqwampLASATVL--PATEwvACLASIAAAVGQEKGv 443
Cdd:cd02766 159 DLIViwGINPAATNIHLMRIIQEARKRGAKVvvidpYRTATAA------RADLHIQirPGTD--GALALGVAKVLFREG- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 444 aapqsavVTDAALIAAQSLLAGEHKAVLLgngaAHHPlaaqllalaNWIGEQCGASVG-------YLTEAANTV------ 510
Cdd:cd02766 230 -------LYDRDFLARHTEGFEELKAHLE----TYTP---------EWAAEITGVSAEeieelarLYGEAKPPSirlgyg 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 511 ------GAQ---LVGALPGL--------GGLNAGqMLAGGLKATILLNTEP------QWDAAAGVATLDalgqsEMVVSL 567
Cdd:cd02766 290 mqryrnGGQnvrAIDALPALtgnigvpgGGAFYS-NSGPPVKALWVYNSNPvaqapdSNKVRKGLARED-----LFVVVH 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 568 TPFKTN-MAFSDVLLPIAPFTEtSGSFVNAEGR--LQSFHAVVKPLGETRPAWKVLRALADILGLPGFGF-DSSLEVLGR 643
Cdd:cd02766 364 DQFMTDtARYADIVLPATTFLE-HEDVYASYWHyyLQYNEPAIPPPGEARSNTEIFRELAKRLGFGEPPFeESDEEWLDQ 442
|
...
gi 1101172364 644 ALD 646
Cdd:cd02766 443 ALD 445
|
|
| MopB_DMSOR-like |
cd02751 |
The MopB_DMSOR-like CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
224-313 |
3.43e-08 |
|
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: 56.85 E-value: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 224 PHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIAD--RDRfsyeaLNADDRLTKPMIKQG--------------GQWNE 287
Cdd:cd02751 1 PTACHWGPFKAHVKDGVIVRVEPDDTDQPRPCPRGRsvRDR-----VYSPDRIKYPMKRVGwlgngpgsrelrgeGEFVR 75
|
90 100
....*....|....*....|....*.
gi 1101172364 288 VDWKTALEYVAHGLRNIKSEHGASAV 313
Cdd:cd02751 76 ISWDEALDLVASELKRIREKYGNEAI 101
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
2-73 |
5.88e-08 |
|
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.
Pssm-ID: 238126 [Multi-domain] Cd Length: 84 Bit Score: 50.47 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 2 IEIELDGKKVGIAEGSTVMHAAEKAGTYIPHFCYHKklsiaaNCRMCLVDIEKM----------------PKPMPACATS 65
Cdd:cd00207 3 INVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAG------ACGTCKVEVVEGevdqsdpslldeeeaeGGYVLACQTR 76
|
....*...
gi 1101172364 66 VTQGMVVR 73
Cdd:cd00207 77 VTDGLVIE 84
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
268-632 |
1.82e-07 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 54.67 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 268 LNADDRLTKPMIKQG----GQWNEVDWKTALEYVAHGLRNIKSEHGASAVgALVSPHSTIEELYLTgaLVRGLGSENIdy 343
Cdd:PRK15488 93 LYDPQRIVKPLKRVGergeGKWQEISWDEAYQEIAAKLNAIKQQHGPESV-AFSSKSGSLSSHLFH--LATAFGSPNT-- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 344 rlrnaeFdrtqpgARWLGMPIAGLSTLQSVLvvGSSLRKD-----------HPLF-------AQRIRQAARNGCA----- 400
Cdd:PRK15488 168 ------F------THASTCPAGYAIAAKVMF--GGKLKRDlanskyiinfgHNLYeginmsdTRGLMTAQMEKGAklvvf 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 401 ---VHAVASAAPQW---------AMPLA--------------------------SATVLPAT-EWVACLASIAAA----V 437
Cdd:PRK15488 234 eprFSVVASKADEWhairpgtdlAVVLAlchvlieenlydkafverytsgfeelAASVKEYTpEWAEAISDVPADdirrI 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 438 GQEKGVAAPQsAVV--------TDA------ALIAAQSL---------------------LAGEHKAVLLGN-GAAHHPL 481
Cdd:PRK15488 314 ARELAAAAPH-AIVdfghratfTPEefdmrrAIFAANVLlgnierkgglyfgknasvynkLAGEKVAPTLAKpGVKGMPK 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 482 AAQLLAlanwigEQCGASVGYLTEAANTVGAQLVGALpglgglnagQMLAGGLKATILLNTEP---QWDAAAGVATLDAL 558
Cdd:PRK15488 393 PTAKRI------DLVGEQFKYIAAGGGVVQSIIDATL---------TQKPYQIKGWVMSRHNPmqtVTDRADVVKALKKL 457
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1101172364 559 gqsEMVVSLTPFKTNMA-FSDVLLPIAPFTETSGSFVNAEGRLQSF---HAVVKPLGETRPAWKVLRALADILGLPGF 632
Cdd:PRK15488 458 ---DLVVVCDVYLSESAaYADVVLPESTYLERDEEISDKSGKNPAYalrQRVVEPIGDTKPSWQIFKELGEKMGLGQY 532
|
|
| MopB_Arsenate-R |
cd02757 |
This CD includes the respiratory arsenate reductase, As(V), catalytic subunit (ArrA) and other ... |
514-632 |
3.46e-07 |
|
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: 53.60 E-value: 3.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 514 LVGALPGLGGLNAGqMLAGGLKATILLNTEPQWDAAAGVATLDALGQSEMVVSLTPFKTNMA-FSDVLLPIAPFTETSG- 591
Cdd:cd02757 340 LVGSIDSKGGLCPN-MGVPKIKVYFTYLDNPVFSNPDGMSWEEALAKIPFHVHLSPFMSETTyFADIVLPDGHHFERWDv 418
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1101172364 592 -SFVNAEGRLQSFH-AVVKPLGETRPAWKVLRALADILGLPGF 632
Cdd:cd02757 419 mSQENNLHPWLSIRqPVVKSLGEVREETEILIELAKKLDPKGS 461
|
|
| MopB_PHLH |
cd02764 |
The MopB_PHLH CD includes a group of related uncharacterized putative hydrogenase-like ... |
435-625 |
2.32e-06 |
|
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: 50.95 E-value: 2.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 435 AAVGQEKGVAAPQSAVVTDAALIAAQSLLAGEHKAVLLGNGAAHHPLAAQLLALANWIGEQCGASVGYLTEAANTVGAQL 514
Cdd:cd02764 287 ALNLAFKPAKVAELTVDLDKALAALAKALAAAGKSLVVAGSELSQTAGADTQVAVNALNSLLGNDGKTVDHARPIKGGEL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 515 vgALPGLGGLNAGQMLAGGLKATILLNTEPQWDAAAGVATLDALGQSEMVVSLTPFKTNMA-FSDVLLPIAPFTETSGSF 593
Cdd:cd02764 367 --GNQQDLKALASRINAGKVSALLVYDVNPVYDLPQGLGFAKALEKVPLSVSFGDRLDETAmLCDWVAPMSHGLESWGDA 444
|
170 180 190
....*....|....*....|....*....|..
gi 1101172364 594 VNAEGRLQSFHAVVKPLGETRPAWKVLRALAD 625
Cdd:cd02764 445 ETPDGTYSICQPVIAPLFDTRSAQESLLLALG 476
|
|
| MopB_DMSOR-BSOR-TMAOR |
cd02769 |
The MopB_DMSOR-BSOR-TMAOR CD contains dimethylsulfoxide reductase (DMSOR), biotin sulfoxide ... |
234-313 |
1.53e-04 |
|
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: 44.95 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 234 VQVKNNRVMRVVPFENEAV-NECWIADRDrfsyeALNADDRLTKPMIKQG---------------GQWNEVDWKTALEYV 297
Cdd:cd02769 11 ARVKDGRIVGVRPFEEDPDpSPLLDGVPD-----AVYSPTRIKYPMVRRGwlekgpgsdrslrgkEEFVRVSWDEALDLV 85
|
90
....*....|....*.
gi 1101172364 298 AHGLRNIKSEHGASAV 313
Cdd:cd02769 86 AAELKRVRKTYGNEAI 101
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
58-205 |
1.85e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 44.63 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 58 PMPACATSVTQGMVVRTKTDKAVKAQQSVMEFLLINHPLDCPICDQGGECQLQDLAVGYGGVKSRYEEEKRVVKVKDVGP 137
Cdd:COG4624 5 LRACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGP 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 138 lISMQEMTRCIHCTRCVRFGQEIAgvmelgMSQRGEHSEIeafvgqtVDSE--LSGNMIDICPVGALTSK 205
Cdd:COG4624 85 -SIIRDKEKCKNCYPCVRACPVKA------IKVDDGKAEI-------DEEKciSCGQCVAVCPFGAITEK 140
|
|
| Molybdop_Fe4S4 |
smart00926 |
Molybdopterin oxidoreductase Fe4S4 domain; The molybdopterin oxidoreductase Fe4S4 domain is ... |
220-269 |
5.00e-04 |
|
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: 38.38 E-value: 5.00e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1101172364 220 KSISPHDSTGANLIVQVKNNRVMRVVPFENEAVNECWIADRDRFSYEALN 269
Cdd:smart00926 5 PTVCPLCGVGCGLLVEVKDGRVVRVRGDPDHPVNRGRLCPKGRAGLEQVY 54
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
272-342 |
6.09e-04 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 43.35 E-value: 6.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1101172364 272 DRLTKPMI--KQG-----GQWNEVDWKTALEYVAHGLRNIKSEHGASAVGALVSPHSTIEELYLTGALVR-GLGSENID 342
Cdd:PRK13532 96 DRLTQPLLrmKDGkydkeGEFTPVSWDQAFDVMAEKFKKALKEKGPTAVGMFGSGQWTIWEGYAASKLMKaGFRSNNID 174
|
|
| MopB_2 |
cd02763 |
The MopB_2 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
552-632 |
3.14e-03 |
|
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: 40.97 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1101172364 552 VATLDALgQSEMVvsltpfktnmAFSDVLLPIAPFTETSGSFV-------NAEGRLQSF-HAVVKPLGETRPAWKVLRAL 623
Cdd:cd02763 461 IIVCDAF-YSEMV----------AFADLVLPDTTYLERHDAMSlldrpisEADGPVDAIrVPIVEPKGDVKPFQEVLIEL 529
|
....*....
gi 1101172364 624 ADILGLPGF 632
Cdd:cd02763 530 GTRLGLPGF 538
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
4-52 |
3.95e-03 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 36.73 E-value: 3.95e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1101172364 4 IELDGKKVGI---AEGSTVMHAAEKAGTYIPHFCYHkklsiaANCRMCLVDI 52
Cdd:pfam00111 1 VTINGKGVTIevpDGETTLLDAAEEAGIDIPYSCRG------GGCGTCAVKV 46
|
|
| |
