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Conserved domains on  [gi|1958673199|ref|XP_038946974|]
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kynurenine 3-monooxygenase isoform X5 [Rattus norvegicus]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11428987)

NAD(P)/FAD-dependent oxidoreductase catalyzes the hydroxylation of specific substrates; similar to kynurenine 3-monooxygenase which catalyzes the hydroxylation of L-kynurenine to form 3-hydroxy-L-kynurenine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 24-326 5.75e-31

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


:

Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 119.66  E-value: 5.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  24 ACFLAKRNFQVDVYEAREDIRVanfmRGRSInlALSYRGRQALKAVGLEDQIVSKGVPMKARMIH-SLSGKK-SAIPYG- 100
Cdd:COG0654    19 ALALARAGIRVTVVERAPPPRP----DGRGI--ALSPRSLELLRRLGLWDRLLARGAPIRGIRVRdGSDGRVlARFDAAe 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 101 NKSQYILSISREKLNKDLLTAVESYpNAKVHFGHKLSKCCPEEGILTML---GpnkvpRDITCDLIVGCDGAYSTVRAHL 177
Cdd:COG0654    93 TGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTladG-----RTLRADLVVGADGARSAVRRLL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 178 MKKPR-FDYSQQYIphgymeltippkngeyamepnclhiWprnafmmialpnmdksftctlfmsfeefeklpthSDVLDF 256
Cdd:COG0654   167 GIGFTgRDYPQRAL-------------------------W----------------------------------AGVRTE 187

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 257 FQKNFPDAIPLMGEqalMRDFFLLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLV 326
Cdd:COG0654   188 LRARLAAAGPRLGE---LLELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAA 253
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 24-326 5.75e-31

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 119.66  E-value: 5.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  24 ACFLAKRNFQVDVYEAREDIRVanfmRGRSInlALSYRGRQALKAVGLEDQIVSKGVPMKARMIH-SLSGKK-SAIPYG- 100
Cdd:COG0654    19 ALALARAGIRVTVVERAPPPRP----DGRGI--ALSPRSLELLRRLGLWDRLLARGAPIRGIRVRdGSDGRVlARFDAAe 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 101 NKSQYILSISREKLNKDLLTAVESYpNAKVHFGHKLSKCCPEEGILTML---GpnkvpRDITCDLIVGCDGAYSTVRAHL 177
Cdd:COG0654    93 TGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTladG-----RTLRADLVVGADGARSAVRRLL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 178 MKKPR-FDYSQQYIphgymeltippkngeyamepnclhiWprnafmmialpnmdksftctlfmsfeefeklpthSDVLDF 256
Cdd:COG0654   167 GIGFTgRDYPQRAL-------------------------W----------------------------------AGVRTE 187

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 257 FQKNFPDAIPLMGEqalMRDFFLLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLV 326
Cdd:COG0654   188 LRARLAAAGPRLGE---LLELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAA 253
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 24-323 3.24e-10

Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 60.68  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  24 ACFLAKRNFQVDVYEAREDIRVAN-FMRGRSInlALSYRGRQALKAVGLEDQIVskgvPMKARMIHSL----SGKKSAIP 98
Cdd:TIGR01988  15 ALALARSGLKVALIEATPLPAPADpGFDNRVS--ALSAASIRLLEKLGVWDKIE----PARAQPIRDIhvsdGGSFGALR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  99 YgNKSQYILS-----ISREKLNKDLLTAVESYPNAKVHFGHKLS--KCCPEEGILTmLGPNKVprdITCDLIVGCDGAYS 171
Cdd:TIGR01988  89 F-DADEIGLEalgyvVENRVLQQALWERLQELPNVTLLCPARVVelPRHSDHVELT-LDDGQQ---LRARLLVGADGANS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 172 TVRAHL-MKKPRFDYSQQYI--------PHGY--MELTIPpkNGEYAM----EPNCLHIW---PRNAFMMIALPnmdksf 233
Cdd:TIGR01988 164 KVRQLAgIPTTGWDYGQSAVvanvkherPHQGtaWERFTP--TGPLALlplpDNRSSLVWtlpPEEAERLLALS------ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 234 tctlfmsFEEFeklpthsdvLDFFQKNFPdaiPLMGEQALMRDFFLLPAQPMISVKcspfHLKSRCVLMGDAAHAIVPFF 313
Cdd:TIGR01988 236 -------DEEF---------LAELQRAFG---SRLGAITLVGERHAFPLSLTHAKR----YVAPRLALIGDAAHTIHPLA 292

                         330
                  ....*....|
gi 1958673199 314 GQGMNAGFED 323
Cdd:TIGR01988 293 GQGLNLGLRD 302
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 66-323 7.74e-10

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 59.65  E-value: 7.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  66 LKAVGLEDQIVSKGVPmKARMIHSLSGKKSAIPYGNKS--QYILSISREKLNKDLLTAVESYPnAKVHFGHKL-SKCCPE 142
Cdd:pfam01494  53 LRQAGLEDRILAEGVP-HEGMGLAFYNTRRRADLDFLTspPRVTVYPQTELEPILVEHAEARG-AQVRFGTEVlSLEQDG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 143 EGILTML--GPNKVPRDITCDLIVGCDGAYSTVRAHLmkkpRFDY-SQQYIPHGYMELTIPPKNGEYAMEPNCLHIWPRN 219
Cdd:pfam01494 131 DGVTAVVrdRRDGEEYTVRAKYLVGCDGGRSPVRKTL----GIEFeGFEGVPFGSLDVLFDAPDLSDPVERAFVHYLIYA 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 220 A----FMMIALPNMDKS---FTCTLFMSFEEFEKLPTHSDVldffqknFPDAIPLMGEQALMRDFFLLPAQPMISVKCSP 292
Cdd:pfam01494 207 PhsrgFMVGPWRSAGREryyVQVPWDEEVEERPEEFTDEEL-------KQRLRSIVGIDLALVEILWKSIWGVASRVATR 279

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958673199 293 FHlKSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:pfam01494 280 YR-KGRVFLAGDAAHIHPPTGGQGLNTAIQD 309
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
118-323 7.08e-09

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 56.84  E-value: 7.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 118 LLTAVESYPNAKVHFGHKLSKCCPEEG--ILTMLGPNKVPRDITCDLIVGCDGAYSTVRaHLMKKPRFDYSQqyiPHGYM 195
Cdd:PRK06183  119 LRAGLARFPHVRVRFGHEVTALTQDDDgvTVTLTDADGQRETVRARYVVGCDGANSFVR-RTLGVPFEDLTF---PERWL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 196 ELTIPPKNGEYAMEPNCLHIWPRNAFMMIALPNMDKSFtctlfmsfeEFEKLP--THSDVLDffqknfPDAIplmgeQAL 273
Cdd:PRK06183  195 VVDVLIANDPLGGPHTYQYCDPARPYTSVRLPHGRRRW---------EFMLLPgeTEEQLAS------PENV-----WRL 254

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958673199 274 MRDFFLLPAQP-MISVKCSPFHL-------KSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK06183  255 LAPWGPTPDDAeLIRHAVYTFHArvadrwrSGRVLLAGDAAHLMPPFAGQGMNSGIRD 312
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 24-326 5.75e-31

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 119.66  E-value: 5.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  24 ACFLAKRNFQVDVYEAREDIRVanfmRGRSInlALSYRGRQALKAVGLEDQIVSKGVPMKARMIH-SLSGKK-SAIPYG- 100
Cdd:COG0654    19 ALALARAGIRVTVVERAPPPRP----DGRGI--ALSPRSLELLRRLGLWDRLLARGAPIRGIRVRdGSDGRVlARFDAAe 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 101 NKSQYILSISREKLNKDLLTAVESYpNAKVHFGHKLSKCCPEEGILTML---GpnkvpRDITCDLIVGCDGAYSTVRAHL 177
Cdd:COG0654    93 TGLPAGLVVPRADLERALLEAARAL-GVELRFGTEVTGLEQDADGVTVTladG-----RTLRADLVVGADGARSAVRRLL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 178 MKKPR-FDYSQQYIphgymeltippkngeyamepnclhiWprnafmmialpnmdksftctlfmsfeefeklpthSDVLDF 256
Cdd:COG0654   167 GIGFTgRDYPQRAL-------------------------W----------------------------------AGVRTE 187

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 257 FQKNFPDAIPLMGEqalMRDFFLLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLV 326
Cdd:COG0654   188 LRARLAAAGPRLGE---LLELSPRSAFPLRRRRAERWR-RGRVVLLGDAAHTMHPLGGQGANLALRDAAA 253
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
24-216 8.54e-14

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 70.77  E-value: 8.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  24 ACFLAKRNFQVDVYEAREDIRVANfMRGrsinlALSYRGRQALKAVGLEDQIVSkgvPMKARMIHSLSGKKSAIPYGNKS 103
Cdd:COG0644     9 ARRLARAGLSVLLLEKGSFPGDKI-CGG-----GLLPRALEELEPLGLDEPLER---PVRGARFYSPGGKSVELPPGRGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 104 QYIlsISREKLNKDLLTAVESYpNAKVHFGHKLSKCCPEEGILTMLGPNkvPRDITCDLIVGCDGAYSTVRAHLMKKPRF 183
Cdd:COG0644    80 GYV--VDRARFDRWLAEQAEEA-GAEVRTGTRVTDVLRDDGRVVVRTGD--GEEIRADYVVDADGARSLLARKLGLKRRS 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958673199 184 DYSQQYIpHGYMELTIPPKNGEYamEPNCLHIW 216
Cdd:COG0644   155 DEPQDYA-LAIKEHWELPPLEGV--DPGAVEFF 184
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 24-323 3.24e-10

Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 60.68  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  24 ACFLAKRNFQVDVYEAREDIRVAN-FMRGRSInlALSYRGRQALKAVGLEDQIVskgvPMKARMIHSL----SGKKSAIP 98
Cdd:TIGR01988  15 ALALARSGLKVALIEATPLPAPADpGFDNRVS--ALSAASIRLLEKLGVWDKIE----PARAQPIRDIhvsdGGSFGALR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  99 YgNKSQYILS-----ISREKLNKDLLTAVESYPNAKVHFGHKLS--KCCPEEGILTmLGPNKVprdITCDLIVGCDGAYS 171
Cdd:TIGR01988  89 F-DADEIGLEalgyvVENRVLQQALWERLQELPNVTLLCPARVVelPRHSDHVELT-LDDGQQ---LRARLLVGADGANS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 172 TVRAHL-MKKPRFDYSQQYI--------PHGY--MELTIPpkNGEYAM----EPNCLHIW---PRNAFMMIALPnmdksf 233
Cdd:TIGR01988 164 KVRQLAgIPTTGWDYGQSAVvanvkherPHQGtaWERFTP--TGPLALlplpDNRSSLVWtlpPEEAERLLALS------ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 234 tctlfmsFEEFeklpthsdvLDFFQKNFPdaiPLMGEQALMRDFFLLPAQPMISVKcspfHLKSRCVLMGDAAHAIVPFF 313
Cdd:TIGR01988 236 -------DEEF---------LAELQRAFG---SRLGAITLVGERHAFPLSLTHAKR----YVAPRLALIGDAAHTIHPLA 292

                         330
                  ....*....|
gi 1958673199 314 GQGMNAGFED 323
Cdd:TIGR01988 293 GQGLNLGLRD 302
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 66-323 7.74e-10

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 59.65  E-value: 7.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  66 LKAVGLEDQIVSKGVPmKARMIHSLSGKKSAIPYGNKS--QYILSISREKLNKDLLTAVESYPnAKVHFGHKL-SKCCPE 142
Cdd:pfam01494  53 LRQAGLEDRILAEGVP-HEGMGLAFYNTRRRADLDFLTspPRVTVYPQTELEPILVEHAEARG-AQVRFGTEVlSLEQDG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 143 EGILTML--GPNKVPRDITCDLIVGCDGAYSTVRAHLmkkpRFDY-SQQYIPHGYMELTIPPKNGEYAMEPNCLHIWPRN 219
Cdd:pfam01494 131 DGVTAVVrdRRDGEEYTVRAKYLVGCDGGRSPVRKTL----GIEFeGFEGVPFGSLDVLFDAPDLSDPVERAFVHYLIYA 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 220 A----FMMIALPNMDKS---FTCTLFMSFEEFEKLPTHSDVldffqknFPDAIPLMGEQALMRDFFLLPAQPMISVKCSP 292
Cdd:pfam01494 207 PhsrgFMVGPWRSAGREryyVQVPWDEEVEERPEEFTDEEL-------KQRLRSIVGIDLALVEILWKSIWGVASRVATR 279

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958673199 293 FHlKSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:pfam01494 280 YR-KGRVFLAGDAAHIHPPTGGQGLNTAIQD 309
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
118-323 7.08e-09

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 56.84  E-value: 7.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 118 LLTAVESYPNAKVHFGHKLSKCCPEEG--ILTMLGPNKVPRDITCDLIVGCDGAYSTVRaHLMKKPRFDYSQqyiPHGYM 195
Cdd:PRK06183  119 LRAGLARFPHVRVRFGHEVTALTQDDDgvTVTLTDADGQRETVRARYVVGCDGANSFVR-RTLGVPFEDLTF---PERWL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 196 ELTIPPKNGEYAMEPNCLHIWPRNAFMMIALPNMDKSFtctlfmsfeEFEKLP--THSDVLDffqknfPDAIplmgeQAL 273
Cdd:PRK06183  195 VVDVLIANDPLGGPHTYQYCDPARPYTSVRLPHGRRRW---------EFMLLPgeTEEQLAS------PENV-----WRL 254

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958673199 274 MRDFFLLPAQP-MISVKCSPFHL-------KSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK06183  255 LAPWGPTPDDAeLIRHAVYTFHArvadrwrSGRVLLAGDAAHLMPPFAGQGMNSGIRD 312
PRK07364 PRK07364
FAD-dependent hydroxylase;
118-323 2.41e-08

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 55.03  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 118 LLTAVESYPNakvhfghkLSKCCPEEGILTMLGPNKV---------PRDITCDLIVGCDGAYSTVRAHLMKKPR-FDYSQ 187
Cdd:PRK07364  127 LQEFLQSCPN--------ITWLCPAEVVSVEYQQDAAtvtleiegkQQTLQSKLVVAADGARSPIRQAAGIKTKgWKYWQ 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 188 QYI--------PHGYMeltippkngeyAMEpnclHIWPRNAFMMIALPNMDKSFTCTlfMSFEEFEKLPT--HSDVLDFF 257
Cdd:PRK07364  199 SCVtatvkheaPHNDI-----------AYE----RFWPSGPFAILPLPGNRCQIVWT--APHAQAKALLAlpEAEFLAEL 261

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958673199 258 QKNFPDaipLMGEQALMRDFFLLPAQPMISVKcspfHLKSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK07364  262 QQRYGD---QLGKLELLGDRFLFPVQLMQSDR----YVQHRLALVGDAAHCCHPVGGQGLNLGIRD 320
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 156-323 1.04e-07

ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone


Pssm-ID: 273914 [Multi-domain]  Cd Length: 437  Bit Score: 53.22  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 156 RDITCDLIVGCDGAYSTVR-AHLMKKPRFDYSQQYIPhGYMELTIPPKN----------GEYAMEP----NCLHIW---P 217
Cdd:TIGR01989 168 QVLYTKLLIGADGSNSNVRkAANIDTTGWNYNQHAVV-ATLKLEEATENdvawqrflptGPIALLPlpdnNSTLVWstsP 246

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 218 RNAFMMIALPnmDKSFTCTLFMSFE-EFEKLPtHSDVLDFFQKNFPDAIPLMGEQAlMRDFFLLPAqpMISVKCS----- 291
Cdd:TIGR01989 247 EEALRLLSLP--PEDFVDALNAAFDlGYSDHP-YSYLLDYAMEKLNEDIGFRTEGS-KSCFQVPPR--VIGVVDKsraaf 320

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958673199 292 PFHL-------KSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:TIGR01989 321 PLGLghadeyvTKRVALVGDAAHRVHPLAGQGVNLGFGD 359
PRK06753 PRK06753
hypothetical protein; Provisional
 24-326 1.05e-07

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 53.15  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  24 ACFLAKRNFQVDVYEAREDIRVAnfmrGRSINLALSyrGRQALKAVGLEDQIVSKGVPMKARMIHSLSGK---KSAIPYG 100
Cdd:PRK06753   16 AALLQEQGHEVKVFEKNESVKEV----GAGIGIGDN--VIKKLGNHDLAKGIKNAGQILSTMNLLDDKGTllnKVKLKSN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 101 NKSqyiLSISReklnKDLLTAVESY-PNAKVHFGHKLSKCCPEEGILTMLGPNKVPRDItcDLIVGCDGAYSTVRAHLMK 179
Cdd:PRK06753   90 TLN---VTLHR----QTLIDIIKSYvKEDAIFTGKEVTKIENETDKVTIHFADGESEAF--DLCIGADGIHSKVRQSVNA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 180 KPRFDYSqqyiphGY-----MELTIPPKNGEYAMEpnclhIW-PRNAFMMIALPNMDKSFtctlFMSFEEFEKLPTHSDV 253
Cdd:PRK06753  161 DSKVRYQ------GYtcfrgLIDDIDLKLPDCAKE-----YWgTKGRFGIVPLLNNQAYW----FITINAKERDPKYSSF 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 254 ----LDFFQKNFPDAIPLMGEQA-----LMRDFFLLpaQPMISvkcspfHLKSRCVLMGDAAHAIVPFFGQGMNAGFEDC 324
Cdd:PRK06753  226 gkphLQAYFNHYPNEVREILDKQsetgiLHHDIYDL--KPLKS------FVYGRIVLLGDAAHATTPNMGQGAGQAMEDA 297


                  ..
gi 1958673199 325 LV 326
Cdd:PRK06753  298 IV 299
PRK06126 PRK06126
hypothetical protein; Provisional
 118-323 6.01e-07

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 51.15  E-value: 6.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 118 LLTAVESYPNAKVHFGHKLSKCCP-EEGILTM---LGPNKvPRDITCDLIVGCDGAYSTVRAHL---------------- 177
Cdd:PRK06126  132 LLEHAAAQPGVTLRYGHRLTDFEQdADGVTATvedLDGGE-SLTIRADYLVGCDGARSAVRRSLgisyegtsglqrdlsi 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 178 -MKKPRFdysQQYIPH--GYMELTI-PPKNGEYAmepnclHIWPRNAFMMIALPnmdksftctlfmsFEEFEKLPTHSDV 253
Cdd:PRK06126  211 yIRAPGL---AALVGHdpAWMYWLFnPDRRGVLV------AIDGRDEWLFHQLR-------------GGEDEFTIDDVDA 268

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958673199 254 LDFFQKnfpdaipLMGEQAlmrDFFLLPAQPMISVK-CSPFHLKSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK06126  269 RAFVRR-------GVGEDI---DYEVLSVVPWTGRRlVADSYRRGRVFLAGDAAHLFTPTGGYGMNTGIGD 329
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 296-327 1.30e-06

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 49.77  E-value: 1.30e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1958673199 296 KSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVF 327
Cdd:PRK08849  278 KNNCVLLGDAAHTINPLAGQGVNLGFKDVDVL 309
PRK06847 PRK06847
hypothetical protein; Provisional
 27-330 1.39e-06

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 49.49  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  27 LAKRNFQVDVYEAREDIRVAnfmrGRSINL---ALsyrgrQALKAVGLEDQIVSKGVPMKARMIHSLSGKKSA------- 96
Cdd:PRK06847   23 LRRAGIAVDLVEIDPEWRVY----GAGITLqgnAL-----RALRELGVLDECLEAGFGFDGVDLFDPDGTLLAelptprl 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  97 ----IPYGNksqyilSISREKLNKDLLTAVESyPNAKVHFGHKLSKCCP-EEGIltmlgpnkvprDITC--------DLI 163
Cdd:PRK06847   94 agddLPGGG------GIMRPALARILADAARA-AGADVRLGTTVTAIEQdDDGV-----------TVTFsdgttgryDLV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 164 VGCDGAYSTVRAHLM---KKPRF----------------DYSQQYIP-------------HGYMELTIPPKNGEYaMEPn 211
Cdd:PRK06847  156 VGADGLYSKVRSLVFpdePEPEYtgqgvwravlprpaevDRSLMYLGpttkagvvplsedLMYLFVTEPRPDNPR-IEP- 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 212 clHIWPRnafmmiALPNMDKSFTctlfmsfeefeklpthSDVLDFFQKNFPDAiplmgEQALMRDF--FLLPAqpmisvk 289
Cdd:PRK06847  234 --DTLAA------LLRELLAPFG----------------GPVLQELREQITDD-----AQVVYRPLetLLVPA------- 277

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1958673199 290 csPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDCLVF-DEL 330
Cdd:PRK06847  278 --PWH-RGRVVLIGDAAHATTPHLAQGAGMAIEDAIVLaEEL 316
PRK07538 PRK07538
hypothetical protein; Provisional
 24-177 1.57e-06

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 49.51  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  24 ACFLAKRNFQVDVYEAREDIRVAnfmrGRSINLaLSYRGRQaLKAVGLEDQIVSKGVPMKARMIHSLSGKKsaI---PYG 100
Cdd:PRK07538   16 ALTLHQRGIEVVVFEAAPELRPL----GVGINL-LPHAVRE-LAELGLLDALDAIGIRTRELAYFNRHGQR--IwsePRG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 101 NKSQYI---LSISREKLNKDLLTAV-ESYPNAKVHFGHKLSKCCP-EEGILTMLGPN--KVPRDITCDLIVGCDGAYSTV 173
Cdd:PRK07538   88 LAAGYDwpqYSIHRGELQMLLLDAVrERLGPDAVRTGHRVVGFEQdADVTVVFLGDRagGDLVSVRGDVLIGADGIHSAV 167


                  ....
gi 1958673199 174 RAHL 177
Cdd:PRK07538  168 RAQL 171
PRK06185 PRK06185
FAD-dependent oxidoreductase;
118-318 3.19e-06

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 48.70  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 118 LLTAVESYPNAKVHFGHKLSKCCPEEGI---LTMLGPNKvPRDITCDLIVGCDGAYSTVR--AHLmkKPR-----FDYSq 187
Cdd:PRK06185  114 LAEEASAYPNFTLRMGAEVTGLIEEGGRvtgVRARTPDG-PGEIRADLVVGADGRHSRVRalAGL--EVRefgapMDVL- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 188 qyiphgYMELTIPPKNGEYAMEpnclHIWPRNafMMIALPNMDKsFTCTLFMSFEEFEKLptHSDVLDFFQKNFPDAIPL 267
Cdd:PRK06185  190 ------WFRLPREPDDPESLMG----RFGPGQ--GLIMIDRGDY-WQCGYVIPKGGYAAL--RAAGLEAFRERVAELAPE 254

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958673199 268 MGEQAL----MRDFFLLpaqpmiSVKCSpfHLK--SR--CVLMGDAAHAIVPFFGQGMN 318
Cdd:PRK06185  255 LADRVAelksWDDVKLL------DVRVD--RLRrwHRpgLLCIGDAAHAMSPVGGVGIN 305
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 156-323 2.44e-05

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 45.92  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 156 RDITCDLIVGCDGAYSTVRaHLMKKP--RFDYSQQYI--------PHGYMELTIPPKNGEYAM----EPN-CLHIWPRNA 220
Cdd:PRK08850  153 QALTAKLVVGADGANSWLR-RQMDIPltHWDYGHSALvanvrtvdPHNSVARQIFTPQGPLAFlpmsEPNmSSIVWSTEP 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 221 FMMIALPNMDKS-FTCTLFMSFEEfeKLPTHSDVLDFFqknfpdAIPLMGEQAlmRDFfllpaqpmisvkcspfhLKSRC 299
Cdd:PRK08850  232 LRAEALLAMSDEqFNKALTAEFDN--RLGLCEVVGERQ------AFPLKMRYA--RDF-----------------VRERV 284

                         170       180
                  ....*....|....*....|....
gi 1958673199 300 VLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK08850  285 ALVGDAAHTIHPLAGQGVNLGLLD 308
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
296-323 2.57e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 45.72  E-value: 2.57e-05
                          10        20
                  ....*....|....*....|....*...
gi 1958673199 296 KSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK07608  279 APRVALVGDAAHLIHPLAGQGMNLGLRD 306
PRK07045 PRK07045
putative monooxygenase; Reviewed
 50-349 3.65e-05

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 45.28  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199  50 RGRSINLA--LSYRGRQALKAVGLEDQIVSKGVPMKARMihSLSGKKSAIPYGNKSQ-----YILSISREKLNKDLLTAV 122
Cdd:PRK07045   39 RNRAQNGAdlLKPSGIGVVRAMGLLDDVFAAGGLRRDAM--RLYHDKELIASLDYRSasalgYFILIPCEQLRRLLLAKL 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 123 ESYPNAKVHFGHKLSKCCPEE-GILTML----GPNKVPRditcdLIVGCDGAYSTVRAHLMKKP--RFDYSQqyiPHGYM 195
Cdd:PRK07045  117 DGLPNVRLRFETSIERIERDAdGTVTSVtlsdGERVAPT-----VLVGADGARSMIRDDVLRMPaeRVPYAT---PMAFG 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 196 ELTIPPKngeyAMEPNCLHIwPRNAFMMIALPNMDKSftCTLFMSFEEFEKLPTHSDVL---------DFFQKNFPDAIP 266
Cdd:PRK07045  189 TIALTDS----VRECNRLYV-DSNQGLAYFYPIGDQA--TRLVVSFPADEMQGYLADTTrtkllarlnEFVGDESADAMA 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958673199 267 LMGEQALmrdfflLPAQPMISVKCSPFHlKSRCVLMGDAAHAIVPFFGQGMNAGFEDClvfDELMDKFNNDLISEVLLCD 346
Cdd:PRK07045  262 AIGAGTA------FPLIPLGRMNLDRYH-KRNVVLLGDAAHSIHPITGQGMNLAIEDA---GELGACLDLHLSGQIALAD 331


                  ...
gi 1958673199 347 LLA 349
Cdd:PRK07045  332 ALE 334
PRK08013 PRK08013
oxidoreductase; Provisional
 298-323 1.14e-04

oxidoreductase; Provisional


Pssm-ID: 236139 [Multi-domain]  Cd Length: 400  Bit Score: 43.50  E-value: 1.14e-04
                          10        20
                  ....*....|....*....|....*.
gi 1958673199 298 RCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK08013  283 RLALVGDAAHTIHPLAGQGVNLGFMD 308
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
296-323 4.06e-04

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 41.89  E-value: 4.06e-04
                          10        20
                  ....*....|....*....|....*...
gi 1958673199 296 KSRCVLMGDAAHAIVPFFGQGMNAGFED 323
Cdd:PRK07333  279 APRFALVGDAAHGIHPIAGQGLNLGLKD 306
PRK05714 PRK05714
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 301-331 8.45e-04

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 168201 [Multi-domain]  Cd Length: 405  Bit Score: 40.97  E-value: 8.45e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1958673199 301 LMGDAAHAIVPFFGQGMNAGFEDCLVFDELM 331
Cdd:PRK05714  289 LIGDAAHTIHPLAGQGVNLGFLDAAVLAEVL 319
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 300-332 1.26e-03

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 40.35  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958673199 300 VLMGDAAHAIVPFFGQGMNAGFEDClvfDELMD 332
Cdd:PRK08020  284 ALVGDAAHTINPLAGQGVNLGYRDV---DALLD 313
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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