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Conserved domains on  [gi|15231052|ref|NP_188648|]
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cytochrome P450, family 705, subfamily A, polypeptide 22 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
75-505 0e+00

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: 789.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQEQ 154
Cdd:cd20655   1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 155 SRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMFLAVLlR 234
Cdd:cd20655  81 FRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEAEEVRKLVKESAELAGKFNASDF-I 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 235 RQLQKLGISLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQG---TVMLDVLLAAYGDENAEYKITKNHIKAFFVDLFIG 311
Cdd:cd20655 160 WPLKKLDLQGFGKRIMDVSNRFDELLERIIKEHEEKRKKRKEggsKDLLDILLDAYEDENAEYKITRNHIKAFILDLFIA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 312 ATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGG 391
Cdd:cd20655 240 GTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKING 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 392 FYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMM 471
Cdd:cd20655 320 YDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQELDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTAIAAM 399
                       410       420       430
                ....*....|....*....|....*....|....*
gi 15231052 472 VQCFDWR-IEGEKVNMKEAVkGTILTMAHPLKLTP 505
Cdd:cd20655 400 VQCFDWKvGDGEKVNMEEAS-GLTLPRAHPLKCVP 433
 
Name Accession Description Interval E-value
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
75-505 0e+00

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: 789.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQEQ 154
Cdd:cd20655   1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 155 SRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMFLAVLlR 234
Cdd:cd20655  81 FRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEAEEVRKLVKESAELAGKFNASDF-I 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 235 RQLQKLGISLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQG---TVMLDVLLAAYGDENAEYKITKNHIKAFFVDLFIG 311
Cdd:cd20655 160 WPLKKLDLQGFGKRIMDVSNRFDELLERIIKEHEEKRKKRKEggsKDLLDILLDAYEDENAEYKITRNHIKAFILDLFIA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 312 ATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGG 391
Cdd:cd20655 240 GTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKING 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 392 FYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMM 471
Cdd:cd20655 320 YDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQELDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTAIAAM 399
                       410       420       430
                ....*....|....*....|....*....|....*
gi 15231052 472 VQCFDWR-IEGEKVNMKEAVkGTILTMAHPLKLTP 505
Cdd:cd20655 400 VQCFDWKvGDGEKVNMEEAS-GLTLPRAHPLKCVP 433
PLN02687 PLN02687
flavonoid 3'-monooxygenase
59-511 9.66e-98

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 305.20  E-value: 9.66e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   59 LSTLTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFM 138
Cdd:PLN02687  51 LGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRAL 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  139 KKLTVMKLLGPQAQEQSRDIRADDIKRFCRNLLDKARKKeSVEIGKEAMNLMNNILCKMSMGRS-FSEENGE-TEKLRGL 216
Cdd:PLN02687 131 RKICAVHLFSAKALDDFRHVREEEVALLVRELARQHGTA-PVNLGQLVNVCTTNALGRAMVGRRvFAGDGDEkAREFKEM 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  217 VTESIGLMKKM----FLAVLLRRQLQKLgISLFKKdimgVSNKFDVLLEKVLVEHR--EKPEKDQGTVMLDVLLAAYGDE 290
Cdd:PLN02687 210 VVELMQLAGVFnvgdFVPALRWLDLQGV-VGKMKR----LHRRFDAMMNGIIEEHKaaGQTGSEEHKDLLSTLLALKREQ 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  291 NA---EYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIK 367
Cdd:PLN02687 285 QAdgeGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIK 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  368 EALRLHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERREQaLKFLP 446
Cdd:PLN02687 365 ETFRLHPSTPLsLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPGGEHAGVDVKGSD-FELIP 443
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231052  447 FGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEG----EKVNMKEAVkGTILTMAHPLKLTPVTRQPP 511
Cdd:PLN02687 444 FGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADgqtpDKLNMEEAY-GLTLQRAVPLMVHPRPRLLP 511
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
64-488 7.22e-81

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: 259.52  E-value: 7.22e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052    64 HKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTA-VDESLVFGSSSFVTAPYGDYWKFMKKLT 142
Cdd:pfam00067  23 HSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPwFATSRGPFLGKGIVFANGPRWRQLRRFL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   143 VMKLLGPQAQEQsRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSF-SEENGETEKLRGLVTESI 221
Cdd:pfam00067 103 TPTFTSFGKLSF-EPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERFgSLEDPKFLELVKAVQELS 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   222 GLMKKMFLAVLLR-RQLQKLGISLFKKdIMGVSNKFDVLLEKVLVEHREKPEKDQGTVM--LDVLLAAYGDENAEyKITK 298
Cdd:pfam00067 182 SLLSSPSPQLLDLfPILKYFPGPHGRK-LKRARKKIKDLLDKLIEERRETLDSAKKSPRdfLDALLLAKEEEDGS-KLTD 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   299 NHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGP- 377
Cdd:pfam00067 260 EELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPl 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   378 LLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERreqalkFLPFGSGRRGCPGS 457
Cdd:pfam00067 340 LLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFA------FLPFGAGPRNCLGE 413
                         410       420       430
                  ....*....|....*....|....*....|..
gi 15231052   458 NLAYMIVGSAIGMMVQCFDWRI-EGEKVNMKE 488
Cdd:pfam00067 414 RLARMEMKLFLATLLQNFEVELpPGTDPPDID 445
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
73-482 2.74e-42

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: 155.44  E-value: 2.74e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  73 RYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTApYGDYWKFMKKLtVMKLLGPQAQ 152
Cdd:COG2124  30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTL-DGPEHTRLRRL-VQPAFTPRRV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 153 EQSRDIraddIKRFCRNLLDKARKKESVEIGKE-AMNLMNNILCKMsmgrsFSEENGETEKLRGLVTESIGLMKKMFLAV 231
Cdd:COG2124 108 AALRPR----IREIADELLDRLAARGPVDLVEEfARPLPVIVICEL-----LGVPEEDRDRLRRWSDALLDALGPLPPER 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 232 LLRRQlqklgislfkkdimGVSNKFDVLLEKVLVEHREKPEKDqgtvMLDVLLAAYGDENaeyKITKNHIKAFFVDLFIG 311
Cdd:COG2124 179 RRRAR--------------RARAELDAYLRELIAERRAEPGDD----LLSALLAARDDGE---RLSDEELRDELLLLLLA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 312 ATDTSVQTIQWTMAEIMNNTHILERMREEidsvvgksrliqetdlpnLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGG 391
Cdd:COG2124 238 GHETTANALAWALYALLRHPEQLARLRAE------------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGG 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 392 FYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERflassrsgqederreQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMM 471
Cdd:COG2124 300 VTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------------PPNAHLPFGGGPHRCLGAALARLEARIALATL 364
                       410
                ....*....|..
gi 15231052 472 VQCF-DWRIEGE 482
Cdd:COG2124 365 LRRFpDLRLAPP 376
 
Name Accession Description Interval E-value
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
75-505 0e+00

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: 789.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQEQ 154
Cdd:cd20655   1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 155 SRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMFLAVLlR 234
Cdd:cd20655  81 FRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEAEEVRKLVKESAELAGKFNASDF-I 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 235 RQLQKLGISLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQG---TVMLDVLLAAYGDENAEYKITKNHIKAFFVDLFIG 311
Cdd:cd20655 160 WPLKKLDLQGFGKRIMDVSNRFDELLERIIKEHEEKRKKRKEggsKDLLDILLDAYEDENAEYKITRNHIKAFILDLFIA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 312 ATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGG 391
Cdd:cd20655 240 GTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKING 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 392 FYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMM 471
Cdd:cd20655 320 YDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQELDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTAIAAM 399
                       410       420       430
                ....*....|....*....|....*....|....*
gi 15231052 472 VQCFDWR-IEGEKVNMKEAVkGTILTMAHPLKLTP 505
Cdd:cd20655 400 VQCFDWKvGDGEKVNMEEAS-GLTLPRAHPLKCVP 433
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
75-501 1.21e-150

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: 437.37  E-value: 1.21e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQEQ 154
Cdd:cd20618   1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGQDIVFAPYGPHWRHLRKICTLELFSAKRLES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 155 SRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFS----EENGETEKLRGLVTESIGLMKKMFLA 230
Cdd:cd20618  81 FQGVRKEELSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRYFgeseKESEEAREFKELIDEAFELAGAFNIG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 231 VLLRrQLQKLGISLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAAYGDENAEYKITKNHIKAFFVDLFI 310
Cdd:cd20618 161 DYIP-WLRWLDLQGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLDMLA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 311 GATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLL-PREFQQGCKI 389
Cdd:cd20618 240 AGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLlPHESTEDCKV 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 390 GGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSrsgqEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIG 469
Cdd:cd20618 320 AGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESD----IDDVKGQDFELLPFGSGRRMCPGMPLGLRMVQLTLA 395
                       410       420       430
                ....*....|....*....|....*....|....*
gi 15231052 470 MMVQCFDWR---IEGEKVNMKEAVkGTILTMAHPL 501
Cdd:cd20618 396 NLLHGFDWSlpgPKPEDIDMEEKF-GLTVPRAVPL 429
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
73-501 5.91e-134

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: 394.91  E-value: 5.91e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  73 RYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQ 152
Cdd:cd11072   1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGKDIAFAPYGEYWRQMRKICVLELLSAKRV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 153 EQSRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGEteKLRGLVTESIGL--------- 223
Cdd:cd11072  81 QSFRSIREEEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQD--KFKELVKEALELlggfsvgdy 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 224 ---MKKMFLAVLLRRQLQKlgislfkkdimgVSNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAA--YGDENAEYKITK 298
Cdd:cd11072 159 fpsLGWIDLLTGLDRKLEK------------VFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLrlQKEGDLEFPLTR 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 299 NHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL 378
Cdd:cd11072 227 DNIKAIILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPL 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 379 L-PREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSR--SGQEderreqaLKFLPFGSGRRGCP 455
Cdd:cd11072 307 LlPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIdfKGQD-------FELIPFGAGRRICP 379
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 15231052 456 GSNLAYMIVGSAIGMMVQCFDWR----IEGEKVNMKEAVkGTILTMAHPL 501
Cdd:cd11072 380 GITFGLANVELALANLLYHFDWKlpdgMKPEDLDMEEAF-GLTVHRKNPL 428
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
71-505 3.10e-123

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: 367.63  E-value: 3.10e-123
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  71 SSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQ 150
Cdd:cd11073   1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 151 AQEQSRDIRADDIKRFCRNLLDKARKKESVEIGKEA----MNLMNNILCKMSMGRSFSEENGEtekLRGLVTESIGLMKK 226
Cdd:cd11073  81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAfltsLNLISNTLFSVDLVDPDSESGSE---FKELVREIMELAGK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 227 M-------FLAVL----LRRQLQKLgislFKKdIMGVsnkFDVLLEKVLVEHREKPEKDqgtVMLDVLLAAYGDENAEYK 295
Cdd:cd11073 158 PnvadffpFLKFLdlqgLRRRMAEH----FGK-LFDI---FDGFIDERLAEREAGGDKK---KDDDLLLLLDLELDSESE 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 296 ITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPP 375
Cdd:cd11073 227 LTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPP 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 376 GPLL-PREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRS--GQEDErreqalkFLPFGSGRR 452
Cdd:cd11073 307 APLLlPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDfkGRDFE-------LIPFGSGRR 379
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15231052 453 GCPGSNLAYMIVGSAIGMMVQCFDWRIE----GEKVNMKEAVkGTILTMAHPLKLTP 505
Cdd:cd11073 380 ICPGLPLAERMVHLVLASLLHSFDWKLPdgmkPEDLDMEEKF-GLTLQKAVPLKAIP 435
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
75-501 3.20e-114

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: 344.20  E-value: 3.20e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQEQ 154
Cdd:cd20653   1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAPYGDHWRNLRRITTLEIFSSHRLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 155 SRDIRADDIKRFCRNLLDKARKK-ESVEIGKEAMNLMNNILCKMSMGRSFSEENG----ETEKLRGLVTESIGLMKKM-- 227
Cdd:cd20653  81 FSSIRRDEIRRLLKRLARDSKGGfAKVELKPLFSELTFNNIMRMVAGKRYYGEDVsdaeEAKLFRELVSEIFELSGAGnp 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 228 --FLAVLlrrqlQKLGISLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTvMLDVLLAAYGDENAEYkiTKNHIKAFF 305
Cdd:cd20653 161 adFLPIL-----RWFDFQGLEKRVKKLAKRRDAFLQGLIDEHRKNKESGKNT-MIDHLLSLQESQPEYY--TDEIIKGLI 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 306 VDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLL-PREFQ 384
Cdd:cd20653 233 LVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLvPHESS 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 385 QGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFlassrsgqEDERREqALKFLPFGSGRRGCPGSNLAYMIV 464
Cdd:cd20653 313 EDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF--------EGEERE-GYKLIPFGLGRRACPGAGLAQRVV 383
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 15231052 465 GSAIGMMVQCFDW-RIEGEKVNMKEAvKGTILTMAHPL 501
Cdd:cd20653 384 GLALGSLIQCFEWeRVGEEEVDMTEG-KGLTMPKAIPL 420
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
75-508 5.92e-109

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: 331.31  E-value: 5.92e-109
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQEQ 154
Cdd:cd20657   1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMAYNAQDMVFAPYGPRWRLLRKLCNLHLFGGKALED 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 155 SRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMG-RSFSEENG-ETEKLRGLVTEsigLMKKM----- 227
Cdd:cd20657  81 WAHVRENEVGHMLKSMAEASRKGEPVVLGEMLNVCMANMLGRVMLSkRVFAAKAGaKANEFKEMVVE---LMTVAgvfni 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 228 --FLAVLLRRQLQklGIslfKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTVM-LDVLLAAYGDENAEYKITKNHIKAF 304
Cdd:cd20657 158 gdFIPSLAWMDLQ--GV---EKKMKRLHKRFDALLTKILEEHKATAQERKGKPDfLDFVLLENDDNGEGERLTDTNIKAL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 305 FVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREF 383
Cdd:cd20657 233 LLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLnLPRIA 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 384 QQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQedERREQALKFLPFGSGRRGCPGSNLAYMI 463
Cdd:cd20657 313 SEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGRNAKV--DVRGNDFELIPFGAGRRICAGTRMGIRM 390
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 15231052 464 VGSAIGMMVQCFDWRIEG----EKVNMKEAVkGTILTMAHPLKLTPVTR 508
Cdd:cd20657 391 VEYILATLVHSFDWKLPAgqtpEELNMEEAF-GLALQKAVPLVAHPTPR 438
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
75-505 1.41e-100

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: 309.93  E-value: 1.41e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQEQ 154
Cdd:cd20654   1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMGYNYAMFGFAPYGPYWRELRKIATLELLSNRRLEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 155 SRDIRADDIKRFCRNLLDKARKKES------VEIGKEAMNLMNNILCKMSMG-RSFS----EENGETEKLRGLVTESIGL 223
Cdd:cd20654  81 LKHVRVSEVDTSIKELYSLWSNNKKggggvlVEMKQWFADLTFNVILRMVVGkRYFGgtavEDDEEAERYKKAIREFMRL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 224 MKKMFL--AVLLRRQLQKLGislFKKDIMGVSNKFDVLLEKVLVEHREK----PEKDQGTVMLDVLLAAYGDENaeyKIT 297
Cdd:cd20654 161 AGTFVVsdAIPFLGWLDFGG---HEKAMKRTAKELDSILEEWLEEHRQKrsssGKSKNDEDDDDVMMLSILEDS---QIS 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 298 KNH----IKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLH 373
Cdd:cd20654 235 GYDadtvIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLY 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 374 PPGPLL-PREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRsgqEDERREQALKFLPFGSGRR 452
Cdd:cd20654 315 PPGPLLgPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHK---DIDVRGQNFELIPFGSGRR 391
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231052 453 GCPGSNLAYMIVGSAIGMMVQCFDW-RIEGEKVNMKEAVkGTILTMAHPLK--LTP 505
Cdd:cd20654 392 SCPGVSFGLQVMHLTLARLLHGFDIkTPSNEPVDMTEGP-GLTNPKATPLEvlLTP 446
PLN02687 PLN02687
flavonoid 3'-monooxygenase
59-511 9.66e-98

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 305.20  E-value: 9.66e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   59 LSTLTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFM 138
Cdd:PLN02687  51 LGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRAL 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  139 KKLTVMKLLGPQAQEQSRDIRADDIKRFCRNLLDKARKKeSVEIGKEAMNLMNNILCKMSMGRS-FSEENGE-TEKLRGL 216
Cdd:PLN02687 131 RKICAVHLFSAKALDDFRHVREEEVALLVRELARQHGTA-PVNLGQLVNVCTTNALGRAMVGRRvFAGDGDEkAREFKEM 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  217 VTESIGLMKKM----FLAVLLRRQLQKLgISLFKKdimgVSNKFDVLLEKVLVEHR--EKPEKDQGTVMLDVLLAAYGDE 290
Cdd:PLN02687 210 VVELMQLAGVFnvgdFVPALRWLDLQGV-VGKMKR----LHRRFDAMMNGIIEEHKaaGQTGSEEHKDLLSTLLALKREQ 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  291 NA---EYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIK 367
Cdd:PLN02687 285 QAdgeGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIK 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  368 EALRLHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERREQaLKFLP 446
Cdd:PLN02687 365 ETFRLHPSTPLsLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPGGEHAGVDVKGSD-FELIP 443
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231052  447 FGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEG----EKVNMKEAVkGTILTMAHPLKLTPVTRQPP 511
Cdd:PLN02687 444 FGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADgqtpDKLNMEEAY-GLTLQRAVPLMVHPRPRLLP 511
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
58-501 2.98e-97

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 303.31  E-value: 2.98e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   58 LLSTLTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKF 137
Cdd:PLN00110  47 LLGNMPHVALAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRPPNAGATHLAYGAQDMVFADYGPRWKL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  138 MKKLTVMKLLGPQAQEQSRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRS-FSEENGETEKLRGL 216
Cdd:PLN00110 127 LRKLSNLHMLGGKALEDWSQVRTVELGHMLRAMLELSQRGEPVVVPEMLTFSMANMIGQVILSRRvFETKGSESNEFKDM 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  217 VTESIGLMKKM----FLAVLLRRQLQklGIslfKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTV-MLDVLLAAYGDEN 291
Cdd:PLN00110 207 VVELMTTAGYFnigdFIPSIAWMDIQ--GI---ERGMKHLHKKFDKLLTRMIEEHTASAHERKGNPdFLDVVMANQENST 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  292 AEyKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALR 371
Cdd:PLN00110 282 GE-KLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFR 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  372 LHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLaSSRSGQEDERREQaLKFLPFGSG 450
Cdd:PLN00110 361 KHPSTPLnLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFL-SEKNAKIDPRGND-FELIPFGAG 438
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15231052  451 RRGCPGSNLAYMIVGSAIGMMVQCFDWRI-EGEKVNMKEAVkGTILTMAHPL 501
Cdd:PLN00110 439 RRICAGTRMGIVLVEYILGTLVHSFDWKLpDGVELNMDEAF-GLALQKAVPL 489
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
57-511 2.07e-94

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 296.35  E-value: 2.07e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   57 LLLSTLTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWK 136
Cdd:PLN03112  47 LQLGPLPHRDLASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRPRTLAAVHLAYGCGDVALAPLGPHWK 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  137 FMKKLTVMKLLGPQAQEQSRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSF----SEENGETEK 212
Cdd:PLN03112 127 RMRRICMEHLLTTKRLESFAKHRAEEARHLIQDVWEAAQTGKPVNLREVLGAFSMNNVTRMLLGKQYfgaeSAGPKEAME 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  213 LRGLVTESIGLMKKMFLAVLLRrQLQKLGISLFKKDIMGVSNKFDVLLEKVLVEHRE--KPEKDQGTVM--LDVLLAAYG 288
Cdd:PLN03112 207 FMHITHELFRLLGVIYLGDYLP-AWRWLDPYGCEKKMREVEKRVDEFHDKIIDEHRRarSGKLPGGKDMdfVDVLLSLPG 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  289 dENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKE 368
Cdd:PLN03112 286 -ENGKEHMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRE 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  369 ALRLHPPGP-LLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASsrsgqEDERREQA----LK 443
Cdd:PLN03112 365 TFRMHPAGPfLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPA-----EGSRVEIShgpdFK 439
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231052  444 FLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWR----IEGEKVNMKEaVKGTILTMAHPLKLTPVTRQPP 511
Cdd:PLN03112 440 ILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSppdgLRPEDIDTQE-VYGMTMPKAKPLRAVATPRLAP 510
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
73-502 2.04e-81

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: 259.87  E-value: 2.04e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  73 RYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLV-FGSSSFVTAPYGDYWKFMKKLTVMKLLGPQA 151
Cdd:cd11075   1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVLFsSNKHMVNSSPYGPLWRTLRRNLVSEVLSPSR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 152 QEQSRDIRADDIKRFCRNLLDKARKKES-VEIGKEAMNLMNNILCKMSMGRSFSEEngeteklrglVTESIGLMKKMFLA 230
Cdd:cd11075  81 LKQFRPARRRALDNLVERLREEAKENPGpVNVRDHFRHALFSLLLYMCFGERLDEE----------TVRELERVQRELLL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 231 VLLRRQ----LQKLGISLFKKDIMGVSNkFDVLLEKVLV-------EHREKPEKDQGTvmLDVLLAAYGDENAE---YKI 296
Cdd:cd11075 151 SFTDFDvrdfFPALTWLLNRRRWKKVLE-LRRRQEEVLLplirarrKRRASGEADKDY--TDFLLLDLLDLKEEggeRKL 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 297 TKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPG 376
Cdd:cd11075 228 TDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPG 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 377 P-LLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLAssrsGQEDER-----REqaLKFLPFGSG 450
Cdd:cd11075 308 HfLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLA----GGEAADidtgsKE--IKMMPFGAG 381
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 15231052 451 RRGCPGSNLAYMIVGSAIGMMVQCFDWR-IEGEKVNMKEAVKGTILtMAHPLK 502
Cdd:cd11075 382 RRICPGLGLATLHLELFVARLVQEFEWKlVEGEEVDFSEKQEFTVV-MKNPLR 433
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
64-488 7.22e-81

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: 259.52  E-value: 7.22e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052    64 HKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTA-VDESLVFGSSSFVTAPYGDYWKFMKKLT 142
Cdd:pfam00067  23 HSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPwFATSRGPFLGKGIVFANGPRWRQLRRFL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   143 VMKLLGPQAQEQsRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSF-SEENGETEKLRGLVTESI 221
Cdd:pfam00067 103 TPTFTSFGKLSF-EPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGERFgSLEDPKFLELVKAVQELS 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   222 GLMKKMFLAVLLR-RQLQKLGISLFKKdIMGVSNKFDVLLEKVLVEHREKPEKDQGTVM--LDVLLAAYGDENAEyKITK 298
Cdd:pfam00067 182 SLLSSPSPQLLDLfPILKYFPGPHGRK-LKRARKKIKDLLDKLIEERRETLDSAKKSPRdfLDALLLAKEEEDGS-KLTD 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   299 NHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGP- 377
Cdd:pfam00067 260 EELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPl 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   378 LLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERreqalkFLPFGSGRRGCPGS 457
Cdd:pfam00067 340 LLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFA------FLPFGAGPRNCLGE 413
                         410       420       430
                  ....*....|....*....|....*....|..
gi 15231052   458 NLAYMIVGSAIGMMVQCFDWRI-EGEKVNMKE 488
Cdd:pfam00067 414 RLARMEMKLFLATLLQNFEVELpPGTDPPDID 445
PLN02183 PLN02183
ferulate 5-hydroxylase
57-479 4.52e-77

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 251.31  E-value: 4.52e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   57 LLLSTLTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWK 136
Cdd:PLN02183  51 LMMDQLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPANIAISYLTYDRADMAFAHYGPFWR 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  137 FMKKLTVMKLLGPQAQEQSRDIRaDDIKRFCRNLldKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEenGETEKLRGL 216
Cdd:PLN02183 131 QMRKLCVMKLFSRKRAESWASVR-DEVDSMVRSV--SSNIGKPVNIGELIFTLTRNITYRAAFGSSSNE--GQDEFIKIL 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  217 VTESiglmkKMFLAVLLRRQLQKLGI---SLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQG--------TVMLDVLLA 285
Cdd:PLN02183 206 QEFS-----KLFGAFNVADFIPWLGWidpQGLNKRLVKARKSLDGFIDDIIDDHIQKRKNQNAdndseeaeTDMVDDLLA 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  286 AYGDE---------NAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDL 356
Cdd:PLN02183 281 FYSEEakvnesddlQNSIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDL 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  357 PNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassRSGQEDE 436
Cdd:PLN02183 361 EKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFL---KPGVPDF 437
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 15231052  437 RREQaLKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRI 479
Cdd:PLN02183 438 KGSH-FEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWEL 479
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
75-497 8.58e-77

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: 247.51  E-value: 8.58e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLvFGSSSFVTApYGDYWKFMKKLTV--MKLLGPQAQ 152
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEII-SGGKGILFS-NGDYWKELRRFALssLTKTKLKKK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 153 EQSRdIrADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEEN-GETEKLRGLVTESIGLMKK--MFL 229
Cdd:cd20617  79 MEEL-I-EEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDdGEFLKLVKPIEEIFKELGSgnPSD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 230 AVLLRRQLQKLGISLFKKDImgvsNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAAYGDENAEYKITKNHIKAFFVDLF 309
Cdd:cd20617 157 FIPILLPFYFLYLKKLKKSY----DKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDLF 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 310 IGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQQGCK 388
Cdd:cd20617 233 LAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLgLPRVTTEDTE 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 389 IGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAI 468
Cdd:cd20617 313 IGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFL-------ENDGNKLSEQFIPFGIGKRNCVGENLARDELFLFF 385
                       410       420
                ....*....|....*....|....*....
gi 15231052 469 GMMVQCFDWRIEGEKVNMKEAVKGTILTM 497
Cdd:cd20617 386 ANLLLNFKFKSSDGLPIDEKEVFGLTLKP 414
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
81-503 5.30e-72

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: 235.72  E-value: 5.30e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  81 RIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQ---EQSRD 157
Cdd:cd20658   7 RLGNTHVIPVTCPKIAREILRKQDAVFASRPLTYATEIISGGYKTTVISPYGEQWKKMRKVLTTELMSPKRHqwlHGKRT 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 158 IRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMG-RSFSE--ENGeteklrGLVTESIGLMKKMFLAV--- 231
Cdd:cd20658  87 EEADNLVAYVYNMCKKSNGGGLVNVRDAARHYCGNVIRKLMFGtRYFGKgmEDG------GPGLEEVEHMDAIFTALkcl 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 232 ----------LLRRqLQKLGISLFKKDIMGVSNKF-DVLLEKVLVEHREKpEKDQGTVMLDVLLAAyGDENAEYKITKNH 300
Cdd:cd20658 161 yafsisdylpFLRG-LDLDGHEKIVREAMRIIRKYhDPIIDERIKQWREG-KKKEEEDWLDVFITL-KDENGNPLLTPDE 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 301 IKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGP-LL 379
Cdd:cd20658 238 IKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPfNV 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 380 PREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLAssrSGQEDERREQALKFLPFGSGRRGCPGSNL 459
Cdd:cd20658 318 PHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLN---EDSEVTLTEPDLRFISFSTGRRGCPGVKL 394
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 15231052 460 AYMIVGSAIGMMVQCFDWRIEG--EKVNMKEAVKGtiLTMAHPLKL 503
Cdd:cd20658 395 GTAMTVMLLARLLQGFTWTLPPnvSSVDLSESKDD--LFMAKPLVL 438
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
74-502 1.61e-70

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: 231.61  E-value: 1.61e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQE 153
Cdd:cd20656   1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGQDLIWADYGPHYVKVRKLCTLELFTPKRLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 154 QSRDIRADDIKRFCRNLLDKARKKESveIGKeAMNLMN-------NILCKMSMGRSFSEENGETEK----LRGLVTESIG 222
Cdd:cd20656  81 SLRPIREDEVTAMVESIFNDCMSPEN--EGK-PVVLRKylsavafNNITRLAFGKRFVNAEGVMDEqgveFKAIVSNGLK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 223 LMKKMFLA---VLLRRQLqklgiSLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAAYGDEnaeYKITKN 299
Cdd:cd20656 158 LGASLTMAehiPWLRWMF-----PLSEKAFAKHGARRDRLTKAIMEEHTLARQKSGGGQQHFVALLTLKEQ---YDLSED 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 300 HIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL- 378
Cdd:cd20656 230 TVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLm 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 379 LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgQED-ERREQALKFLPFGSGRRGCPGS 457
Cdd:cd20656 310 LPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFL------EEDvDIKGHDFRLLPFGAGRRVCPGA 383
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 15231052 458 NLAYMIVGSAIGMMVQCFDWR----IEGEKVNMKEAvKGTILTMAHPLK 502
Cdd:cd20656 384 QLGINLVTLMLGHLLHHFSWTppegTPPEEIDMTEN-PGLVTFMRTPLQ 431
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
75-482 7.06e-68

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: 223.55  E-value: 7.06e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTapYGDYWKFMKKLtVMKLLGPQAQEQ 154
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTL--DGPEHRRLRRL-LAPAFTPRALAA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 155 SRDIRADDIKRFCRNLLDKARKKESVEigKEAMNLMNNILCKMSMGrsfSEENGETEKLRGLVTESIGLMKKMFLAVLLR 234
Cdd:cd00302  78 LRPVIREIARELLDRLAAGGEVGDDVA--DLAQPLALDVIARLLGG---PDLGEDLEELAELLEALLKLLGPRLLRPLPS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 235 RQLQKlgislFKKDIMGVSNKFDVLLEkvlvEHREKPEKDQGTVMLDvllaaygDENAEYKITKNHIKAFFVDLFIGATD 314
Cdd:cd00302 153 PRLRR-----LRRARARLRDYLEELIA----RRRAEPADDLDLLLLA-------DADDGGGLSDEEIVAELLTLLLAGHE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 315 TSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSrliQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYI 394
Cdd:cd00302 217 TTASLLAWALYLLARHPEVQERLRAEIDAVLGDG---TPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTI 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 395 PEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqeDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQC 474
Cdd:cd00302 294 PAGTLVLLSLYAAHRDPEVFPDPDEFDPERFL--------PEREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRR 365

                ....*...
gi 15231052 475 FDWRIEGE 482
Cdd:cd00302 366 FDFELVPD 373
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
86-501 2.92e-66

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: 220.28  E-value: 2.92e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  86 PIILVSSASVAYEIfrtqdVNISSRGVTAVDES---LVFGSS-SFvtAPYGDYWKFMKKLTVMKLLGPQAQEQSRDIRAD 161
Cdd:cd11076  14 RVVITSHPETAREI-----LNSPAFADRPVKESayeLMFNRAiGF--APYGEYWRNLRRIASNHLFSPRRIAASEPQRQA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 162 DIKRFCRNLLDKARKKESVEIGK--EAMNLmNNILCKMsMGRS--FSEENGETEKLRGLVTESIGLMKKM-------FLA 230
Cdd:cd11076  87 IAAQMVKAIAKEMERSGEVAVRKhlQRASL-NNIMGSV-FGRRydFEAGNEEAEELGEMVREGYELLGAFnwsdhlpWLR 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 231 VL----LRRQLQKLgislfkkdimgVSnKFDVLLEKVLVEHREKPEKDQGTVML--DVLLAAYGDEnaeyKITKNHIKAF 304
Cdd:cd11076 165 WLdlqgIRRRCSAL-----------VP-RVNTFVGKIIEEHRAKRSNRARDDEDdvDVLLSLQGEE----KLSDSDMIAV 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 305 FVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLP--RE 382
Cdd:cd11076 229 LWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGPLLSwaRL 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 383 FQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSrSGQEDERREQALKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd11076 309 AIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAE-GGADVSVLGSDLRLAPFGAGRRVCPGKALGLA 387
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 15231052 463 IVGSAIGMMVQCFDWRIEGEK-VNMKEAVKGTiLTMAHPL 501
Cdd:cd11076 388 TVHLWVAQLLHEFEWLPDDAKpVDLSEVLKLS-CEMKNPL 426
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
49-505 7.68e-65

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 218.41  E-value: 7.68e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   49 LPIIGHVHLLLSTLTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVT 128
Cdd:PLN03234  36 LPIIGNLHQMEKFNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGF 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  129 APYGDYWKFMKKLTVMKLLGPQAQEQSRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENG 208
Cdd:PLN03234 116 GQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGT 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  209 ETEKLRGLVTESIGLMKKMFLAVLLR-----RQLQKLGISLfKKDIMGVSNKFDVLLEKVLVEHREKPEKDQgtvMLDVL 283
Cdd:PLN03234 196 EMKRFIDILYETQALLGTLFFSDLFPyfgflDNLTGLSARL-KKAFKELDTYLQELLDETLDPNRPKQETES---FIDLL 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  284 LAAYGDENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLH 363
Cdd:PLN03234 272 MQIYKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLK 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  364 AVIKEALRLHPPGP-LLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWED-PEEFKPERFLASSRSgqeDERREQA 441
Cdd:PLN03234 352 AVIKESLRLEPVIPiLLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERFMKEHKG---VDFKGQD 428
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231052  442 LKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWR----IEGEKVNMkEAVKGTILTMAHPLKLTP 505
Cdd:PLN03234 429 FELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSlpkgIKPEDIKM-DVMTGLAMHKKEHLVLAP 495
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
74-501 1.16e-64

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: 215.90  E-value: 1.16e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLtVMKLLGPQAQE 153
Cdd:cd11065   1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELMGWGMRLLLMPYGPRWRLHRRL-FHQLLNPSAVR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 154 QSRDIRADDIKRFCRNLLDKARKKESvEIGKEAmnlmNNILCKMSMGRSFSEENGEteklrgLVTESIGLMKKMFLAV-- 231
Cdd:cd11065  80 KYRPLQELESKQLLRDLLESPDDFLD-HIRRYA----ASIILRLAYGYRVPSYDDP------LLRDAEEAMEGFSEAGsp 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 232 ---------LLR-----------RQLQKLgislfKKDIMGVsnkFDVLLEKVLveHREKPEKDQGTVMLDVLLAaygdEN 291
Cdd:cd11065 149 gaylvdffpFLRylpswlgapwkRKAREL-----RELTRRL---YEGPFEAAK--ERMASGTATPSFVKDLLEE----LD 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 292 AEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALR 371
Cdd:cd11065 215 KEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLR 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 372 LHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERREQAlkflPFGSG 450
Cdd:cd11065 295 WRPVAPLgIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPDPPHF----AFGFG 370
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231052 451 RRGCPGSNLAYMIVGSAIGMMVQCFDWR-----IEGEKVNMKEAVKGTIltmAHPL 501
Cdd:cd11065 371 RRICPGRHLAENSLFIAIARLLWAFDIKkpkdeGGKEIPDEPEFTDGLV---SHPL 423
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
74-462 1.83e-63

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: 212.84  E-value: 1.83e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKL-LGPQAQ 152
Cdd:cd11027   1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGKDIAFGDYSPTWKLHRKLAHSALrLYASGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 153 EQSRDIRADDIKRFCRNLldKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMFLAVL 232
Cdd:cd11027  81 PRLEEKIAEEAEKLLKRL--ASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKFFELLGAGSLLDI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 233 LRRqLQKL---GISLFKKDImgvsNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAAYGDENAEYK-----ITKNHIKAF 304
Cdd:cd11027 159 FPF-LKYFpnkALRELKELM----KERDEILRKKLEEHKETFDPGNIRDLTDALIKAKKEAEDEGDedsglLTDDHLVMT 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 305 FVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREF 383
Cdd:cd11027 234 ISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLaLPHKT 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 384 QQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqeDERREQALK---FLPFGSGRRGCPGSNLA 460
Cdd:cd11027 314 TCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFL--------DENGKLVPKpesFLPFSAGRRVCLGESLA 385

                ..
gi 15231052 461 YM 462
Cdd:cd11027 386 KA 387
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
62-476 3.95e-62

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 211.51  E-value: 3.95e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   62 LTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKL 141
Cdd:PLN02394  51 LNHRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGDHWRKMRRI 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  142 TVMKLLGPQAQEQSRDIRADDIKRFCRNLL-DKARKKESVEIGKEAMNLMNNILCKMSMGRSF-SEENGETEKLRGLVTE 219
Cdd:PLN02394 131 MTVPFFTNKVVQQYRYGWEEEADLVVEDVRaNPEAATEGVVIRRRLQLMMYNIMYRMMFDRRFeSEDDPLFLKLKALNGE 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  220 SIGLMKKM------FLAVL---LRRQLQKLgislfkKDimgVSNKFDVLLEKVLVEHREK------PEKDQGTVMLDVLL 284
Cdd:PLN02394 211 RSRLAQSFeynygdFIPILrpfLRGYLKIC------QD---VKERRLALFKDYFVDERKKlmsakgMDKEGLKCAIDHIL 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  285 AAygDENAEykITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHA 364
Cdd:PLN02394 282 EA--QKKGE--INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQA 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  365 VIKEALRLHPPGPLL-PREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqEDERREQA-- 441
Cdd:PLN02394 358 VVKETLRLHMAIPLLvPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFL-------EEEAKVEAng 430
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 15231052  442 --LKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFD 476
Cdd:PLN02394 431 ndFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFE 467
PLN02655 PLN02655
ent-kaurene oxidase
53-485 1.95e-57

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 198.04  E-value: 1.95e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   53 GHVHLLLSTLTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYG 132
Cdd:PLN02655  11 GNLLQLKEKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVLTRDKSMVATSDYG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  133 DYWKFMKKLTVMKLLGPQAQEQSRDIRADDIkrfcRNLLDK--ARKKESVEIGKEAMNLMNNILCKMSMGRSFSE--ENG 208
Cdd:PLN02655  91 DFHKMVKRYVMNNLLGANAQKRFRDTRDMLI----ENMLSGlhALVKDDPHSPVNFRDVFENELFGLSLIQALGEdvESV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  209 ETEKL-RGLVTESI--GLMKKMFLAVL------LRRQLQKLGISLFKKDIMGVSNKFDVLLEKVLVEHREK-PEKDQGTV 278
Cdd:PLN02655 167 YVEELgTEISKEEIfdVLVHDMMMCAIevdwrdFFPYLSWIPNKSFETRVQTTEFRRTAVMKALIKQQKKRiARGEERDC 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  279 MLDVLLAAygdenaEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRlIQETDLPN 358
Cdd:PLN02655 247 YLDFLLSE------ATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDER-VTEEDLPN 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  359 LPYLHAVIKEALRLHPPGPLLPREF-QQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqeDER 437
Cdd:PLN02655 320 LPYLNAVFHETLRKYSPVPLLPPRFvHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFL--------GEK 391
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15231052  438 REQA--LKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRI---EGEKVN 485
Cdd:PLN02655 392 YESAdmYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLregDEEKED 444
PLN02966 PLN02966
cytochrome P450 83A1
31-505 5.35e-56

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 194.97  E-value: 5.35e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   31 KKPKDSRvnFDLPPSPPSLPIIGHVHLLLSTLTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSR 110
Cdd:PLN02966  21 QKPKTKR--YKLPPGPSPLPVIGNLLQLQKLNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  111 GVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQEQSRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLM 190
Cdd:PLN02966  99 PPHRGHEFISYGRRDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAADKSEVVDISELMLTFT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  191 NNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMFLAVLLRRQ--LQKL-GISLFKKDIMGVSNKF-DVLLEKVLVE 266
Cdd:PLN02966 179 NSVVCRQAFGKKYNEDGEEMKRFIKILYGTQSVLGKIFFSDFFPYCgfLDDLsGLTAYMKECFERQDTYiQEVVNETLDP 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  267 HREKPEKDQgtvMLDVLLAAYGDENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVG 346
Cdd:PLN02966 259 KRVKPETES---MIDLLMEIYKEQPFASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMK 335
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  347 K--SRLIQETDLPNLPYLHAVIKEALRLHPPGPLL-PREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKP 422
Cdd:PLN02966 336 EkgSTFVTEDDVKNLPYFRALVKETLRIEPVIPLLiPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRP 415
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  423 ERFLAssrsgQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRI----EGEKVNMkEAVKGTILTMA 498
Cdd:PLN02966 416 ERFLE-----KEVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLpngmKPDDINM-DVMTGLAMHKS 489

                 ....*..
gi 15231052  499 HPLKLTP 505
Cdd:PLN02966 490 QHLKLVP 496
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
73-476 1.98e-55

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: 191.92  E-value: 1.98e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  73 RYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQ 152
Cdd:cd11074   2 KFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGEHWRKMRRIMTVPFFTNKVV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 153 EQSRDIRADDIKRFCRNLldKARKKESVE---IGKEAMNLMNNILCKMSMGRSF-SEENGETEKLRGLVTESIGLMKKM- 227
Cdd:cd11074  82 QQYRYGWEEEAARVVEDV--KKNPEAATEgivIRRRLQLMMYNNMYRIMFDRRFeSEDDPLFVKLKALNGERSRLAQSFe 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 228 -----FLAVL---LRRQLQKLgislfkKDimgVSNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAAYGDENAEYK--IT 297
Cdd:cd11074 160 ynygdFIPILrpfLRGYLKIC------KE---VKERRLQLFKDYFVDERKKLGSTKSTKNEGLKCAIDHILDAQKKgeIN 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 298 KNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGP 377
Cdd:cd11074 231 EDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLRMAIP 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 378 LL-PREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqEDERREQA----LKFLPFGSGRR 452
Cdd:cd11074 311 LLvPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFL-------EEESKVEAngndFRYLPFGVGRR 383
                       410       420
                ....*....|....*....|....
gi 15231052 453 GCPGSNLAYMIVGSAIGMMVQCFD 476
Cdd:cd11074 384 SCPGIILALPILGITIGRLVQNFE 407
PLN02971 PLN02971
tryptophan N-hydroxylase
80-510 1.26e-53

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 189.48  E-value: 1.26e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   80 LRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQEQSRDIR 159
Cdd:PLN02971  98 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNR 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  160 ADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMG-RSFSEEngeTEKLRGLVTESIGLMKKMF------LAVL 232
Cdd:PLN02971 178 AEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGtRTFSEK---TEPDGGPTLEDIEHMDAMFeglgftFAFC 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  233 LRRQLQKL-GISL-----FKKDIMGVSNKF-DVLLEKVLVEHREKpEKDQGTVMLDVLLAAyGDENAEYKITKNHIKAFF 305
Cdd:PLN02971 255 ISDYLPMLtGLDLnghekIMRESSAIMDKYhDPIIDERIKMWREG-KRTQIEDFLDIFISI-KDEAGQPLLTADEIKPTI 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  306 VDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQ 384
Cdd:PLN02971 333 KELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVAL 412
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  385 QGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSrsgQEDERREQALKFLPFGSGRRGCPGSNLAYMIV 464
Cdd:PLN02971 413 SDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEC---SEVTLTENDLRFISFSTGKRGCAAPALGTAIT 489
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 15231052  465 GSAIGMMVQCFDWRIEGEKVNMKEAVKGTILTMAHPLKLTPVTRQP 510
Cdd:PLN02971 490 TMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVMVGELRLS 535
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
75-483 2.47e-50

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: 177.79  E-value: 2.47e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEI--------------FRTQDVNiSSRGVTAVDeslvfgsssfvtapyGDYWKFMKK 140
Cdd:cd20651   1 GDVVGLKLGKDKVVVVSGYEAVREVlsreefdgrpdgffFRLRTFG-KRLGITFTD---------------GPFWKEQRR 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 141 LTVMKL---------LGPQAQEQSRDIRaDDIKRfcrnlldkaRKKESVEIGkeamNLMN----NILCKMSMGRSFSEEN 207
Cdd:cd20651  65 FVLRHLrdfgfgrrsMEEVIQEEAEELI-DLLKK---------GEKGPIQMP----DLFNvsvlNVLWAMVAGERYSLED 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 208 GETEKLRGLVTE---SIGLMKKMFLAVLLRRQL--QKLGISLFKKDIMGVSNkfdvLLEKVLVEHREKPEKDQGTVMLDV 282
Cdd:cd20651 131 QKLRKLLELVHLlfrNFDMSGGLLNQFPWLRFIapEFSGYNLLVELNQKLIE----FLKEEIKEHKKTYDEDNPRDLIDA 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 283 LLAAYGDENA-EYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPY 361
Cdd:cd20651 207 YLREMKKKEPpSSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPY 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 362 LHAVIKEALRLHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERreq 440
Cdd:cd20651 287 TEAVILEVLRIFTLVPIgIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEW--- 363
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 15231052 441 alkFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEK 483
Cdd:cd20651 364 ---FLPFGAGKRRCLGESLARNELFLFFTGLLQNFTFSPPNGS 403
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
74-475 1.51e-48

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: 173.15  E-value: 1.51e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLvFGSSSFVTApyGDYWKFMKKLTV-------MKL 146
Cdd:cd11055   2 YGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRPLFILLDEP-FDSSLLFLK--GERWKRLRTTLSptfssgkLKL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 147 LGPqaqeqsrdIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMG-RSFSEENGE---TEKLRGLVTESIG 222
Cdd:cd11055  79 MVP--------IINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGiDVDSQNNPDdpfLKAAKKIFRNSII 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 223 LMKKMFLAVLLRRQLQKLGISLFKKDIMgvsNKFDVLLEKVlVEHREKPEKDQGTVMLDVLL-AAYGDENA-EYKITKNH 300
Cdd:cd11055 151 RLFLLLLLFPLRLFLFLLFPFVFGFKSF---SFLEDVVKKI-IEQRRKNKSSRRKDLLQLMLdAQDSDEDVsKKKLTDDE 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 301 IKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLP 380
Cdd:cd11055 227 IVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFIS 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 381 REFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLAssrsgqEDERREQALKFLPFGSGRRGCPGSNLA 460
Cdd:cd11055 307 RECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSP------ENKAKRHPYAYLPFGAGPRNCIGMRFA 380
                       410
                ....*....|....*
gi 15231052 461 YMIVGSAIGMMVQCF 475
Cdd:cd11055 381 LLEVKLALVKILQKF 395
PLN03018 PLN03018
homomethionine N-hydroxylase
88-511 2.69e-47

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 172.12  E-value: 2.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   88 ILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLT---VMKLLGPQAQEQSRDIRADDIK 164
Cdd:PLN03018  89 ITINSDEIAREAFRERDADLADRPQLSIMETIGDNYKSMGTSPYGEQFMKMKKVItteIMSVKTLNMLEAARTIEADNLI 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  165 RFCRNLLDKArkkESVEIGKEAMNLMNNILCKMSMGRS-------FSEEN--GETEKLR-GLVTESIGLMKKMFLAVLLR 234
Cdd:PLN03018 169 AYIHSMYQRS---ETVDVRELSRVYGYAVTMRMLFGRRhvtkenvFSDDGrlGKAEKHHlEVIFNTLNCLPGFSPVDYVE 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  235 RQLQKLGI----SLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAaYGDENAEYKITKNHIKAFFVDLFI 310
Cdd:PLN03018 246 RWLRGWNIdgqeERAKVNVNLVRSYNNPIIDERVELWREKGGKAAVEDWLDTFIT-LKDQNGKYLVTPDEIKAQCVEFCI 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  311 GATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREF-QQGCKI 389
Cdd:PLN03018 325 AAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVaRQDTTL 404
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  390 GGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIG 469
Cdd:PLN03018 405 GGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDGITKEVTLVETEMRFVSFSTGRRGCVGVKVGTIMMVMMLA 484
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 15231052  470 MMVQCFDWRIEGEKVNMKEAVKGTILTMAHPLKLTPVTRQPP 511
Cdd:PLN03018 485 RFLQGFNWKLHQDFGPLSLEEDDASLLMAKPLLLSVEPRLAP 526
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
67-462 3.85e-47

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: 168.92  E-value: 3.85e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  67 LQKLSSRYGPLLYLRIFNV-PIILVSSASVAYEIFrTQDVNISSRGVTAVDESLVFGSSSFVTAPyGDYWKFMKKLTVMK 145
Cdd:cd11053   4 LERLRARYGDVFTLRVPGLgPVVVLSDPEAIKQIF-TADPDVLHPGEGNSLLEPLLGPNSLLLLD-GDRHRRRRKLLMPA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 146 LLGPQAQEQSRDIRadDIkrfCRNLLDKARKKESVEIGKEAMNLMNNIlckmsMGRS-FSEENGET-EKLRGLVTESIGL 223
Cdd:cd11053  82 FHGERLRAYGELIA--EI---TEREIDRWPPGQPFDLRELMQEITLEV-----ILRVvFGVDDGERlQELRRLLPRLLDL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 224 MKKMFLAV-LLRRQLqkLGISLFKKdIMGVSNKFDVLLEKVLVEHREKPEkDQGTVMLDVLLAAyGDENAEyKITKNHIK 302
Cdd:cd11053 152 LSSPLASFpALQRDL--GPWSPWGR-FLRARRRIDALIYAEIAERRAEPD-AERDDILSLLLSA-RDEDGQ-PLSDEELR 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 303 AFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLiqeTDLPNLPYLHAVIKEALRLHPPGPLLPRE 382
Cdd:cd11053 226 DELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDP---EDIAKLPYLDAVIKETLRLYPVAPLVPRR 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 383 FQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEderreqalkFLPFGSGRRGCPGSNLAYM 462
Cdd:cd11053 303 VKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRKPSPYE---------YLPFGGGVRRCIGAAFALL 373
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
157-478 6.58e-47

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: 168.14  E-value: 6.58e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 157 DIRADDIKRFCRNLLDKARKKEsVEIGKEAMNLMNNILCKMSMGRSFSEEngeTEKLRGLVTESIG-LMKKMFLAVLLRR 235
Cdd:cd20620  79 DAMVEATAALLDRWEAGARRGP-VDVHAEMMRLTLRIVAKTLFGTDVEGE---ADEIGDALDVALEyAARRMLSPFLLPL 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 236 QLQKLGISLFKKDImgvsNKFDVLLEKVLVEHREKPEkDQGTVmLDVLLAAYGDENAEyKITKNHIKAFFVDLFIGATDT 315
Cdd:cd20620 155 WLPTPANRRFRRAR----RRLDEVIYRLIAERRAAPA-DGGDL-LSMLLAARDEETGE-PMSDQQLRDEVMTLFLAGHET 227
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 316 SVQTIQWTMAEIMNNTHILERMREEIDSVVGkSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIP 395
Cdd:cd20620 228 TANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYRIP 306
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 396 EKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrSGQEDERREQAlkFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCF 475
Cdd:cd20620 307 AGSTVLISPYVTHRDPRFWPDPEAFDPERFT----PEREAARPRYA--YFPFGGGPRICIGNHFAMMEAVLLLATIAQRF 380

                ...
gi 15231052 476 DWR 478
Cdd:cd20620 381 RLR 383
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
73-502 2.20e-45

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: 164.62  E-value: 2.20e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  73 RYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDE-SLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQA 151
Cdd:cd11054   3 KYGPIVREKLGGRDIVHLFDPDDIEKVFRNEGKYPIRPSLEPLEKyRKKRGKPLGLLNSNGEEWHRLRSAVQKPLLRPKS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 152 Q----EQSRDIrADD-IKRfcrnlLDKARKKESVEIGkeamNLMNNI-------LCKMSMGRSF----SEENGETEKLrg 215
Cdd:cd11054  83 VasylPAINEV-ADDfVER-----IRRLRDEDGEEVP----DLEDELykwslesIGTVLFGKRLgcldDNPDSDAQKL-- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 216 lvTESIGLM-----KKMFLAVLLRrqlqKLGISLFKK------DIMGVSNKfdvLLEKVL--VEHREKPEKDQGTVMLDV 282
Cdd:cd11054 151 --IEAVKDIfessaKLMFGPPLWK----YFPTPAWKKfvkawdTIFDIASK---YVDEALeeLKKKDEEDEEEDSLLEYL 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 283 LLAAygdenaeyKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYL 362
Cdd:cd11054 222 LSKP--------GLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYL 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 363 HAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSrsgqEDERREQAL 442
Cdd:cd11054 294 KACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDD----SENKNIHPF 369
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 443 KFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEKVNMKEAvkgTILTMAHPLK 502
Cdd:cd11054 370 ASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHEELKVKTR---LILVPDKPLK 426
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
74-489 4.20e-45

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: 164.01  E-value: 4.20e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSR------GVTAVDESLVFGSssfvtapYGDYWKFMKKLTVMKLl 147
Cdd:cd11028   1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRpdfysfQFISNGKSMAFSD-------YGPRWKLHRKLAQNAL- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 148 gpqaqeqsrdiRADDIKRfCRNLLDKARKKESVEIGKEAMNLMN----------------NILCKMSMGRSFSEENgetE 211
Cdd:cd11028  73 -----------RTFSNAR-THNPLEEHVTEEAEELVTELTENNGkpgpfdprneiylsvgNVICAICFGKRYSRDD---P 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 212 KLRGLV------TESIG------LMKKMFLavLLRRQLQKLgislfkKDIMGVSNKFdvLLEKVLvEHREKPEKDQGTVM 279
Cdd:cd11028 138 EFLELVksnddfGAFVGagnpvdVMPWLRY--LTRRKLQKF------KELLNRLNSF--ILKKVK-EHLDTYDKGHIRDI 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 280 LDVLLAAYGDENAEYK----ITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETD 355
Cdd:cd11028 207 TDALIKASEEKPEEEKpevgLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSD 286
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 356 LPNLPYLHAVIKEALRLHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLasSRSGQE 434
Cdd:cd11028 287 RPNLPYTEAFILETMRHSSFVPFtIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFL--DDNGLL 364
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15231052 435 DERReqALKFLPFGSGRRGCPGSNLAYMIVGSAI-GMMVQCFDWRIEGEKVNMKEA 489
Cdd:cd11028 365 DKTK--VDKFLPFGAGRRRCLGEELARMELFLFFaTLLQQCEFSVKPGEKLDLTPI 418
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
82-476 1.06e-44

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: 162.71  E-value: 1.06e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  82 IFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTApyGDYWKFM-KKLTV------MKLLGPQAQEQ 154
Cdd:cd11056  10 LFRRPALLVRDPELIKQILVKDFAHFHDRGLYSDEKDDPLSANLFSLD--GEKWKELrQKLTPaftsgkLKNMFPLMVEV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 155 SrdiraddiKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMG---RSFSEENGETEKL-RGLVTESIGLMKKMFLA 230
Cdd:cd11056  88 G--------DELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGldaNSLNDPENEFREMgRRLFEPSRLRGLKFMLL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 231 VLLRRQLQKLGISLFKKDimgVSNKFDVLLEKVlVEHREKPE---KDqgtvMLDVLLAAY-----GDENAEYKITKNHIK 302
Cdd:cd11056 160 FFFPKLARLLRLKFFPKE---VEDFFRKLVRDT-IEYREKNNivrND----FIDLLLELKkkgkiEDDKSEKELTDEELA 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 303 AFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKS--RLIQETdLPNLPYLHAVIKEALRLHPPGPLLP 380
Cdd:cd11056 232 AQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHggELTYEA-LQEMKYLDQVVNETLRKYPPLPFLD 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 381 REFQQGCKIGG--FYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFlassrSGQEDERREQALkFLPFGSGRRGCPGSN 458
Cdd:cd11056 311 RVCTKDYTLPGtdVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERF-----SPENKKKRHPYT-YLPFGDGPRNCIGMR 384
                       410
                ....*....|....*...
gi 15231052 459 LAYMIVGSAIGMMVQCFD 476
Cdd:cd11056 385 FGLLQVKLGLVHLLSNFR 402
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
74-462 4.25e-44

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: 161.04  E-value: 4.25e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKL------- 146
Cdd:cd20674   1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTGKLVSQGGQDLSLGDYSLLWKAHRKLTRSALqlgirns 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 147 LGPQAQEQSRDiraddikrFCRNLLDKArkKESVEIGKEAMNLMNNILCKMSMGRSFSEENgETEKLRGLVTESIGLMKK 226
Cdd:cd20674  81 LEPVVEQLTQE--------LCERMRAQA--GTPVDIQEEFSLLTCSIICCLTFGDKEDKDT-LVQAFHDCVQELLKTWGH 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 227 MFLAVL----LRRQLQKLGISLFKKDImgvsNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAAYGD---ENAEYKITKN 299
Cdd:cd20674 150 WSIQALdsipFLRFFPNPGLRRLKQAV----ENRDHIVESQLRQHKESLVAGQWRDMTDYMLQGLGQprgEKGMGQLLEG 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 300 HIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL- 378
Cdd:cd20674 226 HVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLa 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 379 LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQederreqalKFLPFGSGRRGCPGSN 458
Cdd:cd20674 306 LPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAANR---------ALLPFGCGARVCLGEP 376

                ....
gi 15231052 459 LAYM 462
Cdd:cd20674 377 LARL 380
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
74-462 7.59e-44

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: 160.56  E-value: 7.59e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLtVMKLL-----G 148
Cdd:cd20673   1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRNGKDIAFADYSATWQLHRKL-VHSAFalfgeG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 149 PQAQEQsrdIRADDIKRFCRNLLdkARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLR----GLV-TESIGL 223
Cdd:cd20673  80 SQKLEK---IICQEASSLCDTLA--THNGESIDLSPPLFRAVTNVICLLCFNSSYKNGDPELETILnyneGIVdTVAKDS 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 224 MKKMF--LAVLLRRQLQKLgislfkKDIMGVSNKfdvLLEKVLVEHREKPEKDQGTVMLDVLLAA--------YGDENAE 293
Cdd:cd20673 155 LVDIFpwLQIFPNKDLEKL------KQCVKIRDK---LLQKKLEEHKEKFSSDSIRDLLDALLQAkmnaennnAGPDQDS 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 294 YKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLH 373
Cdd:cd20673 226 VGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIR 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 374 PPGPLL-PREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQederREQALKFLPFGSGRR 452
Cdd:cd20673 306 PVAPLLiPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQL----ISPSLSYLPFGAGPR 381
                       410
                ....*....|
gi 15231052 453 GCPGSNLAYM 462
Cdd:cd20673 382 VCLGEALARQ 391
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
264-484 8.21e-44

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: 160.07  E-value: 8.21e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 264 LVEHREKPEKDQGTVMLDVLLaaygdeNAEYK----ITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMRE 339
Cdd:cd11042 178 IIQKRRKSPDKDEDDMLQTLM------DAKYKdgrpLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALRE 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 340 EIDSVVGKS-RLIQETDLPNLPYLHAVIKEALRLHPPGPLLPR----EFQQGCkiGGFYIPEKTTLLINAYVVMRDPNVW 414
Cdd:cd11042 252 EQKEVLGDGdDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRkarkPFEVEG--GGYVIPKGHIVLASPAVSHRDPEIF 329
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231052 415 EDPEEFKPERFLassrsgqeDERREQALK----FLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEKV 484
Cdd:cd11042 330 KNPDEFDPERFL--------KGRAEDSKGgkfaYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSPF 395
PLN00168 PLN00168
Cytochrome P450; Provisional
67-508 1.26e-43

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 161.66  E-value: 1.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   67 LQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKL 146
Cdd:PLN00168  63 LRRLIARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVASSRLLGESDNTITRSSYGPVWRLLRRNLVAET 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  147 LGPQAQEQSRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGET--EKLRGLVTESIGLM 224
Cdd:PLN00168 143 LHPSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVETFQYAMFCLLVLMCFGERLDEPAVRAiaAAQRDWLLYVSKKM 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  225 K--KMFLAV---LLRRQLQKLGISLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTV---MLDVLLAAYGDENAEYKI 296
Cdd:PLN00168 223 SvfAFFPAVtkhLFRGRLQKALALRRRQKELFVPLIDARREYKNHLGQGGEPPKKETTFehsYVDTLLDIRLPEDGDRAL 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  297 TKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVG-KSRLIQETDLPNLPYLHAVIKEALRLHPP 375
Cdd:PLN00168 303 TDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGdDQEEVSEEDVHKMPYLKAVVLEGLRKHPP 382
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  376 GP-LLPREFQQGCKIGGFYIPEKTTllINAYVV-M-RDPNVWEDPEEFKPERFLASSRSGQEDERREQALKFLPFGSGRR 452
Cdd:PLN00168 383 AHfVLPHKAAEDMEVGGYLIPKGAT--VNFMVAeMgRDEREWERPMEFVPERFLAGGDGEGVDVTGSREIRMMPFGVGRR 460
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15231052  453 GCPGSNLAYMIVGSAIGMMVQCFDWR-IEGEKVNMKEAVKGTILtMAHPLKLTPVTR 508
Cdd:PLN00168 461 ICAGLGIAMLHLEYFVANMVREFEWKeVPGDEVDFAEKREFTTV-MAKPLRARLVPR 516
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
164-462 2.59e-43

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: 158.84  E-value: 2.59e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 164 KRFCRNLLDKArKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRglvtESIglmkKMFLAVLLRR-------- 235
Cdd:cd20628  85 KILVEKLKKKA-GGGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYV----KAV----KRILEIILKRifspwlrf 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 236 ----QLQKLGiSLFKKD---IMGVSNKfdvLLEKVLVEHREKPEKDQGT---------VMLDVLLAAYGDENaeyKITKN 299
Cdd:cd20628 156 dfifRLTSLG-KEQRKAlkvLHDFTNK---VIKERREELKAEKRNSEEDdefgkkkrkAFLDLLLEAHEDGG---PLTDE 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 300 HIKAFfVDLFIGA-TDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKS-RLIQETDLPNLPYLHAVIKEALRLHPPGP 377
Cdd:cd20628 229 DIREE-VDTFMFAgHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDdRRPTLEDLNKMKYLERVIKETLRLYPSVP 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 378 LLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLAssrsgqEDERREQALKFLPFGSGRRGCPGS 457
Cdd:cd20628 308 FIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLP------ENSAKRHPYAYIPFSAGPRNCIGQ 381

                ....*
gi 15231052 458 NLAYM 462
Cdd:cd20628 382 KFAML 386
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
173-462 3.24e-43

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: 158.62  E-value: 3.24e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 173 KARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMkkmFLAVLLRRQLQKLGISLFKKDIMGV 252
Cdd:cd11059  94 EAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDSRERELLRRLLA---SLAPWLRWLPRYLPLATSRLIIGIY 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 253 SNKFDV-------LLEKVLVEHREKPEKDQGTVMLDVLLAAYGDENaeykITKNHIKAFFVDLFIGATDTSVQTIQWTMA 325
Cdd:cd11059 171 FRAFDEieewaldLCARAESSLAESSDSESLTVLLLEKLKGLKKQG----LDDLEIASEALDHIVAGHDTTAVTLTYLIW 246
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 326 EIMNNTHILERMREEIDSVVGKSRLIQE-TDLPNLPYLHAVIKEALRLHPPGPL-LPREF-QQGCKIGGFYIPEKTTLLI 402
Cdd:cd11059 247 ELSRPPNLQEKLREELAGLPGPFRGPPDlEDLDKLPYLNAVIRETLRLYPPIPGsLPRVVpEGGATIGGYYIPGGTIVST 326
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 403 NAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERReqalKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd11059 327 QAYSLHRDPEVFPDPEEFDPERWLDPSGETAREMKR----AFWPFGSGSRMCIGMNLALM 382
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
163-482 7.12e-43

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: 157.38  E-value: 7.12e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 163 IKRFCRNLLDKARKKES--VEIGKEAMNLMNNILCKMSMGRSF----SEENGETEKLRGLVTESIGLMKKM-FLAVLLRR 235
Cdd:cd11061  81 VEQLCEQLDDRAGKPVSwpVDMSDWFNYLSFDVMGDLAFGKSFgmleSGKDRYILDLLEKSMVRLGVLGHApWLRPLLLD 160
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 236 QLQKLGISLFKKDIMGVSNKfdvllekvLVEHREKPEKDQGTVMLDVLLAAYgDENAEYKITKNHIKAFFVDLFIGATDT 315
Cdd:cd11061 161 LPLFPGATKARKRFLDFVRA--------QLKERLKAEEEKRPDIFSYLLEAK-DPETGEGLDLEELVGEARLLIVAGSDT 231
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 316 SVQTIQWTMAEIMNNTHILERMREEIDSVV-GKSRLIQETDLPNLPYLHAVIKEALRLHPPGP-LLPREF-QQGCKIGGF 392
Cdd:cd11061 232 TATALSAIFYYLARNPEAYEKLRAELDSTFpSDDEIRLGPKLKSLPYLRACIDEALRLSPPVPsGLPRETpPGGLTIDGE 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 393 YIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrSGQEDERREQAlKFLPFGSGRRGCPGSNLAYMIVGSAIGMMV 472
Cdd:cd11061 312 YIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWL----SRPEELVRARS-AFIPFSIGPRGCIGKNLAYMELRLVLARLL 386
                       330
                ....*....|
gi 15231052 473 QCFDWRIEGE 482
Cdd:cd11061 387 HRYDFRLAPG 396
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
163-462 1.69e-42

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: 156.59  E-value: 1.69e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 163 IKRFCRNLLDKARKKESVEIGKE----AMNLMNNIlckmSMGRSFS-EENGEteKLRGLVTESIGLMKKMFLAVL---LR 234
Cdd:cd11060  84 IDLLVDLLDEKAVSGKEVDLGKWlqyfAFDVIGEI----TFGKPFGfLEAGT--DVDGYIASIDKLLPYFAVVGQipwLD 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 235 RQLQKLGISLFKKDIMGVSNKFDVLLEKVlVEHREKPEKDQGTV--MLDVLLAAyGDENAEyKITKNHIKAFFVDLFIGA 312
Cdd:cd11060 158 RLLLKNPLGPKRKDKTGFGPLMRFALEAV-AERLAEDAESAKGRkdMLDSFLEA-GLKDPE-KVTDREVVAEALSNILAG 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 313 TDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGK---SRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREF-QQGC 387
Cdd:cd11060 235 SDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEgklSSPITFAEAQKLPYLQAVIKEALRLHPPVGLpLERVVpPGGA 314
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231052 388 KIGGFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFLassRSGQEDERREQALkFLPFGSGRRGCPGSNLAYM 462
Cdd:cd11060 315 TICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWL---EADEEQRRMMDRA-DLTFGAGSRTCLGKNIALL 386
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
73-482 2.74e-42

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: 155.44  E-value: 2.74e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  73 RYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTApYGDYWKFMKKLtVMKLLGPQAQ 152
Cdd:COG2124  30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLLTL-DGPEHTRLRRL-VQPAFTPRRV 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 153 EQSRDIraddIKRFCRNLLDKARKKESVEIGKE-AMNLMNNILCKMsmgrsFSEENGETEKLRGLVTESIGLMKKMFLAV 231
Cdd:COG2124 108 AALRPR----IREIADELLDRLAARGPVDLVEEfARPLPVIVICEL-----LGVPEEDRDRLRRWSDALLDALGPLPPER 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 232 LLRRQlqklgislfkkdimGVSNKFDVLLEKVLVEHREKPEKDqgtvMLDVLLAAYGDENaeyKITKNHIKAFFVDLFIG 311
Cdd:COG2124 179 RRRAR--------------RARAELDAYLRELIAERRAEPGDD----LLSALLAARDDGE---RLSDEELRDELLLLLLA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 312 ATDTSVQTIQWTMAEIMNNTHILERMREEidsvvgksrliqetdlpnLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGG 391
Cdd:COG2124 238 GHETTANALAWALYALLRHPEQLARLRAE------------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGG 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 392 FYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERflassrsgqederreQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMM 471
Cdd:COG2124 300 VTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------------PPNAHLPFGGGPHRCLGAALARLEARIALATL 364
                       410
                ....*....|..
gi 15231052 472 VQCF-DWRIEGE 482
Cdd:COG2124 365 LRRFpDLRLAPP 376
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
72-505 3.99e-41

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: 152.33  E-value: 3.99e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  72 SRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDEslVFGSSSFVTAPyGDYWKFMKKLtVMKLLGPQA 151
Cdd:cd11043   3 KRYGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWYPKSVRK--LLGKSSLLTVS-GEEHKRLRGL-LLSFLGPEA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 152 qeqSRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGrsfSEENGETEKLRGLVTEsigLMKKMFlAV 231
Cdd:cd11043  79 ---LKDRLLGDIDELVRQHLDSWWRGKSVVVLELAKKMTFELICKLLLG---IDPEEVVEELRKEFQA---FLEGLL-SF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 232 LLrrqlqKLGISLFKKDIMGvSNKFDVLLEKVLVEHREKPEKDQGTV-MLDVLLAAyGDENAEYkITKNHIKAFFVDLFI 310
Cdd:cd11043 149 PL-----NLPGTTFHRALKA-RKRIRKELKKIIEERRAELEKASPKGdLLDVLLEE-KDEDGDS-LTDEEILDNILTLLF 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 311 GATDTSVQTIQWTMAEIMNNTHILERMREEIDSVV----GKSRLIQEtDLPNLPYLHAVIKEALRLHPPGPLLPREFQQG 386
Cdd:cd11043 221 AGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAkrkeEGEGLTWE-DYKSMKYTWQVINETLRLAPIVPGVFRKALQD 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 387 CKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFlassrsgqEDERREQALKFLPFGSGRRGCPGSNLAYMIVGS 466
Cdd:cd11043 300 VEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRW--------EGKGKGVPYTFLPFGGGPRLCPGAELAKLEILV 371
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 15231052 467 AIGMMVQCFDWR-IEGEKVNMKeavKGTILTMAHPLKLTP 505
Cdd:cd11043 372 FLHHLVTRFRWEvVPDEKISRF---PLPRPPKGLPIRLSP 408
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
127-462 4.31e-41

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: 153.01  E-value: 4.31e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 127 VTAPYGDYWKFMKKLTVMKL---------LGPQAQEQSRDIraddikrfcrnlldkarKKESVEIGKEAMN-------LM 190
Cdd:cd20666  53 VFAPYGPVWRQQRKFSHSTLrhfglgklsLEPKIIEEFRYV-----------------KAEMLKHGGDPFNpfpivnnAV 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 191 NNILCKMSMGRSFSEENGETEKLRGLVTES--IGLMKKMFLaVLLRRQLQKLGISLFKkDIMGVSNKFDVLLEKVLVEHR 268
Cdd:cd20666 116 SNVICSMSFGRRFDYQDVEFKTMLGLMSRGleISVNSAAIL-VNICPWLYYLPFGPFR-ELRQIEKDITAFLKKIIADHR 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 269 EKPEKDQGTVMLDVLLAAYGDE---NAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVV 345
Cdd:cd20666 194 ETLDPANPRDFIDMYLLHIEEEqknNAESSFNEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVI 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 346 GKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPER 424
Cdd:cd20666 274 GPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLsIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSR 353
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15231052 425 FLasSRSGQEDERReqalKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20666 354 FL--DENGQLIKKE----AFIPFGIGRRVCMGEQLAKM 385
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
230-462 3.16e-40

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: 150.48  E-value: 3.16e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 230 AVLLRRQLQKLGISLFKKDIMGVSNKFDVLLEKVL---VEHREKPEKDQGTVMLDVLLAAYGDENAEYKITKNHIKAFFV 306
Cdd:cd20621 156 RLIFGRKSWKLFPTKKEKKLQKRVKELRQFIEKIIqnrIKQIKKNKDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFI 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 307 DLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGP-LLPREFQQ 385
Cdd:cd20621 236 TFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPfLFPRVATQ 315
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231052 386 GCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSrsgqedERREQALKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20621 316 DHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQN------NIEDNPFVFIPFSAGPRNCIGQHLALM 386
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
305-462 1.24e-39

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: 148.82  E-value: 1.24e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 305 FVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQ 384
Cdd:cd20613 239 FVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELT 318
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231052 385 QGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASsrsgqEDERREQAlKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20613 319 KDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPE-----APEKIPSY-AYFPFSLGPRSCIGQQFAQI 390
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
75-496 1.97e-39

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: 148.33  E-value: 1.97e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  75 GPLLYLRIFNVPIILVSSASVAYEIFRtQDVnISSRGVTAVDESLVFGSSsfVTAPYGDYWKFMKKLTV-------MKLL 147
Cdd:cd20652   1 GSIFSLKMGSVYTVVLSDPKLIRDTFR-RDE-FTGRAPLYLTHGIMGGNG--IICAEGDLWRDQRRFVHdwlrqfgMTKF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 148 GPQAQEQSRDIRADdIKRFCRNLldKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKM 227
Cdd:cd20652  77 GNGRAKMEKRIATG-VHELIKHL--KAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFLQEEGTKLIGVA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 228 ----FLAVLlrRQLQKlgislFKKDIMGVSN---KFDVLLEKVLVEHR--EKPEKDQGTVM--LDVLLAAYGD-ENAEYK 295
Cdd:cd20652 154 gpvnFLPFL--RHLPS-----YKKAIEFLVQgqaKTHAIYQKIIDEHKrrLKPENPRDAEDfeLCELEKAKKEgEDRDLF 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 296 ITKNHIKAF---FVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRL 372
Cdd:cd20652 227 DGFYTDEQLhhlLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRI 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 373 HPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDErreqalKFLPFGSGR 451
Cdd:cd20652 307 RSVVPLgIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPE------AFIPFQTGK 380
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 15231052 452 RGCPGSNLAYMIVGSAIGMMVQCFDWRI-EGEKVNMKEAVKGTILT 496
Cdd:cd20652 381 RMCLGDELARMILFLFTARILRKFRIALpDGQPVDSEGGNVGITLT 426
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
74-460 8.16e-39

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: 146.48  E-value: 8.16e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESlVFGSSSFVTAPyGDYWKFMKKLTVMKL----LGP 149
Cdd:cd20662   1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRER-IFNKNGLIFSS-GQTWKEQRRFALMTLrnfgLGK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 150 QAQEQSrdiraddIKRFCRNLLD--KARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKM 227
Cdd:cd20662  79 KSLEER-------IQEECRHLVEaiREEKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 228 flavllRRQLQKLGISLFK------KDIMGVSNKFDVLLEKVLVEHREKPEKDQGTVMLDVLL---AAYGDENAEYKItK 298
Cdd:cd20662 152 ------MSQLYNAFPWIMKylpgshQTVFSNWKKLKLFVSDMIDKHREDWNPDEPRDFIDAYLkemAKYPDPTTSFNE-E 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 299 NHIkAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL 378
Cdd:cd20662 225 NLI-CSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPL 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 379 -LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassRSGQEDERReqalKFLPFGSGRRGCPGS 457
Cdd:cd20662 304 nVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFL---ENGQFKKRE----AFLPFSMGKRACLGE 376

                ...
gi 15231052 458 NLA 460
Cdd:cd20662 377 QLA 379
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
161-479 2.49e-38

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: 145.09  E-value: 2.49e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 161 DDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFS---EENGETEKLRGL--VTESIGLMKKM-FLAVLLR 234
Cdd:cd11062  80 EKVDKLVSRLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGyldEPDFGPEFLDALraLAEMIHLLRHFpWLLKLLR 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 235 RqlqkLGISLFKKDIMGVSNKFDVL---LEKVLVEHREKPEKDQGTVMLDVLLAAYGDENAEYKITKNHIKAFFVDLFIG 311
Cdd:cd11062 160 S----LPESLLKRLNPGLAVFLDFQesiAKQVDEVLRQVSAGDPPSIVTSLFHALLNSDLPPSEKTLERLADEAQTLIGA 235
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 312 ATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQE-TDLPNLPYLHAVIKEALRL-HP-PGPLlPREF-QQGC 387
Cdd:cd11062 236 GTETTARTLSVATFHLLSNPEILERLREELKTAMPDPDSPPSlAELEKLPYLTAVIKEGLRLsYGvPTRL-PRVVpDEGL 314
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 388 KIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSA 467
Cdd:cd11062 315 YYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWL------GAAEKGKLDRYLVPFSKGSRSCLGINLAYAELYLA 388
                       330
                ....*....|..
gi 15231052 468 IGMMVQCFDWRI 479
Cdd:cd11062 389 LAALFRRFDLEL 400
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
280-483 3.39e-37

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: 141.92  E-value: 3.39e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 280 LDVLLAAYgDENAEyKITKNHIKAFfVDLFIGAT-DTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPN 358
Cdd:cd20659 209 LDILLTAR-DEDGK-GLTDEEIRDE-VDTFLFAGhDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSK 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 359 LPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgQEDERR 438
Cdd:cd20659 286 LPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFL------PENIKK 359
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15231052 439 EQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEK 483
Cdd:cd20659 360 RDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNH 404
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
74-462 1.18e-36

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: 140.39  E-value: 1.18e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDEsLVFGSSSfVTAPYGDYWKFMKKLTVMKL----LGP 149
Cdd:cd11026   1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFD-RVTKGYG-VVFSNGERWKQLRRFSLTTLrnfgMGK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 150 QAQEQSrdiraddIKRFCRNLLDKARKKESVEIGKEAM--NLMNNILCKMSMGRSFSEENGETEKLRGLVTESI------ 221
Cdd:cd11026  79 RSIEER-------IQEEAKFLVEAFRKTKGKPFDPTFLlsNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLrllssp 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 222 -GLMKKMFLAVLLRrqlqklgISLFKKDIMGVSNKFDVLLEKVLVEHRE--KPEKDQGTV--MLDVLLAAYGDENAEYKI 296
Cdd:cd11026 152 wGQLYNMFPPLLKH-------LPGPHQKLFRNVEEIKSFIRELVEEHREtlDPSSPRDFIdcFLLKMEKEKDNPNSEFHE 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 297 tKNHIKAFFvDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPG 376
Cdd:cd11026 225 -ENLVMTVL-DLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIV 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 377 PL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqeDE----RREQAlkFLPFGSGR 451
Cdd:cd11026 303 PLgVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFL--------DEqgkfKKNEA--FMPFSAGK 372
                       410
                ....*....|.
gi 15231052 452 RGCPGSNLAYM 462
Cdd:cd11026 373 RVCLGEGLARM 383
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
259-505 7.78e-36

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: 138.16  E-value: 7.78e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 259 LLEKVLVEHREKPEkDQGTVmLDVLLAAYGDENAeyKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMR 338
Cdd:cd11049 183 LVDEIIAEYRASGT-DRDDL-LSLLLAARDEEGR--PLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLH 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 339 EEIDSVVGKsRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPE 418
Cdd:cd11049 259 AELDAVLGG-RPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPE 337
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 419 EFKPERFLaSSRSGqedERREQAlkFLPFGSGRRGCPGSNLAY---MIVGSAIGMmvqcfDWRIE---GEKVnmKEAVKG 492
Cdd:cd11049 338 RFDPDRWL-PGRAA---AVPRGA--FIPFGAGARKCIGDTFALtelTLALATIAS-----RWRLRpvpGRPV--RPRPLA 404
                       250
                ....*....|...
gi 15231052 493 TilTMAHPLKLTP 505
Cdd:cd11049 405 T--LRPRRLRMRV 415
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
73-503 1.07e-35

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


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 138.23  E-value: 1.07e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  73 RYGPLLylrIFNVP--IILVSSASVAYEIFRTQDVNISSRGVTAVDEslVFGSSsfVTAPYGDYWKFMKKltVMKllgPQ 150
Cdd:cd11070   1 KLGAVK---ILFVSrwNILVTKPEYLTQIFRRRDDFPKPGNQYKIPA--FYGPN--VISSEGEDWKRYRK--IVA---PA 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 151 AQEQSRDIRADDI----KRFCRNLLDKArkKESVEIGKEAMNLMN----NILCKMSMGRSFseenGETEKLRGLVTESIG 222
Cdd:cd11070  69 FNERNNALVWEESirqaQRLIRYLLEEQ--PSAKGGGVDVRDLLQrlalNVIGEVGFGFDL----PALDEEESSLHDTLN 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 223 LMKKMFL-AVLLR-RQLQKLGISLFKKDI--MGVSNKF-DVLLEKVLVEHREKPEKDQGT--VMLDVLLAAYGDEnaeyK 295
Cdd:cd11070 143 AIKLAIFpPLFLNfPFLDRLPWVLFPSRKraFKDVDEFlSELLDEVEAELSADSKGKQGTesVVASRLKRARRSG----G 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 296 ITKNHIK--AFFvdLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVG--KSRLIQETDLPNLPYLHAVIKEALR 371
Cdd:cd11070 219 LTEKELLgnLFI--FFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGdePDDWDYEEDFPKLPYLLAVIYETLR 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 372 LHPPGPLLPREFQQGCKI-----GGFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFLASSRSGQEDERREQALK-F 444
Cdd:cd11070 297 LYPPVQLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSGEIGAATRFTPARGaF 376
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 445 LPFGSGRRGCPGSNLA-YMIVGsAIGMMVQCFDWRIEGEKVnMKEAVKGTILTMAHPLKL 503
Cdd:cd11070 377 IPFSAGPRACLGRKFAlVEFVA-ALAELFRQYEWRVDPEWE-EGETPAGATRDSPAKLRL 434
PTZ00404 PTZ00404
cytochrome P450; Provisional
59-460 1.54e-35

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 138.32  E-value: 1.54e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   59 LSTLTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAvdeSLVFGSSSF-VTAPYGDYWKF 137
Cdd:PTZ00404  46 LGNLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIP---SIKHGTFYHgIVTSSGEYWKR 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  138 MKKLTV--MKLLGPQAQEQSRDIRADDikrfcrnLLDKARKKES--------VEIGKEAMNLMNNILCKMSMGRSFSEEN 207
Cdd:PTZ00404 123 NREIVGkaMRKTNLKHIYDLLDDQVDV-------LIESMKKIESsgetfeprYYLTKFTMSAMFKYIFNEDISFDEDIHN 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  208 GETEKLRGLVTESIGLMK--KMFLAVLLRRQLQKLGISLFKKDIMGVSNkfdvLLEKVLVEHRE--KPEKDQGtvMLDVL 283
Cdd:PTZ00404 196 GKLAELMGPMEQVFKDLGsgSLFDVIEITQPLYYQYLEHTDKNFKKIKK----FIKEKYHEHLKtiDPEVPRD--LLDLL 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  284 LAAYGDENAEYKITknhIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLH 363
Cdd:PTZ00404 270 IKEYGTNTDDDILS---ILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTV 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  364 AVIKEALRLHPPGPL-LPREFQQGCKIG-GFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSgqederreqa 441
Cdd:PTZ00404 347 AIIKETLRYKPVSPFgLPRSTSNDIIIGgGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSN---------- 416
                        410
                 ....*....|....*....
gi 15231052  442 LKFLPFGSGRRGCPGSNLA 460
Cdd:PTZ00404 417 DAFMPFSIGPRNCVGQQFA 435
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
80-500 2.35e-35

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: 136.62  E-value: 2.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  80 LRIFNVPIILVSSASVAYEIfrTQDVNISSRGVTAVDESLVFGSSSFVTAPyGDYWKFMKKLtvmklLGP----QAQEQS 155
Cdd:cd11051   5 LWPFAPPLLVVTDPELAEQI--TQVTNLPKPPPLRKFLTPLTGGSSLISME-GEEWKRLRKR-----FNPgfspQHLMTL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 156 RDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRGLVT-----ESIGLMKKMFLA 230
Cdd:cd11051  77 VPTILDEVEIFAAILRELAESGEVFSLEELTTNLTFDVIGRVTLDIDLHAQTGDNSLLTALRLllalyRSLLNPFKRLNP 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 231 VLLRRQLQklgislfkkdimgVSNKFDVLLEKVLvehREKPEKDqgtvmldvllaaygdenaeykITKNHIKAFfvdLFI 310
Cdd:cd11051 157 LRPLRRWR-------------NGRRLDRYLKPEV---RKRFELE---------------------RAIDQIKTF---LFA 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 311 GaTDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKS-----RLIQETD--LPNLPYLHAVIKEALRLHPPGPLLpREF 383
Cdd:cd11051 197 G-HDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDpsaaaELLREGPelLNQLPYTTAVIKETLRLFPPAGTA-RRG 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 384 QQGCKI----GGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsGQED-ERREQALKFLPFGSGRRGCPGSN 458
Cdd:cd11051 275 PPGVGLtdrdGKEYPTDGCIVYVCHHAIHRDPEYWPRPDEFIPERWL-----VDEGhELYPPKSAWRPFERGPRNCIGQE 349
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 15231052 459 LAYMIVGSAIGMMVQCFDWRIEGEKVNMKEAVKGTILTM------AHP 500
Cdd:cd11051 350 LAMLELKIILAMTVRRFDFEKAYDEWDAKGGYKGLKELFvtgqgtAHP 397
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
65-497 3.28e-34

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: 134.03  E-value: 3.28e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  65 KSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSsFVTAPyGDYWKfMKKLTVM 144
Cdd:cd11046   1 LDLYKWFLEYGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDKKGLLAEILEPIMGKG-LIPAD-GEIWK-KRRRALV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 145 KLLGPQAQEQSRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFseengeteklrGLVTESIGLM 224
Cdd:cd11046  78 PALHKDYLEMMVRVFGRCSERLMEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDF-----------GSVTEESPVI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 225 KKMFLAVLLRRQLQKLGISLFK----KDIMGVSNKFD---VLLEKVLV-----------EHREKPEKDQGTVMLDV---- 282
Cdd:cd11046 147 KAVYLPLVEAEHRSVWEPPYWDipaaLFIVPRQRKFLrdlKLLNDTLDdlirkrkemrqEEDIELQQEDYLNEDDPsllr 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 283 LLAAYGDENAEYKITKNHIKAFFvdlfIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYL 362
Cdd:cd11046 227 FLVDMRDEDVDSKQLRDDLMTML----IAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYT 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 363 HAVIKEALRLHPPGPLLPREFQQGCKI--GGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLasSRSGQEDERREQ 440
Cdd:cd11046 303 RRVLNESLRLYPQPPVLIRRAVEDDKLpgGGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFL--DPFINPPNEVID 380
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15231052 441 ALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEKVNMKEAVKGTILTM 497
Cdd:cd11046 381 DFAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPRHVGMTTGATIHTK 437
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
74-460 4.26e-34

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: 133.55  E-value: 4.26e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLR-IFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTapYGDYWKFMKKLtvmkLLGPQAQ 152
Cdd:cd11069   1 YGGLIRYRgLFGSERLLVTDPKALKHILVTNSYDFEKPPAFRRLLRRILGDGLLAA--EGEEHKRQRKI----LNPAFSY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 153 EQSRDIRA---DDIKRFCRNLLDKARKKESVEIGKEAMNLMN----NILCKMSMGRSF---SEENGE-TEKLRGLVTESI 221
Cdd:cd11069  75 RHVKELYPifwSKAEELVDKLEEEIEESGDESISIDVLEWLSratlDIIGLAGFGYDFdslENPDNElAEAYRRLFEPTL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 222 GLMKKMFLAVLLRRQLQKLGISLFKKDIMGVSNKFDVLLEKVLVEHREK---PEKDQGTVMLDVLLAAyGDENAEYKITK 298
Cdd:cd11069 155 LGSLLFILLLFLPRWLVRILPWKANREIRRAKDVLRRLAREIIREKKAAlleGKDDSGKDILSILLRA-NDFADDERLSD 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 299 NHIKAFfVDLFIGA-TDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRL--IQETDLPNLPYLHAVIKEALRLHPP 375
Cdd:cd11069 234 EELIDQ-ILTFLAAgHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDgdLSYDDLDRLPYLNAVCRETLRLYPP 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 376 GPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFLAssrsgqEDERREQALK-----FLPFGS 449
Cdd:cd11069 313 VPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLE------PDGAASPGGAgsnyaLLTFLH 386
                       410
                ....*....|.
gi 15231052 450 GRRGCPGSNLA 460
Cdd:cd11069 387 GPRSCIGKKFA 397
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
291-485 9.90e-34

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: 132.32  E-value: 9.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 291 NAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEAL 370
Cdd:cd11058 208 DEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQLPYLNAVIQEAL 287
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 371 RLHPPGPL-LPREF-QQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERREqALKflPFG 448
Cdd:cd11058 288 RLYPPVPAgLPRVVpAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFDNDKKE-AFQ--PFS 364
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15231052 449 SGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEKVN 485
Cdd:cd11058 365 VGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPESED 401
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
80-501 5.29e-33

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: 130.40  E-value: 5.29e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  80 LRIFNVPIILVSSASVAYE-IFRTQDVNISsRGVTAVDESL-VFGSSSFVTApyGDYWKFMKKLTVMKLLGPQAQEQSRD 157
Cdd:cd11064   5 GPWPGGPDGIVTADPANVEhILKTNFDNYP-KGPEFRDLFFdLLGDGIFNVD--GELWKFQRKTASHEFSSRALREFMES 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 158 IRADDIKRFCRNLLDKA-RKKESVEIGKEAMNLMNNILCKMSMG-----RSFSEENGETEK----------LRGLVTESI 221
Cdd:cd11064  82 VVREKVEKLLVPLLDHAaESGKVVDLQDVLQRFTFDVICKIAFGvdpgsLSPSLPEVPFAKafddaseavaKRFIVPPWL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 222 GLMKKmFLAVLLRRQLqklgislfKKDIMGVsnkfDVLLEKVLVEHREKPEKDQGTVM----LDVLLAAYGDENAEYKIT 297
Cdd:cd11064 162 WKLKR-WLNIGSEKKL--------REAIRVI----DDFVYEVISRRREELNSREEENNvredLLSRFLASEEEEGEPVSD 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 298 KnHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVV-----GKSRLIQETDLPNLPYLHAVIKEALRL 372
Cdd:cd11064 229 K-FLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLpklttDESRVPTYEELKKLVYLHAALSESLRL 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 373 HPPGPL----------LPrefqqgckiGGFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFLassrSGQEDERREQA 441
Cdd:cd11064 308 YPPVPFdskeavnddvLP---------DGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWL----DEDGGLRPESP 374
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15231052 442 LKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRI-EGEKVnmkEAVKGTILTMAHPL 501
Cdd:cd11064 375 YKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVvPGHKV---EPKMSLTLHMKGGL 432
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
261-499 1.11e-32

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: 129.21  E-value: 1.11e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 261 EKVLVEHREKP--EKDQGTVMLDVLLAAYGDEnaeyKITKNHIkaffVDLFIGATDTSVQTIQWTMAEIMNNTHILERMR 338
Cdd:cd11063 183 DKALARKEESKdeESSDRYVFLDELAKETRDP----KELRDQL----LNILLAGRDTTASLLSFLFYELARHPEVWAKLR 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 339 EEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL----------LPRefqqgckiGG-------FYIPEKTTLL 401
Cdd:cd11063 255 EEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLnsrvavrdttLPR--------GGgpdgkspIFVPKGTRVL 326
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 402 INAYVVMRDPNVW-EDPEEFKPERFLASSRSGQEderreqalkFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDwRIE 480
Cdd:cd11063 327 YSVYAMHRRKDIWgPDAEEFRPERWEDLKRPGWE---------YLPFNGGPRICLGQQFALTEASYVLVRLLQTFD-RIE 396
                       250
                ....*....|....*....
gi 15231052 481 GEKVnmKEAVKGTILTMAH 499
Cdd:cd11063 397 SRDV--RPPEERLTLTLSN 413
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
65-476 2.09e-32

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: 128.84  E-value: 2.09e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  65 KSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIF----RTQDVnissrgVTAVDESLVFGSSSFVTApYGD--YWKFM 138
Cdd:cd11068   3 QSLLRLADELGPIFKLTLPGRRVVVVSSHDLIAELCdesrFDKKV------SGPLEELRDFAGDGLFTA-YTHepNWGKA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 139 KKLtVMKLLGPQAqeqsrdIRA--DDIKRFCRNLLDK-ARK--KESVEIGKEAMNL-MNNI-LCkmSMGRSF-SEENGE- 209
Cdd:cd11068  76 HRI-LMPAFGPLA------MRGyfPMMLDIAEQLVLKwERLgpDEPIDVPDDMTRLtLDTIaLC--GFGYRFnSFYRDEp 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 210 ----TEKLRGLVTESIGLMKKMFLAVLLRRQLQKlgislFKKDImgvsnkfdVLLEKV---LVEHREKPEKDQGTVMLDV 282
Cdd:cd11068 147 hpfvEAMVRALTEAGRRANRPPILNKLRRRAKRQ-----FREDI--------ALMRDLvdeIIAERRANPDGSPDDLLNL 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 283 LLAA--------YGDENAEYKItknhikaffVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGkSRLIQET 354
Cdd:cd11068 214 MLNGkdpetgekLSDENIRYQM---------ITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLG-DDPPPYE 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 355 DLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFY-IPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFLAssrsG 432
Cdd:cd11068 284 QVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGKYpLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLP----E 359
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 15231052 433 QEDERREQALKflPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFD 476
Cdd:cd11068 360 EFRKLPPNAWK--PFGNGQRACIGRQFALQEATLVLAMLLQRFD 401
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
176-462 3.18e-32

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: 128.15  E-value: 3.18e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 176 KKESVEIGKEAMNLMN-------NILCKMSMGRSFS-EENGETEKLRGLVTESiglmkkmflAVLLRRQLQKLGISLFKK 247
Cdd:cd20660  89 KKLKKEVGKEEFDIFPyitlcalDIICETAMGKSVNaQQNSDSEYVKAVYRMS---------ELVQKRQKNPWLWPDFIY 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 248 DIMGVSNKFDVLLE-------KVLVEHREKPEK--------DQGTV--------MLDVLLAAYGDENaeyKITKNHIKAF 304
Cdd:cd20660 160 SLTPDGREHKKCLKilhgftnKVIQERKAELQKsleeeeedDEDADigkrkrlaFLDLLLEASEEGT---KLSDEDIREE 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 305 fVDLFI-GATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKS-RLIQETDLPNLPYLHAVIKEALRLHPPGPLLPRE 382
Cdd:cd20660 237 -VDTFMfEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSdRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRT 315
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 383 FQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLAssrsgqEDERREQALKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20660 316 LSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLP------ENSAGRHPYAYIPFSAGPRNCIGQKFALM 389
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
74-462 6.39e-32

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: 127.12  E-value: 6.39e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFG--SSSFVTAPYGDYWKFMKKLTVMKL----L 147
Cdd:cd20663   1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGpkSQGVVLARYGPAWREQRRFSVSTLrnfgL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 148 GPQAQEQSR--------DIRADDIKR-FC-RNLLDKArkkesveigkeamnlMNNILCKMSMGRSFSEENGETEKLRGLV 217
Cdd:cd20663  81 GKKSLEQWVteeaghlcAAFTDQAGRpFNpNTLLNKA---------------VCNVIASLIFARRFEYEDPRFIRLLKLL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 218 TESI----GLMKKMF--LAVLLRrqlqklgISLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTVML-DVLLA--AYG 288
Cdd:cd20663 146 EESLkeesGFLPEVLnaFPVLLR-------IPGLAGKVFPGQKAFLALLDELLTEHRTTWDPAQPPRDLtDAFLAemEKA 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 289 DENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKE 368
Cdd:cd20663 219 KGNPESSFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHE 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 369 ALRLHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrSGQEDERREQAlkFLPF 447
Cdd:cd20663 299 VQRFGDIVPLgVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFL----DAQGHFVKPEA--FMPF 372
                       410
                ....*....|....*
gi 15231052 448 GSGRRGCPGSNLAYM 462
Cdd:cd20663 373 SAGRRACLGEPLARM 387
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
310-463 1.20e-31

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: 126.56  E-value: 1.20e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 310 IGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVG-KSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCK 388
Cdd:cd11057 237 FAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPdDGQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQ 316
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231052 389 IG-GFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFLAssrsgqEDERREQALKFLPFGSGRRGCPGSNLAYMI 463
Cdd:cd11057 317 LSnGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLP------ERSAQRHPYAFIPFSAGPRNCIGWRYAMIS 387
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
169-475 5.37e-31

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: 124.76  E-value: 5.37e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 169 NLLDKARKKES-----VEIGKEAMNLMNNILCKMSMGRSFseENGeteklrglvtesiglmKKMFLavlLRRQLQKL--- 240
Cdd:cd11052  98 DMLERWKKQMGeegeeVDVFEEFKALTADIISRTAFGSSY--EEG----------------KEVFK---LLRELQKIcaq 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 241 --------GISLFKKDIMGVSNKFDVLLEKVL---VEHREKPEK-----DQGTVMLDVLLAAYGDENAEYKITKNHI--- 301
Cdd:cd11052 157 anrdvgipGSRFLPTKGNKKIKKLDKEIEDSLleiIKKREDSLKmgrgdDYGDDLLGLLLEANQSDDQNKNMTVQEIvde 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 302 -KAFFvdlFIGATDTSVqTIQWTMAEIMNNTHILERMREEIDSVVGKSrlIQETD-LPNLPYLHAVIKEALRLHPPGPLL 379
Cdd:cd11052 237 cKTFF---FAGHETTAL-LLTWTTMLLAIHPEWQEKAREEVLEVCGKD--KPPSDsLSKLKTVSMVINESLRLYPPAVFL 310
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 380 PREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFLASSRSGqederREQALKFLPFGSGRRGCPGSN 458
Cdd:cd11052 311 TRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGVAKA-----AKHPMAFLPFGLGPRNCIGQN 385
                       330
                ....*....|....*..
gi 15231052 459 LAYMIVGSAIGMMVQCF 475
Cdd:cd11052 386 FATMEAKIVLAMILQRF 402
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
170-462 9.00e-31

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: 124.10  E-value: 9.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 170 LLDKARKKesveIGKEAMNLMN-------NILCKMSMGRSF-SEENGETEKLRGL--VTESIGLMKKM------FLAVLL 233
Cdd:cd20680  98 LVEKLEKH----VDGEAFNCFFditlcalDIICETAMGKKIgAQSNKDSEYVQAVyrMSDIIQRRQKMpwlwldLWYLMF 173
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 234 R------RQLQKLGiSLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAAYGDENAE--YKITKNHIKAFf 305
Cdd:cd20680 174 KegkehnKNLKILH-TFTDNVIAERAEEMKAEEDKTGDSDGESPSKKKRKAFLDMLLSVTDEEGNKlsHEDIREEVDTF- 251
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 306 vdLFIGAtDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKS-RLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQ 384
Cdd:cd20680 252 --MFEGH-DTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSdRPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLC 328
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231052 385 QGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGqedeRREQAlkFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20680 329 EDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSG----RHPYA--YIPFSAGPRNCIGQRFALM 400
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
272-476 9.97e-31

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: 123.59  E-value: 9.97e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 272 EKDQGTVMLDVLLAAYGDENAeykITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRL- 350
Cdd:cd11083 197 LAEAPETLLAMMLAEDDPDAR---LTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVp 273
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 351 IQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSR 430
Cdd:cd11083 274 PLLEALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGAR 353
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15231052 431 SGQEDERREqalkFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFD 476
Cdd:cd11083 354 AAEPHDPSS----LLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFD 395
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
259-478 3.14e-30

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: 122.04  E-value: 3.14e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 259 LLEKVLveHREKPEK--DQGTVMLDVLLAAyGDENAEYKITK---NHikafFVDLFIGATDTSVQTIQWTMAEIMNNTHI 333
Cdd:cd11045 172 YLEEYF--RRRIPERraGGGDDLFSALCRA-EDEDGDRFSDDdivNH----MIFLMMAAHDTTTSTLTSMAYFLARHPEW 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 334 LERMREEIDSVvGKSRLIQEtDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNV 413
Cdd:cd11045 245 QERLREESLAL-GKGTLDYE-DLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEY 322
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231052 414 WEDPEEFKPERFLassrsgqeDERREQA---LKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWR 478
Cdd:cd11045 323 WPNPERFDPERFS--------PERAEDKvhrYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWW 382
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
111-462 9.03e-30

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: 121.07  E-value: 9.03e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 111 GVTAVDESLVFGSSSFVTAPY-----------------GDYWKFMKKLTVMKL----LGPQAQE----QSRDIRADDIKR 165
Cdd:cd20664  19 GYKTVKEALVNHAEAFGGRPIipifedfnkgygilfsnGENWKEMRRFTLTTLrdfgMGKKTSEdkilEEIPYLIEVFEK 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 166 FcrnlldkarKKESVEIgKEAMNL-MNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMflAVLLRRQLQKLGisL 244
Cdd:cd20664  99 H---------KGKPFET-TLSMNVaVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGSP--SVQLYNMFPWLG--P 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 245 FKKDIMGV-SNKFDVL--LEKVLVEHREKPEKDQGTVMLDVLLAAY--GDENAEYKITKNHIKAFFVDLFIGATDTSVQT 319
Cdd:cd20664 165 FPGDINKLlRNTKELNdfLMETFMKHLDVLEPNDQRGFIDAFLVKQqeEEESSDSFFHDDNLTCSVGNLFGAGTDTTGTT 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 320 IQWTMAEIMNNTHILERMREEIDSVVGkSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQQGCKIGGFYIPEKT 398
Cdd:cd20664 245 LRWGLLLMMKYPEIQKKVQEEIDRVIG-SRQPQVEHRKNMPYTDAVIHEIQRFANIVPMnLPHATTRDVTFRGYFIPKGT 323
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231052 399 TLLINAYVVMRDPNVWEDPEEFKPERFLASsrSGQEDERReqalKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20664 324 YVIPLLTSVLQDKTEWEKPEEFNPEHFLDS--QGKFVKRD----AFMPFSAGRRVCIGETLAKM 381
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
67-476 1.01e-29

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: 120.93  E-value: 1.01e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  67 LQKLSSRY---GPLLYLRIFNVPIILVSSASVAYEIFRTQDvNISSRGVTAVDESLVFGSSS-----FVTAPYGDYWKFM 138
Cdd:cd11040   1 LLRNGKKYfsgGPIFTIRLGGQKIYVITDPELISAVFRNPK-TLSFDPIVIVVVGRVFGSPEsakkkEGEPGGKGLIRLL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 139 KKLTVMKLLGPQAQEQSRDIRADDIKRFCRNLLDKArKKESVEIGkeAMNLMNNILCKMSM----GRSFSEENGEteklr 214
Cdd:cd11040  80 HDLHKKALSGGEGLDRLNEAMLENLSKLLDELSLSG-GTSTVEVD--LYEWLRDVLTRATTealfGPKLPELDPD----- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 215 glvtesiglmkkmflavlLRRQLQKLgISLFKKDIMGVSNKF--------DVLLEKVLVEHREKPEKDQGTVmldVLLAA 286
Cdd:cd11040 152 ------------------LVEDFWTF-DRGLPKLLLGLPRLLarkayaarDRLLKALEKYYQAAREERDDGS---ELIRA 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 287 YGDENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQET-----DLPNLPY 361
Cdd:cd11040 210 RAKVLREAGLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAIldltdLLTSCPL 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 362 LHAVIKEALRLHPPGPlLPREFQQGC-KIGGFYIPEKTTLLINAYVVMRDPNVWE-DPEEFKPERFLassRSGQEDERRE 439
Cdd:cd11040 290 LDSTYLETLRLHSSST-SVRLVTEDTvLGGGYLLRKGSLVMIPPRLLHMDPEIWGpDPEEFDPERFL---KKDGDKKGRG 365
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 15231052 440 QALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFD 476
Cdd:cd11040 366 LPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFD 402
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
192-500 1.75e-29

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: 120.50  E-value: 1.75e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 192 NILCKMSMGRSFSEENgetEKLRGLVTesiglMKKMFLAV-----------LLR----RQLQKLgislfkKDImgvSNKF 256
Cdd:cd20676 127 NVICAMCFGKRYSHDD---QELLSLVN-----LSDEFGEVagsgnpadfipILRylpnPAMKRF------KDI---NKRF 189
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 257 DVLLEKVLVEHREKPEKDQGTVMLDVLLA----AYGDENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTH 332
Cdd:cd20676 190 NSFLQKIVKEHYQTFDKDNIRDITDSLIEhcqdKKLDENANIQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPE 269
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 333 ILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDP 411
Cdd:cd20676 270 IQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPFtIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDE 349
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 412 NVWEDPEEFKPERFLasSRSGQEDERREqALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRI-EGEKVNMKeAV 490
Cdd:cd20676 350 KLWKDPSSFRPERFL--TADGTEINKTE-SEKVMLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVpPGVKVDMT-PE 425
                       330
                ....*....|
gi 15231052 491 KGtiLTMAHP 500
Cdd:cd20676 426 YG--LTMKHK 433
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
260-477 2.93e-29

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: 119.70  E-value: 2.93e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 260 LEKVLVEHREKPEKDQGTVmLDVLLAAyGDENAeYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMRE 339
Cdd:cd11044 186 LEQAIRERQEEENAEAKDA-LGLLLEA-KDEDG-EPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQ 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 340 EIDSVVGKSRLIQEtDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEE 419
Cdd:cd11044 263 EQDALGLEEPLTLE-SLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPER 341
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15231052 420 FKPERFLAssrSGQEDERreQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDW 477
Cdd:cd11044 342 FDPERFSP---ARSEDKK--KPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDW 394
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
259-484 8.11e-28

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: 115.85  E-value: 8.11e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 259 LLEKVLVEHREKPEKDQGTVMLDVL-----LAAYGDENAEYKITKNHIKAFFvdlfiGATDTSVQTIQWTMAEIMNNTHI 333
Cdd:cd11041 186 LIIPEIERRRKLKKGPKEDKPNDLLqwlieAAKGEGERTPYDLADRQLALSF-----AAIHTTSMTLTHVLLDLAAHPEY 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 334 LERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQQGCKIG-GFYIPEKTTLLINAYVVMRDP 411
Cdd:cd11041 261 IEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVsLRRKVLKDVTLSdGLTLPKGTRIAVPAHAIHRDP 340
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 412 NVWEDPEEFKPERFLaSSRSGQEDERREQA----LKFLPFGSGRRGCPG----SNLAYMIvgsaIGMMVQCFDWRIEGEK 483
Cdd:cd11041 341 DIYPDPETFDGFRFY-RLREQPGQEKKHQFvstsPDFLGFGHGRHACPGrffaSNEIKLI----LAHLLLNYDFKLPEGG 415

                .
gi 15231052 484 V 484
Cdd:cd11041 416 E 416
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
222-478 9.67e-28

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: 115.20  E-value: 9.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 222 GLMKKMFLAV----LLRRQLQKLGISLFKKDIMgvsNKFDVLLEKVlvehREKPEKDQGTVMLDVLL----AAYGDENAE 293
Cdd:cd20650 148 DFLDPLFLSItvfpFLTPILEKLNISVFPKDVT---NFFYKSVKKI----KESRLDSTQKHRVDFLQlmidSQNSKETES 220
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 294 YKITKNH--IKAFFVDLFIGATDTSvQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALR 371
Cdd:cd20650 221 HKALSDLeiLAQSIIFIFAGYETTS-STLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLR 299
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 372 LHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFlassrsGQEDERREQALKFLPFGSGR 451
Cdd:cd20650 300 LFPIAGRLERVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERF------SKKNKDNIDPYIYLPFGSGP 373
                       250       260
                ....*....|....*....|....*..
gi 15231052 452 RGCPGSNLAYMIVGSAIGMMVQCFDWR 478
Cdd:cd20650 374 RNCIGMRFALMNMKLALVRVLQNFSFK 400
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
306-503 2.15e-26

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: 111.47  E-value: 2.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 306 VDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQ 384
Cdd:cd20667 231 IDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVgAVRQCV 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 385 QGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDErreqalKFLPFGSGRRGCPGSNLAYMIV 464
Cdd:cd20667 311 TSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNE------AFLPFSAGHRVCLGEQLARMEL 384
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 15231052 465 GSAIGMMVQCFDWRI-EGEK-VNMKEAVKGTIltMAHPLKL 503
Cdd:cd20667 385 FIFFTTLLRTFNFQLpEGVQeLNLEYVFGGTL--QPQPYKI 423
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
256-462 2.34e-26

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: 111.25  E-value: 2.34e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 256 FDVLLEKVLvEHREKPEKDQGTVMLDVLLAAYGDE---NAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTH 332
Cdd:cd20675 189 YNFVLDKVL-QHRETLRGGAPRDMMDAFILALEKGksgDSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPD 267
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 333 ILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDP 411
Cdd:cd20675 268 VQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSSFVPVtIPHATTADTSILGYHIPKDTVVFVNQWSVNHDP 347
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15231052 412 NVWEDPEEFKPERFLasSRSGQEDerREQALKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20675 348 QKWPNPEVFDPTRFL--DENGFLN--KDLASSVMIFSVGKRRCIGEELSKM 394
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
220-503 5.46e-26

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: 110.13  E-value: 5.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 220 SIGLMKKMFLAVLLRRQLQKLGISLFKKDIMGVSNKFDV---LLEKVLVEHREKPEKDQGTV--MLDVLLAAYgdenaey 294
Cdd:cd20646 155 SIGEMFKLSEIVTLLPKWTRPYLPFWKRYVDAWDTIFSFgkkLIDKKMEEIEERVDRGEPVEgeYLTYLLSSG------- 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 295 KITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHP 374
Cdd:cd20646 228 KLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYP 307
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 375 PGPLLPREF-QQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassRSGQedeRREQALKFLPFGSGRRG 453
Cdd:cd20646 308 VVPGNARVIvEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWL---RDGG---LKHHPFGSIPFGYGVRA 381
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15231052 454 CPGSNLAYMIVGSAIGMMVQCFDWRIEGEKVNMKeAVKGTILTMAHPLKL 503
Cdd:cd20646 382 CVGRRIAELEMYLALSRLIKRFEVRPDPSGGEVK-AITRTLLVPNKPINL 430
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
74-460 2.81e-25

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: 108.26  E-value: 2.81e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSR------GVTAVDESLVFGSSsfvtapYGDYWKFMKKLtVMKLL 147
Cdd:cd20677   1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRpdfytfSLIANGKSMTFSEK------YGESWKLHKKI-AKNAL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 148 GPQAQEQSRDiraddikRFCRNLLDKARKKESVEIGKEAMNL----------------MNNILCKMSMGRSFSEENGETE 211
Cdd:cd20677  74 RTFSKEEAKS-------STCSCLLEEHVCAEASELVKTLVELskekgsfdpvslitcaVANVVCALCFGKRYDHSDKEFL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 212 KLRGLVTEsiglMKKMFLAVLLRR---QLQKLGISLFKKDIMGVsNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAAYG 288
Cdd:cd20677 147 TIVEINND----LLKASGAGNLADfipILRYLPSPSLKALRKFI-SRLNNFIAKSVQDHYATYDKNHIRDITDALIALCQ 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 289 DENAEYK---ITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAV 365
Cdd:cd20677 222 ERKAEDKsavLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAF 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 366 IKEALRLHPPGPL-LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLasSRSGQEDERREQalKF 444
Cdd:cd20677 302 INEVFRHSSFVPFtIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFL--DENGQLNKSLVE--KV 377
                       410
                ....*....|....*.
gi 15231052 445 LPFGSGRRGCPGSNLA 460
Cdd:cd20677 378 LIFGMGVRKCLGEDVA 393
PLN02738 PLN02738
carotene beta-ring hydroxylase
259-511 9.20e-25

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 108.08  E-value: 9.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  259 LLEKVLVEHREKPEKDQGTVMLDVLLAAyGDEnaeykITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMR 338
Cdd:PLN02738 356 MVEEEELQFHEEYMNERDPSILHFLLAS-GDD-----VSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQ 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  339 EEIDSVVGkSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPE 418
Cdd:PLN02738 430 EEVDSVLG-DRFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAE 508
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  419 EFKPERFlasSRSGQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEKVNMKEAVKGTILTmA 498
Cdd:PLN02738 509 KFNPERW---PLDGPNPNETNQNFSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQLAPGAPPVKMTTGATIHT-T 584
                        250
                 ....*....|....*
gi 15231052  499 HPLKLTpVTR--QPP 511
Cdd:PLN02738 585 EGLKMT-VTRrtKPP 598
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
296-476 9.91e-25

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


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 106.43  E-value: 9.91e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 296 ITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPP 375
Cdd:cd20645 222 LSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPS 301
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 376 GPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqEDERREQALKFLPFGSGRRGCP 455
Cdd:cd20645 302 VPFTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWL-------QEKHSINPFAHVPFGIGKRMCI 374
                       170       180
                ....*....|....*....|.
gi 15231052 456 GSNLAYMIVGSAIGMMVQCFD 476
Cdd:cd20645 375 GRRLAELQLQLALCWIIQKYQ 395
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
322-476 1.26e-24

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: 105.86  E-value: 1.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 322 WTMAEIMNNTHILERMREEIDSVVGKSRL----IQETDLPNLPYLHAVIKEALRLHPPGpLLPREFQQGCKIGGFYIPEK 397
Cdd:cd20635 232 WTLAFILSHPSVYKKVMEEISSVLGKAGKdkikISEDDLKKMPYIKRCVLEAIRLRSPG-AITRKVVKPIKIKNYTIPAG 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 398 TTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgQEDERREQALK-FLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFD 476
Cdd:cd20635 311 DMLMLSPYWAHRNPKYFPDPELFKPERWK------KADLEKNVFLEgFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYD 384
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
192-462 2.35e-24

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: 105.26  E-value: 2.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 192 NILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMFLAVLlrRQLQKLGISL-FKKDIMGVSNKFDVLLEKVLVEHREK 270
Cdd:cd20671 115 NITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLF--NLYPVLGAFLkLHKPILDKVEEVCMILRTLIEARRPT 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 271 PEKDQGTVMLDVLLA-AYGDENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSR 349
Cdd:cd20671 193 IDGNPLHSYIEALIQkQEEDDPKETLFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGC 272
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 350 LIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASs 429
Cdd:cd20671 273 LPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDA- 351
                       250       260       270
                ....*....|....*....|....*....|...
gi 15231052 430 rsgqeDERREQALKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20671 352 -----EGKFVKKEAFLPFSAGRRVCVGESLART 379
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
280-460 2.58e-24

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: 105.44  E-value: 2.58e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 280 LDVLLAAYgDENAEyKITKNHIKAFfVDLFIGAT-DTSVQTIQW---TMAeiMNNTHiLERMREEIDSVVGKSRLIQETD 355
Cdd:cd20678 221 LDILLFAK-DENGK-SLSDEDLRAE-VDTFMFEGhDTTASGISWilyCLA--LHPEH-QQRCREEIREILGDGDSITWEH 294
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 356 LPNLPYLHAVIKEALRLHPPGPLLPRE------FQQGCKiggfyIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASS 429
Cdd:cd20678 295 LDQMPYTTMCIKEALRLYPPVPGISRElskpvtFPDGRS-----LPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPEN 369
                       170       180       190
                ....*....|....*....|....*....|.
gi 15231052 430 RSGqedeRREQAlkFLPFGSGRRGCPGSNLA 460
Cdd:cd20678 370 SSK----RHSHA--FLPFSAGPRNCIGQQFA 394
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
169-479 2.54e-23

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: 102.14  E-value: 2.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 169 NLLDK------ARKKESVEIGKEAMNLMNNILCKMSMGRSFsEENGETEKLRGlvtesiglmKKMFLAVLLRRQLQKLGI 242
Cdd:cd20639  98 DMLDKweamaeAGGEGEVDVAEWFQNLTEDVISRTAFGSSY-EDGKAVFRLQA---------QQMLLAAEAFRKVYIPGY 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 243 SLF--KKDIMgvSNKFDVLLEKVL---VEHREK-----PEKDQGTVMLDVLLAAYGDENaEYKITKNHI----KAFFvdl 308
Cdd:cd20639 168 RFLptKKNRK--SWRLDKEIRKSLlklIERRQTaaddeKDDEDSKDLLGLMISAKNARN-GEKMTVEEIieecKTFF--- 241
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 309 FIGATDTSvQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCK 388
Cdd:cd20639 242 FAGKETTS-NLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLYPPAVATIRRAKKDVK 320
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 389 IGGFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFlassrSGQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSA 467
Cdd:cd20639 321 LGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARF-----ADGVARAAKHPLAFIPFGLGPRTCVGQNLAILEAKLT 395
                       330
                ....*....|..
gi 15231052 468 IGMMVQCFDWRI 479
Cdd:cd20639 396 LAVILQRFEFRL 407
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
122-479 1.58e-22

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: 99.99  E-value: 1.58e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 122 GSSSFVTAPYGDYWKFMKKLTVMKLLGPQA----QEQSRDIRADDIKRFcRNLLDKARKKESVE-----IGKEAMNLMNN 192
Cdd:cd20647  53 GRSTGLISAEGEQWLKMRSVLRQKILRPRDvavySGGVNEVVADLIKRI-KTLRSQEDDGETVTnvndlFFKYSMEGVAT 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 193 ILCKMSMGrsfSEENgETEKLRGLVTESIGLMKKMFLAVL--------LR-------RQLQKLGISLFKKDIMGVSNKFd 257
Cdd:cd20647 132 ILYECRLG---CLEN-EIPKQTVEYIEALELMFSMFKTTMyagaipkwLRpfipkpwEEFCRSWDGLFKFSQIHVDNRL- 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 258 vlleKVLVEHREKPEKDQGTVMLDVLLAAygdenaeyKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERM 337
Cdd:cd20647 207 ----REIQKQMDRGEEVKGGLLTYLLVSK--------ELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQV 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 338 REEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDP 417
Cdd:cd20647 275 YEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRA 354
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231052 418 EEFKPERFLassRSGQEDerREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRI 479
Cdd:cd20647 355 EEFRPERWL---RKDALD--RVDNFGSIPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIKV 411
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
273-460 2.17e-22

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


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 99.77  E-value: 2.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 273 KDQGTVM--LDVLLAAyGDENAEyKITKNHIKAFfVDLFI-GATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVgKSR 349
Cdd:cd20679 217 KAKSKTLdfIDVLLLS-KDEDGK-ELSDEDIRAE-ADTFMfEGHDTTASGLSWILYNLARHPEYQERCRQEVQELL-KDR 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 350 LIQET---DLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKI-GGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERF 425
Cdd:cd20679 293 EPEEIewdDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRF 372
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15231052 426 lassrsGQEDERREQALKFLPFGSGRRGCPGSNLA 460
Cdd:cd20679 373 ------DPENSQGRSPLAFIPFSAGPRNCIGQTFA 401
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
307-462 5.48e-22

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: 98.30  E-value: 5.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 307 DLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQQ 385
Cdd:cd20669 233 NLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMsLPHAVTR 312
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231052 386 GCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDErreqalKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20669 313 DTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKND------AFMPFSAGKRICLGESLARM 383
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
301-460 7.20e-22

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


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 97.86  E-value: 7.20e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 301 IKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLP 380
Cdd:cd20643 235 IKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQ 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 381 REFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqedERREQALKFLPFGSGRRGCPGSNLA 460
Cdd:cd20643 315 RYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWL---------SKDITHFRNLGFGFGPRQCLGRRIA 385
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
74-475 7.65e-22

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: 97.87  E-value: 7.65e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNIS-SRGVTAVDESLvFGSSSF------------VTAP--YGDYWKFM 138
Cdd:cd20640  11 YGPIFTYSTGNKQFLYVSRPEMVKEINLCVSLDLGkPSYLKKTLKPL-FGGGILtsngphwahqrkIIAPefFLDKVKGM 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 139 KKLTV---MKLLGP------QAQEQSRDIRAD-DIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENG 208
Cdd:cd20640  90 VDLMVdsaQPLLSSweeridRAGGMAADIVVDeDLRAFSADVISRACFGSSYSKGKEIFSKLRELQKAVSKQSVLFSIPG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 209 etekLRGLVTESIGLMKKmflavlLRRQLQKLgislfkkdimgvsnkfdvLLEkvLVEHREKPEKDQGTVMLDVLLAAYG 288
Cdd:cd20640 170 ----LRHLPTKSNRKIWE------LEGEIRSL------------------ILE--IVKEREEECDHEKDLLQAILEGARS 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 289 --DENAEYKitknhikAFFVD----LFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVgKSRLIQETDLPNLPYL 362
Cdd:cd20640 220 scDKKAEAE-------DFIVDncknIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVC-KGGPPDADSLSRMKTV 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 363 HAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFlassRSGQEDERREQA 441
Cdd:cd20640 292 TMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERF----SNGVAAACKPPH 367
                       410       420       430
                ....*....|....*....|....*....|....
gi 15231052 442 LkFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCF 475
Cdd:cd20640 368 S-YMPFGAGARTCLGQNFAMAELKVLVSLILSKF 400
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
74-480 1.43e-21

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: 97.00  E-value: 1.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFV--TAPYGDYWKfMKKLTVMKLLGPQA 151
Cdd:cd11066   1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRPTFYTFHKVVSSTQGFTigTSPWDESCK-RRRKAAASALNRPA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 152 QEQSRDIRADDIKRFCRNLL-DKARKKESVEIGKEAMNLMNNILCKMSMGRSFsEENGETEKLRGL--VTESIGLMK--- 225
Cdd:cd11066  80 VQSYAPIIDLESKSFIRELLrDSAEGKGDIDPLIYFQRFSLNLSLTLNYGIRL-DCVDDDSLLLEIieVESAISKFRsts 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 226 ---KMFLAVLlrRQLQKLGISLFKKDIMGvsNKFDVLLEKVLVEHREkpEKDQGTVMLDVLLAAYGDENAeyKITKNHIK 302
Cdd:cd11066 159 snlQDYIPIL--RYFPKMSKFRERADEYR--NRRDKYLKKLLAKLKE--EIEDGTDKPCIVGNILKDKES--KLTDAELQ 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 303 AFFVDLFIGATDTSVQTIQWTMAEIM--NNTHILERMREEIDSVVGKSRLIQETDLPN--LPYLHAVIKEALRLHPPGPL 378
Cdd:cd11066 231 SICLTMVSAGLDTVPLNLNHLIGHLShpPGQEIQEKAYEEILEAYGNDEDAWEDCAAEekCPYVVALVKETLRYFTVLPL 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 379 -LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSrsgqedERREQALKFLPFGSGRRGCPGS 457
Cdd:cd11066 311 gLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDAS------GDLIPGPPHFSFGAGSRMCAGS 384
                       410       420
                ....*....|....*....|...
gi 15231052 458 NLAYMIVGSAIGMMVqcFDWRIE 480
Cdd:cd11066 385 HLANRELYTAICRLI--LLFRIG 405
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
111-462 3.19e-21

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: 96.04  E-value: 3.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 111 GVTAVDESLVFGSSSFVTAP------------------YGDYWKFMKKLTV--MKLLGPQAQEQSRDIRADdikrfCRNL 170
Cdd:cd20661  30 GYDAVKECLVHQSEIFADRPslplfmkltnmggllnskYGRGWTEHRKLAVncFRYFGYGQKSFESKISEE-----CKFF 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 171 LD--KARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMFlaVLLRRQLQKLGISLFKKD 248
Cdd:cd20661 105 LDaiDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAW--VFLYNAFPWIGILPFGKH 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 249 IMGVSNK---FDVLLEKV--LVEHReKPEKDQGtvmldvLLAAYGDE------NAEYKITKNHIKAFFVDLFIGATDTSV 317
Cdd:cd20661 183 QQLFRNAaevYDFLLRLIerFSENR-KPQSPRH------FIDAYLDEmdqnknDPESTFSMENLIFSVGELIIAGTETTT 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 318 QTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQQGCKIGGFYIPE 396
Cdd:cd20661 256 NVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSKDAVVRGYSIPK 335
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15231052 397 KTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDErreqalKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20661 336 GTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKE------AFVPFSLGRRHCLGEQLARM 395
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
132-480 8.33e-21

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: 94.82  E-value: 8.33e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 132 GDYWKFMKKLTVMKLLGPQAQEQSRDIRADDIKRFCRNLLDKARKKES---VEIGKE----AMNLMNNILCKMSMGRSFS 204
Cdd:cd20648  64 GEEWQRLRSLLAKHMLKPKAVEAYAGVLNAVVTDLIRRLRRQRSRSSPgvvKDIAGEfykfGLEGISSVLFESRIGCLEA 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 205 EENGETEKlrglVTESIGlmkKMFLAVLLRRQLQKLGISLFKKDIMGVSNKFDVLLE--KVLVEHREK--------PEKD 274
Cdd:cd20648 144 NVPEETET----FIQSIN---TMFVMTLLTMAMPKWLHRLFPKPWQRFCRSWDQMFAfaKGHIDRRMAevaaklprGEAI 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 275 QGTVMLDVLlaaygdenAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQET 354
Cdd:cd20648 217 EGKYLTYFL--------AREKLPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAA 288
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 355 DLPNLPYLHAVIKEALRLHPPGPLLPREF-QQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGq 433
Cdd:cd20648 289 DVARMPLLKAVVKEVLRLYPVIPGNARVIpDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGDTH- 367
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 15231052 434 ederreQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIE 480
Cdd:cd20648 368 ------HPYASLPFGFGKRSCIGRRIAELEVYLALARILTHFEVRPE 408
PLN02936 PLN02936
epsilon-ring hydroxylase
308-486 1.03e-20

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 94.86  E-value: 1.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  308 LFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGkSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQ-QG 386
Cdd:PLN02936 286 MLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQvED 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  387 CKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASsrSGQEDERREQaLKFLPFGSGRRGCPGSNLAYMIVGS 466
Cdd:PLN02936 365 VLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLD--GPVPNETNTD-FRYIPFSGGPRKCVGDQFALLEAIV 441
                        170       180
                 ....*....|....*....|.
gi 15231052  467 AIGMMVQCFDWR-IEGEKVNM 486
Cdd:PLN02936 442 ALAVLLQRLDLElVPDQDIVM 462
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
259-462 1.06e-20

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: 94.25  E-value: 1.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 259 LLEKVlVEHREKPEKDQGTVMLDVLLAAYGDE--NAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILER 336
Cdd:cd20665 184 ILEKV-KEHQESLDVNNPRDFIDCFLIKMEQEkhNQQSEFTLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAK 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 337 MREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALR---LHPPGplLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNV 413
Cdd:cd20665 263 VQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRyidLVPNN--LPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKE 340
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15231052 414 WEDPEEFKPERFLASSRSGQEDERreqalkFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20665 341 FPNPEKFDPGHFLDENGNFKKSDY------FMPFSAGKRICAGEGLARM 383
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
138-484 4.02e-20

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


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 92.90  E-value: 4.02e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 138 MKKLTVMKLLGPQAQEQSrdiraddIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFsEENGEteklrglV 217
Cdd:cd20641  82 MDKLKSMTQVMADCTERM-------FQEWRKQRNNSETERIEVEVSREFQDLTADIIATTAFGSSY-AEGIE-------V 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 218 TESIGLMKKMFLAVLLRRQL-------QKLGISLFKKDimgvsNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAAY--- 287
Cdd:cd20641 147 FLSQLELQKCAAASLTNLYIpgtqylpTPRNLRVWKLE-----KKVRNSIKRIIDSRLTSEGKGYGDDLLGLMLEAAssn 221
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 288 -GDENAEYKITKNHI----KAFFvdlfIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYL 362
Cdd:cd20641 222 eGGRRTERKMSIDEIidecKTFF----FAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLM 297
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 363 HAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFL-ASSRSGQEderrEQ 440
Cdd:cd20641 298 NMVLMETLRLYGPVINIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFAnGVSRAATH----PN 373
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 15231052 441 ALkfLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEKV 484
Cdd:cd20641 374 AL--LSFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLSPEYV 415
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
258-475 4.91e-20

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: 92.34  E-value: 4.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 258 VLLEKVLVEHREKPEKDQGTVMLDVLlaaygDEnaeykitknhIKAFFvdlFIGATDTSVqTIQWTMAEIMNNTHILERM 337
Cdd:cd20642 211 ILLESNHKEIKEQGNKNGGMSTEDVI-----EE----------CKLFY---FAGQETTSV-LLVWTMVLLSQHPDWQERA 271
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 338 REEIDSVVGKSRLIQEtDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVW-ED 416
Cdd:cd20642 272 REEVLQVFGNNKPDFE-GLNHLKVVTMILYEVLRLYPPVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWgDD 350
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231052 417 PEEFKPERF---LASSRSGQederreqaLKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCF 475
Cdd:cd20642 351 AKEFNPERFaegISKATKGQ--------VSYFPFGWGPRICIGQNFALLEAKMALALILQRF 404
PLN02290 PLN02290
cytokinin trans-hydroxylase
180-479 6.15e-20

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 92.95  E-value: 6.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  180 VEIGKEAMNLMNNILCKMSMGRSFseENG--------ETEKLRGLVTESIGLMKKMFLAVLLRRQLQKLGISL------- 244
Cdd:PLN02290 197 VEIGEYMTRLTADIISRTEFDSSY--EKGkqifhlltVLQRLCAQATRHLCFPGSRFFPSKYNREIKSLKGEVerllmei 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  245 --FKKDI--MGVSNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLaaygDEnaeykitknhIKAFFvdlFIGAtDTSVQTI 320
Cdd:PLN02290 275 iqSRRDCveIGRSSSYGDDLLGMLLNEMEKKRSNGFNLNLQLIM----DE----------CKTFF---FAGH-ETTALLL 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  321 QWTMAEIMNNTHILERMREEIDSVVGksrliQET----DLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPE 396
Cdd:PLN02290 337 TWTLMLLASNPTWQDKVRAEVAEVCG-----GETpsvdHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLHIPK 411
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  397 KTTLLINAYVVMRDPNVW-EDPEEFKPERFLASSRSgqederreQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCF 475
Cdd:PLN02290 412 GLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFA--------PGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKF 483

                 ....
gi 15231052  476 DWRI 479
Cdd:PLN02290 484 SFTI 487
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
74-462 1.35e-19

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: 91.14  E-value: 1.35e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  74 YGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSsfVTAPYGDYWKFMKK--LTVMKLLGpqa 151
Cdd:cd20670   1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIERNFQGHG--VALANGERWRILRRfsLTILRNFG--- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 152 qEQSRDIRaDDIKRFCRNLLDKARKKESVEIGKEAM--NLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMFl 229
Cdd:cd20670  76 -MGKRSIE-ERIQEEAGYLLEEFRKTKGAPIDPTFFlsRTVSNVISSVVFGSRFDYEDKQFLSLLRMINESFIEMSTPW- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 230 avllrRQLQKLgISLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTV-------MLDV-LLAAYGDEN---AEYKItK 298
Cdd:cd20670 153 -----AQLYDM-YSGIMQYLPGRHNRIYYLIEELKDFIASRVKINEASLdpqnprdFIDCfLIKMHQDKNnphTEFNL-K 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 299 NHIKAFfVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL 378
Cdd:cd20670 226 NLVLTT-LNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPL 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 379 -LPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgQEDERREQALKFLPFGSGRRGCPGS 457
Cdd:cd20670 305 gVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFL------DEQGRFKKNEAFVPFSSGKRVCLGE 378

                ....*
gi 15231052 458 NLAYM 462
Cdd:cd20670 379 AMARM 383
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
290-460 1.37e-19

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: 91.44  E-value: 1.37e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 290 ENAEYKITKNHI--KAFFvdLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIK 367
Cdd:cd20649 251 SKQKRMLTEDEIvgQAFI--FLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIA 328
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 368 EALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLAssrsgqEDERREQALKFLPF 447
Cdd:cd20649 329 ETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTA------EAKQRRHPFVYLPF 402
                       170
                ....*....|...
gi 15231052 448 GSGRRGCPGSNLA 460
Cdd:cd20649 403 GAGPRSCIGMRLA 415
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
306-462 3.12e-19

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: 89.86  E-value: 3.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 306 VDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQ 384
Cdd:cd20668 232 LNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMgLARRVT 311
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231052 385 QGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgQEDERREQALKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20668 312 KDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFL------DDKGQFKKSDAFVPFSIGKRYCFGEGLARM 383
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
226-509 1.82e-18

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 88.14  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  226 KMFLAVLLRRQLQKLGISLFKK---DIMGVSNKFDVLL-----EKVLVEHREKPEKDQGTVMLDVllaaygdENAEYKIT 297
Cdd:PLN02169 222 RHFKPVILWRLQNWIGIGLERKmrtALATVNRMFAKIIssrrkEEISRAETEPYSKDALTYYMNV-------DTSKYKLL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  298 KNHIKAFFVD----LFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVvgksrlIQETDLPNLPYLHAVIKEALRLH 373
Cdd:PLN02169 295 KPKKDKFIRDvifsLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTK------FDNEDLEKLVYLHAALSESMRLY 368
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  374 PPgplLPREFQQGCK----IGGFYIPEKTTLLINAYVVMRDPNVW-EDPEEFKPERFLassrSGQEDERREQALKFLPFG 448
Cdd:PLN02169 369 PP---LPFNHKAPAKpdvlPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWI----SDNGGLRHEPSYKFMAFN 441
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231052  449 SGRRGCPGSNLAYMIVGSAIGMMVQCFDWR-IEGEKVnmkEAVKGTILTMAHPLKLTpVTRQ 509
Cdd:PLN02169 442 SGPRTCLGKHLALLQMKIVALEIIKNYDFKvIEGHKI---EAIPSILLRMKHGLKVT-VTKK 499
PLN02302 PLN02302
ent-kaurenoic acid oxidase
122-460 2.23e-18

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 87.85  E-value: 2.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  122 GSSSFVTAPYGDYWKfMKKLTVMKLLGPQAQEQSRDIRADDIKrfcrNLLDKARKKESVEIGKEAMNLMNNILCKMSMGr 201
Cdd:PLN02302 126 GRKSFVGITGEEHKR-LRRLTAAPVNGPEALSTYIPYIEENVK----SCLEKWSKMGEIEFLTELRKLTFKIIMYIFLS- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  202 sfSEENGETEKLRGLVTEsiglmkkmflavlLRRQLQKLGISL----FKKDIMGvSNKFDVLLEKVLVEHR---EKPEKD 274
Cdd:PLN02302 200 --SESELVMEALEREYTT-------------LNYGVRAMAINLpgfaYHRALKA-RKKLVALFQSIVDERRnsrKQNISP 263
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  275 QGTVMLDVLLAAYgDENAEyKITKNHIkaffVDLFI----GATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVgKSRL 350
Cdd:PLN02302 264 RKKDMLDLLLDAE-DENGR-KLDDEEI----IDLLLmylnAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIA-KKRP 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  351 IQET-----DLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERF 425
Cdd:PLN02302 337 PGQKgltlkDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRW 416
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 15231052  426 lassrsgqeDERREQALKFLPFGSGRRGCPGSNLA 460
Cdd:PLN02302 417 ---------DNYTPKAGTFLPFGLGSRLCPGNDLA 442
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
86-460 3.02e-18

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: 87.14  E-value: 3.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  86 PIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTApyGDYWKFMKK--LTVMKLLGpqAQEQSRDIRaddI 163
Cdd:cd20672  13 PVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPIFQGYGVIFAN--GERWKTLRRfsLATMRDFG--MGKRSVEER---I 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 164 KRFCRNLLDKARKKESVEIGKEAM--NLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMFlavllrRQLQKLg 241
Cdd:cd20672  86 QEEAQCLVEELRKSKGALLDPTFLfqSITANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISSFS------SQVFEL- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 242 ISLFKKDIMGVSNKFDVLLEKVL------VE-HREKPEKDQGTVMLDVLLAAYGDENAEYKITKNH--IKAFFVDLFIGA 312
Cdd:cd20672 159 FSGFLKYFPGAHRQIYKNLQEILdyighsVEkHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHqnLMISVLSLFFAG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 313 TDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPL-LPREFQQGCKIGG 391
Cdd:cd20672 239 TETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIgVPHRVTKDTLFRG 318
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231052 392 FYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDErreqalKFLPFGSGRRGCPGSNLA 460
Cdd:cd20672 319 YLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSE------AFMPFSTGKRICLGEGIA 381
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
308-462 3.95e-18

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: 86.34  E-value: 3.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 308 LFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRliQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGC 387
Cdd:cd20614 216 LVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAAGDVPR--TPAELRRFPLAEALFRETLRLHPPVPFVFRRVLEEI 293
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231052 388 KIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqEDERREQALKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd20614 294 ELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWL-------GRDRAPNPVELLQFGGGPHFCLGYHVACV 361
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
308-484 9.55e-18

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: 85.81  E-value: 9.55e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 308 LFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSV----VGKSRL--IQETDLPNLPYLHAVIKEALRLHPPGPLLPR 381
Cdd:cd20622 270 YLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAhpeaVAEGRLptAQEIAQARIPYLDAVIEEILRCANTAPILSR 349
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 382 EFQQGCKIGGFYIPEKTTLLINAY---------------------VVMRDPNVWE--DPEEFKPERFLASSRSGQEDERR 438
Cdd:cd20622 350 EATVDTQVLGYSIPKGTNVFLLNNgpsylsppieidesrrssssaAKGKKAGVWDskDIADFDPERWLVTDEETGETVFD 429
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15231052 439 EQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVqcfdWRIEGEKV 484
Cdd:cd20622 430 PSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLLV----WNFELLPL 471
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
290-509 1.45e-17

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 85.60  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  290 ENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDS--------------------VVGKSR 349
Cdd:PLN03195 282 EDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELKAlekerakeedpedsqsfnqrVTQFAG 361
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  350 LIQETDLPNLPYLHAVIKEALRLHPPGPLLPRE------FQQGCKI--GGF--YIPekttllinaYVVMRDPNVW-EDPE 418
Cdd:PLN03195 362 LLTYDSLGKLQYLHAVITETLRLYPAVPQDPKGileddvLPDGTKVkaGGMvtYVP---------YSMGRMEYNWgPDAA 432
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  419 EFKPERFLASSRSgqedeRREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRI-EGEKVNMKEAvkgTILTM 497
Cdd:PLN03195 433 SFKPERWIKDGVF-----QNASPFKFTAFQAGPRICLGKDSAYLQMKMALALLCRFFKFQLvPGHPVKYRMM---TILSM 504
                        250
                 ....*....|..
gi 15231052  498 AHPLKLTpVTRQ 509
Cdd:PLN03195 505 ANGLKVT-VSRR 515
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
250-480 1.20e-16

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


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 81.36  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 250 MGVSNKFDVLLEKVLVEHREKPekdqGTVMLDVLLAA-YGDEnaeyKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIM 328
Cdd:cd11080 150 LRCAEQLSQYLLPVIEERRVNP----GSDLISILCTAeYEGE----ALSDEDIKALILNVLLAATEPADKTLALMIYHLL 221
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 329 NNTHILERMREEidsvvgksrliqetdlPNLpyLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTL--LINAyv 406
Cdd:cd11080 222 NNPEQLAAVRAD----------------RSL--VPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVfcLIGA-- 281
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231052 407 VMRDPNVWEDPEEFKPER---FLASSRSGqederreqALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCF-DWRIE 480
Cdd:cd11080 282 ANRDPAAFEDPDTFNIHRedlGIRSAFSG--------AADHLAFGSGRHFCVGAALAKREIEIVANQVLDALpNIRLE 351
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
257-460 1.64e-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: 81.81  E-value: 1.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 257 DVLLEKVLVEHREKPEKDQGTVMLDVLLAAygdenaeyKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILER 336
Cdd:cd20644 197 DNCIQKIYQELAFGRPQHYTGIVAELLLQA--------ELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQI 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 337 MREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWED 416
Cdd:cd20644 269 LRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPR 348
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15231052 417 PEEFKPERFLASSRSGqederreQALKFLPFGSGRRGCPGSNLA 460
Cdd:cd20644 349 PERYDPQRWLDIRGSG-------RNFKHLAFGFGMRQCLGRRLA 385
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
335-463 1.22e-15

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: 78.84  E-value: 1.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 335 ERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLL----PREFQQGCKIGGFYIPEKTTLLINAYVVMRD 410
Cdd:cd11071 261 ARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPLQygraRKDFVIESHDASYKIKKGELLVGYQPLATRD 340
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15231052 411 PNVWEDPEEFKPERFLassrsGQEDERreqaLKFLPFGSGR---------RGCPGSNLAYMI 463
Cdd:cd11071 341 PKVFDNPDEFVPDRFM-----GEEGKL----LKHLIWSNGPeteeptpdnKQCPGKDLVVLL 393
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
308-478 2.00e-15

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


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 78.06  E-value: 2.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 308 LFiGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVV-GKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLP----RE 382
Cdd:cd11082 229 LF-ASQDASTSSLVWALQLLADHPDVLAKVREEQARLRpNDEPPLTLDLLEEMKYTRQVVKEVLRYRPPAPMVPhiakKD 307
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 383 FQQGckiGGFYIPeKTTLLInayvvmrdPNVWE-------DPEEFKPERFlasSRSGQEDerREQALKFLPFGSGRRGCP 455
Cdd:cd11082 308 FPLT---EDYTVP-KGTIVI--------PSIYDscfqgfpEPDKFDPDRF---SPERQED--RKYKKNFLVFGAGPHQCV 370
                       170       180
                ....*....|....*....|...
gi 15231052 456 GSNLAYMIVGSAIGMMVQCFDWR 478
Cdd:cd11082 371 GQEYAINHLMLFLALFSTLVDWK 393
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
260-464 1.15e-14

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


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 76.04  E-value: 1.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 260 LEKVLvehREKPEKDQG---TVMLDVLLAAYGDENAEykITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILER 336
Cdd:cd20637 188 LEKAI---REKLQGTQGkdyADALDILIESAKEHGKE--LTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEK 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 337 MREEI--DSVVGKSRLIQET----DLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRD 410
Cdd:cd20637 263 LREELrsNGILHNGCLCEGTlrldTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSVLYSIRDTHDT 342
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15231052 411 PNVWEDPEEFKPERFlassrsGQE-DERREQALKFLPFGSGRRGCPGSNLAYMIV 464
Cdd:cd20637 343 APVFKDVDAFDPDRF------GQErSEDKDGRFHYLPFGGGVRTCLGKQLAKLFL 391
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
314-468 4.76e-14

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: 73.86  E-value: 4.76e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 314 DTSVQTIQWTMAEIMNNTHILERMREEI-----DSVVGKSRLIQETDlpnlPYLHAVIKEALRLHPPGPL-LPREFQQGC 387
Cdd:cd20615 229 DVTTGVLSWNLVFLAANPAVQEKLREEIsaareQSGYPMEDYILSTD----TLLAYCVLESLRLRPLLAFsVPESSPTDK 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 388 KIGGFYIPEKTTLLINAYVV-MRDPNVWEDPEEFKPERFLASSRSgqederreQALK-FLPFGSGRRGCPGSNLAYMIVG 465
Cdd:cd20615 305 IIGGYRIPANTPVVVDTYALnINNPFWGPDGEAYRPERFLGISPT--------DLRYnFWRFGFGPRKCLGQHVADVILK 376

                ...
gi 15231052 466 SAI 468
Cdd:cd20615 377 ALL 379
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
243-481 1.39e-13

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 72.66  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  243 SLFKKDiMGVSNKFDVLLEKVLVEHREKPEKDQgtvmlDVLLAAYGDENAeykITKNHIKAFFVDLFIGATDTSVQTIQW 322
Cdd:PLN02196 216 TLFHKS-MKARKELAQILAKILSKRRQNGSSHN-----DLLGSFMGDKEG---LTDEQIADNIIGVIFAARDTTASVLTW 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  323 TMAEIMNNTHILERMREEIDSVVgKSRLIQET----DLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKT 398
Cdd:PLN02196 287 ILKYLAENPSVLEAVTEEQMAIR-KDKEEGESltweDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGW 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  399 TLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQederreqalkFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWR 478
Cdd:PLN02196 366 KVLPLFRNIHHSADIFSDPGKFDPSRFEVAPKPNT----------FMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWS 435

                 ...
gi 15231052  479 IEG 481
Cdd:PLN02196 436 IVG 438
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
296-468 2.71e-13

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: 71.62  E-value: 2.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 296 ITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKsRLIQETDLPNLPYLHAVIKEALRLHPP 375
Cdd:cd20616 220 LTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGE-RDIQNDDLQKLKVLENFINESMRYQPV 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 376 GPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPnVWEDPEEFKPERFlassrsgqedERREQALKFLPFGSGRRGCP 455
Cdd:cd20616 299 VDFVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENF----------EKNVPSRYFQPFGFGPRSCV 367
                       170
                ....*....|...
gi 15231052 456 GSNLAyMIVGSAI 468
Cdd:cd20616 368 GKYIA-MVMMKAI 379
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
283-487 5.93e-13

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: 70.61  E-value: 5.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 283 LLAAYGDENAEyKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETD------L 356
Cdd:cd20638 214 LLIEHSRRNGE-PLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKGLLSTKPNENKelsmevL 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 357 PNLPYLHAVIKEALRLHPPGPllprefqqgckiGGFYIPEKtTLLINAYVVMRDPNV-------------WEDPEEFKPE 423
Cdd:cd20638 293 EQLKYTGCVIKETLRLSPPVP------------GGFRVALK-TFELNGYQIPKGWNViysicdthdvadiFPNKDEFNPD 359
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15231052 424 RFLAssrSGQEDERReqaLKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEKVNMK 487
Cdd:cd20638 360 RFMS---PLPEDSSR---FSFIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQLLNGPPTMK 417
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
322-515 9.87e-13

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: 69.85  E-value: 9.87e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 322 WTMAEIMNNTHILERMREEIDSVVGKSRLIQEtDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLL 401
Cdd:cd20627 224 WAIYFLTTSEEVQKKLYKEVDQVLGKGPITLE-KIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVL 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 402 INAYVVMRDPNVWEDPEEFKPERFlassrsgqEDERREQALKFLPFgSGRRGCPGSNLAYMIVGSAIGMMVQcfdwrieg 481
Cdd:cd20627 303 YALGVVLQDNTTWPLPYRFDPDRF--------DDESVMKSFSLLGF-SGSQECPELRFAYMVATVLLSVLVR-------- 365
                       170       180       190
                ....*....|....*....|....*....|....
gi 15231052 482 eKVNMkEAVKGTILTMAHPLkltpVTRQPPLTWI 515
Cdd:cd20627 366 -KLRL-LPVDGQVMETKYEL----VTSPREEAWI 393
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
260-479 5.57e-12

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: 67.55  E-value: 5.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 260 LEKVLVEHREKPEKDQGTVMLDVLLAAyGDENAeYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMRE 339
Cdd:cd20636 189 MEKAIEEKLQRQQAAEYCDALDYMIHS-ARENG-KELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQ 266
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 340 EIDS---------VVGKSRLIQetdLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRD 410
Cdd:cd20636 267 ELVShglidqcqcCPGALSLEK---LSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQIPKGWSVMYSIRDTHET 343
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231052 411 PNVWEDPEEFKPERFlassrSGQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRI 479
Cdd:cd20636 344 AAVYQNPEGFDPDRF-----GVEREESKSGRFNYIPFGGGVRSCIGKELAQVILKTLAVELVTTARWEL 407
PLN02774 PLN02774
brassinosteroid-6-oxidase
254-492 6.23e-12

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 67.49  E-value: 6.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  254 NKFDVLLEKVLVEHREKPEKDQGtvMLDVLLAAygdENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHI 333
Cdd:PLN02774 223 KNIVRMLRQLIQERRASGETHTD--MLGYLMRK---EGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKA 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  334 LERMREEIDSVVGKSR---LIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLlinaYVVMR- 409
Cdd:PLN02774 298 LQELRKEHLAIRERKRpedPIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRI----YVYTRe 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  410 ---DPNVWEDPEEFKPERFLASSRSGQEderreqalKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEKVNM 486
Cdd:PLN02774 374 inyDPFLYPDPMTFNPWRWLDKSLESHN--------YFFLFGGGTRLCPGKELGIVEISTFLHYFVTRYRWEEVGGDKLM 445
                        250
                 ....*....|
gi 15231052  487 K----EAVKG 492
Cdd:PLN02774 446 KfprvEAPNG 455
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
264-462 2.40e-11

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


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 65.01  E-value: 2.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 264 LVEHREKPEKDQgtvMLDVLLAAygdENAEYKITKNHIKAFFVDLFIGATDTSvqtiQWTMAEIMnnTHILERmREEIDS 343
Cdd:cd20629 162 LIAERRRAPGDD---LISRLLRA---EVEGEKLDDEEIISFLRLLLPAGSDTT----YRALANLL--TLLLQH-PEQLER 228
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 344 VVGKSRLIQetdlpnlpylhAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFkpe 423
Cdd:cd20629 229 VRRDRSLIP-----------AAIEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVF--- 294
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15231052 424 rflassrsgqeDERREQALKFLpFGSGRRGCPGSNLAYM 462
Cdd:cd20629 295 -----------DIDRKPKPHLV-FGGGAHRCLGEHLARV 321
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
334-478 2.52e-11

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: 65.17  E-value: 2.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 334 LERMREEIDSVVGKsrliqetdlPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNV 413
Cdd:cd20624 225 AARAREEAAVPPGP---------LARPYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRTVPAGTGFLIFAPFFHRDDEA 295
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15231052 414 WEDPEEFKPERFLassrsgqeDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWR 478
Cdd:cd20624 296 LPFADRFVPEIWL--------DGRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEID 352
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
329-482 2.72e-11

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 65.87  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  329 NNTHILERMREEIDSVVGKSR-LIQETDLPNLPYLHAVIKEALRLHPPGPlLPREFQQGCKI--GGFYIPEKTTLLINAY 405
Cdd:PLN02426 322 KHPEVASAIREEADRVMGPNQeAASFEEMKEMHYLHAALYESMRLFPPVQ-FDSKFAAEDDVlpDGTFVAKGTRVTYHPY 400
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231052  406 VVMRDPNVW-EDPEEFKPERFLASSRSgqedeRREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGE 482
Cdd:PLN02426 401 AMGRMERIWgPDCLEFKPERWLKNGVF-----VPENPFKYPVFQAGLRVCLGKEMALMEMKSVAVAVVRRFDIEVVGR 473
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
264-484 3.35e-11

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


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 64.93  E-value: 3.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 264 LVEHREK-PEKDqgtVMLDVLLAAYGDENaeyKITKNHIKAFFVDLFIGATDTSVQTIQWTMaeimnntHILERMREEID 342
Cdd:cd11078 178 LVAERRRePRDD---LISDLLAAADGDGE---RLTDEELVAFLFLLLVAGHETTTNLLGNAV-------KLLLEHPDQWR 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 343 SVVGKSRLIqetdlPNlpylhaVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLI-----NayvvmRDPNVWEDP 417
Cdd:cd11078 245 RLRADPSLI-----PN------AVEETLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLlfgsaN-----RDERVFPDP 308
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15231052 418 EEFkperflassrsgqeDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCF-DWRIEGEKV 484
Cdd:cd11078 309 DRF--------------DIDRPNARKHLTFGHGIHFCLGAALARMEARIALEELLRRLpGMRVPGQEV 362
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
162-477 4.06e-11

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 65.00  E-value: 4.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  162 DIKRFCRNLLDKARKKesVEIGKEAmnlmNNILCKMSMGRSFSEENGE-TEKLRG---LVTESIGLMKKMFLAVLLRRQL 237
Cdd:PLN02987 148 DIDRLIRFNLDSWSSR--VLLMEEA----KKITFELTVKQLMSFDPGEwTESLRKeyvLVIEGFFSVPLPLFSTTYRRAI 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  238 QKLgislfkkdiMGVSNKFDVLLEKVLVEHREKPEKDQGtvMLDVLLAAygDENaeykITKNHIKAFFVDLFIGATDTSv 317
Cdd:PLN02987 222 QAR---------TKVAEALTLVVMKRRKEEEEGAEKKKD--MLAALLAS--DDG----FSDEEIVDFLVALLVAGYETT- 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  318 QTIQWTMAEIMNNTHI-LERMREEIDSVVGK---SRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFY 393
Cdd:PLN02987 284 STIMTLAVKFLTETPLaLAQLKEEHEKIRAMksdSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYT 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  394 IPEKTTLLINAYVVMRDPNVWEDPEEFKPERFlaSSRSGQEDErreqALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQ 473
Cdd:PLN02987 364 IPKGWKVFASFRAVHLDHEYFKDARTFNPWRW--QSNSGTTVP----SNVFTPFGGGPRLCPGYELARVALSVFLHRLVT 437

                 ....
gi 15231052  474 CFDW 477
Cdd:PLN02987 438 RFSW 441
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
322-460 5.10e-10

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: 61.62  E-value: 5.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 322 WTMAEIMNNTHILERMREEIDSVVGKS----RLIQET------DLPNLPYLHAVIKEALRLhPPGPLLPR----EFQQGC 387
Cdd:cd20631 249 WSLFYLLRCPEAMKAATKEVKRTLEKTgqkvSDGGNPivltreQLDDMPVLGSIIKEALRL-SSASLNIRvakeDFTLHL 327
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 388 KIGGFYIPEKTTLlINAY--VVMRDPNVWEDPEEFKPERFLASsrSGQEDE---RREQALK--FLPFGSGRRGCPGSNLA 460
Cdd:cd20631 328 DSGESYAIRKDDI-IALYpqLLHLDPEIYEDPLTFKYDRYLDE--NGKEKTtfyKNGRKLKyyYMPFGSGTSKCPGRFFA 404
PLN02648 PLN02648
allene oxide synthase
335-463 5.68e-10

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 61.49  E-value: 5.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  335 ERMREEIDSVVGKSR-LIQETDLPNLPYLHAVIKEALRLHPPGPL----LPREFQQGCKIGGFYIPEKTTLLINAYVVMR 409
Cdd:PLN02648 308 ARLAEEVRSAVKAGGgGVTFAALEKMPLVKSVVYEALRIEPPVPFqygrAREDFVIESHDAAFEIKKGEMLFGYQPLVTR 387
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15231052  410 DPNVWEDPEEFKPERFLassrsGQEDERreqALKFLPFGSGR---------RGCPGSNLAYMI 463
Cdd:PLN02648 388 DPKVFDRPEEFVPDRFM-----GEEGEK---LLKYVFWSNGRetesptvgnKQCAGKDFVVLV 442
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
361-479 2.00e-09

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


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 59.47  E-value: 2.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 361 YLHAVIKEALRLHPPGPLLP----REFQqgckIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLassrsgqedE 436
Cdd:cd11067 264 YAEAFVQEVRRFYPFFPFVGararRDFE----WQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFL---------G 330
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15231052 437 RREQALKFLPFGSG--RRG--CPGSNLAYMIVGSAIGMMVQCFDWRI 479
Cdd:cd11067 331 WEGDPFDFIPQGGGdhATGhrCPGEWITIALMKEALRLLARRDYYDV 377
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
256-462 4.17e-09

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: 58.37  E-value: 4.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 256 FDVLLEKVlVEHREKPEKDqgtvMLDVLLAAYGDENAeykITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILE 335
Cdd:cd11035 154 LDYLTPLI-AERRANPGDD----LISAILNAEIDGRP---LTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRR 225
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 336 RMREEIDsvvgksrLIQetdlpnlpylhAVIKEALRLHPPgPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWE 415
Cdd:cd11035 226 RLREDPE-------LIP-----------AAVEELLRRYPL-VNVARIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFP 286
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15231052 416 DPEEFKPERflassrsgqederreQALKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd11035 287 DPDTVDFDR---------------KPNRHLAFGAGPHRCLGSHLARL 318
PLN02500 PLN02500
cytochrome P450 90B1
185-479 5.95e-09

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 58.34  E-value: 5.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  185 EAMNLMNNILCKMSMGRSFSEEngETEKLRglvTESIGLMKKMFLAVL------LRRQLQKLGISLfkkdimgvsnKFdv 258
Cdd:PLN02500 179 EAKKFTFNLMAKHIMSMDPGEE--ETEQLK---KEYVTFMKGVVSAPLnfpgtaYRKALKSRATIL----------KF-- 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  259 lLEKVLVEHREKPEKDQGTVMLDVLLaayGDENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMR 338
Cdd:PLN02500 242 -IERKMEERIEKLKEEDESVEEDDLL---GWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELR 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  339 EEIDSVVGKSRLIQET-----DLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNV 413
Cdd:PLN02500 318 EEHLEIARAKKQSGESelnweDYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSL 397
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15231052  414 WEDPEEFKPERFLAS-SRSGQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRI 479
Cdd:PLN02500 398 YDQPQLFNPWRWQQNnNRGGSSGSSSATTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWEL 464
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
143-460 7.08e-09

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: 57.82  E-value: 7.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 143 VMKLLGPQAQEQSRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNIlckmSMGRSFSEENGETEKLRGLVTEsig 222
Cdd:cd20630  69 VRKLVAPAFTPRAIDRLRAEIQAIVDQLLDELGEPEEFDVIREIAEHIPFR----VISAMLGVPAEWDEQFRRFGTA--- 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 223 lMKKMFLAVLLRRQLqklgislfkKDIMGVSNKFDVLLEKVLVEHREKPEKDqgtvmlDVLLAAYGDENAEYKITKNHIK 302
Cdd:cd20630 142 -TIRLLPPGLDPEEL---------ETAAPDVTEGLALIEEVIAERRQAPVED------DLLTTLLRAEEDGERLSEDELM 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 303 AFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEidsvvgksrliqetdlPNLpyLHAVIKEALRLHPPGPL-LPR 381
Cdd:cd20630 206 ALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE----------------PEL--LRNALEEVLRWDNFGKMgTAR 267
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231052 382 EFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSrsgqederreqalkfLPFGSGRRGCPGSNLA 460
Cdd:cd20630 268 YATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRRDPNAN---------------IAFGYGPHFCIGAALA 331
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
67-480 7.58e-09

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 57.83  E-value: 7.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052   67 LQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRtqdvNISSRGVTAVDESL--VFGSSSFVTAPyGDYWKFMKKLTVM 144
Cdd:PLN03141  37 MDKRRSLYGKVFKSHIFGTPTIVSTDAEVNKVVLQ----SDGNAFVPAYPKSLteLMGKSSILLIN-GSLQRRVHGLIGA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  145 KLLGPQAQEQsrdIRADdIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEEngeTEKLRGLVTESI-GL 223
Cdd:PLN03141 112 FLKSPHLKAQ---ITRD-MERYVSESLDSWRDDPPVLVQDETKKIAFEVLVKALISLEPGEE---MEFLKKEFQEFIkGL 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  224 MKK--MFLAVLLRRQLQKlgislfKKDIMGvsnkfdvLLEKVLVEHREK--PEKDQGTV----MLDVLLaayGDENAEyk 295
Cdd:PLN03141 185 MSLpiKLPGTRLYRSLQA------KKRMVK-------LVKKIIEEKRRAmkNKEEDETGipkdVVDVLL---RDGSDE-- 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  296 ITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREE-IDSVVGKSRLIQE---TDLPNLPYLHAVIKEALR 371
Cdd:PLN03141 247 LTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVALQQLTEEnMKLKRLKADTGEPlywTDYMSLPFTQNVITETLR 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052  372 LHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFlassrsgqeDERREQALKFLPFGSGR 451
Cdd:PLN03141 327 MGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRW---------QEKDMNNSSFTPFGGGQ 397
                        410       420
                 ....*....|....*....|....*....
gi 15231052  452 RGCPGSNLAYMIVGSAIGMMVQCFDWRIE 480
Cdd:PLN03141 398 RLCPGLDLARLEASIFLHHLVTRFRWVAE 426
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
365-482 1.73e-08

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


Pssm-ID: 410719  Cd Length: 381  Bit Score: 56.65  E-value: 1.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 365 VIKEALRLHPPGPLLPREFQQgckiGGFYIPEKttllINAYV--VMRDPNVW-EDPEEFKPERFlASSRSGQEDErreqa 441
Cdd:cd20626 261 LVKEALRLYPPTRRIYRAFQR----PGSSKPEI----IAADIeaCHRSESIWgPDALEFNPSRW-SKLTPTQKEA----- 326
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15231052 442 lkFLPFGSGRRGCPG-SNLAYMIVGSAIGMMVQCFD--WRIEGE 482
Cdd:cd20626 327 --FLPFGSGPFRCPAkPVFGPRMIALLVGALLDALGdeWELVSV 368
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
322-483 1.76e-08

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: 56.54  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 322 WTMAEIMNNTHILERMREEIDSVVGKS----------RLIQEtDLPNLPYLHAVIKEALRLHPpGPLLPREFQqgckigg 391
Cdd:cd20632 237 WAMYYLLRHPEALAAVRDEIDHVLQSTgqelgpdfdiHLTRE-QLDSLVYLESAINESLRLSS-ASMNIRVVQ------- 307
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 392 fyipEKTTL--------------LINAY--VVMRDPNVWEDPEEFKPERFLASSRSGQEDERREQALKF--LPFGSGRRG 453
Cdd:cd20632 308 ----EDFTLklesdgsvnlrkgdIVALYpqSLHMDPEIYEDPEVFKFDRFVEDGKKKTTFYKRGQKLKYylMPFGSGSSK 383
                       170       180       190
                ....*....|....*....|....*....|.
gi 15231052 454 CPGSNLAYMIVGSAIGMMVQCFDWRI-EGEK 483
Cdd:cd20632 384 CPGRFFAVNEIKQFLSLLLLYFDLELlEEQK 414
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
321-462 7.77e-08

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 54.28  E-value: 7.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 321 QWTMAE-------IMNNTHILERMREEIDsvvgksRLIQETDLpnlpyLHAVIKEALRLHPPGPLLPREFQQGCKIGGFY 393
Cdd:cd11079 190 NWTVGElgtiaacVGVLVHYLARHPELQA------RLRANPAL-----LPAAIDEILRLDDPFVANRRITTRDVELGGRT 258
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15231052 394 IPEKTTLLINAYVVMRDPNVWEDPEEFKPErflassrsgqederREQALKFLpFGSGRRGCPGSNLAYM 462
Cdd:cd11079 259 IPAGSRVTLNWASANRDERVFGDPDEFDPD--------------RHAADNLV-YGRGIHVCPGAPLARL 312
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
260-462 2.91e-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: 52.72  E-value: 2.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 260 LEKVLVEHREKPEKDqgtVMLDVLLAAYGDEnaeyKITKNHIKAFFVDLFIGATDTSvqtiqwtmAEIMNN------THI 333
Cdd:cd11034 157 LRDLIAERRANPRDD---LISRLIEGEIDGK----PLSDGEVIGFLTLLLLGGTDTT--------SSALSGallwlaQHP 221
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 334 LERmreeidsvvgkSRLIQETDLpnlpyLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYI-PEKTTLLINAyVVMRDPN 412
Cdd:cd11034 222 EDR-----------RRLIADPSL-----IPNAVEEFLRFYSPVAGLARTVTQEVEVGGCRLkPGDRVLLAFA-SANRDEE 284
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15231052 413 VWEDPEEFKPERFlassrsgqedERREqalkfLPFGSGRRGCPGSNLAYM 462
Cdd:cd11034 285 KFEDPDRIDIDRT----------PNRH-----LAFGSGVHRCLGSHLARV 319
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
322-476 8.62e-07

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: 51.30  E-value: 8.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 322 WTMAEIMNNTHILERMREEIDSV-------VGKSRLIQETDLPNLPYLHAVIKEALRLhPPGPLLPREFQQGCKI----- 389
Cdd:cd20634 243 WLLLFLLKHPEAMAAVRGEIQRIkhqrgqpVSQTLTINQELLDNTPVFDSVLSETLRL-TAAPFITREVLQDMKLrladg 321
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 390 GGFYIPEKTTLLINAYVV-MRDPNVWEDPEEFKPERFLASSRSGQED-ERREQALKF--LPFGSGRRGCPGSNLAYMIVG 465
Cdd:cd20634 322 QEYNLRRGDRLCLFPFLSpQMDPEIHQEPEVFKYDRFLNADGTEKKDfYKNGKRLKYynMPWGAGDNVCIGRHFAVNSIK 401
                       170
                ....*....|.
gi 15231052 466 SAIGMMVQCFD 476
Cdd:cd20634 402 QFVFLILTHFD 412
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
364-485 9.71e-07

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: 50.95  E-value: 9.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 364 AVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFkperflassrsgqeDERREQALK 443
Cdd:cd11036 223 AAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRF--------------DLGRPTARS 288
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15231052 444 FlPFGSGRRGCPGSNLAYMIVGSAIGMMVQCF-DWRIEGEKVN 485
Cdd:cd11036 289 A-HFGLGRHACLGAALARAAAAAALRALAARFpGLRAAGPVVR 330
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
322-488 1.72e-06

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: 50.44  E-value: 1.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 322 WTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLP----------NLPYLHAVIKEALRLHPpGPLLPREFQQGCKI-- 389
Cdd:cd20633 246 WLLLYLLKHPEAMKAVREEVEQVLKETGQEVKPGGPlinltrdmllKTPVLDSAVEETLRLTA-APVLIRAVVQDMTLkm 324
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 390 --GGFY-IPEKTTLLINAYV-VMRDPNVWEDPEEFKPERFLASSRSGQED-ERREQALKF--LPFGSGRRGCPGSNLAYM 462
Cdd:cd20633 325 anGREYaLRKGDRLALFPYLaVQMDPEIHPEPHTFKYDRFLNPDGGKKKDfYKNGKKLKYynMPWGAGVSICPGRFFAVN 404
                       170       180
                ....*....|....*....|....*.
gi 15231052 463 IVGSAIGMMVQCFDWriegEKVNMKE 488
Cdd:cd20633 405 EMKQFVFLMLTYFDL----ELVNPDE 426
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
362-460 3.61e-06

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: 49.26  E-value: 3.61e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 362 LHAVIKEALRLHPPGPLLPREFQQGCKI-----GGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERflassrsgqede 436
Cdd:cd20612 240 LRGYVLEALRLNPIAPGLYRRATTDTTVadgggRTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR------------ 307
                        90       100
                ....*....|....*....|....
gi 15231052 437 rreQALKFLPFGSGRRGCPGSNLA 460
Cdd:cd20612 308 ---PLESYIHFGHGPHQCLGEEIA 328
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
264-473 2.16e-05

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: 46.79  E-value: 2.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 264 LVE-HREKPEKDqgtvMLDVLLAAYGDENaeyKITKNHIKAFFVDLFIGATDTsvqtiqwTMAEIMNNTHILERMREEID 342
Cdd:cd11031 176 LVAaRRAEPGDD----LLSALVAARDDDD---RLSEEELVTLAVGLLVAGHET-------TASQIGNGVLLLLRHPEQLA 241
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 343 SVVGKSRLIqetdlPNlpylhAViKEALRLHPPGP--LLPR------EfqqgckIGGFYIPEKTTLLINAYVVMRDPNVW 414
Cdd:cd11031 242 RLRADPELV-----PA-----AV-EELLRYIPLGAggGFPRyatedvE------LGGVTIRAGEAVLVSLNAANRDPEVF 304
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15231052 415 EDPEEFkperflassrsgqeDERREQAlKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQ 473
Cdd:cd11031 305 PDPDRL--------------DLDREPN-PHLAFGHGPHHCLGAPLARLELQVALGALLR 348
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
364-462 1.18e-04

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: 44.51  E-value: 1.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 364 AVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEkttlliNAYVVM------RDPNVWEDPEEFKPERflassrsgqeder 437
Cdd:cd11032 244 GAIEEVLRYRPPVQRTARVTTEDVELGGVTIPA------GQLVIAwlasanRDERQFEDPDTFDIDR------------- 304
                        90       100
                ....*....|....*....|....*
gi 15231052 438 reQALKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd11032 305 --NPNPHLSFGHGIHFCLGAPLARL 327
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
364-462 1.26e-04

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: 44.11  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 364 AVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEkttlliNAYVVM------RDPNVWEDPEEFKPERflassrsgqeder 437
Cdd:cd11037 248 NAFEEAVRLESPVQTFSRTTTRDTELAGVTIPA------GSRVLVflgsanRDPRKWDDPDRFDITR------------- 308
                        90       100
                ....*....|....*....|....*
gi 15231052 438 reQALKFLPFGSGRRGCPGSNLAYM 462
Cdd:cd11037 309 --NPSGHVGFGHGVHACVGQHLARL 331
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
256-473 1.67e-04

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: 44.08  E-value: 1.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 256 FDVLLEKVLVEHREKPekdqGTVMLDVLLAAYGDENaeyKITKNHIKAFFVDLFIGATDTSVQTIqwtmaeiMNNTHILE 335
Cdd:cd20625 164 LAAYFRDLIARRRADP----GDDLISALVAAEEDGD---RLSEDELVANCILLLVAGHETTVNLI-------GNGLLALL 229
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 336 RMREEIDsvvgksRLIQETDLpnLPylhAVIKEALRLHPPGPLLPREFQQGCKIGGFYIP--EKTTLLINAyvVMRDPNV 413
Cdd:cd20625 230 RHPEQLA------LLRADPEL--IP---AAVEELLRYDSPVQLTARVALEDVEIGGQTIPagDRVLLLLGA--ANRDPAV 296
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 414 WEDPEEFKPERflassrsgqEDERReqalkfLPFGSGRRGCPGSNLAYMIVGSAIGMMVQ 473
Cdd:cd20625 297 FPDPDRFDITR---------APNRH------LAFGAGIHFCLGAPLARLEAEIALRALLR 341
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
261-462 9.89e-04

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: 41.36  E-value: 9.89e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 261 EKVLVEHREKPEKDQGTVMLdvllaaygdeNAEY---KITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERM 337
Cdd:cd11033 177 RELAEERRANPGDDLISVLA----------NAEVdgePLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERL 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 338 REEidsvvgksrliqETDLPNLpylhavIKEALRLHPPGPLLPREFQQGCKIGGFYIP--EKttllinayVVM------R 409
Cdd:cd11033 247 RAD------------PSLLPTA------VEEILRWASPVIHFRRTATRDTELGGQRIRagDK--------VVLwyasanR 300
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15231052 410 DPNVWEDPEEF----KPERFLAssrsgqederreqalkflpFGSGRRGCPGSNLAYM 462
Cdd:cd11033 301 DEEVFDDPDRFditrSPNPHLA-------------------FGGGPHFCLGAHLARL 338
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
362-462 2.27e-03

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: 40.21  E-value: 2.27e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15231052 362 LHAVIKEALRLHPPGPLLPREF-QQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERflassrsgqedERREQ 440
Cdd:cd11029 255 WPAAVEELLRYDGPVALATLRFaTEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR-----------DANGH 323
                        90       100
                ....*....|....*....|..
gi 15231052 441 alkfLPFGSGRRGCPGSNLAYM 462
Cdd:cd11029 324 ----LAFGHGIHYCLGAPLARL 341
 
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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