|
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 ... |
42-623 |
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: 814.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 42 VTVNGQEVHVPKGVTVLYACEQAGVDVPRFCYHHKLSIAGNCRMCLVEVEKSPKPVASCAMPVMPGMNIKTTTDLVKKAR 121
Cdd:TIGR01973 1 IFIDGKELEVPKGTTVLQACLSAGIEIPRFCYHEKLSIAGNCRMCLVEVEKFPKPVASCATPVTDGMKISTNSEKVKKAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 122 EGVMEFLLINHPLDCPICDQGGECELQDQSYIFGSDRSRFTEYKRAVEDKELGPLVKTVMTRCIHCTRCVRFSTEIAGVQ 201
Cdd:TIGR01973 81 EGVMEFLLINHPLDCPICDQGGECDLQDQAVMYGSDRSRFREKKRTVENKYLGPLIKTEMTRCIHCTRCVRFANEVAGVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 202 DMGITGRGNQAEVGTYISKLLASELSGNVIDLCPVGALTSKPFAFTARSWELEGTPSIDVTDGLGSNIRVDTRGNEVMRI 281
Cdd:TIGR01973 161 DLGVIGRGNNVEIGTYEGKTLESELSGNLIDICPVGALTSKPYAFKARPWELKSTPSICVHDSVGCNIRVDERNGEIMRI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 282 VPRANEEVNEEWISDKARFSYDALKRQ-RLDRPMVRGSDGKLQETSWEFALDYVAEKLKATEpdAIRAVAGKLCDAESMI 360
Cdd:TIGR01973 241 LPRENDEINEEWLCDKGRFGYDGLNRQdRLTKPLLRNQEGNLLEVSWAEALAIAAEKLKASS--RIGGIAGPRSSLEELF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 361 SLKDMMNKLGASHTT--PEGMANVSADVRSSYLFNSNLVGVEDADYVLLIGTNPRTEAPVLNVRLRRAVIAGGATVTSVG 438
Cdd:TIGR01973 319 ALKKLVRKLGSENFDlrIRNYEFESADLRANYLFNTTLADIEEADLVLLVGADLRQEAPLLNLRLRKAVKKGGAKVALIG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 439 PN-ADLSYPST-----HLGDTTATLEEITSGKHA-VCEAIKAANNPMVIVGSELLRRADSKILLKKIHAMCDELGVVKGD 511
Cdd:TIGR01973 399 IEkWNLTYPANtnlvfHPGLSPKKLDDIASGAHSdIAAALKAAKKPLIIVGDSAISHLDGAALISAAANIAKVIKVRRKE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 512 WNGFNVLHDAGGTVGALDIGFVP--GTSASNDVPAKLVYSLGAEEFDAP----------AGAFIVYQGHHGAQGASKADV 579
Cdd:TIGR01973 479 WNGLNILSSGANSVGLLDLGGEStgLDAALNLGAADALFLLGADLERALdktardalskADAFIIYQGHHGTETAEKADV 558
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1275574916 580 ILPGAAYTEKTGTYVNTEGRAQVAVASMGPVGQAKEDWRILRAL 623
Cdd:TIGR01973 559 ILPGAAFTEKSGTYVNLEGRAQRFEQAVKPPGEAREDWRILRAL 602
|
|
| NuoG |
COG1034 |
NADH dehydrogenase/NADH:ubiquinone oxidoreductase 75 kD subunit (chain G) [Energy production ... |
39-649 |
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: 628.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 39 TVPVTVNGQEVHVPKGVTVLYACEQAGVDVPRFCYHHKLSIAGNCRMCLVEVEKSPKPVASCAMPVMPGMNIKTTTDLVK 118
Cdd:COG1034 1 MVTITIDGKEVEVPKGTTVLQAAEKAGIEIPRFCYHPKLSIAGACRMCLVEVEGAPKPVASCATPVTDGMVVKTDSPKVK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 119 KAREGVMEFLLINHPLDCPICDQGGECELQDQSYIFGSDRSRFTEYKRAVEDKELGPLVKTVMTRCIHCTRCVRFSTEIA 198
Cdd:COG1034 81 KARKGVMEFLLINHPLDCPICDQGGECDLQDQAMEYGVDESRYEEEKRTVPKKDLGPLILLDMNRCILCTRCVRFCDEIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 199 GVQDMGITGRGNQAEVGTYISKLLASELSGNVIDLCPVGALTSKPFAFTARSWELEGTPSIDVTDGLGSNIRVDTRGNEV 278
Cdd:COG1034 161 GDPELGVIGRGEHSEIGTYLGKPLDSEFSGNCIDVCPVGALTSKPFRFKARPWELKKTPSICPHCSVGCNIRVDVRGGKV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 279 MRIVPRANEEVNEEWISDKARFSYDALKR-QRLDRPMVRGsDGKLQETSWEFALDYVAEKLKAtepdairavagkLCDAE 357
Cdd:COG1034 241 YRVLPRENEAVNEEWLCDKGRFGYDGLNSpDRLTRPLVRK-DGELVEASWEEALAAAAEGLKA------------LKKAE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 358 smislkdmmnklgashttpegmanvsadvrssylfnsNLVGVEDAdyvlligtnprteapvlnvrlrraviagGAtvtsv 437
Cdd:COG1034 308 -------------------------------------NSVGAALL----------------------------GA----- 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 438 gpnadlsypsthLGDTTATLEEITSGKhavceaIKAAnnpmVIVGSELLRradskillkkihamcdelgvvkgdwngfnv 517
Cdd:COG1034 318 ------------LPDAAAILEAAEAGK------LKAL----VLLGADPYD------------------------------ 345
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 518 lHDAGGTVGALDigfvpgtsasndvpaklvyslgaeefdapAGAFIVYQGHHGAQGASKADVILPGAAYTEKTGTYVNTE 597
Cdd:COG1034 346 -LDPAAALAALA-----------------------------KADFVVVLDHFGSATAERADVVLPAAAFAEKSGTFVNLE 395
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1275574916 598 GRAQVAVASMGPVGQAKEDWRILRALSEFAGVPLPYNTHEQVHRRLAEVAPH 649
Cdd:COG1034 396 GRVQRFNAAVPPPGEARPDWRVLRALANALGAGLPYDSLEEVRAELAAEAPA 447
|
|
| MopB_Res-Cmplx1_Nad11 |
cd02773 |
MopB_Res_Cmplx1_Nad11: The second domain of the Nad11/75-kDa subunit of the NADH-quinone ... |
258-625 |
0e+00 |
|
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: 558.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 258 SIDVTDGLGSNIRVDTRGNEVMRIVPRANEEVNEEWISDKARFSYDALKRQRLDRPMVRGSdGKLQETSWEFALDYVAEK 337
Cdd:cd02773 2 SIDVLDAVGSNIRVDTRGGEVMRILPRLNEDINEEWISDKTRFAYDGLKRQRLDKPYIRKN-GKLKPATWEEALAAIAKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 338 LKATEPDAIRAVAGKLCDAESMISLKDMMNKLGASH-TTPEGMANVSADVRSSYLFNSNLVGVEDADYVLLIGTNPRTEA 416
Cdd:cd02773 81 LKGVKPDEIAAIAGDLADVESMVALKDLLNKLGSENlACEQDGPDLPADLRSNYLFNTTIAGIEEADAVLLVGTNPRFEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 417 PVLNVRLRRAVIAGGATVTSVGPNADLSYPSTHLGDTTATLEEITSGKHAVCEAIKAANNPMVIVGSELLRRADSKILLK 496
Cdd:cd02773 161 PVLNARIRKAWLHGGLKVGVIGPPVDLTYDYDHLGTDAKTLQDIASGKHPFSKALKDAKKPMIIVGSGALARKDGAAILA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 497 KIHAMCDELGVVKGDWNGFNVLHDAGGTVGALDIGFVPGTSASNDV-PAKLVYSLGAEEFD---APAGAFIVYQGHHGAQ 572
Cdd:cd02773 241 AVAKLAKKNGVVREGWNGFNVLHRAASRVGALDLGFVPGAGAIRKSgPPKVLYLLGADEIDitpIPKDAFVVYQGHHGDR 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1275574916 573 GASKADVILPGAAYTEKTGTYVNTEGRAQVAVASMGPVGQAKEDWRILRALSE 625
Cdd:cd02773 321 GAQIADVILPGAAYTEKSGTYVNTEGRVQQTRKAVSPPGDAREDWKILRALSE 373
|
|
| MopB_NADH-Q-OR-NuoG2 |
cd02768 |
MopB_NADH-Q-OR-NuoG2: The NuoG/Nad11/75-kDa subunit (second domain) of the NADH-quinone ... |
257-626 |
6.80e-148 |
|
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: 435.94 E-value: 6.80e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 257 PSIDVTDGLGSNIRVDTRGNEVMRIVPRANEEVNEEWISDKARFSYDALK-RQRLDRPMVRGsDGKLQETSWEFALDYVA 335
Cdd:cd02768 1 ESIDVHDALGSNIRVDVRGGEVMRILPRENEAINEEWISDKGRFGYDGLNsRQRLTQPLIKK-GGKLVPVSWEEALKTVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 336 EKLKATEPDAIRAVAGKLCDAESMISLKDMMNKLGASHTTPEG---MANVSADVRSSYLFNSNLVGVEDADYVLLIGTNP 412
Cdd:cd02768 80 EGLKAVKGDKIGGIAGPRADLESLFLLKKLLNKLGSNNIDHRLrqsDLPADNRLRGNYLFNTSIAEIEEADAVLLIGSNL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 413 RTEAPVLNVRLRRAVIAGGATVTSVGP-----NADLSYPSTHLGDTTATLEEITSGKH--AVCEAIKAANNPMVIVGSEL 485
Cdd:cd02768 160 RKEAPLLNARLRKAVKKKGAKIAVIGPkdtdlIADLTYPVSPLGASLATLLDIAEGKHlkPFAKSLKKAKKPLIILGSSA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 486 LrRADSKILLKKIHAMCDELGVVKGDWNGFNVLHDAGGTVGA--LDIGFVPGTSASNDvpaklVYSLGAEEFD------- 556
Cdd:cd02768 240 L-RKDGAAILKALANLAAKLGTGAGLWNGLNVLNSVGARLGGagLDAGLALLEPGKAK-----LLLLGEDELDrsnppaa 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1275574916 557 ---APAGAFIVYQGHHGAQGAsKADVILPGAAYTEKTGTYVNTEGRAQVAVASMGPVGQAKEDWRILRALSEF 626
Cdd:cd02768 314 valAAADAFVVYQGHHGDTGA-QADVILPAAAFTEKSGTYVNTEGRVQRFKKAVSPPGDAREDWKILRALSNL 385
|
|
| PRK07860 |
PRK07860 |
NADH dehydrogenase subunit G; Validated |
37-648 |
3.29e-120 |
|
NADH dehydrogenase subunit G; Validated
Pssm-ID: 236118 [Multi-domain] Cd Length: 797 Bit Score: 378.52 E-value: 3.29e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 37 PDTVPVTVNGQEVHVPKGVTVLYACEQAGVDVPRFCYHHKLSIAGNCRMCLVEVEKSPKPVASCAMPVMPGMNIKT--TT 114
Cdd:PRK07860 2 PDLVTLTIDGVEVSVPKGTLVIRAAELLGIQIPRFCDHPLLDPVGACRQCLVEVEGQRKPQASCTTTVTDGMVVKTqlTS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 115 DLVKKAREGVMEFLLINHPLDCPICDQGGECELQDQSYIFGSDRSRFTEYKRAVE-----------DKElgplvktvmtR 183
Cdd:PRK07860 82 PVADKAQHGVMELLLINHPLDCPVCDKGGECPLQNQAMSNGRAESRFTDVKRTFPkpinistqvllDRE----------R 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 184 CIHCTRCVRFSTEIAGVQDMGITGRGNQAEVGTYISKLLASELSGNVIDLCPVGALTSKPFAFTARSWELEGTPSIDVTD 263
Cdd:PRK07860 152 CVLCARCTRFSDQIAGDPFIDLQERGALQQVGIYEGEPFQSYFSGNTVQICPVGALTGAAYRFRARPFDLVSTPSVCEHC 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 264 GLGSNIRVDTRGNEVMRIVPRANEEVNEEWISDKARFSYD-ALKRQRLDRPMVRGSDGKLQETSWEFALDYVAEKLKATE 342
Cdd:PRK07860 232 ASGCAQRTDHRRGKVLRRLAGDDPEVNEEWNCDKGRWAFTyATQPDRITTPLVRDEDGELEPASWSEALAVAARGLAAAR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 343 PDAIRAVAGKLC--DAESMISLKDMMnkLGAS--------HTTPEG--MANVSADVRSSYLFNSnlvgVEDADYVLLIGT 410
Cdd:PRK07860 312 GRVGVLVGGRLTveDAYAYAKFARVA--LGTNdidfrarpHSAEEAdfLAARVAGRGLGVTYAD----LEKAPAVLLVGF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 411 NPRTEAPVLNVRLRRAVIAGGATVTSVGPNADLSYPSTH-------LGDTTATLEEITSGKHAVCEAIkAANNPMVIVGS 483
Cdd:PRK07860 386 EPEEESPIVFLRLRKAARKHGLKVYSIAPFATRGLEKMGgtllrtaPGGEAAALDALATGAPDVAELL-RTPGAVILVGE 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 484 ellRRADSKILLKKIHAMCDELGvVKGDWngfnVLHDAgGTVGALDIGFVPG---------------------------- 535
Cdd:PRK07860 465 ---RLATVPGALSAAARLADATG-ARLAW----VPRRA-GERGALEAGALPTllpggrpvadpaaraevaaawgvdelpa 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 536 -----------TSASNDVPAKLVYSLGAEEFDAPAGA--------FIV-YQGHHGAQgASKADVILPGAAYTEKTGTYVN 595
Cdd:PRK07860 536 apgrdtagilaAAAAGELGALLVGGVEPADLPDPAAAlaaldaagFVVsLELRHSAV-TERADVVLPVAPVAEKAGTFLN 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1275574916 596 TEGRAQVAVASMGPVGqAKEDWRILRALSEFAGVPLPYNTHEQVHRRLAEVAP 648
Cdd:PRK07860 615 WEGRLRPFEAALRTTG-ALSDLRVLDALADEMGVDLGLPTVAAARAELARLGA 666
|
|
| Molybdopterin |
pfam00384 |
Molybdopterin oxidoreductase; |
309-625 |
9.08e-105 |
|
Molybdopterin oxidoreductase;
Pssm-ID: 395308 [Multi-domain] Cd Length: 359 Bit Score: 323.97 E-value: 9.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 309 RLDRPMVRGSDGKLQETSWEFALDYVAEKLKATEPD------AIRAVAGKLCDAESMISLKDMMNKLGASHTTPEG---- 378
Cdd:pfam00384 1 RLKYPMVRRGDGKFVRVSWDEALDLIAKKLKRIIKKygpdaiAINGGSGGLTDVESLYALKKLLNRLGSKNGNTEDhngd 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 379 -----MANVSADVRSSYLFNSNLVGVEDADYVLLIGTNPRTEAPVLNVRLRRAVIAGGATVTSVGPNADLSYPSTHLGDT 453
Cdd:pfam00384 81 lctaaAAAFGSDLRSNYLFNSSIADIENADLILLIGTNPREEAPILNARIRKAALKGKAKVIVIGPRLDLTYADEHLGIK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 454 TATLEEIT-SGKHAVCEAIKAAN----NPMVIVGSELLRRADSKILLKKIHAMCDELGVVK---GDWNGFNVLHDAGGTV 525
Cdd:pfam00384 161 PGTDLALAlAGAHVFIKELKKDKdfapKPIIIVGAGVLQRQDGEAIFRAIANLADLTGNIGrpgGGWNGLNILQGAASPV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 526 GALDIGFVPG------TSASNDVPAKLVYSLGAEEF------------DAPAGAFIVYQGHHGAQGASKADVILPGAAYT 587
Cdd:pfam00384 241 GALDLGLVPGiksvemINAIKKGGIKVLYLLGNNPFvthadenrvvkaLQKLDLFVVYDGHHGDKTAKYADVILPAAAYT 320
|
330 340 350
....*....|....*....|....*....|....*...
gi 1275574916 588 EKTGTYVNTEGRAQVAVASMGPVGQAKEDWRILRALSE 625
Cdd:pfam00384 321 EKNGTYVNTEGRVQSTKQAVPPPGEAREDWKILRALSE 358
|
|
| MopB_Res-Cmplx1_Nad11-M |
cd02774 |
MopB_Res_Cmplx1_Nad11_M: Mitochondrial-encoded NADH-quinone oxidoreductase/respiratory complex ... |
257-626 |
2.54e-78 |
|
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: 254.98 E-value: 2.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 257 PSIDVTDGLGSNIRVDTRGNEVMRIVPRANEEVNEEWISDKARFSYDALKRQRLDRPMVRGSDGKLQETSWEFALDYVAE 336
Cdd:cd02774 1 ESIDVLDSLGSNIRVDIKGNEILRILPKINDELNEEWISDKIRFSYDSLKYQRIKTPLLKLSNNSFLEIGWKTAFKFLNK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 337 KLKATEPDAIRAVAGKLCDAESMISLKDMMNKLGASHTTPEGM---ANVSADVRSSYLFNSNLVGVEDADYVLLIGTNPR 413
Cdd:cd02774 81 FILLKKFSKLNFIIGSKIDLETLFYYKKLLNKLGSLNTNSNNFlenNNYFNLDLENYLFNNSLKNLDKSDLCLLIGSNLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 414 TEAPVLNVRLRRAVIAGGATVTSVGPNADLSYPSTHLGDTTATLEEITSGKHAVCEAIKAANNPMVIVGSELLRRADSKI 493
Cdd:cd02774 161 VESPILNIRLRNRYNKGNKKIFVIGNKFDTTYPSKHIGLSLNTLLKILEGKHLFCKQLKKSKKPLIIIGSSFSLRKNYSF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 494 LLKKIHAMcdeLGVVKGDWNGFNVLHDAGGTVGALDIGFVPGTSASNdvpaklVYSLGAEEFDAP-AGAFIVYQGHHGAQ 572
Cdd:cd02774 241 IISKLKNF---SSNNENNFNFLNIISNSLYYLGIKKFNSNNKKNLSN------LYYIKETNFQKFnKNNFVIYQGHHFLN 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1275574916 573 GASKADVILPGAAYTEKTGTYVNTEGRAQVAVASMGPVGQAKEDWRILRALSEF 626
Cdd:cd02774 312 LANNSNLILPSKTFFEKEALYLNLEGILQKTKKILSFKENIKSDDNIIFSLILF 365
|
|
| Molybdopterin-Binding |
cd00368 |
Molybdopterin-Binding (MopB) domain of the MopB superfamily of proteins, a large, diverse, ... |
257-625 |
2.27e-68 |
|
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: 229.14 E-value: 2.27e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 257 PSIDVTDGLGSNIRVDTRGNEVMRIVPRANEEVNEEWISDKARFSYDALK-RQRLDRPMVR-GSDGKLQETSWEFALDYV 334
Cdd:cd00368 1 PSVCPFCGVGCGILVYVKDGKVVRIEGDPNHPVNEGRLCDKGRAGLDGLYsPDRLKYPLIRvGGRGKFVPISWDEALDEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 335 AEKLKAT----EPDAIRAVAGKLCDAESMISLKDMMNKLGASHTTPEGM-----ANVSADVRSSYLFNSNLVGVEDADYV 405
Cdd:cd00368 81 AEKLKEIrekyGPDAIAFYGGGGASNEEAYLLQKLLRALGSNNVDSHARlchasAVAALKAFGGGAPTNTLADIENADLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 406 LLIGTNPRTEAPVLNVRLRRAViAGGATVTSVGP-------NADLSYPstHLGDTTATL------EEITSGK----HAVC 468
Cdd:cd00368 161 LLWGSNPAETHPVLAARLRRAK-KRGAKLIVIDPrrtetaaKADEWLP--IRPGTDAALalaewaAEITGVPaetiRALA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 469 EAIKAANNPMVIVGSELLRRADSkillkkihamcdELGVvkgdWNGFNvLHDAGGTVGALDIGFVPGTS--ASNDVPAKL 546
Cdd:cd00368 238 REFAAAKRAVILWGMGLTQHTNG------------TQNV----RAIAN-LAALTGNIGRPGGGLGPGGNplVSAPDANRV 300
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1275574916 547 VYSLGAEEFdapagaFIVYQGHHGAQGAsKADVILPGAAYTEKTGTYVNTEGRAQVAVASMGPVGQAKEDWRILRALSE 625
Cdd:cd00368 301 RAALKKLDF------VVVIDIFMTETAA-YADVVLPAATYLEKEGTYTNTEGRVQLFRQAVEPPGEARSDWEILRELAK 372
|
|
| PTZ00305 |
PTZ00305 |
NADH:ubiquinone oxidoreductase; Provisional |
20-239 |
2.92e-62 |
|
NADH:ubiquinone oxidoreductase; Provisional
Pssm-ID: 140326 [Multi-domain] Cd Length: 297 Bit Score: 210.28 E-value: 2.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 20 GARAGAMRAMSAEAAPNPDTVPVTVNGQEVHV-PKGVTVLYACEQAGVDVPRFCYHHKLSIAGNCRMCLVEVEKSPKPVA 98
Cdd:PTZ00305 49 GVEAAAEGVAAGQYAEHKPRAIMFVNKRPVEIiPQEENLLEVLEREGIRVPKFCYHPILSVAGNCRMCLVQVDGTQNLVV 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 99 SCAMPVMPGMNIKTTTDLVKKAREGVMEFLLINHPLDCPICDQGGECELQDQSYIFGSDRSRFTEYKRAVEDKELGPLVK 178
Cdd:PTZ00305 129 SCATVALPGMSIITDSRLVRDAREGNVELILINHPNDCPICEQATNCDLQNVSMNYGTDIPRYKEDKRAVQDFYFDPQTR 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1275574916 179 TVMTRCIHCTRCVRFSTEIAGVQDMGITGRGNQAEVGTYISKL-LASELSGNVIDLCPVGAL 239
Cdd:PTZ00305 209 VVLNRCIHCTRCVRFLNEHAQDFNLGMIGRGGLSEISTFLDELeVKTDNNMPVSQLCPVGKL 270
|
|
| MopB_NDH-1_NuoG2 |
cd02772 |
MopB_NDH-1_NuoG2: The second domain of the NuoG subunit of the NADH-quinone oxidoreductase ... |
257-623 |
6.75e-61 |
|
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: 210.29 E-value: 6.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 257 PSIDVTDGLGSNIRVDTRGNEVMRIVPRANEEVNEEWISDKARFSYDALKRQ-RLDRPMVRGsDGKLQETSWEFALDYVA 335
Cdd:cd02772 1 KSVSPHDALGSNLVVHVKNNKVMRVVPRENEAINECWLSDRDRFSYEGLNSEdRLTKPMIKK-DGQWQEVDWETALEYVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 336 EKLKAT----EPDAIRAVAGKLCDAESMISLKDMMNKLGaSHttpegmaNVSADVRSS-----------YLFNSNLVGVE 400
Cdd:cd02772 80 EGLSAIikkhGADQIGALASPHSTLEELYLLQKLARGLG-SD-------NIDHRLRQSdfrddakasgaPWLGMPIAEIS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 401 DADYVLLIGTNPRTEAPVLNVRLRRAViAGGATVTSVGPNA-DLSYPSTH------------LGDTTATLEEITS----- 462
Cdd:cd02772 152 ELDRVLVIGSNLRKEHPLLAQRLRQAV-KKGAKLSAINPADdDFLFPLSGkaivapsalanaLAQVAKALAEEKGlavpd 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 463 ---------GKHAVCEAIKAANNPMVIVGSELLRRADSkillKKIHAMCDELGVVKGdwNGFNVLHDAGGTVGALDIGFV 533
Cdd:cd02772 231 edakveaseEARKIAASLVSAERAAVFLGNLAQNHPQA----ATLRALAQEIAKLTG--ATLGVLGEGANSVGAYLAGAL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 534 PGTS------ASNDVPAKLVysLGAE-EFDA--PAGA--------FIVYQGHHGAQGA-SKADVILPGAAYTEKTGTYVN 595
Cdd:cd02772 305 PHGGlnaaamLEQPRKAYLL--LNVEpELDCanPAQAlaalnqaeFVVALSAFASAALlDYADVLLPIAPFTETSGTFVN 382
|
410 420
....*....|....*....|....*...
gi 1275574916 596 TEGRAQVAVASMGPVGQAKEDWRILRAL 623
Cdd:cd02772 383 LEGRVQSFKGVVKPLGEARPAWKVLRVL 410
|
|
| 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 ... |
257-647 |
1.11e-39 |
|
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: 152.54 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 257 PSIDVTDGLGSNIRVDTRGNEVMRIVPRANEEVNEEWISDKARFSYDALK-RQRLDRPMVRGsDGKLQETSWEFALDYVA 335
Cdd:cd02771 1 PSICHHCSVGCNISLGERYGELRRVENRYNGAVNHYFLCDRGRFGYGYVNsRDRLTQPLIRR-GGTLVPVSWNEALDVAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 336 EKLKATEPDAIRAVAGKLCDaESMISLKDMMNK-LGASHTTPEGMANVSADVRSSYLFNSNLVGVEDADYVLLIGTNPRT 414
Cdd:cd02771 80 ARLKEAKDKVGGIGSPRASN-ESNYALQKLVGAvLGTNNVDHRARRLIAEILRNGPIYIPSLRDIESADAVLVLGEDLTQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 415 EAPVLNVRLRRAV-----------------------IAG---------GATVTSVGPNADLSY---PSTHLGDTTATLEE 459
Cdd:cd02771 159 TAPRIALALRQAArrkavelaalsgipkwqdaavrnIAQgaksplfivNALATRLDDIAAESIrasPGGQARLGAALARA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 460 ITSGKHAVC------------EAIKAANNPMVIVGSELLRRADSK------ILLKKIHAMCDELGVVKgdwngfnvlhdA 521
Cdd:cd02771 239 VDASAAGVSglapkekaariaARLTGAKKPLIVSGTLSGSLELIKaaanlaKALKRRGENAGLTLAVE-----------E 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 522 GGTVGALDIG---FVPGTS------ASNDVPAKLVYSLGAE--------EFDAPAGA--FIVYQGHHGAQGASKADVILP 582
Cdd:cd02771 308 GNSPGLLLLGghvTEPGLDldgalaALEDGSADALIVLGNDlyrsaperRVEAALDAaeFVVVLDHFLTETAERADVVLP 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1275574916 583 GAAYTEKTGTYVNTEGRAQ-VAVASMGPVGQAKEDWRILRALSEFAGVPLPYNTHEQVHRRLAEVA 647
Cdd:cd02771 388 AASFAEKSGTFVNYEGRAQrFFKAYDDPAGDARSDWRWLHALAAKLGGKLVPSDAAILDEIIALVP 453
|
|
| PRK08493 |
PRK08493 |
NADH-quinone oxidoreductase subunit G; |
42-427 |
1.14e-38 |
|
NADH-quinone oxidoreductase subunit G;
Pssm-ID: 236277 [Multi-domain] Cd Length: 819 Bit Score: 153.71 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 42 VTVNGQEVHVPKGVTVLYACEQAGVDVPRFCYHHKLSIAGNCRMCLVEVekSPKPVASCAMPVMPGMNIKTTTDLVKKAR 121
Cdd:PRK08493 4 ITINGKECEAQEGEYILNVARRNGIFIPAICYLSGCSPTLACRLCMVEA--DGKRVYSCNTKAKEGMNILTNTPNLMDER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 122 EGVMEFLLINHPLDCPICDQGGECELQDQSYifgsdRSRFTEYKRAVEDKeLGPLVKTVMTR-----CIHCTRCVRFSTE 196
Cdd:PRK08493 82 NAIMQTYDVNHPLECGVCDKSGECELQNFTH-----EMGVNHQPYAIKDT-HKPHKHWGKINydpslCIVCERCVTVCKD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 197 IAGVQDMGITGRGNQA--------------EVGTYISKLLASELSGNVID---------LCPVGALTSKPFAFTARSWEL 253
Cdd:PRK08493 156 KIGESALKTVPRGLDApdksfkesmpkdayAVWSKKQKSLIGPVGGETLDcsfcgeciaVCPVGALSSSDFQYTSNAWEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 254 EGTPSIDVTDGLGSNIRVDTR----GNEVMRIVpRANEEVNEEWISDKARFSYDALKRQRLDrpmvrgsdgklqetswEF 329
Cdd:PRK08493 236 KKIPATCPHCSDCCLIYYDVKhssiLNQESKIY-RVSNDFYFNPLCGAGRFAFDFQNEADKD----------------EK 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 330 ALDYVAEKLKatEPDAIRaVAGKLCDAESMIsLKDMMNKLGASHTTPEG------MANVSADVRSSYlfNSNLVGVEDAD 403
Cdd:PRK08493 299 AFKEAVEAFK--EAKAIK-FNSFITNEEALI-LQRLKKKFGLKLINEEAlkfqqfLKVFSEVSGKSY--SANLEDIKTSD 372
|
410 420
....*....|....*....|....
gi 1275574916 404 YVLLIGTNPRTEAPVLNVRLRRAV 427
Cdd:PRK08493 373 FVVVAGSALKTDNPLLRYAINNAL 396
|
|
| PRK07569 |
PRK07569 |
bidirectional hydrogenase complex protein HoxU; Validated |
43-242 |
1.43e-36 |
|
bidirectional hydrogenase complex protein HoxU; Validated
Pssm-ID: 181037 [Multi-domain] Cd Length: 234 Bit Score: 137.09 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 43 TVNGQEVHVPKGVTVLYACEQAGVDVPRFCYHHKLSIAGNCRMCLVEVEKSPKPVASCAMPVMPGMNIKTTTDLVKKARE 122
Cdd:PRK07569 7 TIDDQLVSAREGETLLEAAREAGIPIPTLCHLDGLSDVGACRLCLVEIEGSNKLLPACVTPVAEGMVVQTNTPRLQEYRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 123 GVMEFLLI--NHPldCPICDQGGECELQDQSYIFGSDRSRFtEY---KRAVEDKElgPLVKTVMTRCIHCTRCVRFSTEI 197
Cdd:PRK07569 87 MIVELLFAegNHV--CAVCVANGNCELQDLAIEVGMDHVRF-PYlfpRRPVDISH--PRFGIDHNRCVLCTRCVRVCDEI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1275574916 198 AGVQDMGITGRGNQAEVGTYISKLLASELS----GNVIDLCPVGALTSK 242
Cdd:PRK07569 162 EGAHTWDVAGRGAKSRVITDLNQPWGTSETctscGKCVQACPTGAIFRK 210
|
|
| YjgC |
COG3383 |
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only]; |
264-651 |
8.15e-34 |
|
Predicted molibdopterin-dependent oxidoreductase YjgC [General function prediction only];
Pssm-ID: 442610 [Multi-domain] Cd Length: 684 Bit Score: 138.09 E-value: 8.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 264 GLGSNIRVDTRGNEVMRIVPRANEEVNEEWISDKARFSYDAL-KRQRLDRPMVRGsDGKLQETSWEFALDYVAEKLKATE 342
Cdd:COG3383 15 GVGCGIDLEVKDGKIVKVEGDPDHPVNRGRLCVKGRFGFEFVnSPDRLTTPLIRR-GGEFREVSWDEALDLVAERLREIQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 343 ----PDAIRAVAGKLCDAESMIslkdMMNKL-----GASHT---TPEGMANVSADVR----SSYLFNSnLVGVEDADYVL 406
Cdd:COG3383 94 aehgPDAVAFYGSGQLTNEENY----LLQKLargvlGTNNIdnnARLCMASAVAGLKqsfgSDAPPNS-YDDIEEADVIL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 407 LIGTNPRTEAPVLNVRLRRAViAGGATVTSVGP-------NADLSYPSTHLGDT-----------------TATLEEITS 462
Cdd:COG3383 169 VIGSNPAEAHPVLARRIKKAK-KNGAKLIVVDPrrtetarLADLHLQIKPGTDLallngllhviieeglvdEDFIAERTE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 463 GKHAVCEAIKAANNPMVI----VGSELLRRADSKILLKKIHAMCDELGV---VKGDWN-------------------GFN 516
Cdd:COG3383 248 GFEELKASVAKYTPERVAeitgVPAEDIREAARLIAEAKRAMILWGMGVnqhTQGTDNvnaiinlalatgnigrpgtGPF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 517 VLHDAGGTVGALDIGFVPGT-----SASNDVPAKLVYSL-GAEEFDAPAGAFIVYQGHHGAQG----------------- 573
Cdd:COG3383 328 PLTGQNNVQGGRDMGALPNVlpgyrDVTDPEHRAKVADAwGVPPLPDKPGLTAVEMFDAIADGeikalwiigenpavsdp 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 574 -------------------------ASKADVILPGAAYTEKTGTYVNTEGRAQVAVASMGPVGQAKEDWRILRALSEFAG 628
Cdd:COG3383 408 danhvrealekleflvvqdifltetAEYADVVLPAASWAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIAELARRLG 487
|
490 500
....*....|....*....|...
gi 1275574916 629 VPLPYNTHEQVHRRLAEVAPHFA 651
Cdd:COG3383 488 YGFDYDSPEEVFDEIARLTPDYS 510
|
|
| MopB_Formate-Dh-H |
cd02753 |
Formate dehydrogenase H (Formate-Dh-H) catalyzes the reversible oxidation of formate to CO2 ... |
264-654 |
4.14e-30 |
|
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: 125.02 E-value: 4.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 264 GLGSNIRVDTRGNEVMRIVPRANEEVNEEWISDKARFSYDALK-RQRLDRPMVRgSDGKLQETSWEFALDYVAEKLKATE 342
Cdd:cd02753 8 GVGCGLELWVKDNKIVGVEPVKGHPVNRGKLCVKGRFGFDFVNsKDRLTKPLIR-KNGKFVEASWDEALSLVASRLKEIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 343 ----PDAI--------------------RAVAG--------KLCDAESMISLKDMmnkLGAShttpeGMANVSADVrssy 390
Cdd:cd02753 87 dkygPDAIaffgsakctneenylfqklaRAVGGtnnvdhcaRLCHSPTVAGLAET---LGSG-----AMTNSIADI---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 391 lfnsnlvgvEDADYVLLIGTNPrTEA-PVLNVRLRRAVIaGGATVTSVGP-------NADL---SYPSTH---------- 449
Cdd:cd02753 155 ---------EEADVILVIGSNT-TEAhPVIARRIKRAKR-NGAKLIVADPrrtelarFADLhlqLRPGTDvallnamahv 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 450 -----LGDTtATLEEITSGKHAVCEAIKAANNPMV--I--VGSELLRRADSKILLKK-------------------IHAM 501
Cdd:cd02753 224 iieegLYDE-EFIEERTEGFEELKEIVEKYTPEYAerItgVPAEDIREAARMYATAKsaailwgmgvtqhshgtdnVMAL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 502 CDeLGVVKGDW----NGFNVLHDAGGTVGALDIGFVPgtsasNDVPA--KLVYSLGAE----EFDAPAGA-------FIV 564
Cdd:cd02753 303 SN-LALLTGNIgrpgTGVNPLRGQNNVQGACDMGALP-----NVLPGyvKALYIMGENpalsDPNTNHVRkalesleFLV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 565 YQGHHGAQGASKADVILPGAAYTEKTGTYVNTEGRAQVAVASMGPVGQAKEDWRILRALSEFAGVPLPYNTHEQVHRRLA 644
Cdd:cd02753 377 VQDIFLTETAELADVVLPAASFAEKDGTFTNTERRVQRVRKAVEPPGEARPDWEIIQELANRLGYPGFYSHPEEIFDEIA 456
|
490
....*....|
gi 1275574916 645 EVAPHFAKLN 654
Cdd:cd02753 457 RLTPQYAGIS 466
|
|
| BisC |
COG0243 |
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion]; |
269-645 |
3.38e-19 |
|
Anaerobic selenocysteine-containing dehydrogenase [Energy production and conversion];
Pssm-ID: 440013 [Multi-domain] Cd Length: 674 Bit Score: 92.21 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 269 IRVDTRGNEVMRIVPRANEEVNEEWISDKARFSYDAL-KRQRLDRPMVRGS---DGKLQETSWEFALDYVAEKLKATE-- 342
Cdd:COG0243 37 LGVKVEDGRVVRVRGDPDHPVNRGRLCAKGAALDERLySPDRLTYPMKRVGprgSGKFERISWDEALDLIAEKLKAIIde 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 343 --PDAI-----RAVAGKLCDAESMISLKdMMNKLGASHTTPEG-MANVSADVRSSYLFNSNLVGV-----EDADYVLLIG 409
Cdd:COG0243 117 ygPEAVafytsGGSAGRLSNEAAYLAQR-FARALGTNNLDDNSrLCHESAVAGLPRTFGSDKGTVsyedlEHADLIVLWG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 410 TNPRTEAPVLNVRLRRAVIAGGATVTSVGPN-------ADLsypstHL-----GDT-----------------TATLEEI 460
Cdd:COG0243 196 SNPAENHPRLLRRLREAAKKRGAKIVVIDPRrtetaaiADE-----WLpirpgTDAalllalahvlieeglydRDFLARH 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 461 TSGKHAVCEAIK-------------------------AANNPMVIVGS---------ELLRRAdskILLkkIHAMCdelg 506
Cdd:COG0243 271 TVGFDELAAYVAaytpewaaeitgvpaedirelarefATAKPAVILWGmglqqhsngTQTVRA---IAN--LALLT---- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 507 vvkGDWngfnvlhdagGTVGALdIGFVPGTSASN--DVPAKLVYSLGAeefdAPAGA---------------FIVYQGHH 569
Cdd:COG0243 342 ---GNI----------GKPGGG-PFSLTGEAILDgkPYPIKALWVYGG----NPAVSapdtnrvrealrkldFVVVIDTF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 570 GAQGASKADVILPGAAYTEKTGTYVNTE-GRAQVAVASMGPVGQAKEDWRILRALSEFAGVPLPYN---THEQVHRRLAE 645
Cdd:COG0243 404 LTETARYADIVLPATTWLERDDIVTNSEdRRVHLSRPAVEPPGEARSDWEIFAELAKRLGFEEAFPwgrTEEDYLRELLE 483
|
|
| Fer2_4 |
pfam13510 |
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ... |
38-114 |
1.78e-18 |
|
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: 80.28 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 38 DTVPVTVNGQEVHVPKGVTVLYACEQAGVDVPRFCYHHK----LSIAGNCRMCLVEVEKSPKpVASCAMPVMPGMNIKTT 113
Cdd:pfam13510 2 RPVTFTFDGRPVTAPEGDTIAAALLANGVRVPRSCKYGRprgiFCAMGECRNCLVEVDGVPN-VRACTTPVREGMVVRTQ 80
|
.
gi 1275574916 114 T 114
Cdd:pfam13510 81 N 81
|
|
| MopB_Nitrate-R-NapA-like |
cd02754 |
Nitrate reductases, NapA (Nitrate-R-NapA), NasA, and NarB catalyze the reduction of nitrate to ... |
264-649 |
1.14e-17 |
|
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: 86.90 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 264 GLGSNIRVDTRGNEVMRIVPRANEEVNEEWISDK-ARFSYDALKRQRLDRPMVRGSDGKLQETSWEFALDYVAEKLKATE 342
Cdd:cd02754 8 GVGCGVEIGVKDGKVVAVRGDPEHPVNRGRLCIKgLNLHKTLNGPERLTRPLLRRNGGELVPVSWDEALDLIAERFKAIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 343 ----PDAIrAV--AGKLCDAESMISLKDMMNKLGASHTTPEG---MAN-VSADVRSsylFNS-----NLVGVEDADYVLL 407
Cdd:cd02754 88 aeygPDSV-AFygSGQLLTEEYYAANKLAKGGLGTNNIDTNSrlcMASaVAGYKRS---FGAdgppgSYDDIEHADCFFL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 408 IGTNPRTEAPVLNVRLRRAVIA-GGATVTSVGP-------NADLSY---PSTHLGDTTATLEEITSGKHAVCEAIKAANN 476
Cdd:cd02754 164 IGSNMAECHPILFRRLLDRKKAnPGAKIIVVDPrrtrtadIADLHLpirPGTDLALLNGLLHVLIEEGLIDRDFIDAHTE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 477 pmvivGSELLRRADSKILLKKIHAMCD----------EL-------------GV---VKGDW--NGFNVLH--------- 519
Cdd:cd02754 244 -----GFEELKAFVADYTPEKVAEITGvpeadireaaRLfgearkvmslwtmGVnqsTQGTAanNAIINLHlatgkigrp 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 520 -----------DAGGT--VGAL----------------------------DIGFVPGTSAsNDVPAKL------------ 546
Cdd:cd02754 319 gsgpfsltgqpNAMGGreVGGLanllpghrsvnnpehraevakfwgvpegTIPPKPGLHA-VEMFEAIedgeikalwvmc 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 547 ---VYSLGAEEFDAPAGA---FIVYQ-GHHGAQGASKADVILPGAAYTEKTGTYVNTEGRAQVAVASMGPVGQAKEDWRI 619
Cdd:cd02754 398 tnpAVSLPNANRVREALErleFVVVQdAFADTETAEYADLVLPAASWGEKEGTMTNSERRVSLLRAAVEPPGEARPDWWI 477
|
490 500 510
....*....|....*....|....*....|....*
gi 1275574916 620 LRALSEFAGVP--LPYNTHEQV---HRRLAEVAPH 649
Cdd:cd02754 478 LADVARRLGFGelFPYTSPEEVfeeYRRLSRGRGA 512
|
|
| NADH-G_4Fe-4S_3 |
pfam10588 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
121-160 |
2.14e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 463159 [Multi-domain] Cd Length: 40 Bit Score: 75.95 E-value: 2.14e-17
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1275574916 121 REGVMEFLLINHPLDCPICDQGGECELQDQSYIFGSDRSR 160
Cdd:pfam10588 1 RKTILELLLSNHPLDCPTCDKNGNCELQDLAYELGVDEVR 40
|
|
| NADH-G_4Fe-4S_3 |
smart00929 |
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region; |
121-161 |
2.39e-17 |
|
NADH-ubiquinone oxidoreductase-G iron-sulfur binding region;
Pssm-ID: 214918 [Multi-domain] Cd Length: 41 Bit Score: 75.70 E-value: 2.39e-17
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1275574916 121 REGVMEFLLINHPLDCPICDQGGECELQDQSYIFGSDRSRF 161
Cdd:smart00929 1 RKTILELLLANHPLDCPVCDKNGECELQDLAYELGVDEQRY 41
|
|
| PRK12814 |
PRK12814 |
putative NADPH-dependent glutamate synthase small subunit; Provisional |
39-147 |
6.55e-16 |
|
putative NADPH-dependent glutamate synthase small subunit; Provisional
Pssm-ID: 139246 [Multi-domain] Cd Length: 652 Bit Score: 81.70 E-value: 6.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 39 TVPVTVNGQEVHVPKGVTVLYACEQAGVDVPRFCYHHKLSIAGNCRMCLVEVEKSPKPVASCAMPVMPGMNIKTTTDLVK 118
Cdd:PRK12814 3 TISLTINGRSVTAAPGTSILEAAASAGITIPTLCFHQELEATGSCWMCIVEIKGKNRFVPACSTAVSEGMVIETENAELH 82
|
90 100
....*....|....*....|....*....
gi 1275574916 119 KAREGVMEFLLINHPLDCPicdqgGECEL 147
Cdd:PRK12814 83 AMRRQSLERLIEQHCGDCL-----GPCEL 106
|
|
| fer2 |
cd00207 |
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ... |
39-111 |
1.33e-12 |
|
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: 63.57 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 39 TVPVTVNGQEVHVPKGVTVLYACEQAGVDVPRFCYHhklsiaGNCRMCLVEVEK----------------SPKPVASCAM 102
Cdd:cd00207 2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRA------GACGTCKVEVVEgevdqsdpslldeeeaEGGYVLACQT 75
|
....*....
gi 1275574916 103 PVMPGMNIK 111
Cdd:cd00207 76 RVTDGLVIE 84
|
|
| NADH_dhqG_C |
pfam09326 |
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at ... |
680-704 |
6.95e-10 |
|
NADH-ubiquinone oxidoreductase subunit G, C-terminal; Members of this family of are found at the C-terminus of NADH dehydrogenases subunit G or NADH-ubiquinone oxidoreductase subunit G. EC:1.6.99.5.
Pssm-ID: 462757 Cd Length: 41 Bit Score: 54.54 E-value: 6.95e-10
|
| MopB_1 |
cd02762 |
The MopB_1 CD includes a group of related uncharacterized bacterial molybdopterin-binding ... |
269-439 |
4.44e-07 |
|
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: 53.17 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 269 IRVDTRGNEVMRIVPRANEEVNEEWISDKA-RFSYDALKRQRLDRPMVRgSDGKLQETSWEFALDYVAEKLKATE----P 343
Cdd:cd02762 13 LVVTVEDGRVASIRGDPDDPLSKGYICPKAaALGDYQNDPDRLRTPMRR-RGGSFEEIDWDEAFDEIAERLRAIRarhgG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 344 DAIRAVAGK------LCDAESMISLKDMMNKLGASHTTPEGManvSADVRSSYLFNSNLVGV----EDADYVLLIGTNP- 412
Cdd:cd02762 92 DAVGVYGGNpqahthAGGAYSPALLKALGTSNYFSAATADQK---PGHFWSGLMFGHPGLHPvpdiDRTDYLLILGANPl 168
|
170 180 190
....*....|....*....|....*....|...
gi 1275574916 413 ------RTEAPVlnVRLRRAVIAGGATVTSVGP 439
Cdd:cd02762 169 qsngslRTAPDR--VLRLKAAKDRGGSLVVIDP 199
|
|
| MopB_Formate-Dh-Na-like |
cd02752 |
Formate dehydrogenase N, alpha subunit (Formate-Dh-Na) is a major component of nitrate ... |
309-625 |
1.06e-06 |
|
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: 52.02 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 309 RLDRPMVR--GSDgKLQETSWEFALDYVAEKLKATE----------------PDAIRAVAGKLCDAESMISLKDMMNKLG 370
Cdd:cd02752 54 RLKYPMYRapGSG-KWEEISWDEALDEIARKMKDIRdasfveknaagvvvnrPDSIAFLGSAKLSNEECYLIRKFARALG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 371 ASH----------TTPEGMANvsadvrsSY---LFNSNLVGVEDADYVLLIGTNPRTEAPVLNVRLRRAVIAGGATVTSV 437
Cdd:cd02752 133 TNNldhqariuhsPTVAGLAN-------TFgrgAMTNSWNDIKNADVILVMGGNPAEAHPVSFKWILEAKEKNGAKLIVV 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 438 GPN-------ADLsYPSTHLGDTTATL---------------EEITSGKHA----VCEAI---KAANNPMVI-------- 480
Cdd:cd02752 206 DPRftrtaakADL-YVPIRSGTDIAFLggminyiirytpeevEDICGVPKEdflkVAEMFaatGRPDKPGTIlyamgwtq 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 481 --VGSELLRradskillkkihAMC------DELGVVKGdwnGFNVLHDAGGTVGALDIG--------------FVPGTSA 538
Cdd:cd02752 285 htVGSQNIR------------AMCilqlllGNIGVAGG---GVNALRGHSNVQGATDLGllshnlpgylggqnPNSSFPN 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 539 SNDVP---AKLVYSLGAEEFDAPAGAFivYQGHHGAQGASKADV-ILPGAAYTEKTGTYVNTEGRAQVAVASMGPVGQAK 614
Cdd:cd02752 350 ANKVRralDKLDWLVVIDPFPTETAAF--WKNPGMDPKSIQTEVfLLPAACQYEKEGSITNSGRWLQWRYKVVEPPGEAK 427
|
410
....*....|.
gi 1275574916 615 EDWRILRALSE 625
Cdd:cd02752 428 SDGDILVELAK 438
|
|
| Fer2 |
pfam00111 |
2Fe-2S iron-sulfur cluster binding domain; |
42-90 |
1.08e-05 |
|
2Fe-2S iron-sulfur cluster binding domain;
Pssm-ID: 395061 [Multi-domain] Cd Length: 77 Bit Score: 44.05 E-value: 1.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1275574916 42 VTVNG--QEVHVPKGVT-VLYACEQAGVDVPRFCYHhklsiaGNCRMCLVEV 90
Cdd:pfam00111 1 VTINGkgVTIEVPDGETtLLDAAEEAGIDIPYSCRG------GGCGTCAVKV 46
|
|
| MopB_Nitrate-R-NarG-like |
cd02750 |
Respiratory nitrate reductase A (NarGHI), alpha chain (NarG) and related proteins. Under ... |
308-636 |
3.55e-05 |
|
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: 46.93 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 308 QRLDRPMVRG---SDGKLQETSWEFALDYVAEKL----KATEPDAI------------RAVAG----KLCDAeSMISLKD 364
Cdd:cd02750 65 DRVKYPLKRVgarGEGKWKRISWDEALELIADAIidtiKKYGPDRVigfspipamsmvSYAAGsrfaSLIGG-VSLSFYD 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 365 MMNKL-GASHTT--PEGMANVSADvrssyLFNSnlvgvedaDYVLLIGTNP---RT-EAPVLN-VRLRraviagGATVTS 436
Cdd:cd02750 144 WYGDLpPGSPQTwgEQTDVPESAD-----WYNA--------DYIIMWGSNVpvtRTpDAHFLTeARYN------GAKVVV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 437 VGPN-------ADLSYPST---------------------------------HLGDTTATLEEIT--SGKHAVCEAIKAA 474
Cdd:cd02750 205 VSPDyspsakhADLWVPIKpgtdaalalamahviikeklydedylkeytdlpFLVYTPAWQEAITgvPRETVIRLAREFA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 475 NN--PMVIVG--------SELLRRAdsKILLKkihAMCDELGVVKGDWNGFnvlhdaggtVGALDIGFVpgtSASNdvpa 544
Cdd:cd02750 285 TNgrSMIIVGaginhwyhGDLCYRA--LILLL---ALTGNEGKNGGGWAHY---------VGQPRVLFV---WRGN---- 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 545 KLVYSLGAEEF--DAPAGA--FIVYQGHHGAQGASKADVILPGAAYTEKTG-------TYVNTEGRAqvavasMGPVGQA 613
Cdd:cd02750 344 LFGSSGKGHEYfeDAPEGKldLIVDLDFRMDSTALYSDIVLPAATWYEKHDlsttdmhPFIHPFSPA------VDPLWEA 417
|
410 420
....*....|....*....|...
gi 1275574916 614 KEDWRILRALSEfagvPLPYNTH 636
Cdd:cd02750 418 KSDWEIFKALAK----KVPWRTL 436
|
|
| MopB_Thiosulfate-R-like |
cd02755 |
The MopB_Thiosulfate-R-like CD contains thiosulfate-, sulfur-, and polysulfide-reductases, and ... |
308-439 |
3.47e-04 |
|
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: 43.83 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 308 QRLDRPMVRGS---DGKLQETSWEFALDYVAEKLKA-TEPDAIRAVAGkLCDAESMIS-LKDMMNKLGASHTTPEGMANV 382
Cdd:cd02755 54 DRLKKPLIRVGergEGKFREASWDEALQYIASKLKEiKEQHGPESVLF-GGHGGCYSPfFKHFAAAFGSPNIFSHESTCL 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1275574916 383 SADVRSSYLFNSNLVGVEDAD-----YVLLIGTNpRTEAPVlNVRLRR--AVIAGGATVTSVGP 439
Cdd:cd02755 133 ASKNLAWKLVIDSFGGEVNPDfenarYIILFGRN-LAEAII-VVDARRlmKALENGAKVVVVDP 194
|
|
| PRK15488 |
PRK15488 |
thiosulfate reductase PhsA; Provisional |
308-376 |
6.52e-04 |
|
thiosulfate reductase PhsA; Provisional
Pssm-ID: 237973 [Multi-domain] Cd Length: 759 Bit Score: 43.12 E-value: 6.52e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1275574916 308 QRLDRPMVRGS---DGKLQETSWEFALDYVAEKLkatepDAIRAVAGklcdAESMI------SLKDMMNKLGASHTTP 376
Cdd:PRK15488 97 QRIVKPLKRVGergEGKWQEISWDEAYQEIAAKL-----NAIKQQHG----PESVAfssksgSLSSHLFHLATAFGSP 165
|
|
| PRK13532 |
PRK13532 |
nitrate reductase catalytic subunit NapA; |
574-627 |
9.92e-04 |
|
nitrate reductase catalytic subunit NapA;
Pssm-ID: 237416 [Multi-domain] Cd Length: 830 Bit Score: 42.58 E-value: 9.92e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1275574916 574 ASKADVILPGAAYTEKTGTYVNTEGRAQVAVASMGPVGQAKED-WRILralsEFA 627
Cdd:PRK13532 518 ALAADLILPTAMWVEKEGAYGNAERRTQFWRQQVKAPGEAKSDlWQLV----EFS 568
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| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
98-242 |
2.70e-03 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 40.78 E-value: 2.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 98 ASCAMPVMPGMNIKTTTDLVKKAREGVMEFLLINHPLDCPICDQGGECELQDQSYIFGSDRSRFTEYKRAVEDKELGPLV 177
Cdd:COG4624 7 ACCCCCIEEGDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSI 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1275574916 178 KTVMTRCIHCTRCVRFSTEIAgvqdmgITGRGNQAEVgtyiskllASEL---SGNVIDLCPVGALTSK 242
Cdd:COG4624 87 IRDKEKCKNCYPCVRACPVKA------IKVDDGKAEI--------DEEKcisCGQCVAVCPFGAITEK 140
|
|
| MopB_Arsenite-Ox |
cd02756 |
Arsenite oxidase (Arsenite-Ox) oxidizes arsenite to the less toxic arsenate; it transfers the ... |
527-620 |
3.56e-03 |
|
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: 40.54 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275574916 527 ALDIGFVPGTSaSNDVPAKLVYSlgAEEfdaPAGAFIVYQGHHGAQGASKADVILPGAAYTEKTGTYVN-TEGRAQVAVA 605
Cdd:cd02756 469 AVEAALYAGTY-DREAMVCLIGD--AIQ---PGGLFIVVQDIYPTKLAEDAHVILPAAANGEMNETSMNgHERRLRLYEK 542
|
90
....*....|....*
gi 1275574916 606 SMGPVGQAKEDWRIL 620
Cdd:cd02756 543 FMDPPGEAMPDWWIA 557
|
|
| MopB_3 |
cd02766 |
The MopB_3 CD includes a group of related uncharacterized bacterial and archaeal ... |
308-343 |
4.84e-03 |
|
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: 39.92 E-value: 4.84e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1275574916 308 QRLDRPMVRGSD--GKLQETSWEFALDYVAEKLKATEP 343
Cdd:cd02766 54 DRLLTPLKRVGRkgGQWERISWDEALDTIAAKLKEIKA 91
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