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Conserved domains on  [gi|30692923|ref|NP_568533|]
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cytochrome p450 81d1 [Arabidopsis thaliana]

Protein Classification

cytochrome P450( domain architecture ID 15335019)

cytochrome P450 catalyzes the oxidation of organic species by molecular oxygen, by the oxidative addition of atomic oxygen into an unactivated C-H or C-C bond

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
71-487 0e+00

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


:

Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 780.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHkVAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd20653   1 GPIFSLRFGSRLVVVVSSP-SAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAPYGDHWRNLRRITTLEIFSSHRLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAKRVRKLVADVGANTSSGN 230
Cdd:cd20653  80 SFSSIRRDEIRRLLKRLARDSKGGFAKVELKPLFSELTFNNIMRMVAGKRYYGEDVSDAEEAKLFRELVSEIFELSGAGN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 AVDYVPILRLFS--SYENRVKKLGEETDKFLQGLIDDKRGQQETGT-TMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAG 307
Cdd:cd20653 160 PADFLPILRWFDfqGLEKRVKKLAKRRDAFLQGLIDEHRKNKESGKnTMIDHLLSLQESQPEYYTDEIIKGLILVMLLAG 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 308 TNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGS 387
Cdd:cd20653 240 TDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVPHESSEDCKIGG 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 388 YDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE-EAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERV 466
Cdd:cd20653 320 YDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEErEGYKLIPFGLGRRACPGAGLAQRVVGLALGSLIQCFEWERV 399
                       410       420
                ....*....|....*....|.
gi 30692923 467 GNVEVDMKEGVGNTVPKAIPL 487
Cdd:cd20653 400 GEEEVDMTEGKGLTMPKAIPL 420
 
Name Accession Description Interval E-value
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
71-487 0e+00

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 780.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHkVAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd20653   1 GPIFSLRFGSRLVVVVSSP-SAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAPYGDHWRNLRRITTLEIFSSHRLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAKRVRKLVADVGANTSSGN 230
Cdd:cd20653  80 SFSSIRRDEIRRLLKRLARDSKGGFAKVELKPLFSELTFNNIMRMVAGKRYYGEDVSDAEEAKLFRELVSEIFELSGAGN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 AVDYVPILRLFS--SYENRVKKLGEETDKFLQGLIDDKRGQQETGT-TMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAG 307
Cdd:cd20653 160 PADFLPILRWFDfqGLEKRVKKLAKRRDAFLQGLIDEHRKNKESGKnTMIDHLLSLQESQPEYYTDEIIKGLILVMLLAG 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 308 TNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGS 387
Cdd:cd20653 240 TDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVPHESSEDCKIGG 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 388 YDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE-EAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERV 466
Cdd:cd20653 320 YDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEErEGYKLIPFGLGRRACPGAGLAQRVVGLALGSLIQCFEWERV 399
                       410       420
                ....*....|....*....|.
gi 30692923 467 GNVEVDMKEGVGNTVPKAIPL 487
Cdd:cd20653 400 GEEEVDMTEGKGLTMPKAIPL 420
PLN02687 PLN02687
flavonoid 3'-monooxygenase
15-489 2.21e-109

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 334.47  E-value: 2.21e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   15 SLIFLIISFKFL------KPKKQNLPPSPPGWlPIIGHLRLLKPPIHRTLRSFSETLdhndgGGVMSLRLGSRLVYVVSS 88
Cdd:PLN02687  11 TVAVSVLVWCLLlrrggsGKHKRPLPPGPRGW-PVLGNLPQLGPKPHHTMAALAKTY-----GPLFRLRFGFVDVVVAAS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   89 HKVAAEecFGK-NDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVRTDEVRRLISRL 167
Cdd:PLN02687  85 ASVAAQ--FLRtHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVALLVREL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  168 SRLAGTkkTVVELKPMLMDLTFNNIMRMMTGKRYYGEEttDEEEAKRVRKLVADVGANTSSGNAVDYVPILRLF--SSYE 245
Cdd:PLN02687 163 ARQHGT--APVNLGQLVNVCTTNALGRAMVGRRVFAGD--GDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLdlQGVV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  246 NRVKKLGEETDKFLQGLIDDKR----GQQETGTTMIDHLLVLQKSDI-----EYYTDQIIKGIILIMVIAGTNTSAVTLE 316
Cdd:PLN02687 239 GKMKRLHRRFDAMMNGIIEEHKaagqTGSEEHKDLLSTLLALKREQQadgegGRITDTEIKALLLNLFTAGTDTTSSTVE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  317 WALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTL 396
Cdd:PLN02687 319 WAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATL 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  397 LVNAWAIHRDPNTWDDPDSFKPERF----EKEEEAQK-----LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVG 467
Cdd:PLN02687 399 LVNVWAIARDPEQWPDPLEFRPDRFlpggEHAGVDVKgsdfeLIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELAD 478
                        490       500
                 ....*....|....*....|....*
gi 30692923  468 NV---EVDMKEGVGNTVPKAIPLKA 489
Cdd:PLN02687 479 GQtpdKLNMEEAYGLTLQRAVPLMV 503
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
35-464 1.93e-93

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 291.49  E-value: 1.93e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923    35 PSPPGWLPIIGHLRLL--KPPIHRTLRSFSETLdhndgGGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQ-VI 111
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLgrKGNLHSVFTKLQKKY-----GPIFRLYLGPKPVVVLSGPE-AVKEVLIKKGEEFSGRPDePW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   112 IGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNcFLYVRTDEVRRLISRLSRLAGTKKtVVELKPMLMDLTFNN 191
Cdd:pfam00067  75 FATSRGPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLS-FEPRVEEEARDLVEKLRKTAGEPG-VIDITDLLFRAALNV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   192 IMRMMTGKRYygeETTDEEEAKRVRKLVADVGAN--TSSGNAVDYVPILRLF-SSYENRVKKLGEETDKFLQGLIDDKRG 268
Cdd:pfam00067 153 ICSILFGERF---GSLEDPKFLELVKAVQELSSLlsSPSPQLLDLFPILKYFpGPHGRKLKRARKKIKDLLDKLIEERRE 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   269 ----QQETGTTMIDHLLVLQ-KSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLD 343
Cdd:pfam00067 230 tldsAKKSPRDFLDALLLAKeEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   344 RLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEK 423
Cdd:pfam00067 310 RSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLD 389
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 30692923   424 EEEAQK----LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWE 464
Cdd:pfam00067 390 ENGKFRksfaFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVE 434
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
71-488 7.21e-47

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 167.76  E-value: 7.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAApYGDHWRNLRRLCTiEIFSTHRLN 150
Cdd:COG2124  32 GPVFRVRLPGGGAWLVTRYE-DVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTL-DGPEHTRLRRLVQ-PAFTPRRVA 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 cfLYVRT--DEVRRLISRLSRlAGTkktvVELKPMLMDLTFNNIMRMMTGkryygeetTDEEEAKRVRKLVADVGAntss 228
Cdd:COG2124 109 --ALRPRirEIADELLDRLAA-RGP----VDLVEEFARPLPVIVICELLG--------VPEEDRDRLRRWSDALLD---- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 229 gnAVDYVPILRLFssyenRVKKLGEETDKFLQGLIDDKRgqQETGTTMIDHLLVLQkSDIEYYTDQIIKGIILIMVIAGT 308
Cdd:COG2124 170 --ALGPLPPERRR-----RARRARAELDAYLRELIAERR--AEPGDDLLSALLAAR-DDGERLSDEELRDELLLLLLAGH 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 309 NTSAVTLEWALSNLLNHPDViskardeidnrvgLDRLIEEadlseLPYLKNIVLETLRLHPATPLLvPHMASEDCKIGSY 388
Cdd:COG2124 240 ETTANALAWALYALLRHPEQ-------------LARLRAE-----PELLPAAVEETLRLYPPVPLL-PRTATEDVELGGV 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 389 DMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERfekeeEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFE-WERVG 467
Cdd:COG2124 301 TIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-----PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPdLRLAP 375
                       410       420
                ....*....|....*....|.
gi 30692923 468 NVEVDMKEGVGNTVPKAIPLK 488
Cdd:COG2124 376 PEELRWRPSLTLRGPKSLPVR 396
 
Name Accession Description Interval E-value
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
71-487 0e+00

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 780.63  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHkVAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd20653   1 GPIFSLRFGSRLVVVVSSP-SAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAPYGDHWRNLRRITTLEIFSSHRLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAKRVRKLVADVGANTSSGN 230
Cdd:cd20653  80 SFSSIRRDEIRRLLKRLARDSKGGFAKVELKPLFSELTFNNIMRMVAGKRYYGEDVSDAEEAKLFRELVSEIFELSGAGN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 AVDYVPILRLFS--SYENRVKKLGEETDKFLQGLIDDKRGQQETGT-TMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAG 307
Cdd:cd20653 160 PADFLPILRWFDfqGLEKRVKKLAKRRDAFLQGLIDEHRKNKESGKnTMIDHLLSLQESQPEYYTDEIIKGLILVMLLAG 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 308 TNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGS 387
Cdd:cd20653 240 TDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVPHESSEDCKIGG 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 388 YDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE-EAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERV 466
Cdd:cd20653 320 YDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEErEGYKLIPFGLGRRACPGAGLAQRVVGLALGSLIQCFEWERV 399
                       410       420
                ....*....|....*....|.
gi 30692923 467 GNVEVDMKEGVGNTVPKAIPL 487
Cdd:cd20653 400 GEEEVDMTEGKGLTMPKAIPL 420
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
71-487 4.37e-179

Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is considerably larger than in other taxa. In individual plant genomes, CYPs form the third largest family of plant genes; the two largest gene families code for F-box proteins and receptor-like kinases. CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. However, there is a phenomenon called family creep, where a sequence (below 40% identity) is absorbed into a large family; this is seen in the plant CYP71 and CYP89 families. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP71 clan has expanded dramatically and represents 50% of all plant CYPs; it includes several families including CYP71, CYP73, CYP76, CYP81, CYP82, CYP89, and CYP93, among others. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410711 [Multi-domain]  Cd Length: 429  Bit Score: 509.40  E-value: 4.37e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd20618   1 GPLMYLRLGSVPTVVVSSPE-MAKEVLKTQDAVFASRPRTAAGKIFSYNGQDIVFAPYGPHWRHLRKICTLELFSAKRLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRLAGTKKtVVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAKRVRKLVADVGANTSSGN 230
Cdd:cd20618  80 SFQGVRKEELSHLVKSLLEESESGK-PVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEAREFKELIDEAFELAGAFN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 AVDYVPILRLF--SSYENRVKKLGEETDKFLQGLIDDKR----GQQETGTTMIDHLLVLQKSDIEYYTDQIIKGIILIMV 304
Cdd:cd20618 159 IGDYIPWLRWLdlQGYEKRMKKLHAKLDRFLQKIIEEHRekrgESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLDML 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 305 IAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCK 384
Cdd:cd20618 239 AAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLPHESTEDCK 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 385 IGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQ------KLLAFGLGRRACPGSGLAQRIVGLALGSLI 458
Cdd:cd20618 319 VAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDvkgqdfELLPFGSGRRMCPGMPLGLRMVQLTLANLL 398
                       410       420       430
                ....*....|....*....|....*....|.
gi 30692923 459 QCFEWE--RVGNVEVDMKEGVGNTVPKAIPL 487
Cdd:cd20618 399 HGFDWSlpGPKPEDIDMEEKFGLTVPRAVPL 429
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
71-494 7.18e-147

cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically reside in dicots and are usually induced by distinct environmental stresses. Characterized members include: Glycine max CYP82A3 that is induced by infection, salinity and drought stresses, and is involved in the jasmonic acid and ethylene signaling pathway, enhancing plant resistance; Arabidopsis thaliana CYP82G1 that catalyzes the breakdown of the C(20)-precursor (E,E)-geranyllinalool to the insect-induced C(16)-homoterpene (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT); and Papaver somniferum CYP82N4, also called methyltetrahydroprotoberberine 14-monooxygenase, and CYP82Y1, also called N-methylcanadine 1-hydroxylase. CYP82N4 catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively, in the biosynthesis of isoquinoline alkaloid sanguinarine. CYP82Y1 catalyzes the 1-hydroxylation of N-methylcanadine to 1-hydroxy-N-methylcanadine, the first committed step in the formation of noscapine. CYP82 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 428.19  E-value: 7.18e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAaEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd20654   1 GPIFTLRLGSHPTLVVSSWEMA-KECFTTNDKAFSSRPKTAAAKLMGYNYAMFGFAPYGPYWRELRKIATLELLSNRRLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRLAGTKKTV-----VELKPMLMDLTFNNIMRMMTGKRYYGEETT-DEEEAKRVRKLVADVGA 224
Cdd:cd20654  80 KLKHVRVSEVDTSIKELYSLWSNNKKGgggvlVEMKQWFADLTFNVILRMVVGKRYFGGTAVeDDEEAERYKKAIREFMR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 225 NTSSGNAVDYVPILRL--FSSYENRVKKLGEETDKFLQGLIDD---KRGQQETGTTMIDHLLVLQKSDIE------YYTD 293
Cdd:cd20654 160 LAGTFVVSDAIPFLGWldFGGHEKAMKRTAKELDSILEEWLEEhrqKRSSSGKSKNDEDDDDVMMLSILEdsqisgYDAD 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 294 QIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPL 373
Cdd:cd20654 240 TVIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYPPGPL 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 374 LVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF---EKEEEAQ----KLLAFGLGRRACPGSGLA 446
Cdd:cd20654 320 LGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFlttHKDIDVRgqnfELIPFGSGRRSCPGVSFG 399
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 30692923 447 QRIVGLALGSLIQCFEWERVGNVEVDMKEGVGNTVPKAIPLKAICKAR 494
Cdd:cd20654 400 LQVMHLTLARLLHGFDIKTPSNEPVDMTEGPGLTNPKATPLEVLLTPR 447
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
71-487 7.70e-141

cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome P450 family 71 (CYP71) proteins, as well as some CYPs designated as belonging to a different family including CYP99A1, CYP83B1, and CYP84A1, among others. Characterized CYP71 enzymes include: parsnip (Pastinaca sativa) CYP71AJ4, also called angelicin synthase, that converts (+)-columbianetin to angelicin, an angular furanocumarin; periwinkle (Catharanthus roseus) CYP71D351, also called tabersonine 16-hydroxylase 2, that is involved in the foliar biosynthesis of vindoline; sorghum CYP71E1, also called 4-hydroxyphenylacetaldehyde oxime monooxygenase, that catalyzes the conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile; as well as maize CYP71C1, CYP71C2, and CYP71C4, which are monooxygenases catalyzing the oxidation of 3-hydroxyindolin-2-one, indolin-2-one, and indole, respectively. CYPs within a single CYP71 subfamily, such as the C subfamily, usually metabolize similar/related compounds. The CYP71-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410695 [Multi-domain]  Cd Length: 428  Bit Score: 411.86  E-value: 7.70e-141
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd11072   3 GPLMLLRLGSVPTVVVSSPE-AAKEVLKTHDLVFASRPKLLAARILSYGGKDIAFAPYGEYWRQMRKICVLELLSAKRVQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRLAGtKKTVVELKPMLMDLTFNNIMRMMTGKRYygeettDEEEAKRVRKLVADVGANTSSGN 230
Cdd:cd11072  82 SFRSIREEEVSLLVKKIRESAS-SSSPVNLSELLFSLTNDIVCRAAFGRKY------EGKDQDKFKELVKEALELLGGFS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 AVDYVPILR---LFSSYENRVKKLGEETDKFLQGLIDD----KRGQQETGTTMIDHLLVLQKSDIEYY--TDQIIKGIIL 301
Cdd:cd11072 155 VGDYFPSLGwidLLTGLDRKLEKVFKELDAFLEKIIDEhldkKRSKDEDDDDDDLLDLRLQKEGDLEFplTRDNIKAIIL 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 302 IMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASE 381
Cdd:cd11072 235 DMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLPRECRE 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 382 DCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK-----LLAFGLGRRACPGSGLAQRIVGLALGS 456
Cdd:cd11072 315 DCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIDFKgqdfeLIPFGAGRRICPGITFGLANVELALAN 394
                       410       420       430
                ....*....|....*....|....*....|....
gi 30692923 457 LIQCFEWE---RVGNVEVDMKEGVGNTVPKAIPL 487
Cdd:cd11072 395 LLYHFDWKlpdGMKPEDLDMEEAFGLTVHRKNPL 428
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
71-488 6.27e-135

cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in flowering plants and could be classified into ten subfamilies, CYP93A-K. CYP93A appears to be the ancestor that was derived in flowering plants, and the remaining subfamiles show lineage-specific distribution: CYP93B and CYP93C are present in dicots; CYP93F is distributed only in Poaceae; CYP93G and CYP93J are monocot-specific; CYP93E is unique to legumes; CYP93H and CYP93K are only found in Aquilegia coerulea; and CYP93D is Brassicaceae-specific. Members of this family include: Glycyrrhiza echinata CYP93B1, also called licodione synthase (EC 1.14.14.140), that catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively; and Glycine max CYP93A1, also called 3,9-dihydroxypterocarpan 6A-monooxygenase (EC 1.14.14.93), that is involved in the biosynthesis of the phytoalexin glyceollin. CYP93 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 396.97  E-value: 6.27e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAaEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd20655   1 GPLLHLRIGSVPCVVVSSASVA-KEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRlAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYYGEEttdeEEAKRVRKLVADVGANTSSGN 230
Cdd:cd20655  80 RFRPIRAQELERFLRRLLD-KAEKGESVDIGKELMKLTNNIICRMIMGRSCSEEN----GEAEEVRKLVKESAELAGKFN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 AVDYVPILRLF--SSYENRVKKLGEETDKFLQGLI----DDKRGQQETGTT-MIDHLLVL---QKSDIEYYTDQIiKGII 300
Cdd:cd20655 155 ASDFIWPLKKLdlQGFGKRIMDVSNRFDELLERIIkeheEKRKKRKEGGSKdLLDILLDAyedENAEYKITRNHI-KAFI 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 301 LIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVpHMAS 380
Cdd:cd20655 234 LDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLV-REST 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 381 EDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF----------EKEEEAQKLLAFGLGRRACPGSGLAQRIV 450
Cdd:cd20655 313 EGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFlassrsgqelDVRGQHFKLLPFGSGRRGCPGASLAYQVV 392
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 30692923 451 GLALGSLIQCFEWERVGNVEVDMKEGVGNTVPKAIPLK 488
Cdd:cd20655 393 GTAIAAMVQCFDWKVGDGEKVNMEEASGLTLPRAHPLK 430
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
71-490 6.26e-132

cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant cytochrome P450 family 76 (CYP76 or Cyp76) include: Catharanthus roseus CYP76B6, a multifunctional enzyme catalyzing two sequential oxidation steps leading to the formation of 8-oxogeraniol from geraniol; the Brassicaceae-specific CYP76C subfamily of enzymes that are involved in the metabolism of monoterpenols and phenylurea herbicides; and two P450s from Lamiaceae, CYP76AH and CYP76AK, that are involved in the oxidation of abietane diterpenes. CYP76AH produces ferruginol and 11-hydroxyferruginol, while CYP76AK catalyzes oxidations at the C20 position. Also included in this group is Berberis stolonifera Cyp80, also called berbamunine synthase or (S)-N-methylcoclaurine oxidase [C-O phenol-coupling], that catalyzes the phenol oxidation of N-methylcoclaurine to form the bisbenzylisoquinoline alkaloid berbamunine. The CYP76-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 389.58  E-value: 6.26e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSShKVAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd11073   5 GPIMSLKLGSKTTVVVSS-PEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPKRLD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRLAGtKKTVVELKPMLMDLTFNNIMRMMTGKRYYGEettDEEEAKRVRKLVADVGANTSSGN 230
Cdd:cd11073  84 ATQPLRRRKVRELVRYVREKAG-SGEAVDIGRAAFLTSLNLISNTLFSVDLVDP---DSESGSEFKELVREIMELAGKPN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 AVDYVPILRLF--SSYENRVKKLGEETDKFLQGLIDDKRGQQETGTT-----MIDHLLVLQKSDIEYYTDQIIKGIILIM 303
Cdd:cd11073 160 VADFFPFLKFLdlQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDkkkddDLLLLLDLELDSESELTRNHIKALLLDL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 304 VIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDC 383
Cdd:cd11073 240 FVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAEEDV 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 384 KIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK-----LLAFGLGRRACPGSGLAQRIVGLALGSLI 458
Cdd:cd11073 320 EVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKgrdfeLIPFGSGRRICPGLPLAERMVHLVLASLL 399
                       410       420       430
                ....*....|....*....|....*....|....*
gi 30692923 459 QCFEWERVGNV---EVDMKEGVGNTVPKAIPLKAI 490
Cdd:cd11073 400 HSFDWKLPDGMkpeDLDMEEKFGLTLQKAVPLKAI 434
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
71-494 4.03e-110

cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the biosynthesis of colored class of flavonoids, anthocyanins, which confer a diverse range of colors to flowers from orange to red to violet and blue. The number of hydroxyl groups on the B-ring of anthocyanidins, the chromophores and precursors of anthocyanins, impact the anthocyanin color - the more the bluer. The hydroxylation pattern is determined by CYP75 proteins: flavonoid 3'-hydroxylase (F3'H, EC 1.14.14.82) and and flavonoid 3',5'-hydroxylase (F3'5'H, EC 1.14.14.81), which belong to CYP75B and CYP75A subfamilies, respectively. Both enzymes have broad substrate specificity and catalyze the hydroxylation of flavanones, dihydroflavonols, flavonols and flavones. F3'H catalyzes the 3'-hydroxylation of the flavonoid B-ring to the 3',4'-hydroxylated state. F3'5'H catalysis leads to trihydroxylated delphinidin-based anthocyanins that tend to have violet/blue colours. CYP75 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 333.62  E-value: 4.03e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAAEeCFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd20657   1 GPIMYLKVGSCGVVVASSPPVAKA-FLKTHDANFSNRPPNAGATHMAYNAQDMVFAPYGPRWRLLRKLCNLHLFGGKALE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRlAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYYGEetTDEEEAKRVRKLVADVGANTSSGN 230
Cdd:cd20657  80 DWAHVRENEVGHMLKSMAE-ASRKGEPVVLGEMLNVCMANMLGRVMLSKRVFAA--KAGAKANEFKEMVVELMTVAGVFN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 AVDYVPILRLF--SSYENRVKKLGEETDKFLQGLIDD-KRGQQETGTTMIDHLLVLQK----SDIEYYTDQIIKGIILIM 303
Cdd:cd20657 157 IGDFIPSLAWMdlQGVEKKMKRLHKRFDALLTKILEEhKATAQERKGKPDFLDFVLLEnddnGEGERLTDTNIKALLLNL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 304 VIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDC 383
Cdd:cd20657 237 FTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEAC 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 384 KIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQ--------KLLAFGLGRRACPGSGLAQRIVGLALG 455
Cdd:cd20657 317 EVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGRNAKvdvrgndfELIPFGAGRRICAGTRMGIRMVEYILA 396
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 30692923 456 SLIQCFEWERVGN---VEVDMKEGVGNTVPKAIPLKAICKAR 494
Cdd:cd20657 397 TLVHSFDWKLPAGqtpEELNMEEAFGLALQKAVPLVAHPTPR 438
PLN02687 PLN02687
flavonoid 3'-monooxygenase
15-489 2.21e-109

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 334.47  E-value: 2.21e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   15 SLIFLIISFKFL------KPKKQNLPPSPPGWlPIIGHLRLLKPPIHRTLRSFSETLdhndgGGVMSLRLGSRLVYVVSS 88
Cdd:PLN02687  11 TVAVSVLVWCLLlrrggsGKHKRPLPPGPRGW-PVLGNLPQLGPKPHHTMAALAKTY-----GPLFRLRFGFVDVVVAAS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   89 HKVAAEecFGK-NDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVRTDEVRRLISRL 167
Cdd:PLN02687  85 ASVAAQ--FLRtHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVALLVREL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  168 SRLAGTkkTVVELKPMLMDLTFNNIMRMMTGKRYYGEEttDEEEAKRVRKLVADVGANTSSGNAVDYVPILRLF--SSYE 245
Cdd:PLN02687 163 ARQHGT--APVNLGQLVNVCTTNALGRAMVGRRVFAGD--GDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLdlQGVV 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  246 NRVKKLGEETDKFLQGLIDDKR----GQQETGTTMIDHLLVLQKSDI-----EYYTDQIIKGIILIMVIAGTNTSAVTLE 316
Cdd:PLN02687 239 GKMKRLHRRFDAMMNGIIEEHKaagqTGSEEHKDLLSTLLALKREQQadgegGRITDTEIKALLLNLFTAGTDTTSSTVE 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  317 WALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTL 396
Cdd:PLN02687 319 WAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATL 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  397 LVNAWAIHRDPNTWDDPDSFKPERF----EKEEEAQK-----LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVG 467
Cdd:PLN02687 399 LVNVWAIARDPEQWPDPLEFRPDRFlpggEHAGVDVKgsdfeLIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELAD 478
                        490       500
                 ....*....|....*....|....*
gi 30692923  468 NV---EVDMKEGVGNTVPKAIPLKA 489
Cdd:PLN02687 479 GQtpdKLNMEEAYGLTLQRAVPLMV 503
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
8-494 6.15e-105

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 322.93  E-value: 6.15e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923    8 VVLYSIFS-LIFLIISFKFLKP---KKQNLPPSPPGWlPIIGHLRLLKPPIHRTLRSFsetldHNDGGGVMSLRLGSRLV 83
Cdd:PLN03112   4 FLLSLLFSvLIFNVLIWRWLNAsmrKSLRLPPGPPRW-PIVGNLLQLGPLPHRDLASL-----CKKYGPLVYLRLGSVDA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   84 YVVSSHKVAAEeCFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVRTDEVRRL 163
Cdd:PLN03112  78 ITTDDPELIRE-ILLRQDDVFASRPRTLAAVHLAYGCGDVALAPLGPHWKRMRRICMEHLLTTKRLESFAKHRAEEARHL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  164 ISRLSRLAGTKKtVVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAKRVRKLVADVGANTSSGNAVDYVPILRLFSS 243
Cdd:PLN03112 157 IQDVWEAAQTGK-PVNLREVLGAFSMNNVTRMLLGKQYFGAESAGPKEAMEFMHITHELFRLLGVIYLGDYLPAWRWLDP 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  244 Y--ENRVKKLGEETDKFLQGLIDDKR----GQQETGTTM--IDHLLVLQKSDIEYYTDQI-IKGIILIMVIAGTNTSAVT 314
Cdd:PLN03112 236 YgcEKKMREVEKRVDEFHDKIIDEHRrarsGKLPGGKDMdfVDVLLSLPGENGKEHMDDVeIKALMQDMIAAATDTSAVT 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  315 LEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGT 394
Cdd:PLN03112 316 NEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKT 395
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  395 TLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQ---------KLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEW-- 463
Cdd:PLN03112 396 RVFINTHGLGRNTKIWDDVEEFRPERHWPAEGSRveishgpdfKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWsp 475
                        490       500       510
                 ....*....|....*....|....*....|..
gi 30692923  464 -ERVGNVEVDMKEGVGNTVPKAIPLKAICKAR 494
Cdd:PLN03112 476 pDGLRPEDIDTQEVYGMTMPKAKPLRAVATPR 507
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
71-489 1.37e-102

cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the meta-hydroxylation step in the phenylpropanoid biosynthetic pathway. CYP98A3, also called p-coumaroylshikimate/quinate 3'-hydroxylase, catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. CYP98A8, also called p-coumarate 3-hydroxylase, acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. CYP98 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 314.42  E-value: 1.37e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd20656   2 GPIISVWIGSTLNVVVSSSE-LAKEVLKEKDQQLADRHRTRSAARFSRNGQDLIWADYGPHYVKVRKLCTLELFTPKRLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSR---LAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAKRVRKLVADVGANTS 227
Cdd:cd20656  81 SLRPIREDEVTAMVESIFNdcmSPENEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEQGVEFKAIVSNGLKLGA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 228 SGNAVDYVPILR-LFSSYENRVKKLGEETDKFLQGLIDDKR-GQQETGTTM--IDHLLVLQKSDiEYYTDQIIkGIILIM 303
Cdd:cd20656 161 SLTMAEHIPWLRwMFPLSEKAFAKHGARRDRLTKAIMEEHTlARQKSGGGQqhFVALLTLKEQY-DLSEDTVI-GLLWDM 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 304 VIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDC 383
Cdd:cd20656 239 ITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHKASENV 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 384 KIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK-----LLAFGLGRRACPGSGLAQRIVGLALGSLI 458
Cdd:cd20656 319 KIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKghdfrLLPFGAGRRVCPGAQLGINLVTLMLGHLL 398
                       410       420       430
                ....*....|....*....|....*....|....
gi 30692923 459 QCFEW---ERVGNVEVDMKEGVGNTVPKAIPLKA 489
Cdd:cd20656 399 HHFSWtppEGTPPEEIDMTENPGLVTFMRTPLQA 432
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
71-488 1.45e-94

cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes cytochrome P450 families 73 (CYP77) and 89 (CYP89), which are sister families that share a common ancestor. CYP89, present only in angiosperms, is younger than CYP77, which is already found in lycopods; thus, CYP89 may have evolved from CYP77 after duplication and divergence. Also included in this group is ent-kaurene oxidase, called CYP701A3 in Arabidopsis thaliana and CYP701B1 in Physcomitrella patens, that catalyzes the oxidation of ent-kaurene to form ent-kaurenoic acid. CYP701A3 is sensitive to inhibitor uniconazole-P while CYP701B1 is not. This CYP77/89 group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410698 [Multi-domain]  Cd Length: 433  Bit Score: 293.77  E-value: 1.45e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAAEECFGKNDVVlANRPQVIIGKHVGYNNTNMIA-APYGDHWRNLRRLCTIEIFSTHRL 149
Cdd:cd11075   3 GPIFTLRMGSRPLIVVASRELAHEALVQKGSSF-ASRPPANPLRVLFSSNKHMVNsSPYGPLWRTLRRNLVSEVLSPSRL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 150 NCFLYVRTDEVRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRyygeetTDEEEAKRVRKLVADVGANTSSG 229
Cdd:cd11075  82 KQFRPARRRALDNLVERLREEAKENPGPVNVRDHFRHALFSLLLYMCFGER------LDEETVRELERVQRELLLSFTDF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 230 NAVDYVPILR--LFSSYENRVKKLGEETDKFLQGLIDDKRGQQETG---------TTMIDHLLVLQKSDIEYYTDQIIkg 298
Cdd:cd11075 156 DVRDFFPALTwlLNRRRWKKVLELRRRQEEVLLPLIRARRKRRASGeadkdytdfLLLDLLDLKEEGGERKLTDEELV-- 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 299 iILIM--VIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVP 376
Cdd:cd11075 234 -SLCSefLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHFLLP 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 377 HMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF--EKEEEAQ-------KLLAFGLGRRACPGSGLAQ 447
Cdd:cd11075 313 HAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFlaGGEAADIdtgskeiKMMPFGAGRRICPGLGLAT 392
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 30692923 448 RIVGLALGSLIQCFEWERVGNVEVDMKEGVGNTVPKAIPLK 488
Cdd:cd11075 393 LHLELFVARLVQEFEWKLVEGEEVDFSEKQEFTVVMKNPLR 433
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
35-464 1.93e-93

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 291.49  E-value: 1.93e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923    35 PSPPGWLPIIGHLRLL--KPPIHRTLRSFSETLdhndgGGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQ-VI 111
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLgrKGNLHSVFTKLQKKY-----GPIFRLYLGPKPVVVLSGPE-AVKEVLIKKGEEFSGRPDePW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   112 IGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNcFLYVRTDEVRRLISRLSRLAGTKKtVVELKPMLMDLTFNN 191
Cdd:pfam00067  75 FATSRGPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLS-FEPRVEEEARDLVEKLRKTAGEPG-VIDITDLLFRAALNV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   192 IMRMMTGKRYygeETTDEEEAKRVRKLVADVGAN--TSSGNAVDYVPILRLF-SSYENRVKKLGEETDKFLQGLIDDKRG 268
Cdd:pfam00067 153 ICSILFGERF---GSLEDPKFLELVKAVQELSSLlsSPSPQLLDLFPILKYFpGPHGRKLKRARKKIKDLLDKLIEERRE 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   269 ----QQETGTTMIDHLLVLQ-KSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLD 343
Cdd:pfam00067 230 tldsAKKSPRDFLDALLLAKeEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDK 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   344 RLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEK 423
Cdd:pfam00067 310 RSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLD 389
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 30692923   424 EEEAQK----LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWE 464
Cdd:pfam00067 390 ENGKFRksfaFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVE 434
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
71-482 2.96e-90

cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome P450 families 1 (CYP1) and 2 (CYP2), CYP17A1, and CYP21 in vertebrates, as well as insect and crustacean CYPs similar to CYP15A1 and CYP306A1. CYP1 and CYP2 enzymes are involved in the metabolism of endogenous and exogenous compounds such as hormones, xenobiotics, and drugs. CYP17A1 catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products, while CYP21 catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. Members of this group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410710 [Multi-domain]  Cd Length: 419  Bit Score: 281.79  E-value: 2.96e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAaEECFGKNDVVLANRPQVIIGKHVGYNNtNMIAApYGDHWRNLRRLCTIEiFSTHRLN 150
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEII-KEAFVKNGDNFSDRPLLPSFEIISGGK-GILFS-NGDYWKELRRFALSS-LTKTKLK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVR-TDEVRRLISRLSRLAGTKKtVVELKPMLMDLTFNNIMRMMTGKRYygeETTDEEEAKRVRKLVADVGANTSSG 229
Cdd:cd20617  77 KKMEELiEEEVNKLIESLKKHSKSGE-PFDPRPYFKKFVLNIINQFLFGKRF---PDEDDGEFLKLVKPIEEIFKELGSG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 230 NAVDYVPILRLF-SSYENRVKKLGEETDKFLQGLIDDKRGQQETGT----TMIDHLLVLQKSDIEYYTDQIIKGIILIMV 304
Cdd:cd20617 153 NPSDFIPILLPFyFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNprdlIDDELLLLLKEGDSGLFDDDSIISTCLDLF 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 305 IAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCK 384
Cdd:cd20617 233 LAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTE 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 385 IGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF---EKEEEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCF 461
Cdd:cd20617 313 IGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFlenDGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNF 392
                       410       420
                ....*....|....*....|.
gi 30692923 462 EWERVGNVEVDMKEGVGNTVP 482
Cdd:cd20617 393 KFKSSDGLPIDEKEVFGLTLK 413
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
71-496 7.82e-86

cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus cytochrome P450 64 (CYP64), also called O-methylsterigmatocystin (OMST) oxidoreductase or aflatoxin B synthase or aflatoxin biosynthesis protein Q, and similar fungal cytochrome P450s. CYP64 converts OMST to aflatoxin B1 and converts dihydro-O-methylsterigmatocystin (DHOMST) to aflatoxin B2 in the aflatoxin biosynthesis pathway. The CYP64-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410688 [Multi-domain]  Cd Length: 425  Bit Score: 270.60  E-value: 7.82e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAaEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTiEIFSTHRLN 150
Cdd:cd11065   2 GPIISLKVGGQTIIVLNSPKAA-KDLLEKRSAIYSSRPRMPMAGELMGWGMRLLLMPYGPRWRLHRRLFH-QLLNPSAVR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLsrLAGTKKTVVELKPMlmdlTFNNIMRMMTGKRyygEETTDEEEAKRVRKLVADVGANTSSGN 230
Cdd:cd11065  80 KYRPLQELESKQLLRDL--LESPDDFLDHIRRY----AASIILRLAYGYR---VPSYDDPLLRDAEEAMEGFSEAGSPGA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 A-VDYVPILR-----LFSSYENRVKKLGEETDKFLQGLIDDKRGQQETGT---TMIDHLLvlQKSDIEY-YTDQIIKGII 300
Cdd:cd11065 151 YlVDFFPFLRylpswLGAPWKRKARELRELTRRLYEGPFEAAKERMASGTatpSFVKDLL--EELDKEGgLSEEEIKYLA 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 301 LIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMAS 380
Cdd:cd11065 229 GSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIPHALT 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 381 EDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK------LLAFGLGRRACPGSGLAQRIVGLAL 454
Cdd:cd11065 309 EDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPdppdppHFAFGFGRRICPGRHLAENSLFIAI 388
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 30692923 455 GSLIQCFEWERVGNVEVDMKEgvgntVPKAIPLKAICKARPF 496
Cdd:cd11065 389 ARLLWAFDIKKPKDEGGKEIP-----DEPEFTDGLVSHPLPF 425
PLN02183 PLN02183
ferulate 5-hydroxylase
10-494 2.06e-85

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 272.49  E-value: 2.06e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   10 LYSIFSLIFLIIsFKFLKPKKQNLPPSPPGWlPIIGHLRLLKPPIHRTLRSFSETLdhndgGGVMSLRLGSRLVYVVSSH 89
Cdd:PLN02183  15 FLILISLFLFLG-LISRLRRRLPYPPGPKGL-PIIGNMLMMDQLTHRGLANLAKQY-----GGLFHMRMGYLHMVAVSSP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   90 KVAaEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVRtDEVRRLISRLSR 169
Cdd:PLN02183  88 EVA-RQVLQVQDSVFSNRPANIAISYLTYDRADMAFAHYGPFWRQMRKLCVMKLFSRKRAESWASVR-DEVDSMVRSVSS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  170 LAGTKKTVVELkpmLMDLTFNNIMRMMTGkryygeeTTDEEEAKRVRKLVADVGANTSSGNAVDYVPILRLFSSYE--NR 247
Cdd:PLN02183 166 NIGKPVNIGEL---IFTLTRNITYRAAFG-------SSSNEGQDEFIKILQEFSKLFGAFNVADFIPWLGWIDPQGlnKR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  248 VKKLGEETDKFLQGLIDD---KRGQQ-------ETGTTMIDHLLV-------------LQKSdIEYYTDQIiKGIILIMV 304
Cdd:PLN02183 236 LVKARKSLDGFIDDIIDDhiqKRKNQnadndseEAETDMVDDLLAfyseeakvnesddLQNS-IKLTRDNI-KAIIMDVM 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  305 IAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVpHMASEDCK 384
Cdd:PLN02183 314 FGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLL-HETAEDAE 392
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  385 IGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQ------KLLAFGLGRRACPGSGLAQRIVGLALGSLI 458
Cdd:PLN02183 393 VAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVPDfkgshfEFIPFGSGRRSCPGMQLGLYALDLAVAHLL 472
                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 30692923  459 QCFEWERVGNV---EVDMKEGVGNTVPKAIPLKAICKAR 494
Cdd:PLN02183 473 HCFTWELPDGMkpsELDMNDVFGLTAPRATRLVAVPTYR 511
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
5-462 3.66e-84

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 268.91  E-value: 3.66e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923    5 NIRVVLYSIFSLIFLIISFKFLKPKKQNLPPSPPGwLPIIGH-LRLLKPPIHRTLRSFSETLdhndgGGVMSLRLGSRLV 83
Cdd:PLN02394   3 LLEKTLLGLFVAIVLALLVSKLRGKKLKLPPGPAA-VPIFGNwLQVGDDLNHRNLAEMAKKY-----GDVFLLRMGQRNL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   84 YVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVRTDEVRRL 163
Cdd:PLN02394  77 VVVSSPE-LAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGDHWRKMRRIMTVPFFTNKVVQQYRYGWEEEADLV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  164 ISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAKRVRKLVADVgANTSSGNAVDYVPILRLF-S 242
Cdd:PLN02394 156 VEDVRANPEAATEGVVIRRRLQLMMYNIMYRMMFDRRFESEDDPLFLKLKALNGERSRL-AQSFEYNYGDFIPILRPFlR 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  243 SYENRVKKLGEE-----TDKFLQ---GLIDDKRGQQETGTTMIDHLLVLQKSDiEYYTDQIIKgIILIMVIAGTNTSAVT 314
Cdd:PLN02394 235 GYLKICQDVKERrlalfKDYFVDerkKLMSAKGMDKEGLKCAIDHILEAQKKG-EINEDNVLY-IVENINVAAIETTLWS 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  315 LEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGT 394
Cdd:PLN02394 313 IEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGYDIPAES 392
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30692923  395 TLLVNAWAIHRDPNTWDDPDSFKPERFEKEE---EAQ----KLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFE 462
Cdd:PLN02394 393 KILVNAWWLANNPELWKNPEEFRPERFLEEEakvEANgndfRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFE 467
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
15-494 3.73e-84

flavonoid 3',5'-hydroxylase (F3'5'H); Provisional


Pssm-ID: 177725  Cd Length: 504  Bit Score: 269.03  E-value: 3.73e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   15 SLIFLIISF--KFLKPKK-QNLPPSPPGWlPIIGHLRLLKPPIHRTLRSFSETLdhndgGGVMSLRLGSRLVyVVSSHKV 91
Cdd:PLN00110  11 TLLFFITRFfiRSLLPKPsRKLPPGPRGW-PLLGALPLLGNMPHVALAKMAKRY-----GPVMFLKMGTNSM-VVASTPE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   92 AAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVRTDEVRRLISRLSRLA 171
Cdd:PLN00110  84 AARAFLKTLDINFSNRPPNAGATHLAYGAQDMVFADYGPRWKLLRKLSNLHMLGGKALEDWSQVRTVELGHMLRAMLELS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  172 GTKKTVVeLKPMLMDLTFNNIMRMMTGKRYYgeeTTDEEEAKRVRKLVADVGANTSSGNAVDYVPILRL--FSSYENRVK 249
Cdd:PLN00110 164 QRGEPVV-VPEMLTFSMANMIGQVILSRRVF---ETKGSESNEFKDMVVELMTTAGYFNIGDFIPSIAWmdIQGIERGMK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  250 KLGEETDKFLQGLIDDKRGQQETGTTMIDHLLVL----QKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNH 325
Cdd:PLN00110 240 HLHKKFDKLLTRMIEEHTASAHERKGNPDFLDVVmanqENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKN 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  326 PDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHR 405
Cdd:PLN00110 320 PSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGR 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  406 DPNTWDDPDSFKPERFEKEEEAQ--------KLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDMKEGV 477
Cdd:PLN00110 400 DPDVWENPEEFRPERFLSEKNAKidprgndfELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVELNMDEAF 479
                        490
                 ....*....|....*..
gi 30692923  478 GNTVPKAIPLKAICKAR 494
Cdd:PLN00110 480 GLALQKAVPLSAMVTPR 496
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
73-475 1.17e-81

cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins include: CYP78A5, which is expressed in leaf, flora and embryo, and has been reported to stimulate plant organ growth in Arabidopsis thaliana and to regulate plant architecture, ripening time, and fruit mass in tomato; Glycine max CYP78A10 that functions in regulating seed size/weight and pod number; and Physcomitrella patens CYP78A27 or CYP78A28, which together, are essential in bud formation. The CYP78 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 259.95  E-value: 1.17e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  73 VMSLRLGSRLVyVVSSHKVAAEECFgkNDVVLANRP------QVIIGKHVGYnntnmiaAPYGDHWRNLRRLCTIEIFST 146
Cdd:cd11076   5 LMAFSLGETRV-VITSHPETAREIL--NSPAFADRPvkesayELMFNRAIGF-------APYGEYWRNLRRIASNHLFSP 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 147 HRLNCFLYVRTDEVRRLISRLSRLAgTKKTVVELKPMLMDLTFNNIMRMMTGKRYygEETTDEEEAKRVRKLVAD----V 222
Cdd:cd11076  75 RRIAASEPQRQAIAAQMVKAIAKEM-ERSGEVAVRKHLQRASLNNIMGSVFGRRY--DFEAGNEEAEELGEMVREgyelL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 223 GANtssgNAVDYVPILRLF--SSYENRVKKLGEETDKFLQGLIDDKRGQQETGTTMI----DHLLVLQKSDIEYYTDQIi 296
Cdd:cd11076 152 GAF----NWSDHLPWLRWLdlQGIRRRCSALVPRVNTFVGKIIEEHRAKRSNRARDDeddvDVLLSLQGEEKLSDSDMI- 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 297 kGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLV- 375
Cdd:cd11076 227 -AVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGPLLSw 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 376 PHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQ---------KLLAFGLGRRACPGSGLA 446
Cdd:cd11076 306 ARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGAdvsvlgsdlRLAPFGAGRRVCPGKALG 385
                       410       420
                ....*....|....*....|....*....
gi 30692923 447 QRIVGLALGSLIQCFEWERVGNVEVDMKE 475
Cdd:cd11076 386 LATVHLWVAQLLHEFEWLPDDAKPVDLSE 414
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
71-464 1.70e-81

cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily contains cytochrome P450 17A1 (CYP17A1 or Cyp17a1), cytochrome P450 21 (CYP21 or Cyp21) and similar proteins. CYP17A1, also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione; it catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. This subfamily also contains CYP21, also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2, catalyzes the 21-hydroxylation of steroids and is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. The CYP17A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410653 [Multi-domain]  Cd Length: 428  Bit Score: 259.45  E-value: 1.70e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLctieIFSTHRLN 150
Cdd:cd11027   2 GDVFSLYLGSRLVVVLNSGA-AIKEALVKKSADFAGRPKLFTFDLFSRGGKDIAFGDYSPTWKLHRKL----AHSALRLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVR-----TDEVRRLISRLSRLAGTkktVVELKPMLMDLTFNNIMRMMTGKRYygeeTTDEEEAKRVRKLVADVGAN 225
Cdd:cd11027  77 ASGGPRleekiAEEAEKLLKRLASQEGQ---PFDPKDELFLAVLNVICSITFGKRY----KLDDPEFLRLLDLNDKFFEL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 226 TSSGNAVDYVPILRLFSSYENR-VKKLGEETDKFLQGLIDDKRGQQETGTT--MIDHLLVLQK-------SDIEYYTDQI 295
Cdd:cd11027 150 LGAGSLLDIFPFLKYFPNKALReLKELMKERDEILRKKLEEHKETFDPGNIrdLTDALIKAKKeaedegdEDSGLLTDDH 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 296 IKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLV 375
Cdd:cd11027 230 LVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLAL 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 376 PHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF--EKEEEAQK---LLAFGLGRRACPGSGLAQRIV 450
Cdd:cd11027 310 PHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFldENGKLVPKpesFLPFSAGRRVCLGESLAKAEL 389
                       410
                ....*....|....
gi 30692923 451 GLALGSLIQCFEWE 464
Cdd:cd11027 390 FLFLARLLQKFRFS 403
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
77-494 5.15e-78

cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first committed step in the biosynthesis of the core structure of glucosinolates, the conversion of amino acids to the corresponding aldoximes. Glucosinolates are amino acid-derived natural plant products that function in the defense against herbivores and microorganisms. Arabidopsis thaliana contains seven family members: CYP79B2 and CYP79B3, which metabolize trytophan; CYP79F1 and CYP79F2, which metabolize chain-elongated methionine derivatives with respectively 1-6 or 5-6 additional methylene groups in the side chain; CYP79A2 that metabolizes phenylalanine; and CYP79C1 and CYP79C2, with unknown function. CYP79 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 251.13  E-value: 5.15e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  77 RLGSRLVYVVSSHKVAaEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVR 156
Cdd:cd20658   7 RLGNTHVIPVTCPKIA-REILRKQDAVFASRPLTYATEIISGGYKTTVISPYGEQWKKMRKVLTTELMSPKRHQWLHGKR 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 157 TDEVRRLISRLSRLA--GTKKTVVELKPMLMDLTFNNIMRMMTGKRYYGEETTD----EEEAKRVRKLVADVGAnTSSGN 230
Cdd:cd20658  86 TEEADNLVAYVYNMCkkSNGGGLVNVRDAARHYCGNVIRKLMFGTRYFGKGMEDggpgLEEVEHMDAIFTALKC-LYAFS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 AVDYVPILRLFS--SYENRVKKLGEETDKFLQGLIDDKRGQ-QETGTTMI----DHLLVLQKSDIEY-YTDQIIKGIILI 302
Cdd:cd20658 165 ISDYLPFLRGLDldGHEKIVREAMRIIRKYHDPIIDERIKQwREGKKKEEedwlDVFITLKDENGNPlLTPDEIKAQIKE 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 303 MVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASED 382
Cdd:cd20658 245 LMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNVPHVAMSD 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 383 CKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKE-------EEAQKLLAFGLGRRACPGSGLAQRIVGLALG 455
Cdd:cd20658 325 TTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEdsevtltEPDLRFISFSTGRRGCPGVKLGTAMTVMLLA 404
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 30692923 456 SLIQCFEWERVGNVE-VDMKEGVGNTVPkAIPLKAICKAR 494
Cdd:cd20658 405 RLLQGFTWTLPPNVSsVDLSESKDDLFM-AKPLVLVAKPR 443
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
71-462 1.32e-70

cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called trans-cinnamate 4-monooxygenase (EC 1.14.14.91) or cinnamic acid 4-hydroxylase, catalyzes the regiospecific 4-hydroxylation of cinnamic acid to form precursors of lignin and many other phenolic compounds. It controls the general phenylpropanoid pathway, and controls carbon flux to pigments essential for pollination or UV protection. CYP73 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 231.59  E-value: 1.32e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAaEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLN 150
Cdd:cd11074   4 GDIFLLRMGQRNLVVVSSPELA-KEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGEHWRKMRRIMTVPFFTNKVVQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYygeETTDEEEAKRVRKLVADVG--ANTSS 228
Cdd:cd11074  83 QYRYGWEEEAARVVEDVKKNPEAATEGIVIRRRLQLMMYNNMYRIMFDRRF---ESEDDPLFVKLKALNGERSrlAQSFE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 229 GNAVDYVPILRLF-SSYENRVKKLGEETDKFLQGLIDDKRGQQETGTTM--------IDHLLVLQKSDiEYYTDQIIKgI 299
Cdd:cd11074 160 YNYGDFIPILRPFlRGYLKICKEVKERRLQLFKDYFVDERKKLGSTKSTkneglkcaIDHILDAQKKG-EINEDNVLY-I 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 300 ILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMA 379
Cdd:cd11074 238 VENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLRMAIPLLVPHMN 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 380 SEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF---EKEEEAQ----KLLAFGLGRRACPGSGLAQRIVGL 452
Cdd:cd11074 318 LHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFleeESKVEANgndfRYLPFGVGRRSCPGIILALPILGI 397
                       410
                ....*....|
gi 30692923 453 ALGSLIQCFE 462
Cdd:cd11074 398 TIGRLVQNFE 407
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
22-463 5.06e-67

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 223.80  E-value: 5.06e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   22 SFKFLKP---KKQNLPPSPPGwLPIIGHLRLLKP--PIHRTLRsFSETLdhndgGGVMSLRLGSRLVYVVSSHKVAaEEC 96
Cdd:PLN03234  15 AFFFLRSttkKSLRLPPGPKG-LPIIGNLHQMEKfnPQHFLFR-LSKLY-----GPIFTMKIGGRRLAVISSAELA-KEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   97 FGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVRTDEVRRLISRLSRLAGTKKT 176
Cdd:PLN03234  87 LKTQDLNFTARPLLKGQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  177 VvELKPMLMDLTFNNIMRMMTGKRY--YGEETtdeeeaKRVRKLVADVGANTSS---GNAVDYVPILRLFSSYENRVKKL 251
Cdd:PLN03234 167 V-DLSELLLSFTNCVVCRQAFGKRYneYGTEM------KRFIDILYETQALLGTlffSDLFPYFGFLDNLTGLSARLKKA 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  252 GEETDKFLQGLIDD----KRGQQETgTTMIDHLLVLQKsDIEY---YTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLN 324
Cdd:PLN03234 240 FKELDTYLQELLDEtldpNRPKQET-ESFIDLLMQIYK-DQPFsikFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIK 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  325 HPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIH 404
Cdd:PLN03234 318 YPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVS 397
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30692923  405 RDPNTW-DDPDSFKPERFEKEEEAQ-------KLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEW 463
Cdd:PLN03234 398 RDTAAWgDNPNEFIPERFMKEHKGVdfkgqdfELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDW 464
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
71-472 4.55e-64

cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including Diploptera punctata cytochrome P450 15A1 (CYP15A1 or CYP15A1), Panulirus argus CYP2L1, and CYP303A1, CYP304A1, and CYP305A1 from Drosophila melanogaster. CYP15A1, also called methyl farnesoate epoxidase, catalyzes the conversion of methyl farnesoate to juvenile hormone III acid during juvenile hormone biosynthesis. CYP303A1, CYP304A1, and CYP305A1 may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. The CYP15A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410744 [Multi-domain]  Cd Length: 423  Bit Score: 214.00  E-value: 4.55e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDvvLANRPQVII------GKHVGYNNTNmiaapyGDHWRNLRRlctieiF 144
Cdd:cd20651   1 GDVVGLKLGKDKVVVVSGYE-AVREVLSREE--FDGRPDGFFfrlrtfGKRLGITFTD------GPFWKEQRR------F 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 145 STHRLNCFLYVRT-------DEVRRLISRLSRLAGTkktvvelkPMLMDLTF-----NNIMRMMTGKRYygeettdEEEA 212
Cdd:cd20651  66 VLRHLRDFGFGRRsmeeviqEEAEELIDLLKKGEKG--------PIQMPDLFnvsvlNVLWAMVAGERY-------SLED 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 213 KRVRKLVADV----GANTSSGNAVDYVPILRL----FSSYeNRVKKLGEETDKFLQGLIDDKRGQQETG--TTMIDHLLV 282
Cdd:cd20651 131 QKLRKLLELVhllfRNFDMSGGLLNQFPWLRFiapeFSGY-NLLVELNQKLIEFLKEEIKEHKKTYDEDnpRDLIDAYLR 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 283 ---LQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKN 359
Cdd:cd20651 210 emkKKEPPSSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEA 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 360 IVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEA----QKLLAFGL 435
Cdd:cd20651 290 VILEVLRIFTLVPIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKllkdEWFLPFGA 369
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 30692923 436 GRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVD 472
Cdd:cd20651 370 GKRRCLGESLARNELFLFFTGLLQNFTFSPPNGSLPD 406
PLN02966 PLN02966
cytochrome P450 83A1
1-464 2.24e-63

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 214.61  E-value: 2.24e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923    1 MEETNIRVVLYSIFSLIFLiisFKFLKPKKQNLPPSPPGwLPIIGHL-RLLKPPIHRTLRSFSETLdhndgGGVMSLRLG 79
Cdd:PLN02966   1 MEDIIIGVVALAAVLLFFL---YQKPKTKRYKLPPGPSP-LPVIGNLlQLQKLNPQRFFAGWAKKY-----GPILSYRIG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   80 SRLVYVVSSHKVAaEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVRTDE 159
Cdd:PLN02966  72 SRTMVVISSAELA-KELLKTQDVNFADRPPHRGHEFISYGRRDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  160 VRRLISRLSRlAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYygeeTTDEEEAKRVRKLVadVGANTSSGNAV--DYVP- 236
Cdd:PLN02966 151 ARRMMDKINK-AADKSEVVDISELMLTFTNSVVCRQAFGKKY----NEDGEEMKRFIKIL--YGTQSVLGKIFfsDFFPy 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  237 --ILRLFSSYENRVKKLGEETDKFLQGLI----DDKRGQQETgTTMIDHLLVLQKSD---IEYYTDQIiKGIILIMVIAG 307
Cdd:PLN02966 224 cgFLDDLSGLTAYMKECFERQDTYIQEVVnetlDPKRVKPET-ESMIDLLMEIYKEQpfaSEFTVDNV-KAVILDIVVAG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  308 TNTSAVTLEWALSNLLNHPDVISKARDEIDNRV---GLDRLIEEaDLSELPYLKNIVLETLRLHPATPLLVPHMASEDCK 384
Cdd:PLN02966 302 TDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMkekGSTFVTED-DVKNLPYFRALVKETLRIEPVIPLLIPRACIQDTK 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  385 IGSYDMPRGTTLLVNAWAIHRDPNTWD-DPDSFKPERF-EKEEEAQ----KLLAFGLGRRACPGSGLAQRIVGLALGSLI 458
Cdd:PLN02966 381 IAGYDIPAGTTVNVNAWAVSRDEKEWGpNPDEFRPERFlEKEVDFKgtdyEFIPFGSGRRMCPGMRLGAAMLEVPYANLL 460

                 ....*.
gi 30692923  459 QCFEWE 464
Cdd:PLN02966 461 LNFNFK 466
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
71-486 4.56e-63

cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.


Pssm-ID: 410651 [Multi-domain]  Cd Length: 391  Bit Score: 210.45  E-value: 4.56e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVGYNNTnmIAAPYGDHWRNLRRLCTIEiFSTHRLN 150
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPE-LVREVLRDPRDFSSDAGPGLPALGDFLGDG--LLTLDGPEHRRLRRLLAPA-FTPRALA 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRLAGTKktvVELKPMLMDLTFNNIMRMMTGKRYygeettdEEEAKRVRKLVADVGAntssgn 230
Cdd:cd00302  77 ALRPVIREIARELLDRLAAGGEVG---DDVADLAQPLALDVIARLLGGPDL-------GEDLEELAELLEALLK------ 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 231 AVDYVPILRLFSSYENRVKKLGEETDKFLQGLIDDKRGQQETGTtmiDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNT 310
Cdd:cd00302 141 LLGPRLLRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDL---DLLLLADADDGGGLSDEEIVAELLTLLLAGHET 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 311 SAVTLEWALSNLLNHPDVISKARDEIDnrvGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLvPHMASEDCKIGSYDM 390
Cdd:cd00302 218 TASLLAWALYLLARHPEVQERLRAEID---AVLGDGTPEDLSKLPYLEAVVEETLRLYPPVPLL-PRVATEDVELGGYTI 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 391 PRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQKL--LAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGN 468
Cdd:cd00302 294 PAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEPRYahLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPD 373
                       410
                ....*....|....*...
gi 30692923 469 VEVDMKEGVGNTVPKAIP 486
Cdd:cd00302 374 EELEWRPSLGTLGPASLP 391
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
71-474 3.86e-57

cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of Mycobacterium tuberculosis cytochrome P450 132 (CYP132) and similar proteins. The function of CYP132 is as yet unknown. CYP132 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410713 [Multi-domain]  Cd Length: 406  Bit Score: 195.11  E-value: 3.86e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSS----HKVAAEE--CFGKNDVVlaNRPQVIIGkhvgynntNMIAAPYGDHWRNLRRLCTiEIF 144
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHpdhiQHVLVTNarNYVKGGVY--ERLKLLLG--------NGLLTSEGDLWRRQRRLAQ-PAF 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 145 STHRLNCFLYVRTDEVRRLISRLSRLAGTKktVVELKPMLMDLTFNNIMRMMTGkryygeeTTDEEEAKRVRKLVaDVGA 224
Cdd:cd20620  70 HRRRIAAYADAMVEATAALLDRWEAGARRG--PVDVHAEMMRLTLRIVAKTLFG-------TDVEGEADEIGDAL-DVAL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 225 NTSSGNAVDYVPILRLFSSYEN-RVKKLGEETDKFLQGLIDDKRGQQETGTTMIDHLLVLQKSDI-EYYTDQIIKGIILI 302
Cdd:cd20620 140 EYAARRMLSPFLLPLWLPTPANrRFRRARRRLDEVIYRLIAERRAAPADGGDLLSMLLAARDEETgEPMSDQQLRDEVMT 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 303 MVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGlDRLIEEADLSELPYLKNIVLETLRLHPATPLlVPHMASED 382
Cdd:cd20620 220 LFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLRLYPPAWI-IGREAVED 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 383 CKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQKL----LAFGLGRRACPGSGLAQRIVGLALGSLI 458
Cdd:cd20620 298 DEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPryayFPFGGGPRICIGNHFAMMEAVLLLATIA 377
                       410
                ....*....|....*.
gi 30692923 459 QCFEWERVGNVEVDMK 474
Cdd:cd20620 378 QRFRLRLVPGQPVEPE 393
PLN02655 PLN02655
ent-kaurene oxidase
35-494 4.10e-55

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 191.49  E-value: 4.10e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   35 PSPPGWlPIIGHLRLL---KPpiHRTLRSFSETLdhndgGGVMSLRLGSRLVYVVSSHKVAAEecfgkndvVLANRPQVI 111
Cdd:PLN02655   2 PAVPGL-PVIGNLLQLkekKP--HRTFTKWSEIY-----GPIYTIRTGASSVVVLNSTEVAKE--------AMVTKFSSI 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  112 IGKHVGYN------NTNMIA-APYGDHWRNLRRLCTIEIFSTHRLNCFLYVRTDEVRRLISRLSRLAGTKKT-VVELKPM 183
Cdd:PLN02655  66 STRKLSKAltvltrDKSMVAtSDYGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSGLHALVKDDPHsPVNFRDV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  184 LMDLTFNNIMRMMTGK---RYYGEE---TTDEEEAKRVrkLVADVGANTSSGNAVDYVPILRLF--SSYENRVKKLGEET 255
Cdd:PLN02655 146 FENELFGLSLIQALGEdveSVYVEElgtEISKEEIFDV--LVHDMMMCAIEVDWRDFFPYLSWIpnKSFETRVQTTEFRR 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  256 DKFLQGLIDDKR---GQQETGTTMIDHLLvlqkSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKA 332
Cdd:PLN02655 224 TAVMKALIKQQKkriARGEERDCYLDFLL----SEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  333 RDEIDNRVGLDRLIEEaDLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDD 412
Cdd:PLN02655 300 YREIREVCGDERVTEE-DLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWEN 378
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  413 PDSFKPERFEKEE----EAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWeRVGNVEVDMKEGVGNTVPKAIPLK 488
Cdd:PLN02655 379 PEEWDPERFLGEKyesaDMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEW-RLREGDEEKEDTVQLTTQKLHPLH 457

                 ....*.
gi 30692923  489 AICKAR 494
Cdd:PLN02655 458 AHLKPR 463
PLN02971 PLN02971
tryptophan N-hydroxylase
10-468 5.93e-55

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 192.94  E-value: 5.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   10 LYSIFSLIFLIISFKFL----KPKKQNLPPSPPGWlPIIGHL-RLLKP-PIHRTLRSFSETLDHNdgggVMSLRLGSRLV 83
Cdd:PLN02971  31 LQALVAITLLMILKKLKsssrNKKLHPLPPGPTGF-PIVGMIpAMLKNrPVFRWLHSLMKELNTE----IACVRLGNTHV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   84 YVVSSHKVAaEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVRTDEVRRL 163
Cdd:PLN02971 106 IPVTCPKIA-REIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDHL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  164 ISRLSRLAGTKKTVvELKPMLMDLTFNNIMRMMTGKRYYGEETTDE-----EEAKRVRKLVADVGAnTSSGNAVDYVPIL 238
Cdd:PLN02971 185 TAWLYNMVKNSEPV-DLRFVTRHYCGNAIKRLMFGTRTFSEKTEPDggptlEDIEHMDAMFEGLGF-TFAFCISDYLPML 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  239 R--LFSSYENRVKKLGEETDKFLQGLIDDK-RGQQETGTTMIDHLL-----VLQKSDIEYYTDQIIKGIILIMVIAGTNT 310
Cdd:PLN02971 263 TglDLNGHEKIMRESSAIMDKYHDPIIDERiKMWREGKRTQIEDFLdifisIKDEAGQPLLTADEIKPTIKELVMAAPDN 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  311 SAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDM 390
Cdd:PLN02971 343 PSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHI 422
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  391 PRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKE-------EEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEW 463
Cdd:PLN02971 423 PKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsevtltENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKW 502

                 ....*
gi 30692923  464 ERVGN 468
Cdd:PLN02971 503 KLAGS 507
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
71-489 7.81e-54

cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three functional human members: CYP1A1, CYP1A2 and CYP1B1, which are regulated by the aryl hydrocarbon receptor (AhR), ligand-activated transcriptional factor that dimerizes with AhR nuclear translocator (ARNT). CYP1 enzymes are involved in the metabolism of endogenous hormones, xenobiotics, and drugs. Included in the CYP1 family is CYP1D1 (cytochrome P450 family 1, subfamily D, polypeptide 1), which is not expressed in humans as its gene is pseudogenized due to five nonsense mutations in the putative coding region, but is functional in in other organisms including cynomolgus monkey. Zebrafish CYP1D1 expression is not regulated by AhR. The CYP1 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 187.12  E-value: 7.81e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAAEECFgKNDVVLANRP-----QVII-GKHVGYNntnmiaaPYGDHWRNLRRLCT--IE 142
Cdd:cd11028   2 GDVFQIRMGSRPVVVLNGLETIKQALV-RQGEDFAGRPdfysfQFISnGKSMAFS-------DYGPRWKLHRKLAQnaLR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 143 IFSTHRLNCFL--YVrTDEVRRLISRLSRLAGtkktvvelKPMLMD------LTFNNIM-RMMTGKRYygeeTTDEEEAK 213
Cdd:cd11028  74 TFSNARTHNPLeeHV-TEEAEELVTELTENNG--------KPGPFDprneiyLSVGNVIcAICFGKRY----SRDDPEFL 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 214 RVRKLVADVGANTSSGNAVDYVPILR-LFSSYENRVKKLGEETDKFLQGLIDDKRGQQETGTT--MIDHLL--VLQKSDI 288
Cdd:cd11028 141 ELVKSNDDFGAFVGAGNPVDVMPWLRyLTRRKLQKFKELLNRLNSFILKKVKEHLDTYDKGHIrdITDALIkaSEEKPEE 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 289 EYYTDQIIKGIILIMVI----AGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLET 364
Cdd:cd11028 221 EKPEVGLTDEHIISTVQdlfgAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILET 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 365 LRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE------EAQKLLAFGLGRR 438
Cdd:cd11028 301 MRHSSFVPFTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNglldktKVDKFLPFGAGRR 380
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 30692923 439 ACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDMKEGVGNTVpKAIPLKA 489
Cdd:cd11028 381 RCLGEELARMELFLFFATLLQQCEFSVKPGEKLDLTPIYGLTM-KPKPFKV 430
PLN03018 PLN03018
homomethionine N-hydroxylase
27-464 2.53e-53

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 188.30  E-value: 2.53e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   27 KPKKQNLPPSPPGWlPIIGHLRLL---KPP---IHRTLRSFSETLDHNDGGGVMSLRLGSRLVyvvsshkvaAEECFGKN 100
Cdd:PLN03018  35 KDRSRQLPPGPPGW-PILGNLPELimtRPRskyFHLAMKELKTDIACFNFAGTHTITINSDEI---------AREAFRER 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  101 DVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLYVRTDEVRRLISRLSRLAGTKKTVvEL 180
Cdd:PLN03018 105 DADLADRPQLSIMETIGDNYKSMGTSPYGEQFMKMKKVITTEIMSVKTLNMLEAARTIEADNLIAYIHSMYQRSETV-DV 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  181 KPMLMDLTFNNIMRMMTGKRYYGEET--TDEEEAKRVRKLVADVGANT----SSGNAVDYVPilRLFSSY-----ENRVK 249
Cdd:PLN03018 184 RELSRVYGYAVTMRMLFGRRHVTKENvfSDDGRLGKAEKHHLEVIFNTlnclPGFSPVDYVE--RWLRGWnidgqEERAK 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  250 KLGEETDKFLQGLIDDK------RGQQETGTTMIDHLLVLQKSDIEYY-TDQIIKGIILIMVIAGTNTSAVTLEWALSNL 322
Cdd:PLN03018 262 VNVNLVRSYNNPIIDERvelwreKGGKAAVEDWLDTFITLKDQNGKYLvTPDEIKAQCVEFCIAAIDNPANNMEWTLGEM 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  323 LNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWA 402
Cdd:PLN03018 342 LKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPG 421
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30692923  403 IHRDPNTWDDPDSFKPER------FEKE----EEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWE 464
Cdd:PLN03018 422 LGRNPKIWKDPLVYEPERhlqgdgITKEvtlvETEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWK 493
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
95-483 2.98e-53

cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes vertebrate CYP3A subfamily enzymes and CYP5a1, and similar proteins. CYP5A1, also called thromboxane-A synthase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid. CYP3A enzymes are drug-metabolizing enzymes embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. The CYP3A-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410678 [Multi-domain]  Cd Length: 422  Bit Score: 185.10  E-value: 2.98e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  95 ECFGKNDVVLANRPQVIIGkhVGYNNTNMIAAPyGDHWRNLRRLcTIEIFSTHRLNCFLYVRTDEVRRLISRLSRLAgTK 174
Cdd:cd11055  26 EILVKEFSNFTNRPLFILL--DEPFDSSLLFLK-GERWKRLRTT-LSPTFSSGKLKLMVPIINDCCDELVEKLEKAA-ET 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 175 KTVVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAKRVRKLVADVGANTSSGNAVDYVPILRLFSSYENRVKKLGEE 254
Cdd:cd11055 101 GKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKAAKKIFRNSIIRLFLLLLLFPLRLFLFLLFPFVFGFKSFSF 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 255 TDKFLQGLIDDKRGQQETGTT-MIDHLLVLQKSDIEYY----TDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVI 329
Cdd:cd11055 181 LEDVVKKIIEQRRKNKSSRRKdLLQLMLDAQDSDEDVSkkklTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQ 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 330 SKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVpHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNT 409
Cdd:cd11055 261 EKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFIS-RECKEDCTINGVFIPKGVDVVIPVYAIHHDPEF 339
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30692923 410 WDDPDSFKPERFEKEEEAQ----KLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDMK-EGVGNTVPK 483
Cdd:cd11055 340 WPDPEKFDPERFSPENKAKrhpyAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETEIPLKlVGGATLSPK 418
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
71-477 3.01e-53

cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including insect cytochrome P450 306A1 (CYP306A1 or Cyp306a1) and CYP18A1. CYP306A1 functions as a carbon 25-hydroxylase and has an essential role in ecdysteroid biosynthesis during insect development. CYP18A1 is a 26-hydroxylase and plays a key role in steroid hormone inactivation. The CYP306A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 185.69  E-value: 3.01e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAaEECFGKNdvVLANRPQVIIgKHvGYNNTNMIAAPYGDHWRNLRRlctieiFSTHRLN 150
Cdd:cd20652   1 GSIFSLKMGSVYTVVLSDPKLI-RDTFRRD--EFTGRAPLYL-TH-GIMGGNGIICAEGDLWRDQRR------FVHDWLR 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVR-RLISRLSR--------LAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYygeeTTDEEEAKRVRKLVAD 221
Cdd:cd20652  70 QFGMTKFGNGRaKMEKRIATgvhelikhLKAESGQPVDPSPVLMHSLGNVINDLVFGFRY----KEDDPTWRWLRFLQEE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 222 VGANTSSGNAVDYVPILRLFSSYENRVKKLGE---ETDKFLQGLIDD-----KRGQQETGTTMIDHLLVLQKSDIE---- 289
Cdd:cd20652 146 GTKLIGVAGPVNFLPFLRHLPSYKKAIEFLVQgqaKTHAIYQKIIDEhkrrlKPENPRDAEDFELCELEKAKKEGEdrdl 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 290 ---YYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLR 366
Cdd:cd20652 226 fdgFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQR 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 367 LHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEA----QKLLAFGLGRRACPG 442
Cdd:cd20652 306 IRSVVPLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKylkpEAFIPFQTGKRMCLG 385
                       410       420       430
                ....*....|....*....|....*....|....*
gi 30692923 443 SGLAQRIVGLALGSLIQCFEWERVGNVEVDMKEGV 477
Cdd:cd20652 386 DELARMILFLFTARILRKFRIALPDGQPVDSEGGN 420
PLN00168 PLN00168
Cytochrome P450; Provisional
1-489 2.44e-50

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 179.76  E-value: 2.44e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923    1 MEETNIRVVLYSIFSLIFLIISFKFLKPKKQN---LPPSPPGwLPIIGHLRLLK---PPIHRTLRSFsetldHNDGGGVM 74
Cdd:PLN00168   1 MDATQLLLLAALLLLPLLLLLLGKHGGRGGKKgrrLPPGPPA-VPLLGSLVWLTnssADVEPLLRRL-----IARYGPVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   75 SLRLGSRLVYVVSSHKVAAEECFGKNdVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRLNCFLY 154
Cdd:PLN00168  75 SLRVGSRLSVFVADRRLAHAALVERG-AALADRPAVASSRLLGESDNTITRSSYGPVWRLLRRNLVAETLHPSRVRLFAP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  155 VRTDEVRRLISRLSRLAG--TKKTVVELKPMLMdltFNNIMRMMTGKRYYGEETTDEEEAKRvrklvaDVGANTSSGNAV 232
Cdd:PLN00168 154 ARAWVRRVLVDKLRREAEdaAAPRVVETFQYAM---FCLLVLMCFGERLDEPAVRAIAAAQR------DWLLYVSKKMSV 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  233 -DYVPIL--RLFSSYENRVKKLGEETDKFLQGLIDDKR---------GQQETGTTMIDHLLVLQKSDIEYY-------TD 293
Cdd:PLN00168 225 fAFFPAVtkHLFRGRLQKALALRRRQKELFVPLIDARReyknhlgqgGEPPKKETTFEHSYVDTLLDIRLPedgdralTD 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  294 QIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLD-RLIEEADLSELPYLKNIVLETLRLHPATP 372
Cdd:PLN00168 305 DEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDqEEVSEEDVHKMPYLKAVVLEGLRKHPPAH 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  373 LLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQ----------KLLAFGLGRRACPG 442
Cdd:PLN00168 385 FVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLAGGDGEgvdvtgsreiRMMPFGVGRRICAG 464
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*..
gi 30692923  443 SGLAQRIVGLALGSLIQCFEWERVGNVEVDMKEGVGNTVPKAIPLKA 489
Cdd:PLN00168 465 LGIAMLHLEYFVANMVREFEWKEVPGDEVDFAEKREFTTVMAKPLRA 511
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
71-461 2.98e-48

cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2 (in humans), catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. It is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. Deficiency of this CYP is involved in ~95% of cases of human congenital adrenal hyperplasia, a disorder of adrenal steroidogenesis. There are two CYP21 genes in the human genome, CYP21A1 (a pseudogene) and CYP21A2 (the functional gene). Deficiencies in steroid 21-hydroxylase activity lead to a type of congenital adrenal hyperplasia, which has three clinical forms: a severe form with concurrent defects in both cortisol and aldosterone biosynthesis; a form with adequate aldosterone biosynthesis; and a mild, non-classic form that can be asymptomatic or associated with signs of postpubertal androgen excess without cortisol deficiency. CYP21A2 is also the major autoantigen in autoimmune Addison disease. Cyp21 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410767 [Multi-domain]  Cd Length: 424  Bit Score: 171.83  E-value: 2.98e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSShKVAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCTIEIFSTHRlN 150
Cdd:cd20674   2 GPIYRLRLGLQDVVVLNS-KRTIREALVRKWADFAGRPHSYTGKLVSQGGQDLSLGDYSLLWKAHRKLTRSALQLGIR-N 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTDEVRRLISRLSRLAGTKKTVVELKPMLmdlTFNNIMRMMTGKRYygeetTDEEEAKRVRKLVADVGA--NTSS 228
Cdd:cd20674  80 SLEPVVEQLTQELCERMRAQAGTPVDIQEEFSLL---TCSIICCLTFGDKE-----DKDTLVQAFHDCVQELLKtwGHWS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 229 GNAVDYVPILRLFSSYE-NRVKKLGEETDKFLQGLIDDKRGQQETGT--TMIDHLL--VLQKSDiEYYTDQIIKGIILIM 303
Cdd:cd20674 152 IQALDSIPFLRFFPNPGlRRLKQAVENRDHIVESQLRQHKESLVAGQwrDMTDYMLqgLGQPRG-EKGMGQLLEGHVHMA 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 304 V----IAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMA 379
Cdd:cd20674 231 VvdlfIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRT 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 380 SEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF-EKEEEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLI 458
Cdd:cd20674 311 TRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFlEPGAANRALLPFGCGARVCLGEPLARLELFVFLARLL 390

                ...
gi 30692923 459 QCF 461
Cdd:cd20674 391 QAF 393
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
71-488 7.21e-47

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 167.76  E-value: 7.21e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAApYGDHWRNLRRLCTiEIFSTHRLN 150
Cdd:COG2124  32 GPVFRVRLPGGGAWLVTRYE-DVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTL-DGPEHTRLRRLVQ-PAFTPRRVA 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 cfLYVRT--DEVRRLISRLSRlAGTkktvVELKPMLMDLTFNNIMRMMTGkryygeetTDEEEAKRVRKLVADVGAntss 228
Cdd:COG2124 109 --ALRPRirEIADELLDRLAA-RGP----VDLVEEFARPLPVIVICELLG--------VPEEDRDRLRRWSDALLD---- 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 229 gnAVDYVPILRLFssyenRVKKLGEETDKFLQGLIDDKRgqQETGTTMIDHLLVLQkSDIEYYTDQIIKGIILIMVIAGT 308
Cdd:COG2124 170 --ALGPLPPERRR-----RARRARAELDAYLRELIAERR--AEPGDDLLSALLAAR-DDGERLSDEELRDELLLLLLAGH 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 309 NTSAVTLEWALSNLLNHPDViskardeidnrvgLDRLIEEadlseLPYLKNIVLETLRLHPATPLLvPHMASEDCKIGSY 388
Cdd:COG2124 240 ETTANALAWALYALLRHPEQ-------------LARLRAE-----PELLPAAVEETLRLYPPVPLL-PRTATEDVELGGV 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 389 DMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERfekeeEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFE-WERVG 467
Cdd:COG2124 301 TIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-----PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPdLRLAP 375
                       410       420
                ....*....|....*....|.
gi 30692923 468 NVEVDMKEGVGNTVPKAIPLK 488
Cdd:COG2124 376 PEELRWRPSLTLRGPKSLPVR 396
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
71-473 7.46e-47

cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists of two human members, CYP1A1 and CYP1A2, which overlap in their activities. CYP1A2 is the highly expressed cytochrome enzyme in the human liver, while CYP1A1 is mostly found in extrahepatic tissues. Known common substrates include aromatic compounds such as polycyclic aromatic hydrocarbons, arachidonic acid and eicosapentoic acid, as well as melatonin and 6-hydroxylate melatonin. In addition, CYP1A1 activates procarcinogens into carcinogens via epoxides, and metabolizes heterocyclic aromatic amines of industrial origin. CYP1A2 metabolizes numerous natural products that result in toxic products, such as the transformation of methyleugenol to 1'-hydroxymethyleugenol, estragole to reactive metabolites, and oxidation of nephrotoxins. It also plays an important role in the metabolism of several clinical drugs including analgesics, antipyretics, antipsychotics, antidepressants, anti-inflammatory, and cardiovascular drugs. The CYP1A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 168.65  E-value: 7.46e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAAEECFGKNDVvLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLC--TIEIFS--- 145
Cdd:cd20676   2 GDVLQIQIGSRPVVVLSGLDTIRQALVKQGDD-FKGRPDLYSFRFISDGQSLTFSTDSGPVWRARRKLAqnALKTFSias 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 146 --THRLNCFL--YVRTdEVRRLISRLSRLAGTKKtvvELKPM--LMDLTFNNIMRMMTGKRYygeeTTDEEEAKRVRKLV 219
Cdd:cd20676  81 spTSSSSCLLeeHVSK-EAEYLVSKLQELMAEKG---SFDPYryIVVSVANVICAMCFGKRY----SHDDQELLSLVNLS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 220 ADVGANTSSGNAVDYVPILR-LFSSYENRVKKLGEETDKFLQGLID------DKRGQQETGTTMIDHLL---VLQKSDIE 289
Cdd:cd20676 153 DEFGEVAGSGNPADFIPILRyLPNPAMKRFKDINKRFNSFLQKIVKehyqtfDKDNIRDITDSLIEHCQdkkLDENANIQ 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 290 YYTDQIIkGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHP 369
Cdd:cd20676 233 LSDEKIV-NIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSS 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 370 ATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE-------EAQKLLAFGLGRRACPG 442
Cdd:cd20676 312 FVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADgteinktESEKVMLFGLGKRRCIG 391
                       410       420       430
                ....*....|....*....|....*....|.
gi 30692923 443 SGLAQRIVGLALGSLIQCFEWERVGNVEVDM 473
Cdd:cd20676 392 ESIARWEVFLFLAILLQQLEFSVPPGVKVDM 422
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
67-471 1.89e-46

cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins, including Nostoc sp. probable cytochrome P450 110 (CYP110) and putative cytochrome P450s 139 (CYP139), 138 (CYP138), and 135B1 (CYP135B1) from Mycobacterium bovis. CYP110 genes, unique to cyanobacteria, are widely distributed in heterocyst-forming cyanobacteria including nitrogen-fixing genera Nostoc and Anabaena. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410676 [Multi-domain]  Cd Length: 415  Bit Score: 166.99  E-value: 1.89e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  67 HNDGGGVMSLRLGSRLVYVVSSHKVAAEECF-GKNDVVLANRPQVIIGKHVGynNTNMIAAPYGDHwRNLRRLCTiEIFS 145
Cdd:cd11053   8 RARYGDVFTLRVPGLGPVVVLSDPEAIKQIFtADPDVLHPGEGNSLLEPLLG--PNSLLLLDGDRH-RRRRKLLM-PAFH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 146 THRLNCFLYVRTDEVRRLISRLSRlagtkKTVVELKPMLMDLTFNNIMRMMTGKryygeetTDEEEAKRVRKLVAD-VGA 224
Cdd:cd11053  84 GERLRAYGELIAEITEREIDRWPP-----GQPFDLRELMQEITLEVILRVVFGV-------DDGERLQELRRLLPRlLDL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 225 NTSSGNAVDYV-PILRLFSSYeNRVKKLGEETDKFLQGLIDDKRGQQETGTTMIDHLLVLQKS-DIEYYTDQIIKGIILI 302
Cdd:cd11053 152 LSSPLASFPALqRDLGPWSPW-GRFLRARRRIDALIYAEIAERRAEPDAERDDILSLLLSARDeDGQPLSDEELRDELMT 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 303 MVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNrVGLDRLIEeaDLSELPYLKNIVLETLRLHPATPLlVPHMASED 382
Cdd:cd11053 231 LLFAGHETTATALAWAFYWLHRHPEVLARLLAELDA-LGGDPDPE--DIAKLPYLDAVIKETLRLYPVAPL-VPRRVKEP 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 383 CKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF-EKEEEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCF 461
Cdd:cd11053 307 VELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFlGRKPSPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRF 386
                       410
                ....*....|
gi 30692923 462 EWERVGNVEV 471
Cdd:cd11053 387 RLELTDPRPE 396
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
71-464 3.65e-45

cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or Cyp17a1), also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. It is a dual enzyme that catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reactions. Severe mutations on the enzyme cause combined 17-hydroxylase/17,20-lyase deficiency (17OHD); patients with 17OHD synthesize 11-deoxycorticosterone (DOC) which causes hypertension and hypokalemia. Loss of 17,20-lyase activity precludes sex steroid synthesis and leads to sexual infantilism. Included in this group is a second 17A P450 from teleost fish, CYP17A2, that is more efficient in pregnenolone 17-alpha-hydroxylation than CYP17A1, but does not catalyze the lyase reaction. CYP17A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 163.65  E-value: 3.65e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAaEECFGKNDVVLANRPQVII-------GKHVGYnntnmiaAPYGDHWRNLRRLctieI 143
Cdd:cd20673   2 GPIYSLRMGSHTTVIVGHHQLA-KEVLLKKGKEFSGRPRMVTtdllsrnGKDIAF-------ADYSATWQLHRKL----V 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 144 FSThrlncFLYVRTDEVR--RLISR-----LSRLAGTKKTVVELKPMLMdLTFNNIMRMMTGKRYYGEETTDEEEAKRVR 216
Cdd:cd20673  70 HSA-----FALFGEGSQKleKIICQeasslCDTLATHNGESIDLSPPLF-RAVTNVICLLCFNSSYKNGDPELETILNYN 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 217 KLVADVGANtssGNAVDYVPILRLFSSYE-NRVKKLGEETDKFLQGLIDDKRGQ--QETGTTMIDHLLVLQKS--DIEYY 291
Cdd:cd20673 144 EGIVDTVAK---DSLVDIFPWLQIFPNKDlEKLKQCVKIRDKLLQKKLEEHKEKfsSDSIRDLLDALLQAKMNaeNNNAG 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 292 TDQIIKGII---LIMVI-----AGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLE 363
Cdd:cd20673 221 PDQDSVGLSddhILMTVgdifgAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIRE 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 364 TLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQ------KLLAFGLGR 437
Cdd:cd20673 301 VLRIRPVAPLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQlispslSYLPFGAGP 380
                       410       420
                ....*....|....*....|....*..
gi 30692923 438 RACPGSGLAQRIVGLALGSLIQCFEWE 464
Cdd:cd20673 381 RVCLGEALARQELFLFMAWLLQRFDLE 407
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
71-461 1.16e-43

cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific cytochrome P450 that catalyzes omega- and (omega-1)-hydroxylation of fatty acids such as arachidonic acid, docosahexaenoic acid, and other long chain fatty acids. Mutations in CYP2U1 are associated with hereditary spastic paraplegia (HSP), a neurological disorder, and pigmentary degenerative maculopathy associated with progressive spastic paraplegia. CYP2U1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 159.56  E-value: 1.16e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAAEECFGKNDVvLANRPQV----IIGKHVGynntnMIAAPYGDHWRNLRR--LCTIEIF 144
Cdd:cd20666   2 GNIFSLFIGSQLVVVLNDFESVREALVQKAEV-FSDRPSVplvtILTKGKG-----IVFAPYGPVWRQQRKfsHSTLRHF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 145 STHRLNcFLYVRTDEVRRLISRLSRLAGTKktvVELKPMLMDLTFNNIMRMMTGKRYygeETTDEEEAKRVRKL--VADV 222
Cdd:cd20666  76 GLGKLS-LEPKIIEEFRYVKAEMLKHGGDP---FNPFPIVNNAVSNVICSMSFGRRF---DYQDVEFKTMLGLMsrGLEI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 223 GANTSSGNaVDYVPILRLFSSYENR-VKKLGEETDKFLQGLIDDKRG--QQETGTTMIDHLLV----LQKSDIEY-YTDQ 294
Cdd:cd20666 149 SVNSAAIL-VNICPWLYYLPFGPFReLRQIEKDITAFLKKIIADHREtlDPANPRDFIDMYLLhieeEQKNNAESsFNED 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 295 IIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLL 374
Cdd:cd20666 228 YLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLS 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 375 VPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE----EAQKLLAFGLGRRACPGSGLAQRIV 450
Cdd:cd20666 308 IPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENgqliKKEAFIPFGIGRRVCMGEQLAKMEL 387
                       410
                ....*....|.
gi 30692923 451 GLALGSLIQCF 461
Cdd:cd20666 388 FLMFVSLMQSF 398
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
71-482 2.15e-42

cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, most diverse CYP families in vertebrates. It includes many subfamilies across vertebrate species but not all subfamilies are found in multiple vertebrate taxonomic classes. The CYP2U and CYP2R genes are present in the vertebrate ancestor and are shared across all vertebrate classes, whereas some subfamilies are lineage-specific, such as CYP2B and CYP2S in mammals. CYP2 enzymes play important roles in drug metabolism. The CYP2 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 156.18  E-value: 2.15e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHV--GYNntnmIAAPYGDHWRNLRRlctieiFSTHR 148
Cdd:cd11026   2 GPVFTVYLGSKPVVVLCGYE-AVKEALVDQAEEFSGRPPVPLFDRVtkGYG----VVFSNGERWKQLRR------FSLTT 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 149 LNCF------LYVR-TDEVRRLISRLSrlaGTKKTVVELKPMLMDLTFNNIMRMMTGKRYygeeTTDEEEAKRVRKLVAD 221
Cdd:cd11026  71 LRNFgmgkrsIEERiQEEAKFLVEAFR---KTKGKPFDPTFLLSNAVSNVICSIVFGSRF----DYEDKEFLKLLDLINE 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 222 VGANTSS-----GNAvdYVPILRLFSSYENRVKKLGEETDKFLQGLIDDKRGQQETGTT--MIDHLLV-LQK----SDIE 289
Cdd:cd11026 144 NLRLLSSpwgqlYNM--FPPLLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSPrdFIDCFLLkMEKekdnPNSE 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 290 YYTDQIIKgIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHP 369
Cdd:cd11026 222 FHEENLVM-TVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGD 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 370 ATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE------EAqkLLAFGLGRRACPGS 443
Cdd:cd11026 301 IVPLGVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQgkfkknEA--FMPFSAGKRVCLGE 378
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 30692923 444 GLAQRIVGLALGSLIQCFEWER-VGNVEVDMK---EGVGNTVP 482
Cdd:cd11026 379 GLARMELFLFFTSLLQRFSLSSpVGPKDPDLTprfSGFTNSPR 421
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
71-471 4.29e-41

cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; This subfamily is composed of Streptomyces coelicolor cytochrome P450 170A1 (CYP170A1), Streptomyces avermitilis pentalenene oxygenase, and similar actinobacterial cytochrome P450s. CYP170A1, also called epi-isozizaene 5-monooxygenase (EC 1.14.13.106)/(E)-beta-farnesene synthase (EC 4.2.3.47), catalyzes the two-step allylic oxidation of epi-isozizaene to albaflavenone, which is a sesquiterpenoid antibiotic. Pentalenene oxygenase (EC 1.14.15.32) catalyzes the conversion of pentalenene to pentalen-13-al by stepwise oxidation via pentalen-13-ol, a precursor of the neopentalenolactone antibiotic. The CYP170A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410673 [Multi-domain]  Cd Length: 415  Bit Score: 152.41  E-value: 4.29e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHK------VAAEECFGKNdvVLANRPQVIIGkhVGynntnMIAAPYGDHWRNlRRLctIE-I 143
Cdd:cd11049  13 GDLVRIRLGPRPAYVVTSPElvrqvlVNDRVFDKGG--PLFDRARPLLG--NG-----LATCPGEDHRRQ-RRL--MQpA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 144 FSTHRLNCFLYVRTDEVRRLISRLSrlAGTkktVVELKPMLMDLTFNNIMRMMTGKRYyGEETTDEEeAKRVRKLVADVG 223
Cdd:cd11049  81 FHRSRIPAYAEVMREEAEALAGSWR--PGR---VVDVDAEMHRLTLRVVARTLFSTDL-GPEAAAEL-RQALPVVLAGML 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 224 ANTSSGNAVDYVPIL--RLFSSYENRVKKLgeetdkfLQGLIDDKRGQQETGTTMIDHLLVLQKSDIEYYTDQIIKGIIL 301
Cdd:cd11049 154 RRAVPPKFLERLPTPgnRRFDRALARLREL-------VDEIIAEYRASGTDRDDLLSLLLAARDEEGRPLSDEELRDQVI 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 302 IMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGlDRLIEEADLSELPYLKNIVLETLRLHPATPLLvPHMASE 381
Cdd:cd11049 227 TLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWLL-TRRTTA 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 382 DCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEA----QKLLAFGLGRRACPGSGLAQRIVGLALGSL 457
Cdd:cd11049 305 DVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAavprGAFIPFGAGARKCIGDTFALTELTLALATI 384
                       410
                ....*....|....
gi 30692923 458 IQCFEWERVGNVEV 471
Cdd:cd11049 385 ASRWRLRPVPGRPV 398
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
129-474 4.50e-40

cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of vertebrate cytochrome P450 24A1 (CYP24A1) and similar proteins including several Drosophila proteins such as CYP315A1 (also called protein shadow) and CYP314A1 (also called ecdysone 20-monooxygenase), and vertebrate CYP11 and CYP27 subfamilies. Both CYP314A1 and CYP315A1, which has ecdysteroid C2-hydroxylase activity, are involved in the metabolism of insect hormones. CYP24A1 and CYP27B1 have roles in calcium homeostasis and metabolism, and the regulation of vitamin D. CYP24A1 catabolizes calcitriol (1,25(OH)2D), the physiologically active vitamin D hormone, by catalyzing its hydroxylation, while CYP27B1 is a calcidiol 1-monooxygenase that coverts 25-hydroxyvitamin D3 to calcitriol. The CYP24A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410677 [Multi-domain]  Cd Length: 426  Bit Score: 149.60  E-value: 4.50e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 129 GDHWRNLRRlctieIFSTHRL---NCFLYVRT-DEV-RRLISRLSRLAGTKKTVVE-LKPMLMDLTFNNIMRMMTGKRYY 202
Cdd:cd11054  63 GEEWHRLRS-----AVQKPLLrpkSVASYLPAiNEVaDDFVERIRRLRDEDGEEVPdLEDELYKWSLESIGTVLFGKRLG 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 203 GEETTDEEEAKRVRKLVADVgaNTSSGNAVDYVPILRLFSS-----YENRVKKLGEETDKFLQGLIDD---KRGQQETGT 274
Cdd:cd11054 138 CLDDNPDSDAQKLIEAVKDI--FESSAKLMFGPPLWKYFPTpawkkFVKAWDTIFDIASKYVDEALEElkkKDEEDEEED 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 275 TMIDHLLvlQKSDIeyyTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSEL 354
Cdd:cd11054 216 SLLEYLL--SKPGL---SKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKM 290
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 355 PYLKNIVLETLRLHPATPLLVpHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK----- 429
Cdd:cd11054 291 PYLKACIKESLRLYPVAPGNG-RILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENKnihpf 369
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 30692923 430 -LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNvEVDMK 474
Cdd:cd11054 370 aSLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHE-ELKVK 414
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
71-442 6.88e-40

cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the omega-hydroxylation of the terminal carbon of fatty acids, including essential signaling molecules such as eicosanoids, prostaglandins and leukotrienes, and they are important for chemical defense. There are seven vertebrate family 4 subfamilies: CYP4A, CYP4B, CYP4F, CYP4T, CYP4V, CYP4X, and CYP4Z; three (CYP4X, CYP4A, CYP4Z) are specific to mammals. CYP4 enzymes metabolize fatty acids off various length, level of saturation, and branching. Specific subfamilies show preferences for the length of fatty acids; CYP4B, CYP4A and CYP4V, and CYP4F preferentially metabolize short (C7-C10), medium (C10-C16), and long to very long (C18-C26) fatty acid chains, respectively. CYP4 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410721 [Multi-domain]  Cd Length: 426  Bit Score: 149.21  E-value: 6.88e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEecfgkndVVLANrpQVIIGKHVGYN------NTNMIAAPyGDHWRNLRRLCTiEIF 144
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPE-DIE-------VILSS--SKLITKSFLYDflkpwlGDGLLTST-GEKWRKRRKLLT-PAF 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 145 STHRLNCFLYVRTDEVRRLISRLSRLAGtkKTVVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAKRVRKLVAdvGA 224
Cdd:cd20628  69 HFKILESFVEVFNENSKILVEKLKKKAG--GGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILE--II 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 225 NTSSGNAVDYVPILRLFSSYENRVKKLGEETDKFLQGLIDDKRGQQETG---------------TTMIDHLLVLQKSDIE 289
Cdd:cd20628 145 LKRIFSPWLRFDFIFRLTSLGKEQRKALKVLHDFTNKVIKERREELKAEkrnseeddefgkkkrKAFLDLLLEAHEDGGP 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 290 YyTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLD-RLIEEADLSELPYLKNIVLETLRLH 368
Cdd:cd20628 225 L-TDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDdRRPTLEDLNKMKYLERVIKETLRLY 303
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30692923 369 PATPLlVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK----LLAFGLGRRACPG 442
Cdd:cd20628 304 PSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRhpyaYIPFSAGPRNCIG 380
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
160-446 6.81e-39

unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized fungal cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 146.29  E-value: 6.81e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 160 VRRLISRLSRLAGTKKTVvELKPMLMDLTFNNIMRMMtgkryYGEE-TTDEEEAKRVRKLVADVGANTSSGNAVDYVP-- 236
Cdd:cd11059  84 VLPLIDRIAKEAGKSGSV-DVYPLFTALAMDVVSHLL-----FGESfGTLLLGDKDSRERELLRRLLASLAPWLRWLPry 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 237 -----ILRLFSSYENRVKKLGEETDKFLQGLIDDKRGQQETGTTMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTS 311
Cdd:cd11059 158 lplatSRLIIGIYFRAFDEIEEWALDLCARAESSLAESSDSESLTVLLLEKLKGLKKQGLDDLEIASEALDHIVAGHDTT 237
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 312 AVTLEWALSNLLNHPDVISKARDEIDN-RVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASED-CKIGSYD 389
Cdd:cd11059 238 AVTLTYLIWELSRPPNLQEKLREELAGlPGPFRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLPRVVPEGgATIGGYY 317
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30692923 390 MPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF-----EKEEEAQKLL-AFGLGRRACPGSGLA 446
Cdd:cd11059 318 IPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWldpsgETAREMKRAFwPFGSGSRMCIGMNLA 380
PTZ00404 PTZ00404
cytochrome P450; Provisional
13-494 8.96e-39

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 147.18  E-value: 8.96e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   13 IFSLIFLIISFKFLKPKK--QNLPPSPPGwLPIIGHLRLLKPPIHRTLrsfseTLDHNDGGGVMSLRLGSrLVYVVSSHK 90
Cdd:PTZ00404   8 LFLFIFYIIHNAYKKYKKihKNELKGPIP-IPILGNLHQLGNLPHRDL-----TKMSKKYGGIFRIWFAD-LYTVVLSDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   91 VAAEECFGKNDVVLANRPQVIIGKH-VGYNNtnmIAAPYGDHWRNLRRLCTIEIFSTHrLNCFLYVRTDEVRRLISRLSR 169
Cdd:PTZ00404  81 ILIREMFVDNFDNFSDRPKIPSIKHgTFYHG---IVTSSGEYWKRNREIVGKAMRKTN-LKHIYDLLDDQVDVLIESMKK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  170 LAGTKKTV---VELKPMLMDLTFNNIMRMMTGkryYGEETTDEEEAKRVRKLvADVGANTSSGNAVDYVPILR------- 239
Cdd:PTZ00404 157 IESSGETFeprYYLTKFTMSAMFKYIFNEDIS---FDEDIHNGKLAELMGPM-EQVFKDLGSGSLFDVIEITQplyyqyl 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  240 -LFSSYENRVKKLGEEtdKFLQGLiddKRGQQETGTTMIDHLLvlqksdIEYYT---DQI--IKGIILIMVIAGTNTSAV 313
Cdd:PTZ00404 233 eHTDKNFKKIKKFIKE--KYHEHL---KTIDPEVPRDLLDLLI------KEYGTntdDDIlsILATILDFFLAGVDTSAT 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  314 TLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGS-YDMPR 392
Cdd:PTZ00404 302 SLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFGLPRSTSNDIIIGGgHFIPK 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  393 GTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVD 472
Cdd:PTZ00404 382 DAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGKKID 461
                        490       500
                 ....*....|....*....|..
gi 30692923  473 MKEGVGNTVPKAiPLKAICKAR 494
Cdd:PTZ00404 462 ETEEYGLTLKPN-KFKVLLEKR 482
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
111-471 2.20e-38

plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, cytochrome P450 family 90, subfamily B, polypeptide 1, and cytochrome P450 family 90, subfamily D, polypeptide 2; This family is composed of plant cytochrome P450s including: Arabidopsis thaliana cytochrome P450s 85A1 (CYP85A1 or brassinosteroid-6-oxidase 1), 90A1 (CYP90A1), 88A3 (CYP88A3 or ent-kaurenoic acid oxidase 1), 90B1 (CYP90B1 or Dwarf4 or steroid 22-alpha-hydroxylase), and 90C1 (CYP90C1 or 3-epi-6-deoxocathasterone 23-monooxygenase); Oryza sativa cytochrome P450s 90D2 (CYP90D2 or C6-oxidase), 87A3 (CYP87A3), and 724B1 (CYP724B1 or dwarf protein 11); and Taxus cuspidata cytochrome P450 725A2 (CYP725A2 or taxane 13-alpha-hydroxylase). These enzymes are monooxygenases that catalyze oxidation reactions involved in steroid or hormone biosynthesis. CYP85A1, CYP90D2, and CYP90C1 are involved in brassinosteroids biosynthesis, while CYP88A3 catalyzes three successive oxidations of ent-kaurenoic acid, which is a key step in the synthesis of gibberellins. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410669 [Multi-domain]  Cd Length: 408  Bit Score: 144.63  E-value: 2.20e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 111 IIGKHvgynntnMIAAPYGDHWRNLRRLcTIEIFSTHRLNcflyvrtdevRRLISRLSRLA------GTKKTVVELKPML 184
Cdd:cd11043  49 LLGKS-------SLLTVSGEEHKRLRGL-LLSFLGPEALK----------DRLLGDIDELVrqhldsWWRGKSVVVLELA 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 185 MDLTFNNIMRMMTGkryygeeTTDEEEAKRVRKLVADVGANTSSgnavdyVPILRLFSSYeNRVKKLGEETDKFLQGLID 264
Cdd:cd11043 111 KKMTFELICKLLLG-------IDPEEVVEELRKEFQAFLEGLLS------FPLNLPGTTF-HRALKARKRIRKELKKIIE 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 265 DKR---GQQETGTTMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDE----ID 337
Cdd:cd11043 177 ERRaelEKASPKGDLLDVLLEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEheeiAK 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 338 NRVGLDRLIEEaDLSELPYLKNIVLETLRLHPATPLlVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFK 417
Cdd:cd11043 257 RKEEGEGLTWE-DYKSMKYTWQVINETLRLAPIVPG-VFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFN 334
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30692923 418 PERFEKEEEAQK--LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEV 471
Cdd:cd11043 335 PWRWEGKGKGVPytFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVVPDEKI 390
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
232-486 2.47e-38

Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; Fusarium verticillioides cytochrome P450 monooxygenase FUM15, is also called fumonisin biosynthesis cluster protein 15. The FUM15 gene is part of the gene cluster that mediates the biosynthesis of fumonisins B1, B2, B3, and B4, which are carcinogenic mycotoxins. This FUM15-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410692 [Multi-domain]  Cd Length: 437  Bit Score: 145.11  E-value: 2.47e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 232 VDYVPILRLfssyeNRVKKLGEETDKFLQGLIDDKRGQ--QETGTTMIDHLLVLQKS----DIEYYTDQIIKGIILIMVI 305
Cdd:cd11069 171 VRILPWKAN-----REIRRAKDVLRRLAREIIREKKAAllEGKDDSGKDILSILLRAndfaDDERLSDEELIDQILTFLA 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 306 AGTNTSAVTLEWALSNLLNHPDVISKARDEI-DNRVGL-DRLIEEADLSELPYLKNIVLETLRLHPATPLLVpHMASEDC 383
Cdd:cd11069 246 AGHETTSTALTWALYLLAKHPDVQERLREEIrAALPDPpDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTS-REATKDT 324
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 384 KIGSYDMPRGTTLLVNAWAIHRDPNTW-DDPDSFKPERFEKEEEAQK---------LLAFGLGRRACPGSGLAQ---RIV 450
Cdd:cd11069 325 VIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASpggagsnyaLLTFLHGPRSCIGKKFALaemKVL 404
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 30692923 451 glaLGSLIQCFEWERVGNVEVDMKEGVGNTVPKAIP 486
Cdd:cd11069 405 ---LAALVSRFEFELDPDAEVERPIGIITRPPVDGL 437
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
70-462 4.72e-38

fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This group includes Aspergillus nidulans phenylacetate 2-hydroxylase (encoded by the phacA gene) and similar fungal cytochrome P450s. PhacA catalyzes the ortho-hydroxylation of phenylacetate, the first step of A. nidulans phenylacetate catabolism. The PhacA-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 144.38  E-value: 4.72e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  70 GGGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRP------QVIIGKH---VGynntnmiAAPYGDHWRNLRRLCT 140
Cdd:cd11066   1 NGPVFQIRLGNKRIVVVNSFA-SVRDLWIKNSSALNSRPtfytfhKVVSSTQgftIG-------TSPWDESCKRRRKAAA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 141 IEIF--STHRLNCFLYVrtdEVRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYYG--------EETTDEE 210
Cdd:cd11066  73 SALNrpAVQSYAPIIDL---ESKSFIRELLRDSAEGKGDIDPLIYFQRFSLNLSLTLNYGIRLDCvdddslllEIIEVES 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 211 EAKRVRklvadvganTSSGNAVDYVPILRLFSSYEN---RVKKLGEETDKFLQGLIDDKRGQQETGT---TMIDHLLVLQ 284
Cdd:cd11066 150 AISKFR---------STSSNLQDYIPILRYFPKMSKfreRADEYRNRRDKYLKKLLAKLKEEIEDGTdkpCIVGNILKDK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 285 KSDIeyyTDQIIKGIILIMVIAGTNTSAVTLEWALSnLLNHPDVIS---KARDEIDNRVGLDRLIEE--ADLSELPYLKN 359
Cdd:cd11066 221 ESKL---TDAELQSICLTMVSAGLDTVPLNLNHLIG-HLSHPPGQEiqeKAYEEILEAYGNDEDAWEdcAAEEKCPYVVA 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 360 IVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQKL----LAFGL 435
Cdd:cd11066 297 LVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPgpphFSFGA 376
                       410       420
                ....*....|....*....|....*..
gi 30692923 436 GRRACPGSGLAQRIVGLALGSLIQCFE 462
Cdd:cd11066 377 GSRMCAGSHLANRELYTAICRLILLFR 403
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
71-464 5.84e-38

cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 143.90  E-value: 5.84e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRL-GSRLVYVVSSHkvAAEECF-GKNDVVLANRP----QVIIGKHVGYnntnmiAAPYGDHWRNLRRLCTIEIF 144
Cdd:cd11042   6 GDVFTFNLlGKKVTVLLGPE--ANEFFFnGKDEDLSAEEVygflTPPFGGGVVY------YAPFAEQKEQLKFGLNILRR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 145 STHRLncflYVRT--DEVRRLISRLSRlAGTKKTVVELKPMLMdLTfnnIMRMMTGKRYYgeettdEEEAKRVRKLVADV 222
Cdd:cd11042  78 GKLRG----YVPLivEEVEKYFAKWGE-SGEVDLFEEMSELTI-LT---ASRCLLGKEVR------ELLDDEFAQLYHDL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 223 GANTSSGNAVDyvPILRLFSSYenRVKKLGEETDKFLQGLIDDKRGQ-QETGTTMIDHLLVLQKSDIEYYTDQIIKGIIL 301
Cdd:cd11042 143 DGGFTPIAFFF--PPLPLPSFR--RRDRARAKLKEIFSEIIQKRRKSpDKDEDDMLQTLMDAKYKDGRPLTDDEIAGLLI 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 302 IMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVG-LDRLIEEADLSELPYLKNIVLETLRLHPATPLLVpHMAS 380
Cdd:cd11042 219 ALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGdGDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLM-RKAR 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 381 EDCKI--GSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK------LLAFGLGRRACPGSGLAQRIVGL 452
Cdd:cd11042 298 KPFEVegGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSkggkfaYLPFGAGRHRCIGENFAYLQIKT 377
                       410
                ....*....|..
gi 30692923 453 ALGSLIQCFEWE 464
Cdd:cd11042 378 ILSTLLRNFDFE 389
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
129-474 1.96e-37

cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome P450s from insects and crustaceans, including the CYP6, CYP9 and CYP310 subfamilies, which are involved in the metabolism of insect hormones and xenobiotic detoxification. The CYP6-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410679 [Multi-domain]  Cd Length: 429  Bit Score: 142.68  E-value: 1.96e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 129 GDHWRNLRRLCTiEIFSTHRLNCFLYVRTDEVRRLISRLSRLAGTKKtVVELKPMLMDLTFNNIMRMMTGKRYYGEETTD 208
Cdd:cd11056  58 GEKWKELRQKLT-PAFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGK-ELEIKDLMARYTTDVIASCAFGLDANSLNDPE 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 209 EEEAKRVRKLVADVGANTSSGNAVDYVP-ILRLFssyenRVKKLGEETDKFLQGLIDD----KRGQQETGTTMIDHLLVL 283
Cdd:cd11056 136 NEFREMGRRLFEPSRLRGLKFMLLFFFPkLARLL-----RLKFFPKEVEDFFRKLVRDtieyREKNNIVRNDFIDLLLEL 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 284 QKSDIEY-------YTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNrvgldrLIEEAD------ 350
Cdd:cd11056 211 KKKGKIEddksekeLTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDE------VLEKHGgeltye 284
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 351 -LSELPYLKNIVLETLRLHPATPLLVpHMASEDCKIGS--YDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEA 427
Cdd:cd11056 285 aLQEMKYLDQVVNETLRKYPPLPFLD-RVCTKDYTLPGtdVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKK 363
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 30692923 428 QKL----LAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDMK 474
Cdd:cd11056 364 KRHpytyLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPLK 414
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
160-447 1.05e-36

cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Nectria haematococca cytochrome P450 57A1 (CYP57A1), also called pisatin demethylase, which detoxifies the phytoalexin pisatin; Penicillium aethiopicum P450 monooxygenase gsfF, also called griseofulvin synthesis protein F, which catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A during the biosynthesis of griseofulvin, a spirocyclic fungal natural product used to treat dermatophyte infections; and Penicillium aethiopicum P450 monooxygenase vrtE, also called viridicatumtoxin synthesis protein E, which catalyzes hydroxylation at C5 of the polyketide backbone during the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP57A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410683 [Multi-domain]  Cd Length: 425  Bit Score: 140.41  E-value: 1.05e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 160 VRRLISRLSRLAGTKKTVVELKPMLMdLTFNNIMRMMTGKRY-YGEETTDeeeakrVRKLVADVGANTSSGNAVDYVPIL 238
Cdd:cd11060  84 IDLLVDLLDEKAVSGKEVDLGKWLQY-FAFDVIGEITFGKPFgFLEAGTD------VDGYIASIDKLLPYFAVVGQIPWL 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 239 R--LFSSYENRVKK-------LGEETDKFLQGLIDDKRGQQETGTTMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTN 309
Cdd:cd11060 157 DrlLLKNPLGPKRKdktgfgpLMRFALEAVAERLAEDAESAKGRKDMLDSFLEAGLKDPEKVTDREVVAEALSNILAGSD 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 310 TSAVTLEWALSNLLNHPDVISKARDEIDNRV---GLDRLIEEADLSELPYLKNIVLETLRLHPATPLL----VPHmasED 382
Cdd:cd11060 237 TTAIALRAILYYLLKNPRVYAKLRAEIDAAVaegKLSSPITFAEAQKLPYLQAVIKEALRLHPPVGLPlervVPP---GG 313
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30692923 383 CKIGSYDMPRGTTLLVNAWAIHRDPNTW-DDPDSFKPERFEKEEEAQK------LLAFGLGRRACPGSGLAQ 447
Cdd:cd11060 314 ATICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWLEADEEQRrmmdraDLTFGAGSRTCLGKNIAL 385
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
71-482 3.63e-36

cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and amphibians. CYP2K6 from zebrafish has been shown to catalyze the conversion of aflatoxin B1 (AFB1) to its cytotoxic derivative AFB1 exo-8,9-epoxide, while its ortholog in rainbow trout CYP2K1 is also capable of oxidizing lauric acid. In birds, CYP2K is one of the largest CYP2 subfamilies. The CYP2K subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 138.79  E-value: 3.63e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAAEECFGKNDVvLANRPQVIIGKHV--GYNntnmIAAPYGDHWRNLRR--LCTIEIFST 146
Cdd:cd20664   2 GSIFTVQMGTKKVVVLAGYKTVKEALVNHAEA-FGGRPIIPIFEDFnkGYG----ILFSNGENWKEMRRftLTTLRDFGM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 147 HRLNCFLYVrTDEVRRLISRLSRLAGTKktvVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAKRVRKLVADVGanT 226
Cdd:cd20664  77 GKKTSEDKI-LEEIPYLIEVFEKHKGKP---FETTLSMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTG--S 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 227 SSGNAVDYVPILRLFSSYENRVKKLGEETDKFLQGLIDDKRGQQETGT--TMIDHLLVLQKSDIE----YYTDQIIKGII 300
Cdd:cd20664 151 PSVQLYNMFPWLGPFPGDINKLLRNTKELNDFLMETFMKHLDVLEPNDqrGFIDAFLVKQQEEEEssdsFFHDDNLTCSV 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 301 LIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEaDLSELPYLKNIVLETLRLHPATPLLVPHMAS 380
Cdd:cd20664 231 GNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVE-HRKNMPYTDAVIHEIQRFANIVPMNLPHATT 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 381 EDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE----EAQKLLAFGLGRRACPGSGLAQRIVGLALGS 456
Cdd:cd20664 310 RDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQgkfvKRDAFMPFSAGRRVCIGETLAKMELFLFFTS 389
                       410       420
                ....*....|....*....|....*....
gi 30692923 457 LIQCFEWER---VGNVEVDMKEGVGNTVP 482
Cdd:cd20664 390 LLQRFRFQPppgVSEDDLDLTPGLGFTLN 418
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
292-475 8.69e-36

cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome P450/NADPH--P450 reductase; Cytochrome P450 102A1, also called cytochrome P450(BM-3) or P450BM-3, is a bifunctional cytochrome P450/NADPH--P450 reductase. These proteins fuse an N-terminal cytochrome p450 with a C-terminal cytochrome p450 reductase (CYPOR). It functions as a fatty acid monooxygenase, catalyzing the hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, with activity towards fatty acids with a chain length of 9-18 carbons. Its NADPH-dependent reductase activity (via the C-terminal domain) allows electron transfer from NADPH to the heme iron of the N-terminal cytochrome P450. CYP120A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 138.09  E-value: 8.69e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 292 TDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEaDLSELPYLKNIVLETLRLHPAT 371
Cdd:cd11068 227 SDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPPPYE-QVAKLRYIRRVLDETLRLWPTA 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 372 PLLVPHmASEDCKI-GSYDMPRGTTLLVNAWAIHRDPNTW-DDPDSFKPERFEKEEEAqKLLA-----FGLGRRACPGSG 444
Cdd:cd11068 306 PAFARK-PKEDTVLgGKYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFR-KLPPnawkpFGNGQRACIGRQ 383
                       170       180       190
                ....*....|....*....|....*....|.
gi 30692923 445 LAQRIVGLALGSLIQCFEWERVGNVEVDMKE 475
Cdd:cd11068 384 FALQEATLVLAMLLQRFDFEDDPDYELDIKE 414
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
110-488 3.02e-35

cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces cerevisiae cytochrome P450 56, also called cytochrome P450-DIT2, and similar fungal proteins. CYP56 is involved in spore wall maturation and is thought to catalyze the oxidation of tyrosine residues in the formation of LL-dityrosine-containing precursors of the spore wall. The CYP56-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 136.69  E-value: 3.02e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 110 VIIGKHVGYNNTNMIAApYGDHWRNLRRLCTIEIfsTHRLNCFLYVR-TDEVRRLISRLSRLAGTKK-TVVELKPMLMDL 187
Cdd:cd11070  37 GNQYKIPAFYGPNVISS-EGEDWKRYRKIVAPAF--NERNNALVWEEsIRQAQRLIRYLLEEQPSAKgGGVDVRDLLQRL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 188 TFNNIMRMMTGKRYygeETTDEEEAKRVRKLvadvgaNTSSGNAVDYV----PIL-RLFSSYENRVKKLGEETDKFLQGL 262
Cdd:cd11070 114 ALNVIGEVGFGFDL---PALDEEESSLHDTL------NAIKLAIFPPLflnfPFLdRLPWVLFPSRKRAFKDVDEFLSEL 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 263 IDDKRGQQETGTTMIDHLLVLQKS------DIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEI 336
Cdd:cd11070 185 LDEVEAELSADSKGKQGTESVVASrlkrarRSGGLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEI 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 337 DnRVGLDRLIE---EADLSELPYLKNIVLETLRLHPATPLLvPHMASEDCKI-----GSYDMPRGTTLLVNAWAIHRDPN 408
Cdd:cd11070 265 D-SVLGDEPDDwdyEEDFPKLPYLLAVIYETLRLYPPVQLL-NRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPT 342
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 409 TW-DDPDSFKPERF----EKEEEAQKL-------LAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWeRVGNVEVDMKEG 476
Cdd:cd11070 343 IWgPDADEFDPERWgstsGEIGAATRFtpargafIPFSAGPRACLGRKFALVEFVAALAELFRQYEW-RVDPEWEEGETP 421
                       410
                ....*....|..
gi 30692923 477 VGNTVPKAIPLK 488
Cdd:cd11070 422 AGATRDSPAKLR 433
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
129-468 8.40e-35

cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate cytochrome P450 family 26 enzymes, and similar cytochrome P450s; This family includes cyanobacterial CYP120A1 and vertebrate cytochrome P450s 26A1 (CYP26A1), 26B1 (CYP26B1), and 26C1 (CYP26C1). These are retinoic acid-metabolizing cytochromes that play key roles in retinoic acid (RA) metabolism. Human and zebrafish CYP26a1, as well as Synechocystis CYP120A1 are characterized as RA hydroxylases. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 135.10  E-value: 8.40e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 129 GDHWRNLRRLcTIEIFSTHRLNCFLYVRTDEVRRLISRLSrlagtKKTVVELKPMLMDLTFnnimrMMTGKRYYGEETTD 208
Cdd:cd11044  76 GEEHRRRRKL-LAPAFSREALESYVPTIQAIVQSYLRKWL-----KAGEVALYPELRRLTF-----DVAARLLLGLDPEV 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 209 EEEAkrvrkLVADVGANTSSGNAVdyvPILRLFSSYeNRVKKLGEETDKFLQGLIDDKR-GQQETGTTMIDHLLVLQKSD 287
Cdd:cd11044 145 EAEA-----LSQDFETWTDGLFSL---PVPLPFTPF-GRAIRARNKLLARLEQAIRERQeEENAEAKDALGLLLEAKDED 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 288 IEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNrVGLDRLIEEADLSELPYLKNIVLETLRL 367
Cdd:cd11044 216 GEPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDA-LGLEEPLTLESLKKMPYLDQVIKEVLRL 294
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 368 HPATP-----LLvphmasEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF--EKEEEAQK---LLAFGLGR 437
Cdd:cd11044 295 VPPVGggfrkVL------EDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFspARSEDKKKpfsLIPFGGGP 368
                       330       340       350
                ....*....|....*....|....*....|.
gi 30692923 438 RACPGSGLAQRIVGLALGSLIQCFEWERVGN 468
Cdd:cd11044 369 RECLGKEFAQLEMKILASELLRNYDWELLPN 399
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
71-446 4.40e-34

cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome P450 1B1 (CYP1B1) is expressed in liver and extrahepatic tissues where it carries out the metabolism of numerous xenobiotics, including metabolic activation of polycyclic aromatic hydrocarbons. It is also important in regulating endogenous metabolic pathways, including the metabolism of steroid hormones, fatty acids, melatonin, and vitamins. CYP1B1 is overexpressed in a wide variety of tumors and is associated with angiogenesis. It is also associated with adipogenesis, obesity, hypertension, and atherosclerosis. It is therefore a target for the treatment of metabolic diseases and cancer. Also included in this subfamily are CYP1C proteins from fish, birds and amphibians. The CYP1B1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 133.21  E-value: 4.40e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVyVVSSHKVAAEECFGKNDVVLANRPQVIIGKHVGyNNTNMIAAPYGDHWRNLRRLC--TIEIFST-- 146
Cdd:cd20675   2 GDVFQIRLGSRPV-VVLNGERAIRQALVQQGTDFAGRPDFASFRVVS-GGRSLAFGGYSERWKAHRRVAhsTVRAFSTrn 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 147 -HRLNCFLYVRTDEVRRLISRLSRLAGTKKTVVELKPMLMDLTfnNIMRMMT-GKRYYGEETTDEEEAKRVRKLVADVGA 224
Cdd:cd20675  80 pRTRKAFERHVLGEARELVALFLRKSAGGAYFDPAPPLVVAVA--NVMSAVCfGKRYSHDDAEFRSLLGRNDQFGRTVGA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 225 ntssGNAVDYVPILRLF-----SSYENrVKKLGEETDKFLQGLIDDKRGQQETGTT--MIDHLL-------------VLQ 284
Cdd:cd20675 158 ----GSLVDVMPWLQYFpnpvrTVFRN-FKQLNREFYNFVLDKVLQHRETLRGGAPrdMMDAFIlalekgksgdsgvGLD 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 285 KSDIE-YYTDqiIKGiilimviAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLE 363
Cdd:cd20675 233 KEYVPsTVTD--IFG-------ASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYE 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 364 TLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKE------EEAQKLLAFGLGR 437
Cdd:cd20675 304 AMRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDEngflnkDLASSVMIFSVGK 383

                ....*....
gi 30692923 438 RACPGSGLA 446
Cdd:cd20675 384 RRCIGEELS 392
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
129-462 5.05e-34

Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP72 clan is associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. This clan includes: CYP734 enzymes that are involved in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis; CYP714 enzymes that are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels; and CYP72 family enzymes, among others. The CYP72 clan belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 132.85  E-value: 5.05e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 129 GDHWRNLRRLCTIEiFSTHRLNCFLYVRTDEVRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYygeettd 208
Cdd:cd11052  66 GEKWAKHRRIANPA-FHGEKLKGMVPAMVESVSDMLERWKKQMGEEGEEVDVFEEFKALTADIISRTAFGSSY------- 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 209 eEEAKRVRKLVADVGANTSSGNAVDYVPILRLFSSYENRV-KKLGEETDKFLQGLIDdKRGQQETGTTMIDH----LLVL 283
Cdd:cd11052 138 -EEGKEVFKLLRELQKICAQANRDVGIPGSRFLPTKGNKKiKKLDKEIEDSLLEIIK-KREDSLKMGRGDDYgddlLGLL 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 284 QKSDIEyytDQIIKGIILIMVI--------AGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGlDRLIEEADLSELP 355
Cdd:cd11052 216 LEANQS---DDQNKNMTVQEIVdecktfffAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCG-KDKPPSDSLSKLK 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 356 YLKNIVLETLRLHPATPLLvPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTW-DDPDSFKPERF-----EKEEEAQK 429
Cdd:cd11052 292 TVSMVINESLRLYPPAVFL-TRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFadgvaKAAKHPMA 370
                       330       340       350
                ....*....|....*....|....*....|...
gi 30692923 430 LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFE 462
Cdd:cd11052 371 FLPFGLGPRNCIGQNFATMEAKIVLAMILQRFS 403
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
71-484 7.63e-34

cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is pseudogenized in humans because of five nonsense mutations in the putative coding region. However, in other organisms including cynomolgus monkey, CYP1D1 is a functional drug-metabolizing enzyme that is highly expressed in the liver. CYP1D1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 132.53  E-value: 7.63e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVGYNNTNMIAAPYGDHWRNLRRLCT--IEIFSTHR 148
Cdd:cd20677   2 GDVFQIKLGMLPVVVVSGLE-TIKQVLLKQGESFAGRPDFYTFSLIANGKSMTFSEKYGESWKLHKKIAKnaLRTFSKEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 149 LN-----CFL--YVrTDEVRRLISRLSRLAgTKKTVVELKPMLMDLTFNNIMRMMTGKRYygeETTDEEEAKRVrKLVAD 221
Cdd:cd20677  81 AKsstcsCLLeeHV-CAEASELVKTLVELS-KEKGSFDPVSLITCAVANVVCALCFGKRY---DHSDKEFLTIV-EINND 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 222 VGANTSSGNAVDYVPILRLF-SSYENRVKKLGEETDKFLQGLIDDKRGQQETGTT--MIDHLLVL-QKSDIEYYTDQIIK 297
Cdd:cd20677 155 LLKASGAGNLADFIPILRYLpSPSLKALRKFISRLNNFIAKSVQDHYATYDKNHIrdITDALIALcQERKAEDKSAVLSD 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 298 GIILIMVI----AGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPL 373
Cdd:cd20677 235 EQIISTVNdifgAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSFVPF 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 374 LVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKE------EEAQKLLAFGLGRRACPGSGLAQ 447
Cdd:cd20677 315 TIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDEngqlnkSLVEKVLIFGMGVRKCLGEDVAR 394
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 30692923 448 RIVGLALGSLIQCFEWERVGNVEVDMKEGVGNTV-PKA 484
Cdd:cd20677 395 NEIFVFLTTILQQLKLEKPPGQKLDLTPVYGLTMkPKP 432
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
71-461 1.25e-33

cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, reptiles, and amphibians. The hominin CYP2D subfamily consists of a functional CYP2D6 and two paralogs, CYP2D7 and CYP2D8, that are often not functional in some species. Human CYP2D6 has a high affinity for alkaloids and can detoxify them. It is also responsible for metabolizing about 25% of commonly used drugs, such as antidepressants, beta-blockers, and antiarrhythmics. The CYP2D subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 131.74  E-value: 1.25e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVGY--NNTNMIAAPYGDHWRNLRR--LCTIEIFST 146
Cdd:cd20663   2 GDVFSLQMAWKPVVVLNGLK-AVREALVTCGEDTADRPPVPIFEHLGFgpKSQGVVLARYGPAWREQRRfsVSTLRNFGL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 147 HRLNCFLYVrTDEVRRLISRLSRLAGTKktvVELKPMLMDLTFNNIMRMMTGKRY-YGEETTdeeeaKRVRKLVADvGAN 225
Cdd:cd20663  81 GKKSLEQWV-TEEAGHLCAAFTDQAGRP---FNPNTLLNKAVCNVIASLIFARRFeYEDPRF-----IRLLKLLEE-SLK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 226 TSSG---NAVDYVPILRlfssyenRVKKLgeeTDKFLQGliddkrgqQETGTTMIDHLLVLQK----------------- 285
Cdd:cd20663 151 EESGflpEVLNAFPVLL-------RIPGL---AGKVFPG--------QKAFLALLDELLTEHRttwdpaqpprdltdafl 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 286 SDIEY--------YTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYL 357
Cdd:cd20663 213 AEMEKakgnpessFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYT 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 358 KNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPE-------RFEKEEeaqKL 430
Cdd:cd20663 293 NAVIHEVQRFGDIVPLGVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEhfldaqgHFVKPE---AF 369
                       410       420       430
                ....*....|....*....|....*....|.
gi 30692923 431 LAFGLGRRACPGSGLAQRIVGLALGSLIQCF 461
Cdd:cd20663 370 MPFSAGRRACLGEPLARMELFLFFTCLLQRF 400
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
124-462 6.31e-33

cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect cytochrome P450s from families 313 (CYP313) and 318 (CYP318), and similar proteins. These proteins may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. Their specific function is yet unknown. They belong to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410680 [Multi-domain]  Cd Length: 427  Bit Score: 130.03  E-value: 6.31e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 124 IAAPYgDHWRNLRRL---CtieiFSTHRLNCFLYVRTDEVRRLISRLSRLA--GTKKTVVELKPMLMDLTFNNIMRM-MT 197
Cdd:cd11057  48 FSAPY-PIWKLQRKAlnpS----FNPKILLSFLPIFNEEAQKLVQRLDTYVggGEFDILPDLSRCTLEMICQTTLGSdVN 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 198 GKRYYGEETTDEEEakRVRKLVADVGANtssgnAVDYVPILRLFSSYENRVKKLGEETDKFLQGLIDDKRGQQETGTTM- 276
Cdd:cd11057 123 DESDGNEEYLESYE--RLFELIAKRVLN-----PWLHPEFIYRLTGDYKEEQKARKILRAFSEKIIEKKLQEVELESNLd 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 277 --------------IDHLLVLQKSDiEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGL 342
Cdd:cd11057 196 seedeengrkpqifIDQLLELARNG-EEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPD 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 343 D-RLIEEADLSELPYLKNIVLETLRLHPATPlLVPHMASEDCKIGS-YDMPRGTTLLVNAWAIHRDPNTW-DDPDSFKPE 419
Cdd:cd11057 275 DgQFITYEDLQQLVYLEMVLKETMRLFPVGP-LVGRETTADIQLSNgVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPD 353
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 30692923 420 RFEKEEEAQK----LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFE 462
Cdd:cd11057 354 NFLPERSAQRhpyaFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYR 400
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
300-476 1.14e-32

cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). Members of the CYP97 clan include Arabidopsis thaliana cytochrome P450s 97A3 (CYP97A3), CYP97B3, and CYP97C1. CYP97A3 is also called protein LUTEIN DEFICIENT 5 (LUT5) and CYP97C1 is also called carotene epsilon-monooxygenase or protein LUTEIN DEFICIENT 1 (LUT1). These cytochromes function as beta- and epsilon-ring carotenoid hydroxylases and are involved in the biosynthesis of xanthophylls. CYP97 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410672 [Multi-domain]  Cd Length: 441  Bit Score: 129.41  E-value: 1.14e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 300 ILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVpHMA 379
Cdd:cd11046 245 LMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLI-RRA 323
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 380 SEDCKI--GSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFE------KEEEAQ--KLLAFGLGRRACPGSGLA--Q 447
Cdd:cd11046 324 VEDDKLpgGGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLdpfinpPNEVIDdfAFLPFGGGPRKCLGDQFAllE 403
                       170       180       190
                ....*....|....*....|....*....|
gi 30692923 448 RIVGLALgsLIQCFEWE-RVGNVEVDMKEG 476
Cdd:cd11046 404 ATVALAM--LLRRFDFElDVGPRHVGMTTG 431
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
71-481 1.33e-32

cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in mice and humans. They function as catalysts of arachidonic acid metabolism and are active in the metabolism of fatty acids to generate bioactive compounds. Human CYP2J2, also called arachidonic acid epoxygenase or albendazole monooxygenase (hydroxylating), is a membrane-bound cytochrome P450 primarily expressed in the heart and plays a significant role in cardiovascular diseases. The CYP2J subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 128.76  E-value: 1.33e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAAEECFGKNDVVLaNRPQVIIGKHVgYNNTNMIAAPyGDHWRNLRR--LCTIEIFSTHR 148
Cdd:cd20662   2 GNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFM-NRPETPLRERI-FNKNGLIFSS-GQTWKEQRRfaLMTLRNFGLGK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 149 LNcfLYVRTDEVRRLISRLSRLAGTKKTVVELKpmLMDLTFNNIMRMMTGKRYygeETTDEEEAKRVRKLVADVGANTSS 228
Cdd:cd20662  79 KS--LEERIQEECRHLVEAIREEKGNPFNPHFK--INNAVSNIICSVTFGERF---EYHDEWFQELLRLLDETVYLEGSP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 229 G----NA----VDYVP--ILRLFSSYenrvKKLgeetDKFLQGLIDDKRGQQETGTT--MIDHLLVLQKSDIEYYTDQII 296
Cdd:cd20662 152 MsqlyNAfpwiMKYLPgsHQTVFSNW----KKL----KLFVSDMIDKHREDWNPDEPrdFIDAYLKEMAKYPDPTTSFNE 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 297 KGII---LIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPL 373
Cdd:cd20662 224 ENLIcstLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPL 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 374 LVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK---LLAFGLGRRACPGSGLAQRIV 450
Cdd:cd20662 304 NVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQFKKreaFLPFSMGKRACLGEQLARSEL 383
                       410       420       430
                ....*....|....*....|....*....|.
gi 30692923 451 GLALGSLIQCFEWERVGNVEVDMKEGVGNTV 481
Cdd:cd20662 384 FIFFTSLLQKFTFKPPPNEKLSLKFRMGITL 414
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
236-470 1.71e-32

cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of predominantly fungal cytochrome P450s (CYPs) with similarity to Fusarium fujikuroi Cytochrome P450 503A1 (CYP503A1, also called ent-kaurene oxidase or cytochrome P450-4), Aspergillus nidulans austinol synthesis protein I (ausI), Alternaria alternata tentoxin synthesis protein 1 (TES1), and Acanthamoeba polyphaga mimivirus cytochrome P450 51 (CYP51, also called P450-LIA1 or sterol 14-alpha demethylase). Ent-kaurene oxidase catalyzes three successive oxidations of the 4-methyl group of ent-kaurene to form kaurenoic acid, an intermediate in gibberellin biosynthesis. AusI and TES1 are cytochrome P450 monooxygenases that mediate the biosynthesis of the meroterpenoids, austinol and dehydroaustinol, and the phytotoxin tentoxin, respectively. P450-LIA1 catalyzes the 14-alpha demethylation of obtusifoliol and functions in steroid biosynthesis. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 128.95  E-value: 1.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 236 PILRLFSSYENRVKKLGEETDKFLQGLIDDKRGQQETG-----TTMIDHLLVLQKSDIEYyTDQIIKGIILIMVIAGTNT 310
Cdd:cd11041 164 PLVAPFLPEPRRLRRLLRRARPLIIPEIERRRKLKKGPkedkpNDLLQWLIEAAKGEGER-TPYDLADRQLALSFAAIHT 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 311 SAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGS-YD 389
Cdd:cd11041 243 TSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVTLSDgLT 322
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 390 MPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQKL-------------LAFGLGRRACPGSGLAQRIVGLALGS 456
Cdd:cd11041 323 LPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQekkhqfvstspdfLGFGHGRHACPGRFFASNEIKLILAH 402
                       250
                ....*....|....
gi 30692923 457 LIQCFEWERVGNVE 470
Cdd:cd11041 403 LLLNYDFKLPEGGE 416
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
157-488 1.73e-32

cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium sporotrichioides cytochrome P450 58 (CYP58, also known as Tri4 and trichodiene oxygenase), and similar fungal proteins. CYP58 catalyzes the oxygenation of trichodiene during the biosynthesis of trichothecenes, which are sesquiterpenoid toxins that act by inhibiting protein biosynthesis. The CYP58-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410685 [Multi-domain]  Cd Length: 425  Bit Score: 128.53  E-value: 1.73e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 157 TDEVRRLISRLSRLAGTKKtVVELKPMLMDLTFNNIMRMMTGKRYYGEETTDEEEAkrvrkLVADVGANTSSGNAVDYVP 236
Cdd:cd11062  79 QEKVDKLVSRLREAKGTGE-PVNLDDAFRALTADVITEYAFGRSYGYLDEPDFGPE-----FLDALRALAEMIHLLRHFP 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 237 ILR--LFSSYENRVKKLGEETDKFL-----------QGLIDDKRGQQETGTTMIDHLLVLQKSDIEYYTDQIIKGIILIM 303
Cdd:cd11062 153 WLLklLRSLPESLLKRLNPGLAVFLdfqesiakqvdEVLRQVSAGDPPSIVTSLFHALLNSDLPPSEKTLERLADEAQTL 232
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 304 VIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRV-GLDRLIEEADLSELPYLKNIVLETLRL-HPAT---PLLVPHm 378
Cdd:cd11062 233 IGAGTETTARTLSVATFHLLSNPEILERLREELKTAMpDPDSPPSLAELEKLPYLTAVIKEGLRLsYGVPtrlPRVVPD- 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 379 asEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPER----FEKEEEAQKLLAFGLGRRACPGSGLAQRIVGLAL 454
Cdd:cd11062 312 --EGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERwlgaAEKGKLDRYLVPFSKGSRSCLGINLAYAELYLAL 389
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 30692923 455 GSLIQCFEWERVGNVE--VDMKEGVGNTVPKAIPLK 488
Cdd:cd11062 390 AALFRRFDLELYETTEedVEIVHDFFLGVPKPGSKG 425
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
162-466 3.65e-32

cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, and similar cytochrome P450s; CYP46A1 is also called cholesterol 24-hydroxylase (EC 1.14.14.25), CH24H, cholesterol 24-monooxygenase, or cholesterol 24S-hydroxylase. It catalyzes the conversion of cholesterol into 24S-hydroxycholesterol and, to a lesser extent, 25-hydroxycholesterol. CYP46A1 is associated with high-order brain functions; increased expression improves cognition while a reduction leads to a poor cognitive performance. It also plays a role in the pathogenesis or progression of neurodegenerative disorders. CYP46A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410706 [Multi-domain]  Cd Length: 429  Bit Score: 127.64  E-value: 3.65e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 162 RLISRLSRLAGTKkTVVELKPMLMDLTFNNImrmmtGKRYYGEET-TDEEEAKRVRKLVADV--GANTSSGNavdyvPIL 238
Cdd:cd20613 103 LLVEKLSKKADGK-TEVNMLDEFNRVTLDVI-----AKVAFGMDLnSIEDPDSPFPKAISLVleGIQESFRN-----PLL 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 239 RLF---SSYENRVKKLGEETDKFLQGLIDDKRGQQETGTTMIDHLL--VLQKSDIEYYTDqiikgiILIMV-------IA 306
Cdd:cd20613 172 KYNpskRKYRREVREAIKFLRETGRECIEERLEALKRGEEVPNDILthILKASEEEPDFD------MEELLddfvtffIA 245
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 307 GTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMAsEDCKIG 386
Cdd:cd20613 246 GQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELT-KDIELG 324
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 387 SYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK----LLAFGLGRRACPGSGLAQ---RIVglaLGSLIQ 459
Cdd:cd20613 325 GYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIpsyaYFPFSLGPRSCIGQQFAQieaKVI---LAKLLQ 401

                ....*..
gi 30692923 460 CFEWERV 466
Cdd:cd20613 402 NFKFELV 408
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
71-467 4.21e-32

unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410704 [Multi-domain]  Cd Length: 421  Bit Score: 127.44  E-value: 4.21e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAAEecfgkndvVLANRPQV--------IIGKHVGYNNtnmIAAPYGDHWRNLRRLcTIE 142
Cdd:cd11083   1 GSAYRFRLGRQPVLVISDPELIRE--------VLRRRPDEfrrissleSVFREMGING---VFSAEGDAWRRQRRL-VMP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 143 IFSTHRLNCFLYVRTDEVRRLISRLSRLAGTKKtVVELKPMLMDLTFNnimrmMTGKRYYGEET-TDEEEAKRVRKLVAD 221
Cdd:cd11083  69 AFSPKHLRYFFPTLRQITERLRERWERAAAEGE-AVDVHKDLMRYTVD-----VTTSLAFGYDLnTLERGGDPLQEHLER 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 222 VGAN-TSSGNAVdyVPILRLFSSYENR-VKKLGEETDKFLQGLIDDKR------GQQETGTTMIDHLLVLQKSDIEYYTD 293
Cdd:cd11083 143 VFPMlNRRVNAP--FPYWRYLRLPADRaLDRALVEVRALVLDIIAAARarlaanPALAEAPETLLAMMLAEDDPDARLTD 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 294 QIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIE-EADLSELPYLKNIVLETLRLHPATP 372
Cdd:cd11083 221 DEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPlLEALDRLPYLEAVARETLRLKPVAP 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 373 LLvPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK------LLAFGLGRRACPGSGLA 446
Cdd:cd11083 301 LL-FLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEphdpssLLPFGAGPRLCPGRSLA 379
                       410       420
                ....*....|....*....|.
gi 30692923 447 QRIVGLALGSLIQCFEWERVG 467
Cdd:cd11083 380 LMEMKLVFAMLCRNFDIELPE 400
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
129-477 1.26e-30

cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is composed of family 4 cytochrome P450s from vertebrate subfamilies A (CYP4A), B (CYP4B), F (CYP4F), T (CYP4T), X (CYP4X), and Z (CYP4Z). Also included are similar proteins from lancelets, tunicates, hemichordates, echinoderms, mollusks, annelid worms, sponges, and choanoflagellates, among others. The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B and CYP4F are conserved among vertebrates. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4F enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4B_4F-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410752 [Multi-domain]  Cd Length: 423  Bit Score: 123.44  E-value: 1.26e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 129 GDHWRNLRRLCTiEIFSTHRLNCFLYVRTDEVRRLISRLSRLAGTKKTVvELKPMLMDLTFNNIMR-MMTGKRYYGEETT 207
Cdd:cd20659  54 GKKWKRNRRLLT-PAFHFDILKPYVPVYNECTDILLEKWSKLAETGESV-EVFEDISLLTLDIILRcAFSYKSNCQQTGK 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 208 DEEEAKRVRKLVADVGANTSsgNAVDYVPILRLFSSYENRVKKLGEETDKFLQGLIDDKR----GQQETGTTM------I 277
Cdd:cd20659 132 NHPYVAAVHELSRLVMERFL--NPLLHFDWIYYLTPEGRRFKKACDYVHKFAEEIIKKRRkeleDNKDEALSKrkyldfL 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 278 DHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYL 357
Cdd:cd20659 210 DILLTARDEDGKGLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYL 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 358 KNIVLETLRLHPATPLlVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEkEEEAQKL-----LA 432
Cdd:cd20659 290 TMCIKESLRLYPPVPF-IARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFL-PENIKKRdpfafIP 367
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 30692923 433 FGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDMKEGV 477
Cdd:cd20659 368 FSAGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNHPVEPKPGL 412
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
245-488 1.51e-29

cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces viciae-fabae cytochrome P450 67 (CYP67), also called planta-induced rust protein 16, Cystobasidium minutum (Rhodotorula minuta) cytochrome P450rm, and other fungal cytochrome P450s. P450rm catalyzes the formation of isobutene and 4-hydroxylation of benzoate. The gene encoding CYP67 is a planta-induced gene that is expressed in haustoria and rust-infected leaves. The CYP67-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410684 [Multi-domain]  Cd Length: 418  Bit Score: 120.02  E-value: 1.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 245 ENRVKKLGEETDKFLQGLIDDKRGqqETGTTmidhllvlqksdieyYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLN 324
Cdd:cd11061 183 KERLKAEEEKRPDIFSYLLEAKDP--ETGEG---------------LDLEELVGEARLLIVAGSDTTATALSAIFYYLAR 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 325 HPDVISKARDEIDNRV-GLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPH-MASEDCKIGSYDMPRGTTLLVNAWA 402
Cdd:cd11061 246 NPEAYEKLRAELDSTFpSDDEIRLGPKLKSLPYLRACIDEALRLSPPVPSGLPReTPPGGLTIDGEYIPGGTTVSVPIYS 325
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 403 IHRDPNTWDDPDSFKPER-FEKEEEAQKL----LAFGLGRRACPGSGLA---QRIVglaLGSLIQCFEWERVGNVEVDMK 474
Cdd:cd11061 326 IHRDERYFPDPFEFIPERwLSRPEELVRArsafIPFSIGPRGCIGKNLAymeLRLV---LARLLHRYDFRLAPGEDGEAG 402
                       250
                ....*....|....
gi 30692923 475 EGVGNTVPKAIPLK 488
Cdd:cd11061 403 EGGFKDAFGRGPGD 416
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
129-471 1.75e-28

cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana cytochrome P450s (CYP86A1, CYP86A2, CYP86A4, among others), Petunia x hybrida CYP86A22, and Vicia sativa CYP94A1 and CYP94A2. They are P450-dependent fatty acid omega-hydroxylases that catalyze the omega-hydroxylation of various fatty acids. CYP86A2 acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18; CYP86A22 prefers substrates with chain lengths of C16 and C18; and CYP94A1 acts on various fatty acids from 10 to 18 carbons. They play roles in the biosynthesis of extracellular lipids, cutin synthesis, and plant defense. The CYP86A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410687 [Multi-domain]  Cd Length: 432  Bit Score: 117.31  E-value: 1.75e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 129 GDHWRNLRRLCTIEiFSTHRLNCFLY-VRTDEVRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGK--RYYGEE 205
Cdd:cd11064  56 GELWKFQRKTASHE-FSSRALREFMEsVVREKVEKLLVPLLDHAAESGKVVDLQDVLQRFTFDVICKIAFGVdpGSLSPS 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 206 TTDEEEAKrvrklvADVGANTSSGNAVDYVPIL----RLFS-SYEnrvKKLGEET---DKFLQGLIDDKR----GQQETG 273
Cdd:cd11064 135 LPEVPFAK------AFDDASEAVAKRFIVPPWLwklkRWLNiGSE---KKLREAIrviDDFVYEVISRRReelnSREEEN 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 274 TTMIDHL-LVLQKSDIEY--YTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDN-----RVGLDRL 345
Cdd:cd11064 206 NVREDLLsRFLASEEEEGepVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSklpklTTDESRV 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 346 IEEADLSELPYLKNIVLETLRLHPATPlLVPHMASEDckigsyDM-------PRGTTLLVNAWAIHRDPNTW-DDPDSFK 417
Cdd:cd11064 286 PTYEELKKLVYLHAALSESLRLYPPVP-FDSKEAVND------DVlpdgtfvKKGTRIVYSIYAMGRMESIWgEDALEFK 358
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 418 PERFEKEEE------AQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEV 471
Cdd:cd11064 359 PERWLDEDGglrpesPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKV 418
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
256-481 3.01e-28

cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases catalyze the first hydroxylation step in the assimilation of alkanes and fatty acids by filamentous fungi. The number of CYP52 proteins depend on the fungal species: for example, Candida tropicalis has seven, Candida maltose has eight, and Yarrowia lipolytica has twelve. The CYP52 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410686 [Multi-domain]  Cd Length: 419  Bit Score: 116.50  E-value: 3.01e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 256 DKFLQGLIDDKRGQQETGTTMIDHLlVLQKSDIEYYTDQIIkGIILimviAGTNTSAVTLEWALSNLLNHPDVISKARDE 335
Cdd:cd11063 183 DKALARKEESKDEESSDRYVFLDEL-AKETRDPKELRDQLL-NILL----AGRDTTASLLSFLFYELARHPEVWAKLREE 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 336 IDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVpHMASEDCKI---GSYD------MPRGTTLLVNAWAIHRD 406
Cdd:cd11063 257 VLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNS-RVAVRDTTLprgGGPDgkspifVPKGTRVLYSVYAMHRR 335
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30692923 407 PNTW-DDPDSFKPERFEKEE-EAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFewERVGNVEV-DMKEGVGNTV 481
Cdd:cd11063 336 KDIWgPDAEEFRPERWEDLKrPGWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTF--DRIESRDVrPPEERLTLTL 411
PLN02738 PLN02738
carotene beta-ring hydroxylase
71-476 1.03e-27

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 116.94  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   71 GGVMSLRLGSRLVYVVSSHKVAAE------ECFGKNdvVLANRPQVIIGKhvgynntNMIAAPyGDHWRnLRRLCTIEIF 144
Cdd:PLN02738 165 GGIFRLTFGPKSFLIVSDPSIAKHilrdnsKAYSKG--ILAEILEFVMGK-------GLIPAD-GEIWR-VRRRAIVPAL 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  145 STHRLNCFLYVRTDEVRRLISRLSRlAGTKKTVVELKPMLMDLTFNNImrmmtGKRYYGEE----TTDEEEAKRVRKLVA 220
Cdd:PLN02738 234 HQKYVAAMISLFGQASDRLCQKLDA-AASDGEDVEMESLFSRLTLDII-----GKAVFNYDfdslSNDTGIVEAVYTVLR 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  221 DVGANTSSGNAVDYVPILRLFSSYENRVKKLGEETDKFLQGLIDD-KRGQQETGTTM-----------IDHLLVLQKSDI 288
Cdd:PLN02738 308 EAEDRSVSPIPVWEIPIWKDISPRQRKVAEALKLINDTLDDLIAIcKRMVEEEELQFheeymnerdpsILHFLLASGDDV 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  289 eyyTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGlDRLIEEADLSELPYLKNIVLETLRLH 368
Cdd:PLN02738 388 ---SSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLG-DRFPTIEDMKKLKYTTRVINESLRLY 463
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  369 PATPLLVPHMASEDCkIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF-----EKEEEAQKL--LAFGLGRRACP 441
Cdd:PLN02738 464 PQPPVLIRRSLENDM-LGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpldgpNPNETNQNFsyLPFGGGPRKCV 542
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 30692923  442 GSGLA--QRIVGLALgsLIQCFEWE-RVGNVEVDMKEG 476
Cdd:PLN02738 543 GDMFAsfENVVATAM--LVRRFDFQlAPGAPPVKMTTG 578
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
71-487 1.30e-27

cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members are selectively expressed in lung tissues. They are responsible for the bioactivation of several pneumotoxic and carcinogenic chemicals such as benzene, styrene, naphthalene, and 1,1-dichloroethylene. CYP2F1 and CYP2F3 selectively catalyzes the 3-methyl dehydrogenation of 3-methylindole, forming toxic reactive intermediates that can form adducts with proteins and DNA. The CYP2F subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 114.86  E-value: 1.30e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVA-------AEECFGKNDVVLANRpqviigkhvgYNNTNMIAAPYGDHWRNLRRlctiei 143
Cdd:cd20669   2 GSVYTVYLGPRPVVVLCGYQAVkealvdqAEEFSGRGDYPVFFN----------FTKGNGIAFSNGERWKILRR------ 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 144 FSTHRLNCF-LYVRTDEVRRLISRLSRLAGTKKTvvELKPMlmDLTF-------NNIMRMMTGKRY-YGEettdeeeaKR 214
Cdd:cd20669  66 FALQTLRNFgMGKRSIEERILEEAQFLLEELRKT--KGAPF--DPTFllsravsNIICSVVFGSRFdYDD--------KR 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 215 VRKLVADVGAN---TSS---------GNAVDYVPIL--RLFSSYEnRVKKLGEETDKFLQGLIDdkrgqQETGTTMIDHL 280
Cdd:cd20669 134 LLTILNLINDNfqiMSSpwgelynifPSVMDWLPGPhqRIFQNFE-KLRDFIAESVREHQESLD-----PNSPRDFIDCF 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 281 LVL----QKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPY 356
Cdd:cd20669 208 LTKmaeeKQDPLSHFNMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPY 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 357 LKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK----LLA 432
Cdd:cd20669 288 TDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKkndaFMP 367
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30692923 433 FGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVE-VDMK---EGVGNtVPKAIPL 487
Cdd:cd20669 368 FSAGKRICLGESLARMELFLYLTAILQNFSLQPLGAPEdIDLTplsSGLGN-VPRPFQL 425
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
307-447 1.56e-27

cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of vertebrate cytochrome P450 family 4, subfamily V (CYP4V) enzymes and similar proteins, including invertebrate subfamily C (CYP4C). Insect CYP4C enzymes may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. CYP4V2, the most characterized member of the CYP4V subfamily, is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410753 [Multi-domain]  Cd Length: 429  Bit Score: 114.67  E-value: 1.56e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 307 GTNTSAVTLEWALSNLLNHPDVISKARDEIDnRV--GLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVpHMASEDCK 384
Cdd:cd20660 244 GHDTTAAAINWALYLIGSHPEVQEKVHEELD-RIfgDSDRPATMDDLKEMKYLECVIKEALRLFPSVPMFG-RTLSEDIE 321
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30692923 385 IGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK----LLAFGLGRRACPGSGLAQ 447
Cdd:cd20660 322 IGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRhpyaYIPFSAGPRNCIGQKFAL 388
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
237-474 4.18e-27

cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most abundant CYP subfamily in the liver, consists of drug-metabolizing enzymes. In humans, there are at least four isoforms: CYP3A4, 3A5, 3A7, and 3A3. CYP3A enzymes are embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. They oxidize a variety of structurally unrelated compounds including steroids, fatty acids, and xenobiotics. The CYP3A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 113.28  E-value: 4.18e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 237 ILRLFSSYENRVKKLGEETDK-----FLQGLID---DKRGQQETGTTmiDHLLVLQKsdieyytdqiikgiiLIMVIAGT 308
Cdd:cd20650 179 VTNFFYKSVKKIKESRLDSTQkhrvdFLQLMIDsqnSKETESHKALS--DLEILAQS---------------IIFIFAGY 241
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 309 NTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLvPHMASEDCKIGSY 388
Cdd:cd20650 242 ETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRL-ERVCKKDVEINGV 320
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 389 DMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQKL----LAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWE 464
Cdd:cd20650 321 FIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDpyiyLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFK 400
                       250
                ....*....|
gi 30692923 465 RVGNVEVDMK 474
Cdd:cd20650 401 PCKETQIPLK 410
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
246-474 4.86e-27

cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is composed of CYPs from unicellular ciliates similar to Tetrahymena thermophila CYP5011A1, whose function is still unknown. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410714 [Multi-domain]  Cd Length: 427  Bit Score: 113.12  E-value: 4.86e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 246 NRVKKLgeetDKFLQGLIDDK-----RGQQETGTTMIDHLLVL--QKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWA 318
Cdd:cd20621 177 KRVKEL----RQFIEKIIQNRikqikKNKDEIKDIIIDLDLYLlqKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMC 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 319 LSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLV 398
Cdd:cd20621 253 LYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVNV 332
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 399 NAWAIHRDPNTWDDPDSFKPERFEKEEEAQK----LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDMK 474
Cdd:cd20621 333 GYIYNHFNPKYFENPDEFNPERWLNQNNIEDnpfvFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIEIIPNPKLKLI 412
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
129-462 7.13e-27

cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP734As function as multisubstrate and multifunctional enzymes in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis. Arabidopsis thaliana CYP734A1/BAS1 (formerly CYP72B1) inactivates bioactive brassinosteroids such as castasterone (CS) and brassinolide (BL) by C-26 hydroxylation. Rice CYP734As can catalyze C-22 hydroxylation as well as second and third oxidations to produce aldehyde and carboxylate groups at C-26. CYP734 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 112.54  E-value: 7.13e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 129 GDHWRNLRRLCTiEIFSTHRLNCFLYVRTDEVRRLISRLSRLAGTKKTV-VELKPMLMDLTFNNIMRMMTGKRYygeett 207
Cdd:cd20639  66 GEKWAHHRRVIT-PAFHMENLKRLVPHVVKSVADMLDKWEAMAEAGGEGeVDVAEWFQNLTEDVISRTAFGSSY------ 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 208 deEEAKRVRKLVADVGANTSSGNAVDYVPILRLFSSYENR-VKKLGEETDKFLQGLIDDKRGQQETGTTMID--HLLVLQ 284
Cdd:cd20639 139 --EDGKAVFRLQAQQMLLAAEAFRKVYIPGYRFLPTKKNRkSWRLDKEIRKSLLKLIERRQTAADDEKDDEDskDLLGLM 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 285 ksdIEYYTDQIIKGIILIMVI--------AGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPY 356
Cdd:cd20639 217 ---ISAKNARNGEKMTVEEIIeecktfffAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKT 293
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 357 LKNIVLETLRLHPATPLLVpHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTW-DDPDSFKPERFE--KEEEAQKLLA- 432
Cdd:cd20639 294 LGMILNETLRLYPPAVATI-RRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFAdgVARAAKHPLAf 372
                       330       340       350
                ....*....|....*....|....*....|..
gi 30692923 433 --FGLGRRACPGSGLAQRIVGLALGSLIQCFE 462
Cdd:cd20639 373 ipFGLGPRTCVGQNLAILEAKLTLAVILQRFE 404
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
128-462 3.75e-26

cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is composed of cytochrome P450 monooxygenases that are part of gene clusters involved in the biosynthesis of various compounds such as mycotoxins and alkaloids, including Aspergillus fumigatus gliotoxin biosynthesis protein (GliC), Penicillium rubens roquefortine/meleagrin synthesis protein R (RoqR), Aspergillus oryzae aspirochlorine biosynthesis protein C (AclC), Aspergillus terreus bimodular acetylaranotin synthesis protein ataTC, Kluyveromyces lactis pulcherrimin biosynthesis cluster protein 2 (PUL2), and Aspergillus nidulans aspyridones biosynthesis protein B (ApdB). The GliC-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 110.07  E-value: 3.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 128 YGDHWRNLRRLCtiEIFSTHR--LNcFLYVRTDEVRRLISRLSRLAGTKKT-VVELKPMLMDLTFnnimrMMTGKRYYGE 204
Cdd:cd20615  56 SGTDWKRVRKVF--DPAFSHSaaVY-YIPQFSREARKWVQNLPTNSGDGRRfVIDPAQALKFLPF-----RVIAEILYGE 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 205 ETTDEEEA-KRVRKLVADVGANTSSGNAVDYvPILRLF-SSYENRVKKLGEETDKFLQGLIDDKRGQQETgtTMIDHLLV 282
Cdd:cd20615 128 LSPEEKEElWDLAPLREELFKYVIKGGLYRF-KISRYLpTAANRRLREFQTRWRAFNLKIYNRARQRGQS--TPIVKLYE 204
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 283 -LQKSDI--EYYTDQIIKgiiliMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEI-DNRVGLDRLIEEADLSELPYLK 358
Cdd:cd20615 205 aVEKGDItfEELLQTLDE-----MLFANLDVTTGVLSWNLVFLAANPAVQEKLREEIsAAREQSGYPMEDYILSTDTLLA 279
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 359 NIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAI-HRDPNTWDDPDSFKPERFEKEEEAQ---KLLAFG 434
Cdd:cd20615 280 YCVLESLRLRPLLAFSVPESSPTDKIIGGYRIPANTPVVVDTYALnINNPFWGPDGEAYRPERFLGISPTDlryNFWRFG 359
                       330       340
                ....*....|....*....|....*...
gi 30692923 435 LGRRACPGSGLAQRIVGLALGSLIQCFE 462
Cdd:cd20615 360 FGPRKCLGQHVADVILKALLAHLLEQYE 387
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
294-462 6.09e-26

cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; Cytochrome p450 27B1 (CYP27B1) is also called calcidiol 1-monooxygenase (EC 1.14.15.18), 25-hydroxyvitamin D(3) 1-alpha-hydroxylase (VD3 1A hydroxylase), 25-hydroxyvitamin D-1 alpha hydroxylase, 25-OHD-1 alpha-hydroxylase, 25-hydroxycholecalciferol 1-hydroxylase, or 25-hydroxycholecalciferol 1-monooxygenase. It catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3 or calcitriol), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). It is also active with 25-hydroxy-24-oxo-vitamin D3, and has an important role in normal bone growth, calcium metabolism, and tissue differentiation. CYP27B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 109.84  E-value: 6.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 294 QIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPL 373
Cdd:cd20648 233 KSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPG 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 374 LVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQKLLA---FGLGRRACPGSGLAQRIV 450
Cdd:cd20648 313 NARVIPDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGDTHHPYAslpFGFGKRSCIGRRIAELEV 392
                       170
                ....*....|..
gi 30692923 451 GLALGSLIQCFE 462
Cdd:cd20648 393 YLALARILTHFE 404
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
292-486 1.22e-25

cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome P450 family 7, subfamily B, polypeptide 1, cytochrome P450 family 8, subfamily A, polypeptide 1; This family is composed of cytochrome P450s (CYPs) with similarity to the human P450s CYP7A1, CYP7B1, CYP8B1, CYP39A1 and prostacyclin synthase (CYP8A1). CYP7A1, CYP7B1, CYP8B1, and CYP39A1 are involved in the catabolism of cholesterol to bile acids (BAs) in two major pathways. CYP7A1 (cholesterol 7alpha-hydroxylase) and CYP8B1 (sterol 12-alpha-hydroxylase) function in the classic (or neutral) pathway, which leads to two bile acids: cholic acid (CA) and chenodeoxycholic acid (CDCA). CYP7B1 and CYP39A1 are 7-alpha-hydroxylases involved in the alternative (or acidic) pathway, which leads mainly to the formation of CDCA. Prostacyclin synthase (CYP8A1) catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 108.99  E-value: 1.22e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 292 TDQIIKGIILIMVIAG-TNTSAVTLeWALSNLLNHPDVISKARDEIDNRVGLDR-----LIEEADLSELPYLKNIVLETL 365
Cdd:cd11040 220 SEEDIARAELALLWAInANTIPAAF-WLLAHILSDPELLERIREEIEPAVTPDSgtnaiLDLTDLLTSCPLLDSTYLETL 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 366 RLH--PATPLLVPhmasEDC-KIGSYDMPRGTTLLVNAWAIHRDPNTW-DDPDSFKPERFEKEEEAQK-------LLAFG 434
Cdd:cd11040 299 RLHssSTSVRLVT----EDTvLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKKgrglpgaFRPFG 374
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 30692923 435 LGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDMkEGVGNTVPKAIP 486
Cdd:cd11040 375 GGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWKV-PGMDESPGLGIL 425
PLN02302 PLN02302
ent-kaurenoic acid oxidase
1-466 1.24e-25

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 109.80  E-value: 1.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923    1 MEETNIRVVLYSIFSLIFLIISF--KF--------LKPKKQNLPPSPPGWlPIIGH----LRLLKP--PihrtlRSFSET 64
Cdd:PLN02302   1 MELGSIWVWLAAIVAGVFVLKWVlrRVnswlyepkLGEGQPPLPPGDLGW-PVIGNmwsfLRAFKSsnP-----DSFIAS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   65 LDH--NDGGGVMSLRLGSRLVYVVSShkvaaEECfgknDVVLANRPQVIIG------KHVGYNNtnMIAAPYGDHWRnLR 136
Cdd:PLN02302  75 FISryGRTGIYKAFMFGQPTVLVTTP-----EAC----KRVLTDDDAFEPGwpestvELIGRKS--FVGITGEEHKR-LR 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  137 RLCTIEIFSTHRLNCFLYVRTDEVRRLISRLSrlagTKKTVVELKPMLMdLTFNNIMRMmtgkrYYGEETTDEEEAkrVR 216
Cdd:PLN02302 143 RLTAAPVNGPEALSTYIPYIEENVKSCLEKWS----KMGEIEFLTELRK-LTFKIIMYI-----FLSSESELVMEA--LE 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  217 KLVADVGANTSSgnavdyVPILRLFSSYeNRVKKLGEETDKFLQGLIDDKRGQQET-----GTTMIDHLLVLQKSDIEYY 291
Cdd:PLN02302 211 REYTTLNYGVRA------MAINLPGFAY-HRALKARKKLVALFQSIVDERRNSRKQnisprKKDMLDLLLDAEDENGRKL 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  292 TDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDE----IDNRVGLDRLIEEADLSELPYLKNIVLETLRL 367
Cdd:PLN02302 284 DDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEqeeiAKKRPPGQKGLTLKDVRKMEYLSQVIDETLRL 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  368 HPATPlLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE-EAQKLLAFGLGRRACPGSGLA 446
Cdd:PLN02302 364 INISL-TVFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTpKAGTFLPFGLGSRLCPGNDLA 442
                        490       500
                 ....*....|....*....|
gi 30692923  447 QRIVGLALGSLIQCFEWERV 466
Cdd:PLN02302 443 KLEISIFLHHFLLGYRLERL 462
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
120-476 1.70e-25

cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus nidulans cytochrome P450 59 (CYP59), also called sterigmatocystin biosynthesis P450 monooxygenase stcS, and similar fungal proteins. CYP59 is required for the conversion of versicolorin A to sterigmatocystin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410674 [Multi-domain]  Cd Length: 403  Bit Score: 108.11  E-value: 1.70e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 120 NTNMIAAPyGDHWRNLRRlctieIFS--------THRLNCFLyvrtDEVRRLISRLSRLAGTKKtVVELKPMLMDLTFNN 191
Cdd:cd11051  46 GSSLISME-GEEWKRLRK-----RFNpgfspqhlMTLVPTIL----DEVEIFAAILRELAESGE-VFSLEELTTNLTFDV 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 192 IMRMMTGKRYyGEETTDEEEAKRVRKLVADVGantSSGNAVDYVPILRLFssyenRVKKLGEETDKFLQGLIDDKRGQQE 271
Cdd:cd11051 115 IGRVTLDIDL-HAQTGDNSLLTALRLLLALYR---SLLNPFKRLNPLRPL-----RRWRNGRRLDRYLKPEVRKRFELER 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 272 TgttmidhllvlqksdieyyTDQIiKGIIlimvIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLD-----RLI 346
Cdd:cd11051 186 A-------------------IDQI-KTFL----FAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDpsaaaELL 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 347 EEAD--LSELPYLKNIVLETLRLHPatPLLVPHMASEDCKI-----GSYDMPrGTTLLVNAWAIHRDPNTWDDPDSFKPE 419
Cdd:cd11051 242 REGPelLNQLPYTTAVIKETLRLFP--PAGTARRGPPGVGLtdrdgKEYPTD-GCIVYVCHHAIHRDPEYWPRPDEFIPE 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30692923 420 RFEKEEEAQKL------LAFGLGRRACPGSGLAQ---RIVgLALgsLIQCFEWERvGNVEVDMKEG 476
Cdd:cd11051 319 RWLVDEGHELYppksawRPFERGPRNCIGQELAMlelKII-LAM--TVRRFDFEK-AYDEWDAKGG 380
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
71-461 2.04e-25

cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is expressed during development of the gastrointestinal tract, is silenced after birth in the intestine and colon by epigenetic modifications, but is activated following demethylation in colorectal cancer (CRC). Its expression levels in CRC correlate with the degree of malignancy, are higher in metastases and are predictive of survival. Thus, it is an attractive tumor-specific diagnostic and therapeutic target. CYP2W1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 108.35  E-value: 2.04e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVAAEECFGKNDVvLANRPQVIIGKHVGYNNTNMIAApyGDHWRNLRRLCtieIFSTHRLN 150
Cdd:cd20671   2 GPVFTIHLGMQKTVVLTGYEAVKEALVGTGDE-FADRPPIPIFQAIQHGNGVFFSS--GERWRTTRRFT---VRSMKSLG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 151 CFLYVRTD----EVRRLISRLSRLAGTKKTVVELKPMLMDLTFNnimrMMTGKRY-YGEETTdeeeaKRVRKLVADVGAN 225
Cdd:cd20671  76 MGKRTIEDkileELQFLNGQIDSFNGKPFPLRLLGWAPTNITFA----MLFGRRFdYKDPTF-----VSLLDLIDEVMVL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 226 TSSgnavdyvPILRLFSSY---------ENRVKKLGEETDKFLQGLIDDKRGQQETG--TTMIDHLLVLQKSDIEYYT-- 292
Cdd:cd20671 147 LGS-------PGLQLFNLYpvlgaflklHKPILDKVEEVCMILRTLIEARRPTIDGNplHSYIEALIQKQEEDDPKETlf 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 293 -DQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPAT 371
Cdd:cd20671 220 hDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLL 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 372 PlLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE----EAQKLLAFGLGRRACPGSGLAQ 447
Cdd:cd20671 300 P-HVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEgkfvKKEAFLPFSAGRRVCVGESLAR 378
                       410
                ....*....|....
gi 30692923 448 RIVGLALGSLIQCF 461
Cdd:cd20671 379 TELFIFFTGLLQKF 392
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
265-473 1.17e-24

cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; Cytochrome P450 24A1 (CYP24A1, EC 1.14.15.16) is also called 1,25-dihydroxyvitamin D(3) 24-hydroxylase (24-OHase), vitamin D(3) 24-hydroxylase, or cytochrome P450-CC24. It catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3) or 1,25(OH)2D3). CYP24A1 regulates vitamin D activity through its hydroxylation of calcitriol, the physiologically active vitamin D hormone, which controls gene-expression and signal-transduction processes associated with calcium homeostasis, cellular growth, and the maintenance of heart, muscle, immune, and skin function. CYP24A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 106.04  E-value: 1.17e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 265 DKRGQQETGTTMIDHLlvlqkSDIeYYTDQIIK----GIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRV 340
Cdd:cd20645 198 DKRLQRYSQGPANDFL-----CDI-YHDNELSKkelyAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVL 271
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 341 GLDRLIEEADLSELPYLKNIVLETLRLHPATPlLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPER 420
Cdd:cd20645 272 PANQTPRAEDLKNMPYLKACLKESMRLTPSVP-FTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPER 350
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 30692923 421 FEKEEEAQKLLA---FGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDM 473
Cdd:cd20645 351 WLQEKHSINPFAhvpFGIGKRMCIGRRLAELQLQLALCWIIQKYQIVATDNEPVEM 406
PLN02290 PLN02290
cytokinin trans-hydroxylase
129-461 1.76e-24

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 106.44  E-value: 1.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  129 GDHWRNLRRLCTiEIFSTHRLNCFLYVRTDEVRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYygeettd 208
Cdd:PLN02290 149 GADWYHQRHIAA-PAFMGDRLKGYAGHMVECTKQMLQSLQKAVESGQTEVEIGEYMTRLTADIISRTEFDSSY------- 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  209 eEEAKRVRKLVADVGANTSSGNAVDYVPILRLFSSYENR-VKKLGEETDKFLQGLIDDKRGQQETG--TTMIDHLLVL-- 283
Cdd:PLN02290 221 -EKGKQIFHLLTVLQRLCAQATRHLCFPGSRFFPSKYNReIKSLKGEVERLLMEIIQSRRDCVEIGrsSSYGDDLLGMll 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  284 -----QKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIdNRVGLDRLIEEADLSELPYLK 358
Cdd:PLN02290 300 nemekKRSNGFNLNLQLIMDECKTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEV-AEVCGGETPSVDHLSKLTLLN 378
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  359 NIVLETLRLHPATPLLvPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTW-DDPDSFKPERFEKEEEA--QKLLAFGL 435
Cdd:PLN02290 379 MVINESLRLYPPATLL-PRMAFEDIKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFApgRHFIPFAA 457
                        330       340
                 ....*....|....*....|....*.
gi 30692923  436 GRRACPGSGLAQRIVGLALGSLIQCF 461
Cdd:PLN02290 458 GPRNCIGQAFAMMEAKIILAMLISKF 483
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
71-481 2.27e-24

cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a microsomal enzyme that is required for the activation of vitamin D; it catalyzes the initial step converting vitamin D into 25-hydroxyvitamin D (25(OH)D), the major circulating metabolite of vitamin D. The 1alpha-hydroxylation of 25(OH)D by CYP27B1 generates the fully active vitamin D metabolite, 1,25-dihydroxyvitamin D (1,25(OH)2D). Mutations in the CYP2R1 gene are associated with an atypical form of vitamin D-deficiency rickets, which has been classified as vitamin D dependent rickets type 1B. CYP2R1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 105.28  E-value: 2.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKvAAEECFGKNDVVLANRPQVIIGKHVgynnTNM---IAAPYGDHWRNLRRLCtieifsth 147
Cdd:cd20661  13 GQIFSLDLGGISTVVLNGYD-AVKECLVHQSEIFADRPSLPLFMKL----TNMgglLNSKYGRGWTEHRKLA-------- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 148 rLNCFLYVRTDEvRRLISRLSRLAGTKKTVVEL---KPMLMDLTFNNIMRMMTGKRYYGEETT--DEEEAKRVRKLVADV 222
Cdd:cd20661  80 -VNCFRYFGYGQ-KSFESKISEECKFFLDAIDTykgKPFDPKHLITNAVSNITNLIIFGERFTyeDTDFQHMIEIFSENV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 223 GANTSSG----NAVDYVPILRlFSSYEnRVKKLGEETDKFLQGLID---DKRGQQETGTTMIDHLLVLQKSDIEYYTDQI 295
Cdd:cd20661 158 ELAASAWvflyNAFPWIGILP-FGKHQ-QLFRNAAEVYDFLLRLIErfsENRKPQSPRHFIDAYLDEMDQNKNDPESTFS 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 296 IKGIILI---MVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATP 372
Cdd:cd20661 236 MENLIFSvgeLIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVP 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 373 LLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE----EAQKLLAFGLGRRACPGSGLAQR 448
Cdd:cd20661 316 LGIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNgqfaKKEAFVPFSLGRRHCLGEQLARM 395
                       410       420       430
                ....*....|....*....|....*....|...
gi 30692923 449 IVGLALGSLIQCFEWERVGNVEVDMKEGVGNTV 481
Cdd:cd20661 396 EMFLFFTALLQRFHLHFPHGLIPDLKPKLGMTL 428
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
71-482 2.99e-24

cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of rats and rabbits and may have important functions for the olfactory chemosensory system. It is involved in the metabolism of sex steroids and xenobiotic compounds. In cynomolgus monkeys, CYP2G2 is a functional drug-metabolizing enzyme in nasal mucosa. In humans, two different CYP2G genes, CYP2GP1 and CYP2GP2, are pseudogenes because of loss-of-function deletions/mutations. The CYP2G subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 105.01  E-value: 2.99e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  71 GGVMSLRLGSRLVYVVSSHKVA-------AEECFGKNDVVLANRpqviigKHVGYNntnmIAAPYGDHWRNLRR--LCTI 141
Cdd:cd20670   2 GPVFTVYMGPRPVVVLCGHEAVkealvdqADEFSGRGELATIER------NFQGHG----VALANGERWRILRRfsLTIL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 142 EIFSTHRLNCFLYVRtDEVRRLISRLSRlagTKKTVVELKPMLMDLTFNNIMRMMTGKRYygeettdEEEAKRVRKLV-- 219
Cdd:cd20670  72 RNFGMGKRSIEERIQ-EEAGYLLEEFRK---TKGAPIDPTFFLSRTVSNVISSVVFGSRF-------DYEDKQFLSLLrm 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 220 ---ADVGANTSSGNAVD-YVPILRLFSSYENRVKKLGEETDKFLQGLIDDKRGQQETGT--TMIDHLLV-LQKSDIEYYT 292
Cdd:cd20670 141 ineSFIEMSTPWAQLYDmYSGIMQYLPGRHNRIYYLIEELKDFIASRVKINEASLDPQNprDFIDCFLIkMHQDKNNPHT 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 293 DQIIKGIILI---MVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHP 369
Cdd:cd20670 221 EFNLKNLVLTtlnLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTD 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 370 ATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE----EAQKLLAFGLGRRACPGSGL 445
Cdd:cd20670 301 IVPLGVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQgrfkKNEAFVPFSSGKRVCLGEAM 380
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 30692923 446 AQRIVGLALGSLIQCFEWERV---GNVEVDMK-EGVGNTVP 482
Cdd:cd20670 381 ARMELFLYFTSILQNFSLRSLvppADIDITPKiSGFGNIPP 421
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
163-464 9.77e-24

cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Characterized members, among others, include: Catharanthus roseus cytochrome P450 72A1 (CYP72A1), also called secologanin synthase (EC 1.3.3.9), that catalyzes the conversion of loganin into secologanin, the precursor of monoterpenoid indole alkaloids and ipecac alkaloids; Medicago truncatula CYP72A67 that catalyzes a key oxidative step in hemolytic sapogenin biosynthesis; and Arabidopsis thaliana CYP72C1, an atypical CYP that acts on brassinolide precursors and functions as a brassinosteroid-inactivating enzyme. This family also includes Panax ginseng CYP716A47 that catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis. CYP72 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 103.51  E-value: 9.77e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 163 LISRLSRLAGTKKTV-VELKPMLMDLTFNNIMRMMTGKRYygeettdeEEAKRVRKLVADVGANTSSGNAVDYVPILRLF 241
Cdd:cd20642  97 MISKWEKLVSSKGSCeLDVWPELQNLTSDVISRTAFGSSY--------EEGKKIFELQKEQGELIIQALRKVYIPGWRFL 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 242 SSYEN-RVKKLGEETDKFLQGLIDDKRGQQETGTTMIDHLL-VLQKSDIEYYTDQIIKGIILIM--VI--------AGTN 309
Cdd:cd20642 169 PTKRNrRMKEIEKEIRSSLRGIINKREKAMKAGEATNDDLLgILLESNHKEIKEQGNKNGGMSTedVIeecklfyfAGQE 248
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 310 TSAVTLEWALSNLLNHPDVISKARDEIDNRVGlDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHmASEDCKIGSYD 389
Cdd:cd20642 249 TTSVLLVWTMVLLSQHPDWQERAREEVLQVFG-NNKPDFEGLNHLKVVTMILYEVLRLYPPVIQLTRA-IHKDTKLGDLT 326
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 390 MPRGTTLLVNAWAIHRDPNTW-DDPDSFKPERF-EKEEEAQK----LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEW 463
Cdd:cd20642 327 LPAGVQVSLPILLVHRDPELWgDDAKEFNPERFaEGISKATKgqvsYFPFGWGPRICIGQNFALLEAKMALALILQRFSF 406

                .
gi 30692923 464 E 464
Cdd:cd20642 407 E 407
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
256-454 1.23e-23

cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins including Sinorhizobium fredii CYPBJ-4 homolog. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 102.91  E-value: 1.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 256 DKFLQGLIDDKRGQQETgTTMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDE 335
Cdd:cd20614 170 DARLSQLVATARANGAR-TGLVAALIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDE 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 336 IDNRVGLDRliEEADLSELPYLKNIVLETLRLHPATPLlVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDS 415
Cdd:cd20614 249 AAAAGDVPR--TPAELRRFPLAEALFRETLRLHPPVPF-VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDR 325
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 30692923 416 FKPERFEKEEEAQK---LLAFGLGRRACPGSGLA-----QRIVGLAL 454
Cdd:cd20614 326 FRPERWLGRDRAPNpveLLQFGGGPHFCLGYHVAcvelvQFIVALAR 372
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
317-442 1.55e-23

cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also called 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) or oxysterol 7-alpha-hydroxylase. It is involved in the metabolism of bile acids and has a preference for 24-hydroxycholesterol, converting it into the 7-alpha-hydroxylated product. It may play a role in the alternative bile acid synthesis pathway in the liver. CYP39A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410728  Cd Length: 410  Bit Score: 102.39  E-value: 1.55e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 317 WALSNLLNHPDVISKARDEIDNRVGLDRL----IEEADLSELPYLKNIVLETLRLHPatPLLVPHMASEDCKIGSYDMPR 392
Cdd:cd20635 232 WTLAFILSHPSVYKKVMEEISSVLGKAGKdkikISEDDLKKMPYIKRCVLEAIRLRS--PGAITRKVVKPIKIKNYTIPA 309
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30692923 393 GTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE-EAQKLL----AFGLGRRACPG 442
Cdd:cd20635 310 GDMLMLSPYWAHRNPKYFPDPELFKPERWKKADlEKNVFLegfvAFGGGRYQCPG 364
PLN02936 PLN02936
epsilon-ring hydroxylase
300-476 2.55e-23

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 102.95  E-value: 2.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  300 ILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDnRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMA 379
Cdd:PLN02936 283 LLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELD-RVLQGRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQ 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  380 SEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKE----EEAQ---KLLAFGLGRRACPGSGLA--QRIV 450
Cdd:PLN02936 362 VEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDgpvpNETNtdfRYIPFSGGPRKCVGDQFAllEAIV 441
                        170       180
                 ....*....|....*....|....*.
gi 30692923  451 GLALgsLIQCFEWERVGNVEVDMKEG 476
Cdd:PLN02936 442 ALAV--LLQRLDLELVPDQDIVMTTG 465
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
129-447 4.59e-23

cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 (CYP4V2) is the most characterized member of the CYP4V subfamily. It is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410773 [Multi-domain]  Cd Length: 440  Bit Score: 101.38  E-value: 4.59e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 129 GDHWRNLRRLCTiEIFSTHRLNCFLYVRTDEVRRLISRLSRLAGTkktvvELKPMLMDLTF---NNIMRMMTGKRYYGEE 205
Cdd:cd20680  65 GEKWRSRRKMLT-PTFHFTILSDFLEVMNEQSNILVEKLEKHVDG-----EAFNCFFDITLcalDIICETAMGKKIGAQS 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 206 TTDEEEAKRVRK-------------LVADVGANTSsGNAVDYVPILRLFSSYEN-----RVKKLGEETDKflqglIDDKR 267
Cdd:cd20680 139 NKDSEYVQAVYRmsdiiqrrqkmpwLWLDLWYLMF-KEGKEHNKNLKILHTFTDnviaeRAEEMKAEEDK-----TGDSD 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 268 GQQETGT---TMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVG-LD 343
Cdd:cd20680 213 GESPSKKkrkAFLDMLLSVTDEEGNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGkSD 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 344 RLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMaSEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEK 423
Cdd:cd20680 293 RPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSL-CEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFP 371
                       330       340
                ....*....|....*....|....*...
gi 30692923 424 EEEAQK----LLAFGLGRRACPGSGLAQ 447
Cdd:cd20680 372 ENSSGRhpyaYIPFSAGPRNCIGQRFAL 399
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
277-462 7.24e-23

cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group includes CYP2C, and similar CYPs including mammalian CYP2E1, also called 4-nitrophenol 2-hydroxylase, as well as chicken CYP2H1 and CYP2H2. The CYP2C subfamily is composed of four human members (CYP2C8, CYP2C9, CYP2C18, CYP2C19) that metabolize approximately 20% of clinically used drugs, and all four exhibit genetic polymorphisms that results in toxicity or altered efficacy of some drugs in affected individuals. CYP2E1 participates in the metabolism of endogenous substrates, including acetone and fatty acids, and exogenous compounds such as anesthetics, ethanol, nicotine, acetaminophen, aspartame, and chlorzoxazone, among others. The CYP2C-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 100.80  E-value: 7.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 277 IDHLLVL--QKSDIE--YYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLS 352
Cdd:cd20665 204 IDCFLIKmeQEKHNQqsEFTLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRS 283
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 353 ELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK--- 429
Cdd:cd20665 284 HMPYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKksd 363
                       170       180       190
                ....*....|....*....|....*....|....
gi 30692923 430 -LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFE 462
Cdd:cd20665 364 yFMPFSAGKRICAGEGLARMELFLFLTTILQNFN 397
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
292-474 1.30e-22

cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; Cytochrome P450 5A1 (CYP5A1), also called thromboxane-A synthase (EC 5.3.99.5) or thromboxane synthetase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid that has been implicated in stroke, asthma, and various cardiovascular diseases, due to its acute and chronic effects in promoting platelet aggregation, vasoconstriction, bronchoconstriction, and proliferation. CYP5A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 100.30  E-value: 1.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 292 TDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPAT 371
Cdd:cd20649 258 TEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPA 337
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 372 pLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK----LLAFGLGRRACPGSGLAQ 447
Cdd:cd20649 338 -FRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRhpfvYLPFGAGPRSCIGMRLAL 416
                       170       180
                ....*....|....*....|....*..
gi 30692923 448 RIVGLALGSLIQCFEWERVGNVEVDMK 474
Cdd:cd20649 417 LEIKVTLLHILRRFRFQACPETEIPLQ 443
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
257-462 1.58e-22

cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; Cytochrome P450 27A1 (CYP27A1, EC 1.14.15.15) is also called CYP27, cholestanetriol 26-monooxygenase, sterol 26-hydroxylase, 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase, cytochrome P-450C27/25, sterol 27-hydroxylase, or vitamin D(3) 25-hydroxylase. It catalyzes the first step in the oxidation of the side chain of sterol intermediates, the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, and the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. It also hydroxylates vitamin D3 at the 25-position, as well as cholesterol at positions 24 and 25. CYP27A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 99.73  E-value: 1.58e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 257 KFLQGLIDDK---------RGQQETGTTMIdHLLVLQK-SDIEYYtdqiikGIILIMVIAGTNTSAVTLEWALSNLLNHP 326
Cdd:cd20646 192 SFGKKLIDKKmeeieervdRGEPVEGEYLT-YLLSSGKlSPKEVY------GSLTELLLAGVDTTSNTLSWALYHLARDP 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 327 DVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRD 406
Cdd:cd20646 265 EIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIVEKEVVVGDYLFPKNTLFHLCHYAVSHD 344
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 407 PNTWDDPDSFKPERFEKEEEAQK----LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFE 462
Cdd:cd20646 345 ETNFPEPERFKPERWLRDGGLKHhpfgSIPFGYGVRACVGRRIAELEMYLALSRLIKRFE 404
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
253-458 4.99e-22

cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1.14.15.13), also called pulcherriminic acid synthase or cyclo-L-leucyl-L-leucyl dipeptide oxidase or cytochrome P450 CYPX, catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms the red pigment pulcherrimin via a non-enzymatic spontaneous reaction with Fe(3+). It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 97.54  E-value: 4.99e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 253 EETDKFLQGLIDDKRgqQETGTTMIDHLLVLQKSDIEYyTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVIska 332
Cdd:cd11080 154 EQLSQYLLPVIEERR--VNPGSDLISILCTAEYEGEAL-SDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQL--- 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 333 rdeidNRVGLDRLIEEADLSElpylknivleTLRLHPatPL-LVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWD 411
Cdd:cd11080 228 -----AAVRADRSLVPRAIAE----------TLRYHP--PVqLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFE 290
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 30692923 412 DPDSFKPERFEKEEE-----AQKLLAFGLGRRACPGSGLAQRIVGLALGSLI 458
Cdd:cd11080 291 DPDTFNIHREDLGIRsafsgAADHLAFGSGRHFCVGAALAKREIEIVANQVL 342
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
257-462 1.24e-21

cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3,4-desaturase; Cytochrome P450 27C1 (CYP27C1) is also called all-trans retinol 3,4-desaturase. It catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-didehydroretinal). CYP27C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410740 [Multi-domain]  Cd Length: 433  Bit Score: 97.30  E-value: 1.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 257 KFLQGLIDDK---------RGQQETGTtMIDHLLVLQKSDIEYYTDQIIKgiiliMVIAGTNTSAVTLEWALSNLLNHPD 327
Cdd:cd20647 196 KFSQIHVDNRlreiqkqmdRGEEVKGG-LLTYLLVSKELTLEEIYANMTE-----MLLAGVDTTSFTLSWATYLLARHPE 269
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 328 VISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPlLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDP 407
Cdd:cd20647 270 VQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLP-GNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDE 348
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 408 NTWDDPDSFKPERFEKEEEAQKL-----LAFGLGRRACPGSGLAQRIVGLALGSLIQCFE 462
Cdd:cd20647 349 ENFPRAEEFRPERWLRKDALDRVdnfgsIPFGYGIRSCIGRRIAELEIHLALIQLLQNFE 408
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
129-474 1.27e-21

cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain cleavage enzyme; Cytochrome P450 11A1 (CYP11A1, EC 1.14.15.6) is also called cholesterol side-chain cleavage enzyme, cholesterol desmolase, or cytochrome P450(scc). It catalyzes the side-chain cleavage reaction of cholesterol to form pregnenolone, the precursor of all steroid hormones. Missense or nonsense mutations of the CYP11A1 gene cause mild to severe early-onset adrenal failure depending on the severity of the enzyme dysfunction/deficiency. CYP11A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 97.09  E-value: 1.27e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 129 GDHWRNLRRLCTIEIFSTHRLNCFL----YVRTDEVRRLISRLSRlAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYYGE 204
Cdd:cd20643  63 GEAWRKDRLILNKEVLAPKVIDNFVpllnEVSQDFVSRLHKRIKK-SGSGKWTADLSNDLFRFALESICNVLYGERLGLL 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 205 ETTDEEEAKRVRKLVADVGANTSsgnAVDYVP--ILRLFSS--YENRVKK---LGEETDKFLQGLIDDKRGQQETG---T 274
Cdd:cd20643 142 QDYVNPEAQRFIDAITLMFHTTS---PMLYIPpdLLRLINTkiWRDHVEAwdvIFNHADKCIQNIYRDLRQKGKNEheyP 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 275 TMIDHLLVLQKSDIEYytdqiIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRvgldRLIEEADLSEL 354
Cdd:cd20643 219 GILANLLLQDKLPIED-----IKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAA----RQEAQGDMVKM 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 355 ----PYLKNIVLETLRLHPATPLLVPHMaSEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF-EKEEEAQK 429
Cdd:cd20643 290 lksvPLLKAAIKETLRLHPVAVSLQRYI-TEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWlSKDITHFR 368
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 30692923 430 LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDMK 474
Cdd:cd20643 369 NLGFGFGPRQCLGRRIAETEMQLFLIHMLENFKIETQRLVEVKTT 413
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
306-446 1.78e-21

cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP714 enzymes are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels. They contribute to the production of diverse GA compounds through various oxidations of C and D rings in both monocots and eudicots. CYP714B1 and CYP714B2 encode the enzyme GA 13-oxidase, which is required for GA1 biosynthesis, while CYP714D1 encodes GA 16a,17-epoxidase, which inactivates the non-13-hydroxy GAs in rice. Arabidopsis CYP714A1 is an inactivation enzyme that catalyzes the conversion of GA12 to 16-carboxylated GA12 (16-carboxy-16beta,17-dihydro GA12). CYP714 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 96.71  E-value: 1.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 306 AGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGlDRLIEEADLSELPYLKNIVLETLRLHPATPLlVPHMASEDCKI 385
Cdd:cd20640 241 AGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCK-GGPPDADSLSRMKTVTMVIQETLRLYPPAAF-VSREALRDMKL 318
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30692923 386 GSYDMPRGTTLLVNAWAIHRDPNTWD-DPDSFKPERFEK-----EEEAQKLLAFGLGRRACPGSGLA 446
Cdd:cd20640 319 GGLVVPKGVNIWVPVSTLHLDPEIWGpDANEFNPERFSNgvaaaCKPPHSYMPFGAGARTCLGQNFA 385
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
240-446 2.02e-21

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 96.27  E-value: 2.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 240 LFSSYENRVKKLGEETDKflqgLIDDKRGQQETGTTMIDHL-----LVLQKSDIEYyTDQIIKGIILIMVIAGTNTSAVT 314
Cdd:cd20616 169 LYKKYEKAVKDLKDAIEI----LIEQKRRRISTAEKLEDHMdfateLIFAQKRGEL-TAENVNQCVLEMLIAAPDTMSVS 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 315 LEWALSNLLNHPDVISKARDEIDNRVGlDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHmASEDCKIGSYDMPRGT 394
Cdd:cd20616 244 LFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRK-ALEDDVIDGYPVKKGT 321
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 30692923 395 TLLVNAWAIHRDPnTWDDPDSFKPERFEKEEEAQKLLAFGLGRRACPGSGLA 446
Cdd:cd20616 322 NIILNIGRMHRLE-FFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIA 372
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
302-464 3.24e-21

cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 95.73  E-value: 3.24e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 302 IMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPL----LVPH 377
Cdd:cd11058 224 LLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQLPYLNAVIQEALRLYPPVPAglprVVPA 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 378 MASEDCkiGSYdMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK-------LLAFGLGRRACPGSGLAQRIV 450
Cdd:cd11058 304 GGATID--GQF-VPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFdndkkeaFQPFSVGPRNCIGKNLAYAEM 380
                       170
                ....*....|....
gi 30692923 451 GLALGSLIQCFEWE 464
Cdd:cd11058 381 RLILAKLLWNFDLE 394
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
235-483 6.70e-21

fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 monooxygenase TRI13, also called core trichothecene cluster (CTC) protein 13, and similar proteins. The tri13 gene is located in the trichothecene biosynthesis gene cluster in Fusarium species, which produce a great diversity of agriculturally important trichothecene toxins that differ from each other in their pattern of oxygenation and esterification. Trichothecenes comprise a large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including the T2-toxin; TRI13 is required for the addition of the C-4 oxygen of T-2 toxin. The TRI13-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 95.44  E-value: 6.70e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 235 VPILRLF-SSYENRVKKLGEETDKFLQGLID------DKRGQQETGTTMIDHLLVLQKS-------DIEYYTdQIIKGII 300
Cdd:cd20622 189 FPKLSHWfYRNQPSYRRAAKIKDDFLQREIQaiarslERKGDEGEVRSAVDHMVRRELAaaekegrKPDYYS-QVIHDEL 267
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 301 LIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDN----RVGLDRL--IEEADLSELPYLKNIVLETLRLHPATPLL 374
Cdd:cd20622 268 FGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSahpeAVAEGRLptAQEIAQARIPYLDAVIEEILRCANTAPIL 347
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 375 VpHMASEDCKIGSYDMPRGTTLLVNAW---------------------AIHRDPNTWD--DPDSFKPERF--EKEEEAQK 429
Cdd:cd20622 348 S-REATVDTQVLGYSIPKGTNVFLLNNgpsylsppieidesrrssssaAKGKKAGVWDskDIADFDPERWlvTDEETGET 426
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30692923 430 --------LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDMKEGVGNT-VPK 483
Cdd:cd20622 427 vfdpsagpTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPLPEALSGYEAIDGLTrMPK 489
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
310-466 1.06e-20

C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 710; C-22 sterol desaturase (EC 1.14.19.41), also called sterol 22-desaturase, is required for the formation of the C-22 double bond in the sterol side chain of delta22-unsaturated sterols, which are present specifically in fungi and plants. This enzyme is also called cytochrome P450 61 (CYP61) in fungi and cytochrome P450 710 (CYP710) in plants. The CYP61/CYP710 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 94.24  E-value: 1.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 310 TSAVTleWALSNLLNHPDVISKARDEIDN-RVGLDRLIEEADLSELPYLKNIVLETLRLHPATPlLVPHMASEDCKIG-S 387
Cdd:cd11082 237 TSSLV--WALQLLADHPDVLAKVREEQARlRPNDEPPLTLDLLEEMKYTRQVVKEVLRYRPPAP-MVPHIAKKDFPLTeD 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 388 YDMPRGTTLLVNAWAIHRDPNTwdDPDSFKPERF-----EKEEEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFE 462
Cdd:cd11082 314 YTVPKGTIVIPSIYDSCFQGFP--EPDKFDPDRFsperqEDRKYKKNFLVFGAGPHQCVGQEYAINHLMLFLALFSTLVD 391

                ....
gi 30692923 463 WERV 466
Cdd:cd11082 392 WKRH 395
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
287-463 3.67e-20

putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of Mycobacterium tuberculosis putative cytochrome P450 136 (CYP136) and similar proteins. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 92.38  E-value: 3.67e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 287 DIEYYTDQ-IIKGIILIMvIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDnRVGLDRLIEEaDLSELPYLKNIVLETL 365
Cdd:cd11045 203 DGDRFSDDdIVNHMIFLM-MAAHDTTTSTLTSMAYFLARHPEWQERLREESL-ALGKGTLDYE-DLGQLEVTDWVFKEAL 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 366 RLHPATPLLvPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQKL-----LAFGLGRRAC 440
Cdd:cd11045 280 RLVPPVPTL-PRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVhryawAPFGGGAHKC 358
                       170       180
                ....*....|....*....|...
gi 30692923 441 PGSGLAQRIVGLALGSLIQCFEW 463
Cdd:cd11045 359 IGLHFAGMEVKAILHQMLRRFRW 381
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
277-482 4.59e-20

cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) consists of only one functional member CYP2B6, which shows broad substrate specificity and plays a key role in the metabolism of many clinical drugs, environmental toxins, and endogenous compounds. Rodents have multiple functional CYP2B proteins; mouse subfamily members include CYP2B9, 2B10, 2B13, 2B19, and 2B23. CYP2B enzymes are highly inducible by chemicals that interact with the constitutive androstane receptor (CAR) and/or pregnane X receptor (PXR), such as rifampicin and phenobarbital. The CYP2B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 92.53  E-value: 4.59e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 277 ID-HLLVLQKSDIEYYTD---QIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLS 352
Cdd:cd20672 204 IDtYLLRMEKEKSNHHTEfhhQNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRA 283
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 353 ELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTL-LVNAWAIHrDPNTWDDPDSFKPERFEKEEEAQK-- 429
Cdd:cd20672 284 KMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTLFRGYLLPKNTEVyPILSSALH-DPQYFEQPDTFNPDHFLDANGALKks 362
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30692923 430 --LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWER-VGNVEVDM--KE-GVGNTVP 482
Cdd:cd20672 363 eaFMPFSTGKRICLGEGIARNELFLFFTTILQNFSVASpVAPEDIDLtpKEsGVGKIPP 421
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
129-446 6.72e-20

cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Arabidopsis thaliana CYP709B3 is involved in abscisic acid (ABA) and salt stress response. CYP709 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 92.13  E-value: 6.72e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 129 GDHWRNLRRLCTiEIFSTHRLNCFLYVRTDEVRRLISRL---SRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRYygee 205
Cdd:cd20641  66 GDDWVRHRRVLN-PAFSMDKLKSMTQVMADCTERMFQEWrkqRNNSETERIEVEVSREFQDLTADIIATTAFGSSY---- 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 206 ttdeEEAKRVRKLVADVGANTSSGNAVDYVPILRLFSSYEN-RVKKLGEETDKFLQGLIDdKRGQQET---GTTMIDHLL 281
Cdd:cd20641 141 ----AEGIEVFLSQLELQKCAAASLTNLYIPGTQYLPTPRNlRVWKLEKKVRNSIKRIID-SRLTSEGkgyGDDLLGLML 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 282 VLQKSDIEYYTDQIIKGIILIM------VIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELP 355
Cdd:cd20641 216 EAASSNEGGRRTERKMSIDEIIdecktfFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLK 295
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 356 YLKNIVLETLRLHPATPLLVpHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTW-DDPDSFKPERFEK-----EEEAQK 429
Cdd:cd20641 296 LMNMVLMETLRLYGPVINIA-RRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANgvsraATHPNA 374
                       330
                ....*....|....*..
gi 30692923 430 LLAFGLGRRACPGSGLA 446
Cdd:cd20641 375 LLSFSLGPRACIGQNFA 391
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
260-454 2.35e-19

cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4F subfamily show diverse specificities among its members: CYP4F2 and CYP4F3 metabolize pro- and anti-inflammatory leukotrienes; CYP4F8 and CYP4F12 metabolize prostaglandins, endoperoxides and arachidonic acid; CYP4F11 and CYP4F12 metabolize VLFA and are unique in the CYP4F subfamily since they also hydroxylate xenobiotics such as benzphetamine, ethylmorphine, erythromycin, and ebastine. CYP4F belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 90.52  E-value: 2.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 260 QGlIDDKRGQQETGTTM--IDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEID 337
Cdd:cd20679 208 QG-VDDFLKAKAKSKTLdfIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQ 286
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 338 NRVGlDRLIEEA---DLSELPYLKNIVLETLRLHPATPLLVPHmASEDCKI-GSYDMPRGTTLLVNAWAIHRDPNTWDDP 413
Cdd:cd20679 287 ELLK-DREPEEIewdDLAQLPFLTMCIKESLRLHPPVTAISRC-CTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDP 364
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 30692923 414 DSFKPERFEKEEEAQK----LLAFGLGRRACPGS--GLAQRIVGLAL 454
Cdd:cd20679 365 EVYDPFRFDPENSQGRsplaFIPFSAGPRNCIGQtfAMAEMKVVLAL 411
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
259-472 4.02e-19

cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is a heme-containing monooxygenase which participates in epothilone biosynthesis where it catalyzes the epoxidation of epothilones C and D into epothilones A and B, respectively. This subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 89.02  E-value: 4.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 259 LQGLIDDKRgqQETGTTMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDn 338
Cdd:cd20630 169 IEEVIAERR--QAPVEDDLLTTLLRAEEDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEPE- 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 339 rvgldrlieeadlselpYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKP 418
Cdd:cd20630 246 -----------------LLRNALEEVLRWDNFGKMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDV 308
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30692923 419 ERfekeeEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCF-EWERVGNVEVD 472
Cdd:cd20630 309 RR-----DPNANIAFGYGPHFCIGAALARLELELAVSTLLRRFpEMELAEPPVFD 358
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
288-464 8.65e-19

cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The function of CYP2AB1 is unknown. CYP2AB1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 88.36  E-value: 8.65e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 288 IEYYTDQIIKGI---------------ILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLS 352
Cdd:cd20667 203 IDCYLAQITKTKddpvstfseenmiqvVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRK 282
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 353 ELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE----EAQ 428
Cdd:cd20667 283 RLPYTNAVIHEVQRLSNVVSVGAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDgnfvMNE 362
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 30692923 429 KLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWE 464
Cdd:cd20667 363 AFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQ 398
PLN02774 PLN02774
brassinosteroid-6-oxidase
256-471 3.03e-18

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 87.14  E-value: 3.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  256 DKFLQGLIDDKRGQQETGTTMIDHLLVLQKSDIEYYTDQIIKGIILIMViAGTNTSAVTLEWALSNLLNHPDVISKARDE 335
Cdd:PLN02774 226 VRMLRQLIQERRASGETHTDMLGYLMRKEGNRYKLTDEEIIDQIITILY-SGYETVSTTSMMAVKYLHDHPKALQELRKE 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  336 ---IDNRVGLDRLIEEADLSELPYLKNIVLETLRLhpATPLL-VPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWD 411
Cdd:PLN02774 305 hlaIRERKRPEDPIDWNDYKSMRFTRAVIFETSRL--ATIVNgVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYP 382
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30692923  412 DPDSFKPERF-EKEEEAQK-LLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEV 471
Cdd:PLN02774 383 DPMTFNPWRWlDKSLESHNyFFLFGGGTRLCPGKELGIVEISTFLHYFVTRYRWEEVGGDKL 444
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
301-461 5.95e-18

cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes CYP2A1, 2A2, and 2A3 in rats; CYP2A4, 2A5, 2A12, 2A20p, 2A21p, 2A22, and 2A23p in mice; CYP2A6, 2A7, 2A13, 2A18P in humans; CYP2A8, 2A9, 2A14, 2A15, 2A16, and 2A17 in hamsters; CYP2A10 and 2A11 in rabbits; and CYP2A19 in pigs. CYP2A enzymes metabolize numerous xenobiotic compounds, including coumarin, aflatoxin B1, nicotine, cotinine, 1,3-butadiene, and acetaminophen, among others, as well as endogenous compounds, including testosterone, progesterone, and other steroid hormones. Human CYP2A6 is responsible for the systemic clearance of nicotine, while CYP2A13 activates the nicotine-derived procarcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) into DNA-altering compounds that cause lung cancer. The CYP2A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 86.00  E-value: 5.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 301 LIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVPHMAS 380
Cdd:cd20668 232 LNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRVT 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 381 EDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK----LLAFGLGRRACPGSGLAQRIVGLALGS 456
Cdd:cd20668 312 KDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKksdaFVPFSIGKRYCFGEGLARMELFLFFTT 391

                ....*
gi 30692923 457 LIQCF 461
Cdd:cd20668 392 IMQNF 396
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
129-471 6.03e-18

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 86.37  E-value: 6.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  129 GDHWRNLRRLCTIEiFSTHRLNCFLYVRTDEVR-RLISRLSRlAGTKKTVVELKPMLMDLTFNNIMrmmtgKRYYGEEtt 207
Cdd:PLN03195 120 GELWRKQRKTASFE-FASKNLRDFSTVVFREYSlKLSSILSQ-ASFANQVVDMQDLFMRMTLDSIC-----KVGFGVE-- 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  208 deeeakrVRKLVADVGAN--TSSGNAVDYVPILRLFSSY--ENRVKKLGEET---------DKFLQGLIDDKRGQQETGT 274
Cdd:PLN03195 191 -------IGTLSPSLPENpfAQAFDTANIIVTLRFIDPLwkLKKFLNIGSEAllsksikvvDDFTYSVIRRRKAEMDEAR 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  275 T--------MIDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDE----------- 335
Cdd:PLN03195 264 KsgkkvkhdILSRFIELGEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSElkalekerake 343
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  336 --IDNRVGLD-RLIEEAD------LSELPYLKNIVLETLRLHPATPLLVPHMASEDCkigsydMPRGTTL----LVN--A 400
Cdd:PLN03195 344 edPEDSQSFNqRVTQFAGlltydsLGKLQYLHAVITETLRLYPAVPQDPKGILEDDV------LPDGTKVkaggMVTyvP 417
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30692923  401 WAIHRDPNTW-DDPDSFKPERFEKEEEAQ-----KLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEV 471
Cdd:PLN03195 418 YSMGRMEYNWgPDAASFKPERWIKDGVFQnaspfKFTAFQAGPRICLGKDSAYLQMKMALALLCRFFKFQLVPGHPV 494
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
306-446 7.75e-17

cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, X, and Z; This group is composed of family 4 cytochrome P450s from subfamilies A (CYP4A), B (CYP4B), T (CYP4T), X (CYP4X), and Z (CYP4Z). The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B is conserved among vertebrates. CYP4As are known for catalyzing arachidonic acid to 20-HETE (20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoic acid), and some can also metabolize lauric and palmitic acid. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4X1 is expressed at high levels in the mammalian brain and may play a role in regulating fat metabolism. CYP4Z1 is a fatty acid hydroxylase that is unique among human CYPs in that it is predominantly expressed in the mammary gland. Monophyly was not found with the CYP4T and CYP4B subfamilies, and further consideration should be given to their nomenclature. The CYP4B-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 82.71  E-value: 7.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 306 AGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPAtpllVPHMASEDCK- 384
Cdd:cd20678 250 EGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPP----VPGISRELSKp 325
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30692923 385 IGSYD---MPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK----LLAFGLGRRACPGSGLA 446
Cdd:cd20678 326 VTFPDgrsLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRhshaFLPFSAGPRNCIGQQFA 394
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
1-467 1.10e-15

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 79.21  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923    1 MEETNIRVVLYSIFSLIFLIISFKFLK---PKKQNLPPSPPGWlpiighlrllkPPIHRTLRSFSEtlDHNDGGGVMSLR 77
Cdd:PLN02196   1 MDFSALFLTLFAGALFLCLLRFLAGFRrssSTKLPLPPGTMGW-----------PYVGETFQLYSQ--DPNVFFASKQKR 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   78 LGSRL--------VYVVSSHKVAAEECFGKNDVVLANRP---QVIIGKHVgynntnmIAAPYGDHWRNLRRLCtieifst 146
Cdd:PLN02196  68 YGSVFkthvlgcpCVMISSPEAAKFVLVTKSHLFKPTFPaskERMLGKQA-------IFFHQGDYHAKLRKLV------- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  147 hrLNCFLyvrTDEVRRLISRLSRLA--------GTK-KTVVELKpmlmDLTFNNIMRMMTGKryygEETTDEEEAKRVRK 217
Cdd:PLN02196 134 --LRAFM---PDAIRNMVPDIESIAqeslnsweGTQiNTYQEMK----TYTFNVALLSIFGK----DEVLYREDLKRCYY 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  218 LVaDVGANTssgnavdyVPIlRLFSSYENRVKKLGEETDKFLQGLIDDKRGQQETGTTMIDHLLvlqkSDIEYYTDQIIK 297
Cdd:PLN02196 201 IL-EKGYNS--------MPI-NLPGTLFHKSMKARKELAQILAKILSKRRQNGSSHNDLLGSFM----GDKEGLTDEQIA 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  298 GIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEidnRVGLDRLIEE------ADLSELPYLKNIVLETLRLhpAT 371
Cdd:PLN02196 267 DNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEE---QMAIRKDKEEgesltwEDTKKMPLTSRVIQETLRV--AS 341
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  372 PL-LVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQKLLAFGLGRRACPGSGLAQRIV 450
Cdd:PLN02196 342 ILsFTFREAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAPKPNTFMPFGNGTHSCPGNELAKLEI 421
                        490
                 ....*....|....*..
gi 30692923  451 GLALGSLIQCFEWERVG 467
Cdd:PLN02196 422 SVLIHHLTTKYRWSIVG 438
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
296-476 1.59e-15

cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes catalyze the final steps in the production of glucocorticoids and mineralocorticoids that takes place in the adrenal gland. There are two human CYP11B isoforms: Cyb11B1 (11-beta-hydroxylase or P45011beta), which catalyzes the final step of cortisol synthesis by a one-step reaction from 11-deoxycortisol; and CYP11B2 (aldosterone synthase or P450aldo), which catalyzes three steps in the synthesis of aldosterone. The CYP11B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 78.73  E-value: 1.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 296 IKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATpLLV 375
Cdd:cd20644 233 IKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVG-ITV 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 376 PHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQ---KLLAFGLGRRACPGSGLAQRIVGL 452
Cdd:cd20644 312 QRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGrnfKHLAFGFGMRQCLGRRLAEAEMLL 391
                       170       180
                ....*....|....*....|....
gi 30692923 453 ALGSLIQCFEWERVGNVEVDMKEG 476
Cdd:cd20644 392 LLMHVLKNFLVETLSQEDIKTVYS 415
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
235-463 1.78e-15

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 78.48  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  235 VPiLRLFSSYENRVKKLGEETDKFLQGLIDDKRGQQETGTTMI-DHLLVLQKSDiEYYTDQIIKGIILIMVIAGTNTSAV 313
Cdd:PLN02987 208 VP-LPLFSTTYRRAIQARTKVAEALTLVVMKRRKEEEEGAEKKkDMLAALLASD-DGFSDEEIVDFLVALLVAGYETTST 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  314 TLEWALSNLLNHPDVISKAR---DEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLLVpHMASEDCKIGSYDM 390
Cdd:PLN02987 286 IMTLAVKFLTETPLALAQLKeehEKIRAMKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIF-RRAMTDIEVKGYTI 364
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30692923  391 PRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEE----EAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEW 463
Cdd:PLN02987 365 PKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSgttvPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSW 441
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
171-485 1.89e-15

fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 78.90  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  171 AGTKKTVVELKPMLMDLTFNNIMRMMTGkryYGEETTDEEEAKRVRKLVADVGANTSSGNAVDYVPILRLFS----SYEN 246
Cdd:PLN02169 166 AAHENIIIDLQDVFMRFMFDTSSILMTG---YDPMSLSIEMLEVEFGEAADIGEEAIYYRHFKPVILWRLQNwigiGLER 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  247 RVKKLGEETDKFLQGLIDDKRGQQ----ETGTTMIDHLLVLQKSDIEYY------TDQIIKGIILIMVIAGTNTSAVTLE 316
Cdd:PLN02169 243 KMRTALATVNRMFAKIISSRRKEEisraETEPYSKDALTYYMNVDTSKYkllkpkKDKFIRDVIFSLVLAGRDTTSSALT 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  317 WALSNLLNHPDVISKARDEIDNRvgldrlIEEADLSELPYLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTL 396
Cdd:PLN02169 323 WFFWLLSKHPQVMAKIRHEINTK------FDNEDLEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLPSGHKVDAESKI 396
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  397 LVNAWAIHRDPNTW-DDPDSFKPERF------EKEEEAQKLLAFGLGRRACPGSGLA---QRIVGLAL-----GSLIQCF 461
Cdd:PLN02169 397 VICIYALGRMRSVWgEDALDFKPERWisdnggLRHEPSYKFMAFNSGPRTCLGKHLAllqMKIVALEIiknydFKVIEGH 476
                        330       340
                 ....*....|....*....|....
gi 30692923  462 EWERVGNVEVDMKEGVGNTVPKAI 485
Cdd:PLN02169 477 KIEAIPSILLRMKHGLKVTVTKKI 500
PLN02500 PLN02500
cytochrome P450 90B1
9-468 5.84e-15

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 77.21  E-value: 5.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923    9 VLYSIFS-LIFLIISFKFLKPKKQNLPPSPPGWlPIIGH-LRLLKPPIHRTLRSFSETLDHNDGGGVMSLRLGSRLVyvv 86
Cdd:PLN02500  14 LLPSILSlLLVFILTKRRPKQKRFNLPPGNMGW-PFLGEtIGYLKPYSATSIGEFMEQHISRYGKIYRSNLFGEPTI--- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923   87 sshkVAAEEcfGKNDVVLANRPQVI-------IGKHVGynNTNMIAApYGDHWRNLRRLcTIEIFSTHRLNCFLYVRTDE 159
Cdd:PLN02500  90 ----VSADA--GLNRFILQNEGRLFecsyprsIGGILG--KWSMLVL-VGDMHRDMRSI-SLNFLSHARLRTHLLKEVER 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  160 VRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKryygEETTD-EEEAKRVRKLVADVGAN---TSSGNAVDYV 235
Cdd:PLN02500 160 HTLLVLDSWKENSTFSAQDEAKKFTFNLMAKHIMSMDPGE----EETEQlKKEYVTFMKGVVSAPLNfpgTAYRKALKSR 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  236 PILRLF--SSYENRVKKLGEETDKFLQgliDDKRGqqetgttmidhlLVLQKSDIEyyTDQIIKgIILIMVIAGTNTSAV 313
Cdd:PLN02500 236 ATILKFieRKMEERIEKLKEEDESVEE---DDLLG------------WVLKHSNLS--TEQILD-LILSLLFAGHETSSV 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  314 TLEWALSNLLNHPDVISKARDE------IDNRVGLDRLIEEaDLSELPYLKNIVLETLRLHPATPLLvPHMASEDCKIGS 387
Cdd:PLN02500 298 AIALAIFFLQGCPKAVQELREEhleiarAKKQSGESELNWE-DYKKMEFTQCVINETLRLGNVVRFL-HRKALKDVRYKG 375
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  388 YDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKE-----------EEAQKLLAFGLGRRACPGSGLAQRIVGLALGS 456
Cdd:PLN02500 376 YDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNnnrggssgsssATTNNFMPFGGGPRLCAGSELAKLEMAVFIHH 455
                        490
                 ....*....|..
gi 30692923  457 LIQCFEWERVGN 468
Cdd:PLN02500 456 LVLNFNWELAEA 467
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
253-461 1.82e-14

cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 74.87  E-value: 1.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 253 EETDKFLQGLIDDKRgqQETGTTMIDHLLVLQKSDiEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKA 332
Cdd:cd11029 172 RELVDYLAELVARKR--AEPGDDLLSALVAARDEG-DRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALL 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 333 RDEidnRVGLDRLIEEadlselpylknivleTLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDD 412
Cdd:cd11029 249 RAD---PELWPAAVEE---------------LLRYDGPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPD 310
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 30692923 413 PDSFKPERfekeeEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCF 461
Cdd:cd11029 311 PDRLDITR-----DANGHLAFGHGIHYCLGAPLARLEAEIALGALLTRF 354
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
258-459 3.38e-14

cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces coelicolor CYP158A1 and CYP158A2, Streptomyces natalensis PimD (also known as CYP107E), Mycobacterium tuberculosis CYP121, and Micromonospora griseorubida MycG (also known as CYP107B). CYP158A1 and CYP158A2 catalyze an unusual oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments; CYP158A2 produces three isomers of biflaviolin and one triflaviolin while CYP158A1 produces only two isomers of biflaviolin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. CYP121 is essential for the viability of M. tuberculosis and is a novel drug target for the inhibition of mycobacterial growth. MycG catalyzes both hydroxylation and epoxidation reactions in the biosynthesis of the 16-membered ring macrolide antibiotic mycinamicin II. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 74.14  E-value: 3.38e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 258 FLQGLIDDKRgqQETGTTMIDHLLVLQKSDIEYyTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDViskardeid 337
Cdd:cd11031 172 YMAELVAARR--AEPGDDLLSALVAARDDDDRL-SEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQ--------- 239
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 338 nrvgLDRLIEEADLseLPylkNIVLETLRLHPATPL-LVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSF 416
Cdd:cd11031 240 ----LARLRADPEL--VP---AAVEELLRYIPLGAGgGFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRL 310
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30692923 417 KPERFEKeeeaqKLLAFGLGRRACPGSGLAQRIVGLALGSLIQ 459
Cdd:cd11031 311 DLDREPN-----PHLAFGHGPHHCLGAPLARLELQVALGALLR 348
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
252-454 4.67e-14

cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains bacterial cytochrome P450s, including those belonging to families 105 (CYP105) and 165 (CYP165). Also included in this group are fungal family 55 proteins (CYP55). CYP105s are predominantly found in bacteria belonging to the phylum Actinobacteria and the order Actinomycetales, and are associated with a wide variety of pathways and processes, from steroid biotransformation to production of macrolide metabolites. CYP105A1 catalyzes two sequential hydroxylations of vitamin D3 with differing specificity and cytochrome P450-SOY (also known as CYP105D1) has been shown to be capable of both oxidation and dealkylation reactions. CYP105D6 and CYP105P1, from the filipin biosynthetic pathway, perform highly regio- and stereospecific hydroxylations. Other members of this group include, but are not limited to: CYP165D3 (also called OxyE) from the teicoplanin biosynthetic gene cluster of Actinoplanes teichomyceticus, which is responsible for the phenolic coupling of the aromatic side chains of the first and third peptide residues in the teicoplanin peptide; Micromonospora griseorubida cytochrome P450 MycCI that catalyzes hydroxylation at the C21 methyl group of mycinamicin VIII, the earliest macrolide form in the postpolyketide synthase tailoring pathway; and Fusarium oxysporum CYP55A1 (also called nitric oxide reductase cytochrome P450nor) that catalyzes an unusual reaction, the direct electron transfer from NAD(P)H to bound heme. The CYP105-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 73.71  E-value: 4.67e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 252 GEETDKFLQGLIDDKRgqQETGTTMIDHLLVLQKSDIEYyTDQIIKGIILIMVIAGTNTSAVTLewALS--NLLNHPDVi 329
Cdd:cd11030 168 GAELRAYLDELVARKR--REPGDDLLSRLVAEHGAPGEL-TDEELVGIAVLLLVAGHETTANMI--ALGtlALLEHPEQ- 241
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 330 skardeidnrvgLDRLIEEADLselpyLKNIVLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNT 409
Cdd:cd11030 242 ------------LAALRADPSL-----VPGAVEELLRYLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAV 304
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30692923 410 WDDPDSFKPERfekeeEAQKLLAFGLGRRACPGSGLA------------QRIVGLAL 454
Cdd:cd11030 305 FPDPDRLDITR-----PARRHLAFGHGVHQCLGQNLArleleialptlfRRFPGLRL 356
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
333-442 1.16e-13

cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic conversions of fatty acid hydroperoxides to bioactive oxylipins in plants, some invertebrates, and bacteria. It includes two dehydrases, namely allene oxide synthase (AOS) and divinyl ether synthase (DES), and two isomerases, hydroperoxide lyase (HPL) and epoxyalcohol synthase (EAS). AOS (EC 4.2.1.92, also called hydroperoxide dehydratase), such as Arabidopsis thaliana CYP74A acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. DES (EC 4.2.1.121), also called colneleate synthase or CYP74D, catalyzes the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid. The linolenate HPL, Arabidopsis thaliana CYP74B2, is required for the synthesis of the green leaf volatiles (GLVs) hexanal and trans-2-hexenal. The fatty acid HPL, Solanum lycopersicum CYP74B, is involved in the biosynthesis of traumatin and C6 aldehydes. The epoxyalcohol synthase Ranunculus japonicus CYP74A88 (also known as RjEAS) specifically converts linoleic acid 9- and 13-hydroperoxides to oxiranyl carbinols 9,10-epoxy-11-hydroxy-12-octadecenoic acid and 11-hydroxy-12,13-epoxy-9-octadecenoic acid, respectively. The CYP74 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 72.68  E-value: 1.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 333 RDEIDNRVGLDRLIEEADLSELPYLKNIVLETLRLHPATPLlVPHMASEDCKI----GSYDMPRGTTLL-VNAWAiHRDP 407
Cdd:cd11071 264 AEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPL-QYGRARKDFVIeshdASYKIKKGELLVgYQPLA-TRDP 341
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 30692923 408 NTWDDPDSFKPERFEKEEEA-QKLLAFGLGR---------RACPG 442
Cdd:cd11071 342 KVFDNPDEFVPDRFMGEEGKlLKHLIWSNGPeteeptpdnKQCPG 386
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
252-459 1.17e-13

cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial CYPs similar to Agrobacterium tumefaciens plant-inducible cytochrome P450-pinF1, which is not essential for virulence but may be involved in the detoxification of plant protective agents at the site of wounding. The P450-pinF1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 72.33  E-value: 1.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 252 GEETDKFLqGLIDDKRGqqETGTTMIDHLLVLQKsDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISK 331
Cdd:cd20629 153 AELYDYVL-PLIAERRR--APGDDLISRLLRAEV-EGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLER 228
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 332 ARdeidnrvgldrlieeADLSELPYLkniVLETLRLHPATpLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWD 411
Cdd:cd20629 229 VR---------------RDRSLIPAA---IEEGLRWEPPV-ASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYP 289
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 30692923 412 DPDSFKPERfekeeEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQ 459
Cdd:cd20629 290 DPDVFDIDR-----KPKPHLVFGGGAHRCLGEHLARVELREALNALLD 332
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
98-464 1.40e-13

cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It effectively metabolizes all-trans retinoic acid (atRA), 9-cis-retinoic acid (9-cis-RA), 13-cis-retinoic acid, and 4-oxo-atRA with the highest intrinsic clearance toward 9-cis-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. Loss of function mutations in the CYP26C1 gene cause type IV focal facial dermal dysplasia (FFDD), a rare syndrome characterized by facial lesions resembling aplasia cutis. CYP26C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 72.56  E-value: 1.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  98 GKNDVVLANRPQ---VIIGKHVGYNNTnmiaapyGDHWRNLRRLCTiEIFSTHRLNCFLYVRTDEVRRLISRLSRLAGTk 174
Cdd:cd20636  50 GEHTLVSTQWPQstrILLGSNTLLNSV-------GELHRQRRKVLA-RVFSRAALESYLPRIQDVVRSEVRGWCRGPGP- 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 175 ktvVELKPMLMDLTFNNIMRMMTGKRYygEETTDEEEAKRVRKLVADVGAntssgnavdyVPILRLFSSYENRVKKLgEE 254
Cdd:cd20636 121 ---VAVYTAAKSLTFRIAVRILLGLRL--EEQQFTYLAKTFEQLVENLFS----------LPLDVPFSGLRKGIKAR-DI 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 255 TDKFLQGLIDDK--RGQQETGTTMIDHLLVLQKSDIEYYTDQIIK--GIILIMVIAGTNTSAVTLEWALsnLLNHPDVIS 330
Cdd:cd20636 185 LHEYMEKAIEEKlqRQQAAEYCDALDYMIHSARENGKELTMQELKesAVELIFAAFSTTASASTSLVLL--LLQHPSAIE 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 331 KARDEIDNRvGLDR-------LIEEADLSELPYLKNIVLETLRLHPatPLLVPH-MASEDCKIGSYDMPRGTTLLVN--- 399
Cdd:cd20636 263 KIRQELVSH-GLIDqcqccpgALSLEKLSRLRYLDCVVKEVLRLLP--PVSGGYrTALQTFELDGYQIPKGWSVMYSird 339
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30692923 400 ---AWAIHRDPNTWDdPDSFKPERFEKEEEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWE 464
Cdd:cd20636 340 theTAAVYQNPEGFD-PDRFGVEREESKSGRFNYIPFGGGVRSCIGKELAQVILKTLAVELVTTARWE 406
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
254-475 2.38e-13

cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes Mycobacterium tuberculosis cytochrome P450 130 (CYP130), Rhodococcus erythropolis CYP116, and similar bacterial proteins. CYP130 catalyzes the N-demethylation of dextromethorphan, and has also shown a natural propensity to bind primary arylamines. CYP116 is involved in the degradation of thiocarbamate herbicides. The CYP130-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 71.48  E-value: 2.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 254 ETDKFLQGLIDDKRGQQETGttMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDViskar 333
Cdd:cd11078 170 ELWAYFADLVAERRREPRDD--LISDLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQ----- 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 334 deidnrvgLDRLieEADLSELPylkNIVLETLRLHPAtpllVPHM---ASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTW 410
Cdd:cd11078 243 --------WRRL--RADPSLIP---NAVEETLRYDSP----VQGLrrtATRDVEIGGVTIPAGARVLLLFGSANRDERVF 305
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30692923 411 DDPDSFKPERfekeEEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEwervgNVEVDMKE 475
Cdd:cd11078 306 PDPDRFDIDR----PNARKHLTFGHGIHFCLGAALARMEARIALEELLRRLP-----GMRVPGQE 361
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
129-468 6.67e-13

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 70.88  E-value: 6.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  129 GDHWRNLRRLCTIEIFSTH-RLNCFLYVRTDEVRRLISRLSRLAGTKKT-VVELKPMLMDLTFNNIMRMMtgkryYGEET 206
Cdd:PLN02426 128 GDSWRFQRKMASLELGSVSiRSYAFEIVASEIESRLLPLLSSAADDGEGaVLDLQDVFRRFSFDNICKFS-----FGLDP 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  207 TDEEEAKRVRKLVA--DVGANTSSGNAVDYVPIL----RLFS-SYENRVKKLGEETDKFLQGLIDDKRgqqETGTTMIDH 279
Cdd:PLN02426 203 GCLELSLPISEFADafDTASKLSAERAMAASPLLwkikRLLNiGSERKLKEAIKLVDELAAEVIRQRR---KLGFSASKD 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  280 LLVLQKSDIEyyTDQIIKGIILIMVIAGTNT--SAVT-LEWALSNllnHPDVISKARDEIDNRVGLDR-LIEEADLSELP 355
Cdd:PLN02426 280 LLSRFMASIN--DDKYLRDIVVSFLLAGRDTvaSALTsFFWLLSK---HPEVASAIREEADRVMGPNQeAASFEEMKEMH 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  356 YLKNIVLETLRLHPATPLLVPHMASEDC-KIGSYdMPRGTTLLVNAWAIHRDPNTWD-DPDSFKPERFEKE-----EEAQ 428
Cdd:PLN02426 355 YLHAALYESMRLFPPVQFDSKFAAEDDVlPDGTF-VAKGTRVTYHPYAMGRMERIWGpDCLEFKPERWLKNgvfvpENPF 433
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 30692923  429 KLLAFGLGRRACPGSGLA---QRIVGLAlgsLIQCFEWERVGN 468
Cdd:PLN02426 434 KYPVFQAGLRVCLGKEMAlmeMKSVAVA---VVRRFDIEVVGR 473
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
258-463 8.60e-13

P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Pseudomonas putida P450cam and Cyp101 proteins from Novosphingobium aromaticivorans such as CYP101C1 and CYP101D2. P450cam catalyzes the hydroxylation of camphor in a process that involves two electron transfers from the iron-sulfur protein, putidaredoxin. CYP101D2 is capable of oxidizing camphor while CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives such as alpha- and beta-ionone and beta-damascone. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 69.54  E-value: 8.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 258 FLQGLIDDKRgqQETGTTMIDHLLvlqKSDIE--YYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDviskarde 335
Cdd:cd11035 156 YLTPLIAERR--ANPGDDLISAIL---NAEIDgrPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPE-------- 222
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 336 iDNRvgldRLIEEADLselpyLKNIVLETLRLHPatPLLVPHMASEDCKIGSYDMPRGTTLLVnAWAIH-RDPNTWDDPD 414
Cdd:cd11035 223 -DRR----RLREDPEL-----IPAAVEELLRRYP--LVNVARIVTRDVEFHGVQLKAGDMVLL-PLALAnRDPREFPDPD 289
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 30692923 415 SFKPERfekeeEAQKLLAFGLGRRACPGSGLAQRIVGLALGsliqcfEW 463
Cdd:cd11035 290 TVDFDR-----KPNRHLAFGAGPHRCLGSHLARLELRIALE------EW 327
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
209-488 1.17e-12

cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus P450 monooxygenase AurH which is uniquely capable of forming a homochiral tetrahydrofuran ring, a vital component of the polyketide antibiotic aureothin. AurH catalyzes an unprecedented tandem oxygenation process: first, it catalyzes an asymmetric hydroxylation of deoxyaureothin to yield (7R)-7-hydroxydeoxyaureothin as an intermediate; and second, it mediates another C-O bond formation that leads to O-heterocyclization. The AurH-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410664 [Multi-domain]  Cd Length: 382  Bit Score: 69.32  E-value: 1.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 209 EEEAKRVRKLVADVGANTSsgnavdyVPILRLFSSYENRVKKLGEetdkFLQGLIDDKRgqQETGTTMIDHLlVLQKSDI 288
Cdd:cd11038 142 EEDWPRVHRWSADLGLAFG-------LEVKDHLPRIEAAVEELYD----YADALIEARR--AEPGDDLISTL-VAAEQDG 207
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 289 EYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDnrvgldrLIEEAdlselpylkniVLETLRLH 368
Cdd:cd11038 208 DRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDQWRALREDPE-------LAPAA-----------VEEVLRWC 269
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 369 PATPLLVpHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTwddpdsFKPERFEKEEEAQKLLAFGLGRRACPGSGLAQR 448
Cdd:cd11038 270 PTTTWAT-REAVEDVEYNGVTIPAGTVVHLCSHAANRDPRV------FDADRFDITAKRAPHLGFGGGVHHCLGAFLARA 342
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 30692923 449 IVGLALGSLIQCFEWERVGNvEVDMKEGVGNTVPKAIPLK 488
Cdd:cd11038 343 ELAEALTVLARRLPTPAIAG-EPTWLPDSGNTGPATLPLR 381
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
266-446 3.29e-12

P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome P450cin (P450cin, also called CYP176A1) and similar proteins. P450cin is a bacterial P450 enzyme that catalyzes the enantiospecific hydroxylation of 1,8-cineole to (1R)-6beta-hydroxycineole; its natural reduction-oxidation partner is cindoxin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 67.75  E-value: 3.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 266 KRGQQETGTTMIDHLLvLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDViskardeidnrvgLDRL 345
Cdd:cd11034 162 AERRANPRDDLISRLI-EGEIDGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPED-------------RRRL 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 346 IEEADLselpyLKNIVLETLRLhpATPLL-VPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKe 424
Cdd:cd11034 228 IADPSL-----IPNAVEEFLRF--YSPVAgLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRTPN- 299
                       170       180
                ....*....|....*....|..
gi 30692923 425 eeaqKLLAFGLGRRACPGSGLA 446
Cdd:cd11034 300 ----RHLAFGSGVHRCLGSHLA 317
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
318-464 4.79e-12

unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 67.49  E-value: 4.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 318 ALSNLLNHPDVISKARDEIDNRVG-LDRlieeadlselPYLKNIVLETLRLHPATPLLVpHMASEDCKIGSYDMPRGTTL 396
Cdd:cd20624 214 ALALLAAHPEQAARAREEAAVPPGpLAR----------PYLRACVLDAVRLWPTTPAVL-RESTEDTVWGGRTVPAGTGF 282
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 397 LVNAWAIHRDPNTWDDPDSFKPERF--EKEEEAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEWE 464
Cdd:cd20624 283 LIFAPFFHRDDEALPFADRFVPEIWldGRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEID 352
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
254-474 1.43e-11

cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, polypeptide 1 (cytochrome P450 20A1 or CYP20A1) is expressed in human hippocampus and substantia nigra. In zebrafish, maternal transcript of CYP20A1 occurs in eggs, suggesting involvement in brain and early development. CYP20A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 65.99  E-value: 1.43e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 254 ETDKFLQGLIDDKRGQQETGTTMIDHLLvlQKSdieyYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKAR 333
Cdd:cd20627 167 EMESVLKKVIKERKGKNFSQHVFIDSLL--QGN----LSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLY 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 334 DEIDNRVGLDRLIEEaDLSELPYLKNIVLETLRLHPATPLlVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDP 413
Cdd:cd20627 241 KEVDQVLGKGPITLE-KIEQLRYCQQVLCETVRTAKLTPV-SARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLP 318
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30692923 414 DSFKPERFEKEEEAQKLLAFGL-GRRACPGSGLAQRIVGLALGSLIQCFEWERVGNVEVDMK 474
Cdd:cd20627 319 YRFDPDRFDDESVMKSFSLLGFsGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETK 380
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
317-446 1.46e-11

cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also called 25-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.29) or oxysterol 7-alpha-hydroxylase. It catalyzes the 7alpha-hydroxylation of both steroids and oxysterols, and is thus implicated in the metabolism of neurosteroids and bile acid synthesis, respectively. It participates in the alternative (or acidic) pathway of cholesterol catabolism and bile acid biosynthesis. It also mediates the formation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) from 25-hydroxycholesterol; 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor in lymphoid cells. CYP7B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410725  Cd Length: 438  Bit Score: 66.17  E-value: 1.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 317 WALSNLLNHPDVISKARDEIDNRVGL---------DRLIEEADLSELPYLKNIVLETLRLHPATplLVPHMASEDCKI-- 385
Cdd:cd20632 237 WAMYYLLRHPEALAAVRDEIDHVLQStgqelgpdfDIHLTREQLDSLVYLESAINESLRLSSAS--MNIRVVQEDFTLkl 314
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30692923 386 ---GSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERF-EKEEE-------AQKL----LAFGLGRRACPGSGLA 446
Cdd:cd20632 315 esdGSVNLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFvEDGKKkttfykrGQKLkyylMPFGSGSSKCPGRFFA 390
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
253-466 1.80e-11

cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of bacterial cytochrome P450s from multiple families, including Mycobacterium smegmatis CYP164A2, Streptomyces sp. CYP245A1, Bacillus subtilis CYP107H1, Micromonospora echinospora P450 oxidase Calo2, and putative P450s such as Xylella fastidiosa CYP133 and Mycobacterium tuberculosis CYP140. CYP107H1, also called cytochrome P450(BioI), catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. CYP245A1, also called cytochrome P450 StaP, catalyzes the intramolecular C-C bond formation and oxidative decarboxylation of chromopyrrolic acid (CPA) to form the indolocarbazole core, a key step in staurosporine biosynthesis. CalO2 is involved in calicheamicin biosynthesis. The CYP164-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 65.65  E-value: 1.80e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 253 EETDKFLQGLIDDKRGQqeTGTTMIDHLLVLQKSDiEYYTDQIIKGIILIMVIAGTNTSaVTLewaLSN----LLNHPDV 328
Cdd:cd20625 162 AELAAYFRDLIARRRAD--PGDDLISALVAAEEDG-DRLSEDELVANCILLLVAGHETT-VNL---IGNgllaLLRHPEQ 234
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 329 iskardeidnrvgLDRLIEEADLselpyLKNIVLETLRLHPATpLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPN 408
Cdd:cd20625 235 -------------LALLRADPEL-----IPAAVEELLRYDSPV-QLTARVALEDVEIGGQTIPAGDRVLLLLGAANRDPA 295
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30692923 409 TWDDPDSFKPERfekeeEAQKLLAFGLGRRACPGSGLAqRIVG-LALGSLIQCFEWERV 466
Cdd:cd20625 296 VFPDPDRFDITR-----APNRHLAFGAGIHFCLGAPLA-RLEAeIALRALLRRFPDLRL 348
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
244-488 2.38e-11

cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and bacterial CYPs including Saccharopolyspora erythraea P450 EryK, Saccharolobus solfataricus cytochrome P450 119 (CYP119), Picrophilus torridus CYP231A2, Bacillus subtilis CYP109, Streptomyces himastatinicus HmtT and HmtN, and Bacillus megaterium CYP106A2, among others. EryK, also called erythromycin C-12 hydroxylase, is active during the final steps of erythromycin A (ErA) biosynthesis. CYP106A2 catalyzes the hydroxylation of a variety of 3-oxo-delta(4)-steroids such as progesterone and deoxycorticosterone, mainly in the 15beta-position. It is also capable of hydroxylating a variety of terpenoids. HmtT and HmtN is involved in the post-tailoring of the cyclohexadepsipeptide backbone during the biosynthesis of the himastatin antibiotic. The EryK-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 65.31  E-value: 2.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 244 YENRVKKLGEETDKFLQGLIDDKRgqqetgTTMIDHL---LVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALS 320
Cdd:cd11032 150 EVEEMAEALRELNAYLLEHLEERR------RNPRDDLisrLVEAEVDGERLTDEEIVGFAILLLIAGHETTTNLLGNAVL 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 321 NLLNHPDVISKARdeidnrvgldrlieeADLSELPylkNIVLETLRLHPatPLLVPH-MASEDCKIGSYDMPRGTtlLVN 399
Cdd:cd11032 224 CLDEDPEVAARLR---------------ADPSLIP---GAIEEVLRYRP--PVQRTArVTTEDVELGGVTIPAGQ--LVI 281
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 400 AW--AIHRDPNTWDDPDSFKPERFEKeeeaqKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFE-WERVGNVEVDMKEG 476
Cdd:cd11032 282 AWlaSANRDERQFEDPDTFDIDRNPN-----PHLSFGHGIHFCLGAPLARLEARIALEALLDRFPrIRVDPDVPLELIDS 356
                       250
                ....*....|..
gi 30692923 477 VGNTVPKAIPLK 488
Cdd:cd11032 357 PVVFGVRSLPVR 368
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
257-463 2.80e-10

3-epi-6-deoxocathasterone 23-monooxygenase; Provisional


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 62.45  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  257 KFLQGLIDDKRGQQETGTTMI-----DHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISK 331
Cdd:PLN03141 208 KLVKKIIEEKRRAMKNKEEDEtgipkDVVDVLLRDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVALQQ 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  332 ARDEidnRVGLDRLIEE-------ADLSELPYLKNIVLETLRLHPATpLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIH 404
Cdd:PLN03141 288 LTEE---NMKLKRLKADtgeplywTDYMSLPFTQNVITETLRMGNII-NGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVH 363
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  405 RDPNTWDDPDSFKPERFEKEE-EAQKLLAFGLGRRACPGSGLAQRIVGLALGSLIQCFEW 463
Cdd:PLN03141 364 LDEENYDNPYQFNPWRWQEKDmNNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFRW 423
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
286-447 3.41e-10

C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; This family contains Gaeumannomyces graminis linoleate diol synthase (LDS) and similar proteins including Ssp1 from the phytopathogenic basidiomycete Ustilago maydis. LDS, also called linoleate (8R)-dioxygenase, catalyzes the dioxygenation of linoleic acid to (8R)-hydroperoxylinoleate and the isomerization of the resulting hydroperoxide to (7S,8S)-dihydroxylinoleate. Ssp1 is expressed in mature teliospores, which are produced by U. maydis only after infection of its host plant, maize. Ssp1 is localized on lipid bodies in germinating teliospores, suggesting a role in the mobilization of storage lipids. LDS and Ssp1 contain an N-terminal dioxygenase domain related to animal heme peroxidases, and a C-terminal cytochrome P450 domain. The LDS-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 61.59  E-value: 3.41e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 286 SDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDviSKARDEIdNRvgLDRLIEEADLSelpyLKNIVLETL 365
Cdd:cd20612 178 ALLDAAVADEVRDNVLGTAVGGVPTQSQAFAQILDFYLRRPG--AAHLAEI-QA--LARENDEADAT----LRGYVLEAL 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 366 RLHPATPLLVPHmASEDCKIGSYD-----MPRGTTLLVNAWAIHRDPNTWDDPDSFKPERfekeeEAQKLLAFGLGRRAC 440
Cdd:cd20612 249 RLNPIAPGLYRR-ATTDTTVADGGgrtvsIKAGDRVFVSLASAMRDPRAFPDPERFRLDR-----PLESYIHFGHGPHQC 322

                ....*..
gi 30692923 441 PGSGLAQ 447
Cdd:cd20612 323 LGEEIAR 329
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
361-457 9.61e-10

AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis proteins including anthracycline biosynthesis proteins DnrQ and AknT, and macrolide antibiotic biosynthesis proteins TylM3 and DesVIII. Streptomyces peucetius DnrQ is involved in the biosynthesis of carminomycin and daunorubicin (daunomycin) while Streptomyces galilaeus AknT functions in the biosynthesis of aclacinomycin A. Streptomyces fradiae TylM3 is involved in the biosynthesis of tylosin derived from the polyketide lactone tylactone, and Streptomyces venezuelae functions in the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin. These proteins are required for the glycosylation of specific substrates during the biosynthesis of specific anthracyclines and macrolide antibiotics. Although members of this family belong to the large cytochrome P450 (P450, CYP) superfamily and show significant similarity to cytochrome P450s, they lack heme-binding sites and are not functional cytochromes.


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 60.20  E-value: 9.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 361 VLETLRLHPatPL-LVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERfekeeEAQKLLAFGLGRRA 439
Cdd:cd11036 225 VAETLRYDP--PVrLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR-----PTARSAHFGLGRHA 297
                        90
                ....*....|....*...
gi 30692923 440 CPGSGLAQRIVGLALGSL 457
Cdd:cd11036 298 CLGAALARAAAAAALRAL 315
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
280-472 1.62e-09

cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces sp. P450sky (also called CYP163B3), Sphingopyxis macrogoltabida P450pyr hydroxylase, Novosphingobium aromaticivorans CYP108D1, Pseudomonas sp. cytochrome P450-Terp (P450terp), and Amycolatopsis balhimycina P450 OxyD, as well as several Mycobacterium proteins CYP124, CYP125, CYP126, and CYP142. P450sky is involved in the hydroxylation of three beta-hydroxylated amino acid precursors required for the biosynthesis of the cyclic depsipeptide skyllamycin. P450pyr hydroxylase is an active and selective catalyst for the regio- and stereo-selective hydroxylation at non-activated carbon atoms with a broad substrate range. P450terp catalyzes the hydroxylation of alpha-terpineol as part of its catabolic assimilation. OxyD is involved in beta-hydroxytyrosine formation during vancomycin biosynthesis. CYP124 is a methyl-branched lipid omega-hydroxylase while CYP142 is a cholesterol 27-oxidase with likely roles in host response modulation and cholesterol metabolism. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 59.46  E-value: 1.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 280 LLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDeidNRVGLDRLIEEAdlselpylkn 359
Cdd:cd11033 194 VLANAEVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLRA---DPSLLPTAVEEI---------- 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 360 ivletLRLhpATPllVPHM---ASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERfekeeEAQKLLAFGLG 436
Cdd:cd11033 261 -----LRW--ASP--VIHFrrtATRDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR-----SPNPHLAFGGG 326
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 30692923 437 RRACPGSGLAQRIVGLALGSLIqcfewERVGNVEVD 472
Cdd:cd11033 327 PHFCLGAHLARLELRVLFEELL-----DRVPDIELA 357
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
343-464 2.27e-09

cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The cytochrome P450 152 (CYP152) family enzymes act as peroxygenases, converting fatty acids through oxidative decarboxylation, yielding terminal alkenes, and via alpha- and beta-hydroxylation to yield hydroxy-fatty acids. Included in this family are Bacillus subtilis CYP152A1, also called cytochrome P450BsBeta, that catalyzes the alpha- and beta-hydroxylation of long-chain fatty acids such as myristic acid in the presence of hydrogen peroxide, and Sphingomonas paucimobilis CYP152B1, also called cytochrome P450(SPalpha), that hydroxylates fatty acids with high alpha-regioselectivity. The CYP152 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 59.08  E-value: 2.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 343 DRLIEEADlselPYLKNIVLETLRLHPATPLlVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFE 422
Cdd:cd11067 255 ERLRSGDE----DYAEAFVQEVRRFYPFFPF-VGARARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFL 329
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 30692923 423 -KEEEAQKLLAFGLGRRA----CPGSGLAQRIVGLALGSLIQCFEWE 464
Cdd:cd11067 330 gWEGDPFDFIPQGGGDHAtghrCPGEWITIALMKEALRLLARRDYYD 376
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
308-446 2.32e-09

cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also called 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase (EC 1.14.18.8) or sterol 12-alpha-hydroxylase. It is involved in the classic (or neutral) pathway of cholesterol catabolism and bile acid synthesis, and is responsible for sterol 12alpha-hydroxylation, which directs the synthesis to cholic acid (CA). It converts 7-alpha-hydroxy-4-cholesten-3-one into 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one, but also displays broad substrate specificity including other 7-alpha-hydroxylated C27 steroids. CYP8B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 59.30  E-value: 2.32e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 308 TNTSAVTLeWALSNLLNHPDVISKARDEIDN---------RVGLDRLIEEAD-LSELPYLKNIVLETLRLHPATPLLVPH 377
Cdd:cd20633 238 GNTGPASF-WLLLYLLKHPEAMKAVREEVEQvlketgqevKPGGPLINLTRDmLLKTPVLDSAVEETLRLTAAPVLIRAV 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 378 MASEDCKIGS---YDMPRGTTLLVNAW-AIHRDPNTWDDPDSFKPERFEKEEEAQK-------------LLAFGLGRRAC 440
Cdd:cd20633 317 VQDMTLKMANgreYALRKGDRLALFPYlAVQMDPEIHPEPHTFKYDRFLNPDGGKKkdfykngkklkyyNMPWGAGVSIC 396

                ....*.
gi 30692923 441 PGSGLA 446
Cdd:cd20633 397 PGRFFA 402
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
136-464 9.36e-09

cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is the main all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. CYP26A1 has been shown to upregulate fascin and promote the malignant behavior of breast carcinoma cells. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 57.52  E-value: 9.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 136 RRLCTIEIFSTHRLNCFLYVRTDEVRRLIsrlsRLAGTKKTVVELKPMLMDLTFNNIMRMMTGkryYGEETTDEEEAKRV 215
Cdd:cd20638  82 RKKVIMRAFSREALENYVPVIQEEVRSSV----NQWLQSGPCVLVYPEVKRLMFRIAMRILLG---FEPQQTDREQEQQL 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 216 RKLVADVGANTSSgnavdyVPILRLFSSYENRVK-------KLGEETDKFLQGLiDDKRGQQETGTTMIDHLlvlQKSDi 288
Cdd:cd20638 155 VEAFEEMIRNLFS------LPIDVPFSGLYRGLRarnlihaKIEENIRAKIQRE-DTEQQCKDALQLLIEHS---RRNG- 223
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 289 EYYTDQIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDRLIEEAD------LSELPYLKNIVL 362
Cdd:cd20638 224 EPLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKGLLSTKPNENKelsmevLEQLKYTGCVIK 303
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 363 ETLRLHPATPLLVpHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKE--EEAQKL--LAFGLGRR 438
Cdd:cd20638 304 ETLRLSPPVPGGF-RVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPlpEDSSRFsfIPFGGGSR 382
                       330       340
                ....*....|....*....|....*.
gi 30692923 439 ACPGSGLAQRIVGLALGSLIQCFEWE 464
Cdd:cd20638 383 SCVGKEFAKVLLKIFTVELARHCDWQ 408
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
253-450 3.35e-08

unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s, predominantly from bacteria. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 55.44  E-value: 3.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 253 EETDKFLQGLIDDKRGQQETGTTMIDHLLVLQKSDIEYYTDQIIKGIILIMVIAGTNTSAVTLewalSNLLNHpdvISKA 332
Cdd:cd11079 141 EEFDGIIRDLLADRRAAPRDADDDVTARLLRERVDGRPLTDEEIVSILRNWTVGELGTIAACV----GVLVHY---LARH 213
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 333 RDEidnrvgLDRLieEADLSELPylkNIVLETLRLHpaTPLLV-PHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWD 411
Cdd:cd11079 214 PEL------QARL--RANPALLP---AAIDEILRLD--DPFVAnRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFG 280
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 30692923 412 DPDSFKPERfekeeEAQKLLAFGLGRRACPGSGLAQ---RIV 450
Cdd:cd11079 281 DPDEFDPDR-----HAADNLVYGRGIHVCPGAPLARlelRIL 317
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
358-473 3.46e-08

cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a putative cytochrome P450 of unknown function. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410719  Cd Length: 381  Bit Score: 55.49  E-value: 3.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 358 KNIVLETLRLHPATPLL---VPHMASEDCKIGSYDMPrgttllvnawAIHRDPNTW-DDPDSFKPERFEKEEEAQKL--L 431
Cdd:cd20626 259 KNLVKEALRLYPPTRRIyraFQRPGSSKPEIIAADIE----------ACHRSESIWgPDALEFNPSRWSKLTPTQKEafL 328
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 30692923 432 AFGLGRRACPG-SGLAQRIVGLALGSLIQCF--EWERVGNVEVDM 473
Cdd:cd20626 329 PFGSGPFRCPAkPVFGPRMIALLVGALLDALgdEWELVSVDGRNV 373
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
122-456 7.57e-08

cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is an all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of similar metabolites as CYP26A1. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. In rats, CYP26B1 regulates sex-specific timing of meiotic initiation, independent of RA signaling. CYP26B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 54.47  E-value: 7.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 122 NMIAAPYGDHWRNLRRLCTiEIFSTHRLNCFLyvrtDEVRRLISRLSRLAGTKKTVVELKPMLMDLTFNNIMRMMTGKRy 201
Cdd:cd20637  69 NSLVNSIGDIHRHKRKVFS-KLFSHEALESYL----PKIQQVIQDTLRVWSSNPEPINVYQEAQKLTFRMAIRVLLGFR- 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 202 ygeetTDEEEAKRVRKLVADVGANTSSgnavdyVPILRLFSSYENRVKKLgEETDKFLQGLIDDKRgQQETGTTMIDHLL 281
Cdd:cd20637 143 -----VSEEELSHLFSVFQQFVENVFS------LPLDLPFSGYRRGIRAR-DSLQKSLEKAIREKL-QGTQGKDYADALD 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 282 VLQKSDIEYYTD---QIIKGIILIMVIAGTNTSAVTLEWALSNLLNHPDVISKARDEIDNRVGLDR--LIEEA----DLS 352
Cdd:cd20637 210 ILIESAKEHGKEltmQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELRSNGILHNgcLCEGTlrldTIS 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 353 ELPYLKNIVLETLRLHPatPLLVPH-MASEDCKIGSYDMPRGTTLLVNAWAIH------RDPNTWDdPDSFKPERFEKEE 425
Cdd:cd20637 290 SLKYLDCVIKEVLRLFT--PVSGGYrTALQTFELDGFQIPKGWSVLYSIRDTHdtapvfKDVDAFD-PDRFGQERSEDKD 366
                       330       340       350
                ....*....|....*....|....*....|....
gi 30692923 426 EAQKLLAFGLGRRACPGSGLAQ---RIVGLALGS 456
Cdd:cd20637 367 GRFHYLPFGGGVRTCLGKQLAKlflKVLAVELAS 400
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
303-462 1.85e-07

cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Rhodopseudomonas palustris CYP199A2 and CYP199A4. CYP199A2 catalyzes the oxidation of aromatic carboxylic acids including indole-2-carboxylic acid, 2-naphthoic acid and 4-ethylbenzoic acid. CYP199A4 catalyzes the hydroxylation of para-substituted benzoic acids. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 52.97  E-value: 1.85e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 303 MVIAGTNTSAVTLEWALSNLLNHPDviskardeidnrvGLDRLIEEADLselpyLKNIVLETLRLhpATPLLVPH-MASE 381
Cdd:cd11037 210 YLSAGLDTTISAIGNALWLLARHPD-------------QWERLRADPSL-----APNAFEEAVRL--ESPVQTFSrTTTR 269
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 382 DCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERfekeeEAQKLLAFGLGRRACPGSGLAQ---RIVGLALGSLI 458
Cdd:cd11037 270 DTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR-----NPSGHVGFGHGVHACVGQHLARlegEALLTALARRV 344

                ....
gi 30692923 459 QCFE 462
Cdd:cd11037 345 DRIE 348
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
309-446 2.05e-07

cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also called cholesterol 7-alpha-monooxygenase (EC 1.14.14.23) or cholesterol 7-alpha-hydroxylase. It catalyzes the hydroxylation at position 7 of cholesterol, a rate-limiting step in the classic (or neutral) pathway of cholesterol catabolism and bile acid biosynthesis. It is important for cholesterol homeostasis. CYP7A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 53.15  E-value: 2.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 309 NTSAVTLeWALSNLLNHPDVISKARDEIDN-------RVGLDR---LIEEADLSELPYLKNIVLETLRLHPATplLVPHM 378
Cdd:cd20631 242 NTLPATF-WSLFYLLRCPEAMKAATKEVKRtlektgqKVSDGGnpiVLTREQLDDMPVLGSIIKEALRLSSAS--LNIRV 318
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 379 ASEDCKI-----GSYDMPRGTTLLVNAWAIHRDPNTWDDPDSFKPERFEKEEEAQK-------------LLAFGLGRRAC 440
Cdd:cd20631 319 AKEDFTLhldsgESYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKttfykngrklkyyYMPFGSGTSKC 398

                ....*.
gi 30692923 441 PGSGLA 446
Cdd:cd20631 399 PGRFFA 404
PLN02648 PLN02648
allene oxide synthase
349-432 1.06e-06

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 51.09  E-value: 1.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923  349 ADLSELPYLKNIVLETLRLHPATPLLVPHmASEDCKIGSYD---------MPRGTTLLVNawaihRDPNTWDDPDSFKPE 419
Cdd:PLN02648 328 AALEKMPLVKSVVYEALRIEPPVPFQYGR-AREDFVIESHDaafeikkgeMLFGYQPLVT-----RDPKVFDRPEEFVPD 401
                         90
                 ....*....|...
gi 30692923  420 RFEKeEEAQKLLA 432
Cdd:PLN02648 402 RFMG-EEGEKLLK 413
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
341-450 4.68e-06

cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial metabolism of the military explosive, hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX). XplA has an unusual structural organization comprising a heme domain that is fused to its flavodoxin redox partner. XplA, along with its partner reductase XplB, are plasmid encoded and the xplA gene has now been found in divergent genera across the globe with near sequence identity. It has only been detected at explosive-contaminated sites, suggesting rapid dissemination of this novel catabolic activity, possibly within a 50-year period since the introduction of RDX into the environment. XplA belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 48.58  E-value: 4.68e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 341 GLDRLIEEADLSEL----PYLKN-IVLETLRLHPATPLLVPHmASEDCKIGSYDMPRGTTLLVNAWAIHRDPNTWDDPDS 415
Cdd:cd20619 213 GIELFARRPEVFTAfrndESARAaIINEMVRMDPPQLSFLRF-PTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDV 291
                        90       100       110
                ....*....|....*....|....*....|....*
gi 30692923 416 FKPERfekEEEAQKLLAFGLGRRACPGSGLAQRIV 450
Cdd:cd20619 292 FDHTR---PPAASRNLSFGLGPHSCAGQIISRAEA 323
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
317-442 2.39e-05

prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; Prostacyclin synthase, also called prostaglandin I2 synthase (PGIS) or cytochrome P450 8a1 (CYP8A1), catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 46.68  E-value: 2.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 317 WALSNLLNHPDVISKARDEIdNRVGLDR--------LIEEADLSELPYLKNIVLETLRLHPATplLVPHMASEDCKI--- 385
Cdd:cd20634 243 WLLLFLLKHPEAMAAVRGEI-QRIKHQRgqpvsqtlTINQELLDNTPVFDSVLSETLRLTAAP--FITREVLQDMKLrla 319
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30692923 386 --GSYDMPRGTTLLVNAW-AIHRDPNTWDDPDSFKPERFEKEEEAQKL-------------LAFGLGRRACPG 442
Cdd:cd20634 320 dgQEYNLRRGDRLCLFPFlSPQMDPEIHQEPEVFKYDRFLNADGTEKKdfykngkrlkyynMPWGAGDNVCIG 392
CYP_unk cd20623
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
361-457 2.22e-04

unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of uncharacterized cytochrome P450s. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410716 [Multi-domain]  Cd Length: 367  Bit Score: 43.41  E-value: 2.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30692923 361 VLETLRLHPATPLLVPHMASEDCKIGSYDMPRGTTLLVNAWAIHRDPntWDDPDSFKPErfeKEEEAQklLAFGLGRRAC 440
Cdd:cd20623 244 LNEVLWRDPPLANLAGRFAARDTELGGQWIRAGDLVVLGLAAANADP--RVRPDPGASM---SGNRAH--LAFGAGPHRC 316
                        90
                ....*....|....*..
gi 30692923 441 PGSGLAQRIVGLALGSL 457
Cdd:cd20623 317 PAQELAETIARTAVEVL 333
 
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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