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Conserved domains on  [gi|51247801|pdb|1U13|A]
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Chain A, Cytochrome P450 51

Protein Classification

cytochrome P450( domain architecture ID 15296390)

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

CATH:  1.10.630.10
Gene Ontology:  GO:0004497|GO:0005506|GO:0020037|GO:0016712
PubMed:  16042601|8637843|17023115|27267697|8405421|7678494|28124606
SCOP:  4001206

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 34-446 7.90e-179

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: 506.37  E-value: 7.90e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       34 RDELGDVGTFQLAGKQVVLLSGSHANEFFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEMLHN--AALRGEQMK 111
Cdd:cd11042   2 RKKYGDVFTFNLLGKKVTVLLGPEANEFFFNGKDEDLSAEEVYGFLTPPFGGGVVYYAPFAEQKEQLKFglNILRRGKLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      112 GHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDGRFAKLYHELERGTDPLAYVDPYLPIESF 191
Cdd:cd11042  82 GYVPLIVEEVEKYFAKWGESGEVDLFEEMSELTILTASRCLLGKEVRELLDDEFAQLYHDLDGGFTPIAFFFPPLPLPSF 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      192 RRRDEARNGLVALVADIMNGRIANPptDKSDRDMLDVLIAVKAETGTPrFSADEITGMFISMMFAGHHTSSGTASWTLIE 271
Cdd:cd11042 162 RRRDRARAKLKEIFSEIIQKRRKSP--DKDEDDMLQTLMDAKYKDGRP-LTDDEIAGLLIALLFAGQHTSSATSAWTGLE 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      272 LMRHRDAYAAVIDELDELYGD-GRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEV--QGHRIHEGDLVAAS 348
Cdd:cd11042 239 LLRNPEHLEALREEQKEVLGDgDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVegGGYVIPKGHIVLAS 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      349 PAISNRIPEDFPDPHDFVPARYEQPRQED-LLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPeSYR 427
Cdd:cd11042 319 PAVSHRDPEIFKNPDEFDPERFLKGRAEDsKGGKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSP-FPE 397

                       410
                ....*....|....*....
1U13_A      428 NDHSKMVVQLAQPAAVRYR 446
Cdd:cd11042 398 PDYTTMVVWPKGPARVRYK 416
 
Name Accession Description Interval E-value
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 34-446 7.90e-179

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: 506.37  E-value: 7.90e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       34 RDELGDVGTFQLAGKQVVLLSGSHANEFFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEMLHN--AALRGEQMK 111
Cdd:cd11042   2 RKKYGDVFTFNLLGKKVTVLLGPEANEFFFNGKDEDLSAEEVYGFLTPPFGGGVVYYAPFAEQKEQLKFglNILRRGKLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      112 GHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDGRFAKLYHELERGTDPLAYVDPYLPIESF 191
Cdd:cd11042  82 GYVPLIVEEVEKYFAKWGESGEVDLFEEMSELTILTASRCLLGKEVRELLDDEFAQLYHDLDGGFTPIAFFFPPLPLPSF 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      192 RRRDEARNGLVALVADIMNGRIANPptDKSDRDMLDVLIAVKAETGTPrFSADEITGMFISMMFAGHHTSSGTASWTLIE 271
Cdd:cd11042 162 RRRDRARAKLKEIFSEIIQKRRKSP--DKDEDDMLQTLMDAKYKDGRP-LTDDEIAGLLIALLFAGQHTSSATSAWTGLE 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      272 LMRHRDAYAAVIDELDELYGD-GRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEV--QGHRIHEGDLVAAS 348
Cdd:cd11042 239 LLRNPEHLEALREEQKEVLGDgDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVegGGYVIPKGHIVLAS 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      349 PAISNRIPEDFPDPHDFVPARYEQPRQED-LLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPeSYR 427
Cdd:cd11042 319 PAVSHRDPEIFKNPDEFDPERFLKGRAEDsKGGKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSP-FPE 397

                       410
                ....*....|....*....
1U13_A      428 NDHSKMVVQLAQPAAVRYR 446
Cdd:cd11042 398 PDYTTMVVWPKGPARVRYK 416
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 21-424 8.92e-67

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: 218.99  E-value: 8.92e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       21 EFRTDPIGLMQRVRDElGDVGTFQLAGKQVVLLSGSHANEFFFRAgDDDLDQAKAYPFMTP---IFGEGVVFDASPE-RR 96
Cdd:COG2124  16 AFLRDPYPFYARLREY-GPVFRVRLPGGGAWLVTRYEDVREVLRD-PRTFSSDGGLPEVLRplpLLGDSLLTLDGPEhTR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       97 KEMLHNAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGkkFRDQLDGRFAKLYHELERGT 176
Cdd:COG2124  94 LRRLVQPAFTPRRVAALRPRIREIADELLDRLAARGPVDLVEEFARPLPVIVICELLG--VPEEDRDRLRRWSDALLDAL 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      177 DPLayvdpylPIESFRRRDEARNGLVALVADIMNGRIANPPTDksdrdMLDVLIAvkAETGTPRFSADEITGMFISMMFA 256
Cdd:COG2124 172 GPL-------PPERRRRARRARAELDAYLRELIAERRAEPGDD-----LLSALLA--ARDDGERLSDEELRDELLLLLLA 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      257 GHHTSSGTASWTLIELMRHRDAYAAVIDELdelygdgrsvsfhalrqiPQLENVLKETLRLHPPLIILMRVAKGEFEVQG 336
Cdd:COG2124 238 GHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTATEDVELGG 299

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      337 HRIHEGDLVAASPAISNRIPEDFPDPHDFVPARyeqprqedllNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYE 416
Cdd:COG2124 300 VTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFP 369


                ....*....
1U13_A      417 -FEMAQPPE 424
Cdd:COG2124 370 dLRLAPPEE 378
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 17-441 3.22e-59

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: 200.97  E-value: 3.22e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A         17 GHLEEFRTDPI--GLMQRVRDELGDVGTFQLAGKQVVLLSGSHANEFFFRAGD----DDLDQAKAYPFMTPIFGEGVVFd 90
Cdd:pfam00067  11 GNLLQLGRKGNlhSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGeefsGRPDEPWFATSRGPFLGKGIVF- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A         91 ASPERRKEM--LHNAALRGEQMKGHAATIEDQVRRMIADW----GEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDGR 164
Cdd:pfam00067  90 ANGPRWRQLrrFLTPTFTSFGKLSFEPRVEEEARDLVEKLrktaGEPGVIDITDLLFRAALNVICSILFGERFGSLEDPK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        165 FAKL------YHELERGTDPLAY----VDPYLPIESFRRRDEARNGLVALVADIMNGRIAN-PPTDKSDRDMLDVLIAVK 233
Cdd:pfam00067 170 FLELvkavqeLSSLLSSPSPQLLdlfpILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETlDSAKKSPRDFLDALLLAK 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        234 AETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKE 313
Cdd:pfam00067 250 EEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKE 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        314 TLRLHPPLII-LMRVAKGEFEVQGHRIHEGDLVAASP-AISNRiPEDFPDPHDFVPARYEqPRQEDLLNRWTWIPFGAGR 391
Cdd:pfam00067 330 TLRLHPVVPLlLPREVTKDTVIPGYLIPKGTLVIVNLyALHRD-PEVFPNPEEFDPERFL-DENGKFRKSFAFLPFGAGP 407

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
1U13_A        392 HRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPESYRNDHSKMVVQLAQPA 441
Cdd:pfam00067 408 RNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPY 457
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 192-448 1.14e-30

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 124.15  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       192 RRRDEARNGLVAlvadimNGRIANPPTDKSDRDMLDVLIAVKAETGTP----RFSADEITGMFISMMFAGHHTSSGTASW 267
Cdd:PLN02687 246 RRFDAMMNGIIE------EHKAAGQTGSEEHKDLLSTLLALKREQQADgeggRITDTEIKALLLNLFTAGTDTTSSTVEW 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       268 TLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPL-IILMRVAKGEFEVQGHRIHEG-DLV 345
Cdd:PLN02687 320 AIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTpLSLPRMAAEECEINGYHIPKGaTLL 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       346 AASPAISnRIPEDFPDPHDFVPARY----EQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA- 420
Cdd:PLN02687 400 VNVWAIA-RDPEQWPDPLEFRPDRFlpggEHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELAd 478

                        250       260       270
                 ....*....|....*....|....*....|
1U13_A       421 -QPPESYRNDHS-KMVVQLAQPAAVRYRRR 448
Cdd:PLN02687 479 gQTPDKLNMEEAyGLTLQRAVPLMVHPRPR 508
 
Name Accession Description Interval E-value
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 34-446 7.90e-179

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: 506.37  E-value: 7.90e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       34 RDELGDVGTFQLAGKQVVLLSGSHANEFFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEMLHN--AALRGEQMK 111
Cdd:cd11042   2 RKKYGDVFTFNLLGKKVTVLLGPEANEFFFNGKDEDLSAEEVYGFLTPPFGGGVVYYAPFAEQKEQLKFglNILRRGKLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      112 GHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDGRFAKLYHELERGTDPLAYVDPYLPIESF 191
Cdd:cd11042  82 GYVPLIVEEVEKYFAKWGESGEVDLFEEMSELTILTASRCLLGKEVRELLDDEFAQLYHDLDGGFTPIAFFFPPLPLPSF 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      192 RRRDEARNGLVALVADIMNGRIANPptDKSDRDMLDVLIAVKAETGTPrFSADEITGMFISMMFAGHHTSSGTASWTLIE 271
Cdd:cd11042 162 RRRDRARAKLKEIFSEIIQKRRKSP--DKDEDDMLQTLMDAKYKDGRP-LTDDEIAGLLIALLFAGQHTSSATSAWTGLE 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      272 LMRHRDAYAAVIDELDELYGD-GRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEV--QGHRIHEGDLVAAS 348
Cdd:cd11042 239 LLRNPEHLEALREEQKEVLGDgDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVegGGYVIPKGHIVLAS 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      349 PAISNRIPEDFPDPHDFVPARYEQPRQED-LLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPeSYR 427
Cdd:cd11042 319 PAVSHRDPEIFKNPDEFDPERFLKGRAEDsKGGKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSP-FPE 397

                       410
                ....*....|....*....
1U13_A      428 NDHSKMVVQLAQPAAVRYR 446
Cdd:cd11042 398 PDYTTMVVWPKGPARVRYK 416
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 27-423 1.69e-67

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: 221.30  E-value: 1.69e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       27 IGLMQRVRDELGDVGTFQLAGK-QVVLLSGSHANEFFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPE----RRKEMLh 101
Cdd:cd11053   1 VGFLERLRARYGDVFTLRVPGLgPVVVLSDPEAIKQIFTADPDVLHPGEGNSLLEPLLGPNSLLLLDGDrhrrRRKLLM- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      102 nAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDgRFAKLYHELERGTDPLAY 181
Cdd:cd11053  80 -PAFHGERLRAYGELIAEITEREIDRWPPGQPFDLRELMQEITLEVILRVVFGVDDGERLQ-ELRRLLPRLLDLLSSPLA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      182 VDPYL--------PIESFRRRDEArngLVALVADIMNGRIANPptDKSDRDMLDVLIAVKAETGTPrFSADEITGMFISM 253
Cdd:cd11053 158 SFPALqrdlgpwsPWGRFLRARRR---IDALIYAEIAERRAEP--DAERDDILSLLLSARDEDGQP-LSDEELRDELMTL 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      254 MFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALrqiPQLENVLKETLRLHPPLIILMRVAKGEFE 333
Cdd:cd11053 232 LFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDPEDIAKL---PYLDAVIKETLRLYPVAPLVPRRVKEPVE 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      334 VQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYeqprqedlLNR----WTWIPFGAGRHRCVGAAFAIMQIKAIFS 409
Cdd:cd11053 309 LGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERF--------LGRkpspYEYLPFGGGVRRCIGAAFALLEMKVVLA 380

                       410
                ....*....|....
1U13_A      410 VLLREYEFEMAQPP 423
Cdd:cd11053 381 TLLRRFRLELTDPR 394
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 38-424 3.88e-67

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: 219.69  E-value: 3.88e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       38 GDVGTFQLAGKQVVLLSGSHANEFFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEM--LHNAALRGEQMKGHAA 115
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLrrLLAPAFTPRALAALRP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      116 TIEDQVRRMIADWGEAGE--IDLLDFFAELTIYTSSATLIGKKFRDQLDgRFAKLYHELERGTDPLAyvDPYLPIESFRR 193
Cdd:cd00302  81 VIREIARELLDRLAAGGEvgDDVADLAQPLALDVIARLLGGPDLGEDLE-ELAELLEALLKLLGPRL--LRPLPSPRLRR 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      194 RDEARNGLVALVADIMNGRIANPPTDksdrdmLDVLIAVKAETGtPRFSADEITGMFISMMFAGHHTSSGTASWTLIELM 273
Cdd:cd00302 158 LRRARARLRDYLEELIARRRAEPADD------LDLLLLADADDG-GGLSDEEIVAELLTLLLAGHETTASLLAWALYLLA 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      274 RHRDAYAAVIDELDELYGDGrsvSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISN 353
Cdd:cd00302 231 RHPEVQERLRAEIDAVLGDG---TPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLYAAH 307

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1U13_A      354 RIPEDFPDPHDFVPARYEQPRQEdllNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPE 424
Cdd:cd00302 308 RDPEVFPDPDEFDPERFLPEREE---PRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEE 375
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 21-424 8.92e-67

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: 218.99  E-value: 8.92e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       21 EFRTDPIGLMQRVRDElGDVGTFQLAGKQVVLLSGSHANEFFFRAgDDDLDQAKAYPFMTP---IFGEGVVFDASPE-RR 96
Cdd:COG2124  16 AFLRDPYPFYARLREY-GPVFRVRLPGGGAWLVTRYEDVREVLRD-PRTFSSDGGLPEVLRplpLLGDSLLTLDGPEhTR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       97 KEMLHNAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGkkFRDQLDGRFAKLYHELERGT 176
Cdd:COG2124  94 LRRLVQPAFTPRRVAALRPRIREIADELLDRLAARGPVDLVEEFARPLPVIVICELLG--VPEEDRDRLRRWSDALLDAL 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      177 DPLayvdpylPIESFRRRDEARNGLVALVADIMNGRIANPPTDksdrdMLDVLIAvkAETGTPRFSADEITGMFISMMFA 256
Cdd:COG2124 172 GPL-------PPERRRRARRARAELDAYLRELIAERRAEPGDD-----LLSALLA--ARDDGERLSDEELRDELLLLLLA 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      257 GHHTSSGTASWTLIELMRHRDAYAAVIDELdelygdgrsvsfhalrqiPQLENVLKETLRLHPPLIILMRVAKGEFEVQG 336
Cdd:COG2124 238 GHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTATEDVELGG 299

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      337 HRIHEGDLVAASPAISNRIPEDFPDPHDFVPARyeqprqedllNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYE 416
Cdd:COG2124 300 VTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFP 369


                ....*....
1U13_A      417 -FEMAQPPE 424
Cdd:COG2124 370 dLRLAPPEE 378
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 21-424 1.35e-64

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: 214.07  E-value: 1.35e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       21 EFRTDPIGLMQRVRDELGDVGTFQLAGKQVVLLSGSHANEFFFrAGDDDLDQAKAYPFMTPIFGEGVVF--DASPERRKE 98
Cdd:cd11044   5 EFLRDPEDFIQSRYQKYGPVFKTHLLGRPTVFVIGAEAVRFIL-SGEGKLVRYGWPRSVRRLLGENSLSlqDGEEHRRRR 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       99 MLHNAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDgrfaKLYHELERGTDP 178
Cdd:cd11044  84 KLLAPAFSREALESYVPTIQAIVQSYLRKWLKAGEVALYPELRRLTFDVAARLLLGLDPEVEAE----ALSQDFETWTDG 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      179 LAYVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPPTDKSDrdMLDVLIAVKAETGTPrFSADEITGMFISMMFAGH 258
Cdd:cd11044 160 LFSLPVPLPFTPFGRAIRARNKLLARLEQAIRERQEEENAEAKD--ALGLLLEAKDEDGEP-LSMDELKDQALLLLFAGH 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      259 HTSSGTASWTLIELMRHRDAYAAVIDELDELyGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHR 338
Cdd:cd11044 237 ETTASALTSLCFELAQHPDVLEKLRQEQDAL-GLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQ 315

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      339 IHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd11044 316 IPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWE 395


                ....*...
1U13_A      419 MA--QPPE 424
Cdd:cd11044 396 LLpnQDLE 403
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 17-441 3.22e-59

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: 200.97  E-value: 3.22e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A         17 GHLEEFRTDPI--GLMQRVRDELGDVGTFQLAGKQVVLLSGSHANEFFFRAGD----DDLDQAKAYPFMTPIFGEGVVFd 90
Cdd:pfam00067  11 GNLLQLGRKGNlhSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGeefsGRPDEPWFATSRGPFLGKGIVF- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A         91 ASPERRKEM--LHNAALRGEQMKGHAATIEDQVRRMIADW----GEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDGR 164
Cdd:pfam00067  90 ANGPRWRQLrrFLTPTFTSFGKLSFEPRVEEEARDLVEKLrktaGEPGVIDITDLLFRAALNVICSILFGERFGSLEDPK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        165 FAKL------YHELERGTDPLAY----VDPYLPIESFRRRDEARNGLVALVADIMNGRIAN-PPTDKSDRDMLDVLIAVK 233
Cdd:pfam00067 170 FLELvkavqeLSSLLSSPSPQLLdlfpILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETlDSAKKSPRDFLDALLLAK 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        234 AETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKE 313
Cdd:pfam00067 250 EEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKE 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        314 TLRLHPPLII-LMRVAKGEFEVQGHRIHEGDLVAASP-AISNRiPEDFPDPHDFVPARYEqPRQEDLLNRWTWIPFGAGR 391
Cdd:pfam00067 330 TLRLHPVVPLlLPREVTKDTVIPGYLIPKGTLVIVNLyALHRD-PEVFPNPEEFDPERFL-DENGKFRKSFAFLPFGAGP 407

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
1U13_A        392 HRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPESYRNDHSKMVVQLAQPA 441
Cdd:pfam00067 408 RNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPY 457
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 38-424 6.59e-52

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: 180.08  E-value: 6.59e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       38 GDVGTFQLAGKQVVLLSGSHANEFFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPE-RRKEMLHNAALRGEQMKGHAAT 116
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVKGGVYERLKLLLGNGLLTSEGDLwRRQRRLAQPAFHRRRIAAYADA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      117 IEDQVRRMIADW---GEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDgrfaKLYHELERGTDPLAY--VDPYLPIESF 191
Cdd:cd20620  81 MVEATAALLDRWeagARRGPVDVHAEMMRLTLRIVAKTLFGTDVEGEAD----EIGDALDVALEYAARrmLSPFLLPLWL 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      192 -----RRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLdvLIAVKAETGTPrFSADEITGMFISMMFAGHHTSSGTAS 266
Cdd:cd20620 157 ptpanRRFRRARRRLDEVIYRLIAERRAAPADGGDLLSML--LAARDEETGEP-MSDQQLRDEVMTLFLAGHETTANALS 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      267 WTLIELMRHRDAYAAVIDELDELYGdGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVA 346
Cdd:cd20620 234 WTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYRIPAGSTVL 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      347 ASPAISNRIPEDFPDPHDFVPARYeQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA--QPPE 424
Cdd:cd20620 313 ISPYVTHRDPRFWPDPEAFDPERF-TPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVpgQPVE 391
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 29-417 1.87e-51

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: 179.05  E-value: 1.87e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       29 LMQRVRdELGDVGTFQLAGKQVVLLSGSHANEFFFRAGDDDLDQAKAY-PFMTPIFGEGVVF-DASPER--RKEMlhNAA 104
Cdd:cd11045   3 ARQRYR-RYGPVSWTGMLGLRVVALLGPDANQLVLRNRDKAFSSKQGWdPVIGPFFHRGLMLlDFDEHRahRRIM--QQA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      105 LRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDgRFAKLYHELERGtdPLAYVDP 184
Cdd:cd11045  80 FTRSALAGYLDRMTPGIERALARWPTGAGFQFYPAIKELTLDLATRVFLGVDLGPEAD-KVNKAFIDTVRA--STAIIRT 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      185 YLPIESFRRRDEARNGLVALVAdimnGRIANPPTDKSDrDMLDVLIAVKAETGTpRFSADEITGMFISMMFAGHHTSSGT 264
Cdd:cd11045 157 PIPGTRWWRGLRGRRYLEEYFR----RRIPERRAGGGD-DLFSALCRAEDEDGD-RFSDDDIVNHMIFLMMAAHDTTTST 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      265 ASWTLIELMRHRDAYAAVIDELDELyGDGRsVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDL 344
Cdd:cd11045 231 LTSMAYFLARHPEWQERLREESLAL-GKGT-LDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEVLGYRIPAGTL 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1U13_A      345 VAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEF 417
Cdd:cd11045 309 VAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRW 381
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 81-418 6.63e-51

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: 177.84  E-value: 6.63e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       81 PIFGEGVVFDASPE-RRKEMLHNAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKFRD 159
Cdd:cd11049  56 PLLGNGLATCPGEDhRRQRRLMQPAFHRSRIPAYAEVMREEAEALAGSWRPGRVVDVDAEMHRLTLRVVARTLFSTDLGP 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      160 QLDGRFAKLYHELERGTDPLAYVDPY---LPIESFRRRDEARNGLVALVADIMNGRIANPptdkSDRDMLDVLIAVKAET 236
Cdd:cd11049 136 EAAAELRQALPVVLAGMLRRAVPPKFlerLPTPGNRRFDRALARLRELVDEIIAEYRASG----TDRDDLLSLLLAARDE 211

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      237 GTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGdGRSVSFHALRQIPQLENVLKETLR 316
Cdd:cd11049 212 EGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALR 290

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      317 LHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDlLNRWTWIPFGAGRHRCVG 396
Cdd:cd11049 291 LYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAA-VPRGAFIPFGAGARKCIG 369

                       330       340
                ....*....|....*....|..
1U13_A      397 AAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd11049 370 DTFALTELTLALATIASRWRLR 391
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 45-421 2.44e-43

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: 157.34  E-value: 2.44e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       45 LAGKQVVLLSGSHANEFFFRAGDDDLdqAKAYPF-MTPIFGEGVVFDASPERRKEMlHNAA---LRGEQMKGH-AATIED 119
Cdd:cd11043  13 LFGRPTVVSADPEANRFILQNEGKLF--VSWYPKsVRKLLGKSSLLTVSGEEHKRL-RGLLlsfLGPEALKDRlLGDIDE 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      120 QVRRMIADWGEAGEIDLLDFFAELTIytssaTLIGKKFRDQLDG----RFAKLYHELERGtdpLAYVDPYLPIESFRRRD 195
Cdd:cd11043  90 LVRQHLDSWWRGKSVVVLELAKKMTF-----ELICKLLLGIDPEevveELRKEFQAFLEG---LLSFPLNLPGTTFHRAL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      196 EARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPrFSADEITGMFISMMFAGHHTSSGTASWTLIELMRH 275
Cdd:cd11043 162 KARKRIRKELKKIIEERRAELEKASPKGDLLDVLLEEKDEDGDS-LTDEEILDNILTLLFAGHETTSTTLTLAVKFLAEN 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      276 RDAYAAVIDELDELY---GDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAIS 352
Cdd:cd11043 241 PKVLQELLEEHEEIAkrkEEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARAT 320

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1U13_A      353 NRIPEDFPDPHDFVPARYEqprQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQ 421
Cdd:cd11043 321 HLDPEYFPDPLKFNPWRWE---GKGKGVPYTFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVVP 386
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 75-428 4.33e-41

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: 151.65  E-value: 4.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       75 AYPFMTPIFGEGVVF---DASPERRKEMlhNAALRGEQMKGHAATIEDQVRRMIADWGEA-----GEIDLLDFfaelTIY 146
Cdd:cd11069  41 FRRLLRRILGDGLLAaegEEHKRQRKIL--NPAFSYRHVKELYPIFWSKAEELVDKLEEEieesgDESISIDV----LEW 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      147 TSSATL-------IGKKFrDQLDGR---FAKLYHELERGTD------------PLAYVDpYLPIESFRRRDEARNGLVAL 204
Cdd:cd11069 115 LSRATLdiiglagFGYDF-DSLENPdneLAEAYRRLFEPTLlgsllfilllflPRWLVR-ILPWKANREIRRAKDVLRRL 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      205 VADIMNGRIA--NPPTDKSDRDMLDVLIAVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAV 282
Cdd:cd11069 193 AREIIREKKAalLEGKDDSGKDILSILLRANDFADDERLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERL 272

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      283 IDELDELYGD--GRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDF- 359
Cdd:cd11069 273 REEIRAALPDppDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWg 352

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1U13_A      360 PDPHDFVPARYEQPRQEDLLNRW-TW---IPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPESYRN 428
Cdd:cd11069 353 PDAEEFNPERWLEPDGAASPGGAgSNyalLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPDAEVERP 425
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 70-424 7.52e-41

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: 150.75  E-value: 7.52e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       70 LDQAKAYPFMTPIFGEGVVFdASPE----RRKeML----HNAALrgeqmKGHAATIEDQVRRMIADWGE---AGEIDLLD 138
Cdd:cd20628  32 ITKSFLYDFLKPWLGDGLLT-STGEkwrkRRK-LLtpafHFKIL-----ESFVEVFNENSKILVEKLKKkagGGEFDIFP 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      139 FFAELTIYTSSATLIGKKFRDQLDG---------RFAKLYHEleRGTDPLAYVDP--YLPIESFR--------------- 192
Cdd:cd20628 105 YISLCTLDIICETAMGVKLNAQSNEdseyvkavkRILEIILK--RIFSPWLRFDFifRLTSLGKEqrkalkvlhdftnkv 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      193 ---RRDEARNGLVALVADIMNGRIANPPtdksdrdMLDVLIAVKAETGTprFSADEITGMFISMMFAGHHTSSGTASWTL 269
Cdd:cd20628 183 ikeRREELKAEKRNSEEDDEFGKKKRKA-------FLDLLLEAHEDGGP--LTDEDIREEVDTFMFAGHDTTASAISFTL 253

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      270 IELMRHRDAYAAVIDELDELYG-DGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAAS 348
Cdd:cd20628 254 YLLGLHPEVQEKVYEELDEIFGdDDRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVIS 333

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1U13_A      349 PAISNRIPEDFPDPHDFVPARYEqPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPE 424
Cdd:cd20628 334 IYALHRNPEYFPDPEKFDPDRFL-PENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPPGE 408
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 38-418 3.63e-39

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: 146.20  E-value: 3.63e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       38 GDVGTFQLAGKQVVLLSG-SHANEFFFRAGDDDLDQAKAyPFMTPIFGEGVVFDASPE----RRKEMLHnaALRGEQM-K 111
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDpEIIKEAFVKNGDNFSDRPLL-PSFEIISGGKGILFSNGDywkeLRRFALS--SLTKTKLkK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      112 GHAATIEDQVRRMI------ADWGEagEIDLLDFFaelTIYTSS---ATLIGKKFRDQLDGRFAKLYHELER-----GTD 177
Cdd:cd20617  78 KMEELIEEEVNKLIeslkkhSKSGE--PFDPRPYF---KKFVLNiinQFLFGKRFPDEDDGEFLKLVKPIEEifkelGSG 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      178 PLAYVDPYLPI---ESFRRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPRFSADEITGMFISMM 254
Cdd:cd20617 153 NPSDFIPILLPfyfLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDLF 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      255 FAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPL-IILMRVAKGEFE 333
Cdd:cd20617 233 LAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILpLGLPRVTTEDTE 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      334 VQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWtwIPFGAGRHRCVGAAFAIMQIKAIFSVLLR 413
Cdd:cd20617 313 IGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGNKLSEQF--IPFGIGKRNCVGENLARDELFLFFANLLL 390


                ....*
1U13_A      414 EYEFE 418
Cdd:cd20617 391 NFKFK 395
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 110-418 6.15e-38

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: 142.72  E-value: 6.15e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      110 MKGHAATIEDQVRRMIADWGEA----GEIDLLDFFAELTIYTSSATLIGKKFRDQL--DGRFAKLYHELERGTD---PLA 180
Cdd:cd11055  76 LKLMVPIINDCCDELVEKLEKAaetgKPVDMKDLFQGFTLDVILSTAFGIDVDSQNnpDDPFLKAAKKIFRNSIirlFLL 155

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      181 YVDPYLPIESFRR-----RDEARNGLVALVADIMNGRIANPPTDKsdRDMLDVLI---AVKAETGTPRFSADEITGMFIS 252
Cdd:cd11055 156 LLLFPLRLFLFLLfpfvfGFKSFSFLEDVVKKIIEQRRKNKSSRR--KDLLQLMLdaqDSDEDVSKKKLTDDEIVAQSFI 233

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      253 MMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEF 332
Cdd:cd11055 234 FLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFISRECKEDC 313

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      333 EVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEqPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLL 412
Cdd:cd11055 314 TINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFS-PENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKIL 392


                ....*.
1U13_A      413 REYEFE 418
Cdd:cd11055 393 QKFRFV 398
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 95-424 9.67e-35

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: 133.89  E-value: 9.67e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       95 RRKEMLH---NAALRG--EQMKGHAATIEDQVRRMIADwGEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDGRFAKLY 169
Cdd:cd11061  57 RRRVWSHafsDKALRGyePRILSHVEQLCEQLDDRAGK-PVSWPVDMSDWFNYLSFDVMGDLAFGKSFGMLESGKDRYIL 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      170 HELERGTD---PLAYVDPYLPI----ESFRRRDEARNGLVALVADIMNGRIANPPTDKsdRDMLDVLIAVKAETGTPRFS 242
Cdd:cd11061 136 DLLEKSMVrlgVLGHAPWLRPLlldlPLFPGATKARKRFLDFVRAQLKERLKAEEEKR--PDIFSYLLEAKDPETGEGLD 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      243 ADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELY-GDGRSVSFHALRQIPQLENVLKETLRLHPPL 321
Cdd:cd11061 214 LEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFpSDDEIRLGPKLKSLPYLRACIDEALRLSPPV 293

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      322 -IILMR-VAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAF 399
Cdd:cd11061 294 pSGLPReTPPGGLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVRARSAFIPFSIGPRGCIGKNL 373

                       330       340
                ....*....|....*....|....*
1U13_A      400 AIMQIKAIFSVLLREYEFEMAQPPE 424
Cdd:cd11061 374 AYMELRLVLARLLHRYDFRLAPGED 398
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 199-422 2.47e-34

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: 133.09  E-value: 2.47e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      199 NGLVALVADIMNGRIANPPTDKSDR-DMLDVLIAVKAETGTPrFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRD 277
Cdd:cd11060 176 GPLMRFALEAVAERLAEDAESAKGRkDMLDSFLEAGLKDPEK-VTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPR 254

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      278 AYAAVIDELDELYGDGRS---VSFHALRQIPQLENVLKETLRLHPPLIILM-RVA-KGEFEVQGHRIHEGDLVAASPAIS 352
Cdd:cd11060 255 VYAKLRAEIDAAVAEGKLsspITFAEAQKLPYLQAVIKEALRLHPPVGLPLeRVVpPGGATICGRFIPGGTIVGVNPWVI 334

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1U13_A      353 NRIPEDF-PDPHDFVPARY--EQPRQEDLLNRWtWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQP 422
Cdd:cd11060 335 HRDKEVFgEDADVFRPERWleADEEQRRMMDRA-DLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVDP 406
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 95-426 7.49e-34

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: 131.65  E-value: 7.49e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       95 RRKEMLHNA----ALRGEQMKGHaatIEDQVRRMIADW----GEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDGRFA 166
Cdd:cd11059  57 ARRRLLSGVysksSLLRAAMEPI---IRERVLPLIDRIakeaGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKD 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      167 KLYHELERGTD-----PLAYVDPYLPIESFRR----RDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETG 237
Cdd:cd11059 134 SRERELLRRLLaslapWLRWLPRYLPLATSRLiigiYFRAFDEIEEWALDLCARAESSLAESSDSESLTVLLLEKLKGLK 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      238 TPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGD-GRSVSFHALRQIPQLENVLKETLR 316
Cdd:cd11059 214 KQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPfRGPPDLEDLDKLPYLNAVIRETLR 293

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      317 LHPPL-IILMRVA-KGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDL--LNRWTWiPFGAGRH 392
Cdd:cd11059 294 LYPPIpGSLPRVVpEGGATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETAreMKRAFW-PFGSGSR 372

                       330       340       350
                ....*....|....*....|....*....|....
1U13_A      393 RCVGAAFAIMQIKAIFSVLLREYEFEMAqPPESY 426
Cdd:cd11059 373 MCIGMNLALMEMKLALAAIYRNYRTSTT-TDDDM 405
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 81-424 6.82e-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: 126.33  E-value: 6.82e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       81 PIFGEGVVfDASPE----RRKEM---LHNAALRG-EQMKGHAatIEDQVRRMIADWGEAGEIDLLDFFAELTIytssaTL 152
Cdd:cd11046  55 PIMGKGLI-PADGEiwkkRRRALvpaLHKDYLEMmVRVFGRC--SERLMEKLDAAAETGESVDMEEEFSSLTL-----DI 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      153 IGKKF-------RDQLDGRFAKLY----HELERGTDPLAYVD-PYLPIESFRRRDEARNglVALVADIMNGRIAN----- 215
Cdd:cd11046 127 IGLAVfnydfgsVTEESPVIKAVYlplvEAEHRSVWEPPYWDiPAALFIVPRQRKFLRD--LKLLNDTLDDLIRKrkemr 204

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      216 ----------PPTDKSDRDMLDVLIAVKAETGTPRFSADEItgmfISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDE 285
Cdd:cd11046 205 qeedielqqeDYLNEDDPSLLRFLVDMRDEDVDSKQLRDDL----MTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAE 280

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      286 LDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHR--IHEGDLVAASPAISNRIPEDFPDPH 363
Cdd:cd11046 281 VDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGGGvkVPAGTDIFISVYNLHRSPELWEDPE 360

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1U13_A      364 DFVPARYE---QPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPE 424
Cdd:cd11046 361 EFDPERFLdpfINPPNEVIDDFAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPR 424
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 207-418 1.78e-31

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: 125.06  E-value: 1.78e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      207 DIMNGRIA---NPPTDKSDRDMLDVLIAVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVI 283
Cdd:cd20621 188 KIIQNRIKqikKNKDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLR 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      284 DELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILM-RVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDP 362
Cdd:cd20621 268 QEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLFpRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENP 347

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
1U13_A      363 HDFVPARYEQPrQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd20621 348 DEFNPERWLNQ-NNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIE 402
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 201-418 2.12e-31

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: 124.96  E-value: 2.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      201 LVALVADIMNGRIANPPTDKsdrDMLDVLIAVKAETGTPR------FSADEITGMFISMMFAGHHTSSGTASWTLIELMR 274
Cdd:cd11056 182 FRKLVRDTIEYREKNNIVRN---DFIDLLLELKKKGKIEDdksekeLTDEELAAQAFVFFLAGFETSSSTLSFALYELAK 258

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      275 HRDAYAAVIDELDE-LYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHR--IHEGDLVAASP-A 350
Cdd:cd11056 259 NPEIQEKLREEIDEvLEKHGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDvvIEKGTPVIIPVyA 338

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1U13_A      351 IsNRIPEDFPDPHDFVPARYEqPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd11056 339 L-HHDPKYYPEPEKFDPERFS-PENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVE 404
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 227-419 3.00e-31

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: 124.55  E-value: 3.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      227 DVL-IAVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIP 305
Cdd:cd20613 215 DILtHILKASEEEPDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLE 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      306 QLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYeQPRQEDLLNRWTWI 385
Cdd:cd20613 295 YLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERF-SPEAPEKIPSYAYF 373

                       170       180       190
                ....*....|....*....|....*....|....
1U13_A      386 PFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEM 419
Cdd:cd20613 374 PFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFEL 407
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 192-448 1.14e-30

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 124.15  E-value: 1.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       192 RRRDEARNGLVAlvadimNGRIANPPTDKSDRDMLDVLIAVKAETGTP----RFSADEITGMFISMMFAGHHTSSGTASW 267
Cdd:PLN02687 246 RRFDAMMNGIIE------EHKAAGQTGSEEHKDLLSTLLALKREQQADgeggRITDTEIKALLLNLFTAGTDTTSSTVEW 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       268 TLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPL-IILMRVAKGEFEVQGHRIHEG-DLV 345
Cdd:PLN02687 320 AIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTpLSLPRMAAEECEINGYHIPKGaTLL 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       346 AASPAISnRIPEDFPDPHDFVPARY----EQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA- 420
Cdd:PLN02687 400 VNVWAIA-RDPEQWPDPLEFRPDRFlpggEHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELAd 478

                        250       260       270
                 ....*....|....*....|....*....|
1U13_A       421 -QPPESYRNDHS-KMVVQLAQPAAVRYRRR 448
Cdd:PLN02687 479 gQTPDKLNMEEAyGLTLQRAVPLMVHPRPR 508
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 226-427 1.29e-30

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: 122.76  E-value: 1.29e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      226 LDVLIAVkAETGTpRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDG-RSVSFHALRQI 304
Cdd:cd20660 215 LDLLLEA-SEEGT-KLSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSdRPATMDDLKEM 292

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      305 PQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYeqpRQEDLLNR--W 382
Cdd:cd20660 293 KYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRF---LPENSAGRhpY 369

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1U13_A      383 TWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPESYR 427
Cdd:cd20660 370 AYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESVQKREDLK 414
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 217-424 1.93e-30

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: 122.18  E-value: 1.93e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      217 PTDKSDRDMLDVLIAVKAETGTpRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDG-RS 295
Cdd:cd20680 216 PSKKKRKAFLDMLLSVTDEEGN-KLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSdRP 294

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      296 VSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYeQPRQ 375
Cdd:cd20680 295 VTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERF-FPEN 373

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1U13_A      376 EDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPE 424
Cdd:cd20680 374 SSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVEANQKRE 422
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 79-416 1.99e-30

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: 121.78  E-value: 1.99e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       79 MTPIFGEGVV-FDASPERRKEMLHNAAL--RGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIytssaTLIgk 155
Cdd:cd20614  50 IAPILGGTMAaQDGALHRRARAASNPSFtpKGLSAAGVGALIAEVIEARIRAWLSRGDVAVLPETRDLTL-----EVI-- 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      156 kFR------DQLDGrFAKLYHELERGTDPLAYVDPYLPiesFRRRDEARNGLVALVADIMNGRIANPptdkSDRDMLDVL 229
Cdd:cd20614 123 -FRilgvptDDLPE-WRRQYRELFLGVLPPPVDLPGMP---ARRSRRARAWIDARLSQLVATARANG----ARTGLVAAL 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      230 IAVKAETGTPrFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELygDGRSVSFHALRQIPQLEN 309
Cdd:cd20614 194 IRARDDNGAG-LSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA--GDVPRTPAELRRFPLAEA 270

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      310 VLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARY----EQPRQEDLLNrwtwi 385
Cdd:cd20614 271 LFRETLRLHPPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWlgrdRAPNPVELLQ----- 345

                       330       340       350
                ....*....|....*....|....*....|.
1U13_A      386 pFGAGRHRCVGAAFAIMQIKAIFSVLLREYE 416
Cdd:cd20614 346 -FGGGPHFCLGYHVACVELVQFIVALARELG 375
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 215-418 2.11e-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: 121.89  E-value: 2.11e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      215 NPPTDKSDR---DMLDVLIAVKAETGTpRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYG 291
Cdd:cd20659 195 NKDEALSKRkylDFLDILLTARDEDGK-GLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLG 273

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      292 DGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYE 371
Cdd:cd20659 274 DRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFL 353

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1U13_A      372 qprQEDLLNR--WTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd20659 354 ---PENIKKRdpFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELS 399
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 77-425 1.64e-29

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: 119.27  E-value: 1.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       77 PFMTPIFGE-GVVFDASPER---RKEMLHN---AALrgeqmkGHAATIEDQV-RRMIADWGEAG-----EIDLLDFFAEL 143
Cdd:cd11082  39 PNAKKILGEdNLIFMFGEEHkelRKSLLPLftrKAL------GLYLPIQERViRKHLAKWLENSksgdkPIEMRPLIRDL 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      144 TIYTSSATLIGkkfrDQLDGRFAKLYHELERGTDPLAYVDPYLPIESFRRRDEARNGLVALVADIM---NGRIA--NPPT 218
Cdd:cd11082 113 NLETSQTVFVG----PYLDDEARRFRIDYNYFNVGFLALPVDFPGTALWKAIQARKRIVKTLEKCAaksKKRMAagEEPT 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      219 ---DKSDRDMLDVLIAVKAETGTPR--FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDG 293
Cdd:cd11082 189 cllDFWTHEILEEIKEAEEEGEPPPphSSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPND 268

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      294 RS-VSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEV-QGHRIHEGDLVAASPAISNRIPedFPDPHDFVPARYE 371
Cdd:cd11082 269 EPpLTLDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLtEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFS 346

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
1U13_A      372 QPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPES 425
Cdd:cd11082 347 PERQEDRKYKKNFLVFGAGPHQCVGQEYAINHLMLFLALFSTLVDWKRHRTPGS 400
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 132-417 2.03e-29

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: 119.24  E-value: 2.03e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      132 GEIDLLDFFAELTIYTSSATLIGKKFRDQLDG--RFAKLYHEL-----ERGTDPLAYVD-PYLPIESFRRRDEARNGLVA 203
Cdd:cd11057  96 GEFDILPDLSRCTLEMICQTTLGSDVNDESDGneEYLESYERLfeliaKRVLNPWLHPEfIYRLTGDYKEEQKARKILRA 175

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      204 LVADIMNGRIA--------NPPTDKSDRDMLDVLI--AVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELM 273
Cdd:cd11057 176 FSEKIIEKKLQevelesnlDSEEDEENGRKPQIFIdqLLELARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLA 255

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      274 RHRDAYAAVIDELDELYGD-GRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEV-QGHRIHEGDLVAASPAI 351
Cdd:cd11057 256 MHPEVQEKVYEEIMEVFPDdGQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLsNGVVIPKGTTIVIDIFN 335

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1U13_A      352 SNRIPEDF-PDPHDFVPARYEQPRQEDlLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEF 417
Cdd:cd11057 336 MHRRKDIWgPDADQFDPDNFLPERSAQ-RHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRL 401
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 41-448 3.22e-29

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: 118.93  E-value: 3.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       41 GTFQLA--GKQVVLLSGSHANEFFfRAGDDDLDQAKAYPFMTPIFGEGvvfdaSPERRKEMLHNAALRGE---QMKGHAA 115
Cdd:cd11041  12 GPFQLPtpDGPLVVLPPKYLDELR-NLPESVLSFLEALEEHLAGFGTG-----GSVVLDSPLHVDVVRKDltpNLPKLLP 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      116 TIEDQVRRMIAD-WGEAGE---IDLLDFFAELTIYTSSATLIGKKF-RDQ--LD------------GRFAKLYHELERgt 176
Cdd:cd11041  86 DLQEELRAALDEeLGSCTEwteVNLYDTVLRIVARVSARVFVGPPLcRNEewLDltinytidvfaaAAALRLFPPFLR-- 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      177 dPLAYvdPYLPIESFRRRDEARngLVALVADIMNGRIANPPTDKSDR--DMLDVLIAvkAETGTPRFSADEITGMFISMM 254
Cdd:cd11041 164 -PLVA--PFLPEPRRLRRLLRR--ARPLIIPEIERRRKLKKGPKEDKpnDLLQWLIE--AAKGEGERTPYDLADRQLALS 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      255 FAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMR--VAKGEF 332
Cdd:cd11041 237 FAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRrkVLKDVT 316

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      333 EVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQE-DLLNRW-------TWIPFGAGRHRCVGAAFAIMQI 404
Cdd:cd11041 317 LSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQpGQEKKHqfvstspDFLGFGHGRHACPGRFFASNEI 396

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
1U13_A      405 KAIFSVLLREYEFEMA---QPPESYRNDHSKMVVqlaQPAAVRYRRR 448
Cdd:cd11041 397 KLILAHLLLNYDFKLPeggERPKNIWFGEFIMPD---PNAKVLVRRR 440
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 88-425 5.58e-29

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: 117.81  E-value: 5.58e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       88 VFDASPE--RRKEMLHNAALRGEQMKGHAATIEDQVRRMIADWGEAGE----IDLLDFFAELTIYTSSATLIGKKFRdql 161
Cdd:cd11083  51 VFSAEGDawRRQRRLVMPAFSPKHLRYFFPTLRQITERLRERWERAAAegeaVDVHKDLMRYTVDVTTSLAFGYDLN--- 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      162 dgrfaklyhELERGTDP----LAYVDP--------------YLPIESFRRRDEARNGLVALVADIMN---GRIA-NPPTD 219
Cdd:cd11083 128 ---------TLERGGDPlqehLERVFPmlnrrvnapfpywrYLRLPADRALDRALVEVRALVLDIIAaarARLAaNPALA 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      220 KSDRDMLDVLIAVKAETGtpRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGR-SVSF 298
Cdd:cd11083 199 EAPETLLAMMLAEDDPDA--RLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARvPPLL 276

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      299 HALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQE-D 377
Cdd:cd11083 277 EALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAaE 356

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
1U13_A      378 LLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPES 425
Cdd:cd11083 357 PHDPSSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPEPAPA 404
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 203-422 8.86e-29

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: 117.52  E-value: 8.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      203 ALVADIMNGRIANPPTDKSDRDMLDVLI-AVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAA 281
Cdd:cd20657 185 ALLTKILEEHKATAQERKGKPDFLDFVLlENDDNGEGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKK 264

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      282 VIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHP--PLiILMRVAKGEFEVQGHRIHEG-DLVAASPAISnRIPED 358
Cdd:cd20657 265 AQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPstPL-NLPRIASEACEVDGYYIPKGtRLLVNIWAIG-RDPDV 342

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1U13_A      359 FPDPHDFVPARYEQPRQEDLL---NRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQP 422
Cdd:cd20657 343 WENPLEFKPERFLPGRNAKVDvrgNDFELIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKLPAG 409
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 121-440 1.41e-28

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: 116.88  E-value: 1.41e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      121 VRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKF--RDQLDGRFAKLYHELERGTDPLA---YVDPYLPIESF---- 191
Cdd:cd20618  93 VKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRYfgESEKESEEAREFKELIDEAFELAgafNIGDYIPWLRWldlq 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      192 ---RRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWT 268
Cdd:cd20618 173 gyeKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLDMLAAGTDTSAVTIEWA 252

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      269 LIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILM-RVAKGEFEVQGHRIhegdlvaa 347
Cdd:cd20618 253 MAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLpHESTEDCKVAGYDI-------- 324

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      348 sPAIS---------NRIPEDFPDPHDFVPARYEQPRQEDLLNR-WTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEF 417
Cdd:cd20618 325 -PAGTrvlvnvwaiGRDPKVWEDPLEFKPERFLESDIDDVKGQdFELLPFGSGRRMCPGMPLGLRMVQLTLANLLHGFDW 403

                       330       340
                ....*....|....*....|....*
1U13_A      418 EMA-QPPESY-RNDHSKMVVQLAQP 440
Cdd:cd20618 404 SLPgPKPEDIdMEEKFGLTVPRAVP 428
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 77-440 2.19e-28

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: 116.29  E-value: 2.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       77 PFMTPIFGEGVVF----DASPERRkemLHNAALRGEQMKGHAATIEDQVRRMIADWGE--AGEIDLLDFFAELTIYTS-- 148
Cdd:cd11052  51 PGLKKLLGRGLVMsngeKWAKHRR---IANPAFHGEKLKGMVPAMVESVSDMLERWKKqmGEEGEEVDVFEEFKALTAdi 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      149 -SATLIGKKFrdqLDGR--FAKLYHELERGTDPLAYVdpYLPIESF------RRRDEARNGLVALVADIMNGRIANPPTD 219
Cdd:cd11052 128 iSRTAFGSSY---EEGKevFKLLRELQKICAQANRDV--GIPGSRFlptkgnKKIKKLDKEIEDSLLEIIKKREDSLKMG 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      220 KSD---RDMLDVLI-AVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRs 295
Cdd:cd11052 203 RGDdygDDLLGLLLeANQSDDQNKNMTVQEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDK- 281

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      296 VSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEG-DLVAASPAI--SNRIPEDfpDPHDFVPARYEQ 372
Cdd:cd11052 282 PPSDSLSKLKTVSMVINESLRLYPPAVFLTRKAKEDIKLGGLVIPKGtSIWIPVLALhhDEEIWGE--DANEFNPERFAD 359

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      373 --PRQEDLLNrwTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAqppESYRndHSKMVVQLAQP 440
Cdd:cd11052 360 gvAKAAKHPM--AFLPFGLGPRNCIGQNFATMEAKIVLAMILQRFSFTLS---PTYR--HAPTVVLTLRP 422
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 75-442 5.07e-28

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: 114.66  E-value: 5.07e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       75 AYPFMTPIFGEGVVFDASPERRKEM--LHNAALRGEQMKGHAATIEDQVRRMI------ADWGEagEIDLLDFFAELTIY 146
Cdd:cd11051  36 LRKFLTPLTGGSSLISMEGEEWKRLrkRFNPGFSPQHLMTLVPTILDEVEIFAailrelAESGE--VFSLEELTTNLTFD 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      147 TSSATLIGKKFRDQLDGR-----FAKLYHELERGTDPLAYvdpYLPIESFRRRDEARnglvalvadIMngrianpptdks 221
Cdd:cd11051 114 VIGRVTLDIDLHAQTGDNslltaLRLLLALYRSLLNPFKR---LNPLRPLRRWRNGR---------RL------------ 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      222 DRDMLDVLIAvkaetgtpRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHAL 301
Cdd:cd11051 170 DRYLKPEVRK--------RFELERAIDQIKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPSAAAELL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      302 RQIPQLEN-------VLKETLRLHPPLIILMRVAKGefevQGHRIHEGDLVAASPAIS-------NRIPEDFPDPHDFVP 367
Cdd:cd11051 242 REGPELLNqlpyttaVIKETLRLFPPAGTARRGPPG----VGLTDRDGKEYPTDGCIVyvchhaiHRDPEYWPRPDEFIP 317

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1U13_A      368 ARYEQPRQEDL-LNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPP--ESYRNDHSKMVVQLAQPAA 442
Cdd:cd11051 318 ERWLVDEGHELyPPKSAWRPFERGPRNCIGQELAMLELKIILAMTVRRFDFEKAYDEwdAKGGYKGLKELFVTGQGTA 395
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 26-422 6.38e-28

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: 114.72  E-value: 6.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       26 PIGLMQRVRDELGDVGTFQLAGKQVVLLSGSHANEFFFRAGDDDLDQAKAYPfmtpifgegVVFDASPERRKEMLHNAAL 105
Cdd:cd20635   1 PLEFIEKARQKLGPVFTVKAAGERMTFVTDEEDFHVFFKSKDVDFQKAVQDP---------VQNTASISKESFFEYHTKI 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      106 RgEQMKGHAAT---------IEDQVRRMIADWGEAGEIDLLDFFAElTIYTSSA-TLIGK--------KFRDQLDgRFAK 167
Cdd:cd20635  72 H-DMMKGKLASsnlaplsdkLCEEFKEQLELLGSEGTGDLNDLVRH-VMYPAVVnNLFGKgllptseeEIKEFEE-HFVK 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      168 LYHELERGTDplayvdpyLPIESFRRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPRFSadeit 247
Cdd:cd20635 149 FDEQFEYGSQ--------LPEFFLRDWSSSKQWLLSLFEKVVPDAEKTKPLENNSKTLLQHLLDTVDKENAPNYS----- 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      248 gmfISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRS----VSFHALRQIPQLENVLKETLRLHPPLII 323
Cdd:cd20635 216 ---LLLLWASLANAIPITFWTLAFILSHPSVYKKVMEEISSVLGKAGKdkikISEDDLKKMPYIKRCVLEAIRLRSPGAI 292

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      324 LMRVAKgEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQ 403
Cdd:cd20635 293 TRKVVK-PIKIKNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEGFVAFGGGRYQCPGRWFALME 371

                       410
                ....*....|....*....
1U13_A      404 IKAIFSVLLREYEFEMAQP 422
Cdd:cd20635 372 IQMFVAMFLYKYDFTLLDP 390
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
 99-424 1.16e-27

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: 113.39  E-value: 1.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       99 MLHNAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLL-DFFAELTIYTSsATLIGkkFRDQLDGRFAKLYHELergtd 177
Cdd:cd11033  78 RLVSRAFTPRAVARLEDRIRERARRLVDRALARGECDFVeDVAAELPLQVI-ADLLG--VPEEDRPKLLEWTNEL----- 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      178 pLAYVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPpTDksdrDMLDVLiaVKAETGTPRFSADEITGMFISMMFAG 257
Cdd:cd11033 150 -VGADDPDYAGEAEEELAAALAELFAYFRELAEERRANP-GD----DLISVL--ANAEVDGEPLTDEEFASFFILLAVAG 221

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      258 HHTSSGTASWTLIELMRHRDAYAAVIDELDelygdgrsvsfhalrqipQLENVLKETLRLHPPLIILMRVAKGEFEVQGH 337
Cdd:cd11033 222 NETTRNSISGGVLALAEHPDQWERLRADPS------------------LLPTAVEEILRWASPVIHFRRTATRDTELGGQ 283

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      338 RIHEGDLVAASPAISNRIPEDFPDPHDFVPARYeqPRQEdllnrwtwIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYE- 416
Cdd:cd11033 284 RIRAGDKVVLWYASANRDEEVFDDPDRFDITRS--PNPH--------LAFGGGPHFCLGAHLARLELRVLFEELLDRVPd 353


                ....*...
1U13_A      417 FEMAQPPE 424
Cdd:cd11033 354 IELAGEPE 361
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 120-416 1.72e-27

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: 113.96  E-value: 1.72e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      120 QVRRMIADWGEAGE------IDLLDFFAELTIYTSSATLIGKKFrdQLDGRFAKLYHELERG-----TDPLAYVDPYLPI 188
Cdd:cd11070  84 QAQRLIRYLLEEQPsakgggVDVRDLLQRLALNVIGEVGFGFDL--PALDEEESSLHDTLNAiklaiFPPLFLNFPFLDR 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      189 ---ESFRRRDEARNGLV----ALVADIMNGRIANPPTDksDRDMLDVLIAVKAETGTPRFSADEITG-MFIsMMFAGHHT 260
Cdd:cd11070 162 lpwVLFPSRKRAFKDVDeflsELLDEVEAELSADSKGK--QGTESVVASRLKRARRSGGLTEKELLGnLFI-FFIAGHET 238

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      261 SSGTASWTLIELMRHRDAYAAVIDELDELYGDgRSVSFHALRQIPQLE---NVLKETLRLHPPLIILMRVAKGEFEV--- 334
Cdd:cd11070 239 TANTLSFALYLLAKHPEVQDWLREEIDSVLGD-EPDDWDYEEDFPKLPyllAVIYETLRLYPPVQLLNRKTTEPVVVitg 317

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      335 --QGHRIHEGDLVAASPAISNRIPE-DFPDPHDFVPARY----EQPRQEDLL--NRWTWIPFGAGRHRCVGAAFAIMQIK 405
Cdd:cd11070 318 lgQEIVIPKGTYVGYNAYATHRDPTiWGPDADEFDPERWgstsGEIGAATRFtpARGAFIPFSAGPRACLGRKFALVEFV 397

                       330
                ....*....|.
1U13_A      406 AIFSVLLREYE 416
Cdd:cd11070 398 AALAELFRQYE 408
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 63-440 6.68e-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: 112.16  E-value: 6.68e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       63 FRAGDDDLDQAKAYPFMTPIFGEGVVF---DASPERRKEMlhNAALRGEQMKGHAATIEDQVRRMIADW------GEAGE 133
Cdd:cd20639  37 LLTRADHFDRYEAHPLVRQLEGDGLVSlrgEKWAHHRRVI--TPAFHMENLKRLVPHVVKSVADMLDKWeamaeaGGEGE 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      134 IDLLDFFAELTIYTSSATLIGKKFRD-----QLDGRFAKLYHELERGTdplaYVDPY--LPIESFRRR----DEARNGLV 202
Cdd:cd20639 115 VDVAEWFQNLTEDVISRTAFGSSYEDgkavfRLQAQQMLLAAEAFRKV----YIPGYrfLPTKKNRKSwrldKEIRKSLL 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      203 ALVADimNGRIANPPTDKSD-RDMLDVLIAVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAA 281
Cdd:cd20639 191 KLIER--RQTAADDEKDDEDsKDLLGLMISAKNARNGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQER 268

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      282 VIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEG-DLVAASPAISNRIPEDFP 360
Cdd:cd20639 269 ARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLYPPAVATIRRAKKDVKLGGLDIPAGtELLIPIMAIHHDAELWGN 348

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      361 DPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAqppESYRndHSKMVVQLAQP 440
Cdd:cd20639 349 DAAEFNPARFADGVARAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRLS---PSYA--HAPTVLMLLQP 423
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 94-416 8.42e-27

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: 111.16  E-value: 8.42e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       94 ERRKemLHNAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLL-DFFAELTIYTSsATLIG------KKFRDQLDGRfa 166
Cdd:cd11078  74 RLRR--LVSRAFTPRRIAALEPRIRELAAELLDRLAEDGRADFVaDFAAPLPALVI-AELLGvpeedmERFRRWADAF-- 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      167 klyhelergtdpLAYVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPptdksdRDMLDVLIAVKAETGTPRFSADEI 246
Cdd:cd11078 149 ------------ALVTWGRPSEEEQVEAAAAVGELWAYFADLVAERRREP------RDDLISDLLAAADGDGERLTDEEL 210

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      247 TGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAvideldelygdgrsvsfhaLRQIPQL-ENVLKETLRLHPPLIILM 325
Cdd:cd11078 211 VAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRR-------------------LRADPSLiPNAVEETLRYDSPVQGLR 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      326 RVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQedllnrwtwIPFGAGRHRCVGAAFAIMQIK 405
Cdd:cd11078 272 RTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDRPNARKH---------LTFGHGIHFCLGAALARMEAR 342

                       330
                ....*....|.
1U13_A      406 AIFSVLLREYE 416
Cdd:cd11078 343 IALEELLRRLP 353
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 215-423 1.29e-26

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: 111.08  E-value: 1.29e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      215 NPPTDKSDRDMLDVLIAvkaetgTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGR 294
Cdd:cd11054 207 KDEEDEEEDSLLEYLLS------KPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGE 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      295 SVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPR 374
Cdd:cd11054 281 PITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDD 360

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
1U13_A      375 QE-DLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPP 423
Cdd:cd11054 361 SEnKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHEE 410
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 245-418 1.59e-26

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: 110.97  E-value: 1.59e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      245 EITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIIL 324
Cdd:cd20650 228 EILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRL 307

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      325 MRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYeQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQI 404
Cdd:cd20650 308 ERVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERF-SKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNM 386

                       170
                ....*....|....
1U13_A      405 KAIFSVLLREYEFE 418
Cdd:cd20650 387 KLALVRVLQNFSFK 400
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 117-422 4.31e-26

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 110.57  E-value: 4.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       117 IEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDGRFaKLYHELERGTDPLAYvdpYLPIESFRRRDE 196
Cdd:PLN02302 162 IEENVKSCLEKWSKMGEIEFLTELRKLTFKIIMYIFLSSESELVMEALE-REYTTLNYGVRAMAI---NLPGFAYHRALK 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       197 ARNGLVALVADIMNGRIANPPTDKSDR--DMLDVLIAVKAETGTpRFSADEITGMFISMMFAGHHTSSGTASWTLIELMR 274
Cdd:PLN02302 238 ARKKLVALFQSIVDERRNSRKQNISPRkkDMLDLLLDAEDENGR-KLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQE 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       275 HRDAYAAVIDELDELY-----GDGRsVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASP 349
Cdd:PLN02302 317 HPEVLQKAKAEQEEIAkkrppGQKG-LTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWF 395

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1U13_A       350 AISNRIPEDFPDPHDFVPARYEQPRQEDllnrWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQP 422
Cdd:PLN02302 396 RQVHMDPEVYPNPKEFDPSRWDNYTPKA----GTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERLNP 464
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 82-423 6.29e-26

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: 109.13  E-value: 6.29e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       82 IFGEGV---VFDASPERRKEMLHNAALRgEQMKGHAATIEDQVRRMIADWGEAG-------EIDLLDFFAELTIytssat 151
Cdd:cd20638  65 ILGSGClsnLHDSQHKHRKKVIMRAFSR-EALENYVPVIQEEVRSSVNQWLQSGpcvlvypEVKRLMFRIAMRI------ 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      152 LIGKKFRDQLDGRFAKLYHELERGTDPLAYVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIA 231
Cdd:cd20638 138 LLGFEPQQTDREQEQQLVEAFEEMIRNLFSLPIDVPFSGLYRGLRARNLIHAKIEENIRAKIQREDTEQQCKDALQLLIE 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      232 VKAETGTPrFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDEL------YGDGRSVSFHALRQIP 305
Cdd:cd20638 218 HSRRNGEP-LNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKgllstkPNENKELSMEVLEQLK 296

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      306 QLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDlLNRWTWI 385
Cdd:cd20638 297 YTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPED-SSRFSFI 375

                       330       340       350
                ....*....|....*....|....*....|....*....
1U13_A      386 PFGAGRHRCVGAAFAIMQIKaIFSV-LLREYEFEMAQPP 423
Cdd:cd20638 376 PFGGGSRSCVGKEFAKVLLK-IFTVeLARHCDWQLLNGP 413
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 204-427 7.00e-26

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: 109.20  E-value: 7.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      204 LVADIMNGRIANPPTDKsdRDMLDVLI-AVKAETGTpRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAV 282
Cdd:cd11068 191 LVDEIIAERRANPDGSP--DDLLNLMLnGKDPETGE-KLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKA 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      283 IDELDELYGDGRSvSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQG-HRIHEGDLVAASPAISNRIPEDF-P 360
Cdd:cd11068 268 RAEVDEVLGDDPP-PYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgE 346

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1U13_A      361 DPHDFVPARYEqPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEmaqPPESYR 427
Cdd:cd11068 347 DAEEFRPERFL-PEEFRKLPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDFE---DDPDYE 409
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 116-415 4.83e-25

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: 105.71  E-value: 4.83e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      116 TIEDQVRRMIADWGEAGEIDLLDFFAE----LTIytssATLIGKKFRDQldGRFAKLYHELERGTDPLAyvdpylPIESF 191
Cdd:cd20625  87 RIERLVDELLDRLAARGRVDLVADFAYplpvRVI----CELLGVPEEDR--PRFRGWSAALARALDPGP------LLEEL 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      192 RRRDEARNGLVALVADIMNGRIANPPTDksdrdMLDVLIAvkAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIE 271
Cdd:cd20625 155 ARANAAAAELAAYFRDLIARRRADPGDD-----LISALVA--AEEDGDRLSEDELVANCILLLVAGHETTVNLIGNGLLA 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      272 LMRHRDAYAAvideldelygdgrsvsfhaLRQIPQL-ENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPA 350
Cdd:cd20625 228 LLRHPEQLAL-------------------LRADPELiPAAVEELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLLLG 288

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1U13_A      351 ISNRIPEDFPDPHDFVPARYEQPRqedllnrwtwIPFGAGRHRCVGAAFAIMQIKAIFSVLLREY 415
Cdd:cd20625 289 AANRDPAVFPDPDRFDITRAPNRH----------LAFGAGIHFCLGAPLARLEAEIALRALLRRF 343
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 118-424 1.06e-24

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: 105.62  E-value: 1.06e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      118 EDQVRRMIADWGEA----GEIDLLDFFAELTIYTSSATLIGKKFRDQLDGRFAKLYHELER--GTDPLAYVDPYL----P 187
Cdd:cd11072  88 EEEVSLLVKKIRESasssSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQDKFKELVKEALEllGGFSVGDYFPSLgwidL 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      188 IESFRRR-DEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPRF--SADEITGMFISMMFAGHHTSSGT 264
Cdd:cd11072 168 LTGLDRKlEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEFplTRDNIKAIILDMFLAGTDTSATT 247

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      265 ASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPL-IILMRVAKGEFEVQGHRIHEGD 343
Cdd:cd11072 248 LEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPApLLLPRECREDCKINGYDIPAKT 327

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      344 --LVAASpAISnRIPEDFPDPHDFVPARYEQP----RQEDL-LnrwtwIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYE 416
Cdd:cd11072 328 rvIVNAW-AIG-RDPKYWEDPEEFRPERFLDSsidfKGQDFeL-----IPFGAGRRICPGITFGLANVELALANLLYHFD 400


                ....*...
1U13_A      417 FEMAQPPE 424
Cdd:cd11072 401 WKLPDGMK 408
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 218-404 1.63e-24

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: 104.99  E-value: 1.63e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      218 TDKSDRDMLDVLIAV----KAETGTPRfsaDEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDG 293
Cdd:cd20655 200 KEGGSKDLLDILLDAyedeNAEYKITR---NHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKT 276

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      294 RSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASP-AISnRIPEDFPDPHDFVPARY-- 370
Cdd:cd20655 277 RLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKTTLFVNVyAIM-RDPNYWEDPLEFKPERFla 355

                       170       180       190
                ....*....|....*....|....*....|....*....
1U13_A      371 -EQPRQEDLLNRWT--WIPFGAGRHRCVGA--AFAIMQI 404
Cdd:cd20655 356 sSRSGQELDVRGQHfkLLPFGSGRRGCPGAslAYQVVGT 394
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 192-440 3.29e-24

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: 104.15  E-value: 3.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      192 RRRDEARNGLVALVADIMNGRIAN--PPTDKSDRDMLDVLIAVKAETGTPrFSADEITGMFISMMFAGHHTSSGTASWTL 269
Cdd:cd11073 177 RRMAEHFGKLFDIFDGFIDERLAEreAGGDKKKDDDLLLLLDLELDSESE-LTRNHIKALLLDLFVAGTDTTSSTIEWAM 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      270 IELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPL-IILMRVAKGEFEVQGHRIHEGD--LVA 346
Cdd:cd11073 256 AELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPApLLLPRKAEEDVEVMGYTIPKGTqvLVN 335

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      347 ASpAISnRIPEDFPDPHDFVPARYeqprqedLLNRWTW-------IPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEM 419
Cdd:cd11073 336 VW-AIG-RDPSVWEDPLEFKPERF-------LGSEIDFkgrdfelIPFGSGRRICPGLPLAERMVHLVLASLLHSFDWKL 406

                       250       260
                ....*....|....*....|....
1U13_A      420 AQ--PPESY-RNDHSKMVVQLAQP 440
Cdd:cd11073 407 PDgmKPEDLdMEEKFGLTLQKAVP 430
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 203-440 6.18e-24

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 104.16  E-value: 6.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       203 ALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAV 282
Cdd:PLN00110 247 KLLTRMIEEHTASAHERKGNPDFLDVVMANQENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRA 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       283 IDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHP--PLiILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFP 360
Cdd:PLN00110 327 HEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPstPL-NLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWE 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       361 DPHDFVPARYEQPRQEDLL---NRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPESYRNDHSKMVVQL 437
Cdd:PLN00110 406 NPEEFRPERFLSEKNAKIDprgNDFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVELNMDEAFGLALQK 485


                 ...
1U13_A       438 AQP 440
Cdd:PLN00110 486 AVP 488
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 106-434 7.40e-24

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: 102.61  E-value: 7.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      106 RGEQMKGHaatIEDQVRRMIADWGEAGEIDLLDFFA-ELTIyTSSATLIGKKFRDQldGRFAKLYHELERGTDPLAyvdp 184
Cdd:cd11029  96 RVEALRPR---IEEITDELLDALAARGVVDLVADFAyPLPI-TVICELLGVPEEDR--DRFRRWSDALVDTDPPPE---- 165

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      185 ylpiesfrRRDEARNGLVALVADIMNGRIANPptdksDRDMLDVLIAVKAETGtpRFSADEITGMFISMMFAGHHTSSGT 264
Cdd:cd11029 166 --------EAAAALRELVDYLAELVARKRAEP-----GDDLLSALVAARDEGD--RLSEEELVSTVFLLLVAGHETTVNL 230

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      265 ASWTLIELMRHRDAYAAvideldelygdgrsvsfhaLRQIPQL-ENVLKETLRLHPP-LIILMRVAKGEFEVQGHRIHEG 342
Cdd:cd11029 231 IGNGVLALLTHPDQLAL-------------------LRADPELwPAAVEELLRYDGPvALATLRFATEDVEVGGVTIPAG 291

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      343 DLVAASPAISNRIPEDFPDPHDFVPARyeQPRQEdllnrwtwIPFGAGRHRCVGAAFAIMQIKAIFSVLLREY-EFEMAQ 421
Cdd:cd11029 292 EPVLVSLAAANRDPARFPDPDRLDITR--DANGH--------LAFGHGIHYCLGAPLARLEAEIALGALLTRFpDLRLAV 361

                       330
                ....*....|...
1U13_A      422 PPESYRNDHSKMV 434
Cdd:cd11029 362 PPDELRWRPSFLL 374
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 118-401 3.06e-23

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: 101.14  E-value: 3.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      118 EDQVRRMIADW-----GEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDG------RFAKLYHELERGTDpLAYVDPYL 186
Cdd:cd20653  86 RDEIRRLLKRLardskGGFAKVELKPLFSELTFNNIMRMVAGKRYYGEDVSdaeeakLFRELVSEIFELSG-AGNPADFL 164

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      187 PI------ESFRRR--------DEArngLVALVADIMNGRianpptDKSDRDMLDVLIAVKaETgTPRFSADE-ITGMFI 251
Cdd:cd20653 165 PIlrwfdfQGLEKRvkklakrrDAF---LQGLIDEHRKNK------ESGKNTMIDHLLSLQ-ES-QPEYYTDEiIKGLIL 233

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      252 SMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILM-RVAKG 330
Cdd:cd20653 234 VMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVpHESSE 313

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1U13_A      331 EFEVQGHRIHEGD--LVAASpAIsNRIPEDFPDPHDFVPARYEqprQEDLLNRWtWIPFGAGRHRCVGAAFAI 401
Cdd:cd20653 314 DCKIGGYDIPRGTmlLVNAW-AI-HRDPKLWEDPTKFKPERFE---GEEREGYK-LIPFGLGRRACPGAGLAQ 380
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 127-418 6.45e-23

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: 100.52  E-value: 6.45e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      127 DWGEAGEIDLLDFFAELTIYTSSATLIGKKFrDQLDGRFAKLYHELERGTDPLAYVDPYLPI-ESFRRRDEARNGLVALV 205
Cdd:cd11040 115 GGTSTVEVDLYEWLRDVLTRATTEALFGPKL-PELDPDLVEDFWTFDRGLPKLLLGLPRLLArKAYAARDRLLKALEKYY 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      206 ADIMNGRIanpptDKSD--RDMLDVLiavkAETGtprFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVI 283
Cdd:cd11040 194 QAAREERD-----DGSEliRARAKVL----REAG---LSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIR 261

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      284 DELDELYGDGRS-----VSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPED 358
Cdd:cd11040 262 EEIEPAVTPDSGtnailDLTDLLTSCPLLDSTYLETLRLHSSSTSVRLVTEDTVLGGGYLLRKGSLVMIPPRLLHMDPEI 341

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
1U13_A      359 F-PDPHDFVPARYEQPRQEDLLNRW--TWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd11040 342 WgPDPEEFDPERFLKKDGDKKGRGLpgAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVE 404
PLN02183 PLN02183
ferulate 5-hydroxylase
 117-444 6.69e-23

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 101.08  E-value: 6.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       117 IEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSAtlIGKKFRDQLDgRFAKLYHELER--GTDPLAYVDPYL----PIES 190
Cdd:PLN02183 156 VDSMVRSVSSNIGKPVNIGELIFTLTRNITYRAA--FGSSSNEGQD-EFIKILQEFSKlfGAFNVADFIPWLgwidPQGL 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       191 FRRRDEARNGLVALVADIMNGRI-------ANPPTDKSDRDMLDVLIAVKAE----------TGTPRFSADEITGMFISM 253
Cdd:PLN02183 233 NKRLVKARKSLDGFIDDIIDDHIqkrknqnADNDSEEAETDMVDDLLAFYSEeakvnesddlQNSIKLTRDNIKAIIMDV 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       254 MFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFE 333
Cdd:PLN02183 313 MFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAE 392

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       334 VQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLL-NRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLL 412
Cdd:PLN02183 393 VAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVPDFKgSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLL 472

                        330       340       350
                 ....*....|....*....|....*....|....*
1U13_A       413 REYEFEMA---QPPESYRNDhskmVVQLAQPAAVR 444
Cdd:PLN02183 473 HCFTWELPdgmKPSELDMND----VFGLTAPRATR 503
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 89-433 1.50e-22

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 99.62  E-value: 1.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        89 FDASPERrkeMLHNAALRGEQMKGHA--------ATIEDQVRRMIAD-----------WgeagEIDLLDFFAELTIYTSS 149
Cdd:PLN02196 105 FPASKER---MLGKQAIFFHQGDYHAklrklvlrAFMPDAIRNMVPDiesiaqeslnsW----EGTQINTYQEMKTYTFN 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       150 ATLIGKKFRDQLDGR--FAKLYHELERGTDPLAYvdpYLPIESFRRRDEARNGLVALVADIMNGRIANPptdKSDRDMLD 227
Cdd:PLN02196 178 VALLSIFGKDEVLYRedLKRCYYILEKGYNSMPI---NLPGTLFHKSMKARKELAQILAKILSKRRQNG---SSHNDLLG 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       228 VLIAVKAEtgtprFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGD---GRSVSFHALRQI 304
Cdd:PLN02196 252 SFMGDKEG-----LTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDkeeGESLTWEDTKKM 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       305 PQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAasPAISN--RIPEDFPDPHDFVPARYEQPRQEDllnrw 382
Cdd:PLN02196 327 PLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGWKVL--PLFRNihHSADIFSDPGKFDPSRFEVAPKPN----- 399

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
1U13_A       383 TWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPESYRNDHSKM 433
Cdd:PLN02196 400 TFMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIVGTSNGIQYGPFAL 450
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 193-425 6.75e-22

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: 96.87  E-value: 6.75e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      193 RRDEARNGLVALVADIMNGRIANPpTDksdrDMLDVLIAVKAETGtpRFSADEITGMFISMMFAGHHTSSGTASWTLIEL 272
Cdd:cd11031 161 EAEAARQELRGYMAELVAARRAEP-GD----DLLSALVAARDDDD--RLSEEELVTLAVGLLVAGHETTASQIGNGVLLL 233

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      273 MRHRDAYAAvideldelygdgrsvsfhaLRQIPQL-ENVLKETLRLHPP--LIILMRVAKGEFEVQGHRIHEGDLVAASP 349
Cdd:cd11031 234 LRHPEQLAR-------------------LRADPELvPAAVEELLRYIPLgaGGGFPRYATEDVELGGVTIRAGEAVLVSL 294

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1U13_A      350 AISNRIPEDFPDPHDFVPARYEQPRqedllnrwtwIPFGAGRHRCVGAAFAIMQIKAIFSVLLREY-EFEMAQPPES 425
Cdd:cd11031 295 NAANRDPEVFPDPDRLDLDREPNPH----------LAFGHGPHHCLGAPLARLELQVALGALLRRLpGLRLAVPEEE 361
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 104-412 1.66e-21

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: 95.62  E-value: 1.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      104 ALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGkkfrdqLDGRFAKLYHELERGTdpLAYV- 182
Cdd:cd11080  66 AFRGDALDHLLPLIKENAEELIAPFLERGRVDLVNDFGKPFAVNVTMDMLG------LDKRDHEKIHEWHSSV--AAFIt 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      183 ----DPYLPIESFRRRDEARNGLVALVADimngRIANPPTDksdrdMLDVLIAvkAETGTPRFSADEITGMFISMMFAGH 258
Cdd:cd11080 138 slsqDPEARAHGLRCAEQLSQYLLPVIEE----RRVNPGSD-----LISILCT--AEYEGEALSDEDIKALILNVLLAAT 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      259 HTSSGTASWTLIELMRHRDAYAAVideldelygdgrsvsfhalRQIPQL-ENVLKETLRLHPPLIILMRVAKGEFEVQGH 337
Cdd:cd11080 207 EPADKTLALMIYHLLNNPEQLAAV-------------------RADRSLvPRAIAETLRYHPPVQLIPRQASQDVVVSGM 267

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      338 RIHEGDLVAASPAISNRIPEDFPDPHDFVPARyeqprqEDLLNRWTWIP------FGAGRHRCVGAAFAIMQIKAIFSVL 411
Cdd:cd11080 268 EIKKGTTVFCLIGAANRDPAAFEDPDTFNIHR------EDLGIRSAFSGaadhlaFGSGRHFCVGAALAKREIEIVANQV 341


                .
1U13_A      412 L 412
Cdd:cd11080 342 L 342
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 77-434 2.10e-21

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: 95.18  E-value: 2.10e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       77 PFMTPIFGEGVVFDASPERRKEMLHNAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGkk 156
Cdd:cd20630  49 SLARLIKGGLFLLAPEDHARVRKLVAPAFTPRAIDRLRAEIQAIVDQLLDELGEPEEFDVIREIAEHIPFRVISAMLG-- 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      157 FRDQLDGRFAKLYHELERgtdplaYVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPPTDksdrDMLDVLIavKAET 236
Cdd:cd20630 127 VPAEWDEQFRRFGTATIR------LLPPGLDPEELETAAPDVTEGLALIEEVIAERRQAPVED----DLLTTLL--RAEE 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      237 GTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDEldelygdgRSVSFHALRQIPQLENVLKetlr 316
Cdd:cd20630 195 DGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE--------PELLRNALEEVLRWDNFGK---- 262

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      317 lhpplIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRqedllnrwtwIPFGAGRHRCVG 396
Cdd:cd20630 263 -----MGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRRDPNAN----------IAFGYGPHFCIG 327

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
1U13_A      397 AAFAIMQIKAIFSVLLREY-EFEMAQPPE-SYRNDHSKMV 434
Cdd:cd20630 328 AALARLELELAVSTLLRRFpEMELAEPPVfDPHPVLRAIV 367
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 132-416 2.56e-21

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: 95.70  E-value: 2.56e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      132 GEIDLLDFFAELTIYTSSATLIGK-------KFRDQLDGRFAKLYHELERGT------DPLAYVdpyLPIESFRR-RDEA 197
Cdd:cd11063  98 STVDLQDLFFRLTLDSATEFLFGEsvdslkpGGDSPPAARFAEAFDYAQKYLakrlrlGKLLWL---LRDKKFREaCKVV 174

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      198 RNGLVALVADIMNGRIANPPTDKSDR-DMLDVLIAvkaETGTPRFSADEItgmfISMMFAGHHTSSGTASWTLIELMRHR 276
Cdd:cd11063 175 HRFVDPYVDKALARKEESKDEESSDRyVFLDELAK---ETRDPKELRDQL----LNILLAGRDTTASLLSFLFYELARHP 247

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      277 DAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVA-------KGefevqGHR-------IHEG 342
Cdd:cd11063 248 EVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAvrdttlpRG-----GGPdgkspifVPKG 322

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1U13_A      343 DLVAASPAISNRIPEDF-PDPHDFVPARYEqprqEDLLNRWTWIPFGAGRHRCVGAAFAIMQIkAIFSV-LLREYE 416
Cdd:cd11063 323 TRVLYSVYAMHRRKDIWgPDAEEFRPERWE----DLKRPGWEYLPFNGGPRICLGQQFALTEA-SYVLVrLLQTFD 393
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 150-418 5.33e-21

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: 94.91  E-value: 5.33e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      150 ATLIGKKFRDQLDGRFAKLYHelergtDPLAYVDPYLPIEsfRRRD------EARNGLVALVA---DIMNGRIAN----- 215
Cdd:cd20649 168 ARILPNKSRDELNSFFTQCIR------NMIAFRDQQSPEE--RRRDflqlmlDARTSAKFLSVehfDIVNDADESaydgh 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      216 PPTDKSDRDmldvliavKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRS 295
Cdd:cd20649 240 PNSPANEQT--------KPSKQKRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEM 311

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      296 VSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARY-EQPR 374
Cdd:cd20649 312 VDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFtAEAK 391

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
1U13_A      375 QEDllNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd20649 392 QRR--HPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQ 433
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 117-418 1.07e-20

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: 93.82  E-value: 1.07e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      117 IEDQVRRMIADW--GEAGEIDLLDFFAELTIYTSSATLIGKKF--RDQLDGRFAKLYHELERGTDPLAYVDPYLPI---- 188
Cdd:cd20651  84 IQEEAEELIDLLkkGEKGPIQMPDLFNVSVLNVLWAMVAGERYslEDQKLRKLLELVHLLFRNFDMSGGLLNQFPWlrfi 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      189 ----ESFRRRDEARNGLVALVADIMNGRIANPPTDKSdRDMLDVLIA--VKAETGTPRFSADEITGMFISMMFAGHHTSS 262
Cdd:cd20651 164 apefSGYNLLVELNQKLIEFLKEEIKEHKKTYDEDNP-RDLIDAYLRemKKKEPPSSSFTDDQLVMICLDLFIAGSETTS 242

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      263 GTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHP--PLIILMRVAKgEFEVQGHRIH 340
Cdd:cd20651 243 NTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTlvPIGIPHRALK-DTTLGGYRIP 321

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1U13_A      341 EGDLVAASPAISNRIPEDFPDPHDFVPARYEQPrQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd20651 322 KDTTILASLYSVHMDPEYWGDPEEFRPERFLDE-DGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQNFTFS 398
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 34-422 1.39e-20

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: 93.75  E-value: 1.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       34 RDELGDVGTFQLAGKQVVLLSGSHaNEFFFRAGDDDLDQAKaYPFMTPI-FGEGVVFDASPE---RRKEMLHNAALRGeQ 109
Cdd:cd20636  19 REKYGNVFKTHLLGRPVIRVTGAE-NIRKILLGEHTLVSTQ-WPQSTRIlLGSNTLLNSVGElhrQRRKVLARVFSRA-A 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      110 MKGHAATIEDQVRRMIADW-GEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDGRFAKLYHELERGTDPLAyVDpyLPI 188
Cdd:cd20636  96 LESYLPRIQDVVRSEVRGWcRGPGPVAVYTAAKSLTFRIAVRILLGLRLEEQQFTYLAKTFEQLVENLFSLP-LD--VPF 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      189 ESFRRRDEARNGLVALVADIMNGRI-ANPPTDKSDrdMLDVLIAVKAETGTpRFSADEITGMFISMMFAGHHTSSGTASW 267
Cdd:cd20636 173 SGLRKGIKARDILHEYMEKAIEEKLqRQQAAEYCD--ALDYMIHSARENGK-ELTMQELKESAVELIFAAFSTTASASTS 249

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      268 TLIELMRHRDAYAAVIDELDElYGDGRS-------VSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIH 340
Cdd:cd20636 250 LVLLLLQHPSAIEKIRQELVS-HGLIDQcqccpgaLSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQIP 328

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      341 EGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA 420
Cdd:cd20636 329 KGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGRFNYIPFGGGVRSCIGKELAQVILKTLAVELVTTARWELA 408


                ..
1U13_A      421 QP 422
Cdd:cd20636 409 TP 410
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 240-422 1.51e-20

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: 93.28  E-value: 1.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      240 RFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHP 319
Cdd:cd20648 229 KLPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYP 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      320 PLIILMRV-AKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQprQEDLLNRWTWIPFGAGRHRCVGAA 398
Cdd:cd20648 309 VIPGNARViPDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLG--KGDTHHPYASLPFGFGKRSCIGRR 386

                       170       180
                ....*....|....*....|....
1U13_A      399 FAIMQIKAIFSVLLREYEFEMAQP 422
Cdd:cd20648 387 IAELEVYLALARILTHFEVRPEPG 410
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 81-436 1.55e-20

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: 93.25  E-value: 1.55e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       81 PIFGEGVVFDASPE---RRK----EMLHnaalrgEQMKGHAATIEDQVRRMIADW--------GEAGEI----DLLDFFA 141
Cdd:cd20640  56 PLFGGGILTSNGPHwahQRKiiapEFFL------DKVKGMVDLMVDSAQPLLSSWeeridragGMAADIvvdeDLRAFSA 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      142 ELTiytsSATLIGKKFrdqLDGR--FAKLyHELERG---TDPLAYVDP--YLPIESFRRRDEARNGLVALVADIMNGRIA 214
Cdd:cd20640 130 DVI----SRACFGSSY---SKGKeiFSKL-RELQKAvskQSVLFSIPGlrHLPTKSNRKIWELEGEIRSLILEIVKEREE 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      215 NPPTDKsdrdmlDVLIAVKAETGTPRFSADE----ITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELY 290
Cdd:cd20640 202 ECDHEK------DLLQAILEGARSSCDKKAEaedfIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVC 275

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      291 GdGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDF-PDPHDFVPAR 369
Cdd:cd20640 276 K-GGPPDADSLSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPER 354

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      370 YEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAqpPEsYRndHS---KMVVQ 436
Cdd:cd20640 355 FSNGVAAACKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLILSKFSFTLS--PE-YQ--HSpafRLIVE 419
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 181-416 3.84e-20

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: 91.51  E-value: 3.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      181 YVDPYLPIESFRRRDEARNGLVALVADIMNGRIANPPTDksdrdmldvLIA--VKAETGTPRFSADEITGMFISMMFAGH 258
Cdd:cd11032 141 LGDDSFEEEEVEEMAEALRELNAYLLEHLEERRRNPRDD---------LISrlVEAEVDGERLTDEEIVGFAILLLIAGH 211

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      259 HTSSGTASWTLIELMRHRDAYAAVideldelygdgrsvsfhalRQIPQL-ENVLKETLRLHPPLIILMRVAKGEFEVQGH 337
Cdd:cd11032 212 ETTTNLLGNAVLCLDEDPEVAARL-------------------RADPSLiPGAIEEVLRYRPPVQRTARVTTEDVELGGV 272

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1U13_A      338 RIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRqedllnrwtwIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYE 416
Cdd:cd11032 273 TIPAGQLVIAWLASANRDERQFEDPDTFDIDRNPNPH----------LSFGHGIHFCLGAPLARLEARIALEALLDRFP 341
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 38-426 4.97e-20

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: 91.89  E-value: 4.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       38 GDVGTFQLAGKQVVLL-SGSHANEFFFRAGDDDLDQAKAYPFmtPIFGEG---VVF-DASPE---RRKeMLHnAALRGEQ 109
Cdd:cd11027   2 GDVFSLYLGSRLVVVLnSGAAIKEALVKKSADFAGRPKLFTF--DLFSRGgkdIAFgDYSPTwklHRK-LAH-SALRLYA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      110 MKGHA--ATIEDQV----RRMIADWGEAgeIDLLDFFAELTIYTSSATLIGKKFrDQLDGRFAKLYHELERGTDPLAYVD 183
Cdd:cd11027  78 SGGPRleEKIAEEAekllKRLASQEGQP--FDPKDELFLAVLNVICSITFGKRY-KLDDPEFLRLLDLNDKFFELLGAGS 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      184 P--------YLPIESFRRRDEA---RNGLVALVADimNGRIANPPtdKSDRDMLDVLIAVKAE------TGTPRFSADEI 246
Cdd:cd11027 155 LldifpflkYFPNKALRELKELmkeRDEILRKKLE--EHKETFDP--GNIRDLTDALIKAKKEaedegdEDSGLLTDDHL 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      247 TGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILM- 325
Cdd:cd11027 231 VMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALp 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      326 RVAKGEFEVQGHRIHEGDLVaaspaISN-----RIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFA 400
Cdd:cd11027 311 HKTTCDTTLRGYTIPKGTTV-----LVNlwalhHDPKEWDDPDEFRPERFLDENGKLVPKPESFLPFSAGRRVCLGESLA 385

                       410       420
                ....*....|....*....|....*...
1U13_A      401 IMQIKAIFSVLLREYEFEMAQ--PPESY 426
Cdd:cd11027 386 KAELFLFLARLLQKFRFSPPEgePPPEL 413
PLN02936 PLN02936
epsilon-ring hydroxylase
 219-419 1.47e-19

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 91.01  E-value: 1.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       219 DKSDRDMLDVLIAVKAETGTPRFSADeitgmFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGdGRSVSF 298
Cdd:PLN02936 257 NDSDPSVLRFLLASREEVSSVQLRDD-----LLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTY 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       299 HALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQG-HRIHEGDLVAASPAISNRIPEDFPDPHDFVPARY--EQPRQ 375
Cdd:PLN02936 331 EDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGgYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdlDGPVP 410

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
1U13_A       376 EDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEM 419
Cdd:PLN02936 411 NETNTDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLEL 454
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 218-424 2.01e-19

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: 90.37  E-value: 2.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      218 TDKSDRDMLDV-LIAVKAETGTPRFSADE-ITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRS 295
Cdd:cd20654 212 KSKNDEDDDDVmMLSILEDSQISGYDADTvIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRW 291

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      296 VSFHALRQIPQLENVLKETLRLHPPLIILM-RVAKGEFEVQGHRIHEGDLVaaspaISN-----RIPEDFPDPHDFVPAR 369
Cdd:cd20654 292 VEESDIKNLVYLQAIVKETLRLYPPGPLLGpREATEDCTVGGYHVPKGTRL-----LVNvwkiqRDPNVWSDPLEFKPER 366

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
1U13_A      370 Y-EQPRQEDLL-NRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLreYEFEMAQPPE 424
Cdd:cd20654 367 FlTTHKDIDVRgQNFELIPFGSGRRSCPGVSFGLQVMHLTLARLL--HGFDIKTPSN 421
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 117-414 4.86e-19

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: 88.03  E-value: 4.86e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      117 IEDQVRR----MIADWGEAGEIDLLDFFAELTIYTSSATLIGKKFrDQLDgRFAKLYHELERGTDPlayvdpylpiesfR 192
Cdd:cd11035  80 LEPRIREraveLIESFAPRGECDFVADFAEPFPTRVFLELMGLPL-EDLD-RFLEWEDAMLRPDDA-------------E 144

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      193 RRDEARNGLVALVADIMNGRIANPptdksDRDMLDVLIAvkAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIEL 272
Cdd:cd11035 145 ERAAAAQAVLDYLTPLIAERRANP-----GDDLISAILN--AEIDGRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHL 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      273 MRHRDAYAAVIDELDelygdgrsvsfhalrQIPqleNVLKETLRLHPPlIILMRVAKGEFEVQGHRIHEGDLVAASPAIS 352
Cdd:cd11035 218 ARHPEDRRRLREDPE---------------LIP---AAVEELLRRYPL-VNVARIVTRDVEFHGVQLKAGDMVLLPLALA 278

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
1U13_A      353 NRIPEDFPDPHDFVPARyeqprqedllNRWTWIPFGAGRHRCVGAAFAIMQIKaifsVLLRE 414
Cdd:cd11035 279 NRDPREFPDPDTVDFDR----------KPNRHLAFGAGPHRCLGSHLARLELR----IALEE 326
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 192-413 5.09e-19

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: 88.35  E-value: 5.09e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      192 RRRDEARNGLVALVADIMNGRIANPptdksDRDMLDVLIAVKAETGtpRFSADEITGMFISMMFAGHHTSSGTASWTLIE 271
Cdd:cd11030 162 EEAAAAGAELRAYLDELVARKRREP-----GDDLLSRLVAEHGAPG--ELTDEELVGIAVLLLVAGHETTANMIALGTLA 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      272 LMRHRDAYAAVIDEldelygdgrsvsfhalrqiPQL-ENVLKETLRLHP-PLIILMRVAKGEFEVQGHRIHEGDLVAASP 349
Cdd:cd11030 235 LLEHPEQLAALRAD-------------------PSLvPGAVEELLRYLSiVQDGLPRVATEDVEIGGVTIRAGEGVIVSL 295

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
1U13_A      350 AISNRIPEDFPDPHDFVPARyEQPRQedllnrwtwIPFGAGRHRCVGAAFAIMQIKAIFSVLLR 413
Cdd:cd11030 296 PAANRDPAVFPDPDRLDITR-PARRH---------LAFGHGVHQCLGQNLARLELEIALPTLFR 349
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 192-422 6.17e-19

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: 88.80  E-value: 6.17e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      192 RRRDEARNGLVALVADIMNGRIA----NPPTDKSDRDMLDVLIAVKAETGTPrFSADEITGMFISMMFAGHHTSSGTASW 267
Cdd:cd11064 174 KKLREAIRVIDDFVYEVISRRREelnsREEENNVREDLLSRFLASEEEEGEP-VSDKFLRDIVLNFILAGRDTTAAALTW 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      268 TLIELMRHRDAYAAVIDELDELY-----GDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVA-KGEFEVQGHRIHE 341
Cdd:cd11064 253 FFWLLSKNPRVEEKIREELKSKLpklttDESRVPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAvNDDVLPDGTFVKK 332

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      342 GDLVAASPAISNRIPEDF-PDPHDFVPARYeqprqedlLNRWTWI---------PFGAGRHRCVGAAFAIMQIKAIFSVL 411
Cdd:cd11064 333 GTRIVYSIYAMGRMESIWgEDALEFKPERW--------LDEDGGLrpespykfpAFNAGPRICLGKDLAYLQMKIVAAAI 404

                       250
                ....*....|.
1U13_A      412 LREYEFEMAQP 422
Cdd:cd11064 405 LRRFDFKVVPG 415
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 186-425 6.99e-19

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: 88.41  E-value: 6.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      186 LPIESFRRRDEARnglvALVADIMNGRIANpptdKSDR-DMLDVLIavKAETGTPRFSADEITGMFISMMFAGHHTSSGT 264
Cdd:cd11058 167 IPKSLRKKRKEHF----QYTREKVDRRLAK----GTDRpDFMSYIL--RNKDEKKGLTREELEANASLLIIAGSETTATA 236

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      265 ASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPL-IILMR-VAKGEFEVQGHRIHEG 342
Cdd:cd11058 237 LSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQLPYLNAVIQEALRLYPPVpAGLPRvVPAGGATIDGQFVPGG 316

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      343 DLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLN--RWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA 420
Cdd:cd11058 317 TSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFDNdkKEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELD 396


                ....*
1U13_A      421 qpPES 425
Cdd:cd11058 397 --PES 399
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 114-420 8.49e-19

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: 87.39  E-value: 8.49e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      114 AATIEDQVRRMIAD----WGEAGEIDLLDFFAELTIYTSSATLIGkkFRDQLDGRFAklyhelergtdplAYVDPYLPIE 189
Cdd:cd11034  77 VEAFRPRVRQLTNDlidaFIERGECDLVTELANPLPARLTLRLLG--LPDEDGERLR-------------DWVHAILHDE 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      190 SFRRRDEARNGLVALVADIMNGRIANPPTDksdrdMLDVLIAvkAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTL 269
Cdd:cd11034 142 DPEEGAAAFAELFGHLRDLIAERRANPRDD-----LISRLIE--GEIDGKPLSDGEVIGFLTLLLLGGTDTTSSALSGAL 214

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      270 IELMRHRDAYAAVIDELDelygdgrsvsfhalrqipQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASP 349
Cdd:cd11034 215 LWLAQHPEDRRRLIADPS------------------LIPNAVEEFLRFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAF 276

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1U13_A      350 AISNRIPEDFPDPHDFVPARYEQPRqedllnrwtwIPFGAGRHRCVGAAFAIMQIKAIFS-VLLREYEFEMA 420
Cdd:cd11034 277 ASANRDEEKFEDPDRIDIDRTPNRH----------LAFGSGVHRCLGSHLARVEARVALTeVLKRIPDFELD 338
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 242-433 1.66e-18

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: 87.16  E-value: 1.66e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      242 SADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPL 321
Cdd:cd20656 227 SEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPT 306

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      322 -IILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFA 400
Cdd:cd20656 307 pLMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKGHDFRLLPFGAGRRVCPGAQLG 386

                       170       180       190
                ....*....|....*....|....*....|...
1U13_A      401 IMQIKAIFSVLLREYEFemaQPPESYRNDHSKM 433
Cdd:cd20656 387 INLVTLMLGHLLHHFSW---TPPEGTPPEEIDM 416
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 224-424 2.47e-18

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: 86.95  E-value: 2.47e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      224 DMLDVLIAVKAETGTpRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQ 303
Cdd:cd20678 219 DFLDILLFAKDENGK-SLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQ 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      304 IPQLENVLKETLRLHPPLIILMR-VAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYeQPRQEDLLNRW 382
Cdd:cd20678 298 MPYTTMCIKEALRLYPPVPGISReLSKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRF-SPENSSKRHSH 376

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
1U13_A      383 TWIPFGAGRHRCVGAAFAIMQIK-AIFSVLLReyeFEMAQPPE 424
Cdd:cd20678 377 AFLPFSAGPRNCIGQQFAMNEMKvAVALTLLR---FELLPDPT 416
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 244-420 2.83e-18

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: 86.51  E-value: 2.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      244 DEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLII 323
Cdd:cd20647 236 EEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLPG 315

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      324 LMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQ 403
Cdd:cd20647 316 NGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRVDNFGSIPFGYGIRSCIGRRIAELE 395

                       170
                ....*....|....*..
1U13_A      404 IKAIFSVLLREYEFEMA 420
Cdd:cd20647 396 IHLALIQLLQNFEIKVS 412
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 98-421 4.59e-18

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: 86.14  E-value: 4.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       98 EMLHNAALrgeqmKGHAATIEDQVRRMIADWGE-----AGEIDLLDFFAELTIYTSSATLIGKKFRDqldgrfaKLYHEL 172
Cdd:cd11075  74 EVLSPSRL-----KQFRPARRRALDNLVERLREeakenPGPVNVRDHFRHALFSLLLYMCFGERLDE-------ETVREL 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      173 ER----------GTDPLAYVdPYLPIESFRRRDEARNGLVALVADIMNG-------RIANPPTDKSDRD-MLDVLIAVKA 234
Cdd:cd11075 142 ERvqrelllsftDFDVRDFF-PALTWLLNRRRWKKVLELRRRQEEVLLPlirarrkRRASGEADKDYTDfLLLDLLDLKE 220

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      235 ETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKET 314
Cdd:cd11075 221 EGGERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLET 300

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      315 LRLHPPL-IILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWT----WIPFGA 389
Cdd:cd11075 301 LRRHPPGhFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAADIDTGSkeikMMPFGA 380

                       330       340       350
                ....*....|....*....|....*....|..
1U13_A      390 GRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQ 421
Cdd:cd11075 381 GRRICPGLGLATLHLELFVARLVQEFEWKLVE 412
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 74-420 8.02e-18

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: 85.19  E-value: 8.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       74 KAYPFMTPIFGEGVVF----DASPERRkemLHNAALRGEQMKGHAATIEDQVRRMIADW--------GEAGEIDLLDFFA 141
Cdd:cd20641  48 KARPEILKLSGKGLVFvngdDWVRHRR---VLNPAFSMDKLKSMTQVMADCTERMFQEWrkqrnnseTERIEVEVSREFQ 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      142 ELTIYTSSATLIGKKFRDqlDGRFAKLYHELER-GTDPLAYVD----PYLPIESFRRRDEARNGLVALVADIMNGRIANP 216
Cdd:cd20641 125 DLTADIIATTAFGSSYAE--GIEVFLSQLELQKcAAASLTNLYipgtQYLPTPRNLRVWKLEKKVRNSIKRIIDSRLTSE 202

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      217 PTDKSDrDMLDVLI-AVKAETGTPR----FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYG 291
Cdd:cd20641 203 GKGYGD-DLLGLMLeAASSNEGGRRterkMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECG 281

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      292 DGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDF-PDPHDFVPARY 370
Cdd:cd20641 282 KDKIPDADTLSKLKLMNMVLMETLRLYGPVINIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRF 361

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
1U13_A      371 EqprqeDLLNRWTWIP-----FGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA 420
Cdd:cd20641 362 A-----NGVSRAATHPnallsFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLS 411
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 220-398 1.04e-17

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: 85.11  E-value: 1.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      220 KSDRDMLDVLIAVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSfh 299
Cdd:cd20658 212 KEEEDWLDVFITLKDENGNPLLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQ-- 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      300 aLRQIPQLENV---LKETLRLHPPLIILM-RVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQ 375
Cdd:cd20658 290 -ESDIPNLNYVkacAREAFRLHPVAPFNVpHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDS 368

                       170       180
                ....*....|....*....|....*
1U13_A      376 EDLL--NRWTWIPFGAGRHRCVGAA 398
Cdd:cd20658 369 EVTLtePDLRFISFSTGRRGCPGVK 393
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 38-400 1.74e-17

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: 84.17  E-value: 1.74e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       38 GDVGTFQLAGKQVVLLSgSHanefffRAGDDDLD-QAKAY---PFMtPIFGEGVVFDASP----------ERRKeMLHnA 103
Cdd:cd11065   2 GPIISLKVGGQTIIVLN-SP------KAAKDLLEkRSAIYssrPRM-PMAGELMGWGMRLllmpygprwrLHRR-LFH-Q 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      104 ALRGEQMKGHAATIEDQVRRMIADWGEAGEidllDFFAELTIYTSSATLI------GKKFRDQLDGRFAKLYHELERGTD 177
Cdd:cd11065  72 LLNPSAVRKYRPLQELESKQLLRDLLESPD----DFLDHIRRYAASIILRlaygyrVPSYDDPLLRDAEEAMEGFSEAGS 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      178 PLAY-VD--P---YLP---IESFRRR-DEARNGLVALVadimngrianpptdksDRDMLDVLIAVKAETGTPRFSA---- 243
Cdd:cd11065 148 PGAYlVDffPflrYLPswlGAPWKRKaRELRELTRRLY----------------EGPFEAAKERMASGTATPSFVKdlle 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      244 ----------DEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKE 313
Cdd:cd11065 212 eldkegglseEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKE 291

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      314 TLRLHPPLII-LMRVAKGEFEVQGHRIHEG-DLVAASPAIsNRIPEDFPDPHDFVPARYEQPRQE--DLLNRWTWIpFGA 389
Cdd:cd11065 292 VLRWRPVAPLgIPHALTEDDEYEGYFIPKGtTVIPNAWAI-HHDPEVYPDPEEFDPERYLDDPKGtpDPPDPPHFA-FGF 369

                       410
                ....*....|.
1U13_A      390 GRHRCVGAAFA 400
Cdd:cd11065 370 GRRICPGRHLA 380
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 203-425 3.79e-17

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: 83.07  E-value: 3.79e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      203 ALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETG-TPRFSADEItgmfISMMFAGHHTSSGTASWTLIELMRHRDAYAA 281
Cdd:cd11062 185 KQVDEVLRQVSAGDPPSIVTSLFHALLNSDLPPSEkTLERLADEA----QTLIGAGTETTARTLSVATFHLLSNPEILER 260

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      282 VIDELDELYGDGRS-VSFHALRQIPQLENVLKETLRLHPPLII-LMRVA-KGEFEVQGHRIHEGDLVAASPAISNRIPED 358
Cdd:cd11062 261 LREELKTAMPDPDSpPSLAELEKLPYLTAVIKEGLRLSYGVPTrLPRVVpDEGLYYKGWVIPPGTPVSMSSYFVHHDEEI 340

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1U13_A      359 FPDPHDFVPARYEQPRQEDLLNRWtWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPES 425
Cdd:cd11062 341 FPDPHEFRPERWLGAAEKGKLDRY-LVPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYETTEE 406
PLN02738 PLN02738
carotene beta-ring hydroxylase
 222-423 8.30e-17

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 83.04  E-value: 8.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       222 DRDMLDVLIAVKAETGTPRFSADEITgmfisMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDgRSVSFHAL 301
Cdd:PLN02738 373 DPSILHFLLASGDDVSSKQLRDDLMT-----MLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGD-RFPTIEDM 446

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       302 RQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARY--EQPRQEDLL 379
Cdd:PLN02738 447 KKLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWplDGPNPNETN 526

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
1U13_A       380 NRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA--QPP 423
Cdd:PLN02738 527 QNFSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQLApgAPP 572
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 106-423 1.65e-16

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 81.79  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       106 RGEQMKGHAAtieDQVRRMIADWGEAGE----IDLLDFFAELTIYTSSATLIGKKF------RDQLDGRFAKLYHELERG 175
Cdd:PLN03112 141 RLESFAKHRA---EEARHLIQDVWEAAQtgkpVNLREVLGAFSMNNVTRMLLGKQYfgaesaGPKEAMEFMHITHELFRL 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       176 TDPLaYVDPYLPI--------------ESFRRRDEARNGLVALVADIMNGRIANpptdKSDRDMLDVLIAVKAETGTPRF 241
Cdd:PLN03112 218 LGVI-YLGDYLPAwrwldpygcekkmrEVEKRVDEFHDKIIDEHRRARSGKLPG----GKDMDFVDVLLSLPGENGKEHM 292

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       242 SADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHP-- 319
Cdd:PLN03112 293 DDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPag 372

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       320 PLII---LMRVAKgefeVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARY---EQPRQEDL-LNRWTWIPFGAGRH 392
Cdd:PLN03112 373 PFLIpheSLRATT----INGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHwpaEGSRVEIShGPDFKILPFSAGKR 448

                        330       340       350
                 ....*....|....*....|....*....|..
1U13_A       393 RCVGaafAIMQIKAIFSVLLREYE-FEMAQPP 423
Cdd:PLN03112 449 KCPG---APLGVTMVLMALARLFHcFDWSPPD 477
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 224-413 2.04e-16

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: 80.89  E-value: 2.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      224 DMLDVLIAVKAETGTpRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRS--VSFHAL 301
Cdd:cd20679 224 DFIDVLLLSKDEDGK-ELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPeeIEWDDL 302

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      302 RQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHR-IHEGDLVAASPAISNRIPEDFPDPHDFVPARYEqprQEDLLN 380
Cdd:cd20679 303 AQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLPDGRvIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFD---PENSQG 379

                       170       180       190
                ....*....|....*....|....*....|....*.
1U13_A      381 R--WTWIPFGAGRHRCVGAAFAIMQIKAIFSV-LLR 413
Cdd:cd20679 380 RspLAFIPFSAGPRNCIGQTFAMAEMKVVLALtLLR 415
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 186-420 3.09e-16

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: 80.28  E-value: 3.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      186 LPIESFRRRDEARNGLVALVADIMNGRIANPpTDKSDRDMLDVLIAVKAETGTpRFSADEITGMFISMMFAGHHTSSGTA 265
Cdd:cd20637 169 LPFSGYRRGIRARDSLQKSLEKAIREKLQGT-QGKDYADALDILIESAKEHGK-ELTMQELKDSTIELIFAAFATTASAS 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      266 SWTLIELMRHrdayAAVIDEL-DELYGDG---------RSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQ 335
Cdd:cd20637 247 TSLIMQLLKH----PGVLEKLrEELRSNGilhngclceGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELD 322

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      336 GHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREY 415
Cdd:cd20637 323 GFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELASTS 402


                ....*
1U13_A      416 EFEMA 420
Cdd:cd20637 403 RFELA 407
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 186-424 3.61e-16

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: 80.50  E-value: 3.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      186 LPIESFRRRDEARNglvALVADIMNGRIanpptdkSDRDMLDVLIAVKAET--GTPRFSADEITGMFISMMFAGHHTSSG 263
Cdd:cd20631 176 LPIHMFKTAKSARE---ALAERLLHENL-------QKRENISELISLRMLLndTLSTLDEMEKARTHVAMLWASQANTLP 245

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      264 TASWTLIELMRHRDAYAAVIDELDELYG--------DGRSVSF--HALRQIPQLENVLKETLRLHPPLIILmRVAKGEFE 333
Cdd:cd20631 246 ATFWSLFYLLRCPEAMKAATKEVKRTLEktgqkvsdGGNPIVLtrEQLDDMPVLGSIIKEALRLSSASLNI-RVAKEDFT 324

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      334 V-----QGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLN--------RWTWIPFGAGRHRCVGAAFA 400
Cdd:cd20631 325 LhldsgESYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTfykngrklKYYYMPFGSGTSKCPGRFFA 404

                       250       260
                ....*....|....*....|....*...
1U13_A      401 IMQIKAIFSVLLREYEFEM----AQPPE 424
Cdd:cd20631 405 INEIKQFLSLMLCYFDMELldgnAKCPP 432
PLN02971 PLN02971
tryptophan N-hydroxylase
 224-421 8.23e-16

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 79.70  E-value: 8.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       224 DMLDVLIAVKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQ 303
Cdd:PLN02971 306 DFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPK 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       304 IPQLENVLKETLRLHPPLII-LMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLL--N 380
Cdd:PLN02971 386 LNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLteN 465

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
1U13_A       381 RWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQ 421
Cdd:PLN02971 466 DLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAG 506
PTZ00404 PTZ00404
cytochrome P450; Provisional
 223-417 9.58e-16

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 79.00  E-value: 9.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       223 RDMLDVLIAvkaETGTprfSADE----ITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSF 298
Cdd:PTZ00404 263 RDLLDLLIK---EYGT---NTDDdilsILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLL 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       299 HALRQIPQLENVLKETLRLHPPLII-LMRVAKGEFEV-QGHRIHEGDLVAAS-PAISnRIPEDFPDPHDFVPARYEQPRQ 375
Cdd:PTZ00404 337 SDRQSTPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIgGGHFIPKDAQILINyYSLG-RNEKYFENPEQFDPSRFLNPDS 415

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
1U13_A       376 EDllnrwTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEF 417
Cdd:PTZ00404 416 ND-----AFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKL 452
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 223-418 1.01e-15

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: 78.88  E-value: 1.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      223 RDMLDVLIAVKAETGTPRFSADEITGMFI-SMMF----AGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVS 297
Cdd:cd11028 204 RDITDALIKASEEKPEEEKPEVGLTDEHIiSTVQdlfgAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPR 283

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      298 FHALRQIPQLENVLKETLRlHP---PLIIlMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPR 374
Cdd:cd11028 284 LSDRPNLPYTEAFILETMR-HSsfvPFTI-PHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDN 361

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
1U13_A      375 QE---DLLNRwtWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd11028 362 GLldkTKVDK--FLPFGAGRRRCLGEELARMELFLFFATLLQQCEFS 406
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 69-440 2.51e-15

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: 77.71  E-value: 2.51e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       69 DLDQAKAYPFMTpIFGEGVV-FDASPERRKEMLHNAALRGEQMKGHAATIEDQVRRMIADWGE------AGEIDLLDFFA 141
Cdd:cd20642  42 DFQKPKTNPLTK-LLATGLAsYEGDKWAKHRKIINPAFHLEKLKNMLPAFYLSCSEMISKWEKlvsskgSCELDVWPELQ 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      142 ELTIYTSSATLIGKKFRDqlDGRFAKLYHEL-ERGTDPL--AYVdP---YLPIESFRRRDEARNGLVALVADIMNGRI-- 213
Cdd:cd20642 121 NLTSDVISRTAFGSSYEE--GKKIFELQKEQgELIIQALrkVYI-PgwrFLPTKRNRRMKEIEKEIRSSLRGIINKREka 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      214 ---ANPPTDksdrDMLDVLIavKAETGTPRFSADEITGMFISMM--------FAGHHTSSGTASWTLIELMRHRDAYAAV 282
Cdd:cd20642 198 mkaGEATND----DLLGILL--ESNHKEIKEQGNKNGGMSTEDVieecklfyFAGQETTSVLLVWTMVLLSQHPDWQERA 271

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      283 IDELDELYGDGRSvSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPE---Df 359
Cdd:cd20642 272 REEVLQVFGNNKP-DFEGLNHLKVVTMILYEVLRLYPPVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPElwgD- 349

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      360 pDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQppeSYRndHSKMVVQLAQ 439
Cdd:cd20642 350 -DAKEFNPERFAEGISKATKGQVSYFPFGWGPRICIGQNFALLEAKMALALILQRFSFELSP---SYV--HAPYTVLTLQ 423


                .
1U13_A      440 P 440
Cdd:cd20642 424 P 424
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 188-417 2.67e-15

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: 77.37  E-value: 2.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      188 IESFRRRDEARNGLVALVADIMNGRianPPTDK-SDRDMldvlIAVKAEtgtprfsadeitgmfisMMFAGHHTSSGTAS 266
Cdd:cd11076 190 IEEHRAKRSNRARDDEDDVDVLLSL---QGEEKlSDSDM----IAVLWE-----------------MIFRGTDTVAILTE 245

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      267 WTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHP--PLIILMRVAKGEFEVQGHRIHEGdl 344
Cdd:cd11076 246 WIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPpgPLLSWARLAIHDVTVGGHVVPAG-- 323

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      345 vaaSPAISN-----RIPEDFPDPHDFVPARY-EQPRQEDLLNRWTWI---PFGAGRHRCVGAAFAIMQIKAIFSVLLREY 415
Cdd:cd11076 324 ---TTAMVNmwaitHDPHVWEDPLEFKPERFvAAEGGADVSVLGSDLrlaPFGAGRRVCPGKALGLATVHLWVAQLLHEF 400


                ..
1U13_A      416 EF 417
Cdd:cd11076 401 EW 402
PLN02290 PLN02290
cytokinin trans-hydroxylase
 255-440 3.10e-15

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 77.55  E-value: 3.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       255 FAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGdGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEV 334
Cdd:PLN02290 326 FAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCG-GETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKL 404

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       335 QGHRIHEGdLVAASPAISNRIPEDF--PDPHDFVPARYEQPRqedLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLL 412
Cdd:PLN02290 405 GDLHIPKG-LSIWIPVLAIHHSEELwgKDANEFNPDRFAGRP---FAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLI 480

                        170       180
                 ....*....|....*....|....*...
1U13_A       413 REYEFEMAqppESYRndHSKMVVQLAQP 440
Cdd:PLN02290 481 SKFSFTIS---DNYR--HAPVVVLTIKP 503
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 5-429 6.11e-15

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 76.65  E-value: 6.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A         5 ALPRVSGGHdehgHLEEFrtDPIGLMQRVRDELGDVGTFQLAGKQVVLLSGSHANEFFFRAGDDDL--------DQAKAY 76
Cdd:PLN03234  35 GLPIIGNLH----QMEKF--NPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFtarpllkgQQTMSY 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        77 PFMTPIFGEgvvFDASPERRKEMLHNAALRGEQMKGHAATIEDQVRRMI------ADwgEAGEIDLLDFFAELTIYTSSA 150
Cdd:PLN03234 109 QGRELGFGQ---YTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMdkiykaAD--QSGTVDLSELLLSFTNCVVCR 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       151 TLIGKKFRDQLD--GRFAKLYHELERGTDPLAYVDPYlPIESF--------RRRDEARNGLVALVADIMNGRI-ANPPTD 219
Cdd:PLN03234 184 QAFGKRYNEYGTemKRFIDILYETQALLGTLFFSDLF-PYFGFldnltglsARLKKAFKELDTYLQELLDETLdPNRPKQ 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       220 KSDrDMLDVLIAV-KAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSF 298
Cdd:PLN03234 263 ETE-SFIDLLMQIyKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSE 341

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       299 HALRQIPQLENVLKETLRLHPPL-IILMRVAKGEFEVQGHRIHEGDLVAASP-AISNRIPEDFPDPHDFVPARY-EQPRQ 375
Cdd:PLN03234 342 EDIPNLPYLKAVIKESLRLEPVIpILLHRETIADAKIGGYDIPAKTIIQVNAwAVSRDTAAWGDNPNEFIPERFmKEHKG 421

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
1U13_A       376 EDLLNR-WTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLreYEFEMAQP----PESYRND 429
Cdd:PLN03234 422 VDFKGQdFELLPFGSGRRMCPAMHLGIAMVEIPFANLL--YKFDWSLPkgikPEDIKMD 478
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 154-420 1.71e-14

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: 75.20  E-value: 1.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      154 GKKFrDQLDGRFAKLYHELERGTD-----PLAYVDP-----YLPIESFRRRDEARNGLVALVADIMNGR-----IANPpt 218
Cdd:cd20666 125 GRRF-DYQDVEFKTMLGLMSRGLEisvnsAAILVNIcpwlyYLPFGPFRELRQIEKDITAFLKKIIADHretldPANP-- 201

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      219 dksdRDMLDV-LIAVKAE---TGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGR 294
Cdd:cd20666 202 ----RDFIDMyLLHIEEEqknNAESSFNEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDR 277

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      295 SVSFHALRQIPQLENVLKETLRLHP--PLIIlMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQ 372
Cdd:cd20666 278 APSLTDKAQMPFTEATIMEVQRMTVvvPLSI-PHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLD 356

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
1U13_A      373 pRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA 420
Cdd:cd20666 357 -ENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLP 403
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 218-424 2.27e-14

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: 74.66  E-value: 2.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      218 TDKSDRDMLDVLIAVK--AETGTPRFSADE--ITGMFISM----MF-AGHHTSSGTASWTLIELMRHRDAYAAVIDELDE 288
Cdd:cd20673 196 SSDSIRDLLDALLQAKmnAENNNAGPDQDSvgLSDDHILMtvgdIFgAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQ 275

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      289 LYGDGRSVSFHALRQIPQLENVLKETLRLHP--PLII----LMRVAKGEFEV-QGHRI--------HEgdlvaaspaisn 353
Cdd:cd20673 276 NIGFSRTPTLSDRNHLPLLEATIREVLRIRPvaPLLIphvaLQDSSIGEFTIpKGTRVvinlwalhHD------------ 343

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1U13_A      354 riPEDFPDPHDFVPARYEQPRQEDLLN-RWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEM---AQPPE 424
Cdd:cd20673 344 --EKEWDQPDQFMPERFLDPTGSQLISpSLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLEVpdgGQLPS 416
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 244-418 2.27e-14

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: 75.03  E-value: 2.27e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      244 DEITGMFIsmmfAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELY----GDGRSVSFHALRQ--IPQLENVLKETLRL 317
Cdd:cd20622 265 DELFGYLI----AGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHpeavAEGRLPTAQEIAQarIPYLDAVIEEILRC 340

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      318 HPPLIILMRVAKGEFEVQGHRIHEGD---LVAASPAISNRIPE--------------------DFPDPHDFVPARY--EQ 372
Cdd:cd20622 341 ANTAPILSREATVDTQVLGYSIPKGTnvfLLNNGPSYLSPPIEidesrrssssaakgkkagvwDSKDIADFDPERWlvTD 420

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1U13_A      373 PRQEDLL---NRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd20622 421 EETGETVfdpSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELL 469
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 220-425 3.00e-14

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: 74.37  E-value: 3.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      220 KSDRDMLDVLIA----VKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRS 295
Cdd:cd20674 197 GQWRDMTDYMLQglgqPRGEKGMGQLLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGAS 276

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      296 VSFHALRQIPQLENVLKETLRLHP--PLIILMRVAKGEfEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQP 373
Cdd:cd20674 277 PSYKDRARLPLLNATIAEVLRLRPvvPLALPHRTTRDS-SIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEP 355

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
1U13_A      374 RQEdllNRWTwIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEmaqPPES 425
Cdd:cd20674 356 GAA---NRAL-LPFGCGARVCLGEPLARLELFVFLARLLQAFTLL---PPSD 400
PLN02966 PLN02966
cytochrome P450 83A1
 118-435 3.08e-14

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 74.78  E-value: 3.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       118 EDQVRRMIADWGEAGE----IDLLDFFAELTIYTSSATLIGKKFRDqlDGRFAKLYHELERGT----------------- 176
Cdd:PLN02966 148 EEEARRMMDKINKAADksevVDISELMLTFTNSVVCRQAFGKKYNE--DGEEMKRFIKILYGTqsvlgkiffsdffpycg 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       177 --DPLAYVDPYLPiESFRRRDEArngLVALVADIMNGRIANPPTDKsdrdMLDVLIAV-KAETGTPRFSADEITGMFISM 253
Cdd:PLN02966 226 flDDLSGLTAYMK-ECFERQDTY---IQEVVNETLDPKRVKPETES----MIDLLMEIyKEQPFASEFTVDNVKAVILDI 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       254 MFAGHHTSSGTASWTLIELMRH----RDAYAAVIDELDElygDGRS-VSFHALRQIPQLENVLKETLRLHPPLIILM-RV 327
Cdd:PLN02966 298 VVAGTDTAAAAVVWGMTYLMKYpqvlKKAQAEVREYMKE---KGSTfVTEDDVKNLPYFRALVKETLRIEPVIPLLIpRA 374

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       328 AKGEFEVQGHRIHEGDLVAASP-AISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKA 406
Cdd:PLN02966 375 CIQDTKIAGYDIPAGTTVNVNAwAVSRDEKEWGPNPDEFRPERFLEKEVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEV 454

                        330       340
                 ....*....|....*....|....*....
1U13_A       407 IFSVLLREYEFEMaqpPESYRNDHSKMVV 435
Cdd:PLN02966 455 PYANLLLNFNFKL---PNGMKPDDINMDV 480
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 240-416 3.48e-14

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: 73.93  E-value: 3.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      240 RFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHP 319
Cdd:cd20646 228 KLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYP 307

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      320 PLIILMRV-AKGEFEVQGHRIHEGDL-VAASPAISnRIPEDFPDPHDFVPARY---EQPRQedllNRWTWIPFGAGRHRC 394
Cdd:cd20646 308 VVPGNARViVEKEVVVGDYLFPKNTLfHLCHYAVS-HDETNFPEPERFKPERWlrdGGLKH----HPFGSIPFGYGVRAC 382

                       170       180
                ....*....|....*....|..
1U13_A      395 VGAAFAIMQIKAIFSVLLREYE 416
Cdd:cd20646 383 VGRRIAELEMYLALSRLIKRFE 404
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 242-415 9.87e-14

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: 72.78  E-value: 9.87e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      242 SADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDgRSVSFHALRQIPQLENVLKETLRLHPPL 321
Cdd:cd20616 221 TAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGE-RDIQNDDLQKLKVLENFINESMRYQPVV 299

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      322 IILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIpEDFPDPHDF--------VPARYEQPrqedllnrwtwipFGAGRHR 393
Cdd:cd20616 300 DFVMRKALEDDVIDGYPVKKGTNIILNIGRMHRL-EFFPKPNEFtlenfeknVPSRYFQP-------------FGFGPRS 365

                       170       180
                ....*....|....*....|..
1U13_A      394 CVGAAFAIMQIKAIFSVLLREY 415
Cdd:cd20616 366 CVGKYIAMVMMKAILVTLLRRF 387
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 267-423 1.15e-13

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 72.84  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       267 WTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIIL-----MRVAKgefeVQGHRI-H 340
Cdd:PLN02394 315 WGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLvphmnLEDAK----LGGYDIpA 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       341 EGDLVAASPAISNRiPEDFPDPHDFVPARY--EQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLReyEFE 418
Cdd:PLN02394 391 ESKILVNAWWLANN-PELWKNPEEFRPERFleEEAKVEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQ--NFE 467


                 ....*
1U13_A       419 MAQPP 423
Cdd:PLN02394 468 LLPPP 472
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 244-424 1.28e-13

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: 72.44  E-value: 1.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      244 DEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLII 323
Cdd:cd20643 233 EDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVS 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      324 LMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYeqPRQEDllNRWTWIPFGAGRHRCVGAAFAIMQ 403
Cdd:cd20643 313 LQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERW--LSKDI--THFRNLGFGFGPRQCLGRRIAETE 388

                       170       180
                ....*....|....*....|.
1U13_A      404 IKAIFSVLLREYEFEMAQPPE 424
Cdd:cd20643 389 MQLFLIHMLENFKIETQRLVE 409
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 234-424 3.95e-13

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: 70.86  E-value: 3.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      234 AETGTPRFSADEItgMFisMMFAGHHTSSGTAS-WTLIELMRHRDAYAAVIDELDELYGDGR----------SVSFHALR 302
Cdd:cd20633 216 AEHGMPEYMQDRF--MF--LLLWASQGNTGPASfWLLLYLLKHPEAMKAVREEVEQVLKETGqevkpggpliNLTRDMLL 291

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      303 QIPQLENVLKETLRLH--PpliILMRVAKGEFEV-----QGHRIHEGDLVAASPAISNRI-PEDFPDPHDFVPARYEQP- 373
Cdd:cd20633 292 KTPVLDSAVEETLRLTaaP---VLIRAVVQDMTLkmangREYALRKGDRLALFPYLAVQMdPEIHPEPHTFKYDRFLNPd 368

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
1U13_A      374 --RQEDLLN-----RWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPE 424
Cdd:cd20633 369 ggKKKDFYKngkklKYYNMPWGAGVSICPGRFFAVNEMKQFVFLMLTYFDLELVNPDE 426
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 301-425 4.64e-13

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: 70.08  E-value: 4.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      301 LRQIP-QLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARyeqpRQEDLL 379
Cdd:cd11079 220 LRANPaLLPAAIDEILRLDDPFVANRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR----HAADNL 295

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
1U13_A      380 NrwtwipFGAGRHRCVGAAFAIMQIKAIFSVLLREYE---------FEMAQPPES 425
Cdd:cd11079 296 V------YGRGIHVCPGAPLARLELRILLEELLAQTEaitlaaggpPERATYPVG 344
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 223-425 5.06e-13

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: 70.67  E-value: 5.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      223 RDMLDV-LIAVKAETGTPR--FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFH 299
Cdd:cd11026 201 RDFIDCfLLKMEKEKDNPNseFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLE 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      300 ALRQIPQLENVLKETLRLHP--PLIILMRVAKgEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARY--EQPRq 375
Cdd:cd11026 281 DRAKMPYTDAVIHEVQRFGDivPLGVPHAVTR-DTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFldEQGK- 358

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
1U13_A      376 edLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPES 425
Cdd:cd11026 359 --FKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSPVGPKD 406
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 242-418 7.14e-13

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: 69.87  E-value: 7.14e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      242 SADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPL 321
Cdd:cd20644 229 SLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVG 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      322 IILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDllNRWTWIPFGAGRHRCVGAAFAI 401
Cdd:cd20644 309 ITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSG--RNFKHLAFGFGMRQCLGRRLAE 386

                       170
                ....*....|....*..
1U13_A      402 MQIKAIFSVLLREYEFE 418
Cdd:cd20644 387 AEMLLLLMHVLKNFLVE 403
PLN03018 PLN03018
homomethionine N-hydroxylase
 39-440 1.15e-12

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 69.66  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        39 DVGTFQLAGKQVVLLSGSHANEFFFRAGDDDLDQAKAYPFMTPIFGEGVVFDASPERRKEMLHNAALRGEQMKGHAATIE 118
Cdd:PLN03018  77 DIACFNFAGTHTITINSDEIAREAFRERDADLADRPQLSIMETIGDNYKSMGTSPYGEQFMKMKKVITTEIMSVKTLNML 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       119 DQVRRMIAD---------WGEAGEIDLLDFFAELTIYTSSATLIGKK-------FRDqlDGRFAKL-YHELE-------- 173
Cdd:PLN03018 157 EAARTIEADnliayihsmYQRSETVDVRELSRVYGYAVTMRMLFGRRhvtkenvFSD--DGRLGKAeKHHLEvifntlnc 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       174 -RGTDPLAYVDPYLPIESFRRRDEARNGLVALVAD----IMNGRIA---NPPTDKSDRDMLDVLIAVKAETGTPRFSADE 245
Cdd:PLN03018 235 lPGFSPVDYVERWLRGWNIDGQEERAKVNVNLVRSynnpIIDERVElwrEKGGKAAVEDWLDTFITLKDQNGKYLVTPDE 314

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       246 ITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPL-IIL 324
Cdd:PLN03018 315 IKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAhYVP 394

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       325 MRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQ----PRQEDLL-NRWTWIPFGAGRHRCVGAAF 399
Cdd:PLN03018 395 PHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQgdgiTKEVTLVeTEMRFVSFSTGRRGCVGVKV 474

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
1U13_A       400 AIMQIKAIFSVLLREYEFEMAQP--PESYRNDHSKMVvqLAQP 440
Cdd:PLN03018 475 GTIMMVMMLARFLQGFNWKLHQDfgPLSLEEDDASLL--MAKP 515
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 208-434 1.24e-12

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: 69.10  E-value: 1.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      208 IMNGRIANPPTDKSD-RDMLDVLIAVKAETG---TPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVI 283
Cdd:cd20667 184 IKKEVIRHELRTNEApQDFIDCYLAQITKTKddpVSTFSEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQ 263

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      284 DELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLII-LMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDP 362
Cdd:cd20667 264 QELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVgAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETP 343

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1U13_A      363 HDFVPARYEQpRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMaqpPESYRNDHSKMV 434
Cdd:cd20667 344 HKFNPGHFLD-KDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQL---PEGVQELNLEYV 411
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 256-418 1.30e-12

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: 69.25  E-value: 1.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      256 AGHH-----TSSG----TASWTLIELMRHRDAYAAVIDELDELY---GDGRSVSF------HALRQIPQLENVLKETLRL 317
Cdd:cd20632 217 AAHHfaflwASVGntipATFWAMYYLLRHPEALAAVRDEIDHVLqstGQELGPDFdihltrEQLDSLVYLESAINESLRL 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      318 HPPLIILmRVAKGEFEVQ---GHRIH--EGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQE---------DLlnRWT 383
Cdd:cd20632 297 SSASMNI-RVVQEDFTLKlesDGSVNlrKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKkttfykrgqKL--KYY 373

                       170       180       190
                ....*....|....*....|....*....|....*
1U13_A      384 WIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd20632 374 LMPFGSGSSKCPGRFFAVNEIKQFLSLLLLYFDLE 408
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 280-416 1.39e-12

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: 69.21  E-value: 1.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      280 AAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGH----RIHEGDLVAASPAISNRI 355
Cdd:cd11071 261 ARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIESHdasyKIKKGELLVGYQPLATRD 340

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1U13_A      356 PEDFPDPHDFVPARYEQPRQEdLLNRWTW------IPFGAGRHRCVGAAFAIMQIKAIFSVLLREYE 416
Cdd:cd11071 341 PKVFDNPDEFVPDRFMGEEGK-LLKHLIWsngpetEEPTPDNKQCPGKDLVVLLARLFVAELFLRYD 406
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 242-424 5.02e-12

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: 67.22  E-value: 5.02e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      242 SADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAvideldelygdgrsvsfhaLRQIPQL-ENVLKETLRLHPP 320
Cdd:cd11037 199 TEDEAPLLMRDYLSAGLDTTISAIGNALWLLARHPDQWER-------------------LRADPSLaPNAFEEAVRLESP 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      321 LIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARyeQPRQEdllnrwtwIPFGAGRHRCVGAAFA 400
Cdd:cd11037 260 VQTFSRTTTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR--NPSGH--------VGFGHGVHACVGQHLA 329

                       170       180
                ....*....|....*....|....*
1U13_A      401 IMQIKAIFSVLLREYE-FEMAQPPE 424
Cdd:cd11037 330 RLEGEALLTALARRVDrIELAGPPV 354
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 22-433 5.75e-12

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: 67.17  E-value: 5.75e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       22 FRTDPIGLMQRVRDELG-DVGTFQLAGKQVVLLSGSHANEFFFraGDDDLDQAKAYPFMT--PIFGEGVVF---DASPER 95
Cdd:cd11067   6 LLREGYRFISNRCRRLGsDAFRTRLMGRPAICLRGPEAARLFY--DEDRFTRKGAMPPRVqkTLFGKGGVQgldGEAHRH 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       96 RKEMLhNAALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFfAELTIYTSSATLIGKKFRDqldgrfaklyHELERG 175
Cdd:cd11067  84 RKAMF-MSLMTPERVARLARLFRREWRAALARWEGRDEVVLFDE-AQEVLTRAACRWAGVPLPE----------EDVERR 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      176 TDPLAYVdpylpIESF-------------RRRDEARngLVALVADIMNGRIANPPTDksdrdMLDVLIAVKAETGTP--- 239
Cdd:cd11067 152 ARDLAAM-----IDGAgavgprhwrarlaRRRAERW--AAELIEDVRAGRLAPPEGT-----PLAAIAHHRDPDGELlpe 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      240 RFSADEITGMF-----IS--MMFAGHHtssgtaswtlieLMRHRDAYAAVIDELDELygdgrsvsfhalrqipqLENVLK 312
Cdd:cd11067 220 RVAAVELLNLLrptvaVArfVTFAALA------------LHEHPEWRERLRSGDEDY-----------------AEAFVQ 270

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      313 ETLRLHP--PLiiLMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQedllNRWTWIPFGAG 390
Cdd:cd11067 271 EVRRFYPffPF--VGARARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEG----DPFDFIPQGGG 344

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
1U13_A      391 R----HRCVGAAFAIMQIKAIFSVLLREYEFEMaqPPESYRNDHSKM 433
Cdd:cd11067 345 DhatgHRCPGEWITIALMKEALRLLARRDYYDV--PPQDLSIDLNRM 389
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 149-423 5.79e-12

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: 67.26  E-value: 5.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      149 SATLIGKKFrDQLDGRFAKLYHELERG----TDPLAYV-DPYLPI-ESFRRRDEARNGLVALVADIMNGRI-ANPPT-DK 220
Cdd:cd20670 119 SSVVFGSRF-DYEDKQFLSLLRMINESfiemSTPWAQLyDMYSGImQYLPGRHNRIYYLIEELKDFIASRVkINEASlDP 197

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      221 SD-RDMLDV-LIAVKAETGTPR--FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSV 296
Cdd:cd20670 198 QNpRDFIDCfLIKMHQDKNNPHteFNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLP 277

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      297 SFHALRQIPQLENVLKETLRLHP--PLIILMRVAKgEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARY--EQ 372
Cdd:cd20670 278 SVDDRVKMPYTDAVIHEIQRLTDivPLGVPHNVIR-DTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFldEQ 356

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
1U13_A      373 PRqedLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPP 423
Cdd:cd20670 357 GR---FKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSLRSLVPP 404
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 221-424 5.89e-12

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: 67.13  E-value: 5.89e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      221 SDRDMLD-VLIAVKAETGTPR--FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVS 297
Cdd:cd20668 199 SPRDFIDsFLIRMQEEKKNPNteFYMKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPK 278

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      298 FHALRQIPQLENVLKETLRLHP--PLIILMRVAKgEFEVQGHRIHEGDLVAasPAISN--RIPEDFPDPHDFVPARYEQP 373
Cdd:cd20668 279 FEDRAKMPYTEAVIHEIQRFGDviPMGLARRVTK-DTKFRDFFLPKGTEVF--PMLGSvlKDPKFFSNPKDFNPQHFLDD 355

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
1U13_A      374 RQEdLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPE 424
Cdd:cd20668 356 KGQ-FKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFKSPQSPE 405
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 78-421 6.59e-12

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 67.31  E-value: 6.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        78 FMTPIFGEGVVFDASPERRKEMLHNAA-------------LRGEQ----MKG------HAATIEDQVRRMIADWGEAgEI 134
Cdd:PLN02987  71 FMTHLFGEPTVFSADPETNRFILQNEGklfecsypgsisnLLGKHslllMKGnlhkkmHSLTMSFANSSIIKDHLLL-DI 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       135 DLLDFFaELTIYTSSATLIGKKFRDQLDGRFAKLYhelerGTDPLAYVDPY-----LPIESF------------RRRDEA 197
Cdd:PLN02987 150 DRLIRF-NLDSWSSRVLLMEEAKKITFELTVKQLM-----SFDPGEWTESLrkeyvLVIEGFfsvplplfsttyRRAIQA 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       198 RNGLV-ALVADIMNGRIANPPTDKSDRDMLDVLIAvkAETGtprFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHR 276
Cdd:PLN02987 224 RTKVAeALTLVVMKRRKEEEEGAEKKKDMLAALLA--SDDG---FSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETP 298

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       277 DAYAAVIDELDELYG---DGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISN 353
Cdd:PLN02987 299 LALAQLKEEHEKIRAmksDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVH 378

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
1U13_A       354 RIPEDFPDPHDFVPARYeQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQ 421
Cdd:PLN02987 379 LDHEYFKDARTFNPWRW-QSNSGTTVPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSWVPAE 445
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
 300-414 7.51e-12

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: 66.36  E-value: 7.51e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      300 ALRQIPQL-ENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQedl 378
Cdd:cd11036 213 RLRPDPELaAAAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGRPTARSA--- 289

                        90       100       110
                ....*....|....*....|....*....|....*.
1U13_A      379 lnrwtwiPFGAGRHRCVGAAFAIMQIKAIFSVLLRE 414
Cdd:cd11036 290 -------HFGLGRHACLGAALARAAAAAALRALAAR 318
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 38-423 8.26e-12

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: 66.75  E-value: 8.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       38 GDVGTFQLAGKQVVLLSG---------SHANEFffraGDDDLdqakaypfmTPIF-----GEGVVFdASPERRKEMLHNA 103
Cdd:cd20664   2 GSIFTVQMGTKKVVVLAGyktvkealvNHAEAF----GGRPI---------IPIFedfnkGYGILF-SNGENWKEMRRFT 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      104 ALRGEQMKGHAATIEDQVRRMIADWGEAGEIDLLDFFaELTIYTSSAT-------LIGKKFRDQlDGRFAKL----YHEL 172
Cdd:cd20664  68 LTTLRDFGMGKKTSEDKILEEIPYLIEVFEKHKGKPF-ETTLSMNVAVsniiasiVLGHRFEYT-DPTLLRMvdriNENM 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      173 ERGTDPLAYVDPYLPIESFRRRDeaRNGLVALVADIMNGRIAN-----PPTDKSD-RDMLDVLIAVK---AETGTPRFSA 243
Cdd:cd20664 146 KLTGSPSVQLYNMFPWLGPFPGD--INKLLRNTKELNDFLMETfmkhlDVLEPNDqRGFIDAFLVKQqeeEESSDSFFHD 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      244 DEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGdGRSVSFHALRQIPQLENVLKETLRLHPPLII 323
Cdd:cd20664 224 DNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIG-SRQPQVEHRKNMPYTDAVIHEIQRFANIVPM 302

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      324 -LMRVAKGEFEVQGHRIHEGDLVAasPAISNRIPED--FPDPHDFVPARYEQpRQEDLLNRWTWIPFGAGRHRCVGAAFA 400
Cdd:cd20664 303 nLPHATTRDVTFRGYFIPKGTYVI--PLLTSVLQDKteWEKPEEFNPEHFLD-SQGKFVKRDAFMPFSAGRRVCIGETLA 379

                       410       420
                ....*....|....*....|...
1U13_A      401 IMQIKAIFSVLLREYEFemaQPP 423
Cdd:cd20664 380 KMELFLFFTSLLQRFRF---QPP 399
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 224-413 1.02e-11

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: 66.17  E-value: 1.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      224 DMLDVLIAVKAETGTprFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVideldelYGDgrsvsfHALrq 303
Cdd:cd20629 173 DLISRLLRAEVEGEK--LDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERV-------RRD------RSL-- 235

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      304 IPQLenvLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFvparyeqprqeDLLNRWT 383
Cdd:cd20629 236 IPAA---IEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVF-----------DIDRKPK 301

                       170       180       190
                ....*....|....*....|....*....|.
1U13_A      384 W-IPFGAGRHRCVGAAFAIMQIKAIFSVLLR 413
Cdd:cd20629 302 PhLVFGGGAHRCLGEHLARVELREALNALLD 332
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 243-413 1.09e-11

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: 66.21  E-value: 1.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      243 ADEITGMFISMMFAGHHTSSGTASWTLIELMRH-RDAYAAVIDELDelygDGRSVSFHALRQIpqlenVLkETLRLHPPL 321
Cdd:cd20612 185 ADEVRDNVLGTAVGGVPTQSQAFAQILDFYLRRpGAAHLAEIQALA----RENDEADATLRGY-----VL-EALRLNPIA 254

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      322 IILMRVAKGEFEVQ-----GHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARyeqPRQEDLLnrwtwipFGAGRHRCVG 396
Cdd:cd20612 255 PGLYRRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR---PLESYIH-------FGHGPHQCLG 324

                       170
                ....*....|....*..
1U13_A      397 AAFAIMQIKAIFSVLLR 413
Cdd:cd20612 325 EEIARAALTEMLRVVLR 341
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 89-413 1.70e-11

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: 65.80  E-value: 1.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       89 FDASPERRKEMLhNAALRGEQMKGHAATI----EDQVRRMIADWGE-AGEIDLLDFFAELTIYTSSATLIGKKFRDQLDG 163
Cdd:cd11066  60 WDESCKRRRKAA-ASALNRPAVQSYAPIIdlesKSFIRELLRDSAEgKGDIDPLIYFQRFSLNLSLTLNYGIRLDCVDDD 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      164 RFAKLYHELERG--------TDPLAYVdPYL----PIESFR-RRDEARNGLvalvADIMNGRIANPPTDKSDRDMLDVLI 230
Cdd:cd11066 139 SLLLEIIEVESAiskfrstsSNLQDYI-PILryfpKMSKFReRADEYRNRR----DKYLKKLLAKLKEEIEDGTDKPCIV 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      231 AV---KAETgtpRFSADEITGMFISMMFAGHHTSSGTASWtLIELMRHRDAYA---AVIDELDELYGDGRSVSFHAL--R 302
Cdd:cd11066 214 GNilkDKES---KLTDAELQSICLTMVSAGLDTVPLNLNH-LIGHLSHPPGQEiqeKAYEEILEAYGNDEDAWEDCAaeE 289

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      303 QIPQLENVLKETLRLHPPLIILM-RVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRqEDLLNR 381
Cdd:cd11066 290 KCPYVVALVKETLRYFTVLPLGLpRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDAS-GDLIPG 368

                       330       340       350
                ....*....|....*....|....*....|..
1U13_A      382 WTWIPFGAGRHRCVGAAFAimqIKAIFSVLLR 413
Cdd:cd11066 369 PPHFSFGAGSRMCAGSHLA---NRELYTAICR 397
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 267-423 4.19e-11

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: 64.42  E-value: 4.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      267 WTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHPPLIILmrvakgefeVQGHRIHEG---- 342
Cdd:cd11074 255 WGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLRMAIPLL---------VPHMNLHDAklgg 325

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      343 -DLVAASPAISN-----RIPEDFPDPHDFVPARY--EQPRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLRe 414
Cdd:cd11074 326 yDIPAESKILVNawwlaNNPAHWKKPEEFRPERFleEESKVEANGNDFRYLPFGVGRRSCPGIILALPILGITIGRLVQ- 404


                ....*....
1U13_A      415 yEFEMAQPP 423
Cdd:cd11074 405 -NFELLPPP 412
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 240-416 4.30e-11

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: 64.44  E-value: 4.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      240 RFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLHP 319
Cdd:cd20645 221 ELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTP 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      320 PLIILMRVAKGEFEVQGHRIHEGD-LVAASPAISNRiPEDFPDPHDFVPARYEQprQEDLLNRWTWIPFGAGRHRCVGAA 398
Cdd:cd20645 301 SVPFTSRTLDKDTVLGDYLLPKGTvLMINSQALGSS-EEYFEDGRQFKPERWLQ--EKHSINPFAHVPFGIGKRMCIGRR 377

                       170
                ....*....|....*...
1U13_A      399 FAIMQIKAIFSVLLREYE 416
Cdd:cd20645 378 LAELQLQLALCWIIQKYQ 395
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 226-429 5.45e-11

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: 64.05  E-value: 5.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      226 LDVLIAVKAETGTPR--FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQ 303
Cdd:cd20671 202 IEALIQKQEEDDPKEtlFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKA 281

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      304 IPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAasPAISN--------RIPEDFpDPHDFVPAryeqprQ 375
Cdd:cd20671 282 LPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVI--PLLSSvlldktqwETPYQF-NPNHFLDA------E 352

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
1U13_A      376 EDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFemAQPPESYRND 429
Cdd:cd20671 353 GKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTF--LPPPGVSPAD 404
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 233-420 8.78e-11

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: 63.58  E-value: 8.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      233 KAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLK 312
Cdd:cd20652 222 DRDLFDGFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACIS 301

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      313 ETLRLHP--PLIILMRVAKgEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPAR-------YEQPRQedllnrwt 383
Cdd:cd20652 302 ESQRIRSvvPLGIPHGCTE-DAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERfldtdgkYLKPEA-------- 372

                       170       180       190
                ....*....|....*....|....*....|....*..
1U13_A      384 WIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA 420
Cdd:cd20652 373 FIPFQTGKRMCLGDELARMILFLFTARILRKFRIALP 409
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 221-424 1.13e-10

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: 63.24  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      221 SDRDMLDV-LIAVKAETGTP--RFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVS 297
Cdd:cd20669 199 SPRDFIDCfLTKMAEEKQDPlsHFNMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPT 278

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      298 FHALRQIPQLENVLKETLRLHP--PLIILMRVAKgEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQ 375
Cdd:cd20669 279 LEDRARMPYTDAVIHEIQRFADiiPMSLPHAVTR-DTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNG 357

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
1U13_A      376 EdLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPE 424
Cdd:cd20669 358 S-FKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQPLGAPE 405
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 26-408 1.92e-10

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 62.45  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A        26 PIGLMQRVRDELGDVGTFQLAGKQVVLLSGSHANEFFFRAgdDDLDQAKAYP-FMTPIFGEG--VVFDASPERRKEMLHN 102
Cdd:PLN03141  33 PESFMDKRRSLYGKVFKSHIFGTPTIVSTDAEVNKVVLQS--DGNAFVPAYPkSLTELMGKSsiLLINGSLQRRVHGLIG 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       103 AALRGEQMKGH-AATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDgrfaKLYHELERGTDPLAY 181
Cdd:PLN03141 111 AFLKSPHLKAQiTRDMERYVSESLDSWRDDPPVLVQDETKKIAFEVLVKALISLEPGEEME----FLKKEFQEFIKGLMS 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       182 VDPYLPIESFRRRDEARNGLVALVADIMNGRIA-----NPPTDKSDRDMLDVLIavkaETGTPRFSADEITGMFISMMFA 256
Cdd:PLN03141 187 LPIKLPGTRLYRSLQAKKRMVKLVKKIIEEKRRamknkEEDETGIPKDVVDVLL----RDGSDELTDDLISDNMIDMMIP 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       257 GHHT------------SSGTASWTLI--ELMRHRDAYAAVIDELDelYGDGRSVSFhalrqipqLENVLKETLRLHPPLI 322
Cdd:PLN03141 263 GEDSvpvlmtlavkflSDCPVALQQLteENMKLKRLKADTGEPLY--WTDYMSLPF--------TQNVITETLRMGNIIN 332

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       323 ILMRVAKGEFEVQGHRIHEGDLVAASpAISNRIPED-FPDPHDFVPARYeqprQEDLLNRWTWIPFGAGRHRCVGAAFAI 401
Cdd:PLN03141 333 GVMRKAMKDVEIKGYLIPKGWCVLAY-FRSVHLDEEnYDNPYQFNPWRW----QEKDMNNSSFTPFGGGQRLCPGLDLAR 407


                 ....*..
1U13_A       402 MQIkAIF 408
Cdd:PLN03141 408 LEA-SIF 413
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 267-422 2.75e-10

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: 62.08  E-value: 2.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      267 WTLIELMRHRDAYAAVIDELDEL-YGDGRSVSFHA------LRQIPQLENVLKETLRL-HPPLI-------ILMRVAKGe 331
Cdd:cd20634 243 WLLLFLLKHPEAMAAVRGEIQRIkHQRGQPVSQTLtinqelLDNTPVFDSVLSETLRLtAAPFItrevlqdMKLRLADG- 321

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      332 fevQGHRIHEGDLVAASPAISNRI-PEDFPDPHDFVPARYEQP---------RQEDLLNRWTwIPFGAGRHRCVGAAFAI 401
Cdd:cd20634 322 ---QEYNLRRGDRLCLFPFLSPQMdPEIHQEPEVFKYDRFLNAdgtekkdfyKNGKRLKYYN-MPWGAGDNVCIGRHFAV 397

                       170       180
                ....*....|....*....|.
1U13_A      402 MQIKAIFSVLLREYEFEMAQP 422
Cdd:cd20634 398 NSIKQFVFLILTHFDVELKDP 418
PLN02655 PLN02655
ent-kaurene oxidase
 264-425 7.91e-10

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 60.53  E-value: 7.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       264 TASWTLIELMRHRDAYAAVIDELDELYGDGRsVSFHALRQIPQLENVLKETLRLHPPL-IILMRVAKGEFEVQGHRIHEG 342
Cdd:PLN02655 281 TTEWAMYELAKNPDKQERLYREIREVCGDER-VTEEDLPNLPYLNAVFHETLRKYSPVpLLPPRFVHEDTTLGGYDIPAG 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       343 DLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEdLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQP 422
Cdd:PLN02655 360 TQIAINIYGCNMDKKRWENPEEWDPERFLGEKYE-SADMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLREG 438


                 ...
1U13_A       423 PES 425
Cdd:PLN02655 439 DEE 441
PLN00168 PLN00168
Cytochrome P450; Provisional
 121-449 8.48e-10

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 60.73  E-value: 8.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       121 VRRMIAD-WGEAGEIDLLDFFAELTIYTSSATLIGKKFRDQLDGRFAKLYHELERgtDPLAYVD---------PYLPIES 190
Cdd:PLN00168 158 VRRVLVDkLRREAEDAAAPRVVETFQYAMFCLLVLMCFGERLDEPAVRAIAAAQR--DWLLYVSkkmsvfaffPAVTKHL 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       191 FRRRDEA----RNGLVALVADIMNGR--------IANPPTDKS---DRDMLDVLIAVK-AETGTPRFSADEITGMFISMM 254
Cdd:PLN00168 236 FRGRLQKalalRRRQKELFVPLIDARreyknhlgQGGEPPKKEttfEHSYVDTLLDIRlPEDGDRALTDDEIVNLCSEFL 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       255 FAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDG-RSVSFHALRQIPQLENVLKETLRLHPPL-IILMRVAKGEF 332
Cdd:PLN00168 316 NAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDqEEVSEEDVHKMPYLKAVVLEGLRKHPPAhFVLPHKAAEDM 395

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       333 EVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARY-EQPRQEDLLNRWT----WIPFGAGRHRCVGAAFAIMQIKAI 407
Cdd:PLN00168 396 EVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFlAGGDGEGVDVTGSreirMMPFGVGRRICAGLGIAMLHLEYF 475

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
1U13_A       408 FSVLLREYEFEMAQPPESYRNDHSKMVVQLAQPAAVRYRRRT 449
Cdd:PLN00168 476 VANMVREFEWKEVPGDEVDFAEKREFTTVMAKPLRARLVPRR 517
PLN02774 PLN02774
brassinosteroid-6-oxidase
 116-418 9.08e-10

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 60.56  E-value: 9.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       116 TIEDQVRRMIADWGEAGEIDLLDFFAELTIYtSSATLIGKKFRDQLDGRFAKLYHELERGTDPLAyVDpyLPIESFRRRD 195
Cdd:PLN02774 144 KIDEFMRSHLSGWDGLKTIDIQEKTKEMALL-SALKQIAGTLSKPISEEFKTEFFKLVLGTLSLP-ID--LPGTNYRSGV 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       196 EARNGLVALVADIMNGRIANPPTDKsdrDMLDVLIavKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRH 275
Cdd:PLN02774 220 QARKNIVRMLRQLIQERRASGETHT---DMLGYLM--RKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDH 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       276 RDAyaavIDELDELYGDGRS-------VSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAAS 348
Cdd:PLN02774 295 PKA----LQELRKEHLAIRErkrpedpIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVY 370

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       349 PAISNRIPEDFPDPHDFVPARYeqpRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFE 418
Cdd:PLN02774 371 TREINYDPFLYPDPMTFNPWRW---LDKSLESHNYFFLFGGGTRLCPGKELGIVEISTFLHYFVTRYRWE 437
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 201-429 3.58e-09

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: 58.15  E-value: 3.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      201 LVALVADimngRIANPptdksDRDMLDVLIAvkAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYA 280
Cdd:cd11038 181 ADALIEA----RRAEP-----GDDLISTLVA--AEQDGDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDQWR 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      281 AvideldelygdgrsvsfhaLRQIPQL-ENVLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRipedf 359
Cdd:cd11038 250 A-------------------LREDPELaPAAVEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANR----- 305

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      360 pDPHDFVPARYEQPRQEDLLnrwtwIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPESYRND 429
Cdd:cd11038 306 -DPRVFDADRFDITAKRAPH-----LGFGGGVHHCLGAFLARAELAEALTVLARRLPTPAIAGEPTWLPD 369
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 223-423 3.99e-09

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: 58.27  E-value: 3.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      223 RDMLDVLIA--VKAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHA 300
Cdd:cd20662 201 RDFIDAYLKemAKYPDPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLAD 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      301 LRQIPQLENVLKETLRLHP--PLIILMRVAKgEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQedL 378
Cdd:cd20662 281 RESMPYTNAVIHEVQRMGNiiPLNVPREVAV-DTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQ--F 357

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1U13_A      379 LNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFemaQPP 423
Cdd:cd20662 358 KKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTF---KPP 399
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
 297-414 6.80e-09

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: 57.44  E-value: 6.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      297 SFHALRQIPQLEN-VLKETLRLHPPLIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFvpaRYEQPrQ 375
Cdd:cd20619 223 VFTAFRNDESARAaIINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVF---DHTRP-P 298

                        90       100       110
                ....*....|....*....|....*....|....*....
1U13_A      376 EDLLNrwtwIPFGAGRHRCVGAAFAIMQIKAIFSVLLRE 414
Cdd:cd20619 299 AASRN----LSFGLGPHSCAGQIISRAEATTVFAVLAER 333
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 223-431 1.30e-08

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: 56.94  E-value: 1.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      223 RDMLDVLIAV----KAETGTPRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSF 298
Cdd:cd20675 209 RDMMDAFILAlekgKSGDSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCI 288

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      299 HALRQIPQLENVLKETLRLHP--PLIILMRVAKgEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFVPARY---EQP 373
Cdd:cd20675 289 EDQPNLPYVMAFLYEAMRFSSfvPVTIPHATTA-DTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFldeNGF 367

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
1U13_A      374 RQEDLLNRwTWIpFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEmAQPPESYRNDHS 431
Cdd:cd20675 368 LNKDLASS-VMI-FSVGKRRCIGEELSKMQLFLFTSILAHQCNFT-ANPNEPLTMDFS 422
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
 281-418 4.44e-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: 55.10  E-value: 4.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      281 AVIDELDELYGDGRSVsfhalrqipqlENVLKETLRLHPPliiLMRVAKGEFEVQG--HRIHEGDLVAA--SPAISNrip 356
Cdd:cd20626 243 ANADFAKSATKDGISA-----------KNLVKEALRLYPP---TRRIYRAFQRPGSskPEIIAADIEAChrSESIWG--- 305

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
1U13_A      357 edfPDPHDFVPARYEQ--PRQEDLlnrwtWIPFGAGRHRCVG-AAFAIMQIKAIFSVLLREYEFE 418
Cdd:cd20626 306 ---PDALEFNPSRWSKltPTQKEA-----FLPFGSGPFRCPAkPVFGPRMIALLVGALLDALGDE 362
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 251-423 5.57e-08

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 55.08  E-value: 5.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       251 ISMMFAGHHT-SSGTASWTLIeLMRHRDAYAAVIDELDELYGDGR-SVSFHALRQIPQLENVLKETLRLHPPLIILMRVA 328
Cdd:PLN02426 299 VSFLLAGRDTvASALTSFFWL-LSKHPEVASAIREEADRVMGPNQeAASFEEMKEMHYLHAALYESMRLFPPVQFDSKFA 377

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       329 KGEfEV--QGHRIHEGDLVAASPAISNRIPEDF-PDPHDFVPARYeqprqedlLNRWTWIP--------FGAGRHRCVGA 397
Cdd:PLN02426 378 AED-DVlpDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERW--------LKNGVFVPenpfkypvFQAGLRVCLGK 448

                        170       180
                 ....*....|....*....|....*.
1U13_A       398 AFAIMQIKAIFSVLLREYEFEMAQPP 423
Cdd:PLN02426 449 EMALMEMKSVAVAVVRRFDIEVVGRS 474
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 239-425 1.28e-07

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: 53.44  E-value: 1.28e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      239 PRFSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGD-GRSVSFHALRQIPQLENVLKETLRL 317
Cdd:cd20615 209 GDITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREQsGYPMEDYILSTDTLLAYCVLESLRL 288

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      318 HPpliiLMRVAKGEF-----EVQGHRIHEG-DLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLL-NRWTwipFGAG 390
Cdd:cd20615 289 RP----LLAFSVPESsptdkIIGGYRIPANtPVVVDTYALNINNPFWGPDGEAYRPERFLGISPTDLRyNFWR---FGFG 361

                       170       180       190
                ....*....|....*....|....*....|....*
1U13_A      391 RHRCVGAAFAIMQIKAIFSVLLREYEFEMAQPPES 425
Cdd:cd20615 362 PRKCLGQHVADVILKALLAHLLEQYELKLPDQGEN 396
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 261-425 3.57e-07

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: 52.08  E-value: 3.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      261 SSGTASWTLIELMRHRDAYAAVIDEldELYGDGRSVSFHALRQipqlenVLKETLRLHPPLIILMRVAKGEFEVQGHRIH 340
Cdd:cd20624 206 AAGMALLRALALLAAHPEQAARARE--EAAVPPGPLARPYLRA------CVLDAVRLWPTTPAVLRESTEDTVWGGRTVP 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      341 EGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLlnrWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEMA 420
Cdd:cd20624 278 AGTGFLIFAPFFHRDDEALPFADRFVPEIWLDGRAQPD---EGLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPL 354


                ....*
1U13_A      421 QPPES 425
Cdd:cd20624 355 ESPRS 359
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 214-422 4.54e-07

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: 52.00  E-value: 4.54e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      214 ANPPtdksdRDMLDVLIA-VKAETGTPRFS-ADEITGMFISMMF-AGHHTSSGTASWTLIELMRHRDAYAAVIDELDELY 290
Cdd:cd20663 201 AQPP-----RDLTDAFLAeMEKAKGNPESSfNDENLRLVVADLFsAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVI 275

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      291 GDGRSVSFHALRQIPQLENVLKETLRLHP--PLIiLMRVAKGEFEVQGHRIHEGDLVAasPAISNRIPED--FPDPHDFV 366
Cdd:cd20663 276 GQVRRPEMADQARMPYTNAVIHEVQRFGDivPLG-VPHMTSRDIEVQGFLIPKGTTLI--TNLSSVLKDEtvWEKPLRFH 352

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
1U13_A      367 PARYEQpRQEDLLNRWTWIPFGAGRHRCVGAAFAIMQIKAIFSVLLREYEFEM--AQP 422
Cdd:cd20663 353 PEHFLD-AQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVpaGQP 409
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 192-427 1.10e-06

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 50.93  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       192 RRR----DEARNGLVALVADIMNGRI---ANPPTDKSDRDMLDVLIavkaetgtprfsadeitgmfiSMMFAGHHTSSGT 264
Cdd:PLN03195 253 RRRkaemDEARKSGKKVKHDILSRFIelgEDPDSNFTDKSLRDIVL---------------------NFVIAGRDTTATT 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       265 ASWTLIELMRHRDAYAAVIDELDELYGD--------------------GRSVSFHALRQIPQLENVLKETLRLHPPLiil 324
Cdd:PLN03195 312 LSWFVYMIMMNPHVAEKLYSELKALEKErakeedpedsqsfnqrvtqfAGLLTYDSLGKLQYLHAVITETLRLYPAV--- 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       325 MRVAKGEFE----VQGHRIHEGDLVAASPAISNRIPEDF-PDPHDFVPARYEQPRQEDLLNRWTWIPFGAGRHRCVGAAF 399
Cdd:PLN03195 389 PQDPKGILEddvlPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDGVFQNASPFKFTAFQAGPRICLGKDS 468

                        250       260
                 ....*....|....*....|....*....
1U13_A       400 AIMQIKAIFSVLLREYEFEMAQ-PPESYR 427
Cdd:PLN03195 469 AYLQMKMALALLCRFFKFQLVPgHPVKYR 497
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 246-421 1.48e-06

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 50.39  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       246 ITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDgrsvsfHALRQIPQLENVLKETLRLHPPLIILM 325
Cdd:PLN02169 302 IRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKFDN------EDLEKLVYLHAALSESMRLYPPLPFNH 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       326 RV-AKGEFEVQGHRIH-EGDLVAASPAISNRIPEDFPDPHDFVPARYEQP----RQEDllnRWTWIPFGAGRHRCVGAAF 399
Cdd:PLN02169 376 KApAKPDVLPSGHKVDaESKIVICIYALGRMRSVWGEDALDFKPERWISDngglRHEP---SYKFMAFNSGPRTCLGKHL 452

                        170       180
                 ....*....|....*....|..
1U13_A       400 AIMQIKAIFSVLLREYEFEMAQ 421
Cdd:PLN02169 453 ALLQMKIVALEIIKNYDFKVIE 474
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 253-440 1.57e-06

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: 50.20  E-value: 1.57e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      253 MMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDELYGDGRSVSFHALRQIPQLENVLKETLRLH--PPLIILMRVAKg 330
Cdd:cd20661 246 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCniVPLGIFHATSK- 324

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      331 EFEVQGHRIHEGDLVaaspaISNRIPEDF-----PDPHDFVPARYEQPRQEdLLNRWTWIPFGAGRHRCVGAAFAIMQIK 405
Cdd:cd20661 325 DAVVRGYSIPKGTTV-----ITNLYSVHFdekywSDPEVFHPERFLDSNGQ-FAKKEAFVPFSLGRRHCLGEQLARMEMF 398

                       170       180       190
                ....*....|....*....|....*....|....*
1U13_A      406 AIFSVLLReyEFEMAQPPESYRNDHSKMVVQLaQP 440
Cdd:cd20661 399 LFFTALLQ--RFHLHFPHGLIPDLKPKLGMTL-QP 430
PLN02648 PLN02648
allene oxide synthase
 292-384 2.55e-06

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 49.55  E-value: 2.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       292 DGRSVSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQGH----RIHEGDLVAASPAISNRIPEDFPDPHDFVP 367
Cdd:PLN02648 321 GGGGVTFAALEKMPLVKSVVYEALRIEPPVPFQYGRAREDFVIESHdaafEIKKGEMLFGYQPLVTRDPKVFDRPEEFVP 400

                         90
                 ....*....|....*..
1U13_A       368 ARYEQPRQEDLLNRWTW 384
Cdd:PLN02648 401 DRFMGEEGEKLLKYVFW 417
PLN02500 PLN02500
cytochrome P450 90B1
 186-426 9.25e-06

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 47.94  E-value: 9.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       186 LPIESFRRRDEARNGLVALVADIMNGRIANPPTDKSDRDMLDVLIAVKAETGtprFSADEITGMFISMMFAGHHTSSGTA 265
Cdd:PLN02500 223 FPGTAYRKALKSRATILKFIERKMEERIEKLKEEDESVEEDDLLGWVLKHSN---LSTEQILDLILSLLFAGHETSSVAI 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       266 SWTLIELmrhrDAYAAVIDELDELYGD--------GRS-VSFHALRQIPQLENVLKETLRLHPPLIILMRVAKGEFEVQG 336
Cdd:PLN02500 300 ALAIFFL----QGCPKAVQELREEHLEiarakkqsGESeLNWEDYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYKG 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A       337 HRIHEGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEDLLNRWT------WIPFGAGRHRCVGAAFAIMQIKAIFSV 410
Cdd:PLN02500 376 YDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRGGSSGSSsattnnFMPFGGGPRLCAGSELAKLEMAVFIHH 455

                        250
                 ....*....|....*.
1U13_A       411 LLREYEFEMAQPPESY 426
Cdd:PLN02500 456 LVLNFNWELAEADQAF 471
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 213-404 6.48e-05

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: 44.95  E-value: 6.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      213 IANPptdksdRDMLD-VLIAVKAETGTPR--FSADEITGMFISMMFAGHHTSSGTASWTLIELMRHRDAYAAVIDELDEL 289
Cdd:cd20665 197 VNNP------RDFIDcFLIKMEQEKHNQQseFTLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRV 270

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      290 YGDGRSVSFHALRQIPQLENVLKETLR---LHPplIILMRVAKGEFEVQGHRIHEGDLVAASPAISNRIPEDFPDPHDFV 366
Cdd:cd20665 271 IGRHRSPCMQDRSHMPYTDAVIHEIQRyidLVP--NNLPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFD 348

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
1U13_A      367 PARYEQP----RQEDLlnrwtWIPFGAGRHRCVGAAFAIMQI 404
Cdd:cd20665 349 PGHFLDEngnfKKSDY-----FMPFSAGKRICAGEGLARMEL 385
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
 104-407 2.41e-03

P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Agrobacterium tumefaciens P450-pinF2, whose expression is induced by the presence of wounded plant tissue and by plant phenolic compounds such as acetosyringone. P450-pinF2 may be involved in the detoxification of plant protective agents at the site of wounding. 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: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 40.18  E-value: 2.41e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      104 ALRGEQMKGH-AATIEDQVRRMIADWGEAGEIDLLDFFAELTIYTSSATLIGKKfrdqlDGRFAKLYHELERGTDPLAYV 182
Cdd:cd11039  77 TFSPKTVKSYwAALFRAVVQRFLDDIEPGGAADLFTELAEPVSARCLKDILGLT-----ETSNAELDRWSQAMIDGAGNY 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      183 --DPylpiESFRRRDEARNGLVALVADIMNGRIANPptDKSdrdmldvLIAVKAETGTPRfSADEITGMFISMMFAGHHT 260
Cdd:cd11039 152 sgDP----EVEARCDEATAGIDAAIDALIPVHRSNP--NPS-------LLSVMLNAGMPM-SLEQIRANIKVAIGGGLNE 217

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1U13_A      261 SSGTASWTLIELMRHRDAYAAVIDELDelygdgrsvsfHALRqipqlenVLKETLRLHPPLIILMRVAKGEFEVQGHRIH 340
Cdd:cd11039 218 PRDAIAGTCWGLLSNPEQLAEVMAGDV-----------HWLR-------AFEEGLRWISPIGMSPRRVAEDFEIRGVTLP 279

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1U13_A      341 EGDLVAASPAISNRIPEDFPDPHDFVPARYEQPRQEdllnrwtwipFGAGRHRCVGAAFAIMQIKAI 407
Cdd:cd11039 280 AGDRVFLMFGSANRDEARFENPDRFDVFRPKSPHVS----------FGAGPHFCAGAWASRQMVGEI 336
 
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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