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Conserved domains on  [gi|822093467|gb|AKH61484|]
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CYP76AD/P450 tyrosinase fusion protein [Expression vector pWCD2433]

Protein Classification

cytochrome P450( domain architecture ID 15297177)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
60-493 0e+00

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: 682.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  60 AKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLPVSPKWRNFRKITAVHLLSPQ 139
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 140 RLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHTSQEFKELIWNIMEDIGKPNY 219
Cdd:cd11073   81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSESGSEFKELVREIMELAGKPNV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 220 ADYFPILGCVDPSGIRRRLACSFDKLIAVFQGIICERLAPDSS-TTTTTTTDDVLDVLLQLFKQNELTMGEINHLLVDIF 298
Cdd:cd11073  161 ADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAgGDKKKDDDLLLLLDLELDSESELTRNHIKALLLDLF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 299 DAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVE 378
Cdd:cd11073  241 VAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAEEDVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 379 LYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMNLAIRMLTLMLATLLQ 458
Cdd:cd11073  321 VMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKGRDFELIPFGSGRRICPGLPLAERMVHLVLASLLH 400
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 822093467 459 FFNWKLEGDISPKDLDMDEKFGIALQKTKPLKLIP 493
Cdd:cd11073  401 SFDWKLPDGMKPEDLDMEEKFGLTLQKAVPLKAIP 435
 
Name Accession Description Interval E-value
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
60-493 0e+00

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: 682.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  60 AKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLPVSPKWRNFRKITAVHLLSPQ 139
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 140 RLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHTSQEFKELIWNIMEDIGKPNY 219
Cdd:cd11073   81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSESGSEFKELVREIMELAGKPNV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 220 ADYFPILGCVDPSGIRRRLACSFDKLIAVFQGIICERLAPDSS-TTTTTTTDDVLDVLLQLFKQNELTMGEINHLLVDIF 298
Cdd:cd11073  161 ADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAgGDKKKDDDLLLLLDLELDSESELTRNHIKALLLDLF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 299 DAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVE 378
Cdd:cd11073  241 VAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAEEDVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 379 LYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMNLAIRMLTLMLATLLQ 458
Cdd:cd11073  321 VMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKGRDFELIPFGSGRRICPGLPLAERMVHLVLASLLH 400
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 822093467 459 FFNWKLEGDISPKDLDMDEKFGIALQKTKPLKLIP 493
Cdd:cd11073  401 SFDWKLPDGMKPEDLDMEEKFGLTLQKAVPLKAIP 435
PLN02687 PLN02687
flavonoid 3'-monooxygenase
41-496 4.12e-120

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 362.21  E-value: 4.12e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  41 IIGNILEVGKKPHRSFANLAKIHGPLISLRLGSVTTIVVSSADVAkEMFLK-KDHPLSNRTiPNSvtAGDHHKLT---MS 116
Cdd:PLN02687  44 VLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVA-AQFLRtHDANFSNRP-PNS--GAEHMAYNyqdLV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 117 WLPVSPKWRNFRKITAVHLLSPQRLDacqTFRHAKVQQLYEYVQECAQKGQ--AVDIGKAAFTTSLNLLSKLFFSVEL-A 193
Cdd:PLN02687 120 FAPYGPRWRALRKICAVHLFSAKALD---DFRHVREEEVALLVRELARQHGtaPVNLGQLVNVCTTNALGRAMVGRRVfA 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 194 HHKSHTSQEFKELIWNIMEDIGKPNYADYFPILGCVDPSGI---RRRLACSFDkliAVFQGIICERLApdSSTTTTTTTD 270
Cdd:PLN02687 197 GDGDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLDLQGVvgkMKRLHRRFD---AMMNGIIEEHKA--AGQTGSEEHK 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 271 DVLDVLLQLFKQNE-------LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQES 343
Cdd:PLN02687 272 DLLSTLLALKREQQadgeggrITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSES 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 344 DIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI----GCE 419
Cdd:PLN02687 352 DLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpggeHAG 431
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822093467 420 IDVKGRDFGLLPFGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKDLDMDEKFGIALQKTKPLKLIPIPR 496
Cdd:PLN02687 432 VDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQTPDKLNMEEAYGLTLQRAVPLMVHPRPR 508
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
41-493 1.35e-90

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: 284.17  E-value: 1.35e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467   41 IIGNILEVGKK--PHRSFANLAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSV-TAGDHHKLTMSW 117
Cdd:pfam00067   9 LFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFaTSRGPFLGKGIV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  118 LPVSPKWRNFRKITAVHLLSPQRL---DACQtfrhAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAH 194
Cdd:pfam00067  89 FANGPRWRQLRRFLTPTFTSFGKLsfePRVE----EEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERFGS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  195 HKSHTSQEFKELIWNIMEDIGKPNYA--DYFPILGcVDPSGIRRRLACSFDKLIAVFQGIICERLAP-DSSTTTTTTTDD 271
Cdd:pfam00067 165 LEDPKFLELVKAVQELSSLLSSPSPQllDLFPILK-YFPGPHGRKLKRARKKIKDLLDKLIEERRETlDSAKKSPRDFLD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  272 VLDVLLQLFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYL 351
Cdd:pfam00067 244 ALLLAKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYL 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  352 QAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDvKGRDFGLLP 431
Cdd:pfam00067 324 DAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGK-FRKSFAFLP 402
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822093467  432 FGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKdlDMDEKFGIaLQKTKPLKLIP 493
Cdd:pfam00067 403 FGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPP--DIDETPGL-LLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
47-445 8.21e-35

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: 134.64  E-value: 8.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  47 EVGKKPHRSFANLAKiHGPLISLRLGSVTTIVVSSADVAKEMfLKKDHPLSNRTIPNSVTAgdHHKLTMSWLPVS--PKW 124
Cdd:COG2124   16 AFLRDPYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREV-LRDPRTFSSDGGLPEVLR--PLPLLGDSLLTLdgPEH 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 125 RNFRKITAvHLLSPQRLDAcqtfRHAKVQQL-YEYVQECAQKGQaVDIGKAAFTTSLNLLSKLFFSVELAHHkshtsQEF 203
Cdd:COG2124   92 TRLRRLVQ-PAFTPRRVAA----LRPRIREIaDELLDRLAARGP-VDLVEEFARPLPVIVICELLGVPEEDR-----DRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 204 KELIwnimedigkpnyADYFPILGCVDPSGIRRRLAcSFDKLIAVFQGIICERLA-PDSStttttttddvldvllqLF-- 280
Cdd:COG2124  161 RRWS------------DALLDALGPLPPERRRRARR-ARAELDAYLRELIAERRAePGDD----------------LLsa 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 ------KQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEikqvlgkdkqiqesdiinLPYLQAI 354
Cdd:COG2124  212 llaardDGERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE------------------PELLPAA 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 355 IKETLRLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERfigceidvkgRDFGLLPFGA 434
Cdd:COG2124  274 VEETLRLYPP-VPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPFGG 342
                        410
                 ....*....|.
gi 822093467 435 GRRICPGMNLA 445
Cdd:COG2124  343 GPHRCLGAALA 353
 
Name Accession Description Interval E-value
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
60-493 0e+00

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: 682.72  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  60 AKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLPVSPKWRNFRKITAVHLLSPQ 139
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 140 RLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHTSQEFKELIWNIMEDIGKPNY 219
Cdd:cd11073   81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSESGSEFKELVREIMELAGKPNV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 220 ADYFPILGCVDPSGIRRRLACSFDKLIAVFQGIICERLAPDSS-TTTTTTTDDVLDVLLQLFKQNELTMGEINHLLVDIF 298
Cdd:cd11073  161 ADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAgGDKKKDDDLLLLLDLELDSESELTRNHIKALLLDLF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 299 DAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVE 378
Cdd:cd11073  241 VAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAEEDVE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 379 LYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMNLAIRMLTLMLATLLQ 458
Cdd:cd11073  321 VMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKGRDFELIPFGSGRRICPGLPLAERMVHLVLASLLH 400
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 822093467 459 FFNWKLEGDISPKDLDMDEKFGIALQKTKPLKLIP 493
Cdd:cd11073  401 SFDWKLPDGMKPEDLDMEEKFGLTLQKAVPLKAIP 435
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
64-489 8.24e-156

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: 450.08  E-value: 8.24e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNR--TIPNSVTAGDHHklTMSWLPVSPKWRNFRKITAVHLLSPQRL 141
Cdd:cd20618    1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRprTAAGKIFSYNGQ--DIVFAPYGPHWRHLRKICTLELFSAKRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 142 DACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLN-----LLSKLFFSVELAhhKSHTSQEFKELIWNIMEDIGK 216
Cdd:cd20618   79 ESFQGVRKEELSHLVKSLLEESESGKPVNLREHLSDLTLNnitrmLFGKRYFGESEK--ESEEAREFKELIDEAFELAGA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 217 PNYADYFPILGCVDPSGIRRRLACSFDKLIAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQNELTMGEINHLLVD 296
Cdd:cd20618  157 FNIGDYIPWLRWLDLQGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLD 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 297 IFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKADTD 376
Cdd:cd20618  237 MLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLPHESTED 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 377 VELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEID-VKGRDFGLLPFGAGRRICPGMNLAIRMLTLMLAT 455
Cdd:cd20618  317 CKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDdVKGQDFELLPFGSGRRMCPGMPLGLRMVQLTLAN 396
                        410       420       430
                 ....*....|....*....|....*....|....
gi 822093467 456 LLQFFNWKLEGdISPKDLDMDEKFGIALQKTKPL 489
Cdd:cd20618  397 LLHGFDWSLPG-PKPEDIDMEEKFGLTVPRAVPL 429
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
63-489 3.26e-144

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: 420.33  E-value: 3.26e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEmFLK-KDHPLSNRtiPNSVTAgdhHKLT-----MSWLPVSPKWRNFRKITAVHLL 136
Cdd:cd11072    2 YGPLMLLRLGSVPTVVVSSPEAAKE-VLKtHDLVFASR--PKLLAA---RILSyggkdIAFAPYGEYWRQMRKICVLELL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 137 SPQRLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVElahHKSHTSQEFKELIWNIMEDIGK 216
Cdd:cd11072   76 SAKRVQSFRSIREEEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRK---YEGKDQDKFKELVKEALELLGG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 217 PNYADYFPILGCVDP-SGIRRRLACSFDKLIAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQNE--LTMGEINHL 293
Cdd:cd11072  153 FSVGDYFPSLGWIDLlTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEfpLTRDNIKAI 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 294 LVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKA 373
Cdd:cd11072  233 ILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLPREC 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 374 DTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMNLAIRMLTLML 453
Cdd:cd11072  313 REDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIDFKGQDFELIPFGAGRRICPGITFGLANVELAL 392
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 822093467 454 ATLLQFFNWKLEGDISPKDLDMDEKFGIALQKTKPL 489
Cdd:cd11072  393 ANLLYHFDWKLPDGMKPEDLDMEEAFGLTVHRKNPL 428
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
64-496 6.78e-128

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: 379.07  E-value: 6.78e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEmFLKK-DHPLSNRTiPNSvtaGDHHKL----TMSWLPVSPKWRNFRKITAVHLLSP 138
Cdd:cd20657    1 GPIMYLKVGSCGVVVASSPPVAKA-FLKThDANFSNRP-PNA---GATHMAynaqDMVFAPYGPRWRLLRKLCNLHLFGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 139 QRLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVEL-AHHKSHTSQEFKELIWNIMEDIGKP 217
Cdd:cd20657   76 KALEDWAHVRENEVGHMLKSMAEASRKGEPVVLGEMLNVCMANMLGRVMLSKRVfAAKAGAKANEFKEMVVELMTVAGVF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 218 NYADYFPILGCVDPSGIRR---RLACSFDkliAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQNE-LTMGEINHL 293
Cdd:cd20657  156 NIGDFIPSLAWMDLQGVEKkmkRLHKRFD---ALLTKILEEHKATAQERKGKPDFLDFVLLENDDNGEGErLTDTNIKAL 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 294 LVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKA 373
Cdd:cd20657  233 LLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIA 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 374 DTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIG---CEIDVKGRDFGLLPFGAGRRICPGMNLAIRMLT 450
Cdd:cd20657  313 SEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPgrnAKVDVRGNDFELIPFGAGRRICAGTRMGIRMVE 392
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 822093467 451 LMLATLLQFFNWKLEGDISPKDLDMDEKFGIALQKTKPLKLIPIPR 496
Cdd:cd20657  393 YILATLVHSFDWKLPAGQTPEELNMEEAFGLALQKAVPLVAHPTPR 438
PLN02687 PLN02687
flavonoid 3'-monooxygenase
41-496 4.12e-120

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 362.21  E-value: 4.12e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  41 IIGNILEVGKKPHRSFANLAKIHGPLISLRLGSVTTIVVSSADVAkEMFLK-KDHPLSNRTiPNSvtAGDHHKLT---MS 116
Cdd:PLN02687  44 VLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVA-AQFLRtHDANFSNRP-PNS--GAEHMAYNyqdLV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 117 WLPVSPKWRNFRKITAVHLLSPQRLDacqTFRHAKVQQLYEYVQECAQKGQ--AVDIGKAAFTTSLNLLSKLFFSVEL-A 193
Cdd:PLN02687 120 FAPYGPRWRALRKICAVHLFSAKALD---DFRHVREEEVALLVRELARQHGtaPVNLGQLVNVCTTNALGRAMVGRRVfA 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 194 HHKSHTSQEFKELIWNIMEDIGKPNYADYFPILGCVDPSGI---RRRLACSFDkliAVFQGIICERLApdSSTTTTTTTD 270
Cdd:PLN02687 197 GDGDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLDLQGVvgkMKRLHRRFD---AMMNGIIEEHKA--AGQTGSEEHK 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 271 DVLDVLLQLFKQNE-------LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQES 343
Cdd:PLN02687 272 DLLSTLLALKREQQadgeggrITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSES 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 344 DIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI----GCE 419
Cdd:PLN02687 352 DLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpggeHAG 431
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822093467 420 IDVKGRDFGLLPFGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKDLDMDEKFGIALQKTKPLKLIPIPR 496
Cdd:PLN02687 432 VDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQTPDKLNMEEAYGLTLQRAVPLMVHPRPR 508
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
64-493 1.33e-113

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: 342.27  E-value: 1.33e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMFlkKDHPL--SNRTIPNSVTAGDHHKLTMSWLPVSPKWRNFRKITAVHLLSPQRL 141
Cdd:cd20655    1 GPLLHLRIGSVPCVVVSSASVAKEIL--KTHDLnfSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRAL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 142 DACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSvELAHHKSHTSQEFKELIWNIMEDIGKPNYAD 221
Cdd:cd20655   79 ERFRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMG-RSCSEENGEAEEVRKLVKESAELAGKFNASD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 222 YFPILGCVDPSGIRRRLACSFDKLIAVFQGIICERL-APDSSTTTTTTTDDVLDVLLQLFKQNE--LTMGEINHLLVDIF 298
Cdd:cd20655  158 FIWPLKKLDLQGFGKRIMDVSNRFDELLERIIKEHEeKRKKRKEGGSKDLLDILLDAYEDENAEykITRNHIKAFILDLF 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 299 DAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVfLLPRKADTDVE 378
Cdd:cd20655  238 IAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGP-LLVRESTEGCK 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 379 LYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI-----GCEIDVKGRDFGLLPFGAGRRICPGMNLAIRMLTLML 453
Cdd:cd20655  317 INGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLassrsGQELDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTAI 396
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 822093467 454 ATLLQFFNWKLEGDISpkdLDMDEKFGIALQKTKPLKLIP 493
Cdd:cd20655  397 AAMVQCFDWKVGDGEK---VNMEEASGLTLPRAHPLKCVP 433
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
6-496 4.42e-101

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 312.56  E-value: 4.42e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467   6 LAMILAIWFISFHFIKLLFSQQTTKLLPPGPKPLpIIGNILEVGKKPHRSFANLAKIHGPLISLRLGSVTTIVVSSADVA 85
Cdd:PLN00110   7 LAAATLLFFITRFFIRSLLPKPSRKLPPGPRGWP-LLGALPLLGNMPHVALAKMAKRYGPVMFLKMGTNSMVVASTPEAA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  86 KEmFLKK-DHPLSNRTIPNSVTAGDHHKLTMSWLPVSPKWRNFRKITAVHLLSPQRLDACQTFRHAKVQQLYEYVQECAQ 164
Cdd:PLN00110  86 RA-FLKTlDINFSNRPPNAGATHLAYGAQDMVFADYGPRWKLLRKLSNLHMLGGKALEDWSQVRTVELGHMLRAMLELSQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 165 KGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHTSQEFKELIWNIMEDIGKPNYADYFPILGCVDPSGIRR---RLACS 241
Cdd:PLN00110 165 RGEPVVVPEMLTFSMANMIGQVILSRRVFETKGSESNEFKDMVVELMTTAGYFNIGDFIPSIAWMDIQGIERgmkHLHKK 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 242 FDKLIAvfqGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPE 321
Cdd:PLN00110 245 FDKLLT---RMIEEHTASAHERKGNPDFLDVVMANQENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 322 MMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDP 401
Cdd:PLN00110 322 ILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDP 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 402 NAWQNADIFSPERFIG---CEIDVKGRDFGLLPFGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDIspkDLDMDEK 478
Cdd:PLN00110 402 DVWENPEEFRPERFLSeknAKIDPRGNDFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGV---ELNMDEA 478
                        490
                 ....*....|....*...
gi 822093467 479 FGIALQKTKPLKLIPIPR 496
Cdd:PLN00110 479 FGLALQKAVPLSAMVTPR 496
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
64-489 9.79e-99

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: 303.76  E-value: 9.79e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtiPNSVTA---GDHHKlTMSWLPVSPKWRNFRKITAVHLLSPQR 140
Cdd:cd20653    1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANR--PRFLTGkhiGYNYT-TVGSAPYGDHWRNLRRITTLEIFSSHR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 141 LDACQTFRHAKVQ----QLYeyvQECAQKGQAVDIgKAAFT--TSLNLLS----KLFFSVElaHHKSHTSQEFKELIWNI 210
Cdd:cd20653   78 LNSFSSIRRDEIRrllkRLA---RDSKGGFAKVEL-KPLFSelTFNNIMRmvagKRYYGED--VSDAEEAKLFRELVSEI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 211 MEDIGKPNYADYFPILGCVDPSGIRRRLACSFDKLIAVFQGIICERLAPDSSTTTttttddvldvllqlfkqnelTMgeI 290
Cdd:cd20653  152 FELSGAGNPADFLPILRWFDFQGLEKRVKKLAKRRDAFLQGLIDEHRKNKESGKN--------------------TM--I 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 291 NHLL-------------------VDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYL 351
Cdd:cd20653  210 DHLLslqesqpeyytdeiikgliLVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYL 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 352 QAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVkgrdFGLLP 431
Cdd:cd20653  290 QNIISETLRLYPAAPLLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEEREG----YKLIP 365
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 822093467 432 FGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDispKDLDMDEKFGIALQKTKPL 489
Cdd:cd20653  366 FGLGRRACPGAGLAQRVVGLALGSLIQCFEWERVGE---EEVDMTEGKGLTMPKAIPL 420
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
41-496 7.11e-96

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 299.43  E-value: 7.11e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  41 IIGNILEVGKKPHRSFANLAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNR--TIPNSVTAGDHHKLTMSwl 118
Cdd:PLN03112  42 IVGNLLQLGPLPHRDLASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRprTLAAVHLAYGCGDVALA-- 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 119 PVSPKWRNFRKITAVHLLSPQRLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLN-----LLSKLFFSVELA 193
Cdd:PLN03112 120 PLGPHWKRMRRICMEHLLTTKRLESFAKHRAEEARHLIQDVWEAAQTGKPVNLREVLGAFSMNnvtrmLLGKQYFGAESA 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 194 HHKShtSQEFKELIWNIMEDIGKPNYADYFPILGCVDPSGIRRRLACSFDKLIAVFQGIICERLAPDSSTTTTTTTDDVL 273
Cdd:PLN03112 200 GPKE--AMEFMHITHELFRLLGVIYLGDYLPAWRWLDPYGCEKKMREVEKRVDEFHDKIIDEHRRARSGKLPGGKDMDFV 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 274 DVLLQLFKQN---ELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPY 350
Cdd:PLN03112 278 DVLLSLPGENgkeHMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNY 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 351 LQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEID----VKGRD 426
Cdd:PLN03112 358 LRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAEGSrveiSHGPD 437
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 427 FGLLPFGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKDLDMDEKFGIALQKTKPLKLIPIPR 496
Cdd:PLN03112 438 FKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDGLRPEDIDTQEVYGMTMPKAKPLRAVATPR 507
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
63-490 1.83e-93

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: 290.54  E-value: 1.83e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLPVSPKWRNFRKITAVHLLSPQRLD 142
Cdd:cd20656    1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGQDLIWADYGPHYVKVRKLCTLELFTPKRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 143 ACQTFRH----AKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHTSQ---EFKELIWNIMEDIG 215
Cdd:cd20656   81 SLRPIREdevtAMVESIFNDCMSPENEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEqgvEFKAIVSNGLKLGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 216 KPNYADYFPILGCVDP--------SGIRRRlacsfdkliAVFQGIICE-RLAPDSSTTTTTTTDDVLDvllqLFKQNELT 286
Cdd:cd20656  161 SLTMAEHIPWLRWMFPlsekafakHGARRD---------RLTKAIMEEhTLARQKSGGGQQHFVALLT----LKEQYDLS 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 287 MGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTV 366
Cdd:cd20656  228 EDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTP 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 367 FLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMNLAI 446
Cdd:cd20656  308 LMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKGHDFRLLPFGAGRRVCPGAQLGI 387
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 822093467 447 RMLTLMLATLLQFFNWKLEGDISPKDLDMDEKFGIALQKTKPLK 490
Cdd:cd20656  388 NLVTLMLGHLLHHFSWTPPEGTPPEEIDMTENPGLVTFMRTPLQ 431
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
64-496 3.06e-93

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: 290.67  E-value: 3.06e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtiPNSvTAGDH--HKLTM-SWLPVSPKWRNFRKITAVHLLSPQR 140
Cdd:cd20654    1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSR--PKT-AAAKLmgYNYAMfGFAPYGPYWRELRKIATLELLSNRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 141 LDACQTFRHAKVQ----QLYEYV--QECAQKGQAVDIGKAAFTTSLNLL-----SKLFFSVELAHHKSHtSQEFKELIWN 209
Cdd:cd20654   78 LEKLKHVRVSEVDtsikELYSLWsnNKKGGGGVLVEMKQWFADLTFNVIlrmvvGKRYFGGTAVEDDEE-AERYKKAIRE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 210 IMEDIGKPNYADYFPILGCVDPSGIRRRLACSFDKLIAVFQGIICE-RLAPDSSTTTTTTTDDVLDVLLQLFKQNELTMG 288
Cdd:cd20654  157 FMRLAGTFVVSDAIPFLGWLDFGGHEKAMKRTAKELDSILEEWLEEhRQKRSSSGKSKNDEDDDDVMMLSILEDSQISGY 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 289 E----INHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPP 364
Cdd:cd20654  237 DadtvIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYPP 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 365 TVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGC--EIDVKGRDFGLLPFGAGRRICPGM 442
Cdd:cd20654  317 GPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTThkDIDVRGQNFELIPFGSGRRSCPGV 396
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 822093467 443 NLAIRMLTLMLATLLQFFNWKLEgdiSPKDLDMDEKFGIALQKTKPLKLIPIPR 496
Cdd:cd20654  397 SFGLQVMHLTLARLLHGFDIKTP---SNEPVDMTEGPGLTNPKATPLEVLLTPR 447
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
41-493 1.35e-90

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: 284.17  E-value: 1.35e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467   41 IIGNILEVGKK--PHRSFANLAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSV-TAGDHHKLTMSW 117
Cdd:pfam00067   9 LFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFaTSRGPFLGKGIV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  118 LPVSPKWRNFRKITAVHLLSPQRL---DACQtfrhAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAH 194
Cdd:pfam00067  89 FANGPRWRQLRRFLTPTFTSFGKLsfePRVE----EEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERFGS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  195 HKSHTSQEFKELIWNIMEDIGKPNYA--DYFPILGcVDPSGIRRRLACSFDKLIAVFQGIICERLAP-DSSTTTTTTTDD 271
Cdd:pfam00067 165 LEDPKFLELVKAVQELSSLLSSPSPQllDLFPILK-YFPGPHGRKLKRARKKIKDLLDKLIEERRETlDSAKKSPRDFLD 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  272 VLDVLLQLFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYL 351
Cdd:pfam00067 244 ALLLAKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYL 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  352 QAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDvKGRDFGLLP 431
Cdd:pfam00067 324 DAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGK-FRKSFAFLP 402
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822093467  432 FGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKdlDMDEKFGIaLQKTKPLKLIP 493
Cdd:pfam00067 403 FGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPP--DIDETPGL-LLPPKPYKLKF 461
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
62-490 2.90e-86

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: 272.19  E-value: 2.90e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  62 IHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTA---GDHHKLTMSwlPVSPKWRNFRKITAVHLLSP 138
Cdd:cd11075    1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVlfsSNKHMVNSS--PYGPLWRTLRRNLVSEVLSP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 139 QRLDACQTFRHAKVQQLYEYVQECAQ-KGQAVDIGKAAFTTSLNLLSKLFFSVELahhkshTSQEFKELIWNIME---DI 214
Cdd:cd11075   79 SRLKQFRPARRRALDNLVERLREEAKeNPGPVNVRDHFRHALFSLLLYMCFGERL------DEETVRELERVQRElllSF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 215 GKPNYADYFPILGCVdpsgIRRRLACSFDKL----IAVFQGIICERLA----PDSSTTTTTTTDDVLDVLLQLFKQNELT 286
Cdd:cd11075  153 TDFDVRDFFPALTWL----LNRRRWKKVLELrrrqEEVLLPLIRARRKrrasGEADKDYTDFLLLDLLDLKEEGGERKLT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 287 MGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTV 366
Cdd:cd11075  229 DEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGH 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 367 FLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI----GCEIDVKGRDFGLLPFGAGRRICPGM 442
Cdd:cd11075  309 FLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLaggeAADIDTGSKEIKMMPFGAGRRICPGL 388
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 822093467 443 NLAIRMLTLMLATLLQFFNWKLEGDispKDLDMDEKFGIALQKTKPLK 490
Cdd:cd11075  389 GLATLHLELFVARLVQEFEWKLVEG---EEVDFSEKQEFTVVMKNPLR 433
PLN02183 PLN02183
ferulate 5-hydroxylase
5-497 2.26e-85

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 272.49  E-value: 2.26e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467   5 TLAMILAIWFISFHFIKLLFSQQTTKLLPPGPKPLPIIGNILEVGKKPHRSFANLAKIHGPLISLRLGSVTTIVVSSADV 84
Cdd:PLN02183  10 TSPSFFLILISLFLFLGLISRLRRRLPYPPGPKGLPIIGNMLMMDQLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPEV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  85 AKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLPVSPKWRNFRKITAVHLLSPQRLDACQTFRHaKVQQLYEYVQEcaQ 164
Cdd:PLN02183  90 ARQVLQVQDSVFSNRPANIAISYLTYDRADMAFAHYGPFWRQMRKLCVMKLFSRKRAESWASVRD-EVDSMVRSVSS--N 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 165 KGQAVDIGKAAFTTSLNLLSKLFFSVelahhKSHTSQ-EFKELIWNIMEDIGKPNYADYFPILGCVDPSGIRRRLACSFD 243
Cdd:PLN02183 167 IGKPVNIGELIFTLTRNITYRAAFGS-----SSNEGQdEFIKILQEFSKLFGAFNVADFIPWLGWIDPQGLNKRLVKARK 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 244 KLIAVFQGIICERLAP--------DSSTTTTTTTDDVLDVLLQLFKQNE---------LTMGEINHLLVDIFDAGTDTTS 306
Cdd:PLN02183 242 SLDGFIDDIIDDHIQKrknqnadnDSEEAETDMVDDLLAFYSEEAKVNEsddlqnsikLTRDNIKAIIMDVMFGGTETVA 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 307 STFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKADtDVELYGYIVPK 386
Cdd:PLN02183 322 SAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAE-DAEVAGYFIPK 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 387 DAQILVNLWAIGRDPNAWQNADIFSPERFIGCEI-DVKGRDFGLLPFGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLE 465
Cdd:PLN02183 401 RSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVpDFKGSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWELP 480
                        490       500       510
                 ....*....|....*....|....*....|..
gi 822093467 466 GDISPKDLDMDEKFGiaLQKTKPLKLIPIPRY 497
Cdd:PLN02183 481 DGMKPSELDMNDVFG--LTAPRATRLVAVPTY 510
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
65-489 7.25e-78

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: 249.94  E-value: 7.25e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  65 PLISLRLGSVTTIVVSSADVAKEMFLKK---DHPLS--------NRTI---PNsvtaGDHhkltmswlpvspkWRNFRKI 130
Cdd:cd11076    4 RLMAFSLGETRVVITSHPETAREILNSPafaDRPVKesayelmfNRAIgfaPY----GEY-------------WRNLRRI 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 131 TAVHLLSPQRLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSL-NLLSKLFFSVELAHHKSHTSQEFKELIWN 209
Cdd:cd11076   67 ASNHLFSPRRIAASEPQRQAIAAQMVKAIAKEMERSGEVAVRKHLQRASLnNIMGSVFGRRYDFEAGNEEAEELGEMVRE 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 210 IMEDIGKPNYADYFPILGCVDPSGIRRRLACSFDKLIAVFQGIICERLAPDSSTTTTTTTDDVLDvllqLFKQNELTMGE 289
Cdd:cd11076  147 GYELLGAFNWSDHLPWLRWLDLQGIRRRCSALVPRVNTFVGKIIEEHRAKRSNRARDDEDDVDVL----LSLQGEEKLSD 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 290 ---INHLLVDIFdAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTV 366
Cdd:cd11076  223 sdmIAVLWEMIF-RGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGP 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 367 FL-LPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI----GCEIDVKGRDFGLLPFGAGRRICPG 441
Cdd:cd11076  302 LLsWARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVaaegGADVSVLGSDLRLAPFGAGRRVCPG 381
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 822093467 442 MNLAIRMLTLMLATLLQFFNWKLEGDispKDLDMDEKFGIALQKTKPL 489
Cdd:cd11076  382 KALGLATVHLWVAQLLHEFEWLPDDA---KPVDLSEVLKLSCEMKNPL 426
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
64-491 8.34e-78

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: 249.82  E-value: 8.34e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVT-AGDHHKLTMSWlpvSPKWRNFRKITAVHLLSPQRLD 142
Cdd:cd20617    1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEiISGGKGILFSN---GDYWKELRRFALSSLTKTKLKK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 143 ACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHTSQEFKELIWNIMEDIGKPNYADY 222
Cdd:cd20617   78 KMEELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDDGEFLKLVKPIEEIFKELGSGNPSDF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 223 FPILGCVDPSGIRRRLAcSFDKLIAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQNELTMGEINHLLVDIFDAGT 302
Cdd:cd20617  158 IPILLPFYFLYLKKLKK-SYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDLFLAGT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 303 DTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELYGY 382
Cdd:cd20617  237 DTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTEIGGY 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 383 IVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIgcEIDVKGRDFGLLPFGAGRRICPGMNLAIrmltlmlatlLQFF-- 460
Cdd:cd20617  317 FIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFL--ENDGNKLSEQFIPFGIGKRNCVGENLAR----------DELFlf 384
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 822093467 461 ------NWKLEGDISPKDLDmDEKFGIALqKTKPLKL 491
Cdd:cd20617  385 fanlllNFKFKSSDGLPIDE-KEVFGLTL-KPKPFKV 419
PLN02966 PLN02966
cytochrome P450 83A1
41-493 1.17e-76

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 249.28  E-value: 1.17e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  41 IIGNILEVGK-KPHRSFANLAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLP 119
Cdd:PLN02966  39 VIGNLLQLQKlNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRPPHRGHEFISYGRRDMALNH 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 120 VSPKWRNFRKITAVHLLSPQRLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELaHHKSHT 199
Cdd:PLN02966 119 YTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAADKSEVVDISELMLTFTNSVVCRQAFGKKY-NEDGEE 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 200 SQEFKELIWNIMEDIGKPNYADYFPILGCVDP-SGIRRRLACSFDKLIAVFQGIICERLAPDSsttTTTTTDDVLDVLLQ 278
Cdd:PLN02966 198 MKRFIKILYGTQSVLGKIFFSDFFPYCGFLDDlSGLTAYMKECFERQDTYIQEVVNETLDPKR---VKPETESMIDLLME 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 279 LFKQ----NELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQ--IQESDIINLPYLQ 352
Cdd:PLN02966 275 IYKEqpfaSEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGStfVTEDDVKNLPYFR 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 353 AIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCEIDVKGRDFGLLP 431
Cdd:PLN02966 355 ALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKGTDYEFIP 434
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822093467 432 FGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKDLDMDEKFGIALQKTKPLKLIP 493
Cdd:PLN02966 435 FGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMKPDDINMDVMTGLAMHKSQHLKLVP 496
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
41-493 1.61e-74

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 243.45  E-value: 1.61e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  41 IIGNILEVGK-KPHRSFANLAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLP 119
Cdd:PLN03234  38 IIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGFGQ 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 120 VSPKWRNFRKITAVHLLSPQRLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHT 199
Cdd:PLN03234 118 YTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEM 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 200 sQEFKELIWNIMEDIGKPNYADYFPILGCVDP-SGIRRRLACSFDKLIAVFQGIICERLAPDSSTTTTTTTDDVLDvllQ 278
Cdd:PLN03234 198 -KRFIDILYETQALLGTLFFSDLFPYFGFLDNlTGLSARLKKAFKELDTYLQELLDETLDPNRPKQETESFIDLLM---Q 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 279 LFKQN----ELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAI 354
Cdd:PLN03234 274 IYKDQpfsiKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAV 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 355 IKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCE--IDVKGRDFGLLP 431
Cdd:PLN03234 354 IKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPERFMKEHkgVDFKGQDFELLP 433
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822093467 432 FGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKDLDMDEKFGIALQKTKPLKLIP 493
Cdd:PLN03234 434 FGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKGIKPEDIKMDVMTGLAMHKKEHLVLAP 495
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
63-445 1.57e-60

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: 204.75  E-value: 1.57e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtiPNSVT---AGDHHK-LTMSwlPVSPKWRNFRKI--TAVHll 136
Cdd:cd11027    1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGR--PKLFTfdlFSRGGKdIAFG--DYSPTWKLHRKLahSALR-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 137 spQRLDACQTFRhAKVQQLYEYVQEC--AQKGQAVDIGKAAFTTSLNLLSKLFFSvelahhKSHTS--QEFKELIW---N 209
Cdd:cd11027   75 --LYASGGPRLE-EKIAEEAEKLLKRlaSQEGQPFDPKDELFLAVLNVICSITFG------KRYKLddPEFLRLLDlndK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 210 IMEDIGKPNYADYFPILGCVdPSGIRRRLACSFDKLIAVFQ--------------------GIICERLAPDSSTTTtttt 269
Cdd:cd11027  146 FFELLGAGSLLDIFPFLKYF-PNKALRELKELMKERDEILRkkleehketfdpgnirdltdALIKAKKEAEDEGDE---- 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 270 ddvldvllqlfKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLP 349
Cdd:cd11027  221 -----------DSGLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLP 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 350 YLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceIDVKGRDF-- 427
Cdd:cd11027  290 YLEATIAEVLRLSSVVPLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERF----LDENGKLVpk 365
                        410       420
                 ....*....|....*....|
gi 822093467 428 --GLLPFGAGRRICPGMNLA 445
Cdd:cd11027  366 peSFLPFSAGRRVCLGESLA 385
PLN02655 PLN02655
ent-kaurene oxidase
41-496 3.43e-60

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 204.98  E-value: 3.43e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  41 IIGNILEVG-KKPHRSFANLAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLP 119
Cdd:PLN02655   9 VIGNLLQLKeKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVLTRDKSMVATSD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 120 VSPKWRNFRKITAVHLLSPQRLDACQTFRHAKVQQLYEYV-QECAQKGQAVDIGKAAFTTSLNLLS------KLFFSVEL 192
Cdd:PLN02655  89 YGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSGLhALVKDDPHSPVNFRDVFENELFGLSliqalgEDVESVYV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 193 AHHKSHTSQE--FKELIWNIMEDIGKPNYADYFPILgcvdpSGIRRRlacSFDKLI--------AVFQGIICERLAPDSS 262
Cdd:PLN02655 169 EELGTEISKEeiFDVLVHDMMMCAIEVDWRDFFPYL-----SWIPNK---SFETRVqttefrrtAVMKALIKQQKKRIAR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 263 TTTTTTTDDVLdvllqLFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGkDKQIQE 342
Cdd:PLN02655 241 GEERDCYLDFL-----LSEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCG-DERVTE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 343 SDIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDV 422
Cdd:PLN02655 315 EDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYES 394
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822093467 423 KGRdFGLLPFGAGRRICPGMNLAIRMLTLMLATLLQFFNWKL-EGDISPKDLdmdekFGIALQKTKPLKLIPIPR 496
Cdd:PLN02655 395 ADM-YKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLrEGDEEKEDT-----VQLTTQKLHPLHAHLKPR 463
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
64-446 8.90e-60

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: 201.59  E-value: 8.90e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMfLKKDHPLSNRTIPNSVTAGDHHKLTMSWLpVSPKWRNFRKITAvHLLSPQRLDA 143
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREV-LRDPRDFSSDAGPGLPALGDFLGDGLLTL-DGPEHRRLRRLLA-PAFTPRALAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 144 CQTFRHAKVQQLYEYVQECAQKGqaVDIGKAAFTTSLNLLSKLFFSVELAHHkshtSQEFKELIWNIMEDIGKPnyadyf 223
Cdd:cd00302   78 LRPVIREIARELLDRLAAGGEVG--DDVADLAQPLALDVIARLLGGPDLGED----LEELAELLEALLKLLGPR------ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 224 piLGCVDPSGIRRRLACSFDKLIAVFQGIICERLAPDSSTTTTTTTDdvldvllQLFKQNELTMGEINHLLVDIFDAGTD 303
Cdd:cd00302  146 --LLRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDLLLLA-------DADDGGGLSDEEIVAELLTLLLAGHE 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 304 TTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDkqiQESDIINLPYLQAIIKETLRLHPPtVFLLPRKADTDVELYGYI 383
Cdd:cd00302  217 TTASLLAWALYLLARHPEVQERLRAEIDAVLGDG---TPEDLSKLPYLEAVVEETLRLYPP-VPLLPRVATEDVELGGYT 292
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822093467 384 VPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRdfgLLPFGAGRRICPGMNLAI 446
Cdd:cd00302  293 IPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEPRYA---HLPFGAGPHRCLGARLAR 352
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
70-496 1.68e-58

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: 199.90  E-value: 1.68e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  70 RLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLPVSPKWRNFRKITAVHLLSPQRLDACQTFRH 149
Cdd:cd20658    7 RLGNTHVIPVTCPKIAREILRKQDAVFASRPLTYATEIISGGYKTTVISPYGEQWKKMRKVLTTELMSPKRHQWLHGKRT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 150 AKVQQLYEYVQECAQK---GQAVDIGKAAFTTSLNLLSKLFFSVElahHKSHTSQ---------EFKELIWNIMEDIGKP 217
Cdd:cd20658   87 EEADNLVAYVYNMCKKsngGGLVNVRDAARHYCGNVIRKLMFGTR---YFGKGMEdggpgleevEHMDAIFTALKCLYAF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 218 NYADYFPILGCVDPSGIRRRLACSFdKLIAVFQG-IICERLapdsstttttttddvldvllQLFKQNE------------ 284
Cdd:cd20658  164 SISDYLPFLRGLDLDGHEKIVREAM-RIIRKYHDpIIDERI--------------------KQWREGKkkeeedwldvfi 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 ----------LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAI 354
Cdd:cd20658  223 tlkdengnplLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKAC 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 355 IKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI--GCEIDVKGRDFGLLPF 432
Cdd:cd20658  303 AREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLneDSEVTLTEPDLRFISF 382
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822093467 433 GAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKDLdMDEKFGIALqkTKPLKLIPIPR 496
Cdd:cd20658  383 STGRRGCPGVKLGTAMTVMLLARLLQGFTWTLPPNVSSVDL-SESKDDLFM--AKPLVLVAKPR 443
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
64-445 9.78e-58

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: 197.03  E-value: 9.78e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtiPNSVTAGD--HHKLTMSWLPVSPKWRNFRKITAvHLLSPQRL 141
Cdd:cd11065    2 GPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSR--PRMPMAGElmGWGMRLLLMPYGPRWRLHRRLFH-QLLNPSAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 142 DacqtfRHAKVQQ------LYEYVQEcaqkgqAVDIGKAAFTTSLNLLSKLFFSVELahhKSHTSQEFKELIW--NIMED 213
Cdd:cd11065   79 R-----KYRPLQEleskqlLRDLLES------PDDFLDHIRRYAASIILRLAYGYRV---PSYDDPLLRDAEEamEGFSE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 214 IGKPNYA--DYFPILGCVdPS----GIRRRLACSFDKLIAVFQGI-------ICERLAPDSstttttttdDVLDVLLQLF 280
Cdd:cd11065  145 AGSPGAYlvDFFPFLRYL-PSwlgaPWKRKARELRELTRRLYEGPfeaakerMASGTATPS---------FVKDLLEELD 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLR 360
Cdd:cd11065  215 KEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLR 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 361 LHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI-GCEIDVKGRDFGLLPFGAGRRIC 439
Cdd:cd11065  295 WRPVAPLGIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLdDPKGTPDPPDPPHFAFGFGRRIC 374

                 ....*.
gi 822093467 440 PGMNLA 445
Cdd:cd11065  375 PGRHLA 380
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
41-446 1.62e-53

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 188.02  E-value: 1.62e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  41 IIGNILEVGKK-PHRSFANLAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTiPNSV----TA-------- 107
Cdd:PLN02394  40 IFGNWLQVGDDlNHRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRT-RNVVfdifTGkgqdmvft 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 108 --GDHhkltmswlpvspkWRNFRKITAVhllspqrldacqTFRHAKVQQLYEYV--QECAQKGQAVDIGKAAFTTSL--- 180
Cdd:PLN02394 119 vyGDH-------------WRKMRRIMTV------------PFFTNKVVQQYRYGweEEADLVVEDVRANPEAATEGVvir 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 181 --------NLLSKLFF-----SVE---------LAHHKSHTSQEFKEliwnimedigkpNYADYFPILGCVdpsgIRRRL 238
Cdd:PLN02394 174 rrlqlmmyNIMYRMMFdrrfeSEDdplflklkaLNGERSRLAQSFEY------------NYGDFIPILRPF----LRGYL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 239 A-CS--FDKLIAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQNEltmGEINH-----LLVDIFDAGTDTTSSTFE 310
Cdd:PLN02394 238 KiCQdvKERRLALFKDYFVDERKKLMSAKGMDKEGLKCAIDHILEAQKK---GEINEdnvlyIVENINVAAIETTLWSIE 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 311 WVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQI 390
Cdd:PLN02394 315 WGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGYDIPAESKI 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 822093467 391 LVNLWAIGRDPNAWQNADIFSPERFIGCE--IDVKGRDFGLLPFGAGRRICPGMNLAI 446
Cdd:PLN02394 395 LVNAWWLANNPELWKNPEEFRPERFLEEEakVEANGNDFRFLPFGVGRRSCPGIILAL 452
PLN00168 PLN00168
Cytochrome P450; Provisional
59-496 2.36e-51

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 182.46  E-value: 2.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  59 LAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLPVSPKWRNFRKITAVHLLSP 138
Cdd:PLN00168  66 LIARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVASSRLLGESDNTITRSSYGPVWRLLRRNLVAETLHP 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 139 QRLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHTSqEFKELIWNIMEDIGKPN 218
Cdd:PLN00168 146 SRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVETFQYAMFCLLVLMCFGERLDEPAVRAI-AAAQRDWLLYVSKKMSV 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 219 YAdYFPILGCVDPSG-------IRRRLACSFDKLI---AVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQN--ELT 286
Cdd:PLN00168 225 FA-FFPAVTKHLFRGrlqkalaLRRRQKELFVPLIdarREYKNHLGQGGEPPKKETTFEHSYVDTLLDIRLPEDGdrALT 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 287 MGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDK-QIQESDIINLPYLQAIIKETLRLHPPT 365
Cdd:PLN00168 304 DDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQeEVSEEDVHKMPYLKAVVLEGLRKHPPA 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 366 VFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI----GCEIDVKG-RDFGLLPFGAGRRICP 440
Cdd:PLN00168 384 HFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLaggdGEGVDVTGsREIRMMPFGVGRRICA 463
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 822093467 441 GMNLAIRMLTLMLATLLQFFNWK-LEGDispkDLDMDEKFGIALQKTKPLKLIPIPR 496
Cdd:PLN00168 464 GLGIAMLHLEYFVANMVREFEWKeVPGD----EVDFAEKREFTTVMAKPLRARLVPR 516
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
63-490 4.82e-50

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: 176.74  E-value: 4.82e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtiPNSVTAG---DHHKlTMSWLPVSPKWRNFRKI--TAVHLLS 137
Cdd:cd20673    1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGR--PRMVTTDllsRNGK-DIAFADYSATWQLHRKLvhSAFALFG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 138 P--QRLDA--CQtfrhaKVQQLYEYVQECAqkGQAVDIGKAAFTTSLNLLSKLFFSVelAHHKS----HTSQEFKEliwN 209
Cdd:cd20673   78 EgsQKLEKiiCQ-----EASSLCDTLATHN--GESIDLSPPLFRAVTNVICLLCFNS--SYKNGdpelETILNYNE---G 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 210 IMEDIGKPNYADYFPIL------------GCVDpsgIRRRL----------ACSFDKLIAVFQGIICERLAPDSSTTTTT 267
Cdd:cd20673  146 IVDTVAKDSLVDIFPWLqifpnkdleklkQCVK---IRDKLlqkkleehkeKFSSDSIRDLLDALLQAKMNAENNNAGPD 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 268 ttddvldvllqlfkQNELTMGEiNHLLV---DIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESD 344
Cdd:cd20673  223 --------------QDSVGLSD-DHILMtvgDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSD 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 345 IINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI---GCEID 421
Cdd:cd20673  288 RNHLPLLEATIREVLRIRPVAPLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLdptGSQLI 367
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822093467 422 VKGRDFglLPFGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKDLdmDEKFGIALQkTKPLK 490
Cdd:cd20673  368 SPSLSY--LPFGAGPRVCLGEALARQELFLFMAWLLQRFDLEVPDGGQLPSL--EGKFGVVLQ-IDPFK 431
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
63-445 1.08e-48

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: 173.10  E-value: 1.08e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFlKKDHPLSNRTIPNSVTA-GDHHKLTMSWLPVS-PKWRNFRKITAVHLLSPQ- 139
Cdd:cd11054    4 YGPIVREKLGGRDIVHLFDPDDIEKVF-RNEGKYPIRPSLEPLEKyRKKRGKPLGLLNSNgEEWHRLRSAVQKPLLRPKs 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 140 -----------------RLDACQTFRHAKV----QQLYEYVQECaqkgqavdIGKAAFTTSLNLLSKlffsvelahHKSH 198
Cdd:cd11054   83 vasylpainevaddfveRIRRLRDEDGEEVpdleDELYKWSLES--------IGTVLFGKRLGCLDD---------NPDS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 199 TSQEFKELIWNIMEDIGK----PNYADYFPilgcvdpSGIRRRLACSFDKLIAVFQGIICERLapDSSTTTTTTTDDVLD 274
Cdd:cd11054  146 DAQKLIEAVKDIFESSAKlmfgPPLWKYFP-------TPAWKKFVKAWDTIFDIASKYVDEAL--EELKKKDEEDEEEDS 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 275 VLLQLFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAI 354
Cdd:cd11054  217 LLEYLLSKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKAC 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 355 IKETLRLHPPTVFLLpRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRD-FGLLPFG 433
Cdd:cd11054  297 IKESLRLYPVAPGNG-RILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENKNIHpFASLPFG 375
                        410
                 ....*....|..
gi 822093467 434 AGRRICPGMNLA 445
Cdd:cd11054  376 FGPRMCIGRRFA 387
PTZ00404 PTZ00404
cytochrome P450; Provisional
41-487 1.86e-48

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 173.76  E-value: 1.86e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  41 IIGNILEVGKKPHRSFANLAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSwlPV 120
Cdd:PTZ00404  39 ILGNLHQLGNLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVT--SS 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 121 SPKWRNFRKITaVHLLSPQRLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHTS 200
Cdd:PTZ00404 117 GEYWKRNREIV-GKAMRKTNLKHIYDLLDDQVDVLIESMKKIESSGETFEPRYYLTKFTMSAMFKYIFNEDISFDEDIHN 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 201 QEFKELIW---NIMEDIGKPNYADYFPILGCVDPSGIRRRLACsFDKLIAVFQGIICERLA---PDSSTTTTTTTDDvld 274
Cdd:PTZ00404 196 GKLAELMGpmeQVFKDLGSGSLFDVIEITQPLYYQYLEHTDKN-FKKIKKFIKEKYHEHLKtidPEVPRDLLDLLIK--- 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 275 vllQLFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAI 354
Cdd:PTZ00404 272 ---EYGTNTDDDILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAI 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 355 IKETLRLHPPTVFLLPRKADTDVELY-GYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVkgrdfGLLPFG 433
Cdd:PTZ00404 349 IKETLRYKPVSPFGLPRSTSNDIIIGgGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSND-----AFMPFS 423
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 822093467 434 AGRRICPGMNLAIRMLTLMLATLlqFFNWKLEgDISPKDLDMDEKFGIALQKTK 487
Cdd:PTZ00404 424 IGPRNCVGQQFAQDELYLAFSNI--ILNFKLK-SIDGKKIDETEEYGLTLKPNK 474
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
63-491 4.55e-47

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: 169.02  E-value: 4.55e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKlTMSWLPVSPKWRNFRKITAVHLlspqrld 142
Cdd:cd11028    1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFISNGK-SMAFSDYGPRWKLHRKLAQNAL------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 143 acQTFRHAK------------VQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSvelaHHKSHTSQEFKELIWN- 209
Cdd:cd11028   73 --RTFSNARthnpleehvteeAEELVTELTENNGKPGPFDPRNEIYLSVGNVICAICFG----KRYSRDDPEFLELVKSn 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 210 --IMEDIGKPNYADYFPILGCVDPSGIRrrlacSFDKLIAVFQGII-------CERLAPDSSTTTTTTTDDVLDVLLQLF 280
Cdd:cd11028  147 ddFGAFVGAGNPVDVMPWLRYLTRRKLQ-----KFKELLNRLNSFIlkkvkehLDTYDKGHIRDITDALIKASEEKPEEE 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQN-ELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETL 359
Cdd:cd11028  222 KPEvGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETM 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 360 RLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI--GCEID-VKGRDFglLPFGAGR 436
Cdd:cd11028  302 RHSSFVPFTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLddNGLLDkTKVDKF--LPFGAGR 379
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 822093467 437 RICPGMNLAIRMLTLMLATLLQffnwKLEGDISPKD-LDMDEKFGIALqKTKPLKL 491
Cdd:cd11028  380 RRCLGEELARMELFLFFATLLQ----QCEFSVKPGEkLDLTPIYGLTM-KPKPFKV 430
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
64-445 2.31e-46

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: 166.62  E-value: 2.31e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMFLKKDhpLSNRtiPNSVTA-----GDHHKLTMSwlpVSPKWRNFRKITAVHLlsp 138
Cdd:cd20651    1 GDVVGLKLGKDKVVVVSGYEAVREVLSREE--FDGR--PDGFFFrlrtfGKRLGITFT---DGPFWKEQRRFVLRHL--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 139 qrldacQTFRHAKvQQLYEYVQ-ECA--------QKGQAVDIGKAAFTTSLNLLSKLFFSvelaHHKSHTSQEFKELIWN 209
Cdd:cd20651   71 ------RDFGFGR-RSMEEVIQeEAEelidllkkGEKGPIQMPDLFNVSVLNVLWAMVAG----ERYSLEDQKLRKLLEL 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 210 IME-----DIGkPNYADYFPILGCVDPSGIRRRLACSF-DKLIAVFQGIICERLA-----------------------PD 260
Cdd:cd20651  140 VHLlfrnfDMS-GGLLNQFPWLRFIAPEFSGYNLLVELnQKLIEFLKEEIKEHKKtydednprdlidaylremkkkepPS 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 261 SStttttttddvldvllqlFKQNELTMgeinhLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQI 340
Cdd:cd20651  219 SS-----------------FTDDQLVM-----ICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLP 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 341 QESDIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceI 420
Cdd:cd20651  277 TLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERF----L 352
                        410       420
                 ....*....|....*....|....*...
gi 822093467 421 DVKG---RDFGLLPFGAGRRICPGMNLA 445
Cdd:cd20651  353 DEDGkllKDEWFLPFGAGKRRCLGESLA 380
PLN03018 PLN03018
homomethionine N-hydroxylase
41-499 1.21e-45

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 167.11  E-value: 1.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  41 IIGNILE-VGKKPHRSFANLA--KIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSV-TAGDHHKlTMS 116
Cdd:PLN03018  50 ILGNLPElIMTRPRSKYFHLAmkELKTDIACFNFAGTHTITINSDEIAREAFRERDADLADRPQLSIMeTIGDNYK-SMG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 117 WLPVSPKWRNFRKITAVHLLSPQRLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHK 196
Cdd:PLN03018 129 TSPYGEQFMKMKKVITTEIMSVKTLNMLEAARTIEADNLIAYIHSMYQRSETVDVRELSRVYGYAVTMRMLFGRRHVTKE 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 197 SHTSQEFK---------ELIWNIMEDIGKPNYADYFP-ILGCVDPSGIRRRLACSFDKLIAVFQGIICERLAPDSSTTTT 266
Cdd:PLN03018 209 NVFSDDGRlgkaekhhlEVIFNTLNCLPGFSPVDYVErWLRGWNIDGQEERAKVNVNLVRSYNNPIIDERVELWREKGGK 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 267 TTTDDVLDVLLQLFKQNE---LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQES 343
Cdd:PLN03018 289 AAVEDWLDTFITLKDQNGkylVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQES 368
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 344 DIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERF-----IGC 418
Cdd:PLN03018 369 DIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHlqgdgITK 448
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 419 EIDVKGRDFGLLPFGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKDLDMDEKfgiALQKTKPLKLIPIPRYG 498
Cdd:PLN03018 449 EVTLVETEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHQDFGPLSLEEDDA---SLLMAKPLLLSVEPRLA 525

                 .
gi 822093467 499 S 499
Cdd:PLN03018 526 P 526
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
61-446 2.44e-44

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: 161.49  E-value: 2.44e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  61 KIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRT--IPNSVTAGDHHKltMSWLPVSPKWRNFRKITAVhllsp 138
Cdd:cd11074    1 KKFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTrnVVFDIFTGKGQD--MVFTVYGEHWRKMRRIMTV----- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 139 qrldacqTFRHAKVQQLYEYV--QECAQKGQAVDIGKAAFTTSLNLLSKL----------------FFSVE--------- 191
Cdd:cd11074   74 -------PFFTNKVVQQYRYGweEEAARVVEDVKKNPEAATEGIVIRRRLqlmmynnmyrimfdrrFESEDdplfvklka 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 192 LAHHKSHTSQEFKEliwnimedigkpNYADYFPILgcvDPSgIRRRLA-CS--FDKLIAVFQGIICERLAPDSSTTTTTT 268
Cdd:cd11074  147 LNGERSRLAQSFEY------------NYGDFIPIL---RPF-LRGYLKiCKevKERRLQLFKDYFVDERKKLGSTKSTKN 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 269 TDDVLDVLLQLFKQNeltMGEIN-----HLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQES 343
Cdd:cd11074  211 EGLKCAIDHILDAQK---KGEINednvlYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEP 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 344 DIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVK 423
Cdd:cd11074  288 DLHKLPYLQAVVKETLRLRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKVE 367
                        410       420
                 ....*....|....*....|....*
gi 822093467 424 --GRDFGLLPFGAGRRICPGMNLAI 446
Cdd:cd11074  368 anGNDFRYLPFGVGRRSCPGIILAL 392
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
64-445 1.71e-41

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: 153.72  E-value: 1.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMFLKKD----------HPLSNRTIPNSVTAG---DHHKLTMSWLpvspkwRNFrki 130
Cdd:cd20652    1 GSIFSLKMGSVYTVVLSDPKLIRDTFRRDEftgraplyltHGIMGGNGIICAEGDlwrDQRRFVHDWL------RQF--- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 131 tAVHLLSPQRlDACQTFRHAKVQQLYEYVQecAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKShTSQEFKELIWNI 210
Cdd:cd20652   72 -GMTKFGNGR-AKMEKRIATGVHELIKHLK--AESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDP-TWRWLRFLQEEG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 211 MEDIGKPNYADYFPILGCVdPS--GIRRRLACSFDKLIAVFQGIICE---RLAPDSSTTTTTTTDDVLDVLLQLFKQNEL 285
Cdd:cd20652  147 TKLIGVAGPVNFLPFLRHL-PSykKAIEFLVQGQAKTHAIYQKIIDEhkrRLKPENPRDAEDFELCELEKAKKEGEDRDL 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 286 TMG-----EINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLR 360
Cdd:cd20652  226 FDGfytdeQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQR 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 361 LHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFgLLPFGAGRRICP 440
Cdd:cd20652  306 IRSVVPLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEA-FIPFQTGKRMCL 384

                 ....*
gi 822093467 441 GMNLA 445
Cdd:cd20652  385 GDELA 389
PLN02971 PLN02971
tryptophan N-hydroxylase
59-492 4.16e-40

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 152.11  E-value: 4.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  59 LAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTAGDHHKLTMSWLPVSPKWRNFRKITAVHLLSP 138
Cdd:PLN02971  88 MKELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCP 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 139 QRLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHT----SQEFKELIWNIMEDI 214
Cdd:PLN02971 168 ARHRWLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEPdggpTLEDIEHMDAMFEGL 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 215 GKP---NYADYFPILGCVDPSG---IRRRLACSFDKLiavFQGIICERLA--PDSSTTTTTTTDDVLDVLLQLFKQNELT 286
Cdd:PLN02971 248 GFTfafCISDYLPMLTGLDLNGhekIMRESSAIMDKY---HDPIIDERIKmwREGKRTQIEDFLDIFISIKDEAGQPLLT 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 287 MGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTV 366
Cdd:PLN02971 325 ADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAA 404
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 367 FLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIG--CEIDVKGRDFGLLPFGAGRRICPGMNL 444
Cdd:PLN02971 405 FNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNecSEVTLTENDLRFISFSTGKRGCAAPAL 484
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 822093467 445 AIRMLTLMLATLLQFFNWKLEGDISPKDLdMDEKFGIALqkTKPLKLI 492
Cdd:PLN02971 485 GTAITTMMLARLLQGFKWKLAGSETRVEL-MESSHDMFL--SKPLVMV 529
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
285-446 4.57e-40

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: 149.29  E-value: 4.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQ-IQESDIINLPYLQAIIKETLRLHP 363
Cdd:cd11042  208 LTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDpLTYDVLKEMPLLHACIKETLRLHP 287
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 364 PTVFLLpRKADTDVELY--GYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI-GCEIDVKGRDFGLLPFGAGRRICP 440
Cdd:cd11042  288 PIHSLM-RKARKPFEVEggGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLkGRAEDSKGGKFAYLPFGAGRHRCI 366

                 ....*.
gi 822093467 441 GMNLAI 446
Cdd:cd11042  367 GENFAY 372
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
63-445 6.33e-40

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: 149.27  E-value: 6.33e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtiPNSVTAGDHHKLTMSWLPVSpKWRNFRKItavhlLSPqrld 142
Cdd:cd11055    2 YGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNR--PLFILLDEPFDSSLLFLKGE-RWKRLRTT-----LSP---- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 143 acqTFRHAKVQQLYEYVQEC-----------AQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHhKSHTSQEFKELIWNIM 211
Cdd:cd11055   70 ---TFSSGKLKLMVPIINDCcdelveklekaAETGKPVDMKDLFQGFTLDVILSTAFGIDVDS-QNNPDDPFLKAAKKIF 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 212 EDIGKPNY-----ADYFPILGCVDPSGIRRRlacSFDKLIAVFQGIICERLAPDSSTTTTTTtddvldvllQLF------ 280
Cdd:cd11055  146 RNSIIRLFlllllFPLRLFLFLLFPFVFGFK---SFSFLEDVVKKIIEQRRKNKSSRRKDLL---------QLMldaqds 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 ----KQNELTMGEI--NHLLvdIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAI 354
Cdd:cd11055  214 dedvSKKKLTDDEIvaQSFI--FLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMV 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 355 IKETLRLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDvKGRDFGLLPFGA 434
Cdd:cd11055  292 INETLRLYPP-AFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKA-KRHPYAYLPFGA 369
                        410
                 ....*....|.
gi 822093467 435 GRRICPGMNLA 445
Cdd:cd11055  370 GPRNCIGMRFA 380
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
64-445 2.03e-39

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: 147.34  E-value: 2.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMfLKKDHPlsnrtipnsvtagDHHKLTMSWLPVS-----------PKWRNFRKita 132
Cdd:cd20620    1 GDVVRLRLGPRRVYLVTHPDHIQHV-LVTNAR-------------NYVKGGVYERLKLllgnglltsegDLWRRQRR--- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 133 vhLLSPqrldacqTFRHAKVQQLYEYVQECAQK----------GQAVDIGKAAFTTSLNLLSKLFFSVELAHHkshtSQE 202
Cdd:cd20620   64 --LAQP-------AFHRRRIAAYADAMVEATAAlldrweagarRGPVDVHAEMMRLTLRIVAKTLFGTDVEGE----ADE 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 203 FKELIWNIMEDIGKPnYADYFPILGCVdPSGIRRRLACSFDKLIAVFQGIICERLAPDSStttttttddvldvllqlfkQ 282
Cdd:cd20620  131 IGDALDVALEYAARR-MLSPFLLPLWL-PTPANRRFRRARRRLDEVIYRLIAERRAAPAD-------------------G 189
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 283 NELTMGEINHL----------------LVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGkDKQIQESDII 346
Cdd:cd20620  190 GDLLSMLLAARdeetgepmsdqqlrdeVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLP 268
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 347 NLPYLQAIIKETLRLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCeiDVKGRD 426
Cdd:cd20620  269 QLPYTEMVLQESLRLYPP-AWIIGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPE--REAARP 345
                        410       420
                 ....*....|....*....|
gi 822093467 427 -FGLLPFGAGRRICPGMNLA 445
Cdd:cd20620  346 rYAYFPFGGGPRICIGNHFA 365
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
285-445 2.54e-39

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: 147.70  E-value: 2.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLlVDIF-DAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHP 363
Cdd:cd20659  223 LTDEEIRDE-VDTFlFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYP 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 364 PtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIdvKGRD-FGLLPFGAGRRICPGM 442
Cdd:cd20659  302 P-VPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENI--KKRDpFAFIPFSAGPRNCIGQ 378

                 ...
gi 822093467 443 NLA 445
Cdd:cd20659  379 NFA 381
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
278-446 2.27e-37

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: 142.34  E-value: 2.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 278 QLFKQNELTMGEI-NHLLVDIFdAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDK---QIQESDIINLPYLQA 353
Cdd:cd11060  211 GLKDPEKVTDREVvAEALSNIL-AGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGKlssPITFAEAQKLPYLQA 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 354 IIKETLRLHPPTVFLLPRKA-DTDVELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFI-GCEIDVKGRDFGLL 430
Cdd:cd11060  290 VIKEALRLHPPVGLPLERVVpPGGATICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWLeADEEQRRMMDRADL 369
                        170
                 ....*....|....*.
gi 822093467 431 PFGAGRRICPGMNLAI 446
Cdd:cd11060  370 TFGAGSRTCLGKNIAL 385
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
63-483 3.03e-37

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: 141.84  E-value: 3.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtiPN-SVTAGDHHKLTMSWLPVSPKWRNFRKITAvhllspqrl 141
Cdd:cd20666    1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDR--PSvPLVTILTKGKGIVFAPYGPVWRQQRKFSH--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 142 dacQTFRH---------AKVQQLYEYVQECAQKgqavdIGKAAFTTSL---NLLSKLFFSVELAHHKSHTSQEFKELIWN 209
Cdd:cd20666   70 ---STLRHfglgklslePKIIEEFRYVKAEMLK-----HGGDPFNPFPivnNAVSNVICSMSFGRRFDYQDVEFKTMLGL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 210 IME--DIGKPNYADYFPILGCVD--PSGIRRRLAcSFDKLIAVF-QGIIC---ERLAPDSSTTTTTTTDDVLDVLLQLFK 281
Cdd:cd20666  142 MSRglEISVNSAAILVNICPWLYylPFGPFRELR-QIEKDITAFlKKIIAdhrETLDPANPRDFIDMYLLHIEEEQKNNA 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 282 QNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRL 361
Cdd:cd20666  221 ESSFNEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRM 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 362 HPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFgLLPFGAGRRICPG 441
Cdd:cd20666  301 TVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEA-FIPFGIGRRVCMG 379
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 822093467 442 MNLAIRMLTLMLATLLQFFNWKLEGDISPKdlDMDEKFGIAL 483
Cdd:cd20666  380 EQLAKMELFLMFVSLMQSFTFLLPPNAPKP--SMEGRFGLTL 419
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
63-445 5.62e-37

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: 141.31  E-value: 5.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPlISLRLGSVTTIVVSSADVAKEMFLKKD---HPLSNRTIPNsvTAGDHhkLTMSWLPVspkWRNFRKITAVHLLSPQ 139
Cdd:cd11070    2 LGA-VKILFVSRWNILVTKPEYLTQIFRRRDdfpKPGNQYKIPA--FYGPN--VISSEGED---WKRYRKIVAPAFNERN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 140 -RLDACQTFRHAkvQQLYEYVQECAQ--KGQAVDIGKAAFTTSLNLLSKLFFSVEL---AHHKSHTSQEFKELIWNIMed 213
Cdd:cd11070   74 nALVWEESIRQA--QRLIRYLLEEQPsaKGGGVDVRDLLQRLALNVIGEVGFGFDLpalDEEESSLHDTLNAIKLAIF-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 214 igkPNYADYFPILGCVDPSGIRRRLACS--FDKLIAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLfKQNELTMGEIN 291
Cdd:cd11070  150 ---PPLFLNFPFLDRLPWVLFPSRKRAFkdVDEFLSELLDEVEAELSADSKGKQGTESVVASRLKRAR-RSGGLTEKELL 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 292 HLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDII--NLPYLQAIIKETLRLHPPtVFLL 369
Cdd:cd11070  226 GNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEEDfpKLPYLLAVIYETLRLYPP-VQLL 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 370 PRKADTDVELY-----GYIVPKDAQILVNLWAIGRDPNAWQN-ADIFSPERFIGcEIDVKGRDFGL-------LPFGAGR 436
Cdd:cd11070  305 NRKTTEPVVVItglgqEIVIPKGTYVGYNAYATHRDPTIWGPdADEFDPERWGS-TSGEIGAATRFtpargafIPFSAGP 383

                 ....*....
gi 822093467 437 RICPGMNLA 445
Cdd:cd11070  384 RACLGRKFA 392
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
53-445 1.15e-36

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: 140.35  E-value: 1.15e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  53 HRSFANLAKIHGPLISLRLGSVTTIVVSSADVAKEMFLKKDHP--------LSN----RTIPNS-VTAGDHhkltmswlp 119
Cdd:cd20613    1 HDLLLEWAKEYGPVFVFWILHRPIVVVSDPEAVKEVLITLNLPkpprvysrLAFlfgeRFLGNGlVTEVDH--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 120 vsPKWRNFRKITAvHLLSPQRLDAC-QTFrHAKVQQLYEYVQECAQKGQAVD------------IGKAAFTTSLNLLskl 186
Cdd:cd20613   72 --EKWKKRRAILN-PAFHRKYLKNLmDEF-NESADLLVEKLSKKADGKTEVNmldefnrvtldvIAKVAFGMDLNSI--- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 187 ffsvelaHHKSHtsqEFKELIWNIMEDIGKpnyaDYFPILGCVDPSGI--RRRLACSFDKLIAVFQGIICERLA------ 258
Cdd:cd20613  145 -------EDPDS---PFPKAISLVLEGIQE----SFRNPLLKYNPSKRkyRREVREAIKFLRETGRECIEERLEalkrge 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 259 --PDSstttttttddVLDVLLQLFKQNE-LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLG 335
Cdd:cd20613  211 evPND----------ILTHILKASEEEPdFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLG 280
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 336 KDKQIQESDIINLPYLQAIIKETLRLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERF 415
Cdd:cd20613  281 SKQYVEYEDLGKLEYLSQVLKETLRLYPP-VPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERF 359
                        410       420       430
                 ....*....|....*....|....*....|
gi 822093467 416 IGCEIDVKGRdFGLLPFGAGRRICPGMNLA 445
Cdd:cd20613  360 SPEAPEKIPS-YAYFPFSLGPRSCIGQQFA 388
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
59-445 1.65e-36

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: 139.64  E-value: 1.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  59 LAKIHGPLISLRLGSV-TTIVVSSADVAKEMFLKKDHPLSNRTIPNSVTA--GDHHKLTMSwlpvSPKWRNFRKitavhL 135
Cdd:cd11053    7 LRARYGDVFTLRVPGLgPVVVLSDPEAIKQIFTADPDVLHPGEGNSLLEPllGPNSLLLLD----GDRHRRRRK-----L 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 136 LSPqrldacqTFRHAKVQQLYEYVQECA-------QKGQAVDIGKAAFTTSLNLLSKLFFSVelahHKSHTSQEFKELIW 208
Cdd:cd11053   78 LMP-------AFHGERLRAYGELIAEITereidrwPPGQPFDLRELMQEITLEVILRVVFGV----DDGERLQELRRLLP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 209 NIMEDIGKP--NYADYFPILGCVDPSGIRRRLACSFDKLIAvfqGIICE-RLAPDSStttttttddvldvllqlfKQNEL 285
Cdd:cd11053  147 RLLDLLSSPlaSFPALQRDLGPWSPWGRFLRARRRIDALIY---AEIAErRAEPDAE------------------RDDIL 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 286 TM--------------GEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDkqiQESDIINLPYL 351
Cdd:cd11053  206 SLllsardedgqplsdEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDP---DPEDIAKLPYL 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 352 QAIIKETLRLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIgceidvkGRDFG--- 428
Cdd:cd11053  283 DAVIKETLRLYPV-APLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFL-------GRKPSpye 354
                        410
                 ....*....|....*..
gi 822093467 429 LLPFGAGRRICPGMNLA 445
Cdd:cd11053  355 YLPFGGGVRRCIGAAFA 371
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
64-445 2.22e-36

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: 139.47  E-value: 2.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMFLKK-------DHPLSNRTIP---NSVTAGDHhkltmswlpvSPKWRNFRKITAV 133
Cdd:cd20674    2 GPIYRLRLGLQDVVVLNSKRTIREALVRKwadfagrPHSYTGKLVSqggQDLSLGDY----------SLLWKAHRKLTRS 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 134 HLLSPQRLDAcqtfrHAKVQQL-YEYVQEC-AQKGQAVDIGKAAFTTSLNLLSKLFFSVElaHHKSHTSQEFKELIWNIM 211
Cdd:cd20674   72 ALQLGIRNSL-----EPVVEQLtQELCERMrAQAGTPVDIQEEFSLLTCSIICCLTFGDK--EDKDTLVQAFHDCVQELL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 212 EDIGKPNYA--DYFPILGCVDPSGIRRRLacsfdKLIAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQ------- 282
Cdd:cd20674  145 KTWGHWSIQalDSIPFLRFFPNPGLRRLK-----QAVENRDHIVESQLRQHKESLVAGQWRDMTDYMLQGLGQprgekgm 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 283 NELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLH 362
Cdd:cd20674  220 GQLLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLR 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 363 PPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceIDVKGRDFGLLPFGAGRRICPGM 442
Cdd:cd20674  300 PVVPLALPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERF----LEPGAANRALLPFGCGARVCLGE 375

                 ...
gi 822093467 443 NLA 445
Cdd:cd20674  376 PLA 378
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
63-447 1.89e-35

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: 137.06  E-value: 1.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtiPNSVTagdHHKL-------TMSWLPVSPKWRNFRKITAVHL 135
Cdd:cd11066    1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSR--PTFYT---FHKVvsstqgfTIGTSPWDESCKRRRKAAASAL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 136 LSPqrldACQTFRHAKVQQLYEYVQE----CAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAhhkshtSQEFKELIWNIM 211
Cdd:cd11066   76 NRP----AVQSYAPIIDLESKSFIREllrdSAEGKGDIDPLIYFQRFSLNLSLTLNYGIRLD------CVDDDSLLLEII 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 212 ED---IGK-----PNYADYFPILGCVDPSG--------IRRRLACSFDKLIAVFQGIICERLAPDSSTTTTTTTddvldv 275
Cdd:cd11066  146 EVesaISKfrstsSNLQDYIPILRYFPKMSkfreradeYRNRRDKYLKKLLAKLKEEIEDGTDKPCIVGNILKD------ 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 276 llqlfKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNP--EMMEKAQEEIKQVLGKDKQIQESDIIN--LPYL 351
Cdd:cd11066  220 -----KESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWEDCAAEekCPYV 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 352 QAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDvKGRDFGLLP 431
Cdd:cd11066  295 VALVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGD-LIPGPPHFS 373
                        410
                 ....*....|....*.
gi 822093467 432 FGAGRRICPGMNLAIR 447
Cdd:cd11066  374 FGAGSRMCAGSHLANR 389
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
296-445 3.36e-35

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: 136.15  E-value: 3.36e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 296 DIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLH---PPTVfllPRK 372
Cdd:cd11026  233 DLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGdivPLGV---PHA 309
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822093467 373 ADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceIDVKGRdF----GLLPFGAGRRICPGMNLA 445
Cdd:cd11026  310 VTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHF----LDEQGK-FkkneAFMPFSAGKRVCLGEGLA 381
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
47-445 8.21e-35

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: 134.64  E-value: 8.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  47 EVGKKPHRSFANLAKiHGPLISLRLGSVTTIVVSSADVAKEMfLKKDHPLSNRTIPNSVTAgdHHKLTMSWLPVS--PKW 124
Cdd:COG2124   16 AFLRDPYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREV-LRDPRTFSSDGGLPEVLR--PLPLLGDSLLTLdgPEH 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 125 RNFRKITAvHLLSPQRLDAcqtfRHAKVQQL-YEYVQECAQKGQaVDIGKAAFTTSLNLLSKLFFSVELAHHkshtsQEF 203
Cdd:COG2124   92 TRLRRLVQ-PAFTPRRVAA----LRPRIREIaDELLDRLAARGP-VDLVEEFARPLPVIVICELLGVPEEDR-----DRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 204 KELIwnimedigkpnyADYFPILGCVDPSGIRRRLAcSFDKLIAVFQGIICERLA-PDSStttttttddvldvllqLF-- 280
Cdd:COG2124  161 RRWS------------DALLDALGPLPPERRRRARR-ARAELDAYLRELIAERRAePGDD----------------LLsa 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 ------KQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEikqvlgkdkqiqesdiinLPYLQAI 354
Cdd:COG2124  212 llaardDGERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE------------------PELLPAA 273
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 355 IKETLRLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERfigceidvkgRDFGLLPFGA 434
Cdd:COG2124  274 VEETLRLYPP-VPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPFGG 342
                        410
                 ....*....|.
gi 822093467 435 GRRICPGMNLA 445
Cdd:COG2124  343 GPHRCLGAALA 353
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
281-446 9.26e-35

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: 134.96  E-value: 9.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQNELTMGEI-NHllVD--IFdAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDK-QIQESDIINLPYLQAIIK 356
Cdd:cd20628  221 DGGPLTDEDIrEE--VDtfMF-AGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDrRPTLEDLNKMKYLERVIK 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 357 ETLRLHPPTVFLlPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGcEiDVKGRD-FGLLPFGAG 435
Cdd:cd20628  298 ETLRLYPSVPFI-GRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLP-E-NSAKRHpYAYIPFSAG 374
                        170
                 ....*....|.
gi 822093467 436 RRICPGMNLAI 446
Cdd:cd20628  375 PRNCIGQKFAM 385
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
281-446 1.68e-34

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: 134.30  E-value: 1.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLR 360
Cdd:cd20621  221 LEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLR 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 361 LHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI-GCEIDVKGRDFglLPFGAGRRIC 439
Cdd:cd20621  301 LYNPAPFLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLnQNNIEDNPFVF--IPFSAGPRNC 378

                 ....*..
gi 822093467 440 PGMNLAI 446
Cdd:cd20621  379 IGQHLAL 385
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
64-445 4.84e-34

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: 132.79  E-value: 4.84e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEMFLKKDH------PLSNRTI--PNS--VTAGDHHKLTmswlpvspkwrnfRKITAV 133
Cdd:cd11044   22 GPVFKTHLLGRPTVFVIGAEAVRFILSGEGKlvrygwPRSVRRLlgENSlsLQDGEEHRRR-------------RKLLAP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 134 HLlSPQRLDACQTFRHAKVQQlyeYVQECAQKGQaVDIGKAAFTTSLNLLSKLFFSVELAHHKSHTSQEFKELIWNIMEd 213
Cdd:cd11044   89 AF-SREALESYVPTIQAIVQS---YLRKWLKAGE-VALYPELRRLTFDVAARLLLGLDPEVEAEALSQDFETWTDGLFS- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 214 igkpnyadyFPILgcVDPSGIRRRLAcSFDKLIAVFQGIICERLApdsSTTTTTTTDDVLDVLLQLFKQNELTMGEINHL 293
Cdd:cd11044  163 ---------LPVP--LPFTPFGRAIR-ARNKLLARLEQAIRERQE---EENAEAKDALGLLLEAKDEDGEPLSMDELKDQ 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 294 LVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQvLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLpRKA 373
Cdd:cd11044  228 ALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDA-LGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGF-RKV 305
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822093467 374 DTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI-GCEIDVKGRdFGLLPFGAGRRICPGMNLA 445
Cdd:cd11044  306 LEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSpARSEDKKKP-FSLIPFGGGPRECLGKEFA 377
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
63-491 3.18e-32

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


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 127.90  E-value: 3.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtiPNSVT---AGDHHKLTMSwLPVSPKWRNFRKITAVHLLSPQ 139
Cdd:cd20677    1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGR--PDFYTfslIANGKSMTFS-EKYGESWKLHKKIAKNALRTFS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 140 RLDA------CQTFRH--AKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHkshtSQEFKELIwNIM 211
Cdd:cd20677   78 KEEAksstcsCLLEEHvcAEASELVKTLVELSKEKGSFDPVSLITCAVANVVCALCFGKRYDHS----DKEFLTIV-EIN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 212 EDI----GKPNYADYFPILGCVdPSGIRRRLA------------------CSFDK---------LIAVfqgiiCERLAPD 260
Cdd:cd20677  153 NDLlkasGAGNLADFIPILRYL-PSPSLKALRkfisrlnnfiaksvqdhyATYDKnhirditdaLIAL-----CQERKAE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 261 SstttttttddvldvllqlfKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQI 340
Cdd:cd20677  227 D-------------------KSAVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLP 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 341 QESDIINLPYLQAIIKETLRlHPPTV-FLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI--G 417
Cdd:cd20677  288 RFEDRKSLHYTEAFINEVFR-HSSFVpFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLdeN 366
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822093467 418 CEIDvKGRDFGLLPFGAGRRICPGMNLAIRMLTLMLATLLQffnwKLEGDISPKD-LDMDEKFGIALqKTKPLKL 491
Cdd:cd20677  367 GQLN-KSLVEKVLIFGMGVRKCLGEDVARNEIFVFLTTILQ----QLKLEKPPGQkLDLTPVYGLTM-KPKPYRL 435
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
290-446 6.90e-32

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: 127.00  E-value: 6.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 290 INHLLVDIFdAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVL--GKDKQIQESDIINLPYLQAIIKETLRLHPPtVF 367
Cdd:cd11069  237 IDQILTFLA-AGHETTSTALTWALYLLAKHPDVQERLREEIRAALpdPPDGDLSYDDLDRLPYLNAVCRETLRLYPP-VP 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 368 LLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCEIDVK----GRDFGLLPFGAGRRICPGM 442
Cdd:cd11069  315 LTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASpggaGSNYALLTFLHGPRSCIGK 394

                 ....
gi 822093467 443 NLAI 446
Cdd:cd11069  395 KFAL 398
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
63-483 1.21e-31

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: 126.07  E-value: 1.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNR-TIPNSVTAGDHHKLTMSwlpVSPKWRNFRKITavhlLSpqrl 141
Cdd:cd20664    1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRpIIPIFEDFNKGYGILFS---NGENWKEMRRFT----LT---- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 142 dacqTFR---------HAKVQQLYEYVQEC--AQKGQAVDIgkaafTTSLNL-LSKLFFSVELAHHKSHTSQEFKELIWN 209
Cdd:cd20664   70 ----TLRdfgmgkktsEDKILEEIPYLIEVfeKHKGKPFET-----TLSMNVaVSNIIASIVLGHRFEYTDPTLLRMVDR 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 210 IMEDI---GKPNYADY--FPILGCVdPSGIRRRLACSF---DKLIAVFQGIIcERLAPDSSTTTT----TTTDDVLDVLL 277
Cdd:cd20664  141 INENMkltGSPSVQLYnmFPWLGPF-PGDINKLLRNTKelnDFLMETFMKHL-DVLEPNDQRGFIdaflVKQQEEEESSD 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 278 QLFKQNELTMgeinhLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKdKQIQESDIINLPYLQAIIKE 357
Cdd:cd20664  219 SFFHDDNLTC-----SVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGS-RQPQVEHRKNMPYTDAVIHE 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 358 TLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDfGLLPFGAGRR 437
Cdd:cd20664  293 IQRFANIVPMNLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRD-AFMPFSAGRR 371
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 822093467 438 ICPGMNLAIRMLTLMLATLLQFFNWKLEGDISPKDLDMDEKFGIAL 483
Cdd:cd20664  372 VCIGETLAKMELFLFFTSLLQRFRFQPPPGVSEDDLDLTPGLGFTL 417
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
300-475 2.57e-31

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: 125.55  E-value: 2.57e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHpPTVFLLPRKADTDVEL 379
Cdd:cd11046  251 AGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLY-PQPPVLIRRAVEDDKL 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 380 --YGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGR---DFGLLPFGAGRRICPGMNLAIRMLTLMLA 454
Cdd:cd11046  330 pgGGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNEvidDFAFLPFGGGPRKCLGDQFALLEATVALA 409
                        170       180
                 ....*....|....*....|.
gi 822093467 455 TLLQffNWKLEGDISPKDLDM 475
Cdd:cd11046  410 MLLR--RFDFELDVGPRHVGM 428
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
297-446 2.67e-31

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: 125.03  E-value: 2.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 297 IFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDII-NLPYLQAIIKETLRLHPPTVFLLPRKADT 375
Cdd:cd11061  224 LIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLGPKLkSLPYLRACIDEALRLSPPVPSGLPRETPP 303
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822093467 376 D-VELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKgRDFG-LLPFGAGRRICPGMNLAI 446
Cdd:cd11061  304 GgLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELV-RARSaFIPFSIGPRGCIGKNLAY 375
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
284-445 3.84e-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: 3.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 284 ELTMGEI-NHLLVdIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGK-DKQIQESDIINLPYLQAIIKETLRL 361
Cdd:cd11056  224 ELTDEELaAQAFV-FFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKhGGELTYEALQEMKYLDQVVNETLRK 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 362 HPPTVFLLpRKA--DTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGcEIDVKGRDFGLLPFGAGRRIC 439
Cdd:cd11056  303 YPPLPFLD-RVCtkDYTLPGTDVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSP-ENKKKRHPYTYLPFGDGPRNC 380

                 ....*.
gi 822093467 440 PGMNLA 445
Cdd:cd11056  381 IGMRFG 386
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
197-445 4.33e-31

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


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 124.74  E-value: 4.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 197 SHTSQEFKELIwNIMEDIGKP----NYADYFPILGCVdPSGIRRRLACSFDKLIAVFQGIICE----------RLAPDSs 262
Cdd:cd20676  139 SHDDQELLSLV-NLSDEFGEVagsgNPADFIPILRYL-PNPAMKRFKDINKRFNSFLQKIVKEhyqtfdkdniRDITDS- 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 263 tttttttddvldvllqLFKQNE-----------LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIK 331
Cdd:cd20676  216 ----------------LIEHCQdkkldenaniqLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELD 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 332 QVLGKDKQIQESDIINLPYLQAIIKETLRlHPPTV-FLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIF 410
Cdd:cd20676  280 EVIGRERRPRLSDRPQLPYLEAFILETFR-HSSFVpFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSF 358
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 822093467 411 SPERFI---GCEIDVKGRDFGLLpFGAGRRICPGMNLA 445
Cdd:cd20676  359 RPERFLtadGTEINKTESEKVML-FGLGKRRCIGESIA 395
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
63-445 7.93e-31

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: 123.75  E-value: 7.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtipnSVTAGDHHKLTMSWLPVSP--KWRNFRKITAVHLlspqr 140
Cdd:cd20662    1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNR----PETPLRERIFNKNGLIFSSgqTWKEQRRFALMTL----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 141 ldacQTFRHAKvQQLYEYVQ-ECAQKGQAV-DIGKAAFTTSLNL---LSKLFFSVELAHHKSHTSQEFKELIWNIMEDI- 214
Cdd:cd20662   72 ----RNFGLGK-KSLEERIQeECRHLVEAIrEEKGNPFNPHFKInnaVSNIICSVTFGERFEYHDEWFQELLRLLDETVy 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 215 -----------GKPNYADYFPilgcvdpsGIRRRLACSFDKLIAVFQGIIC---ERLAPDSSTTTTTTTDDvldvllQLF 280
Cdd:cd20662  147 legspmsqlynAFPWIMKYLP--------GSHQTVFSNWKKLKLFVSDMIDkhrEDWNPDEPRDFIDAYLK------EMA 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQNELTMG-EINHLL---VDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIK 356
Cdd:cd20662  213 KYPDPTTSfNEENLIcstLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIH 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 357 ETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGcEIDVKGRDfGLLPFGAGR 436
Cdd:cd20662  293 EVQRMGNIIPLNVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLE-NGQFKKRE-AFLPFSMGK 370

                 ....*....
gi 822093467 437 RICPGMNLA 445
Cdd:cd20662  371 RACLGEQLA 379
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
280-445 1.78e-30

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: 122.79  E-value: 1.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 280 FKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQE-SDIINLPYLQAIIKET 358
Cdd:cd11059  212 LKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPFRGPPDlEDLDKLPYLNAVIRET 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 359 LRLHPPTVFLLPRKADTDVELY-GYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEID-VKGRDFGLLPFGAGR 436
Cdd:cd11059  292 LRLYPPIPGSLPRVVPEGGATIgGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGEtAREMKRAFWPFGSGS 371

                 ....*....
gi 822093467 437 RICPGMNLA 445
Cdd:cd11059  372 RMCIGMNLA 380
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
289-445 7.06e-30

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: 121.13  E-value: 7.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 289 EINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVF- 367
Cdd:cd11063  216 ELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLn 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 368 --------LLPRK--ADTDVELYgyiVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFigceIDVKGRDFGLLPFGAGR 436
Cdd:cd11063  296 srvavrdtTLPRGggPDGKSPIF---VPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERW----EDLKRPGWEYLPFNGGP 368

                 ....*....
gi 822093467 437 RICPGMNLA 445
Cdd:cd11063  369 RICLGQQFA 377
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
283-445 1.06e-29

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: 120.36  E-value: 1.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 283 NELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKA---QEEIKQVLGKDKQIQESDIINLPYLQAIIKETL 359
Cdd:cd11043  204 DSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELleeHEEIAKRKEEGEGLTWEDYKSMKYTWQVINETL 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 360 RLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRdfgLLPFGAGRRIC 439
Cdd:cd11043  284 RLAPI-VPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGVPYT---FLPFGGGPRLC 359

                 ....*.
gi 822093467 440 PGMNLA 445
Cdd:cd11043  360 PGAELA 365
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
63-445 3.86e-29

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: 118.90  E-value: 3.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFlkkdhplsnrtipnsVTAGDHHKltmswlpVSPKWRNFRKITAVHLL-SPQRL 141
Cdd:cd11049   12 HGDLVRIRLGPRPAYVVTSPELVRQVL---------------VNDRVFDK-------GGPLFDRARPLLGNGLAtCPGED 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 142 DACQ------TFRHAKVQQLYEYVQECA-------QKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHkshTSQEFKELIW 208
Cdd:cd11049   70 HRRQrrlmqpAFHRSRIPAYAEVMREEAealagswRPGRVVDVDAEMHRLTLRVVARTLFSTDLGPE---AAAELRQALP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 209 NIMEDIGKpnYADYFPILGCVDPSGIRRrlacsFDKLIAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQNELTMG 288
Cdd:cd11049  147 VVLAGMLR--RAVPPKFLERLPTPGNRR-----FDRALARLRELVDEIIAEYRASGTDRDDLLSLLLAARDEEGRPLSDE 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 289 EINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGkDKQIQESDIINLPYLQAIIKETLRLHPPtVFL 368
Cdd:cd11049  220 ELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPP-VWL 297
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822093467 369 LPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRdFGLLPFGAGRRICPGMNLA 445
Cdd:cd11049  298 LTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPR-GAFIPFGAGARKCIGDTFA 373
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
280-445 5.28e-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: 118.86  E-value: 5.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 280 FKQNELTMGEI-NHLLVDIFdAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDII-NLPYLQAIIKE 357
Cdd:cd11057  218 RNGEEFTDEEImDEIDTMIF-AGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGQFITYEDLqQLVYLEMVLKE 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 358 TLRLHPPTVFLLpRKADTDVEL-YGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGcEiDVKGRD-FGLLPFGA 434
Cdd:cd11057  297 TMRLFPVGPLVG-RETTADIQLsNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLP-E-RSAQRHpYAFIPFSA 373
                        170
                 ....*....|.
gi 822093467 435 GRRICPGMNLA 445
Cdd:cd11057  374 GPRNCIGWRYA 384
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
63-445 7.50e-29

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: 118.18  E-value: 7.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNRtiPN-----SVTAGDhhklTMSWLPVSPKWRNFRKI--TAVHL 135
Cdd:cd20675    1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGR--PDfasfrVVSGGR----SLAFGGYSERWKAHRRVahSTVRA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 136 LSPQRLDACQTF-RH--AKVQQLYEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFsvelAHHKSHTSQEFKELIWN--- 209
Cdd:cd20675   75 FSTRNPRTRKAFeRHvlGEARELVALFLRKSAGGAYFDPAPPLVVAVANVMSAVCF----GKRYSHDDAEFRSLLGRndq 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 210 IMEDIGKPNYADYFPILGCVdPSGIRRrLACSFDKLIAVFQGII-------CERLAPDSSTTTTTTTDDVLDVLLQLFKQ 282
Cdd:cd20675  151 FGRTVGAGSLVDVMPWLQYF-PNPVRT-VFRNFKQLNREFYNFVldkvlqhRETLRGGAPRDMMDAFILALEKGKSGDSG 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 283 NELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLH 362
Cdd:cd20675  229 VGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFS 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 363 ---PPTVfllPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGcEIDVKGRD--FGLLPFGAGRR 437
Cdd:cd20675  309 sfvPVTI---PHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLD-ENGFLNKDlaSSVMIFSVGKR 384

                 ....*...
gi 822093467 438 ICPGMNLA 445
Cdd:cd20675  385 RCIGEELS 392
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
297-446 1.08e-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: 117.83  E-value: 1.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 297 IFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESdIINLPYLQAIIKETLRLHPPtVFLLPRKADTD 376
Cdd:cd11052  240 FFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPSDS-LSKLKTVSMVINESLRLYPP-AVFLTRKAKED 317
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822093467 377 VELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMNLAI 446
Cdd:cd11052  318 IKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGVAKAAKHPMAFLPFGLGPRNCIGQNFAT 388
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
89-445 1.46e-28

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: 117.35  E-value: 1.46e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  89 FLKKDHPLSNR-TIPNSV-TAGDH--HKLtmswlpvspkwRnfRKITAvHLLSPQRLDACQTFRHAKVQQLYEYVQECAQ 164
Cdd:cd11062   29 RRKDPPYFYGAfGAPGSTfSTVDHdlHRL-----------R--RKALS-PFFSKRSILRLEPLIQEKVDKLVSRLREAKG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 165 KGQAVDIGKA--AFTT----------SLNLLSKLFFSVELahhkSHTSQEFKELIWNIMedigkpnyadYFPILGcVDPS 232
Cdd:cd11062   95 TGEPVNLDDAfrALTAdviteyafgrSYGYLDEPDFGPEF----LDALRALAEMIHLLR----------HFPWLL-KLLR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 233 GIRRRLACSFDKL---IAVFQGIICERLA-----PDSSTTTTTTTDDVLDVLLQLFKQNELTMGEINHLLVDIFDAGTDT 304
Cdd:cd11062  160 SLPESLLKRLNPGlavFLDFQESIAKQVDevlrqVSAGDPPSIVTSLFHALLNSDLPPSEKTLERLADEAQTLIGAGTET 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 305 TSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQE-SDIINLPYLQAIIKETLRLHPPTVFLLPRKADTDVELY-GY 382
Cdd:cd11062  240 TARTLSVATFHLLSNPEILERLREELKTAMPDPDSPPSlAELEKLPYLTAVIKEGLRLSYGVPTRLPRVVPDEGLYYkGW 319
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822093467 383 IVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKgRDFGLLPFGAGRRICPGMNLA 445
Cdd:cd11062  320 VIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEKGK-LDRYLVPFSKGSRSCLGINLA 381
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
295-446 2.26e-27

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


Pssm-ID: 410753 [Multi-domain]  Cd Length: 429  Bit Score: 113.90  E-value: 2.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 295 VDIFD-AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQES-DIINLPYLQAIIKETLRLHPpTVFLLPRK 372
Cdd:cd20660  237 VDTFMfEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSDRPATMdDLKEMKYLECVIKEALRLFP-SVPMFGRT 315
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822093467 373 ADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGcEiDVKGRD-FGLLPFGAGRRICPGMNLAI 446
Cdd:cd20660  316 LSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLP-E-NSAGRHpYAYIPFSAGPRNCIGQKFAL 388
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
285-446 6.93e-27

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


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 112.54  E-value: 6.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPP 364
Cdd:cd20639  228 MTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLYPP 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 365 TVFLLpRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQN-ADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMN 443
Cdd:cd20639  308 AVATI-RRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWGNdAAEFNPARFADGVARAAKHPLAFIPFGLGPRTCVGQN 386

                 ...
gi 822093467 444 LAI 446
Cdd:cd20639  387 LAI 389
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
124-445 1.03e-25

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


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 109.07  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 124 WRNFRKITAVHLLSPQRLDACQTFRHAKVQQL---YEYVQECAQKGQAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHTS 200
Cdd:cd20648   67 WQRLRSLLAKHMLKPKAVEAYAGVLNAVVTDLirrLRRQRSRSSPGVVKDIAGEFYKFGLEGISSVLFESRIGCLEANVP 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 201 QEFKELIWNImedigkpNYADYFPILGCVDPSGIRR-------RLACSFDKLIAVFQGIICERLAPDSSTTTTTTTDDVL 273
Cdd:cd20648  147 EETETFIQSI-------NTMFVMTLLTMAMPKWLHRlfpkpwqRFCRSWDQMFAFAKGHIDRRMAEVAAKLPRGEAIEGK 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 274 DVLLQLFKQNeLTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLgKDKQI-QESDIINLPYLQ 352
Cdd:cd20648  220 YLTYFLAREK-LPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAAL-KDNSVpSAADVARMPLLK 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 353 AIIKETLRLHPptvfLLPRKA----DTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGceIDVKGRDFG 428
Cdd:cd20648  298 AVVKEVLRLYP----VIPGNArvipDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLG--KGDTHHPYA 371
                        330
                 ....*....|....*..
gi 822093467 429 LLPFGAGRRICPGMNLA 445
Cdd:cd20648  372 SLPFGFGKRSCIGRRIA 388
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
294-484 1.71e-25

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: 108.39  E-value: 1.71e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 294 LVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKA 373
Cdd:cd20667  230 VIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAVRQC 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 374 DTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDfGLLPFGAGRRICPGMNLAIRMLTLML 453
Cdd:cd20667  310 VTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNE-AFLPFSAGHRVCLGEQLARMELFIFF 388
                        170       180       190
                 ....*....|....*....|....*....|..
gi 822093467 454 ATLLQFFNWKL-EGDispKDLDMDEKFGIALQ 484
Cdd:cd20667  389 TTLLRTFNFQLpEGV---QELNLEYVFGGTLQ 417
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
281-445 2.08e-25

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: 108.05  E-value: 2.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQNELTMGEI--NHLLVDIfdAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKET 358
Cdd:cd11058  209 EKKGLTREELeaNASLLII--AGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQLPYLNAVIQEA 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 359 LRLHPPTVFLLPRKADTD-VELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGceiDVKGRDFG-----LLPF 432
Cdd:cd11058  287 LRLYPPVPAGLPRVVPAGgATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLG---DPRFEFDNdkkeaFQPF 363
                        170
                 ....*....|...
gi 822093467 433 GAGRRICPGMNLA 445
Cdd:cd11058  364 SVGPRNCIGKNLA 376
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
300-445 2.45e-25

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: 107.79  E-value: 2.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDK-QIQESDIINLPYLQAIIKETLRLHpPTVFLLPRKADTDVE 378
Cdd:cd11083  233 AGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARvPPLLEALDRLPYLEAVARETLRLK-PVAPLLFLEPNEDTV 311
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822093467 379 LYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEID-VKGRDFGLLPFGAGRRICPGMNLA 445
Cdd:cd11083  312 VGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAaEPHDPSSLLPFGAGPRLCPGRSLA 379
PLN02302 PLN02302
ent-kaurenoic acid oxidase
244-445 8.38e-25

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 107.11  E-value: 8.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 244 KLIAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQNE-LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEM 322
Cdd:PLN02302 241 KLVALFQSIVDERRNSRKQNISPRKKDMLDLLLDAEDENGRkLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEV 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 323 MEKAQEE----IKQVLGKDKQIQESDIINLPYLQAIIKETLRL--HPPTVFllpRKADTDVELYGYIVPKDAQILVNLWA 396
Cdd:PLN02302 321 LQKAKAEqeeiAKKRPPGQKGLTLKDVRKMEYLSQVIDETLRLinISLTVF---REAKTDVEVNGYTIPKGWKVLAWFRQ 397
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 822093467 397 IGRDPNAWQNADIFSPERFIGCEIdvkgRDFGLLPFGAGRRICPGMNLA 445
Cdd:PLN02302 398 VHMDPEVYPNPKEFDPSRWDNYTP----KAGTFLPFGLGSRLCPGNDLA 442
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
279-445 9.89e-25

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: 106.28  E-value: 9.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 279 LFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKET 358
Cdd:cd20646  223 LLSSGKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKET 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 359 LRLHPptvfLLPRKA----DTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGcEIDVKGRDFGLLPFGA 434
Cdd:cd20646  303 LRLYP----VVPGNArvivEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLR-DGGLKHHPFGSIPFGY 377
                        170
                 ....*....|.
gi 822093467 435 GRRICPGMNLA 445
Cdd:cd20646  378 GVRACVGRRIA 388
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
281-441 1.17e-24

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: 106.22  E-value: 1.17e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLR 360
Cdd:cd11041  219 GEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQR 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 361 LHPPTVFLLPRKADTDVEL-YGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI------GCEIDVK----GRDFgl 429
Cdd:cd11041  299 LNPLSLVSLRRKVLKDVTLsDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYrlreqpGQEKKHQfvstSPDF-- 376
                        170
                 ....*....|..
gi 822093467 430 LPFGAGRRICPG 441
Cdd:cd11041  377 LGFGHGRHACPG 388
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
281-475 1.22e-24

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: 105.81  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLR 360
Cdd:cd20665  218 QQSEFTLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQR 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 361 ---LHPPTvflLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFgLLPFGAGRR 437
Cdd:cd20665  298 yidLVPNN---LPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDY-FMPFSAGKR 373
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 822093467 438 ICPGMNLAIRMLTLMLATLLQFFNWKLEGDisPKDLDM 475
Cdd:cd20665  374 ICAGEGLARMELFLFLTTILQNFNLKSLVD--PKDIDT 409
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
292-487 1.27e-24

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: 105.91  E-value: 1.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 292 HLLVDIFDAGTDTTSSTFeWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDII-----NLPYLQAIIKETLRLHppTV 366
Cdd:cd11040  227 AELALLWAINANTIPAAF-WLLAHILSDPELLERIREEIEPAVTPDSGTNAILDLtdlltSCPLLDSTYLETLRLH--SS 303
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 367 FLLPRKADTD-VELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGC--EIDVKGRDFGLLPFGAGRRICPGM 442
Cdd:cd11040  304 STSVRLVTEDtVLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKdgDKKGRGLPGAFRPFGGGASLCPGR 383
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 822093467 443 NLAIRMLTLMLATLLQFFNWKLEGDISPKDLDMDEKFGIALQKTK 487
Cdd:cd11040  384 HFAKNEILAFVALLLSRFDVEPVGGGDWKVPGMDESPGLGILPPK 428
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
297-491 1.42e-24

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: 105.96  E-value: 1.42e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 297 IFdAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVfLLPRKADTD 376
Cdd:cd20650  237 IF-AGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAG-RLERVCKKD 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 377 VELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceiDVKGRD----FGLLPFGAGRRICPGMNLAIRMLTLM 452
Cdd:cd20650  315 VEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERF-----SKKNKDnidpYIYLPFGSGPRNCIGMRFALMNMKLA 389
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 822093467 453 LATLLQFFNWKL--EGDIsPKDLDmdekFGIALQKTKPLKL 491
Cdd:cd20650  390 LVRVLQNFSFKPckETQI-PLKLS----LQGLLQPEKPIVL 425
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
300-445 1.57e-24

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: 105.75  E-value: 1.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVL-----GKDKQIQESDIINLPYLQAIIKETLRLHPPtVFLLPRKAD 374
Cdd:cd11064  241 AGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLpklttDESRVPTYEELKKLVYLHAALSESLRLYPP-VPFDSKEAV 319
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822093467 375 TDVELY-GYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCEIDVKGRD-FGLLPFGAGRRICPGMNLA 445
Cdd:cd11064  320 NDDVLPdGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDGGLRPESpYKFPAFNAGPRICLGKDLA 393
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
279-445 1.66e-24

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: 105.77  E-value: 1.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 279 LFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKET 358
Cdd:cd20647  227 LLVSKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKET 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 359 LRLHPptvfLLP---RKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFGLLPFGAG 435
Cdd:cd20647  307 LRLFP----VLPgngRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRVDNFGSIPFGYG 382
                        170
                 ....*....|
gi 822093467 436 RRICPGMNLA 445
Cdd:cd20647  383 IRSCIGRRIA 392
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
300-441 3.22e-24

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: 104.96  E-value: 3.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKqIQESDIINLPYLQAIIKETLRLHpPTVFLLPRKADTDVEL 379
Cdd:cd11068  241 AGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDP-PPYEQVAKLRYIRRVLDETLRLW-PTAPAFARKPKEDTVL 318
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822093467 380 YG-YIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCEIDvKGRDFGLLPFGAGRRICPG 441
Cdd:cd11068  319 GGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFR-KLPPNAWKPFGNGQRACIG 381
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
279-445 3.31e-24

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


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 104.50  E-value: 3.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 279 LFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKET 358
Cdd:cd20645  216 IYHDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKES 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 359 LRLhPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIgcEIDVKGRDFGLLPFGAGRRI 438
Cdd:cd20645  296 MRL-TPSVPFTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWL--QEKHSINPFAHVPFGIGKRM 372

                 ....*..
gi 822093467 439 CPGMNLA 445
Cdd:cd20645  373 CIGRRLA 379
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
63-484 2.26e-23

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: 102.18  E-value: 2.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  63 HGPLISLRLGSVTTIVVSSADVAKEMFLKKDHPLSNR-TIP--NSVTAGDHhkltmSWLPVSPKWRNFRKITavhLLSPQ 139
Cdd:cd20671    1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRpPIPifQAIQHGNG-----VFFSSGERWRTTRRFT---VRSMK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 140 RLDACQTFRHAKVQQLYEYVQECAQKGQAVDIGKAAFTTS-LNLLSKLFFSVELaHHKSHTSQEFKELIWNIMEDIGKP- 217
Cdd:cd20671   73 SLGMGKRTIEDKILEELQFLNGQIDSFNGKPFPLRLLGWApTNITFAMLFGRRF-DYKDPTFVSLLDLIDEVMVLLGSPg 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 218 -NYADYFPILGCVdpSGIRRRLACSFDKLIAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKQNELtMGEINHL--L 294
Cdd:cd20671  152 lQLFNLYPVLGAF--LKLHKPILDKVEEVCMILRTLIEARRPTIDGNPLHSYIEALIQKQEEDDPKETL-FHDANVLacT 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 295 VDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLhpptVFLL---PR 371
Cdd:cd20671  229 LDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRF----ITLLphvPR 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 372 KADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceIDVKGRDF---GLLPFGAGRRICPGMNLAIRM 448
Cdd:cd20671  305 CTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHF----LDAEGKFVkkeAFLPFSAGRRVCVGESLARTE 380
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 822093467 449 LTLMLATLLQFFNWKLEGDISPKDLDMDEKFGIALQ 484
Cdd:cd20671  381 LFIFFTGLLQKFTFLPPPGVSPADLDATPAAAFTMR 416
PLN02936 PLN02936
epsilon-ring hydroxylase
294-446 3.80e-23

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 102.18  E-value: 3.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 294 LVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGkDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKA 373
Cdd:PLN02936 283 LLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQ 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 374 DTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceiDVKG-------RDFGLLPFGAGRRICPGMNLAI 446
Cdd:PLN02936 362 VEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERF-----DLDGpvpnetnTDFRYIPFSGGPRKCVGDQFAL 436
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
300-445 4.63e-23

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: 101.20  E-value: 4.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKqiQESDIIN-LPYLQAIIKETLRLHPPtVFLLPRKADTDVE 378
Cdd:cd20642  245 AGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNK--PDFEGLNhLKVVTMILYEVLRLYPP-VIQLTRAIHKDTK 321
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822093467 379 LYGYIVPKDAQILVNLWAIGRDPNAWQN-ADIFSPERFI-GCEIDVKGRdFGLLPFGAGRRICPGMNLA 445
Cdd:cd20642  322 LGDLTLPAGVQVSLPILLVHRDPELWGDdAKEFNPERFAeGISKATKGQ-VSYFPFGWGPRICIGQNFA 389
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
300-446 5.36e-23

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: 101.45  E-value: 5.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTvFLLPRKADTDVEL 379
Cdd:cd20649  272 AGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPA-FRFAREAAEDCVV 350
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822093467 380 YGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGcEIDVKGRDFGLLPFGAGRRICPGMNLAI 446
Cdd:cd20649  351 LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTA-EAKQRRHPFVYLPFGAGPRSCIGMRLAL 416
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
295-446 8.11e-23

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: 100.81  E-value: 8.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 295 VDIFD-AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPtVFLLPRKA 373
Cdd:cd20678  244 VDTFMfEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPP-VPGISREL 322
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822093467 374 DTDVELY-GYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFiGCEIDVKGRDFGLLPFGAGRRICPGMNLAI 446
Cdd:cd20678  323 SKPVTFPdGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRF-SPENSSKRHSHAFLPFSAGPRNCIGQQFAM 395
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
292-445 8.50e-23

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: 100.54  E-value: 8.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 292 HLLV-DIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLP 370
Cdd:cd20663  232 RLVVaDLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVP 311
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822093467 371 RKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceIDVKGRdF----GLLPFGAGRRICPGMNLA 445
Cdd:cd20663  312 HMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHF----LDAQGH-FvkpeAFMPFSAGRRACLGEPLA 385
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
64-447 1.19e-22

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: 100.05  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467  64 GPLISLRLGSVTTIVVSSADVAKEmFLKKDHplsnrtipnsvtagDHHK---LTMSWLPVS-----------PKWRNFRK 129
Cdd:cd20615    1 GPIYRIWSGPTPEIVLTTPEHVKE-FYRDSN--------------KHHKapnNNSGWLFGQllgqcvgllsgTDWKRVRK 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 130 ItavhllspqrLDACQTFRHA----KVQQLY--EYVQECAQKGQAVDIGKAAFTTSLNLLSkLFFSVELAHhkSHTSQEF 203
Cdd:cd20615   66 V----------FDPAFSHSAAvyyiPQFSREarKWVQNLPTNSGDGRRFVIDPAQALKFLP-FRVIAEILY--GELSPEE 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 204 KELIWNI---MEDI------GKPNYADYFPILgcvdPSGIRRRLAcSFDKLIAVF-QGIICERLAPDSSTTTTtttddvl 273
Cdd:cd20615  133 KEELWDLaplREELfkyvikGGLYRFKISRYL----PTAANRRLR-EFQTRWRAFnLKIYNRARQRGQSTPIV------- 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 274 dvllQLFKQNE---LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLG-----KDKQIQESDI 345
Cdd:cd20615  201 ----KLYEAVEkgdITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREqsgypMEDYILSTDT 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 346 inlpYLQAIIKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIG-RDPNAWQNADIFSPERFigceIDVKG 424
Cdd:cd20615  277 ----LLAYCVLESLRLRPLLAFSVPESSPTDKIIGGYRIPANTPVVVDTYALNiNNPFWGPDGEAYRPERF----LGISP 348
                        410       420
                 ....*....|....*....|....*
gi 822093467 425 RDF--GLLPFGAGRRICPGMNLAIR 447
Cdd:cd20615  349 TDLryNFWRFGFGPRKCLGQHVADV 373
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
290-445 1.63e-22

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: 99.31  E-value: 1.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 290 INHLLVDIFdAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIkQVLGKDkQIQESDIINLPYLQAIIKETLRLHPPtVFLL 369
Cdd:cd11045  213 VNHMIFLMM-AAHDTTTSTLTSMAYFLARHPEWQERLREES-LALGKG-TLDYEDLGQLEVTDWVFKEALRLVPP-VPTL 288
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822093467 370 PRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMNLA 445
Cdd:cd11045  289 PRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRYAWAPFGGGAHKCIGLHFA 364
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
280-478 3.51e-22

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: 98.72  E-value: 3.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 280 FKQNELTMGEINhllvdIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETL 359
Cdd:cd20668  222 FYMKNLVMTTLN-----LFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQ 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 360 RLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceIDVKG---RDFGLLPFGAGR 436
Cdd:cd20668  297 RFGDVIPMGLARRVTKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHF----LDDKGqfkKSDAFVPFSIGK 372
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 822093467 437 RICPGMNLAIRMLTLMLATLLQffNWKLEGDISPKDLDMDEK 478
Cdd:cd20668  373 RYCFGEGLARMELFLFFTTIMQ--NFRFKSPQSPEDIDVSPK 412
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
300-446 6.61e-22

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: 98.23  E-value: 6.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVL-GKD-KQIQESDIINLPYLQAIIKETLRLHPPtVFLLPRKADTDV 377
Cdd:cd20679  255 EGHDTTASGLSWILYNLARHPEYQERCRQEVQELLkDREpEEIEWDDLAQLPFLTMCIKESLRLHPP-VTAISRCCTQDI 333
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822093467 378 ELY-GYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceiD---VKGRD-FGLLPFGAGRRICPGMNLAI 446
Cdd:cd20679  334 VLPdGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRF-----DpenSQGRSpLAFIPFSAGPRNCIGQTFAM 402
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
279-445 1.03e-21

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


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 97.48  E-value: 1.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 279 LFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVlgkdKQIQESDIINL----PYLQAI 354
Cdd:cd20643  224 LLLQDKLPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAA----RQEAQGDMVKMlksvPLLKAA 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 355 IKETLRLHPPTVfLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIdvkgRDFGLLPFGA 434
Cdd:cd20643  300 IKETLRLHPVAV-SLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDI----THFRNLGFGF 374
                        170
                 ....*....|.
gi 822093467 435 GRRICPGMNLA 445
Cdd:cd20643  375 GPRQCLGRRIA 385
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
295-446 1.26e-21

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: 97.14  E-value: 1.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 295 VDIFD-AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGK-DKQIQESDIINLPYLQAIIKETLRLHPPtVFLLPRK 372
Cdd:cd20680  248 VDTFMfEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKsDRPVTMEDLKKLRYLECVIKESLRLFPS-VPLFARS 326
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 822093467 373 ADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIgcEIDVKGRD-FGLLPFGAGRRICPGMNLAI 446
Cdd:cd20680  327 LCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFF--PENSSGRHpYAYIPFSAGPRNCIGQRFAL 399
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
300-445 2.11e-21

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: 95.97  E-value: 2.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVlgKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLlPRKADTDVEL 379
Cdd:cd20614  219 AGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA--GDVPRTPAELRRFPLAEALFRETLRLHPPVPFV-FRRVLEEIEL 295
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822093467 380 YGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDfgLLPFGAGRRICPGMNLA 445
Cdd:cd20614  296 GGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDRAPNPVE--LLQFGGGPHFCLGYHVA 359
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
297-446 2.60e-21

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


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 95.94  E-value: 2.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 297 IFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKdkQIQESDII-NLPYLQAIIKETLRLHPPTVFLlPRKADT 375
Cdd:cd20640  238 IYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKG--GPPDADSLsRMKTVTMVIQETLRLYPPAAFV-SREALR 314
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822093467 376 DVELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMNLAI 446
Cdd:cd20640  315 DMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACKPPHSYMPFGAGARTCLGQNFAM 386
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
295-478 2.76e-21

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: 96.15  E-value: 2.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 295 VDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKAD 374
Cdd:cd20670  232 LNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGVPHNVI 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 375 TDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceIDVKGR---DFGLLPFGAGRRICPGMNLAIRMLTL 451
Cdd:cd20670  312 RDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHF----LDEQGRfkkNEAFVPFSSGKRVCLGEAMARMELFL 387
                        170       180
                 ....*....|....*....|....*..
gi 822093467 452 MLATLLQffNWKLEGDISPKDLDMDEK 478
Cdd:cd20670  388 YFTSILQ--NFSLRSLVPPADIDITPK 412
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
300-445 7.82e-21

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: 94.24  E-value: 7.82e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKD------KQIQESDIIN-LPYLQAIIKETLRLHP--------- 363
Cdd:cd11051  196 AGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDpsaaaeLLREGPELLNqLPYTTAVIKETLRLFPpagtarrgp 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 364 PTVFLlprkADTDVELYgyivPKDAQIL-VNLWAIGRDPNAWQNADIFSPERFIGCEID----VKGrdfGLLPFGAGRRI 438
Cdd:cd11051  276 PGVGL----TDRDGKEY----PTDGCIVyVCHHAIHRDPEYWPRPDEFIPERWLVDEGHelypPKS---AWRPFERGPRN 344

                 ....*..
gi 822093467 439 CPGMNLA 445
Cdd:cd11051  345 CIGQELA 351
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
297-478 9.61e-21

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


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 94.46  E-value: 9.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 297 IFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKADTD 376
Cdd:cd20672  234 LFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKD 313
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 377 VELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceIDVKG---RDFGLLPFGAGRRICPGMNLAIRMLTLML 453
Cdd:cd20672  314 TLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHF----LDANGalkKSEAFMPFSTGKRICLGEGIARNELFLFF 389
                        170       180
                 ....*....|....*....|....*
gi 822093467 454 ATLLQffNWKLEGDISPKDLDMDEK 478
Cdd:cd20672  390 TTILQ--NFSVASPVAPEDIDLTPK 412
PLN02290 PLN02290
cytokinin trans-hydroxylase
298-446 9.72e-21

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 95.27  E-value: 9.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 298 FDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQEsDIINLPYLQAIIKETLRLHPPTVfLLPRKADTDV 377
Cdd:PLN02290 325 FFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVD-HLSKLTLLNMVINESLRLYPPAT-LLPRMAFEDI 402
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 378 ELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGcEIDVKGRDFglLPFGAGRRICPGMNLAI 446
Cdd:PLN02290 403 KLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAG-RPFAPGRHF--IPFAAGPRNCIGQAFAM 469
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
281-475 1.99e-20

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: 93.29  E-value: 1.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQNELTMGEINHLLV---DIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKE 357
Cdd:cd20669  215 KQDPLSHFNMETLVMtthNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHE 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 358 TLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDfGLLPFGAGRR 437
Cdd:cd20669  295 IQRFADIIPMSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKND-AFMPFSAGKR 373
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 822093467 438 ICPGMNLAIRMLTLMLATLLQffNWKLEGDISPKDLDM 475
Cdd:cd20669  374 ICLGESLARMELFLYLTAILQ--NFSLQPLGAPEDIDL 409
PLN02738 PLN02738
carotene beta-ring hydroxylase
294-491 3.50e-20

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 93.82  E-value: 3.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 294 LVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGkDKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPRKA 373
Cdd:PLN02738 396 LMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLG-DRFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSL 474
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 374 DTDVeLYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI--GCEIDVKGRDFGLLPFGAGRRICPGMNLAIRMLTL 451
Cdd:PLN02738 475 ENDM-LGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWPldGPNPNETNQNFSYLPFGGGPRKCVGDMFASFENVV 553
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 822093467 452 MLATLLQFFNWKLEGDISPKDLDMdekfGIALQKTKPLKL 491
Cdd:PLN02738 554 ATAMLVRRFDFQLAPGAPPVKMTT----GATIHTTEGLKM 589
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
278-445 1.70e-19

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: 90.67  E-value: 1.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 278 QLFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKE 357
Cdd:cd20644  221 ELLLQAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKE 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 358 TLRLHPPTVFLlPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIgcEIDVKGRDFGLLPFGAGRR 437
Cdd:cd20644  301 TLRLYPVGITV-QRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWL--DIRGSGRNFKHLAFGFGMR 377

                 ....*...
gi 822093467 438 ICPGMNLA 445
Cdd:cd20644  378 QCLGRRLA 385
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
300-445 3.37e-19

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: 90.05  E-value: 3.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQ------IQEsdIIN--LPYLQAIIKETLRlHPPTVFLLPR 371
Cdd:cd20622  273 AGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEAVAegrlptAQE--IAQarIPYLDAVIEEILR-CANTAPILSR 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 372 KADTDVELYGYIVPKDAQILVNLW---------------------AIGRDPNAWQNADI--FSPERFI-----GCEIDVK 423
Cdd:cd20622  350 EATVDTQVLGYSIPKGTNVFLLNNgpsylsppieidesrrssssaAKGKKAGVWDSKDIadFDPERWLvtdeeTGETVFD 429
                        170       180
                 ....*....|....*....|..
gi 822093467 424 GRDFGLLPFGAGRRICPGMNLA 445
Cdd:cd20622  430 PSAGPTLAFGLGPRGCFGRRLA 451
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
300-484 3.56e-19

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: 89.87  E-value: 3.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRL---HPPTVFllpRKADTD 376
Cdd:cd20661  249 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFcniVPLGIF---HATSKD 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 377 VELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDfGLLPFGAGRRICPGMNLAIRMLTLMLATL 456
Cdd:cd20661  326 AVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKE-AFVPFSLGRRHCLGEQLARMEMFLFFTAL 404
                        170       180
                 ....*....|....*....|....*...
gi 822093467 457 LQFFNWKLEGDISPkdlDMDEKFGIALQ 484
Cdd:cd20661  405 LQRFHLHFPHGLIP---DLKPKLGMTLQ 429
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
282-481 4.26e-19

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: 89.43  E-value: 4.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 282 QNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKqIQESDIIN-LPYLQAIIKETLR 360
Cdd:cd20641  228 ERKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDK-IPDADTLSkLKLMNMVLMETLR 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 361 LHPPTVFLLpRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRIC 439
Cdd:cd20641  307 LYGPVINIA-RRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHPNALLSFSLGPRAC 385
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 822093467 440 PGMNLAIRMLTLMLATLLQFFNWKLEGDI--SPKD-LDMDEKFGI 481
Cdd:cd20641  386 IGQNFAMIEAKTVLAMILQRFSFSLSPEYvhAPADhLTLQPQYGL 430
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
308-441 1.17e-17

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: 85.05  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 308 TFeWVMTELIRNPEMMEKAQEEIKQVLGKDKQ----IQESDIINLPYLQAIIKETLRLHPPTVflLPRKADTDVELYGYI 383
Cdd:cd20635  230 TF-WTLAFILSHPSVYKKVMEEISSVLGKAGKdkikISEDDLKKMPYIKRCVLEAIRLRSPGA--ITRKVVKPIKIKNYT 306
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 384 VPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCeiDVKGRDF--GLLPFGAGRRICPG 441
Cdd:cd20635  307 IPAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKA--DLEKNVFleGFVAFGGGRYQCPG 364
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
282-445 2.24e-17

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 84.60  E-value: 2.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 282 QNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEiKQVLGKDKQIQES----DIINLPYLQAIIKE 357
Cdd:PLN02196 257 KEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEE-QMAIRKDKEEGESltweDTKKMPLTSRVIQE 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 358 TLRLHPPTVFLLpRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigcEIDVKGRDFglLPFGAGRR 437
Cdd:PLN02196 336 TLRVASILSFTF-REAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRF---EVAPKPNTF--MPFGNGTH 409

                 ....*...
gi 822093467 438 ICPGMNLA 445
Cdd:PLN02196 410 SCPGNELA 417
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
289-447 1.05e-16

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: 81.75  E-value: 1.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 289 EINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEeikqvlgkDKQIqesdiinlpyLQAIIKETLRLHPPtVFL 368
Cdd:cd11080  193 DIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRA--------DRSL----------VPRAIAETLRYHPP-VQL 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 369 LPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERfigCEIDVKgRDFGL----LPFGAGRRICPGMNL 444
Cdd:cd11080  254 IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHR---EDLGIR-SAFSGaadhLAFGSGRHFCVGAAL 329

                 ...
gi 822093467 445 AIR 447
Cdd:cd11080  330 AKR 332
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
285-445 1.34e-16

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: 81.19  E-value: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEkaqeeikQVLGkdkqiQESdiinlpYLQAIIKETLRLHPP 364
Cdd:cd20629  188 LDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLE-------RVRR-----DRS------LIPAAIEEGLRWEPP 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 365 tVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNadifsPERFigceiDVKGRDFGLLPFGAGRRICPGMNL 444
Cdd:cd20629  250 -VASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPD-----PDVF-----DIDRKPKPHLVFGGGAHRCLGEHL 318

                 .
gi 822093467 445 A 445
Cdd:cd20629  319 A 319
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
279-445 2.93e-16

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: 80.87  E-value: 2.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 279 LFKQN--ELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGkDKQIQESDIINLPYLQAIIK 356
Cdd:cd20616  212 IFAQKrgELTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQKLKVLENFIN 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 357 ETLRLHpPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNaWQNADIFSPERFigcEIDVKGRDFglLPFGAGR 436
Cdd:cd20616  291 ESMRYQ-PVVDFVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEF-FPKPNEFTLENF---EKNVPSRYF--QPFGFGP 363

                 ....*....
gi 822093467 437 RICPGMNLA 445
Cdd:cd20616  364 RSCVGKYIA 372
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
162-445 5.79e-16

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: 79.88  E-value: 5.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 162 CAQKGqAVDIGKAAFTTSLNLLSKLFFSVELAHHKSHT-SQEFKELIWNIME---DIgkpnyadyfPILGCvdPSGIRRR 237
Cdd:cd20636  115 CRGPG-PVAVYTAAKSLTFRIAVRILLGLRLEEQQFTYlAKTFEQLVENLFSlplDV---------PFSGL--RKGIKAR 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 238 lacsfDKLIAVFQGIICERLAPDSSTTTTTTTDDVLDVLLQLFKqnELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELI 317
Cdd:cd20636  183 -----DILHEYMEKAIEEKLQRQQAAEYCDALDYMIHSARENGK--ELTMQELKESAVELIFAAFSTTASASTSLVLLLL 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 318 RNPEMMEKAQEEI-KQVLGKDKQ-----IQESDIINLPYLQAIIKETLRLHPPtVFLLPRKADTDVELYGYIVPKDAQIL 391
Cdd:cd20636  256 QHPSAIEKIRQELvSHGLIDQCQccpgaLSLEKLSRLRYLDCVVKEVLRLLPP-VSGGYRTALQTFELDGYQIPKGWSVM 334
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 822093467 392 VNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMNLA 445
Cdd:cd20636  335 YSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGRFNYIPFGGGVRSCIGKELA 388
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
289-445 6.55e-16

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 80.02  E-value: 6.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 289 EINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQ---IQESDIINLPYLQAIIKETLRLHPPT 365
Cdd:PLN02987 267 EIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKSDsysLEWSDYKSMPFTQCVVNETLRVANII 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 366 --VFllpRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEI-DVKGRDFglLPFGAGRRICPGM 442
Cdd:PLN02987 347 ggIF---RRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGtTVPSNVF--TPFGGGPRLCPGY 421

                 ...
gi 822093467 443 NLA 445
Cdd:PLN02987 422 ELA 424
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
290-446 3.47e-15

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 77.74  E-value: 3.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 290 INHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIkqvlgkDKQIQESDIINLPYLQAIIKETLRLHPPTVFLL 369
Cdd:PLN02169 302 IRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI------NTKFDNEDLEKLVYLHAALSESMRLYPPLPFNH 375
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822093467 370 PRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCEIDVKGR-DFGLLPFGAGRRICPGMNLAI 446
Cdd:PLN02169 376 KAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGLRHEpSYKFMAFNSGPRTCLGKHLAL 454
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
289-446 4.99e-15

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: 76.90  E-value: 4.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 289 EINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQESDIIN-LPYLQAIIKETLRLHPPtVF 367
Cdd:cd11082  220 EIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEPPLTLDLLEeMKYTRQVVKEVLRYRPP-AP 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 368 LLPRKADTDVEL-YGYIVPKDAQILVNLWAIGRDPnaWQNADIFSPERFI--GCEIDVKGRDFglLPFGAGRRICPGMNL 444
Cdd:cd11082  299 MVPHIAKKDFPLtEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSpeRQEDRKYKKNF--LVFGAGPHQCVGQEY 374

                 ..
gi 822093467 445 AI 446
Cdd:cd11082  375 AI 376
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
284-445 6.00e-15

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: 76.81  E-value: 6.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 284 ELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQ--VLGKDKQIQES----DIINLPYLQAIIKE 357
Cdd:cd20637  221 ELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELRSngILHNGCLCEGTlrldTISSLKYLDCVIKE 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 358 TLRLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRDFGLLPFGAGRR 437
Cdd:cd20637  301 VLRLFTP-VSGGYRTALQTFELDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGRFHYLPFGGGVR 379

                 ....*...
gi 822093467 438 ICPGMNLA 445
Cdd:cd20637  380 TCLGKQLA 387
PLN02774 PLN02774
brassinosteroid-6-oxidase
285-446 4.38e-14

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 74.43  E-value: 4.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEE---IKQVLGKDKQIQESDIINLPYLQAIIKETLRL 361
Cdd:PLN02774 260 LTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEhlaIRERKRPEDPIDWNDYKSMRFTRAVIFETSRL 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 362 HPPTVFLLpRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIgcEIDVKGRDFGLLpFGAGRRICPG 441
Cdd:PLN02774 340 ATIVNGVL-RKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWL--DKSLESHNYFFL-FGGGTRLCPG 415

                 ....*
gi 822093467 442 MNLAI 446
Cdd:PLN02774 416 KELGI 420
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
285-445 6.03e-14

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: 73.69  E-value: 6.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEI--KQVLGK----DKQIQESDIINLPYLQAIIKET 358
Cdd:cd20638  226 LNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELqeKGLLSTkpneNKELSMEVLEQLKYTGCVIKET 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 359 LRLHPPtvflLP---RKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKGRdFGLLPFGAG 435
Cdd:cd20638  306 LRLSPP----VPggfRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSR-FSFIPFGGG 380
                        170
                 ....*....|
gi 822093467 436 RRICPGMNLA 445
Cdd:cd20638  381 SRSCVGKEFA 390
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
300-446 4.05e-12

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 68.18  E-value: 4.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSS---TFEWVMTeliRNPEMMEKAQEEIKQVLGKDKQIQESD-IINLPYLQAIIKETLRLHPPTVFLLPRKADT 375
Cdd:PLN02426 304 AGRDTVASaltSFFWLLS---KHPEVASAIREEADRVMGPNQEAASFEeMKEMHYLHAALYESMRLFPPVQFDSKFAAED 380
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822093467 376 DVELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCEIDVKGRDFGLLPFGAGRRICPGMNLAI 446
Cdd:PLN02426 381 DVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGVFVPENPFKYPVFQAGLRVCLGKEMAL 452
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
285-445 6.78e-12

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: 67.07  E-value: 6.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEikqvlgkdkqiqesdiinlPYL-QAIIKETLRLHP 363
Cdd:cd20630  199 LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE-------------------PELlRNALEEVLRWDN 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 364 PTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERfigceiDVKGRdfglLPFGAGRRICPGMN 443
Cdd:cd20630  260 FGKMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR------DPNAN----IAFGYGPHFCIGAA 329

                 ..
gi 822093467 444 LA 445
Cdd:cd20630  330 LA 331
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
300-464 2.42e-11

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 65.96  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIK---QVLGKDKQIQESDIIN-----------------LPYLQAIIKETL 359
Cdd:PLN03195 303 AGRDTTATTLSWFVYMIMMNPHVAEKLYSELKaleKERAKEEDPEDSQSFNqrvtqfaglltydslgkLQYLHAVITETL 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 360 RLHpPTVFLLPRKA-DTDVELYGYIVPKDAQILVNLWAIGRDPNAW-QNADIFSPERFIGCEIDVKGRDFGLLPFGAGRR 437
Cdd:PLN03195 383 RLY-PAVPQDPKGIlEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDGVFQNASPFKFTAFQAGPR 461
                        170       180
                 ....*....|....*....|....*..
gi 822093467 438 ICPGMNLAIRMLTLMLATLLQFFNWKL 464
Cdd:PLN03195 462 ICLGKDSAYLQMKMALALLCRFFKFQL 488
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
284-445 2.66e-11

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 65.53  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 284 ELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEE------IKQVLGKDkqIQESDIINLPYLQAIIKE 357
Cdd:PLN03141 246 ELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVALQQLTEEnmklkrLKADTGEP--LYWTDYMSLPFTQNVITE 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 358 TLRLhPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIgcEIDVKGRDFGllPFGAGRR 437
Cdd:PLN03141 324 TLRM-GNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQ--EKDMNNSSFT--PFGGGQR 398

                 ....*...
gi 822093467 438 ICPGMNLA 445
Cdd:PLN03141 399 LCPGLDLA 406
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
303-446 7.36e-11

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: 63.94  E-value: 7.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 303 DTTSSTFeWVMTELIRNPEMMEKAQEEIKQVLGKDKQ----------IQESDIINLPYLQAIIKETLRLHPPTVFLLPRK 372
Cdd:cd20631  242 NTLPATF-WSLFYLLRCPEAMKAATKEVKRTLEKTGQkvsdggnpivLTREQLDDMPVLGSIIKEALRLSSASLNIRVAK 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 373 ADTDVEL---YGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigceIDVKGRD------------FGLLPFGAGRR 437
Cdd:cd20631  321 EDFTLHLdsgESYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRY----LDENGKEkttfykngrklkYYYMPFGSGTS 396

                 ....*....
gi 822093467 438 ICPGMNLAI 446
Cdd:cd20631  397 KCPGRFFAI 405
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
285-445 8.25e-11

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: 63.78  E-value: 8.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVlgkdkqiqesdiinlpylQAIIKETLRLHPP 364
Cdd:cd11078  205 LTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRADPSLI------------------PNAVEETLRYDSP 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 365 tVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIdvkgrdfglLPFGAGRRICPGMNL 444
Cdd:cd11078  267 -VQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDRPNARKH---------LTFGHGIHFCLGAAL 336

                 .
gi 822093467 445 A 445
Cdd:cd11078  337 A 337
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
285-445 9.92e-11

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: 63.38  E-value: 9.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEmmekAQEEIkqvlgkdkqIQESDIInlpylQAIIKETLRLHPP 364
Cdd:cd11035  186 LTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPE----DRRRL---------REDPELI-----PAAVEELLRRYPL 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 365 TVflLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERfigceidvkgRDFGLLPFGAGRRICPGMNL 444
Cdd:cd11035  248 VN--VARIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR----------KPNRHLAFGAGPHRCLGSHL 315

                 .
gi 822093467 445 A 445
Cdd:cd11035  316 A 316
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
320-445 1.08e-10

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: 63.25  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 320 PEMMEKAQEEIKQVLGKdkqiqesdiINLPYLQAIIKETLRLHPPTVFLLpRKADTDVELYGYIVPKDAQILVNLWAIGR 399
Cdd:cd20624  222 PEQAARAREEAAVPPGP---------LARPYLRACVLDAVRLWPTTPAVL-RESTEDTVWGGRTVPAGTGFLIFAPFFHR 291
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 822093467 400 DPNAWQNADIFSPERFIgceidvKGR---DFGLLPFGAGRRICPGMNLA 445
Cdd:cd20624  292 DDEALPFADRFVPEIWL------DGRaqpDEGLVPFSAGPARCPGENLV 334
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
355-445 1.49e-10

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: 62.93  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 355 IKETLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFsperfigceiDVKGRDFGLLPFGA 434
Cdd:cd11029  259 VEELLRYDGPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRL----------DITRDANGHLAFGH 328
                         90
                 ....*....|.
gi 822093467 435 GRRICPGMNLA 445
Cdd:cd11029  329 GIHYCLGAPLA 339
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
350-447 2.14e-10

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: 62.55  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 350 YLQAIIKETLRLHPptvF--LLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDvkgrDF 427
Cdd:cd11067  264 YAEAFVQEVRRFYP---FfpFVGARARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGD----PF 336
                         90       100       110
                 ....*....|....*....|....*....|..
gi 822093467 428 GLLPFGAGR-----RiCPG-------MNLAIR 447
Cdd:cd11067  337 DFIPQGGGDhatghR-CPGewitialMKEALR 367
PLN02500 PLN02500
cytochrome P450 90B1
281-467 2.23e-10

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 62.57  E-value: 2.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKQIQES-----DIINLPYLQAII 355
Cdd:PLN02500 271 KHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIARAKKQSGESelnweDYKKMEFTQCVI 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 356 KETLRLHPpTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFI------GCEIDVKGRDFGL 429
Cdd:PLN02500 351 NETLRLGN-VVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQqnnnrgGSSGSSSATTNNF 429
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 822093467 430 LPFGAGRRICPGMNLAIRMLTLMLATLLQFFNWKLEGD 467
Cdd:PLN02500 430 MPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELAEA 467
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
353-445 5.80e-10

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 60.58  E-value: 5.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 353 AIIKETLRLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNadifsPERFigceiDVKGRDFGLLPF 432
Cdd:cd11036  223 AAVAETLRYDPP-VRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPD-----PDRF-----DLGRPTARSAHF 291
                         90
                 ....*....|...
gi 822093467 433 GAGRRICPGMNLA 445
Cdd:cd11036  292 GLGRHACLGAALA 304
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
284-445 1.60e-09

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: 59.52  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 284 ELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEikqvlgkdkqiqesdiinlPYLQ-AIIKETLRLH 362
Cdd:cd11037  197 EITEDEAPLLMRDYLSAGLDTTISAIGNALWLLARHPDQWERLRAD-------------------PSLApNAFEEAVRLE 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 363 PPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNadifsPERFigceiDVKGRDFGLLPFGAGRRICPGM 442
Cdd:cd11037  258 SP-VQTFSRTTTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDD-----PDRF-----DITRNPSGHVGFGHGVHACVGQ 326

                 ...
gi 822093467 443 NLA 445
Cdd:cd11037  327 HLA 329
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
304-446 2.68e-09

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: 59.24  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 304 TTSSTFeWVMTELIRNPEMMEKAQEEIKQVLG-KDKQIQESDII--------NLPYLQAIIKETLRLH----PPTV---- 366
Cdd:cd20632  231 TIPATF-WAMYYLLRHPEALAAVRDEIDHVLQsTGQELGPDFDIhltreqldSLVYLESAINESLRLSsasmNIRVvqed 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 367 FLLPRKADTDVELY-GYIVPKDAQILvnlwaiGRDPNAWQNADIFSPERFIgcEIDVKGRDFG---------LLPFGAGR 436
Cdd:cd20632  310 FTLKLESDGSVNLRkGDIVALYPQSL------HMDPEIYEDPEVFKFDRFV--EDGKKKTTFYkrgqklkyyLMPFGSGS 381
                        170
                 ....*....|
gi 822093467 437 RICPGMNLAI 446
Cdd:cd20632  382 SKCPGRFFAV 391
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
334-445 3.28e-09

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: 58.52  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 334 LGKDKQIQESDIINLPYLQAIIKETLRLHPPTVfLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPE 413
Cdd:cd11079  210 LARHPELQARLRANPALLPAAIDEILRLDDPFV-ANRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPD 288
                         90       100       110
                 ....*....|....*....|....*....|..
gi 822093467 414 RfigceidvKGRDfgLLPFGAGRRICPGMNLA 445
Cdd:cd11079  289 R--------HAAD--NLVYGRGIHVCPGAPLA 310
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
317-446 5.01e-09

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: 58.43  E-value: 5.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 317 IRNPEMMEKAQEEIKQVLGKDKQIQESDIINLPYLQAIIKETLRLHPPtVFLLPRKADTDVELY----GYIVPKD----- 387
Cdd:cd11071  254 LAGEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPP-VPLQYGRARKDFVIEshdaSYKIKKGellvg 332
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822093467 388 AQILVNlwaigRDPNAWQNADIFSPERFIGCEIDVK-------GRDFGllPFGAGRRICPGMNLAI 446
Cdd:cd11071  333 YQPLAT-----RDPKVFDNPDEFVPDRFMGEEGKLLkhliwsnGPETE--EPTPDNKQCPGKDLVV 391
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
285-445 9.96e-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: 56.99  E-value: 9.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEikqvlgkdkqiqesdiinlPYL-QAIIKETLRLHP 363
Cdd:cd11038  210 LSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDQWRALRED-------------------PELaPAAVEEVLRWCP 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 364 pTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAwqnadiFSPERFigcEIDVKG-RDFGllpFGAGRRICPGM 442
Cdd:cd11038  271 -TTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANRDPRV------FDADRF---DITAKRaPHLG---FGGGVHHCLGA 337

                 ...
gi 822093467 443 NLA 445
Cdd:cd11038  338 FLA 340
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
300-445 2.70e-08

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


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 55.98  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQVLGKDKqIQESDIINLPYLQAIIKETLRlhppTVFLLPRKADTDvEL 379
Cdd:cd20627  213 AGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQVLGKGP-ITLEKIEQLRYCQQVLCETVR----TAKLTPVSARLQ-EL 286
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 380 YG----YIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFigCEIDVKgRDFGLLPFgAGRRICPGMNLA 445
Cdd:cd20627  287 EGkvdqHIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRF--DDESVM-KSFSLLGF-SGSQECPELRFA 352
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
285-445 3.34e-08

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: 55.64  E-value: 3.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTF----------EWVMTELIRNPEMMEKAQEEIkqvlgkdkqiqesdiinlpylqai 354
Cdd:cd20625  197 LSEDELVANCILLLVAGHETTVNLIgngllallrhPEQLALLRADPELIPAAVEEL------------------------ 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 355 iketLRLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERfigceidvkgRDFGLLPFGA 434
Cdd:cd20625  253 ----LRYDSP-VQLTARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITR----------APNRHLAFGA 317
                        170
                 ....*....|.
gi 822093467 435 GRRICPGMNLA 445
Cdd:cd20625  318 GIHFCLGAPLA 328
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
285-445 4.54e-08

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: 55.03  E-value: 4.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMmekaqeeikqvlgKDKQIQESDIInlpylQAIIKETLRLHPP 364
Cdd:cd11034  186 LSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPED-------------RRRLIADPSLI-----PNAVEEFLRFYSP 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 365 TVFLlPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADifsperfiGCEIDVKGRDFglLPFGAGRRICPGMNL 444
Cdd:cd11034  248 VAGL-ARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPD--------RIDIDRTPNRH--LAFGSGVHRCLGSHL 316

                 .
gi 822093467 445 A 445
Cdd:cd11034  317 A 317
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
284-445 5.33e-08

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: 54.84  E-value: 5.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 284 ELTMGEINHLLVDIFDAGTDTTSSTF-----------EwVMTELIRNPEMMEKAQEEIkqvlgkdkqiqesdiinlpylq 352
Cdd:cd11030  203 ELTDEELVGIAVLLLVAGHETTANMIalgtlallehpE-QLAALRADPSLVPGAVEEL---------------------- 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 353 aiiketLRLHPPTVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNadifsPERFigceiDVKGRDFGLLPF 432
Cdd:cd11030  260 ------LRYLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPD-----PDRL-----DITRPARRHLAF 323
                        170
                 ....*....|...
gi 822093467 433 GAGRRICPGMNLA 445
Cdd:cd11030  324 GHGVHQCLGQNLA 336
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
281-445 5.84e-08

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: 54.88  E-value: 5.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 281 KQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEikqvlgkdkqiqesdiinlPYL--QAIiKET 358
Cdd:cd11031  198 DDDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRAD-------------------PELvpAAV-EEL 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 359 LRLHPPT-VFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERfigceidvkgRDFGLLPFGAGRR 437
Cdd:cd11031  258 LRYIPLGaGGGFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDR----------EPNPHLAFGHGPH 327

                 ....*...
gi 822093467 438 ICPGMNLA 445
Cdd:cd11031  328 HCLGAPLA 335
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
302-446 1.20e-07

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: 53.91  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 302 TDTTSSTFeWVMTELIRNPEMMEKAQEEIKQVLGKDKQ---------IQESDI-INLPYLQAIIKETLRLHPPTVFLLPR 371
Cdd:cd20633  238 GNTGPASF-WLLLYLLKHPEAMKAVREEVEQVLKETGQevkpggpliNLTRDMlLKTPVLDSAVEETLRLTAAPVLIRAV 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 372 KADTDVELYG---YIVPK-DAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKgRDF---------GLLPFGAGRRI 438
Cdd:cd20633  317 VQDMTLKMANgreYALRKgDRLALFPYLAVQMDPEIHPEPHTFKYDRFLNPDGGKK-KDFykngkklkyYNMPWGAGVSI 395

                 ....*...
gi 822093467 439 CPGMNLAI 446
Cdd:cd20633  396 CPGRFFAV 403
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
353-414 1.07e-06

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: 50.68  E-value: 1.07e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822093467 353 AIIKETLRLHPPtVFLLPRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPER 414
Cdd:cd11032  244 GAIEEVLRYRPP-VQRTARVTTEDVELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR 304
PLN02648 PLN02648
allene oxide synthase
319-419 2.71e-05

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 46.47  E-value: 2.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 319 NPEMMEKAQEEIKQVLGK-DKQIQESDIINLPYLQAIIKETLRLHPPTVFLLPR-KADTDVE-------------LYGYi 383
Cdd:PLN02648 303 GEELQARLAEEVRSAVKAgGGGVTFAALEKMPLVKSVVYEALRIEPPVPFQYGRaREDFVIEshdaafeikkgemLFGY- 381
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 822093467 384 vpkdaQILVNlwaigRDPNAWQNADIFSPERFIGCE 419
Cdd:PLN02648 382 -----QPLVT-----RDPKVFDRPEEFVPDRFMGEE 407
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
300-446 4.66e-05

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: 45.41  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 300 AGTDTTSSTFEWVMTELIRNPEmmEKAQEEIKQVlgkDKQIQESDiiNLpyLQAIIKETLRLHPPtVFLLPRKADTDVEL 379
Cdd:cd20612  198 GGVPTQSQAFAQILDFYLRRPG--AAHLAEIQAL---ARENDEAD--AT--LRGYVLEALRLNPI-APGLYRRATTDTTV 267
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822093467 380 -----YGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPerfigceidvkGRDFGL-LPFGAGRRICPGMNLAI 446
Cdd:cd20612  268 adgggRTVSIKAGDRVFVSLASAMRDPRAFPDPERFRL-----------DRPLESyIHFGHGPHQCLGEEIAR 329
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
285-445 7.58e-05

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: 44.83  E-value: 7.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 285 LTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMMEKAQEEIKQvlgkdkqiqesdiinlpyLQAIIKETLRLHPP 364
Cdd:cd11033  205 LTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLRADPSL------------------LPTAVEEILRWASP 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 365 TVFLLpRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIF----SPERFIGceidvkgrdfgllpFGAGRRICP 440
Cdd:cd11033  267 VIHFR-RTATRDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFditrSPNPHLA--------------FGGGPHFCL 331

                 ....*
gi 822093467 441 GMNLA 445
Cdd:cd11033  332 GAHLA 336
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
311-446 1.23e-04

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: 44.36  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 311 WVMTELIRNPEMMEKAQEEIKQVLGKDKQ-------IQESDIINLPYLQAIIKETLRLHPPTvfLLPRKADTDVEL---- 379
Cdd:cd20634  243 WLLLFLLKHPEAMAAVRGEIQRIKHQRGQpvsqtltINQELLDNTPVFDSVLSETLRLTAAP--FITREVLQDMKLrlad 320
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 822093467 380 -YGYIVPK-DAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDVKgRDFGL---------LPFGAGRRICPGMNLAI 446
Cdd:cd20634  321 gQEYNLRRgDRLCLFPFLSPQMDPEIHQEPEVFKYDRFLNADGTEK-KDFYKngkrlkyynMPWGAGDNVCIGRHFAV 397
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
278-441 2.72e-03

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: 40.11  E-value: 2.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 278 QLFKQNELTMGEINHLLVDIFDAGTDTTSSTFEWVMTELIRNPEMME--KAQEEIKQvlgkdkqiqesdiinlpylqAII 355
Cdd:cd20619  179 DAARAGEITESEAIATILVFYAVGHMAIGYLIASGIELFARRPEVFTafRNDESARA--------------------AII 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822093467 356 KETLRLHPPTVFLLpRKADTDVELYGYIVPKDAQILVNLWAIGRDPNAWQNADIFSPERFIGCEIDvkgrdfglLPFGAG 435
Cdd:cd20619  239 NEMVRMDPPQLSFL-RFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTRPPAASRN--------LSFGLG 309

                 ....*.
gi 822093467 436 RRICPG 441
Cdd:cd20619  310 PHSCAG 315
 
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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