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Conserved domains on  [gi|302565346|ref|NP_001180887|]
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vitamin D 25-hydroxylase [Macaca mulatta]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
62-497 0e+00

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: 879.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  62 PHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRYGQGWVEHRRLAV 141
Cdd:cd20661    1 PHVYMKKQSQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKYGRGWTEHRKLAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 142 NSFRYFGYGQKSFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELA 221
Cdd:cd20661   81 NCFRYFGYGQKSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 222 ASASVFLYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLI 301
Cdd:cd20661  161 ASAWVFLYNAFPWIGILPFGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 302 FSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFH 381
Cdd:cd20661  241 FSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 382 ATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLF 461
Cdd:cd20661  321 ATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLF 400
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 302565346 462 FTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLIC 497
Cdd:cd20661  401 FTALLQRFHLHFPHGLIPDLKPKLGMTLQPQPYLIC 436
 
Name Accession Description Interval E-value
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
62-497 0e+00

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: 879.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  62 PHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRYGQGWVEHRRLAV 141
Cdd:cd20661    1 PHVYMKKQSQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKYGRGWTEHRKLAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 142 NSFRYFGYGQKSFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELA 221
Cdd:cd20661   81 NCFRYFGYGQKSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 222 ASASVFLYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLI 301
Cdd:cd20661  161 ASAWVFLYNAFPWIGILPFGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 302 FSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFH 381
Cdd:cd20661  241 FSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 382 ATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLF 461
Cdd:cd20661  321 ATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLF 400
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 302565346 462 FTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLIC 497
Cdd:cd20661  401 FTALLQRFHLHFPHGLIPDLKPKLGMTLQPQPYLIC 436
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
57-497 2.43e-127

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: 378.55  E-value: 2.43e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346   57 ASAELPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLF---MKMTKMGGLLNSRYGQgW 133
Cdd:pfam00067  17 GRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFatsRGPFLGKGIVFANGPR-W 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  134 VEHRRLAVNSFRYFGygQKSFESKILEETKFFTDAIETYKGRP--FDFKQLITSAVSNITNLIIFGERF-TYEDTDFQHM 210
Cdd:pfam00067  96 RQLRRFLTPTFTSFG--KLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILFGERFgSLEDPKFLEL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  211 IELFSENVELAASASVFLYNAFPWIGILPfGKHQQLFRNASVVY-DFLSRLIE--KASVNRKPQLPQHFVDAYFDEMDqg 287
Cdd:pfam00067 174 VKAVQELSSLLSSPSPQLLDLFPILKYFP-GPHGRKLKRARKKIkDLLDKLIEerRETLDSAKKSPRDFLDALLLAKE-- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  288 kNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHE 367
Cdd:pfam00067 251 -EEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKE 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  368 VLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRH 447
Cdd:pfam00067 330 TLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRN 409
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 302565346  448 CLGEQLARMEMFLFFTALLQRFHLHFPHEL-VPDLKPRLGMTLQPQPYLIC 497
Cdd:pfam00067 410 CLGERLARMEMKLFLATLLQNFEVELPPGTdPPDIDETPGLLLPPKPYKLK 460
PTZ00404 PTZ00404
cytochrome P450; Provisional
51-501 3.39e-50

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 178.76  E-value: 3.39e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  51 NIYSLAasaELPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSrYG 130
Cdd:PTZ00404  42 NLHQLG---NLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVTS-SG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 131 QGWVEHRRLAVNSFRyfgygqKSFESKILEE-TKFFTDAIETYK-----GRPFDFKQLITSAVSNITNLIIFGERFTYED 204
Cdd:PTZ00404 118 EYWKRNREIVGKAMR------KTNLKHIYDLlDDQVDVLIESMKkiessGETFEPRYYLTKFTMSAMFKYIFNEDISFDE 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 205 T----DFQHMIELFSENVELAASASvflynAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRK---PQLPQHFV 277
Cdd:PTZ00404 192 DihngKLAELMGPMEQVFKDLGSGS-----LFDVIEITQPLYYQYLEHTDKNFKKIKKFIKEKYHEHLKtidPEVPRDLL 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 278 DAYFDEMDQGKNDpsstfSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFK 357
Cdd:PTZ00404 267 DLLIKEYGTNTDD-----DILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQS 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 358 MPYTEAVLHEVLRFCNIVPLGIFHATSEDAVV-RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyfaKKE 436
Cdd:PTZ00404 342 TPYTVAIIKETLRYKPVSPFGLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPD----SND 417
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302565346 437 ALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLICAERR 501
Cdd:PTZ00404 418 AFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGKKIDETEEYGLTLKPNKFKVLLEKR 482
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
62-490 7.61e-46

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: 164.68  E-value: 7.61e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  62 PHVYMRKQSQvYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRYGQGWVEHRRLAV 141
Cdd:COG2124   21 PYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLVQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 142 NSFRyfgyGQ--KSFESKILEETKFFTDAIETykGRPFDFkqliTSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVE 219
Cdd:COG2124  100 PAFT----PRrvAALRPRIREIADELLDRLAA--RGPVDL----VEEFARPLPVIVICELLGVPEEDRDRLRRWSDALLD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 220 LAASasvflynafpwigiLPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEmdqgkndpsSTFSKEN 299
Cdd:COG2124  170 ALGP--------------LPPERRRRARRARAELDAYLRELIAERRAEPGDDLLSALLAARDDG---------ERLSDEE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 300 LIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIdlimgpngkpswddkfkmPYTEAVLHEVLRFCNIVPLGI 379
Cdd:COG2124  227 LRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLP 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 380 FHATsEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaKKEALVPFSLGRRHCLGEQLARMEMF 459
Cdd:COG2124  289 RTAT-EDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCLGAALARLEAR 358
                        410       420       430
                 ....*....|....*....|....*....|...
gi 302565346 460 LFFTALLQRFHlHFphELVPD--LKPRLGMTLQ 490
Cdd:COG2124  359 IALATLLRRFP-DL--RLAPPeeLRWRPSLTLR 388
 
Name Accession Description Interval E-value
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
62-497 0e+00

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: 879.92  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  62 PHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRYGQGWVEHRRLAV 141
Cdd:cd20661    1 PHVYMKKQSQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKYGRGWTEHRKLAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 142 NSFRYFGYGQKSFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELA 221
Cdd:cd20661   81 NCFRYFGYGQKSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 222 ASASVFLYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLI 301
Cdd:cd20661  161 ASAWVFLYNAFPWIGILPFGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRHFIDAYLDEMDQNKNDPESTFSMENLI 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 302 FSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFH 381
Cdd:cd20661  241 FSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFH 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 382 ATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLF 461
Cdd:cd20661  321 ATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLF 400
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 302565346 462 FTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLIC 497
Cdd:cd20661  401 FTALLQRFHLHFPHGLIPDLKPKLGMTLQPQPYLIC 436
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
73-496 0e+00

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: 645.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd11026    1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSN-GERWKQLRRFSLTTLRNFGMGKR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd11026   80 SIEERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLYNMF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 PWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELIIAGT 312
Cdd:cd11026  160 PPLLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSPRDFIDCFLLKMEKEKDNPNSEFHEENLVMTVLDLFFAGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 313 ETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGY 392
Cdd:cd11026  240 ETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRGY 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 393 SIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLH 472
Cdd:cd11026  320 TIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLS 399
                        410       420
                 ....*....|....*....|....*.
gi 302565346 473 FP-HELVPDLKPRL-GMTLQPQPYLI 496
Cdd:cd11026  400 SPvGPKDPDLTPRFsGFTNSPRPYQL 425
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
73-496 3.42e-155

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: 448.09  E-value: 3.42e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd20662    1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFNKNGLIFSS-GQTWKEQRRFALMTLRNFGLGKK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd20662   80 SLEERIQEECRHLVEAIREEKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSPMSQLYNAF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 PWI-GILPfGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMdQGKNDPSSTFSKENLIFSVGELIIAG 311
Cdd:cd20662  160 PWImKYLP-GSHQTVFSNWKKLKLFVSDMIDKHREDWNPDEPRDFIDAYLKEM-AKYPDPTTSFNEENLICSTLDLFFAG 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 312 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 391
Cdd:cd20662  238 TETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAVDTKLAG 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 392 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDsSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHL 471
Cdd:cd20662  318 FHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLE-NGQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTF 396
                        410       420
                 ....*....|....*....|....*
gi 302565346 472 HFPHELVPDLKPRLGMTLQPQPYLI 496
Cdd:cd20662  397 KPPPNEKLSLKFRMGITLSPVPHRI 421
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
73-496 6.23e-151

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: 437.67  E-value: 6.23e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRYGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd20666    1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKGKGIVFAPYGPVWRQQRKFSHSTLRHFGLGKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd20666   81 SLEPKIIEEFRYVKAEMLKHGGDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLMSRGLEISVNSAAILVNIC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 PWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQ-GKNDPSSTFSKENLIFSVGELIIAG 311
Cdd:cd20666  161 PWLYYLPFGPFRELRQIEKDITAFLKKIIADHRETLDPANPRDFIDMYLLHIEEeQKNNAESSFNEDYLFYIIGDLFIAG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 312 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 391
Cdd:cd20666  241 TDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 392 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHL 471
Cdd:cd20666  321 YTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTF 400
                        410       420
                 ....*....|....*....|....*.
gi 302565346 472 HFPHELV-PDLKPRLGMTLQPQPYLI 496
Cdd:cd20666  401 LLPPNAPkPSMEGRFGLTLAPCPFNI 426
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
73-494 1.17e-147

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: 429.23  E-value: 1.17e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd20664    1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYGILFSN-GENWKEMRRFTLTTLRDFGMGKK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd20664   80 TSEDKILEEIPYLIEVFEKHKGKPFETTLSMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGSPSVQLYNMF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 PWIGILPfGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELIIAGT 312
Cdd:cd20664  160 PWLGPFP-GDINKLLRNTKELNDFLMETFMKHLDVLEPNDQRGFIDAFLVKQQEEEESSDSFFHDDNLTCSVGNLFGAGT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 313 ETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNgKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGY 392
Cdd:cd20664  239 DTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSR-QPQVEHRKNMPYTDAVIHEIQRFANIVPMNLPHATTRDVTFRGY 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 393 SIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLH 472
Cdd:cd20664  318 FIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQ 397
                        410       420
                 ....*....|....*....|....*
gi 302565346 473 FPH---ELVPDLKPRLGMTLQPQPY 494
Cdd:cd20664  398 PPPgvsEDDLDLTPGLGFTLNPLPH 422
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
73-494 3.35e-144

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: 420.64  E-value: 3.35e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKM---TKMGGLLNSRYGQGWVEHRRLAVNSFRYFGY 149
Cdd:cd20663    1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLgfgPKSQGVVLARYGPAWREQRRFSVSTLRNFGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 150 GQKSFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLY 229
Cdd:cd20663   81 GKKSLEQWVTEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 230 NAFPWIGILPfGKHQQLFRNASVVYDFLSRLIEKASVNRKP-QLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELI 308
Cdd:cd20663  161 NAFPVLLRIP-GLAGKVFPGQKAFLALLDELLTEHRTTWDPaQPPRDLTDAFLAEMEKAKGNPESSFNDENLRLVVADLF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 309 IAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAV 388
Cdd:cd20663  240 SAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIE 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 389 VRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQR 468
Cdd:cd20663  320 VQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQR 399
                        410       420       430
                 ....*....|....*....|....*....|..
gi 302565346 469 FHLHfphelVPDLKPR------LGMTLQPQPY 494
Cdd:cd20663  400 FSFS-----VPAGQPRpsdhgvFAFLVSPSPY 426
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
73-496 1.23e-142

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: 416.61  E-value: 1.23e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMG-GLLNSRYGQGWVEHRRLAVNSFRYFGYGQ 151
Cdd:cd11027    1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGkDIAFGDYSPTWKLHRKLAHSALRLYASGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 152 KSFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFlyNA 231
Cdd:cd11027   81 PRLEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKFFELLGAGSLL--DI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 232 FPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKN---DPSSTFSKENLIFSVGELI 308
Cdd:cd11027  159 FPFLKYFPNKALRELKELMKERDEILRKKLEEHKETFDPGNIRDLTDALIKAKKEAEDegdEDSGLLTDDHLVMTISDIF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 309 IAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAV 388
Cdd:cd11027  239 GAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALPHKTTCDTT 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 389 VRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKK-EALVPFSLGRRHCLGEQLARMEMFLFFTALLQ 467
Cdd:cd11027  319 LRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVPKpESFLPFSAGRRVCLGESLAKAELFLFLARLLQ 398
                        410       420       430
                 ....*....|....*....|....*....|
gi 302565346 468 RFHLHFPH-ELVPDLKPRLGMTLQPQPYLI 496
Cdd:cd11027  399 KFRFSPPEgEPPPELEGIPGLVLYPLPYKV 428
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
74-496 8.13e-134

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: 393.50  E-value: 8.13e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSrYGQGWVEHRRLAVNSFRYFGYgQKS 153
Cdd:cd20617    1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKGILFS-NGDYWKELRRFALSSLTKTKL-KKK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 154 FESKILEETKFFTDAIETY--KGRPFDFKQLITSAVSNITNLIIFGERF-TYEDTDFQHMIELFSENVELAASASVFLYn 230
Cdd:cd20617   79 MEELIEEEVNKLIESLKKHskSGEPFDPRPYFKKFVLNIINQFLFGKRFpDEDDGEFLKLVKPIEEIFKELGSGNPSDF- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 231 aFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDqgKNDPSSTFSKENLIFSVGELIIA 310
Cdd:cd20617  158 -IPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLL--KEGDSGLFDDDSIISTCLDLFLA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 311 GTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVR 390
Cdd:cd20617  235 GTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTEIG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 391 GYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYfAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFH 470
Cdd:cd20617  315 GYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGN-KLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFK 393
                        410       420
                 ....*....|....*....|....*.
gi 302565346 471 LHFPHELVPDLKPRLGMTLQPQPYLI 496
Cdd:cd20617  394 FKSSDGLPIDEKEVFGLTLKPKPFKV 419
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
73-471 8.94e-130

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: 383.54  E-value: 8.94e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd20665    1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKGLGIVFSN-GERWKETRRFSLMTLRNFGMGKR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd20665   80 SIEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVCNNF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 P-WIGILPfGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELIIAG 311
Cdd:cd20665  160 PaLLDYLP-GSHNKLLKNVAYIKSYILEKVKEHQESLDVNNPRDFIDCFLIKMEQEKHNQQSEFTLENLAVTVTDLFGAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 312 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 391
Cdd:cd20665  239 TETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRN 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 392 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHL 471
Cdd:cd20665  319 YLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNL 398
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
57-497 2.43e-127

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: 378.55  E-value: 2.43e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346   57 ASAELPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLF---MKMTKMGGLLNSRYGQgW 133
Cdd:pfam00067  17 GRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFatsRGPFLGKGIVFANGPR-W 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  134 VEHRRLAVNSFRYFGygQKSFESKILEETKFFTDAIETYKGRP--FDFKQLITSAVSNITNLIIFGERF-TYEDTDFQHM 210
Cdd:pfam00067  96 RQLRRFLTPTFTSFG--KLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILFGERFgSLEDPKFLEL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  211 IELFSENVELAASASVFLYNAFPWIGILPfGKHQQLFRNASVVY-DFLSRLIE--KASVNRKPQLPQHFVDAYFDEMDqg 287
Cdd:pfam00067 174 VKAVQELSSLLSSPSPQLLDLFPILKYFP-GPHGRKLKRARKKIkDLLDKLIEerRETLDSAKKSPRDFLDALLLAKE-- 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  288 kNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHE 367
Cdd:pfam00067 251 -EEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKE 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  368 VLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRH 447
Cdd:pfam00067 330 TLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRN 409
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 302565346  448 CLGEQLARMEMFLFFTALLQRFHLHFPHEL-VPDLKPRLGMTLQPQPYLIC 497
Cdd:pfam00067 410 CLGERLARMEMKLFLATLLQNFEVELPPGTdPPDIDETPGLLLPPKPYKLK 460
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
73-494 4.25e-125

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: 371.79  E-value: 4.25e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSN-GERWKILRRFALQTLRNFGMGKR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd20669   80 SIEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 PWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELIIAGT 312
Cdd:cd20669  160 PSVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 313 ETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGY 392
Cdd:cd20669  240 ETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGF 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 393 SIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLH 472
Cdd:cd20669  320 LIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQ 399
                        410       420
                 ....*....|....*....|....*.
gi 302565346 473 ---FPHELvpDLKPRL-GMTLQPQPY 494
Cdd:cd20669  400 plgAPEDI--DLTPLSsGLGNVPRPF 423
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
74-494 9.14e-124

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: 368.08  E-value: 9.14e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKEclVHQSGIFADRPCLPlFMKMTKMG---GLLNSRyGQGWVEHRRLAVNSFRYFGYG 150
Cdd:cd20651    1 GDVVGLKLGKDKVVVVSGYEAVRE--VLSREEFDGRPDGF-FFRLRTFGkrlGITFTD-GPFWKEQRRFVLRHLRDFGFG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 151 QKSFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLyN 230
Cdd:cd20651   77 RRSMEEVIQEEAEELIDLLKKGEKGPIQMPDLFNVSVLNVLWAMVAGERYSLEDQKLRKLLELVHLLFRNFDMSGGLL-N 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 231 AFPWIG-ILP-FGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQgKNDPSSTFSKENLIFSVGELI 308
Cdd:cd20651  156 QFPWLRfIAPeFSGYNLLVELNQKLIEFLKEEIKEHKKTYDEDNPRDLIDAYLREMKK-KEPPSSSFTDDQLVMICLDLF 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 309 IAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAV 388
Cdd:cd20651  235 IAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALKDTT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 389 VRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQR 468
Cdd:cd20651  315 LGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQN 394
                        410       420
                 ....*....|....*....|....*..
gi 302565346 469 FHLHFPHELVPDLKPRL-GMTLQPQPY 494
Cdd:cd20651  395 FTFSPPNGSLPDLEGIPgGITLSPKPF 421
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
73-495 9.64e-119

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: 355.26  E-value: 9.64e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd20671    1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSS-GERWRTTRRFTVRSMKSLGMGKR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKqLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd20671   80 TIEDKILEELQFLNGQIDSFNGKPFPLR-LLGWAPTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLFNLY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 PWIGILpFGKHQQLFRNASVVYDFLSRLIEKasvnRKPQLPQHFVDAYFDEM--DQGKNDPSST-FSKENLIFSVGELII 309
Cdd:cd20671  159 PVLGAF-LKLHKPILDKVEEVCMILRTLIEA----RRPTIDGNPLHSYIEALiqKQEEDDPKETlFHDANVLACTLDLVM 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 310 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPlGIFHATSEDAVV 389
Cdd:cd20671  234 AGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLP-HVPRCTAADTQF 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 390 RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRF 469
Cdd:cd20671  313 KGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKF 392
                        410       420
                 ....*....|....*....|....*....
gi 302565346 470 HLHFPHELVP---DLKPRLGMTLQPQPYL 495
Cdd:cd20671  393 TFLPPPGVSPadlDATPAAAFTMRPQPQL 421
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
73-496 1.22e-111

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: 337.20  E-value: 1.22e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd20667    1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLFGEKGIICTN-GLTWKQQRRFCMTTLRELGLGKQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd20667   80 ALESQIQHEAAELVKVFAQENGRPFDPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINLGLAFASTIWGRLYDAF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 PWIGILPFGKHQQLFRNASVVYDFLSRLIeKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELIIAGT 312
Cdd:cd20667  160 PWLMRYLPGPHQKIFAYHDAVRSFIKKEV-IRHELRTNEAPQDFIDCYLAQITKTKDDPVSTFSEENMIQVVIDLFLGGT 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 313 ETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGY 392
Cdd:cd20667  239 ETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAVRQCVTSTTMHGY 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 393 SIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLH 472
Cdd:cd20667  319 YVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQ 398
                        410       420
                 ....*....|....*....|....*.
gi 302565346 473 FPhELVPDLKPR--LGMTLQPQPYLI 496
Cdd:cd20667  399 LP-EGVQELNLEyvFGGTLQPQPYKI 423
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
73-496 3.35e-109

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: 330.97  E-value: 3.35e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd20672    1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPIFQGYGVIFAN-GERWKTLRRFSLATMRDFGMGKR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd20672   80 SVEERIQEEAQCLVEELRKSKGALLDPTFLFQSITANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISSFSSQVFELF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 PwiGILPF--GKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELIIA 310
Cdd:cd20672  160 S--GFLKYfpGAHRQIYKNLQEILDYIGHSVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHQNLMISVLSLFFA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 311 GTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVR 390
Cdd:cd20672  238 GTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTLFR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 391 GYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFH 470
Cdd:cd20672  318 GYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFS 397
                        410       420       430
                 ....*....|....*....|....*....|
gi 302565346 471 LHFPheLVP---DLKPR-LGMTLQPQPYLI 496
Cdd:cd20672  398 VASP--VAPediDLTPKeSGVGKIPPTYQI 425
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
73-485 8.18e-109

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: 329.96  E-value: 8.18e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd20670    1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIERNFQGHGVALAN-GERWRILRRFSLTILRNFGMGKR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd20670   80 SIEERIQEEAGYLLEEFRKTKGAPIDPTFFLSRTVSNVISSVVFGSRFDYEDKQFLSLLRMINESFIEMSTPWAQLYDMY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 PwiGILPF--GKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELIIA 310
Cdd:cd20670  160 S--GIMQYlpGRHNRIYYLIEELKDFIASRVKINEASLDPQNPRDFIDCFLIKMHQDKNNPHTEFNLKNLVLTTLNLFFA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 311 GTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVR 390
Cdd:cd20670  238 GTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFR 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 391 GYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFH 470
Cdd:cd20670  318 GYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFS 397
                        410
                 ....*....|....*....
gi 302565346 471 lhfPHELVP----DLKPRL 485
Cdd:cd20670  398 ---LRSLVPpadiDITPKI 413
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
73-494 3.08e-107

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: 325.98  E-value: 3.08e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd20668    1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSN-GERAKQLRRFSIATLRDFGVGKR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYNAF 232
Cdd:cd20668   80 GIEERIQEEAGFLIDALRGTGGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 233 PWI-GILPfGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELIIAG 311
Cdd:cd20668  160 SSVmKHLP-GPQQQAFKELQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEKKNPNTEFYMKNLVMTTLNLFFAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 312 TETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRG 391
Cdd:cd20668  239 TETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRVTKDTKFRD 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 392 YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHL 471
Cdd:cd20668  319 FFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRF 398
                        410       420
                 ....*....|....*....|....*
gi 302565346 472 HFPHELVP-DLKPR-LGMTLQPQPY 494
Cdd:cd20668  399 KSPQSPEDiDVSPKhVGFATIPRNY 423
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
73-494 9.06e-107

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: 325.02  E-value: 9.06e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRYGQGWVEHRRLAVNSFRYFGYGQK 152
Cdd:cd11028    1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFISNGKSMAFSDYGPRWKLHRKLAQNALRTFSNART 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 S--FESKILEETKFftdAIETY-----KGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASAS 225
Cdd:cd11028   81 HnpLEEHVTEEAEE---LVTELtenngKPGPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFLELVKSNDDFGAFVGAGN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 226 vfLYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYF---DEMDQGKNdPSSTFSKENLIF 302
Cdd:cd11028  158 --PVDVMPWLRYLTRRKLQKFKELLNRLNSFILKKVKEHLDTYDKGHIRDITDALIkasEEKPEEEK-PEVGLTDEHIIS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 303 SVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHA 382
Cdd:cd11028  235 TVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPFTIPHA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 383 TSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYF--AKKEALVPFSLGRRHCLGEQLARMEMFL 460
Cdd:cd11028  315 TTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLdkTKVDKFLPFGAGRRRCLGEELARMELFL 394
                        410       420       430
                 ....*....|....*....|....*....|....
gi 302565346 461 FFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPY 494
Cdd:cd11028  395 FFATLLQQCEFSVKPGEKLDLTPIYGLTMKPKPF 428
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
74-496 1.50e-96

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: 298.55  E-value: 1.50e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKECLVHQsgIFADRPclPLFMKMTKMGG-LLNSRYGQGWVEHRRLAVNSFR-----YF 147
Cdd:cd20652    1 GSIFSLKMGSVYTVVLSDPKLIRDTFRRD--EFTGRA--PLYLTHGIMGGnGIICAEGDLWRDQRRFVHDWLRqfgmtKF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 148 GYGQKSFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVF 227
Cdd:cd20652   77 GNGRAKMEKRIATGVHELIKHLKAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFLQEEGTKLIGVAGPV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 228 lyNAFPWIGILPFGKHQQ--LFRNASVVYDFLSRLIEKASVNRKPQLP-------QHFVDAYFDEMDQGKNDpSSTFSKE 298
Cdd:cd20652  157 --NFLPFLRHLPSYKKAIefLVQGQAKTHAIYQKIIDEHKRRLKPENPrdaedfeLCELEKAKKEGEDRDLF-DGFYTDE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 299 NLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLG 378
Cdd:cd20652  234 QLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPLG 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 379 IFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEM 458
Cdd:cd20652  314 IPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMIL 393
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 302565346 459 FLFFTALLQRFHLHFPHEL-VPDLKPRLGMTLQPQPYLI 496
Cdd:cd20652  394 FLFTARILRKFRIALPDGQpVDSEGGNVGITLTPPPFKI 432
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
73-494 2.02e-96

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: 298.47  E-value: 2.02e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPclplfmKMTKMGGLLNSR-------YGQGWVEHRRLAVNSFR 145
Cdd:cd20673    1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRP------RMVTTDLLSRNGkdiafadYSATWQLHRKLVHSAFA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 146 YFGYGQKSFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIElFSEN-VELAASA 224
Cdd:cd20673   75 LFGEGSQKLEKIICQEASSLCDTLATHNGESIDLSPPLFRAVTNVICLLCFNSSYKNGDPELETILN-YNEGiVDTVAKD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 225 SvfLYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYF------DEMDQGKNDPSSTFSKE 298
Cdd:cd20673  154 S--LVDIFPWLQIFPNKDLEKLKQCVKIRDKLLQKKLEEHKEKFSSDSIRDLLDALLqakmnaENNNAGPDQDSVGLSDD 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 299 NLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLG 378
Cdd:cd20673  232 HILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPVAPLL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 379 IFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEAL--VPFSLGRRHCLGEQLARM 456
Cdd:cd20673  312 IPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQLISPSLsyLPFGAGPRVCLGEALARQ 391
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 302565346 457 EMFLFFTALLQRFHLHFPHEL-VPDLKPRLGMTLQPQPY 494
Cdd:cd20673  392 ELFLFMAWLLQRFDLEVPDGGqLPSLEGKFGVVLQIDPF 430
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
73-496 8.10e-90

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: 281.21  E-value: 8.10e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRP---CLPLFMKMTKMGglLNSRYGQGWVEHRRLAVNSFRYFGY 149
Cdd:cd20677    1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPdfyTFSLIANGKSMT--FSEKYGESWKLHKKIAKNALRTFSK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 150 --GQKSFESKILEE--TKFFTDAIETYKGRP-----FDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELfseNVEL 220
Cdd:cd20677   79 eeAKSSTCSCLLEEhvCAEASELVKTLVELSkekgsFDPVSLITCAVANVVCALCFGKRYDHSDKEFLTIVEI---NNDL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 221 -AASASVFLYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKN-DPSSTFSKE 298
Cdd:cd20677  156 lKASGAGNLADFIPILRYLPSPSLKALRKFISRLNNFIAKSVQDHYATYDKNHIRDITDALIALCQERKAeDKSAVLSDE 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 299 NLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLG 378
Cdd:cd20677  236 QIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSFVPFT 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 379 IFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKK--EALVPFSLGRRHCLGEQLARM 456
Cdd:cd20677  316 IPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSlvEKVLIFGMGVRKCLGEDVARN 395
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 302565346 457 EMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLI 496
Cdd:cd20677  396 EIFVFLTTILQQLKLEKPPGQKLDLTPVYGLTMKPKPYRL 435
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
73-494 6.06e-88

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: 276.00  E-value: 6.06e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLF-MKMTKMGGLLNSRYGQGWVEHRRLAVNSFRyfGYGQ 151
Cdd:cd11065    1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAgELMGWGMRLLLMPYGPRWRLHRRLFHQLLN--PSAV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 152 KSFESKILEETK-FFTDAIETykgrPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAASASVFLYN 230
Cdd:cd11065   79 RKYRPLQELESKqLLRDLLES----PDDFLDHIRRYAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGSPGAYLVD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 231 AFPWIGILP--FG-----KHQQLFRNASVVYDFLSRLIEKASVNRKPqlPQHFVDAYFDEMDQGkndpsSTFSKENLIFS 303
Cdd:cd11065  155 FFPFLRYLPswLGapwkrKARELRELTRRLYEGPFEAAKERMASGTA--TPSFVKDLLEELDKE-----GGLSEEEIKYL 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 304 VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHAT 383
Cdd:cd11065  228 AGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIPHAL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 384 SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSG--YFAKKEALVPFSLGRRHCLGEQLARMEMFLF 461
Cdd:cd11065  308 TEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKgtPDPPDPPHFAFGFGRRICPGRHLAENSLFIA 387
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 302565346 462 FTALLQRFHLHFP-----HELVPDLKPRLGMTLQPQPY 494
Cdd:cd11065  388 IARLLWAFDIKKPkdeggKEIPDEPEFTDGLVSHPLPF 425
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
73-496 4.34e-83

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: 263.79  E-value: 4.34e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRYGQGWVEHRRLAVNSFRYFGYG-- 150
Cdd:cd20675    1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDFASFRVVSGGRSLAFGGYSERWKAHRRVAHSTVRAFSTRnp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 151 --QKSFESKILEETKfftDAIE-----TYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMI---ELFSENVEl 220
Cdd:cd20675   81 rtRKAFERHVLGEAR---ELVAlflrkSAGGAYFDPAPPLVVAVANVMSAVCFGKRYSHDDAEFRSLLgrnDQFGRTVG- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 221 AASasvfLYNAFPWIGILP------FGKHQQLFRNasvVYDFLSrliEKASVNR---KPQLPQHFVDAYFDEMDQGKNDP 291
Cdd:cd20675  157 AGS----LVDVMPWLQYFPnpvrtvFRNFKQLNRE---FYNFVL---DKVLQHRetlRGGAPRDMMDAFILALEKGKSGD 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 292 S-STFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLR 370
Cdd:cd20675  227 SgVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMR 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 371 FCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEA--LVPFSLGRRHC 448
Cdd:cd20675  307 FSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFLNKDLAssVMIFSVGKRRC 386
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 302565346 449 LGEQLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLI 496
Cdd:cd20675  387 IGEELSKMQLFLFTSILAHQCNFTANPNEPLTMDFSYGLTLKPKPFTI 434
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
73-497 3.54e-81

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: 258.50  E-value: 3.54e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFmKMTKMGG--LLNSRYGQGWVEHRRLA----VNSFRy 146
Cdd:cd20674    1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTG-KLVSQGGqdLSLGDYSLLWKAHRKLTrsalQLGIR- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 147 fgygqKSFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTyEDTDFQHMIELFSENVELAASASV 226
Cdd:cd20674   79 -----NSLEPVVEQLTQELCERMRAQAGTPVDIQEEFSLLTCSIICCLTFGDKED-KDTLVQAFHDCVQELLKTWGHWSI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 227 FLYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKND-PSSTFSKENLIFSVG 305
Cdd:cd20674  153 QALDSIPFLRFFPNPGLRRLKQAVENRDHIVESQLRQHKESLVAGQWRDMTDYMLQGLGQPRGEkGMGQLLEGHVHMAVV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 306 ELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSE 385
Cdd:cd20674  233 DLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTR 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 386 DAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyfAKKEALVPFSLGRRHCLGEQLARMEMFLFFTAL 465
Cdd:cd20674  313 DSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPG---AANRALLPFGCGARVCLGEPLARLELFVFLARL 389
                        410       420       430
                 ....*....|....*....|....*....|...
gi 302565346 466 LQRFHLHFPH-ELVPDLKPRLGMTLQPQPYLIC 497
Cdd:cd20674  390 LQAFTLLPPSdGALPSLQPVAGINLKVQPFQVR 422
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
73-491 5.70e-72

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: 234.91  E-value: 5.70e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGL-LNSRYGQGWVEHRRLAVNSFRYFGY-- 149
Cdd:cd20676    1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRPDLYSFRFISDGQSLtFSTDSGPVWRARRKLAQNALKTFSIas 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 150 GQKSFESKILEE---------TKFFTDAIETyKGRpFD-FKQLITSaVSNITNLIIFGERFTYEDTDFQHMIELFSENVE 219
Cdd:cd20676   81 SPTSSSSCLLEEhvskeaeylVSKLQELMAE-KGS-FDpYRYIVVS-VANVICAMCFGKRYSHDDQELLSLVNLSDEFGE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 220 LAASASvfLYNAFPWIGILPfGKHQQLFRNASV-VYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSST--FS 296
Cdd:cd20676  158 VAGSGN--PADFIPILRYLP-NPAMKRFKDINKrFNSFLQKIVKEHYQTFDKDNIRDITDSLIEHCQDKKLDENANiqLS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 297 KENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVP 376
Cdd:cd20676  235 DEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVP 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 377 LGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKK---EALVPFSLGRRHCLGEQL 453
Cdd:cd20676  315 FTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEINKtesEKVMLFGLGKRRCIGESI 394
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 302565346 454 ARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQP 491
Cdd:cd20676  395 ARWEVFLFLAILLQQLEFSVPPGVKVDMTPEYGLTMKH 432
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
74-491 2.15e-64

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: 213.92  E-value: 2.15e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRyfGYGQKS 153
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLD-GPEHRRLRRLLAPAFT--PRALAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 154 FESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFsenvelaasasvFLYNAFP 233
Cdd:cd00302   78 LRPVIREIARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLEAL------------LKLLGPR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 234 WIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQhfvdayfdeMDQGKNDPSSTFSKENLIFSVGELIIAGTE 313
Cdd:cd00302  146 LLRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDL---------LLLADADDGGGLSDEEIVAELLTLLLAGHE 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 314 TTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpngKPSWDDKFKMPYTEAVLHEVLRFCNIVPlGIFHATSEDAVVRGYS 393
Cdd:cd00302  217 TTASLLAWALYLLARHPEVQERLRAEIDAVLG---DGTPEDLSKLPYLEAVVEETLRLYPPVP-LLPRVATEDVELGGYT 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 394 IPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGyfAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHF 473
Cdd:cd00302  293 IPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPERE--EPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFEL 370
                        410
                 ....*....|....*...
gi 302565346 474 PHELVPDLKPRLGmTLQP 491
Cdd:cd00302  371 VPDEELEWRPSLG-TLGP 387
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
74-491 2.07e-60

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: 204.33  E-value: 2.07e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMG-GLLNSRYGQGWVEHRRLA---------VNS 143
Cdd:cd20618    1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGqDIVFAPYGPHWRHLRKICtlelfsakrLES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 144 FRYFgygqKSFE-----SKILEETKfftdaietyKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDF----QHMIELF 214
Cdd:cd20618   81 FQGV----RKEElshlvKSLLEESE---------SGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKEseeaREFKELI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 215 SENVELAASASVFLYnaFPWIGILPFGKHQQLFRNASVVYD-FLSRLIEKASVNRKPQLPQHFVDAYFDEMDQgkNDPSS 293
Cdd:cd20618  148 DEAFELAGAFNIGDY--IPWLRWLDLQGYEKRMKKLHAKLDrFLQKIIEEHREKRGESKKGGDDDDDLLLLLD--LDGEG 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 294 TFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCN 373
Cdd:cd20618  224 KLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHP 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 374 IVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEA--LVPFSLGRRHCLGE 451
Cdd:cd20618  304 PGPLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVKGQDfeLLPFGSGRRMCPGM 383
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 302565346 452 QLArMEMFLFFTA-LLQRFHLHFPHEL--VPDLKPRLGMTLQP 491
Cdd:cd20618  384 PLG-LRMVQLTLAnLLHGFDWSLPGPKpeDIDMEEKFGLTVPR 425
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
73-454 1.28e-52

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: 183.82  E-value: 1.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTkmGGLLN---SRYGQGWVEHRRLA--------- 140
Cdd:cd11072    2 YGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILS--YGGKDiafAPYGEYWRQMRKICvlellsakr 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 141 VNSFRYFgygqksFEskilEETKFFTDAIETY--KGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFqhMIELFSENV 218
Cdd:cd11072   80 VQSFRSI------RE----EEVSLLVKKIRESasSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQDK--FKELVKEAL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 219 ELAASASVFLYnaFPWIGILPF--GKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFS 296
Cdd:cd11072  148 ELLGGFSVGDY--FPSLGWIDLltGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEFPLT 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 297 KENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVP 376
Cdd:cd11072  226 RDNIKAIILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAP 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 377 LGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFakK----EaLVPFSLGRRHCLGEQ 452
Cdd:cd11072  306 LLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIDF--KgqdfE-LIPFGAGRRICPGIT 382

                 ..
gi 302565346 453 LA 454
Cdd:cd11072  383 FG 384
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
74-493 6.56e-52

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


Pssm-ID: 410713 [Multi-domain]  Cd Length: 406  Bit Score: 181.24  E-value: 6.56e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPlFMKMTKMGGLLNSRyGQGWVEHRRLAVNSFRyfgyGQK- 152
Cdd:cd20620    1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVKGGVYE-RLKLLLGNGLLTSE-GDLWRRQRRLAQPAFH----RRRi 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 -SFESKILEETKFFTDAIETYKGR-PFDfkqlITSAVSNITNLII----FGERFtyeDTDFQHMIELFSENVELAASAsv 226
Cdd:cd20620   75 aAYADAMVEATAALLDRWEAGARRgPVD----VHAEMMRLTLRIVaktlFGTDV---EGEADEIGDALDVALEYAARR-- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 227 fLYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEK--ASVNRKPQLPQHFVDAYFDEMDQGkndpsstFSKENLIFSV 304
Cdd:cd20620  146 -MLSPFLLPLWLPTPANRRFRRARRRLDEVIYRLIAErrAAPADGGDLLSMLLAARDEETGEP-------MSDQQLRDEV 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 305 GELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATs 384
Cdd:cd20620  218 MTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLRLYPPAWIIGREAV- 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 385 EDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTA 464
Cdd:cd20620  296 EDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLAT 375
                        410       420       430
                 ....*....|....*....|....*....|.
gi 302565346 465 LLQRFHLhfphELVP--DLKPRLGMTLQPQP 493
Cdd:cd20620  376 IAQRFRL----RLVPgqPVEPEPLITLRPKN 402
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
73-491 1.21e-50

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: 178.49  E-value: 1.21e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQsGIFADRPCLPLFMKMTKM----GGLLNSrYGQGWVEHRRLAVNSF---- 144
Cdd:cd11054    4 YGPIVREKLGGRDIVHLFDPDDIEKVFRNE-GKYPIRPSLEPLEKYRKKrgkpLGLLNS-NGEEWHRLRSAVQKPLlrpk 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 145 ---RYFGygqksFESKILEEtkfFTDAIETYK----GRPFDFKQLITS-AVSNITnLIIFGERFTYEDTDFQHMIELFSE 216
Cdd:cd11054   82 svaSYLP-----AINEVADD---FVERIRRLRdedgEEVPDLEDELYKwSLESIG-TVLFGKRLGCLDDNPDSDAQKLIE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 217 NVELAASASVFLYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKAsvnrkpqlpqhfVDAYFDEMDQGKNDPS---- 292
Cdd:cd11054  153 AVKDIFESSAKLMFGPPLWKYFPTPAWKKFVKAWDTIFDIASKYVDEA------------LEELKKKDEEDEEEDSlley 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 293 ----STFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEV 368
Cdd:cd11054  221 llskPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKES 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 369 LRfcnIVPLGIFHA--TSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKE--ALVPFSLG 444
Cdd:cd11054  301 LR---LYPVAPGNGriLPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENKNIHpfASLPFGFG 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 302565346 445 RRHCLGEQLARMEMFLFFTALLQRFHLHFPHElvpDLKPRLGMTLQP 491
Cdd:cd11054  378 PRMCIGRRFAELEMYLLLAKLLQNFKVEYHHE---ELKVKTRLILVP 421
PTZ00404 PTZ00404
cytochrome P450; Provisional
51-501 3.39e-50

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 178.76  E-value: 3.39e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  51 NIYSLAasaELPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSrYG 130
Cdd:PTZ00404  42 NLHQLG---NLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGIVTS-SG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 131 QGWVEHRRLAVNSFRyfgygqKSFESKILEE-TKFFTDAIETYK-----GRPFDFKQLITSAVSNITNLIIFGERFTYED 204
Cdd:PTZ00404 118 EYWKRNREIVGKAMR------KTNLKHIYDLlDDQVDVLIESMKkiessGETFEPRYYLTKFTMSAMFKYIFNEDISFDE 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 205 T----DFQHMIELFSENVELAASASvflynAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRK---PQLPQHFV 277
Cdd:PTZ00404 192 DihngKLAELMGPMEQVFKDLGSGS-----LFDVIEITQPLYYQYLEHTDKNFKKIKKFIKEKYHEHLKtidPEVPRDLL 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 278 DAYFDEMDQGKNDpsstfSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFK 357
Cdd:PTZ00404 267 DLLIKEYGTNTDD-----DILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQS 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 358 MPYTEAVLHEVLRFCNIVPLGIFHATSEDAVV-RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyfaKKE 436
Cdd:PTZ00404 342 TPYTVAIIKETLRYKPVSPFGLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPD----SND 417
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302565346 437 ALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLICAERR 501
Cdd:PTZ00404 418 AFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGKKIDETEEYGLTLKPNKFKVLLEKR 482
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
70-490 1.79e-48

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: 172.72  E-value: 1.79e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  70 SQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPcLPLFMKMTKMGG--LLNSRYGQGWVEHRRLAVNSFryf 147
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRD-VPDAVRALGHHKssIVWPPYGPRWRMLRKICTTEL--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 148 gygqksFESKILEETK-------------FFTDAIEtykGRPFDFKQLITSAVSNITNLIIFGER-FTYEDTDFQHMIEL 213
Cdd:cd11073   77 ------FSPKRLDATQplrrrkvrelvryVREKAGS---GEAVDIGRAAFLTSLNLISNTLFSVDlVDPDSESGSEFKEL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 214 FSENVELAASASVFLYnaFPWIGIL-PFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPS 292
Cdd:cd11073  148 VREIMELAGKPNVADF--FPFLKFLdLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLLLLDLELDSES 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 293 StFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFC 372
Cdd:cd11073  226 E-LTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLH 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 373 NIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSG-YFAKKEALVPFSLGRRHCLGE 451
Cdd:cd11073  305 PPAPLLLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIdFKGRDFELIPFGSGRRICPGL 384
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 302565346 452 QLA-RMeMFLFFTALLQRFHLHFPHELVP---DLKPRLGMTLQ 490
Cdd:cd11073  385 PLAeRM-VHLVLASLLHSFDWKLPDGMKPedlDMEEKFGLTLQ 426
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
73-491 1.60e-47

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: 170.07  E-value: 1.60e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPclPLFMKMTKMGGLLNSRYGQGWVEHRRLAVNSFRyfGYGQK 152
Cdd:cd11055    2 YGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRP--LFILLDEPFDSSLLFLKGERWKRLRTTLSPTFS--SGKLK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETY--KGRPFDFK---QLITSAVSNITnliIFG----ERFTYEDTDFQHMIELFSENVELAAS 223
Cdd:cd11055   78 LMVPIINDCCDELVEKLEKAaeTGKPVDMKdlfQGFTLDVILST---AFGidvdSQNNPDDPFLKAAKKIFRNSIIRLFL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 224 ASVFLYNAFPWIGILPFGKHQQLFrnaSVVYDFLSRLIE---KASVNRKPQLPQHFVDAyfdeMDQGKNDPSSTFSKEN- 299
Cdd:cd11055  155 LLLLFPLRLFLFLLFPFVFGFKSF---SFLEDVVKKIIEqrrKNKSSRRKDLLQLMLDA----QDSDEDVSKKKLTDDEi 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 300 ----LIFsvgelIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCniv 375
Cdd:cd11055  228 vaqsFIF-----LLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLY--- 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 376 PLGIFH--ATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQL 453
Cdd:cd11055  300 PPAFFIsrECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMRF 379
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 302565346 454 ARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQP 491
Cdd:cd11055  380 ALLEVKLALVKILQKFRFVPCKETEIPLKLVGGATLSP 417
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
73-470 9.48e-47

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: 168.19  E-value: 9.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLP----LFMKMTKMggLLNSRYGQGWVEHRR------LAVN 142
Cdd:cd11075    2 YGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANplrvLFSSNKHM--VNSSPYGPLWRTLRRnlvsevLSPS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 143 SFRYFGYGQKSFESKILEetKFFTDAIEtyKGRPFDFKQLITSAVSNITNLIIFGERFTyEDT--DFQHMIELFsenveL 220
Cdd:cd11075   80 RLKQFRPARRRALDNLVE--RLREEAKE--NPGPVNVRDHFRHALFSLLLYMCFGERLD-EETvrELERVQREL-----L 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 221 AASASVFLYNAFPWIGILPF----GKHQQLFRNASVVYDFL--SRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNdpsST 294
Cdd:cd11075  150 LSFTDFDVRDFFPALTWLLNrrrwKKVLELRRRQEEVLLPLirARRKRRASGEADKDYTDFLLLDLLDLKEEGGE---RK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 295 FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNI 374
Cdd:cd11075  227 LTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPP 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 375 VPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGY-----FAKKEALVPFSLGRRHCL 449
Cdd:cd11075  307 GHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAadidtGSKEIKMMPFGAGRRICP 386
                        410       420
                 ....*....|....*....|.
gi 302565346 450 GEQLARMEMFLFFTALLQRFH 470
Cdd:cd11075  387 GLGLATLHLELFVARLVQEFE 407
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
62-490 7.61e-46

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: 164.68  E-value: 7.61e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  62 PHVYMRKQSQvYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLNSRYGQGWVEHRRLAV 141
Cdd:COG2124   21 PYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLVQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 142 NSFRyfgyGQ--KSFESKILEETKFFTDAIETykGRPFDFkqliTSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVE 219
Cdd:COG2124  100 PAFT----PRrvAALRPRIREIADELLDRLAA--RGPVDL----VEEFARPLPVIVICELLGVPEEDRDRLRRWSDALLD 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 220 LAASasvflynafpwigiLPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEmdqgkndpsSTFSKEN 299
Cdd:COG2124  170 ALGP--------------LPPERRRRARRARAELDAYLRELIAERRAEPGDDLLSALLAARDDG---------ERLSDEE 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 300 LIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIdlimgpngkpswddkfkmPYTEAVLHEVLRFCNIVPLGI 379
Cdd:COG2124  227 LRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLP 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 380 FHATsEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaKKEALVPFSLGRRHCLGEQLARMEMF 459
Cdd:COG2124  289 RTAT-EDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCLGAALARLEAR 358
                        410       420       430
                 ....*....|....*....|....*....|...
gi 302565346 460 LFFTALLQRFHlHFphELVPD--LKPRLGMTLQ 490
Cdd:COG2124  359 IALATLLRRFP-DL--RLAPPeeLRWRPSLTLR 388
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
74-489 8.01e-45

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: 163.17  E-value: 8.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKM---TKMGGLlnSRYGQGWVEHRRLAVnsfryfgyg 150
Cdd:cd20654    1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMgynYAMFGF--APYGPYWRELRKIAT--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 151 QKSFESKILEETK---------FFTDAIETYKGR-------PFDFKQLITSAVSNITNLIIFGERF-----TYEDTDFQH 209
Cdd:cd20654   70 LELLSNRRLEKLKhvrvsevdtSIKELYSLWSNNkkggggvLVEMKQWFADLTFNVILRMVVGKRYfggtaVEDDEEAER 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 210 MIELFSENVELAAsasVF-LYNAFPWIGILPFGKH-QQLFRNASVVYDFLSRLIE----KASVNRKPQLPQHFVDAYFDE 283
Cdd:cd20654  150 YKKAIREFMRLAG---TFvVSDAIPFLGWLDFGGHeKAMKRTAKELDSILEEWLEehrqKRSSSGKSKNDEDDDDVMMLS 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 284 MDQGKndPSSTFSKENLIFS-VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpngKPSW---DDKFKMP 359
Cdd:cd20654  227 ILEDS--QISGYDADTVIKAtCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVG---KDRWveeSDIKNLV 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 360 YTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSsgyfaKKEA-- 437
Cdd:cd20654  302 YLQAIVKETLRLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTT-----HKDIdv 376
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 302565346 438 ------LVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTL 489
Cdd:cd20654  377 rgqnfeLIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIKTPSNEPVDMTEGPGLTN 434
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
123-493 1.30e-42

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: 156.53  E-value: 1.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 123 GLLNSRyGQGWVEHRRLAVNSF--RYFgygqKSFESKILEETKFFTDAIETY-KGRPFDFKQLITSAVSNI-------TN 192
Cdd:cd20628   48 GLLTST-GEKWRKRRKLLTPAFhfKIL----ESFVEVFNENSKILVEKLKKKaGGGEFDIFPYISLCTLDIicetamgVK 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 193 LIIFGErftyEDTDFQHMIELFSENVeLAASASVFLYnaFPWIGILpFGKHQQLFRNASVVYDFLSRLIEKasvnRKPQL 272
Cdd:cd20628  123 LNAQSN----EDSEYVKAVKRILEII-LKRIFSPWLR--FDFIFRL-TSLGKEQRKALKVLHDFTNKVIKE----RREEL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 273 PQHFVDAYFDEMDQGK------------NDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEI 340
Cdd:cd20628  191 KAEKRNSEEDDEFGKKkrkafldllleaHEDGGPLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEEL 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 341 DLIMGPNG-KPSWDDKFKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEV 419
Cdd:cd20628  271 DEIFGDDDrRPTLEDLNKMKYLERVIKETLRLYPSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEK 349
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302565346 420 FHPERFLDSSgyFAKKE--ALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHfPHELVPDLKPRLGMTLQPQP 493
Cdd:cd20628  350 FDPDRFLPEN--SAKRHpyAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVL-PVPPGEDLKLIAEIVLRSKN 422
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
137-471 1.43e-41

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: 153.95  E-value: 1.43e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 137 RRLAVNSFryfgYGQKS---FESKILEETKFFTDAIETYK--GRPFDFKQLITSAVSNITNLIIFGERFTY-EDTDFQ-H 209
Cdd:cd11062   58 RRKALSPF----FSKRSilrLEPLIQEKVDKLVSRLREAKgtGEPVNLDDAFRALTADVITEYAFGRSYGYlDEPDFGpE 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 210 MIELFSENVELAASASvflynAFPWIG----ILPFGKHQQLFRNASVVYDFL---SRLIEKASVNRKPQLPQHFVDAYFD 282
Cdd:cd11062  134 FLDALRALAEMIHLLR-----HFPWLLkllrSLPESLLKRLNPGLAVFLDFQesiAKQVDEVLRQVSAGDPPSIVTSLFH 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 283 EMDqGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIM-GPNGKPSWDDKFKMPYT 361
Cdd:cd11062  209 ALL-NSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMpDPDSPPSLAELEKLPYL 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 362 EAVLHEVLRFCNIVPlgifH-----ATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKE 436
Cdd:cd11062  288 TAVIKEGLRLSYGVP----TrlprvVPDEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEKGKLDR 363
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 302565346 437 ALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHL 471
Cdd:cd11062  364 YLVPFSKGSRSCLGINLAYAELYLALAALFRRFDL 398
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
152-476 1.51e-40

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: 150.84  E-value: 1.51e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 152 KSFESKILEETKFFTDAIETYKGRP----FDFKQLITSAVSNITNLIIFGERF-TYEDTDFQHMIELFSENVELAAsasV 226
Cdd:cd11061   71 RGYEPRILSHVEQLCEQLDDRAGKPvswpVDMSDWFNYLSFDVMGDLAFGKSFgMLESGKDRYILDLLEKSMVRLG---V 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 227 FLYnaFPWIgiLPFGKHQQLFRNASV----VYDFLSRLIEKASVNRKPQLP---QHFVDAYfdemdqgKNDPSSTFSKEN 299
Cdd:cd11061  148 LGH--APWL--RPLLLDLPLFPGATKarkrFLDFVRAQLKERLKAEEEKRPdifSYLLEAK-------DPETGEGLDLEE 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 300 LIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFK-MPYTEAVLHEVLRFCNIVPLG 378
Cdd:cd11061  217 LVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLGPKLKsLPYLRACIDEALRLSPPVPSG 296
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 379 IFHAT-SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAK-KEALVPFSLGRRHCLGEQLARM 456
Cdd:cd11061  297 LPRETpPGGLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVRaRSAFIPFSIGPRGCIGKNLAYM 376
                        330       340
                 ....*....|....*....|
gi 302565346 457 EMFLFFTALLQRFHLHFPHE 476
Cdd:cd11061  377 ELRLVLARLLHRYDFRLAPG 396
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
74-497 4.02e-40

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: 149.78  E-value: 4.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFA-DRPCLPLFMKMtKMGGLLnSRYGQGWVEHRRLAVNSFRYFGYgqK 152
Cdd:cd11083    1 GSAYRFRLGRQPVLVISDPELIREVLRRRPDEFRrISSLESVFREM-GINGVF-SAEGDAWRRQRRLVMPAFSPKHL--R 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETY--KGRPFDFKQLITSAVSNITNLIIFGERF-TYEDTDfqHMIelfSENVELaasasVF-- 227
Cdd:cd11083   77 YFFPTLRQITERLRERWERAaaEGEAVDVHKDLMRYTVDVTTSLAFGYDLnTLERGG--DPL---QEHLER-----VFpm 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 228 ----LYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASV--NRKPQLPQHFVDAyfDEMDQGKNDPSSTFSKENLI 301
Cdd:cd11083  147 lnrrVNAPFPYWRYLRLPADRALDRALVEVRALVLDIIAAARArlAANPALAEAPETL--LAMMLAEDDPDARLTDDEIY 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 302 FSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEID-LIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLgIF 380
Cdd:cd11083  225 ANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDaVLGGARVPPLLEALDRLPYLEAVARETLRLKPVAPL-LF 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 381 HATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLD--SSGYFAKKEALVPFSLGRRHCLGEQLARMEM 458
Cdd:cd11083  304 LEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDgaRAAEPHDPSSLLPFGAGPRLCPGRSLALMEM 383
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 302565346 459 FLFFTALLQRFHLHFPhELVPDLKPRLGMTLQPQPYLIC 497
Cdd:cd11083  384 KLVFAMLCRNFDIELP-EPAPAVGEEFAFTMSPEGLRVR 421
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
214-491 4.65e-40

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: 149.59  E-value: 4.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 214 FSENVELAASASVFLYNAfPWIGILPFG-KHQQLFRNA-SVVYDFLSRLIEK--ASVNRKPQLPQ----HFVDAYfdemd 285
Cdd:cd20613  151 FPKAISLVLEGIQESFRN-PLLKYNPSKrKYRREVREAiKFLRETGRECIEErlEALKRGEEVPNdiltHILKAS----- 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 286 qgknDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVL 365
Cdd:cd20613  225 ----EEEPDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVL 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 366 HEVLRFCNIVPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGR 445
Cdd:cd20613  301 KETLRLYPPVP-GTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIPSYAYFPFSLGP 379
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 302565346 446 RHCLGEQLARMEMFLFFTALLQRFHLhfphELVPD--LKPRLGMTLQP 491
Cdd:cd20613  380 RSCIGQQFAQIEAKVILAKLLQNFKF----ELVPGqsFGILEEVTLRP 423
PLN02183 PLN02183
ferulate 5-hydroxylase
60-498 1.10e-39

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 150.39  E-value: 1.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  60 ELPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMT-KMGGLLNSRYGQGWVEHRR 138
Cdd:PLN02183  55 QLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPANIAISYLTyDRADMAFAHYGPFWRQMRK 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 139 LAVNSFryfgYGQKSFES--KILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSE 216
Cdd:PLN02183 135 LCVMKL----FSRKRAESwaSVRDEVDSMVRSVSSNIGKPVNIGELIFTLTRNITYRAAFGSSSNEGQDEFIKILQEFSK 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 217 nvelaasasvfLYNAF------PWIG-ILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFV------------ 277
Cdd:PLN02183 211 -----------LFGAFnvadfiPWLGwIDPQGLNKRLVKARKSLDGFIDDIIDDHIQKRKNQNADNDSeeaetdmvddll 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 278 -----DAYFDEMDQGKNdpSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSW 352
Cdd:PLN02183 280 afyseEAKVNESDDLQN--SIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEE 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 353 DDKFKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSS--G 430
Cdd:PLN02183 358 SDLEKLTYLKCTLKETLRLHPPIPL-LLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGvpD 436
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 302565346 431 YFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVP---DLKPRLGMTLQ--------PQPYLICA 498
Cdd:PLN02183 437 FKGSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWELPDGMKPselDMNDVFGLTAPratrlvavPTYRLQCP 515
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
108-496 1.30e-39

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: 148.52  E-value: 1.30e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 108 DRPCLPLFMKMTKmgGLLNSRYGQgWVEHRRlAVNSfryfgygqkSFESKIL--------EETKFFTDAIETYKGRP-FD 178
Cdd:cd11057   33 NKSFFYDFFRLGR--GLFSAPYPI-WKLQRK-ALNP---------SFNPKILlsflpifnEEAQKLVQRLDTYVGGGeFD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 179 FKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVELAA--SASVFLYNAfpWIGILpFGKHQQLFRNASVVYDF 256
Cdd:cd11057  100 ILPDLSRCTLEMICQTTLGSDVNDESDGNEEYLESYERLFELIAkrVLNPWLHPE--FIYRL-TGDYKEEQKARKILRAF 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 257 LSRLIEKA----------------SVNRKPQLpqhFVDAYFDEMDQGKNdpsstFSKENLIFSVGELIIAGTETTTNVLR 320
Cdd:cd11057  177 SEKIIEKKlqevelesnldseedeENGRKPQI---FIDQLLELARNGEE-----FTDEEIMDEIDTMIFAGNDTSATTVA 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 321 WAILFMALYPNIQGQVQKEIDLIMGPNGKP-SWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTT 399
Cdd:cd11057  249 YTLLLLAMHPEVQEKVYEEIMEVFPDDGQFiTYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSNGVVIPKGTT 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 400 VITNLYSVHFDEKYW-RDPEVFHPERFL--DSSG---YfakkeALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHF 473
Cdd:cd11057  329 IVIDIFNMHRRKDIWgPDADQFDPDNFLpeRSAQrhpY-----AFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKT 403
                        410       420
                 ....*....|....*....|....
gi 302565346 474 PHELvPDLKPRLGMTLQP-QPYLI 496
Cdd:cd11057  404 SLRL-EDLRFKFNITLKLaNGHLV 426
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
73-491 3.45e-39

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: 147.63  E-value: 3.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMG-GLLNSRYGQGWVEHRRLAVNSFryfgYGQ 151
Cdd:cd20656    1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGqDLIWADYGPHYVKVRKLCTLEL----FTP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 152 KSFES--KILEE------TKFFTDAIET-YKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENVE--L 220
Cdd:cd20656   77 KRLESlrPIREDevtamvESIFNDCMSPeNEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEQGVEFKAIVSngL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 221 AASASVFLYNAFPWIGILpFGKHQQLFRNASVVYDFLSRLI--EKASVNRKPQLPQHFVDAYFDEMDQgkndpsSTFSKE 298
Cdd:cd20656  157 KLGASLTMAEHIPWLRWM-FPLSEKAFAKHGARRDRLTKAImeEHTLARQKSGGGQQHFVALLTLKEQ------YDLSED 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 299 NLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLG 378
Cdd:cd20656  230 TVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLM 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 379 IFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL----DSSGYFAKkeaLVPFSLGRRHCLGEQLA 454
Cdd:cd20656  310 LPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLeedvDIKGHDFR---LLPFGAGRRVCPGAQLG 386
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 302565346 455 RMEMFLFFTALLQrfhlHFPHELVPDLKP-RLGMTLQP 491
Cdd:cd20656  387 INLVTLMLGHLLH----HFSWTPPEGTPPeEIDMTENP 420
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
65-491 3.49e-39

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: 146.96  E-value: 3.49e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  65 YMRKQSQVYGEIFSLDLGGI-STVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGL--LNSRYGQgwvEHRRLAV 141
Cdd:cd11053    3 FLERLRARYGDVFTLRVPGLgPVVVLSDPEAIKQIFTADPDVLHPGEGNSLLEPLLGPNSLllLDGDRHR---RRRKLLM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 142 NSFRyfgyGQ--KSFESKILEETKfftDAIETYK-GRPFDFKQLITSAVSNITNLIIFGErftYEDTDFQHMIELFSENV 218
Cdd:cd11053   80 PAFH----GErlRAYGELIAEITE---REIDRWPpGQPFDLRELMQEITLEVILRVVFGV---DDGERLQELRRLLPRLL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 219 ELAASASVFLYNAFP-WIGILPFGKHQQLFRNasvVYDFLSRLIEKASvnrkpqlpQHFVDAYFD---EMDQGKNDPSST 294
Cdd:cd11053  150 DLLSSPLASFPALQRdLGPWSPWGRFLRARRR---IDALIYAEIAERR--------AEPDAERDDilsLLLSARDEDGQP 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 295 FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDlimGPNGKPSWDDKFKMPYTEAVLHEVLRFCNI 374
Cdd:cd11053  219 LSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELD---ALGGDPDPEDIAKLPYLDAVIKETLRLYPV 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 375 VPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyFAKKEALvPFSLGRRHCLGEQLA 454
Cdd:cd11053  296 APL-VPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRK--PSPYEYL-PFGGGVRRCIGAAFA 371
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 302565346 455 RMEMFLFFTALLQRFHLhfphELV--PDLKPRL-GMTLQP 491
Cdd:cd11053  372 LLEMKVVLATLLRRFRL----ELTdpRPERPVRrGVTLAP 407
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
62-498 7.55e-39

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 147.92  E-value: 7.55e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  62 PHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLLN-SRYGQGWVEHRRLA 140
Cdd:PLN03234  50 PQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGfGQYTAYYREMRKMC 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 141 -VNSFRYFGYGqkSFESKILEETKFFTDAIetYKGR----PFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFS 215
Cdd:PLN03234 130 mVNLFSPNRVA--SFRPVREEECQRMMDKI--YKAAdqsgTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFIDILY 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 216 ENVELAASasVFLYNAFPWIGILP--FGKHQQLFRNASVVYDFLSRLI-EKASVNRKPQLPQHFVDAYfdeMDQGKNDP- 291
Cdd:PLN03234 206 ETQALLGT--LFFSDLFPYFGFLDnlTGLSARLKKAFKELDTYLQELLdETLDPNRPKQETESFIDLL---MQIYKDQPf 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 292 SSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRF 371
Cdd:PLN03234 281 SIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVIKESLRL 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 372 CNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRD-PEVFHPERFLDSS---GYFAKKEALVPFSLGRRH 447
Cdd:PLN03234 361 EPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERFMKEHkgvDFKGQDFELLPFGSGRRM 440
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 302565346 448 CLGEQLARMEMFLFFTALLQRFHLHFPHELVP-DLKPRL--GMTLQPQPYLICA 498
Cdd:PLN03234 441 CPAMHLGIAMVEIPFANLLYKFDWSLPKGIKPeDIKMDVmtGLAMHKKEHLVLA 494
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
123-493 8.79e-39

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: 146.25  E-value: 8.79e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 123 GLLNSrYGQGWVEHRRLAVNSFRYfgygQ--KSFESKILEETKFFTDAIETYKGRPFDFKQLITSAV-------SNITNL 193
Cdd:cd20621   50 GLLFS-EGEEWKKQRKLLSNSFHF----EklKSRLPMINEITKEKIKKLDNQNVNIIQFLQKITGEVvirsffgEEAKDL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 194 IIFGERFTYEDTD-FQHMIELFSENVELAASASVFLYNAFpwiGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQL 272
Cdd:cd20621  125 KINGKEIQVELVEiLIESFLYRFSSPYFQLKRLIFGRKSW---KLFPTKKEKKLQKRVKELRQFIEKIIQNRIKQIKKNK 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 273 PQHFVDAYFDEMDQGKNDPSST-FSKENLI--FSVgeLIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGK 349
Cdd:cd20621  202 DEIKDIIIDLDLYLLQKKKLEQeITKEEIIqqFIT--FFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDD 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 350 PSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSS 429
Cdd:cd20621  280 ITFEDLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQN 359
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302565346 430 GYFAKKEALVPFSLGRRHCLGEQLARMEMflffTALLQRFHLHFPHELVPDLKPRLGMTLQPQP 493
Cdd:cd20621  360 NIEDNPFVFIPFSAGPRNCIGQHLALMEA----KIILIYILKNFEIEIIPNPKLKLIFKLLYEP 419
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
71-488 2.86e-38

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: 145.20  E-value: 2.86e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  71 QVYGEIFSLDLGGISTVVLNGYDVVKECLvhQSGIFAdRPCLPLFMK--MTKMGGLLNSRYGQGWVEHRRLAVNSFRyfg 148
Cdd:cd11046    8 LEYGPIYKLAFGPKSFLVISDPAIAKHVL--RSNAFS-YDKKGLLAEilEPIMGKGLIPADGEIWKKRRRALVPALH--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 149 ygqksfeSKILEET-KFFTDAIETY---------KGRPFDFKQLITSAVSNITNLIIFGERF---TYEDTDFQHMIELFS 215
Cdd:cd11046   82 -------KDYLEMMvRVFGRCSERLmekldaaaeTGESVDMEEEFSSLTLDIIGLAVFNYDFgsvTEESPVIKAVYLPLV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 216 EnvelAASASVFL--YNAFPWIG-ILPFGKHQQlfRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDE--------- 283
Cdd:cd11046  155 E----AEHRSVWEppYWDIPAALfIVPRQRKFL--RDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDYLNEddpsllrfl 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 284 MDQGKNDPSSTFSKENLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEA 363
Cdd:cd11046  229 VDMRDEDVDSKQLRDDLM----TMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRR 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 364 VLHEVLRFCNIVPLGIFHATSEDAVVRG-YSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKE----AL 438
Cdd:cd11046  305 VLNESLRLYPQPPVLIRRAVEDDKLPGGgVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNEViddfAF 384
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 302565346 439 VPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLhfphELVPDlKPRLGMT 488
Cdd:cd11046  385 LPFGGGPRKCLGDQFALLEATVALAMLLRRFDF----ELDVG-PRHVGMT 429
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
74-469 6.81e-38

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: 143.51  E-value: 6.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLP----LFMKMTKMGGllnSRYGQGWVEHRRLAV----NSFR 145
Cdd:cd20653    1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLtgkhIGYNYTTVGS---APYGDHWRNLRRITTleifSSHR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 146 YfgygqKSFESKILEETKFF-TDAIETYKGR--PFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMI----ELFSENV 218
Cdd:cd20653   78 L-----NSFSSIRRDEIRRLlKRLARDSKGGfaKVELKPLFSELTFNNIMRMVAGKRYYGEDVSDAEEAklfrELVSEIF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 219 ELAASASVFLYnaFP---WIGILPFGKHqqLFRNASVVYDFLSRLIEKASVNR---KPQLPQHFV-------DAYFDEMD 285
Cdd:cd20653  153 ELSGAGNPADF--LPilrWFDFQGLEKR--VKKLAKRRDAFLQGLIDEHRKNKesgKNTMIDHLLslqesqpEYYTDEII 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 286 QGkndpsstfskenLIFSvgeLIIAGTETTTNVLRWAilfMAL---YPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTE 362
Cdd:cd20653  229 KG------------LILV---MLLAGTDTSAVTLEWA---MSNllnHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQ 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 363 AVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFlDSSGYFAKKeaLVPFS 442
Cdd:cd20653  291 NIISETLRLYPAAPLLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF-EGEEREGYK--LIPFG 367
                        410       420
                 ....*....|....*....|....*..
gi 302565346 443 LGRRHCLGEQLARMEMFLFFTALLQRF 469
Cdd:cd20653  368 LGRRACPGAGLAQRVVGLALGSLIQCF 394
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
137-475 1.59e-36

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


Pssm-ID: 410683 [Multi-domain]  Cd Length: 425  Bit Score: 140.02  E-value: 1.59e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 137 RRLAVNSFrYFGYGQKSFESKILEETKFFTDAIETY--KGRPFDFKQLITS----AVSNITnliiFGERFTY--EDTDFQ 208
Cdd:cd11060   60 LRRKVASG-YSMSSLLSLEPFVDECIDLLVDLLDEKavSGKEVDLGKWLQYfafdVIGEIT----FGKPFGFleAGTDVD 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 209 HMIElfseNVElAASASVFLYNAFPWIG----ILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQH--FVDAYFD 282
Cdd:cd11060  135 GYIA----SID-KLLPYFAVVGQIPWLDrlllKNPLGPKRKDKTGFGPLMRFALEAVAERLAEDAESAKGRkdMLDSFLE 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 283 EmdqGKNDPSStFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDlIMGPNGKPS----WDDKFKM 358
Cdd:cd11060  210 A---GLKDPEK-VTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEID-AAVAEGKLSspitFAEAQKL 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 359 PYTEAVLHEVLRFCNIVPLGIF-HATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGyfAKKE 436
Cdd:cd11060  285 PYLQAVIKEALRLHPPVGLPLErVVPPGGATICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWLEADE--EQRR 362
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 302565346 437 ----ALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPH 475
Cdd:cd11060  363 mmdrADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVD 405
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
99-471 2.11e-36

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: 139.77  E-value: 2.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  99 LVHQsgIFADRPclpLFMKMTKMGGLLN-------SRYGQGWVEHRRLAVNSFRYFGYGQKSfeSKILEETKFFTDAIE- 170
Cdd:cd11070   22 YLTQ--IFRRRD---DFPKPGNQYKIPAfygpnviSSEGEDWKRYRKIVAPAFNERNNALVW--EESIRQAQRLIRYLLe 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 171 ---TYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSEnVELAASASVFLYNAF-PWIGILPFGKHQQL 246
Cdd:cd11070   95 eqpSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHDTLNA-IKLAIFPPLFLNFPFlDRLPWVLFPSRKRA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 247 FRNasvVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKE----NLIFsvgeLIIAGTETTTNVLRWA 322
Cdd:cd11070  174 FKD---VDEFLSELLDEVEAELSADSKGKQGTESVVASRLKRARRSGGLTEKellgNLFI----FFIAGHETTANTLSFA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 323 ILFMALYPNIQGQVQKEIDLIMGPNGKPSW--DDKFKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYS-----IP 395
Cdd:cd11070  247 LYLLAKHPEVQDWLREEIDSVLGDEPDDWDyeEDFPKLPYLLAVIYETLRLYPPVQL-LNRKTTEPVVVITGLgqeivIP 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 396 KGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSG------YFAK-KEALVPFSLGRRHCLGEQLARMEMFLFFTALLQ 467
Cdd:cd11070  326 KGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSGeigaatRFTPaRGAFIPFSAGPRACLGRKFALVEFVAALAELFR 405

                 ....
gi 302565346 468 RFHL 471
Cdd:cd11070  406 QYEW 409
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
61-492 8.93e-36

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: 137.86  E-value: 8.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  61 LPHVYmrKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKmGGLLNSRyGQGWVEHRRLA 140
Cdd:cd11052    1 LPHYY--HWIKQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEGYFGKSPLQPGLKKLLG-RGLVMSN-GEKWAKHRRIA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 141 VNSFryFGYGQKSFESKILEETKFFTDAIETYKGR---PFDFKQLITSAVSNITNLIIFGErfTYED--TDFQHMIELfs 215
Cdd:cd11052   77 NPAF--HGEKLKGMVPAMVESVSDMLERWKKQMGEegeEVDVFEEFKALTADIISRTAFGS--SYEEgkEVFKLLREL-- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 216 enVELAASASVFLYnaFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKasvnRKPQLPQHFVDAYFDE----MDQGKNDp 291
Cdd:cd11052  151 --QKICAQANRDVG--IPGSRFLPTKGNKKIKKLDKEIEDSLLEIIKK----REDSLKMGRGDDYGDDllglLLEANQS- 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 292 sstfSKENLIFSVGELI-------IAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKFKMPYTEAV 364
Cdd:cd11052  222 ----DDQNKNMTVQEIVdecktffFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCG-KDKPPSDSLSKLKTVSMV 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 365 LHEVLRFCNIVPLGIFHAtSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLD-SSGYFAKKEALVPFS 442
Cdd:cd11052  297 INESLRLYPPAVFLTRKA-KEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADgVAKAAKHPMAFLPFG 375
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 302565346 443 LGRRHCLGEQLARMEMFLFFTALLQRFHLHfpheLVPDLK--PRLGMTLQPQ 492
Cdd:cd11052  376 LGPRNCIGQNFATMEAKIVLAMILQRFSFT----LSPTYRhaPTVVLTLRPQ 423
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
65-493 1.08e-35

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


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 137.41  E-value: 1.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  65 YMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFadRPCLPLFMKMTkMGGllNSRYGQGWVEHRRLAvnsf 144
Cdd:cd11044   13 FIQSRYQKYGPVFKTHLLGRPTVFVIGAEAVRFILSGEGKLV--RYGWPRSVRRL-LGE--NSLSLQDGEEHRRRR---- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 145 RYFGygqKSFESKILEE-----TKFFTDAIETYKGRPF-----DFKQLITSavsnITNLIIFGERFTYEDTDFQHMIELF 214
Cdd:cd11044   84 KLLA---PAFSREALESyvptiQAIVQSYLRKWLKAGEvalypELRRLTFD----VAARLLLGLDPEVEAEALSQDFETW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 215 SENVelaasasvflyNAFPWIgiLPFGKhqqlFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAyFDEMDQGKNDPSST 294
Cdd:cd11044  157 TDGL-----------FSLPVP--LPFTP----FGRAIRARNKLLARLEQAIRERQEEENAEAKDA-LGLLLEAKDEDGEP 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 295 FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLiMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNI 374
Cdd:cd11044  219 LSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDA-LGLEEPLTLESLKKMPYLDQVIKEVLRLVPP 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 375 VPLGiFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKE-ALVPFSLGRRHCLGEQL 453
Cdd:cd11044  298 VGGG-FRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPfSLIPFGGGPRECLGKEF 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 302565346 454 ARMEMFLFFTALLQRFHLhfphELVPDLKPRLGMTLQPQP 493
Cdd:cd11044  377 AQLEMKILASELLRNYDW----ELLPNQDLEPVVVPTPRP 412
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
310-492 1.52e-35

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: 137.30  E-value: 1.52e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 310 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVV 389
Cdd:cd20659  238 AGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPF-IARTLTKPITI 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 390 RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyfAKKE---ALVPFSLGRRHCLGEQLARMEMFLFFTALL 466
Cdd:cd20659  317 DGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPEN---IKKRdpfAFIPFSAGPRNCIGQNFAMNEMKVVLARIL 393
                        170       180
                 ....*....|....*....|....*...
gi 302565346 467 QRFHLhfphELVPD--LKPRLGMTLQPQ 492
Cdd:cd20659  394 RRFEL----SVDPNhpVEPKPGLVLRSK 417
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
196-480 1.68e-35

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: 136.94  E-value: 1.68e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 196 FGERFT-YEDTDFQHMIELFSENVELAASASVFLYnaFPWIG-----ILPFGKHQQLFRNASVVYDFLSRLIEKASvnrk 269
Cdd:cd11058  121 FGESFGcLENGEYHPWVALIFDSIKALTIIQALRR--YPWLLrllrlLIPKSLRKKRKEHFQYTREKVDRRLAKGT---- 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 270 pqlpqhfvdayfDEMD-----QGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDlim 344
Cdd:cd11058  195 ------------DRPDfmsyiLRNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIR--- 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 345 gpngkpswdDKFK------------MPYTEAVLHEVLRFCNIVPLGIFHAT-SEDAVVRGYSIPKGTTVITNLYSVHFDE 411
Cdd:cd11058  260 ---------SAFSsedditldslaqLPYLNAVIQEALRLYPPVPAGLPRVVpAGGATIDGQFVPGGTSVSVSQWAAYRSP 330
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302565346 412 KYWRDPEVFHPERFLDSSGYFA---KKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLhfphELVPD 480
Cdd:cd11058  331 RNFHDPDEFIPERWLGDPRFEFdndKKEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDL----ELDPE 398
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
75-490 2.89e-35

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: 136.30  E-value: 2.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  75 EIFSLDLGGISTVVLNGYDVVKECLVHQSgiFADRPclplfMKMTKMGgLLNSR------YGQGWVEHRRLAvnSFRYFG 148
Cdd:cd11076    4 RLMAFSLGETRVVITSHPETAREILNSPA--FADRP-----VKESAYE-LMFNRaigfapYGEYWRNLRRIA--SNHLFS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 149 YGQ-KSFE---SKILEE-TKFFTDAIETyKGRPFDFKQLITSAVSNITNLIiFGER--FTYEDTDFQHMIELFSENVELA 221
Cdd:cd11076   74 PRRiAASEpqrQAIAAQmVKAIAKEMER-SGEVAVRKHLQRASLNNIMGSV-FGRRydFEAGNEEAEELGEMVREGYELL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 222 AsasVF-LYNAFPWIGILPFGKHQQLFRN-ASVVYDFLSRLIEKASVNRkpqlpQHFVDAYFDEMD-----QGkndpSST 294
Cdd:cd11076  152 G---AFnWSDHLPWLRWLDLQGIRRRCSAlVPRVNTFVGKIIEEHRAKR-----SNRARDDEDDVDvllslQG----EEK 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 295 FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNI 374
Cdd:cd11076  220 LSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPP 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 375 VPLGIFHATS-EDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGY-----FAKKEALVPFSLGRRHC 448
Cdd:cd11076  300 GPLLSWARLAiHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGadvsvLGSDLRLAPFGAGRRVC 379
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 302565346 449 LGEQLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQ 490
Cdd:cd11076  380 PGKALGLATVHLWVAQLLHEFEWLPDDAKPVDLSEVLKLSCE 421
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
253-492 1.58e-34

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: 133.85  E-value: 1.58e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 253 VYDFLSRLIEKASVNRKPQLPQH-FVDAYFDEMDQGKNDPSSTFSKENLIFsvgeLIIAGTETTTNVLRWAILFMALYPN 331
Cdd:cd11043  167 IRKELKKIIEERRAELEKASPKGdLLDVLLEEKDEDGDSLTDEEILDNILT----LLFAGHETTSTTLTLAVKFLAENPK 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 332 IQGQVQKEIDLI---MGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVH 408
Cdd:cd11043  243 VLQELLEEHEEIakrKEEGEGLTWEDYKSMKYTWQVINETLRLAPIVP-GVFRKALQDVEYKGYTIPKGWKVLWSARATH 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 409 FDEKYWRDPEVFHPERFLDSSGYFAKkeALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLhfphELVPDLKPRLGMT 488
Cdd:cd11043  322 LDPEYFPDPLKFNPWRWEGKGKGVPY--TFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRW----EVVPDEKISRFPL 395

                 ....
gi 302565346 489 LQPQ 492
Cdd:cd11043  396 PRPP 399
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
311-492 2.12e-34

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: 133.93  E-value: 2.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 311 GTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMG-PNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPlgiFHA--TSEDA 387
Cdd:cd20660  244 GHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGdSDRPATMDDLKEMKYLECVIKEALRLFPSVP---MFGrtLSEDI 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 388 VVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQ 467
Cdd:cd20660  321 EIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILR 400
                        170       180
                 ....*....|....*....|....*
gi 302565346 468 RFHLHfPHELVPDLKPRLGMTLQPQ 492
Cdd:cd20660  401 NFRIE-SVQKREDLKPAGELILRPV 424
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
186-472 4.42e-34

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


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 133.19  E-value: 4.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 186 AVSNITNLIiFGERFTYEDTDFQHMIELFSENVELAASASvFLYNAFPWIGILPFGKHQQLFRNA-SVVYDFLSRLIEKA 264
Cdd:cd11059  111 AMDVVSHLL-FGESFGTLLLGDKDSRERELLRRLLASLAP-WLRWLPRYLPLATSRLIIGIYFRAfDEIEEWALDLCARA 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 265 SvnRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEI-DLI 343
Cdd:cd11059  189 E--SSLAESSDSESLTVLLLEKLKGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELaGLP 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 344 MGPNGKPSWDDKFKMPYTEAVLHEVLRFCN--------IVPLGifhatseDAVVRGYSIPKGTTVITNLYSVHFDEKYWR 415
Cdd:cd11059  267 GPFRGPPDLEDLDKLPYLNAVIRETLRLYPpipgslprVVPEG-------GATIGGYYIPGGTIVSTQAYSLHRDPEVFP 339
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 302565346 416 DPEVFHPERFLDSSG--YFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLH 472
Cdd:cd11059  340 DPEEFDPERWLDPSGetAREMKRAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTS 398
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
230-501 1.68e-33

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: 131.54  E-value: 1.68e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 230 NAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKasvnRKpQLPQHFVDAYFDEMDQGKnDPSST--FSKENLIFSVGEL 307
Cdd:cd11068  165 NRPPILNKLRRRAKRQFREDIALMRDLVDEIIAE----RR-ANPDGSPDDLLNLMLNGK-DPETGekLSDENIRYQMITF 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 308 IIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPnGKPSWDDKFKMPYTEAVLHEVLRFCNIVPlGIFHATSEDA 387
Cdd:cd11068  239 LIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGD-DPPPYEQVAKLRYIRRVLDETLRLWPTAP-AFARKPKEDT 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 388 VVRG-YSIPKGTTVITNLYSVHFDEK-YWRDPEVFHPERFLDssGYFAK--KEALVPFSLGRRHCLGEQLARMEMFLFFT 463
Cdd:cd11068  317 VLGGkYPLKKGDPVLVLLPALHRDPSvWGEDAEEFRPERFLP--EEFRKlpPNAWKPFGNGQRACIGRQFALQEATLVLA 394
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 302565346 464 ALLQRFHLHFPHELVPDLKPRLgmTLQPQPYLICAERR 501
Cdd:cd11068  395 MLLQRFDFEDDPDYELDIKETL--TLKPDGFRLKARPR 430
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
74-497 3.80e-33

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: 130.41  E-value: 3.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRP------CLPL---------------FMK---MTKmggLLNSRy 129
Cdd:cd20655    1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPvpaaaeSLLYgssgfafapygdywkFMKklcMTE---LLGPR- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 130 gqgwvehrrlAVNSFRyfgygqkSFESkilEETKFFTDAI--ETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDF 207
Cdd:cd20655   77 ----------ALERFR-------PIRA---QELERFLRRLldKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 208 QHMIELFSENVELAA--SASVFLYNAFPWiGILPFGKhqqlfRNASVVYDF---LSRLI---EKASVNRKPQLPQHFVDA 279
Cdd:cd20655  137 EEVRKLVKESAELAGkfNASDFIWPLKKL-DLQGFGK-----RIMDVSNRFdelLERIIkehEEKRKKRKEGGSKDLLDI 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 280 YFDEMdqgkNDPSSTF--SKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFK 357
Cdd:cd20655  211 LLDAY----EDENAEYkiTRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPN 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 358 MPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEA 437
Cdd:cd20655  287 LPYLQAVVKETLRLHPPGPL-LVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQELDV 365
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 302565346 438 ------LVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLIC 497
Cdd:cd20655  366 rgqhfkLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCFDWKVGDGEKVNMEEASGLTLPRAHPLKC 431
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
60-474 4.35e-33

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 131.39  E-value: 4.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  60 ELPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMG-GLLNSRYGQGWVEHRR 138
Cdd:PLN02394  50 DLNHRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGqDMVFTVYGDHWRKMRR 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 139 LAVNSFryfgygqksFESKILEETKFFTDA-----IETYKGRP------FDFKQLITSAVSNITNLIIFGERF-TYEDTD 206
Cdd:PLN02394 130 IMTVPF---------FTNKVVQQYRYGWEEeadlvVEDVRANPeaategVVIRRRLQLMMYNIMYRMMFDRRFeSEDDPL 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 207 FQHMIELFSENVELAASasvFLYNAFPWIGIL-PF------------GKHQQLFRNASVvyDFLSRLIEKASVNRKPQ-- 271
Cdd:PLN02394 201 FLKLKALNGERSRLAQS---FEYNYGDFIPILrPFlrgylkicqdvkERRLALFKDYFV--DERKKLMSAKGMDKEGLkc 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 272 LPQHFVDAyfdemdQGKNDpsstFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPS 351
Cdd:PLN02394 276 AIDHILEA------QKKGE----INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVT 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 352 WDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGy 431
Cdd:PLN02394 346 EPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEA- 424
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 302565346 432 faKKEA------LVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFP 474
Cdd:PLN02394 425 --KVEAngndfrFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPP 471
PLN02966 PLN02966
cytochrome P450 83A1
62-480 4.71e-33

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 131.41  E-value: 4.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  62 PHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPclPL----FMKMTKMGGLLNsRYGQGWVEHR 137
Cdd:PLN02966  51 PQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRP--PHrgheFISYGRRDMALN-HYTPYYREIR 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 138 RLAVNSFrYFGYGQKSFESKILEETKFFTDAIETY--KGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFS 215
Cdd:PLN02966 128 KMGMNHL-FSPTRVATFKHVREEEARRMMDKINKAadKSEVVDISELMLTFTNSVVCRQAFGKKYNEDGEEMKRFIKILY 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 216 ENVELAASasVFLYNAFPWIGILP-----FGKHQQLF-RNASVVYDFLSRLIEKASVnrKPQlPQHFVDAYfdeMDQGKN 289
Cdd:PLN02966 207 GTQSVLGK--IFFSDFFPYCGFLDdlsglTAYMKECFeRQDTYIQEVVNETLDPKRV--KPE-TESMIDLL---MEIYKE 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 290 DP-SSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKP--SWDDKFKMPYTEAVLH 366
Cdd:PLN02966 279 QPfASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGSTfvTEDDVKNLPYFRALVK 358
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 367 EVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKE-ALVPFSLG 444
Cdd:PLN02966 359 ETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKGTDyEFIPFGSG 438
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 302565346 445 RRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVPD 480
Cdd:PLN02966 439 RRMCPGMRLGAAMLEVPYANLLLNFNFKLPNGMKPD 474
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
60-490 7.45e-33

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 131.13  E-value: 7.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  60 ELPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRP----CLPLFMKMTKMgglLNSRYGQGWVE 135
Cdd:PLN00110  50 NMPHVALAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRPpnagATHLAYGAQDM---VFADYGPRWKL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 136 HRRLAvnsfRYFGYGQKSFES----KILEETKFFTDAIE-TYKGRPFDFKQLITSAVSNITNLIIFGERF----TYEDTD 206
Cdd:PLN00110 127 LRKLS----NLHMLGGKALEDwsqvRTVELGHMLRAMLElSQRGEPVVVPEMLTFSMANMIGQVILSRRVfetkGSESNE 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 207 FQHMIelfsenVELAASASVFLYNAF----PWI---GILpfGKHQQLFRNASVvydFLSRLIEK--ASVNRKPQLPQhFV 277
Cdd:PLN00110 203 FKDMV------VELMTTAGYFNIGDFipsiAWMdiqGIE--RGMKHLHKKFDK---LLTRMIEEhtASAHERKGNPD-FL 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 278 DAYfdeMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFK 357
Cdd:PLN00110 271 DVV---MANQENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPK 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 358 MPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLdsSGYFAKKEA 437
Cdd:PLN00110 348 LPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFL--SEKNAKIDP 425
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 302565346 438 ------LVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVPDLKPRLGMTLQ 490
Cdd:PLN00110 426 rgndfeLIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVELNMDEAFGLALQ 484
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
220-482 1.01e-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: 129.31  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 220 LAASASVFLYNAF------PWIGILPFGKHQQLFRNASVVYDFLSRLIE--KASVNRKPQlpqhfvdayfdemDQGK--- 288
Cdd:cd11069  150 FEPTLLGSLLFILllflprWLVRILPWKANREIRRAKDVLRRLAREIIRekKAALLEGKD-------------DSGKdil 216
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 289 ------NDPSST--FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEI-DLIMG-PNGKPSWDDKFKM 358
Cdd:cd11069  217 sillraNDFADDerLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIrAALPDpPDGDLSYDDLDRL 296
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 359 PYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKEA 437
Cdd:cd11069  297 PYLNAVCRETLRLYPPVPL-TSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASPGGA 375
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 302565346 438 -----LVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLhfphELVPDLK 482
Cdd:cd11069  376 gsnyaLLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEF----ELDPDAE 421
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
73-474 1.64e-32

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: 128.74  E-value: 1.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMG-GLLNSRYGQGWVEHRRLAVNSFryfgygq 151
Cdd:cd11074    3 FGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGqDMVFTVYGEHWRKMRRIMTVPF------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 152 ksFESKILEETKFFTDA-----IETYKGRP------FDFKQLITSAVSNITNLIIFGERFTYEDTD-FQHMIELFSENVE 219
Cdd:cd11074   76 --FTNKVVQQYRYGWEEeaarvVEDVKKNPeaategIVIRRRLQLMMYNNMYRIMFDRRFESEDDPlFVKLKALNGERSR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 220 LAASasvFLYNAFPWIGIL-PF------------GKHQQLFRNAsvvydFLSRLIEKASVNR-KPQLPQHFVDAYFDEMD 285
Cdd:cd11074  154 LAQS---FEYNYGDFIPILrPFlrgylkickevkERRLQLFKDY-----FVDERKKLGSTKStKNEGLKCAIDHILDAQK 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 286 QGKndpsstFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVL 365
Cdd:cd11074  226 KGE------INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVV 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 366 HEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyfAKKEA------LV 439
Cdd:cd11074  300 KETLRLRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEE---SKVEAngndfrYL 376
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 302565346 440 PFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFP 474
Cdd:cd11074  377 PFGVGRRSCPGIILALPILGITIGRLVQNFELLPP 411
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
73-483 3.19e-32

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: 128.20  E-value: 3.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMK-MTKMGGLL--NSRYGQGWvEHRRLAVNSfryfGY 149
Cdd:cd11066    1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRPTFYTFHKvVSSTQGFTigTSPWDESC-KRRRKAAAS----AL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 150 GQKSFES--KILE-ETKFFTDAI--ETYKGR-PFDFKQLITSAVSNITNLIIFGERFtyedtDFQHMIELFSENVELAAS 223
Cdd:cd11066   76 NRPAVQSyaPIIDlESKSFIRELlrDSAEGKgDIDPLIYFQRFSLNLSLTLNYGIRL-----DCVDDDSLLLEIIEVESA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 224 ASVF------LYNAFPWIGILP----FGKHQQLFRNASVVY--DFLSRLIEKAS-VNRKPQLpqhfvdayfdemdQGKN- 289
Cdd:cd11066  151 ISKFrstssnLQDYIPILRYFPkmskFRERADEYRNRRDKYlkKLLAKLKEEIEdGTDKPCI-------------VGNIl 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 290 -DPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMA--LYPNIQGQVQKEIdLIMGPNGKPSWDDKF---KMPYTEA 363
Cdd:cd11066  218 kDKESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLShpPGQEIQEKAYEEI-LEAYGNDEDAWEDCAaeeKCPYVVA 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 364 VLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSL 443
Cdd:cd11066  297 LVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHFSFGA 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 302565346 444 GRRHCLGEQLARMEMFLFFTALLQRFHLH-FPHELVPDLKP 483
Cdd:cd11066  377 GSRMCAGSHLANRELYTAICRLILLFRIGpKDEEEPMELDP 417
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
194-472 5.69e-32

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: 127.27  E-value: 5.69e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 194 IIFG---ERFTYEDTDFQHMIELFSENvELAASASVFLYNAFPWIGILpFGkhqqLFRNASVVYDFLSRLI-------EK 263
Cdd:cd11056  122 CAFGldaNSLNDPENEFREMGRRLFEP-SRLRGLKFMLLFFFPKLARL-LR----LKFFPKEVEDFFRKLVrdtieyrEK 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 264 ASVNRKPQLpQHFVDAYfDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLI 343
Cdd:cd11056  196 NNIVRNDFI-DLLLELK-KKGKIEDDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEV 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 344 M-GPNGKPSWDDKFKMPYTEAVLHEVLRfcnIVPLGIFHA--TSEDAVVRG--YSIPKGTTVITNLYSVHFDEKYWRDPE 418
Cdd:cd11056  274 LeKHGGELTYEALQEMKYLDQVVNETLR---KYPPLPFLDrvCTKDYTLPGtdVVIEKGTPVIIPVYALHHDPKYYPEPE 350
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 302565346 419 VFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLH 472
Cdd:cd11056  351 KFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVE 404
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
290-469 2.96e-31

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 125.86  E-value: 2.96e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 290 DPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKP---SWDDKFKMPYTEAVLH 366
Cdd:PLN02987 258 ASDDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKSDSyslEWSDYKSMPFTQCVVN 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 367 EVLRFCNIVPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRR 446
Cdd:PLN02987 338 ETLRVANIIG-GIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPR 416
                        170       180
                 ....*....|....*....|...
gi 302565346 447 HCLGEQLARMEMFLFFTALLQRF 469
Cdd:PLN02987 417 LCPGYELARVALSVFLHRLVTRF 439
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
74-490 4.23e-31

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: 124.84  E-value: 4.23e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  74 GEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPclplfmkmTKMGG---------LLNSRYGQGWVEHRRL-AVNS 143
Cdd:cd20657    1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRP--------PNAGAthmaynaqdMVFAPYGPRWRLLRKLcNLHL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 144 FRyfGYGQKSFESKILEETKFFTDAI--ETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTD-----FQHMIelfse 216
Cdd:cd20657   73 FG--GKALEDWAHVRENEVGHMLKSMaeASRKGEPVVLGEMLNVCMANMLGRVMLSKRVFAAKAGakaneFKEMV----- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 217 nVELAASASVFLYNAF-PWIGIL-PFGKHQQLFRNASVVYDFLSRLIE--KASVNRKPQLPQhFVDayFDEMDQGKNDPS 292
Cdd:cd20657  146 -VELMTVAGVFNIGDFiPSLAWMdLQGVEKKMKRLHKRFDALLTKILEehKATAQERKGKPD-FLD--FVLLENDDNGEG 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 293 STFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFC 372
Cdd:cd20657  222 ERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLH 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 373 NIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLdsSGYFAKKEA------LVPFSLGRR 446
Cdd:cd20657  302 PSTPLNLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFL--PGRNAKVDVrgndfeLIPFGAGRR 379
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 302565346 447 HCLGEQL-ARMEMFLFFTaLLQRFHLHFPHELVPD---LKPRLGMTLQ 490
Cdd:cd20657  380 ICAGTRMgIRMVEYILAT-LVHSFDWKLPAGQTPEelnMEEAFGLALQ 426
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
61-489 4.54e-31

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 126.09  E-value: 4.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  61 LPHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRP-CLPLFMKMTKMGGLLNSRYGQGWVEHRRL 139
Cdd:PLN03112  52 LPHRDLASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRPrTLAAVHLAYGCGDVALAPLGPHWKRMRRI 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 140 AVNSF----RYfgygqKSFESKILEETKFFTDAI--ETYKGRPFDFKQLITSAVSNITNLIIFGERF-------TYEDTD 206
Cdd:PLN03112 132 CMEHLlttkRL-----ESFAKHRAEEARHLIQDVweAAQTGKPVNLREVLGAFSMNNVTRMLLGKQYfgaesagPKEAME 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 207 FQHMI-ELFSenvelaASASVFLYNAFP-WIGILPFGKHQQLFRNASVVYDFLSRLIEK----ASVNRKPQLPQHFVDAY 280
Cdd:PLN03112 207 FMHIThELFR------LLGVIYLGDYLPaWRWLDPYGCEKKMREVEKRVDEFHDKIIDEhrraRSGKLPGGKDMDFVDVL 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 281 FDEmdQGKNDPSSTFSKEnLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPY 360
Cdd:PLN03112 281 LSL--PGENGKEHMDDVE-IKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNY 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 361 TEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGyfAKKEA--- 437
Cdd:PLN03112 358 LRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAEG--SRVEIshg 435
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 302565346 438 ----LVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVP---DLKPRLGMTL 489
Cdd:PLN03112 436 pdfkILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDGLRPediDTQEVYGMTM 494
PLN02687 PLN02687
flavonoid 3'-monooxygenase
62-490 2.67e-30

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 123.77  E-value: 2.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  62 PHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECL-VHQSGiFADRPclplfmkmTKMGG---------LLNSRYGQ 131
Cdd:PLN02687  55 PHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLrTHDAN-FSNRP--------PNSGAehmaynyqdLVFAPYGP 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 132 GWVEHRRL-AVNSFRyfGYGQKSFESKILEETKFFTDAI-ETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTD--- 206
Cdd:PLN02687 126 RWRALRKIcAVHLFS--AKALDDFRHVREEEVALLVRELaRQHGTAPVNLGQLVNVCTTNALGRAMVGRRVFAGDGDeka 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 207 --FQHMIelfsenVELAASASVF----LYNAFPWI---GILpfGKHQQLFRNASvvyDFLSRLIEKASVNRKPQLPQHfV 277
Cdd:PLN02687 204 reFKEMV------VELMQLAGVFnvgdFVPALRWLdlqGVV--GKMKRLHRRFD---AMMNGIIEEHKAAGQTGSEEH-K 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 278 D------AYFDEmDQGKNDPSSTFSKE--NLIFSvgeLIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGK 349
Cdd:PLN02687 272 DllstllALKRE-QQADGEGGRITDTEikALLLN---LFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRL 347
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 350 PSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL--- 426
Cdd:PLN02687 348 VSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpgg 427
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 427 DSSGYFAKKE--ALVPFSLGRRHCLGEQLArMEMFLFFTA-LLQRFHLHFPHELVPD---LKPRLGMTLQ 490
Cdd:PLN02687 428 EHAGVDVKGSdfELIPFGAGRRICAGLSWG-LRMVTLLTAtLVHAFDWELADGQTPDklnMEEAYGLTLQ 496
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
303-491 3.75e-30

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: 122.08  E-value: 3.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 303 SVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHA 382
Cdd:cd20646  237 SLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVI 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 383 TSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFF 462
Cdd:cd20646  317 VEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLAL 396
                        170       180       190
                 ....*....|....*....|....*....|....
gi 302565346 463 TALLQRFhlhfphELVPD-----LKPRLGMTLQP 491
Cdd:cd20646  397 SRLIKRF------EVRPDpsggeVKAITRTLLVP 424
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
307-493 6.13e-30

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: 121.21  E-value: 6.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 307 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLgIFHATSED 386
Cdd:cd11049  228 LLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWL-LTRRTTAD 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 387 AVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALL 466
Cdd:cd11049  306 VELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIA 385
                        170       180
                 ....*....|....*....|....*....
gi 302565346 467 QRFHLHfpheLVPDLK--PRLGMTLQPQP 493
Cdd:cd11049  386 SRWRLR----PVPGRPvrPRPLATLRPRR 410
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
292-471 8.26e-30

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: 121.18  E-value: 8.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 292 SSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRF 371
Cdd:cd20647  230 SKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRL 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 372 CNIVPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLdssgyfaKKEAL--------VPFSL 443
Cdd:cd20647  310 FPVLP-GNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWL-------RKDALdrvdnfgsIPFGY 381
                        170       180
                 ....*....|....*....|....*...
gi 302565346 444 GRRHCLGEQLARMEMFLFFTALLQRFHL 471
Cdd:cd20647  382 GIRSCIGRRIAELEIHLALIQLLQNFEI 409
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
307-496 1.12e-29

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: 120.40  E-value: 1.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 307 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMG-PNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSE 385
Cdd:cd11042  220 LLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGdGDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKP 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 386 DAV-VRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKE--ALVPFSLGRRHCLGEQLARMEMFLFF 462
Cdd:cd11042  300 FEVeGGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKGGkfAYLPFGAGRHRCIGENFAYLQIKTIL 379
                        170       180       190
                 ....*....|....*....|....*....|....
gi 302565346 463 TALLQRFHLHFPHELVPDLKPRLGMTLQPQPYLI 496
Cdd:cd11042  380 STLLRNFDFELVDSPFPEPDYTTMVVWPKGPARV 413
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
256-487 2.62e-29

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: 119.87  E-value: 2.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 256 FLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQ 335
Cdd:cd20680  200 EMKAEEDKTGDSDGESPSKKKRKAFLDMLLSVTDEEGNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRK 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 336 VQKEIDLIMGPNGKP-SWDDKFKMPYTEAVLHEVLRFCNIVPLgiFHAT-SEDAVVRGYSIPKGTTVITNLYSVHFDEKY 413
Cdd:cd20680  280 VHKELDEVFGKSDRPvTMEDLKKLRYLECVIKESLRLFPSVPL--FARSlCEDCEIRGFKVPKGVNAVIIPYALHRDPRY 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 414 WRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHL---HFPHELVPD----LKPRLG 486
Cdd:cd20680  358 FPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVeanQKREELGLVgeliLRPQNG 437

                 .
gi 302565346 487 M 487
Cdd:cd20680  438 I 438
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
253-492 3.54e-29

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: 119.06  E-value: 3.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 253 VYDFLSRLIEKASVNRKPQLPQHFVDaYFDEMDQGKNDPSSTFSK---------ENLIFsvgelIIAGTETTTNVLRWAI 323
Cdd:cd20650  179 VTNFFYKSVKKIKESRLDSTQKHRVD-FLQLMIDSQNSKETESHKalsdleilaQSIIF-----IFAGYETTSSTLSFLL 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 324 LFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRfcnIVPLG--IFHATSEDAVVRGYSIPKGTTVI 401
Cdd:cd20650  253 YELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLR---LFPIAgrLERVCKKDVEINGVFIPKGTVVM 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 402 TNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVPDL 481
Cdd:cd20650  330 IPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPCKETQIPL 409
                        250
                 ....*....|.
gi 302565346 482 KPRLGMTLQPQ 492
Cdd:cd20650  410 KLSLQGLLQPE 420
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
70-492 5.37e-29

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: 118.71  E-value: 5.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  70 SQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLfMKMTKMGGLLNSRyGQGWVEHRRLAVNSF----- 144
Cdd:cd20639    8 RKIYGKTFLYWFGPTPRLTVADPELIREILLTRADHFDRYEAHPL-VRQLEGDGLVSLR-GEKWAHHRRVITPAFhmenl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 145 ------------------RYFGYGQKSFESKILEEtkfftdaietykgrpfdFKQLITSAVSNITnliiFGErfTYEDTd 206
Cdd:cd20639   86 krlvphvvksvadmldkwEAMAEAGGEGEVDVAEW-----------------FQNLTEDVISRTA----FGS--SYEDG- 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 207 fQHMIELFSENVELAASA--SVFLynafPWIGILPFGKHQQLFRNASVVYDFLSRLIEkasvNRKPQLPQHFVDAYFDE- 283
Cdd:cd20639  142 -KAVFRLQAQQMLLAAEAfrKVYI----PGYRFLPTKKNRKSWRLDKEIRKSLLKLIE----RRQTAADDEKDDEDSKDl 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 284 ----MDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMP 359
Cdd:cd20639  213 lglmISAKNARNGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLK 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 360 YTEAVLHEVLRfcnIVPLGIF--HATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKE 436
Cdd:cd20639  293 TLGMILNETLR---LYPPAVAtiRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARAAKHP 369
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 302565346 437 -ALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHfpheLVPDL--KPRLGMTLQPQ 492
Cdd:cd20639  370 lAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFR----LSPSYahAPTVLMLLQPQ 424
PLN02655 PLN02655
ent-kaurene oxidase
62-454 1.34e-28

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 118.31  E-value: 1.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  62 PHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPcLPLFM-------KMTKMggllnSRYGQgwv 134
Cdd:PLN02655  21 PHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRK-LSKALtvltrdkSMVAT-----SDYGD--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 135 EHR---RLAVNSFRYFGyGQKSF----ESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGErftyeDTDF 207
Cdd:PLN02655  92 FHKmvkRYVMNNLLGAN-AQKRFrdtrDMLIENMLSGLHALVKDDPHSPVNFRDVFENELFGLSLIQALGE-----DVES 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 208 QHMIEL---------FSENVE--LAASASVFLYNAFPWIGILPFGKHQQL-----FRNASVvydfLSRLIEKasvnRKPQ 271
Cdd:PLN02655 166 VYVEELgteiskeeiFDVLVHdmMMCAIEVDWRDFFPYLSWIPNKSFETRvqtteFRRTAV----MKALIKQ----QKKR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 272 LPQ-HFVDAYFDEMdqgkNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNgKP 350
Cdd:PLN02655 238 IARgEERDCYLDFL----LSEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDE-RV 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 351 SWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSG 430
Cdd:PLN02655 313 TEEDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKY 392
                        410       420
                 ....*....|....*....|....
gi 302565346 431 YFAKKEALVPFSLGRRHCLGEQLA 454
Cdd:PLN02655 393 ESADMYKTMAFGAGKRVCAGSLQA 416
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
61-492 2.95e-28

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: 116.78  E-value: 2.95e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  61 LPHvYMRKQSQvYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMtkMGGLLNSRYGQGWVEHRRLA 140
Cdd:cd20641    1 LPH-YQQWKSQ-YGETFLYWQGTTPRICISDHELAKQVLSDKFGFFGKSKARPEILKL--SGKGLVFVNGDDWVRHRRVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 141 VNSFRYfgygqksfeSKILEETKFFTDA----IETYKgrpfdfKQLITSAVSNITnlIIFGERFTYEDTD---------- 206
Cdd:cd20641   77 NPAFSM---------DKLKSMTQVMADCtermFQEWR------KQRNNSETERIE--VEVSREFQDLTADiiattafgss 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 207 FQHMIELFSENVELAASASVFLYNAF-PWIGILPFGKHQQLFRNASVVYDFLSRLI-EKASVNRK---PQLPQHFVDAYF 281
Cdd:cd20641  140 YAEGIEVFLSQLELQKCAAASLTNLYiPGTQYLPTPRNLRVWKLEKKVRNSIKRIIdSRLTSEGKgygDDLLGLMLEAAS 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 282 DEmdQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYT 361
Cdd:cd20641  220 SN--EGGRRTERKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLM 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 362 EAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKK-EALV 439
Cdd:cd20641  298 NMVLMETLRLYGPVIN-IARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHpNALL 376
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 302565346 440 PFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVPdlKPRLGMTLQPQ 492
Cdd:cd20641  377 SFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLSPEYVH--APADHLTLQPQ 427
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
240-491 3.61e-28

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


Pssm-ID: 410686 [Multi-domain]  Cd Length: 419  Bit Score: 116.12  E-value: 3.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 240 FGKHQQLFRNA------SVVYDFLSRLIEKASVNRKPQLPQHFVDAY--FDEMDQGKNDPsstfsKE--NLIFSVgelII 309
Cdd:cd11063  155 LGKLLWLLRDKkfreacKVVHRFVDPYVDKALARKEESKDEESSDRYvfLDELAKETRDP-----KElrDQLLNI---LL 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 310 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVV 389
Cdd:cd11063  227 AGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLP 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 390 RG--------YSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGyfaKKEALVPFSLGRRHCLGEQLARMEMFL 460
Cdd:cd11063  307 RGggpdgkspIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWEDLKR---PGWEYLPFNGGPRICLGQQFALTEASY 383
                        250       260       270
                 ....*....|....*....|....*....|.
gi 302565346 461 FFTALLQRFHlHFPHELVPDLKPRLGMTLQP 491
Cdd:cd11063  384 VLVRLLQTFD-RIESRDVRPPEERLTLTLSN 413
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
123-485 7.52e-28

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: 115.45  E-value: 7.52e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 123 GLLNSRyGQGWVEHRRLAVNSFRYFGYgqKSFESKILEETKFFTDAIETY--KGRPFDfkqlITSAVSNITNLIIFGERF 200
Cdd:cd20678   59 GLLVLN-GQKWFQHRRLLTPAFHYDIL--KPYVKLMADSVRVMLDKWEKLatQDSSLE----IFQHVSLMTLDTIMKCAF 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 201 TYEDT-----DFQHMIELFSENVELAAS--ASVFLYNAFpwigILPFGKHQQLFRNA-SVVYDFLSRLIE--KASVNRKP 270
Cdd:cd20678  132 SHQGScqldgRSNSYIQAVSDLSNLIFQrlRNFFYHNDF----IYKLSPHGRRFRRAcQLAHQHTDKVIQqrKEQLQDEG 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 271 QLPQHFVDAYFDEMD---QGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPN 347
Cdd:cd20678  208 ELEKIKKKRHLDFLDillFAKDENGKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDG 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 348 GKPSWDDKFKMPYTEAVLHEVLRFCNIVPlGIFHATSED-AVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL 426
Cdd:cd20678  288 DSITWEHLDQMPYTTMCIKEALRLYPPVP-GISRELSKPvTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFS 366
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 302565346 427 DSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVPDLKPRL 485
Cdd:cd20678  367 PENSSKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFELLPDPTRIPIPIPQL 425
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
65-493 1.77e-27

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: 113.95  E-value: 1.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  65 YMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLL-----NSRYgqgwveHRRL 139
Cdd:cd11045    2 FARQRYRRYGPVSWTGMLGLRVVALLGPDANQLVLRNRDKAFSSKQGWDPVIGPFFHRGLMlldfdEHRA------HRRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 140 AVNSFryfgyGQKSFESKILEETKFFTDAIETY-KGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIElfsenV 218
Cdd:cd11045   76 MQQAF-----TRSALAGYLDRMTPGIERALARWpTGAGFQFYPAIKELTLDLATRVFLGVDLGPEADKVNKAFI-----D 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 219 ELAASASVFLYNafpwigiLPFGKHQQLFRNASVVYDFLSRLIekasvnrkPQLPQHFVDAYFDEMDQGKNDPSSTFSKE 298
Cdd:cd11045  146 TVRASTAIIRTP-------IPGTRWWRGLRGRRYLEEYFRRRI--------PERRAGGGDDLFSALCRAEDEDGDRFSDD 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 299 NLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLg 378
Cdd:cd11045  211 DIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL--GKGTLDYEDLGQLEVTDWVFKEALRLVPPVPT- 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 379 IFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAK-KEALVPFSLGRRHCLGEQLARME 457
Cdd:cd11045  288 LPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVhRYAWAPFGGGAHKCIGLHFAGME 367
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 302565346 458 MFLFFTALLQRFHLhfphELVPDLKPRLGMTLQPQP 493
Cdd:cd11045  368 VKAILHQMLRRFRW----WSVPGYYPPWWQSPLPAP 399
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
123-490 3.51e-27

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: 113.45  E-value: 3.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 123 GLLNSRyGQGWVEHRRLAVNSF---RYFGYGQKSFESKILEETKFFTDAIETyKGRPFDFKQLITSAVSNITNLIIFGer 199
Cdd:cd11064   50 GIFNVD-GELWKFQRKTASHEFssrALREFMESVVREKVEKLLVPLLDHAAE-SGKVVDLQDVLQRFTFDVICKIAFG-- 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 200 FTYEDTDFQHMIELFSENVElAASASVFLYNAFP--------WIGIlpfGKHQQLFRNASVVYDFLSRLI-----EKASV 266
Cdd:cd11064  126 VDPGSLSPSLPEVPFAKAFD-DASEAVAKRFIVPpwlwklkrWLNI---GSEKKLREAIRVIDDFVYEVIsrrreELNSR 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 267 NRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKENLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEID--LIM 344
Cdd:cd11064  202 EEENNVREDLLSRFLASEEEEGEPVSDKFLRDIVL----NFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKskLPK 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 345 GPNGK---PSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVF 420
Cdd:cd11064  278 LTTDEsrvPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWgEDALEF 357
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302565346 421 HPERFLDSSGYFAKKEAL--VPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLhfphELVP--DLKPRLGMTLQ 490
Cdd:cd11064  358 KPERWLDEDGGLRPESPYkfPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDF----KVVPghKVEPKMSLTLH 427
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
274-471 8.25e-27

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: 112.21  E-value: 8.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 274 QHFVDAYFDEMDQGKNDP-------SSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGP 346
Cdd:cd20645  194 KHCIDKRLQRYSQGPANDflcdiyhDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPA 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 347 NGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL 426
Cdd:cd20645  274 NQTPRAEDLKNMPYLKACLKESMRLTPSVPF-TSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWL 352
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 302565346 427 DssgyfaKKEAL-----VPFSLGRRHCLGEQLARMEMFLFFTALLQRFHL 471
Cdd:cd20645  353 Q------EKHSInpfahVPFGIGKRMCIGRRLAELQLQLALCWIIQKYQI 396
PLN02971 PLN02971
tryptophan N-hydroxylase
71-474 3.02e-25

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 108.97  E-value: 3.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  71 QVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPcLPLFMKMTKMG--GLLNSRYGQGWVEHRRLAVNSFrYFG 148
Cdd:PLN02971  90 ELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRP-LTYAQKILSNGykTCVITPFGEQFKKMRKVIMTEI-VCP 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 149 YGQKSFESKILEETKFFTDAIETY--KGRPFDFKQLITSAVSNITNLIIFGERFTYEDT---------DFQHMIELFSEn 217
Cdd:PLN02971 168 ARHRWLHDNRAEETDHLTAWLYNMvkNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTepdggptleDIEHMDAMFEG- 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 218 veLAASASVFLYNAFPWIGILPFGKHQQLFRNASVVYD-----FLSRLIEKASVNRKPQLpQHFVDAYFDEMDQGKNdps 292
Cdd:PLN02971 247 --LGFTFAFCISDYLPMLTGLDLNGHEKIMRESSAIMDkyhdpIIDERIKMWREGKRTQI-EDFLDIFISIKDEAGQ--- 320
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 293 STFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFC 372
Cdd:PLN02971 321 PLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLH 400
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 373 NIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKE---ALVPFSLGRRHCL 449
Cdd:PLN02971 401 PVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTEndlRFISFSTGKRGCA 480
                        410       420
                 ....*....|....*....|....*
gi 302565346 450 GEQLARMEMFLFFTALLQRFHLHFP 474
Cdd:PLN02971 481 APALGTAITTMMLARLLQGFKWKLA 505
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
304-488 1.07e-24

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: 106.38  E-value: 1.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 304 VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHAT 383
Cdd:cd20648  239 VTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIP 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 384 SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL---DSSGYFAKkealVPFSLGRRHCLGEQLARMEMFL 460
Cdd:cd20648  319 DRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLgkgDTHHPYAS----LPFGFGKRSCIGRRIAELEVYL 394
                        170       180
                 ....*....|....*....|....*...
gi 302565346 461 fftaLLQRFHLHFPHELVPDLKPRLGMT 488
Cdd:cd20648  395 ----ALARILTHFEVRPEPGGSPVKPMT 418
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
202-492 4.31e-24

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: 105.07  E-value: 4.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 202 YEDTDFQHMIELFSENVELAASASV-----FLYNAFPWIgilpfgkhqqlFRNASVVYDFLSRLIEKASVNRKPQLPQHF 276
Cdd:cd20622  165 APLPDELEAVLDLADSVEKSIKSPFpklshWFYRNQPSY-----------RRAAKIKDDFLQREIQAIARSLERKGDEGE 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 277 VDAYFDEMDQ------GKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGP---- 346
Cdd:cd20622  234 VRSAVDHMVRrelaaaEKEGRKPDYYSQVIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEavae 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 347 NGKPSWDD--KFKMPYTEAVLHEVLRFCNIVPLGIFHATsEDAVVRGYSIPKGTTVITNLY-------SVHFDE------ 411
Cdd:cd20622  314 GRLPTAQEiaQARIPYLDAVIEEILRCANTAPILSREAT-VDTQVLGYSIPKGTNVFLLNNgpsylspPIEIDEsrrsss 392
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 412 --------KYW--RDPEVFHPERFLDSSGYFAKKE------ALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHfph 475
Cdd:cd20622  393 saakgkkaGVWdsKDIADFDPERWLVTDEETGETVfdpsagPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELL--- 469
                        330       340
                 ....*....|....*....|....
gi 302565346 476 elvpDLKPRL-------GMTLQPQ 492
Cdd:cd20622  470 ----PLPEALsgyeaidGLTRMPK 489
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
64-489 6.40e-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: 103.98  E-value: 6.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  64 VYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKEcLVHQSGIFADRPCLPLFMKmtKMGGL-LNSRYGQGWVEHRRLAVN 142
Cdd:cd11040    2 LRNGKKYFSGGPIFTIRLGGQKIYVITDPELISA-VFRNPKTLSFDPIVIVVVG--RVFGSpESAKKKEGEPGGKGLIRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 143 SFRYF------GYGQKSFESKILEETKFFTDAIETYKG---RPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIEL 213
Cdd:cd11040   79 LHDLHkkalsgGEGLDRLNEAMLENLSKLLDELSLSGGtstVEVDLYEWLRDVLTRATTEALFGPKLPELDPDLVEDFWT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 214 FSENVELaasasvFLYNaFPWIgilpfgkhqqLFRNASVVYDFLSRLIEKASVNRKPQLPQ----------HFVDAYFDE 283
Cdd:cd11040  159 FDRGLPK------LLLG-LPRL----------LARKAYAARDRLLKALEKYYQAAREERDDgselirarakVLREAGLSE 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 284 MDQGKNDPSstfskenlifsvgeLIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGP----NGKPSWDDKF-KM 358
Cdd:cd11040  222 EDIARAELA--------------LLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPdsgtNAILDLTDLLtSC 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 359 PYTEAVLHEVLRFCNIvPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLD---SSGYFAK 434
Cdd:cd11040  288 PLLDSTYLETLRLHSS-STSVRLVTEDTVLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKkdgDKKGRGL 366
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 302565346 435 KEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHfPHELVPDLKPRLGMTL 489
Cdd:cd11040  367 PGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVE-PVGGGDWKVPGMDESP 420
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
295-477 1.57e-23

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: 102.12  E-value: 1.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 295 FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpngkpswddkfkmpyteaVLHEVLRFCNI 374
Cdd:cd20630  199 LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEPELLRN------------------ALEEVLRWDNF 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 375 VPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaKKEALVPFSLGRRHCLGEQLA 454
Cdd:cd20630  261 GKMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR---------DPNANIAFGYGPHFCIGAALA 331
                        170       180
                 ....*....|....*....|...
gi 302565346 455 RMEMFLFFTALLQRFhlhFPHEL 477
Cdd:cd20630  332 RLELELAVSTLLRRF---PEMEL 351
PLN02936 PLN02936
epsilon-ring hydroxylase
292-488 1.86e-23

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 103.33  E-value: 1.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 292 SSTFSKENLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKFKMPYTEAVLHEVLRF 371
Cdd:PLN02936 275 SSVQLRDDLL----SMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMRL 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 372 CNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF-LD-------SSGYfakkeALVPFSL 443
Cdd:PLN02936 350 YPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdLDgpvpnetNTDF-----RYIPFSG 424
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 302565346 444 GRRHCLGEQLARMEMFLFFTALLQRFHLhfphELVPDLKprLGMT 488
Cdd:PLN02936 425 GPRKCVGDQFALLEAIVALAVLLQRLDL----ELVPDQD--IVMT 463
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
75-501 3.69e-23

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: 101.67  E-value: 3.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  75 EIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPclpLFMKMTKM-GGLLN---SRYGQGWVEHRRLAVN------SF 144
Cdd:cd20658    2 DIACIRLGNTHVIPVTCPKIAREILRKQDAVFASRP---LTYATEIIsGGYKTtviSPYGEQWKKMRKVLTTelmspkRH 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 145 RYFgYGQKSFESkileetkfftDAIETY---------KGRPFDFKQLITSAVSNITNLIIFGERFTYEDTD--------F 207
Cdd:cd20658   79 QWL-HGKRTEEA----------DNLVAYvynmckksnGGGLVNVRDAARHYCGNVIRKLMFGTRYFGKGMEdggpgleeV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 208 QHMIELFSE-NVELAASASVFLynafPWIGILPFGKHQQLFRNASVVYDFLSRLI--EKASVNR--KPQLPQHFVDAYFD 282
Cdd:cd20658  148 EHMDAIFTAlKCLYAFSISDYL----PFLRGLDLDGHEKIVREAMRIIRKYHDPIidERIKQWRegKKKEEEDWLDVFIT 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 283 EMDQGKNdpsSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTE 362
Cdd:cd20658  224 LKDENGN---PLLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVK 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 363 AVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEA---LV 439
Cdd:cd20658  301 ACAREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEVTLTEPdlrFI 380
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 302565346 440 PFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVP-DLKPRLGMTLQPQPYLICAERR 501
Cdd:cd20658  381 SFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTLPPNVSSvDLSESKDDLFMAKPLVLVAKPR 443
PLN02738 PLN02738
carotene beta-ring hydroxylase
276-488 5.62e-23

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 102.30  E-value: 5.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 276 FVDAYFDEMD--------QGKNDPSSTFSKENLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpN 347
Cdd:PLN02738 364 FHEEYMNERDpsilhfllASGDDVSSKQLRDDLM----TMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLG-D 438
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 348 GKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDaVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF-L 426
Cdd:PLN02738 439 RFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLEND-MLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpL 517
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 302565346 427 DSSGYFAKKE--ALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLhfphELVPDLKPrLGMT 488
Cdd:PLN02738 518 DGPNPNETNQnfSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDF----QLAPGAPP-VKMT 576
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
255-474 1.13e-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: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 255 DFLSRLIEKAsVNRKPQLPqhfVDAYFDEMDQGkndpssTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQG 334
Cdd:cd20615  181 AFNLKIYNRA-RQRGQSTP---IVKLYEAVEKG------DITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQE 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 335 QVQKEidlIMGPNGKPSWDDKFKMPYTEAVLH----EVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSV-HF 409
Cdd:cd20615  251 KLREE---ISAAREQSGYPMEDYILSTDTLLAycvlESLRLRPLLAFSVPESSPTDKIIGGYRIPANTPVVVDTYALnIN 327
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 302565346 410 DEKYWRDPEVFHPERFLDSSGYFAKKeALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFP 474
Cdd:cd20615  328 NPFWGPDGEAYRPERFLGISPTDLRY-NFWRFGFGPRKCLGQHVADVILKALLAHLLEQYELKLP 391
PLN00168 PLN00168
Cytochrome P450; Provisional
66-469 1.85e-22

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 100.41  E-value: 1.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  66 MRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKMTKMGGLL-NSRYGQGWVEHRRLAV--- 141
Cdd:PLN00168  63 LRRLIARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVASSRLLGESDNTItRSSYGPVWRLLRRNLVaet 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 142 ---NSFRYFGYGQKSFESKILEetKFFTDAIETYKGRPFDFKQLitsAVSNITNLIIFGERFtyeDTDFQHMIELFSENV 218
Cdd:PLN00168 143 lhpSRVRLFAPARAWVRRVLVD--KLRREAEDAAAPRVVETFQY---AMFCLLVLMCFGERL---DEPAVRAIAAAQRDW 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 219 ELAASASVFLYNAFPWIGILPF-GKHQQLFRNASVVYDFLSRLIEkASVNRKPQLPQH---------FVDAYFDEMDQGK 288
Cdd:PLN00168 215 LLYVSKKMSVFAFFPAVTKHLFrGRLQKALALRRRQKELFVPLID-ARREYKNHLGQGgeppkkettFEHSYVDTLLDIR 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 289 --NDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPN-GKPSWDDKFKMPYTEAVL 365
Cdd:PLN00168 294 lpEDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDqEEVSEEDVHKMPYLKAVV 373
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 366 HEVLRfcnIVPLGIF---HATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFL--------DSSGyfAK 434
Cdd:PLN00168 374 LEGLR---KHPPAHFvlpHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLaggdgegvDVTG--SR 448
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 302565346 435 KEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRF 469
Cdd:PLN00168 449 EIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREF 483
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
156-469 3.13e-22

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: 98.48  E-value: 3.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 156 SKILEETKFFTDAIETY--KGRPFDFKQLITSAVSNITNLIIFGERFtyedtDFQHMIELFSENVELAASASVFLYNAFP 233
Cdd:cd11051   78 PTILDEVEIFAAILRELaeSGEVFSLEELTTNLTFDVIGRVTLDIDL-----HAQTGDNSLLTALRLLLALYRSLLNPFK 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 234 WIGILpfgKHQQLFRNASVVYDFLSRLIEKAsvnrkpqlpqhfvdayfdemdqgkndpsstFSKENLIFSVGELIIAGTE 313
Cdd:cd11051  153 RLNPL---RPLRRWRNGRRLDRYLKPEVRKR------------------------------FELERAIDQIKTFLFAGHD 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 314 TTTNVLRWAilFMAL--YPNIQGQVQKEIDLIMGPNGKPSW------DDKF-KMPYTEAVLHEVLRfcnIVPLGI----- 379
Cdd:cd11051  200 TTSSTLCWA--FYLLskHPEVLAKVRAEHDEVFGPDPSAAAellregPELLnQLPYTTAVIKETLR---LFPPAGtarrg 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 380 ---FHATSEDavvrGYSIP-KGTTVITNLYSVHFDEKYWRDPEVFHPERFL--DSSGYFAKKEALVPFSLGRRHCLGEQL 453
Cdd:cd11051  275 ppgVGLTDRD----GKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLvdEGHELYPPKSAWRPFERGPRNCIGQEL 350
                        330
                 ....*....|....*.
gi 302565346 454 ARMEMFLFFTALLQRF 469
Cdd:cd11051  351 AMLELKIILAMTVRRF 366
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
62-472 2.47e-21

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 96.54  E-value: 2.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  62 PHVYMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFadRPCLPlfMKMTKMGGLLNSRYGQG--WVEHRRL 139
Cdd:PLN02196  57 PNVFFASKQKRYGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLF--KPTFP--ASKERMLGKQAIFFHQGdyHAKLRKL 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 140 AVNSFRyfgygQKSFESKILEETKFFTDAIETYKGRPFDFKQLITSAVSNITNLIIFGERFTYEDTDFQHMIELFSENve 219
Cdd:PLN02196 133 VLRAFM-----PDAIRNMVPDIESIAQESLNSWEGTQINTYQEMKTYTFNVALLSIFGKDEVLYREDLKRCYYILEKG-- 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 220 laasasvflYNAfpwigiLPFGKHQQLFRNASVVYDFLSRLIEKASVNRKpQLPQHFVD--AYFDEMDQGKNDpsstfsk 297
Cdd:PLN02196 206 ---------YNS------MPINLPGTLFHKSMKARKELAQILAKILSKRR-QNGSSHNDllGSFMGDKEGLTD------- 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 298 ENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKP---SWDDKFKMPYTEAVLHEVLRFCNI 374
Cdd:PLN02196 263 EQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGeslTWEDTKKMPLTSRVIQETLRVASI 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 375 VPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSsgyfAKKEALVPFSLGRRHCLGEQLA 454
Cdd:PLN02196 343 LSF-TFREAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVA----PKPNTFMPFGNGTHSCPGNELA 417
                        410
                 ....*....|....*...
gi 302565346 455 RMEMFLFFTALLQRFHLH 472
Cdd:PLN02196 418 KLEISVLIHHLTTKYRWS 435
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
65-492 3.58e-21

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: 95.81  E-value: 3.58e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  65 YMRKQSQVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSGiFADRPCLPLFMKMTKmgGLLNSRyGQGWVEHRRLAVNSF 144
Cdd:cd20642    3 FIHHTVKTYGKNSFTWFGPIPRVIIMDPELIKEVLNKVYD-FQKPKTNPLTKLLAT--GLASYE-GDKWAKHRKIINPAF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 145 RyfgygqksfeskiLEETK-----FFTDAIETYKgrpfDFKQLITSAVS----------NITNLII----FGErfTYEDT 205
Cdd:cd20642   79 H-------------LEKLKnmlpaFYLSCSEMIS----KWEKLVSSKGSceldvwpelqNLTSDVIsrtaFGS--SYEEG 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 206 dfQHMIELFSENVELAASASVFLYnaFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQH------FVDA 279
Cdd:cd20642  140 --KKIFELQKEQGELIIQALRKVY--IPGWRFLPTKRNRRMKEIEKEIRSSLRGIINKREKAMKAGEATNddllgiLLES 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 280 YFDEMDQGKNdPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKFKMP 359
Cdd:cd20642  216 NHKEIKEQGN-KNGGMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFG-NNKPDFEGLNHLK 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 360 YTEAVLHEVLRfcnIVPLGIF--HATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKE 436
Cdd:cd20642  294 VVTMILYEVLR---LYPPVIQltRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFAEGISKATKGQ 370
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 302565346 437 -ALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLhfphELVPDLK--PRLGMTLQPQ 492
Cdd:cd20642  371 vSYFPFGWGPRICIGQNFALLEAKMALALILQRFSF----ELSPSYVhaPYTVLTLQPQ 425
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
247-485 7.63e-21

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: 94.76  E-value: 7.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 247 FRNA-SVVYDFLSRLIEKasvnRKPQLPQHFVDAYFDEMDQGKN------------DPSSTFSKENLIFSVGELIIAGTE 313
Cdd:cd20679  183 FRRAcRLVHDFTDAVIQE----RRRTLPSQGVDDFLKAKAKSKTldfidvlllskdEDGKELSDEDIRAEADTFMFEGHD 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 314 TTTNVLRWAILFMALYPNIQGQVQKEI-DLIMGPNGKP-SWDDKFKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVR- 390
Cdd:cd20679  259 TTASGLSWILYNLARHPEYQERCRQEVqELLKDREPEEiEWDDLAQLPFLTMCIKESLRLHPPVTA-ISRCCTQDIVLPd 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 391 GYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFH 470
Cdd:cd20679  338 GRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFR 417
                        250
                 ....*....|....*
gi 302565346 471 LhFPHELVPDLKPRL 485
Cdd:cd20679  418 V-LPDDKEPRRKPEL 431
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
73-469 9.34e-21

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


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 94.91  E-value: 9.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  73 YGEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKmtKMGGLLNSRYGQGWVEHRRLAVNSFRyfGYGQK 152
Cdd:cd20649    2 YGPICGYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNRMKANLITK--PMSDSLLCLRDERWKRVRSILTPAFS--AAKMK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 153 SFESKILEETKFFTDAIETY--KGRPFDFKQLITSAVSNITNLIIFGERFTYE---DTDFQHMIELFSEnvELAASASVF 227
Cdd:cd20649   78 EMVPLINQACDVLLRNLKSYaeSGNAFNIQRCYGCFTMDVVASVAFGTQVDSQknpDDPFVKNCKRFFE--FSFFRPILI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 228 LYNAFPWI-----GILPFGKHQQLfrNAsvvydFLSRLIEKASVNRKPQLP--------QHFVDA----------YFD-- 282
Cdd:cd20649  156 LFLAFPFImiplaRILPNKSRDEL--NS-----FFTQCIRNMIAFRDQQSPeerrrdflQLMLDArtsakflsveHFDiv 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 283 -------------EMDQGKNDPSSTFSKENLIFSVGE---LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGP 346
Cdd:cd20649  229 ndadesaydghpnSPANEQTKPSKQKRMLTEDEIVGQafiFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSK 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 347 NGKPSWDDKFKMPYTEAVLHEVLRfcnIVPLGIFHA--TSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPER 424
Cdd:cd20649  309 HEMVDYANVQELPYLDMVIAETLR---MYPPAFRFAreAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPER 385
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 302565346 425 FLDSsgyfAKKE----ALVPFSLGRRHCLGEQLARMEMFLFFTALLQRF 469
Cdd:cd20649  386 FTAE----AKQRrhpfVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRF 430
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
298-492 3.55e-20

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: 92.86  E-value: 3.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 298 ENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIdlimGPNGKPSWDDKFKM----PYTEAVLHEVLRFcN 373
Cdd:cd20643  233 EDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEV----LAARQEAQGDMVKMlksvPLLKAAIKETLRL-H 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 374 IVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDS-SGYFAKkealVPFSLGRRHCLGEQ 452
Cdd:cd20643  308 PVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKdITHFRN----LGFGFGPRQCLGRR 383
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 302565346 453 LARMEMFLFFTALLQRFHLHFPHElvPDLKPRLGMTLQPQ 492
Cdd:cd20643  384 IAETEMQLFLIHMLENFKIETQRL--VEVKTTFDLILVPE 421
PLN02302 PLN02302
ent-kaurenoic acid oxidase
310-471 3.86e-20

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 93.24  E-value: 3.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 310 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMG---PNGKP-SWDDKFKMPYTEAVLHEVLRFCNIVPLgIFHATSE 385
Cdd:PLN02302 298 AGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKkrpPGQKGlTLKDVRKMEYLSQVIDETLRLINISLT-VFREAKT 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 386 DAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFldsSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTAL 465
Cdd:PLN02302 377 DVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRW---DNYTPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHF 453

                 ....*.
gi 302565346 466 LQRFHL 471
Cdd:PLN02302 454 LLGYRL 459
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
175-493 5.43e-20

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: 92.36  E-value: 5.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 175 RPFDFKQLITSAVSNITNLIIFGERFTYeDTDFQHMIELFSENVELAASASVFLYNAF-PWIG-ILPF-GKHQQLFRNA- 250
Cdd:cd11041  106 TEVNLYDTVLRIVARVSARVFVGPPLCR-NEEWLDLTINYTIDVFAAAAALRLFPPFLrPLVApFLPEpRRLRRLLRRAr 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 251 SVVYDFLSRLIEKASVNrKPQLPQHFVDAYfdeMDQGKNDPSSTFskENLIFSVGELIIAGTETTTNVLRWAILFMALYP 330
Cdd:cd11041  185 PLIIPEIERRRKLKKGP-KEDKPNDLLQWL---IEAAKGEGERTP--YDLADRQLALSFAAIHTTSMTLTHVLLDLAAHP 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 331 NIQGQVQKEIDLIMGPNGKpsWDDKF--KMPYTEAVLHEVLRFCNIVPLGIF-HATSEDAVVRGYSIPKGTTVITNLYSV 407
Cdd:cd11041  259 EYIEPLREEIRSVLAEHGG--WTKAAlnKLKKLDSFMKESQRLNPLSLVSLRrKVLKDVTLSDGLTLPKGTRIAVPAHAI 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 408 HFDEKYWRDPEVFHPERF--LDSSGYFAKKEALV-------PFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELV 478
Cdd:cd11041  337 HRDPDIYPDPETFDGFRFyrLREQPGQEKKHQFVstspdflGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGE 416
                        330
                 ....*....|....*
gi 302565346 479 PDLKPRLGMTLQPQP 493
Cdd:cd11041  417 RPKNIWFGEFIMPDP 431
PLN02290 PLN02290
cytokinin trans-hydroxylase
123-493 8.01e-20

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 92.18  E-value: 8.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 123 GLLNSRyGQGWVEHRRLAVNSFryFGYGQKSFESKILEETKFFTDAIETYKGRP---FDFKQLITSAVSNITNLIIFGER 199
Cdd:PLN02290 143 GLLMAN-GADWYHQRHIAAPAF--MGDRLKGYAGHMVECTKQMLQSLQKAVESGqteVEIGEYMTRLTADIISRTEFDSS 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 200 FTYEDTDFQHMIELFSenveLAASASVFLYnaFPWIGILPFGKHQQLFRNASVVYDFLSRLIEK----ASVNRKPQLPQH 275
Cdd:PLN02290 220 YEKGKQIFHLLTVLQR----LCAQATRHLC--FPGSRFFPSKYNREIKSLKGEVERLLMEIIQSrrdcVEIGRSSSYGDD 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 276 FVDAYFDEMDQGKNDPSSTfskeNLIFSVGE---LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNgKPSW 352
Cdd:PLN02290 294 LLGMLLNEMEKKRSNGFNL----NLQLIMDEcktFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGE-TPSV 368
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 353 DDKFKMPYTEAVLHEVLRF---CNIVPLGIFhatsEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFldS 428
Cdd:PLN02290 369 DHLSKLTLLNMVINESLRLyppATLLPRMAF----EDIKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRF--A 442
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302565346 429 SGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHE------LVPDLKPRLGMTLQPQP 493
Cdd:PLN02290 443 GRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDNyrhapvVVLTIKPKYGVQVCLKP 513
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
232-471 1.07e-19

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: 91.27  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 232 FPWIgilpFGKHQqlfRNASVVYDFLSRLIEKasvnRKPQLPQhfVDAYFDEMD--------QGKNDpsstFSKENLIFS 303
Cdd:cd20616  166 ISWL----YKKYE---KAVKDLKDAIEILIEQ----KRRRIST--AEKLEDHMDfatelifaQKRGE----LTAENVNQC 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 304 VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHAT 383
Cdd:cd20616  229 VLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKAL 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 384 SEDaVVRGYSIPKGTTVITNLYSVHFDEkYWRDPEVFHPERFLDS--SGYFAkkealvPFSLGRRHCLGEQLARMEMFLF 461
Cdd:cd20616  308 EDD-VIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFEKNvpSRYFQ------PFGFGPRSCVGKYIAMVMMKAI 379
                        250
                 ....*....|
gi 302565346 462 FTALLQRFHL 471
Cdd:cd20616  380 LVTLLRRFQV 389
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
307-485 4.01e-19

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: 88.81  E-value: 4.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 307 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgPNgkpswddkfkmpyteaVLHEVLRFCNIVPLgIFHATSED 386
Cdd:cd11032  206 LLIAGHETTTNLLGNAVLCLDEDPEVAARLRADPSLI--PG----------------AIEEVLRYRPPVQR-TARVTTED 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 387 AVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERflDSSGYFAkkealvpFSLGRRHCLGEQLARMEMFLFFTALL 466
Cdd:cd11032  267 VELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR--NPNPHLS-------FGHGIHFCLGAPLARLEARIALEALL 337
                        170       180
                 ....*....|....*....|
gi 302565346 467 QRfhlhFPH-ELVPDLKPRL 485
Cdd:cd11032  338 DR----FPRiRVDPDVPLEL 353
PLN02500 PLN02500
cytochrome P450 90B1
293-470 6.10e-18

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 86.46  E-value: 6.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 293 STFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKE---IDLIMGPNG--KPSWDDKFKMPYTEAVLHE 367
Cdd:PLN02500 273 SNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEhleIARAKKQSGesELNWEDYKKMEFTQCVINE 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 368 VLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLD-------SSGYFAKKEALVP 440
Cdd:PLN02500 353 TLRLGNVVRF-LHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQnnnrggsSGSSSATTNNFMP 431
                        170       180       190
                 ....*....|....*....|....*....|
gi 302565346 441 FSLGRRHCLGEQLARMEMFLFFTALLQRFH 470
Cdd:PLN02500 432 FGGGPRLCAGSELAKLEMAVFIHHLVLNFN 461
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
234-469 1.00e-17

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: 84.72  E-value: 1.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 234 WIGI---LPFGKHQQLFRNA-SVVYDFLSRLIEKASVNRKPQLPQHFVDAyFDEMDQgkndpsstFSKENLIFSVGELII 309
Cdd:cd11038  154 DLGLafgLEVKDHLPRIEAAvEELYDYADALIEARRAEPGDDLISTLVAA-EQDGDR--------LSDEELRNLIVALLF 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 310 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgpngkpswddkfkmpytEAVLHEVLRFCNIVPLGIFHATsEDAVV 389
Cdd:cd11038  225 AGVDTTRNQLGLAMLTFAEHPDQWRALREDPELA------------------PAAVEEVLRWCPTTTWATREAV-EDVEY 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 390 RGYSIPKGTTVITNLYSVHfdekywRDPEVFHPERFlDSSgyfAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRF 469
Cdd:cd11038  286 NGVTIPAGTVVHLCSHAAN------RDPRVFDADRF-DIT---AKRAPHLGFGGGVHHCLGAFLARAELAEALTVLARRL 355
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
259-469 3.55e-17

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 83.64  E-value: 3.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 259 RLIEKASVNRKPQLPQHFVDAYFDEmdqGKNDPSSTFSKENLIfsvgELIIAGTETTTNVLRWAILFMALYP-------- 330
Cdd:PLN03141 218 RRAMKNKEEDETGIPKDVVDVLLRD---GSDELTDDLISDNMI----DMMIPGEDSVPVLMTLAVKFLSDCPvalqqlte 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 331 -NIQGQVQKEIdlimgpNGKP-SWDDKFKMPYTEAVLHEVLRFCNIVpLGIFHATSEDAVVRGYSIPKGTTVITNLYSVH 408
Cdd:PLN03141 291 eNMKLKRLKAD------TGEPlYWTDYMSLPFTQNVITETLRMGNII-NGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVH 363
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 302565346 409 FDEKYWRDPEVFHPERFLDSSgyfAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRF 469
Cdd:PLN03141 364 LDEENYDNPYQFNPWRWQEKD---MNNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRF 421
PLN03018 PLN03018
homomethionine N-hydroxylase
61-501 6.15e-17

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 83.52  E-value: 6.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346  61 LPHVYMRKQSQVY---------GEIFSLDLGGISTVVLNGYDVVKECLVHQSGIFADRPCLPLFMKM----TKMGgllNS 127
Cdd:PLN03018  54 LPELIMTRPRSKYfhlamkelkTDIACFNFAGTHTITINSDEIAREAFRERDADLADRPQLSIMETIgdnyKSMG---TS 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 128 RYGQGWVEHRRLAVNSFRYFGYGQKSFESKILEETKFFTDAIETY-KGRPFDFKQLITSAVSNITNLIIFGERFTYEDTd 206
Cdd:PLN03018 131 PYGEQFMKMKKVITTEIMSVKTLNMLEAARTIEADNLIAYIHSMYqRSETVDVRELSRVYGYAVTMRMLFGRRHVTKEN- 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 207 fqhmieLFSENVELAASASVFLYNAFPWIGILPF-----------------GKHQQLFRNASVVYDFLSRLI-EKASVNR 268
Cdd:PLN03018 210 ------VFSDDGRLGKAEKHHLEVIFNTLNCLPGfspvdyverwlrgwnidGQEERAKVNVNLVRSYNNPIIdERVELWR 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 269 K---PQLPQHFVDAYFDEMDQGKNdpsSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMG 345
Cdd:PLN03018 284 EkggKAAVEDWLDTFITLKDQNGK---YLVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVG 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 346 PNGKPSWDDKFKMPYTEAVLHEVLRF---CNIVPLgifHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHP 422
Cdd:PLN03018 361 KDRLVQESDIPNLNYLKACCRETFRIhpsAHYVPP---HVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEP 437
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 423 ERFLDSSGyFAKKEALV-------PFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVP-DLKPRLGMTLQPQPY 494
Cdd:PLN03018 438 ERHLQGDG-ITKEVTLVetemrfvSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHQDFGPlSLEEDDASLLMAKPL 516

                 ....*..
gi 302565346 495 LICAERR 501
Cdd:PLN03018 517 LLSVEPR 523
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
290-487 1.38e-16

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: 81.46  E-value: 1.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 290 DPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgpngkpswddkfkmpytEAVLHEVL 369
Cdd:cd11031  197 DDDDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRADPELV------------------PAAVEELL 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 370 RFcniVPL----GIFHATSEDAVVRGYSIPKGTTVITNLYSVHfdekywRDPEVF-HPERFLdssgyFAKKEAL-VPFSL 443
Cdd:cd11031  259 RY---IPLgaggGFPRYATEDVELGGVTIRAGEAVLVSLNAAN------RDPEVFpDPDRLD-----LDREPNPhLAFGH 324
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 302565346 444 GRRHCLGEQLARMEMFLFFTALLQRF---HLHFPHElvpDLKPRLGM 487
Cdd:cd11031  325 GPHHCLGAPLARLELQVALGALLRRLpglRLAVPEE---ELRWREGL 368
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
274-480 1.50e-16

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: 81.52  E-value: 1.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 274 QHFVDAYFDEMDQGKNDPSStFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKP-SW 352
Cdd:cd11082  196 HEILEEIKEAEEEGEPPPPH-SSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEPPlTL 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 353 DDKFKMPYTEAVLHEVLRFCNIVPLgIFHATSEDAVV-RGYSIPKGTTVITNLYSVHFDEkyWRDPEVFHPERFLDSSG- 430
Cdd:cd11082  275 DLLEEMKYTRQVVKEVLRYRPPAPM-VPHIAKKDFPLtEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQe 351
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 302565346 431 -YFAKKEALVpFSLGRRHCLGEQLARMEMFLfFTALLQRfHLHFPHELVPD 480
Cdd:cd11082  352 dRKYKKNFLV-FGAGPHQCVGQEYAINHLML-FLALFST-LVDWKRHRTPG 399
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
306-492 1.81e-16

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: 81.43  E-value: 1.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 306 ELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRfcnIVPLGIF--HAT 383
Cdd:cd20644  239 ELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLR---LYPVGITvqRVP 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 384 SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYFAKKEALvPFSLGRRHCLGEQLARMEMFLFFT 463
Cdd:cd20644  316 SSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKHL-AFGFGMRQCLGRRLAEAEMLLLLM 394
                        170       180
                 ....*....|....*....|....*....
gi 302565346 464 ALLQRFHLHFPHElvPDLKPRLGMTLQPQ 492
Cdd:cd20644  395 HVLKNFLVETLSQ--EDIKTVYSFILRPE 421
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
269-467 2.60e-16

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: 81.01  E-value: 2.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 269 KPQLPQHFVDAY--FDEMDQGKNDPsstFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEID----L 342
Cdd:cd20638  201 REDTEQQCKDALqlLIEHSRRNGEP---LNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQekglL 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 343 IMGPNGKPSWDDKF--KMPYTEAVLHEVLRFCNIVPLGiFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVF 420
Cdd:cd20638  278 STKPNENKELSMEVleQLKYTGCVIKETLRLSPPVPGG-FRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEF 356
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 302565346 421 HPERFLDSSGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQ 467
Cdd:cd20638  357 NPDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELAR 403
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
295-470 6.74e-16

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: 79.18  E-value: 6.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 295 FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgpngkPSWddkfkmpyteavLHEVLRFCNI 374
Cdd:cd11078  205 LTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRADPSLI------PNA------------VEETLRYDSP 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 375 VPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVHfdekywRDPEVF-HPERF-LDSSGyfAKKeaLVPFSLGRRHCLGEQ 452
Cdd:cd11078  267 VQ-GLRRTATRDVEIGGVTIPAGARVLLLFGSAN------RDERVFpDPDRFdIDRPN--ARK--HLTFGHGIHFCLGAA 335
                        170
                 ....*....|....*...
gi 302565346 453 LARMEMFLFFTALLQRFH 470
Cdd:cd11078  336 LARMEARIALEELLRRLP 353
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
283-483 2.37e-15

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: 77.87  E-value: 2.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 283 EMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFkmPYTE 362
Cdd:cd20614  192 ALIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAAGDVPRTPAELRRF--PLAE 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 363 AVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDssgyfaKKEALVP-- 440
Cdd:cd20614  270 ALFRETLRLHPPVPF-VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLG------RDRAPNPve 342
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 302565346 441 ---FSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHELVPDLKP 483
Cdd:cd20614  343 llqFGGGPHFCLGYHVACVELVQFIVALARELGAAGIRPLLVGVLP 388
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
310-492 2.60e-15

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: 77.84  E-value: 2.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 310 AGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGpNGKPSWDDKFKMPYTEAVLHEVLRfcnIVPLGIFHA--TSEDA 387
Cdd:cd20640  241 AGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCK-GGPPDADSLSRMKTVTMVIQETLR---LYPPAAFVSreALRDM 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 388 VVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDS-SGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTAL 465
Cdd:cd20640  317 KLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGvAAACKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLI 396
                        170       180       190
                 ....*....|....*....|....*....|.
gi 302565346 466 LQRFHL----HFPHElvpdlkPRLGMTLQPQ 492
Cdd:cd20640  397 LSKFSFtlspEYQHS------PAFRLIVEPE 421
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
307-479 6.33e-15

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: 76.42  E-value: 6.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 307 LIIAGTETTTNVLRWAILFMALYPniqGQ---VQKEIDLImgpngkpswddkfkmpytEAVLHEVLRFCNIVPLGIFHAT 383
Cdd:cd11029  219 LLVAGHETTVNLIGNGVLALLTHP---DQlalLRADPELW------------------PAAVEELLRYDGPVALATLRFA 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 384 SEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERflDSSGYFAkkealvpFSLGRRHCLGEQLARMEMFLFFT 463
Cdd:cd11029  278 TEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR--DANGHLA-------FGHGIHYCLGAPLARLEAEIALG 348
                        170       180
                 ....*....|....*....|
gi 302565346 464 ALLQRF-HLHF---PHELVP 479
Cdd:cd11029  349 ALLTRFpDLRLavpPDELRW 368
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
254-469 1.10e-14

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 75.64  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 254 YDFLSRLIEkasvnRKPQLPQhfvDAYFDEM--DQGKNDPsstFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPN 331
Cdd:cd11030  172 RAYLDELVA-----RKRREPG---DDLLSRLvaEHGAPGE---LTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPE 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 332 IQGQVQKEIDLImgpngkPSWDDkfkmpyteavlhEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHfde 411
Cdd:cd11030  241 QLAALRADPSLV------PGAVE------------ELLRYLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLPAAN--- 299
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 302565346 412 kywRDPEVF-HPERF---LDSSGYFAkkealvpFSLGRRHCLGEQLARMEMFLFFTALLQRF 469
Cdd:cd11030  300 ---RDPAVFpDPDRLditRPARRHLA-------FGHGVHQCLGQNLARLELEIALPTLFRRF 351
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
307-469 3.74e-14

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: 73.87  E-value: 3.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 307 LIIAGTETTTNVLrwAILFMAL--YPNIQGQVQKEIDLImgpngkpswddkfkmpytEAVLHEVLRFCNIVpLGIFHATS 384
Cdd:cd20629  200 LLPAGSDTTYRAL--ANLLTLLlqHPEQLERVRRDRSLI------------------PAAIEEGLRWEPPV-ASVPRMAL 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 385 EDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfAKKEALVpFSLGRRHCLGEQLARMEMFLFFTA 464
Cdd:cd20629  259 RDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR--------KPKPHLV-FGGGAHRCLGEHLARVELREALNA 329

                 ....*
gi 302565346 465 LLQRF 469
Cdd:cd20629  330 LLDRL 334
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
308-472 1.08e-13

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 73.19  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 308 IIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMGPNGKPSWDDKFK-MPYTEAVLHEVLRFCNIVPLGIFHATSED 386
Cdd:PLN02426 302 LLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNQEAASFEEMKeMHYLHAALYESMRLFPPVQFDSKFAAEDD 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 387 AVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKEALVP-FSLGRRHCLGEQLARMEMFLFFTA 464
Cdd:PLN02426 382 VLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGVFVPENPFKYPvFQAGLRVCLGKEMALMEMKSVAVA 461

                 ....*...
gi 302565346 465 LLQRFHLH 472
Cdd:PLN02426 462 VVRRFDIE 469
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
321-472 1.24e-13

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: 72.73  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 321 WAILFMALYPNIQGQVQKEIDLIMGPNGKPSW----DDKFKMPYTEAVLHEVLRFCNivPLGIFHATSEDAVVRGYSIPK 396
Cdd:cd20635  232 WTLAFILSHPSVYKKVMEEISSVLGKAGKDKIkiseDDLKKMPYIKRCVLEAIRLRS--PGAITRKVVKPIKIKNYTIPA 309
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 302565346 397 GTTVITNLYSVHFDEKYWRDPEVFHPERFLDSS-GYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLH 472
Cdd:cd20635  310 GDMLMLSPYWAHRNPKYFPDPELFKPERWKKADlEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFT 386
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
305-468 1.58e-13

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: 72.18  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 305 GELI---IAGTETTtNVLR------WAILFMAL----YPNIQGQVQKEIDlimgpngkpswddkfkmPYTEAVLHEVLRF 371
Cdd:cd11067  214 GELLperVAAVELL-NLLRptvavaRFVTFAALalheHPEWRERLRSGDE-----------------DYAEAFVQEVRRF 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 372 CNIVPL--GIfhaTSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGYfakKEALVP-----FSLG 444
Cdd:cd11067  276 YPFFPFvgAR---ARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGD---PFDFIPqgggdHATG 349
                        170       180
                 ....*....|....*....|....*..
gi 302565346 445 RRhCLGEQL--ARMEMFL-FFTALLQR 468
Cdd:cd11067  350 HR-CPGEWItiALMKEALrLLARRDYY 375
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
307-469 1.73e-13

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: 71.81  E-value: 1.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 307 LIIAGTETTTNVLRWAILFMALYPniqGQVQKeidLIMGPngkpswddkfkmPYTEAVLHEVLRFCNIVPLGIFHATsED 386
Cdd:cd20625  209 LLVAGHETTVNLIGNGLLALLRHP---EQLAL---LRADP------------ELIPAAVEELLRYDSPVQLTARVAL-ED 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 387 AVVRGYSIPKGTTVITNLYSVHfdekywRDPEVF-HPERF-LDSSGyfakkEALVPFSLGRRHCLGEQLARMEMFLFFTA 464
Cdd:cd20625  270 VEIGGQTIPAGDRVLLLLGAAN------RDPAVFpDPDRFdITRAP-----NRHLAFGAGIHFCLGAPLARLEAEIALRA 338

                 ....*
gi 302565346 465 LLQRF 469
Cdd:cd20625  339 LLRRF 343
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
241-489 3.07e-13

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 71.73  E-value: 3.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 241 GKHQQLFRNASVVYDFLSRLI-----EKASVNRKPQLPQHFVDAYFDEMDQgknDPSSTFSKENLIFSVGELIIAGTETT 315
Cdd:PLN03195 232 GSEALLSKSIKVVDDFTYSVIrrrkaEMDEARKSGKKVKHDILSRFIELGE---DPDSNFTDKSLRDIVLNFVIAGRDTT 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 316 TNVLRWAILFMALYPNIQGQVQKEIDLI-------MGPNGKPS-------------WDDKFKMPYTEAVLHEVLRFCNIV 375
Cdd:PLN03195 309 ATTLSWFVYMIMMNPHVAEKLYSELKALekerakeEDPEDSQSfnqrvtqfaglltYDSLGKLQYLHAVITETLRLYPAV 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 376 PLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLdSSGYF--AKKEALVPFSLGRRHCLGEQ 452
Cdd:PLN03195 389 PQDPKGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWI-KDGVFqnASPFKFTAFQAGPRICLGKD 467
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 302565346 453 LARMEMFLfFTALLQRFhlhFPHELVP--DLKPRLGMTL 489
Cdd:PLN03195 468 SAYLQMKM-ALALLCRF---FKFQLVPghPVKYRMMTIL 502
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
257-472 5.08e-12

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: 67.54  E-value: 5.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 257 LSRLIEKASVNRKPQLPQHFVdaYFDEMDQGkNDPSSTFSKENLIFSvgeliIAGTETTTNVLRWAILFMALYPNIQGQV 336
Cdd:cd20627  168 MESVLKKVIKERKGKNFSQHV--FIDSLLQG-NLSEQQVLEDSMIFS-----LAGCVITANLCTWAIYFLTTSEEVQKKL 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 337 QKEIDLIMGpNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRgYSIPKGTTVITNLYSVHFDEKYWRD 416
Cdd:cd20627  240 YKEVDQVLG-KGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQ-HIIPKETLVLYALGVVLQDNTTWPL 317
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 302565346 417 PEVFHPERFLDSSgyFAKKEALVPFSlGRRHCLGEQLARMEMFLFFTALLQRFHLH 472
Cdd:cd20627  318 PYRFDPDRFDDES--VMKSFSLLGFS-GSQECPELRFAYMVATVLLSVLVRKLRLL 370
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
307-469 7.73e-12

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: 66.78  E-value: 7.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 307 LIIAGTETTTNVLRWAILFMALYPniqGQVQKeidLIMGPNGKPSwddkfkmpyteAVlHEVLRFcnIVPLGIF--HATs 384
Cdd:cd11033  217 LAVAGNETTRNSISGGVLALAEHP---DQWER---LRADPSLLPT-----------AV-EEILRW--ASPVIHFrrTAT- 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 385 EDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaKKEALVPFSLGRRHCLGEQLARMEMFLFFTA 464
Cdd:cd11033  276 RDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR---------SPNPHLAFGGGPHFCLGAHLARLELRVLFEE 346

                 ....*
gi 302565346 465 LLQRF 469
Cdd:cd11033  347 LLDRV 351
PLN02774 PLN02774
brassinosteroid-6-oxidase
296-469 1.70e-11

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 66.34  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 296 SKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKE---IDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFC 372
Cdd:PLN02774 261 TDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEhlaIRERKRPEDPIDWNDYKSMRFTRAVIFETSRLA 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 373 NIVPlGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSgyFAKKEALVPFSLGRRHCLGEQ 452
Cdd:PLN02774 341 TIVN-GVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKS--LESHNYFFLFGGGTRLCPGKE 417
                        170
                 ....*....|....*..
gi 302565346 453 LARMEMFLFFTALLQRF 469
Cdd:PLN02774 418 LGIVEISTFLHYFVTRY 434
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
295-458 5.76e-11

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: 64.03  E-value: 5.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 295 FSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgpngkpswddkfkmpytEAVLHEVLRFCNI 374
Cdd:cd11080  189 LSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRADRSLV------------------PRAIAETLRYHPP 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 375 VPLgIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF-LDSSGYFAKKEALVPFSLGRRHCLGEQL 453
Cdd:cd11080  251 VQL-IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREdLGIRSAFSGAADHLAFGSGRHFCVGAAL 329

                 ....*
gi 302565346 454 ARMEM 458
Cdd:cd11080  330 AKREI 334
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
219-455 6.26e-11

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: 64.47  E-value: 6.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 219 ELAASASVFLYNAFPWIGILPFGKHQQLFRNASVVYDFLSRLIEKASVNRKPQLPQHFVDAYFDEMDQGKNDPSSTFSKE 298
Cdd:cd20636  151 YLAKTFEQLVENLFSLPLDVPFSGLRKGIKARDILHEYMEKAIEEKLQRQQAAEYCDALDYMIHSARENGKELTMQELKE 230
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 299 NLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEID---LIMGPNGKP---SWDDKFKMPYTEAVLHEVLRFC 372
Cdd:cd20636  231 SAV----ELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVshgLIDQCQCCPgalSLEKLSRLRYLDCVVKEVLRLL 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 373 NIVPLGIFHA--TSEdavVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF-----LDSSGYFakkeALVPFSLGR 445
Cdd:cd20636  307 PPVSGGYRTAlqTFE---LDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFgvereESKSGRF----NYIPFGGGV 379
                        250
                 ....*....|
gi 302565346 446 RHCLGEQLAR 455
Cdd:cd20636  380 RSCIGKELAQ 389
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
299-470 2.19e-10

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: 62.66  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 299 NLIFSVGeliIAGTETTTNVLRWAILFMALY-PNIQGQVQKEIDLIMGPNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPL 377
Cdd:cd11071  228 NLLFMLG---FNAFGGFSALLPSLLARLGLAgEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPL 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 378 gIFHATSEDAVV----RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGyfaKKEALVPFSLGR-------- 445
Cdd:cd11071  305 -QYGRARKDFVIeshdASYKIKKGELLVGYQPLATRDPKVFDNPDEFVPDRFMGEEG---KLLKHLIWSNGPeteeptpd 380
                        170       180
                 ....*....|....*....|....*.
gi 302565346 446 -RHCLGEQLARMEMFLFFTALLQRFH 470
Cdd:cd11071  381 nKQCPGKDLVVLLARLFVAELFLRYD 406
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
318-494 2.71e-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: 62.09  E-value: 2.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 318 VLRwAILFMALYPNIQGQVQKEIdliMGPNGKPSWddkfkmPYTEAVLHEVLRFCNIVPLgIFHATSEDAVVRGYSIPKG 397
Cdd:cd20624  211 LLR-ALALLAAHPEQAARAREEA---AVPPGPLAR------PYLRACVLDAVRLWPTTPA-VLRESTEDTVWGGRTVPAG 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 398 TTVITnlysvhFDEKYWRDPEV------FHPERFLDssGYFAKKEALVPFSLGRRHCLGEQLARMEMFLFFTALLQRfhl 471
Cdd:cd20624  280 TGFLI------FAPFFHRDDEAlpfadrFVPEIWLD--GRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRR--- 348
                        170       180
                 ....*....|....*....|...
gi 302565346 472 hfpHELVPDLKPRLGmTLQPQPY 494
Cdd:cd20624  349 ---AEIDPLESPRSG-PGEPLPG 367
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
200-490 5.49e-10

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: 61.40  E-value: 5.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 200 FTYEDTDFQHMIELFSENVElaasasvflyNAFPWIGILPFGKHQQLFRnasvVYDFLSRLIEKAsVNRKPQLPQ--HFV 277
Cdd:cd20637  141 FRVSEEELSHLFSVFQQFVE----------NVFSLPLDLPFSGYRRGIR----ARDSLQKSLEKA-IREKLQGTQgkDYA 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 278 DAyFDEMDQGKNDPSSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEID----LIMGP--NGKPS 351
Cdd:cd20637  206 DA-LDILIESAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELRsngiLHNGClcEGTLR 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 352 WDDKFKMPYTEAVLHEVLRFCNIVPLGiFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERF-----L 426
Cdd:cd20637  285 LDTISSLKYLDCVIKEVLRLFTPVSGG-YRTALQTFELDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFgqersE 363
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 427 DSSGYFakkeALVPFSLGRRHCLGEQLARMEMFLFFTAL--LQRFHLH---FPH-ELVPDLKPRLGMTLQ 490
Cdd:cd20637  364 DKDGRF----HYLPFGGGVRTCLGKQLAKLFLKVLAVELasTSRFELAtrtFPRmTTVPVVHPVDGLRVK 429
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
304-468 6.49e-10

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: 60.67  E-value: 6.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 304 VGELIIAGTETTTNVLRWAILFMALYPNiQGQVQKEidlimgpngKPSwddkfKMPyteAVLHEVLRFCNivPLGIFH-A 382
Cdd:cd11037  207 MRDYLSAGLDTTISAIGNALWLLARHPD-QWERLRA---------DPS-----LAP---NAFEEAVRLES--PVQTFSrT 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 383 TSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERflDSSGYfakkealVPFSLGRRHCLGEQLARMEMFLFF 462
Cdd:cd11037  267 TTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR--NPSGH-------VGFGHGVHACVGQHLARLEGEALL 337

                 ....*.
gi 302565346 463 TALLQR 468
Cdd:cd11037  338 TALARR 343
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
226-458 9.62e-10

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 60.79  E-value: 9.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 226 VFLYNAFPWIGIlpfGKHQQLFRNASVVYDFLSRLI---EKASVNRKPQLPQHfVDA--YFDEMDQGKND---PSSTFSK 297
Cdd:PLN02169 227 VILWRLQNWIGI---GLERKMRTALATVNRMFAKIIssrRKEEISRAETEPYS-KDAltYYMNVDTSKYKllkPKKDKFI 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 298 ENLIFSvgeLIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIdlimgpNGKPSWDDKFKMPYTEAVLHEVLRFCNIVPL 377
Cdd:PLN02169 303 RDVIFS---LVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI------NTKFDNEDLEKLVYLHAALSESMRLYPPLPF 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 378 GIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYW-RDPEVFHPERFLDSSGYFAKKEA--LVPFSLGRRHCLGEQLA 454
Cdd:PLN02169 374 NHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGLRHEPSykFMAFNSGPRTCLGKHLA 453

                 ....
gi 302565346 455 RMEM 458
Cdd:PLN02169 454 LLQM 457
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
151-468 8.59e-08

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: 54.27  E-value: 8.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 151 QKSFESKILEETKFFTDAIETYKGRPF-----------DFKQL-ITSAVSNITNLIIFGERFTYEDTDFQHMIELFSEnv 218
Cdd:cd20612   62 QRELMRKALYSPDLAKDVVFFYELQTRallvessrlggSGGQVdIVRDVANLVPARFCADLFGLPLKTKENPRGGYTE-- 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 219 elaASASVFLYNAFPWI-GILPFGKHQQLFRNASVVYDFLSRLIEKASVNRkpqlpqhfvdayfdemdqgkndpssTFSk 297
Cdd:cd20612  140 ---AELYRALAAIFAYIfFDLDPAKSFQLRRAAQAAAARLGALLDAAVADE-------------------------VRD- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 298 eNLIFsvgeLIIAGTETTTNVLRWAILFMALYPNiqgqvQKEIDLIMGPNGKPSWDDKFKMPYteaVLhEVLRFCNIVPl 377
Cdd:cd20612  191 -NVLG----TAVGGVPTQSQAFAQILDFYLRRPG-----AAHLAEIQALARENDEADATLRGY---VL-EALRLNPIAP- 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 378 GIFHATSEDAVV-----RGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSsgYFAkkealvpFSLGRRHCLGEQ 452
Cdd:cd20612  256 GLYRRATTDTTVadgggRTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDRPLES--YIH-------FGHGPHQCLGEE 326
                        330
                 ....*....|....*.
gi 302565346 453 LARMEMFLFFTALLQR 468
Cdd:cd20612  327 IARAALTEMLRVVLRL 342
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
307-469 5.93e-07

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: 51.57  E-value: 5.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 307 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLImgpngkpswddkfkmpyTEAVlHEVLRFCNIVpLGIFHATSED 386
Cdd:cd11034  198 LLLGGTDTTSSALSGALLWLAQHPEDRRRLIADPSLI-----------------PNAV-EEFLRFYSPV-AGLARTVTQE 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 387 AVVRGYSIPKGTTVITNLYSVHfdekywRDPEVF-HPERF-LDSsgyFAKKEalVPFSLGRRHCLGEQLARMEMFLFFTA 464
Cdd:cd11034  259 VEVGGCRLKPGDRVLLAFASAN------RDEEKFeDPDRIdIDR---TPNRH--LAFGSGVHRCLGSHLARVEARVALTE 327

                 ....*
gi 302565346 465 LLQRF 469
Cdd:cd11034  328 VLKRI 332
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
321-491 1.53e-06

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: 50.38  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 321 WAILFMALYPNIQGQVQKEIDLIMGPNGK---PSWDDKF------KMPYTEAVLHEVLRFC----NI-VPLGIFHATSED 386
Cdd:cd20632  237 WAMYYLLRHPEALAAVRDEIDHVLQSTGQelgPDFDIHLtreqldSLVYLESAINESLRLSsasmNIrVVQEDFTLKLES 316
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 387 AvvRGYSIPKGTTVItnLY--SVHFDEKYWRDPEVFHPERFLDSSG---YFAK-----KEALVPFSLGRRHCLGEQLARM 456
Cdd:cd20632  317 D--GSVNLRKGDIVA--LYpqSLHMDPEIYEDPEVFKFDRFVEDGKkktTFYKrgqklKYYLMPFGSGSSKCPGRFFAVN 392
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 302565346 457 EMFLFFTALLqrfhLHFPHELVPDLKP------RLGMTLQP 491
Cdd:cd20632  393 EIKQFLSLLL----LYFDLELLEEQKPpgldnsRAGLGILP 429
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
307-488 1.63e-06

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: 50.28  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 307 LIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLIMgpngkpswddkfkmpyteAVLHEVLRFCNIVPLGifHATSED 386
Cdd:cd11035  198 LFLAGLDTVASALGFIFRHLARHPEDRRRLREDPELIP------------------AAVEELLRRYPLVNVA--RIVTRD 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 387 AVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaKKEALVPFSLGRRHCLGEQLARMEMFLFftalL 466
Cdd:cd11035  258 VEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR---------KPNRHLAFGAGPHRCLGSHLARLELRIA----L 324
                        170       180
                 ....*....|....*....|...
gi 302565346 467 QRFHLHFPH-ELVPDLKPRLGMT 488
Cdd:cd11035  325 EEWLKRIPDfRLAPGAQPTYHGG 347
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
363-469 7.96e-06

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: 47.87  E-value: 7.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 363 AVLHEVLRFCNIVplgifHATS----EDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERFLDSSGyfakkeal 438
Cdd:cd11036  223 AAVAETLRYDPPV-----RLERrfaaEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGRPTARSA-------- 289
                         90       100       110
                 ....*....|....*....|....*....|.
gi 302565346 439 vPFSLGRRHCLGEQLARMEMFLFFTALLQRF 469
Cdd:cd11036  290 -HFGLGRHACLGAALARAAAAAALRALAARF 319
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
321-491 1.37e-05

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: 47.37  E-value: 1.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 321 WAILFMALYPNIQGQVQKEIDLIMGPNG-KPSWDDKF---------KMPYTEAVLHEVLRFCNiVPLGIFHATSEDAVV- 389
Cdd:cd20631  249 WSLFYLLRCPEAMKAATKEVKRTLEKTGqKVSDGGNPivltreqldDMPVLGSIIKEALRLSS-ASLNIRVAKEDFTLHl 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 390 ---RGYSIPKGTTVItnLYS--VHFDEKYWRDPEVFHPERFLDSSG----YFAK-----KEALVPFSLGRRHCLGEQLAR 455
Cdd:cd20631  328 dsgESYAIRKDDIIA--LYPqlLHLDPEIYEDPLTFKYDRYLDENGkektTFYKngrklKYYYMPFGSGTSKCPGRFFAI 405
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 302565346 456 MEMFLFFTALLQRF--HLHFPHELVPDL-KPRLGM-TLQP 491
Cdd:cd20631  406 NEIKQFLSLMLCYFdmELLDGNAKCPPLdQSRAGLgILPP 445
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
362-468 8.78e-05

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: 44.65  E-value: 8.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 362 EAVLHEVLR-------FCNIvplgifhaTSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHPERfldssgyfaK 434
Cdd:cd11079  228 PAAIDEILRlddpfvaNRRI--------TTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR---------H 290
                         90       100       110
                 ....*....|....*....|....*....|....
gi 302565346 435 KEALVPFSLGRRHCLGEQLARMEMFLFFTALLQR 468
Cdd:cd11079  291 AADNLVYGRGIHVCPGAPLARLELRILLEELLAQ 324
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
321-492 1.44e-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: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 321 WAILFMALYPNIQGQVQKEIDLIMGPNGKP-------SWDDKFKMPYTEAVLHEVLRFcNIVPLgIFHATSEDAVV---- 389
Cdd:cd20634  243 WLLLFLLKHPEAMAAVRGEIQRIKHQRGQPvsqtltiNQELLDNTPVFDSVLSETLRL-TAAPF-ITREVLQDMKLrlad 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 390 -RGYSIPKGTTVITNLY-SVHFDEKYWRDPEVFHPERFLDSSGY----FAKKEALV-----PFSLGRRHCLGEQLARMEM 458
Cdd:cd20634  321 gQEYNLRRGDRLCLFPFlSPQMDPEIHQEPEVFKYDRFLNADGTekkdFYKNGKRLkyynmPWGAGDNVCIGRHFAVNSI 400
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 302565346 459 FLFFTALLQRFHLHF--PHELVPDLKP-RLGM-TLQPQ 492
Cdd:cd20634  401 KQFVFLILTHFDVELkdPEAEIPEFDPsRYGFgLLQPE 438
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
321-491 1.50e-04

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: 44.28  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 321 WAILFMALYPNIQGQVQKEIDLIMGPNGK------PSWDDKFKM----PYTEAVLHEVLRFcNIVPLgIFHATSEDAVV- 389
Cdd:cd20633  246 WLLLYLLKHPEAMKAVREEVEQVLKETGQevkpggPLINLTRDMllktPVLDSAVEETLRL-TAAPV-LIRAVVQDMTLk 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 390 ----RGYSIPKGTTVITNLY-SVHFDEKYWRDPEVFHPERFLDSSGYFAK---------KEALVPFSLGRRHCLGEQLAR 455
Cdd:cd20633  324 mangREYALRKGDRLALFPYlAVQMDPEIHPEPHTFKYDRFLNPDGGKKKdfykngkklKYYNMPWGAGVSICPGRFFAV 403
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 302565346 456 MEMFLFFTALLQRFHLHF--PHELVPDLKP-RLGM-TLQP 491
Cdd:cd20633  404 NEMKQFVFLMLTYFDLELvnPDEEIPSIDPsRWGFgTMQP 443
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
367-458 1.57e-03

P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Agrobacterium tumefaciens P450-pinF2, whose expression is induced by the presence of wounded plant tissue and by plant phenolic compounds such as acetosyringone. P450-pinF2 may be involved in the detoxification of plant protective agents at the site of wounding. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 40.95  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302565346 367 EVLRFcnIVPLGIF-HATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWRDPEVFHperfldssgYFAKKEALVPFSLGR 445
Cdd:cd11039  252 EGLRW--ISPIGMSpRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFD---------VFRPKSPHVSFGAGP 320
                         90
                 ....*....|...
gi 302565346 446 RHCLGEQLARMEM 458
Cdd:cd11039  321 HFCAGAWASRQMV 333
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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