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Conserved domains on  [gi|482570798|gb|EOA34986|]
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hypothetical protein CARUB_v10020078mg [Capsella rubella]

Protein Classification

geranylgeranyl diphosphate reductase( domain architecture ID 11476370)

geranylgeranyl diphosphate reductase catalyzes the reduction of geranylgeranyl diphosphate to phytyl diphosphate, providing phytol for both tocopherol and chlorophyll synthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN00093 PLN00093
geranylgeranyl diphosphate reductase; Provisional
 110-560 0e+00

geranylgeranyl diphosphate reductase; Provisional


:

Pssm-ID: 177713 [Multi-domain]  Cd Length: 450  Bit Score: 910.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 110 STEQTNFVSHVPSSLSLPQRRSSLRVTAARSTPKLSNRKLRVAVIGGGPAGGAAAETLAQGGIETVLIERKMDNCKPCGG 189
Cdd:PLN00093   1 LSHVSSFLPSAPSSAAKSVSRPGLRVLAAAASKKLSGRKLRVAVIGGGPAGACAAETLAKGGIETFLIERKLDNAKPCGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 190 AIPLCMVGEFNLPLDIIDRRVTKMKMISPSNIAVDIGRTLKEHEYIGMVRREVLDAYLRERAEKSGATVINGLFLKMDHP 269
Cdd:PLN00093  81 AIPLCMVGEFDLPLDIIDRKVTKMKMISPSNVAVDIGKTLKPHEYIGMVRREVLDSFLRERAQSNGATLINGLFTRIDVP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 270 ENWDSPYTLHYTEYDGKTGStGTKKTMEVDAVIGADGANSRVAKSIDAGDYDYAIAFQERIRIPDDKMTYYEDLAEMYVG 349
Cdd:PLN00093 161 KDPNGPYVIHYTSYDSGSGA-GTPKTLEVDAVIGADGANSRVAKDIDAGDYDYAIAFQERIKIPDDKMEYYEDLAEMYVG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 350 DDVSPDFYGWVFPKCDHVAVGTGTVTHKGDIKKFQLATRNRAKDKILGGKIIRVEAHPIPEHPRPRRLSKRVALVGDAAG 429
Cdd:PLN00093 240 DDVSPDFYGWVFPKCDHVAVGTGTVVNKPAIKKYQRATRNRAKDKIAGGKIIRVEAHPIPEHPRPRRVRGRVALVGDAAG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 430 YVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGKKMIDEGDLRKYLEKWDKTYLPTYRVLDVLQKVFYRSNPAREAFVEMCA 509
Cdd:PLN00093 320 YVTKCSGEGIYFAAKSGRMCAEAIVEGSENGTRMVDEADLREYLRKWDKKYWPTYKVLDILQKVFYRSNPAREAFVEMCA 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 482570798 510 DEYVQKMTFDSYLYKRVAPGSPLEDIKLAVNTIGSLVRANALRREIEKLNV 560
Cdd:PLN00093 400 DEYVQKMTFDSYLYKRVVPGNPLDDIKLLVNTIGSLVRANALRREMEKLSV 450
 
Name Accession Description Interval E-value
PLN00093 PLN00093
geranylgeranyl diphosphate reductase; Provisional
 110-560 0e+00

geranylgeranyl diphosphate reductase; Provisional


Pssm-ID: 177713 [Multi-domain]  Cd Length: 450  Bit Score: 910.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 110 STEQTNFVSHVPSSLSLPQRRSSLRVTAARSTPKLSNRKLRVAVIGGGPAGGAAAETLAQGGIETVLIERKMDNCKPCGG 189
Cdd:PLN00093   1 LSHVSSFLPSAPSSAAKSVSRPGLRVLAAAASKKLSGRKLRVAVIGGGPAGACAAETLAKGGIETFLIERKLDNAKPCGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 190 AIPLCMVGEFNLPLDIIDRRVTKMKMISPSNIAVDIGRTLKEHEYIGMVRREVLDAYLRERAEKSGATVINGLFLKMDHP 269
Cdd:PLN00093  81 AIPLCMVGEFDLPLDIIDRKVTKMKMISPSNVAVDIGKTLKPHEYIGMVRREVLDSFLRERAQSNGATLINGLFTRIDVP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 270 ENWDSPYTLHYTEYDGKTGStGTKKTMEVDAVIGADGANSRVAKSIDAGDYDYAIAFQERIRIPDDKMTYYEDLAEMYVG 349
Cdd:PLN00093 161 KDPNGPYVIHYTSYDSGSGA-GTPKTLEVDAVIGADGANSRVAKDIDAGDYDYAIAFQERIKIPDDKMEYYEDLAEMYVG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 350 DDVSPDFYGWVFPKCDHVAVGTGTVTHKGDIKKFQLATRNRAKDKILGGKIIRVEAHPIPEHPRPRRLSKRVALVGDAAG 429
Cdd:PLN00093 240 DDVSPDFYGWVFPKCDHVAVGTGTVVNKPAIKKYQRATRNRAKDKIAGGKIIRVEAHPIPEHPRPRRVRGRVALVGDAAG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 430 YVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGKKMIDEGDLRKYLEKWDKTYLPTYRVLDVLQKVFYRSNPAREAFVEMCA 509
Cdd:PLN00093 320 YVTKCSGEGIYFAAKSGRMCAEAIVEGSENGTRMVDEADLREYLRKWDKKYWPTYKVLDILQKVFYRSNPAREAFVEMCA 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 482570798 510 DEYVQKMTFDSYLYKRVAPGSPLEDIKLAVNTIGSLVRANALRREIEKLNV 560
Cdd:PLN00093 400 DEYVQKMTFDSYLYKRVVPGNPLDDIKLLVNTIGSLVRANALRREMEKLSV 450
ChlP TIGR02028
geranylgeranyl reductase; This model represents the reductase which acts reduces the ...
 165-547 0e+00

geranylgeranyl reductase; This model represents the reductase which acts reduces the geranylgeranyl group to the phytyl group in the side chain of chlorophyll. It is unclear whether the enzyme has a preference for acting before or after the attachment of the side chain to chlorophyllide a by chlorophyll synthase. This clade is restricted to plants and cyanobacteria to separate it from the homologues which act in the biosynthesis of bacteriochlorophyll. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 131083  Cd Length: 398  Bit Score: 789.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  165 ETLAQGGIETVLIERKMDNCKPCGGAIPLCMVGEFNLPLDIIDRRVTKMKMISPSNIAVDIGRTLKEHEYIGMVRREVLD 244
Cdd:TIGR02028  17 ETLASAGIQTFLLERKPDNAKPCGGAIPLCMVDEFALPRDIIDRRVTKMKMISPSNIAVDIGRTLKEHEYIGMLRREVLD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  245 AYLRERAEKSGATVINGLFLKMDHPENWDSPYTLHYTEYDgKTGSTGTKKTMEVDAVIGADGANSRVAKSIDAGDYDYAI 324
Cdd:TIGR02028  97 SFLRRRAADAGATLINGLVTKLSLPADADDPYTLHYISSD-SGGPSGTRCTLEVDAVIGADGANSRVAKEIDAGDYSYAI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  325 AFQERIRIPDDKMTYYEDLAEMYVGDDVSPDFYGWVFPKCDHVAVGTGTVTHKGDIKKFQLATRNRAKDKILGGKIIRVE 404
Cdd:TIGR02028 176 AFQERIRLPDEKMAYYDDLAEMYVGDDVSPDFYGWVFPKCDHVAVGTGTVAAKPEIKRLQSGIRARAAGKVAGGRIIRVE 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  405 AHPIPEHPRPRRLSKRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGKKMIDEGDLRKYLEKWDKTYLPTY 484
Cdd:TIGR02028 256 AHPIPEHPRPRRVVGRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEESRLGGAVTEEGDLAGYLRRWDKEYRPTY 335

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 482570798  485 RVLDVLQKVFYRSNPAREAFVEMCADEYVQKMTFDSYLYKRVAPGSPLEDIKLAVNTIGSLVR 547
Cdd:TIGR02028 336 RVLDLLQRVFYRSNAGREAFVEMCADEHVQKRTFDSYLYKRVAPAEPLGDLKLLWRTIGSLVR 398
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
166-478 3.59e-46

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 163.60  E-value: 3.59e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 166 TLAQGGIETVLIERK-MDNCKPCGGAIPLCMVGEFNLP--LDIIDRRVTKMKMISPSNIAVDIGRTlKEHEYigMVRREV 242
Cdd:COG0644   11 RLARAGLSVLLLEKGsFPGDKICGGGLLPRALEELEPLglDEPLERPVRGARFYSPGGKSVELPPG-RGGGY--VVDRAR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 243 LDAYLRERAEKSGATVINGLflKMDHPENWDSPYTLHyteydgktgsTGTKKTMEVDAVIGADGANSRVAKSIDA----- 317
Cdd:COG0644   88 FDRWLAEQAEEAGAEVRTGT--RVTDVLRDDGRVVVR----------TGDGEEIRADYVVDADGARSLLARKLGLkrrsd 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 318 GDYDYAIAFQERIRIPDDKmTYYEDLAEMYVGDDVsPDFYGWVFPKCD-HVAVGtgtvthkgdikkfqlatrnrakdkil 396
Cdd:COG0644  156 EPQDYALAIKEHWELPPLE-GVDPGAVEFFFGEGA-PGGYGWVFPLGDgRVSVG-------------------------- 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 397 ggkiirveahpIPE-HPRPRRLSKRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGKkmIDEGDLRKYLEK 475
Cdd:COG0644  208 -----------IPLgGPRPRLVGDGVLLVGDAAGFVDPLTGEGIHLAMKSGRLAAEAIAEALEGGD--FSAEALAEYERR 274


                 ...
gi 482570798 476 WDK 478
Cdd:COG0644  275 LRE 277
 
Name Accession Description Interval E-value
PLN00093 PLN00093
geranylgeranyl diphosphate reductase; Provisional
 110-560 0e+00

geranylgeranyl diphosphate reductase; Provisional


Pssm-ID: 177713 [Multi-domain]  Cd Length: 450  Bit Score: 910.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 110 STEQTNFVSHVPSSLSLPQRRSSLRVTAARSTPKLSNRKLRVAVIGGGPAGGAAAETLAQGGIETVLIERKMDNCKPCGG 189
Cdd:PLN00093   1 LSHVSSFLPSAPSSAAKSVSRPGLRVLAAAASKKLSGRKLRVAVIGGGPAGACAAETLAKGGIETFLIERKLDNAKPCGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 190 AIPLCMVGEFNLPLDIIDRRVTKMKMISPSNIAVDIGRTLKEHEYIGMVRREVLDAYLRERAEKSGATVINGLFLKMDHP 269
Cdd:PLN00093  81 AIPLCMVGEFDLPLDIIDRKVTKMKMISPSNVAVDIGKTLKPHEYIGMVRREVLDSFLRERAQSNGATLINGLFTRIDVP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 270 ENWDSPYTLHYTEYDGKTGStGTKKTMEVDAVIGADGANSRVAKSIDAGDYDYAIAFQERIRIPDDKMTYYEDLAEMYVG 349
Cdd:PLN00093 161 KDPNGPYVIHYTSYDSGSGA-GTPKTLEVDAVIGADGANSRVAKDIDAGDYDYAIAFQERIKIPDDKMEYYEDLAEMYVG 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 350 DDVSPDFYGWVFPKCDHVAVGTGTVTHKGDIKKFQLATRNRAKDKILGGKIIRVEAHPIPEHPRPRRLSKRVALVGDAAG 429
Cdd:PLN00093 240 DDVSPDFYGWVFPKCDHVAVGTGTVVNKPAIKKYQRATRNRAKDKIAGGKIIRVEAHPIPEHPRPRRVRGRVALVGDAAG 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 430 YVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGKKMIDEGDLRKYLEKWDKTYLPTYRVLDVLQKVFYRSNPAREAFVEMCA 509
Cdd:PLN00093 320 YVTKCSGEGIYFAAKSGRMCAEAIVEGSENGTRMVDEADLREYLRKWDKKYWPTYKVLDILQKVFYRSNPAREAFVEMCA 399

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 482570798 510 DEYVQKMTFDSYLYKRVAPGSPLEDIKLAVNTIGSLVRANALRREIEKLNV 560
Cdd:PLN00093 400 DEYVQKMTFDSYLYKRVVPGNPLDDIKLLVNTIGSLVRANALRREMEKLSV 450
ChlP TIGR02028
geranylgeranyl reductase; This model represents the reductase which acts reduces the ...
 165-547 0e+00

geranylgeranyl reductase; This model represents the reductase which acts reduces the geranylgeranyl group to the phytyl group in the side chain of chlorophyll. It is unclear whether the enzyme has a preference for acting before or after the attachment of the side chain to chlorophyllide a by chlorophyll synthase. This clade is restricted to plants and cyanobacteria to separate it from the homologues which act in the biosynthesis of bacteriochlorophyll. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 131083  Cd Length: 398  Bit Score: 789.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  165 ETLAQGGIETVLIERKMDNCKPCGGAIPLCMVGEFNLPLDIIDRRVTKMKMISPSNIAVDIGRTLKEHEYIGMVRREVLD 244
Cdd:TIGR02028  17 ETLASAGIQTFLLERKPDNAKPCGGAIPLCMVDEFALPRDIIDRRVTKMKMISPSNIAVDIGRTLKEHEYIGMLRREVLD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  245 AYLRERAEKSGATVINGLFLKMDHPENWDSPYTLHYTEYDgKTGSTGTKKTMEVDAVIGADGANSRVAKSIDAGDYDYAI 324
Cdd:TIGR02028  97 SFLRRRAADAGATLINGLVTKLSLPADADDPYTLHYISSD-SGGPSGTRCTLEVDAVIGADGANSRVAKEIDAGDYSYAI 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  325 AFQERIRIPDDKMTYYEDLAEMYVGDDVSPDFYGWVFPKCDHVAVGTGTVTHKGDIKKFQLATRNRAKDKILGGKIIRVE 404
Cdd:TIGR02028 176 AFQERIRLPDEKMAYYDDLAEMYVGDDVSPDFYGWVFPKCDHVAVGTGTVAAKPEIKRLQSGIRARAAGKVAGGRIIRVE 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  405 AHPIPEHPRPRRLSKRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGKKMIDEGDLRKYLEKWDKTYLPTY 484
Cdd:TIGR02028 256 AHPIPEHPRPRRVVGRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEESRLGGAVTEEGDLAGYLRRWDKEYRPTY 335

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 482570798  485 RVLDVLQKVFYRSNPAREAFVEMCADEYVQKMTFDSYLYKRVAPGSPLEDIKLAVNTIGSLVR 547
Cdd:TIGR02028 336 RVLDLLQRVFYRSNAGREAFVEMCADEHVQKRTFDSYLYKRVAPAEPLGDLKLLWRTIGSLVR 398
BchP-ChlP TIGR02023
geranylgeranyl reductase; This model represents a group of geranylgeranyl reductases specific ...
 165-547 0e+00

geranylgeranyl reductase; This model represents a group of geranylgeranyl reductases specific for the biosyntheses of bacteriochlorophyll and chlorophyll. It is unclear whether the processes of isoprenoid ligation to the chlorin ring and reduction of the geranylgeranyl chain to a phytyl chain are necessarily ordered the same way in all species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273932  Cd Length: 388  Bit Score: 617.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  165 ETLAQGGIETVLIERKMDNCKPCGGAIPLCMVGEFNLPLDIIDRRVTKMKMISPSniAVDIGRTLK-EHEYIGMVRREVL 243
Cdd:TIGR02023  17 ETLARAGIETILLERALSNIKPCGGAIPPCLIEEFDIPDSLIDRRVTQMRMISPS--RVPIKVTIPsEDGYVGMVRREVF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  244 DAYLRERAEKSGATVINGLFLKMDHPENwdsPYTLHYTEYdgKTGSTGTKKTMEVDAVIGADGANSRVAKSIDAG-DYDY 322
Cdd:TIGR02023  95 DSYLRERAQKAGAELIHGLFLKLERDRD---GVTLTYRTP--KKGAGGEKGSVEADVVIGADGANSPVAKELGLPkNLPR 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  323 AIAFQERIRIPDDKMTYYEDLAEMYVGDDVSPDFYGWVFPKCDHVAVGTGTVTHKGDIKKFQLATRNRAkdKILGGKIIR 402
Cdd:TIGR02023 170 VIAYQERIKLPDDKMAYYEELADVYYGGEVSPDFYGWVFPKGDHIAVGTGTGTHGFDAKQLQANLRRRA--GLDGGQTIR 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  403 VEAHPIPEHPRPRRLSKRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGkkmiDEGDLRKYLEKWDKTYLP 482
Cdd:TIGR02023 248 REAAPIPMKPRPRWDFGRAMLVGDAAGLVTPASGEGIYFAMKSGQMAAQAIAEYLQNG----DATDLRHYERKFMKLYGT 323

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 482570798  483 TYRVLDVLQKVFYRSNPAREAFVEMCADEYVQKMTFDSYLYKRVAPGSPLEDIKLAVNTIGSLVR 547
Cdd:TIGR02023 324 TFRVLRVLQMVYYRSDRRREVFVEMCRDKDVQRLTFDSYMYKQMAPAPWLAQLKIAAKNIGSLVR 388
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 165-453 1.10e-47

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 167.88  E-value: 1.10e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  165 ETLAQGGIETVLIERKMDN-CKPCGGAIPLCMVGEFNLPLDIIDRRVTKMKMISPSNIAVDIGrtlKEHEYIGMVRREVL 243
Cdd:TIGR02032  17 YRLADKGLRVLLLEKKSFPrYKPCGGALSPRALEELDLPGELIVNLVRGARFFSPNGDSVEIP---IETELAYVIDRDAF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  244 DAYLRERAEKSGATVINGLFLKMDhpenwdspytlhyTEYDGKTGST--GTKKTMEVDAVIGADGANSRVAKSIDAGDYD 321
Cdd:TIGR02032  94 DEQLAERAQEAGAELRLGTRVLDV-------------EIHDDRVVVIvrGSEGTVTAKIVIGADGSRSIVAKKLGLKKEP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  322 YAIAFQERIRIPDDKMTYYEDLAEMYVGDDVSPDFYGWVFPKCD---HVAVGTGTVTHKGDIKK---FQLATRNRAKDki 395
Cdd:TIGR02032 161 REYGVAARAEVEMPDEEVDEDFVEVYIDRGIVPGGYGWVFPKGDgtaNVGVGSRSAEEGEDPKKylkDFLARRPELKD-- 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 482570798  396 lgGKIIRVEAHPIPEHPRPRRLSK-RVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAI 453
Cdd:TIGR02032 239 --AETVEVCGALIPIGRPDEKLVRgNVLLVGDAAGHVNPLTGEGIYYAMRSGDIAAEVV 295
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
166-478 3.59e-46

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 163.60  E-value: 3.59e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 166 TLAQGGIETVLIERK-MDNCKPCGGAIPLCMVGEFNLP--LDIIDRRVTKMKMISPSNIAVDIGRTlKEHEYigMVRREV 242
Cdd:COG0644   11 RLARAGLSVLLLEKGsFPGDKICGGGLLPRALEELEPLglDEPLERPVRGARFYSPGGKSVELPPG-RGGGY--VVDRAR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 243 LDAYLRERAEKSGATVINGLflKMDHPENWDSPYTLHyteydgktgsTGTKKTMEVDAVIGADGANSRVAKSIDA----- 317
Cdd:COG0644   88 FDRWLAEQAEEAGAEVRTGT--RVTDVLRDDGRVVVR----------TGDGEEIRADYVVDADGARSLLARKLGLkrrsd 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 318 GDYDYAIAFQERIRIPDDKmTYYEDLAEMYVGDDVsPDFYGWVFPKCD-HVAVGtgtvthkgdikkfqlatrnrakdkil 396
Cdd:COG0644  156 EPQDYALAIKEHWELPPLE-GVDPGAVEFFFGEGA-PGGYGWVFPLGDgRVSVG-------------------------- 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 397 ggkiirveahpIPE-HPRPRRLSKRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGKkmIDEGDLRKYLEK 475
Cdd:COG0644  208 -----------IPLgGPRPRLVGDGVLLVGDAAGFVDPLTGEGIHLAMKSGRLAAEAIAEALEGGD--FSAEALAEYERR 274


                 ...
gi 482570798 476 WDK 478
Cdd:COG0644  275 LRE 277
PRK11445 PRK11445
FAD-binding protein;
166-459 1.05e-11

FAD-binding protein;


Pssm-ID: 183139 [Multi-domain]  Cd Length: 351  Bit Score: 66.62  E-value: 1.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 166 TLAQ--GGIETVLIERKMDNC------KPCGGAIP------LCMVGeFNLPLDII-DRRVTKMKMIspsniavDIGRTLK 230
Cdd:PRK11445  15 ALARllAGKMKVIAIDKKHQCgtegfsKPCGGLLApdaqksFAKDG-LTLPKDVIaNPQIFAVKTI-------DLANSLT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 231 EH---EYIGMvRREVLDAYLRERAEKSGATVINGLFLKMdhpENWDSPYTLHYTEydgktgsTGTKKTMEVDAVIGADGA 307
Cdd:PRK11445  87 RNyqrSYINI-DRHKFDLWLKSLIPASVEVYHNSLCRKI---WREDDGYHVIFRA-------DGWEQHITARYLVGADGA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 308 NSRVAKSI--DAGDYDYaIAFQERIRIPDDKmTYYEdlaemYVGDDVSPDFYGWVFPKCDHVAVGtGTVTHKGDIKKFql 385
Cdd:PRK11445 156 NSMVRRHLypDHQIRKY-VAIQQWFAEKHPV-PFYS-----CIFDNEITDCYSWSISKDGYFIFG-GAYPMKDGRERF-- 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 386 aTRNRAKDKILG---GKIIRVEAHPIPehpRPRRLSK------RVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEG 456
Cdd:PRK11445 226 -ETLKEKLSAFGfqfGKPVKTEACTVL---RPSRWQDfvcgkdNAFLIGEAAGFISPSSLEGISYALDSARILSEVLNKQ 301


                 ...
gi 482570798 457 SQN 459
Cdd:PRK11445 302 PEK 304
PRK10015 PRK10015
oxidoreductase; Provisional
 159-455 9.48e-08

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 54.60  E-value: 9.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 159 AGGAAAETLAQGGIETVLIER-KMDNCKPCGGAIPLCMVGEFNLP----LDIIDRRVTKMK---MISPSNIAVDIGR--- 227
Cdd:PRK10015  16 AGSVAALVMARAGLDVLVIERgDSAGCKNMTGGRLYAHTLEAIIPgfaaSAPVERKVTREKisfLTEESAVTLDFHReqp 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 228 -TLKEHEYigMVRREVLDAYLRERAEKSGATVINGlfLKMDhpenwdspytLHYTEYDGKTGSTGTKKTMEVDAVIGADG 306
Cdd:PRK10015  96 dVPQHASY--TVLRNRLDPWLMEQAEQAGAQFIPG--VRVD----------ALVREGNKVTGVQAGDDILEANVVILADG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 307 ANSRVAKSID----AGDYDYAIAFQERIRIP----DDK--MTYYEDLAEMYVGDDvSPDFYGWVFPKCDHVAVGTGTVTH 376
Cdd:PRK10015 162 VNSMLGRSLGmvpaSDPHHYAVGVKEVIGLTpeqiNDRfnITGEEGAAWLFAGSP-SDGLMGGGFLYTNKDSISLGLVCG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 377 KGDIKKFQLATRNRAKD---------KILGGKIIRVEAHPIPE---HPRPRRLSKRVALVGDAAGYVTKC--SGEGIYFA 442
Cdd:PRK10015 241 LGDIAHAQKSVPQMLEDfkqhpairpLISGGKLLEYSAHMVPEgglAMVPQLVNDGVMIVGDAAGFCLNLgfTVRGMDLA 320

                        330
                 ....*....|...
gi 482570798 443 AKSGRMCAEAIVE 455
Cdd:PRK10015 321 IASAQAAATTVIA 333
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 167-331 3.25e-05

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: 46.08  E-value: 3.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 167 LAQGGIETVLIERKMDNCK-PCGGAI-PLCMvgEFNLPLDIIDR------RVTKMKMISPSN--IAVDIGRTLKEHEYIG 236
Cdd:COG0654   22 LARAGIRVTVVERAPPPRPdGRGIALsPRSL--ELLRRLGLWDRllargaPIRGIRVRDGSDgrVLARFDAAETGLPAGL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 237 MVRREVLDAYLRERAEKSGATVInglflkmdhpenWDSPYT-LHYTEyDGKTGSTGTKKTMEVDAVIGADGANSRVAKSI 315
Cdd:COG0654  100 VVPRADLERALLEAARALGVELR------------FGTEVTgLEQDA-DGVTVTLADGRTLRADLVVGADGARSAVRRLL 166

                        170       180
                 ....*....|....*....|....*..
gi 482570798 316 DAG--DYDY---------AIAFQERIR 331
Cdd:COG0654  167 GIGftGRDYpqralwagvRTELRARLA 193
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 418-500 6.97e-04

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: 42.44  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798  418 SKRVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGKKMIDEGDLRKYLEKWDKTYLPTYRVLDVLQKVFYRS 497
Cdd:TIGR01989 332 TKRVALVGDAAHRVHPLAGQGVNLGFGDVASLVKALAEAVSVGADIGSISSLKPYERERYAKNVVLLGLVDKLHKLYATD 411


                  ...
gi 482570798  498 NPA 500
Cdd:TIGR01989 412 FPP 414
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 420-502 6.46e-03

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 38.98  E-value: 6.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 482570798 420 RVALVGDAAGYVTKCSGEGIYFAAKSGRMCAEAIVEGSQNGKKMIDEGDLRKYlEKWDKTylPTYRVLDVLQ---KVFYR 496
Cdd:PRK08850 283 RVALVGDAAHTIHPLAGQGVNLGLLDAASLAQEILALWQQGRDIGLKRNLRGY-ERWRKA--EAAKMIAAMQgfrDLFSG 359


                 ....*.
gi 482570798 497 SNPARE 502
Cdd:PRK08850 360 SNPAKK 365
 
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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