NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|525313655|ref|NP_001265667|]
View 

24-hydroxycholesterol 7-alpha-hydroxylase isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 49-442 0e+00

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: 693.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  49 PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYRT--------------------GKMG 108
Cdd:cd20635    1 PLEFIEKARQKLGPVFTVKAAGERMTFVTDEEDFHVFFKSKDVDFQKAVQDPVQNTasiskesffeyhtkihdmmkGKLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 109 TVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLP 188
Cdd:cd20635   81 SSNLAPLSDKLCEEFKEQLELLGSEGTGDLNDLVRHVMYPAVVNNLFGKGLLPTSEEEIKEFEEHFVKFDEQFEYGSQLP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 189 ECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVEtetsKENSPNYGLLLLWASLSNAVPVAFWTLAY 268
Cdd:cd20635  161 EFFLRDWSSSKQWLLSLFEKVVPDAEKTKPLENNSKTLLQHLLDTVD----KENAPNYSLLLLWASLANAIPITFWTLAF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 269 VLSHPDIHKAIMEGISSVFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLS 348
Cdd:cd20635  237 ILSHPSVYKKVMEEISSVLGKAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSPGAITRKVVKPIKIKNYTIPAGDMLMLS 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 349 PFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLLDPLPKQSY 428
Cdd:cd20635  317 PYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFTLLDPVPKPSP 396

                        410
                 ....*....|....
gi 525313655 429 LHLVGVPQPEGQCR 442
Cdd:cd20635  397 LHLVGTQQPEGPCR 410
 
Name Accession Description Interval E-value
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 49-442 0e+00

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: 693.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  49 PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYRT--------------------GKMG 108
Cdd:cd20635    1 PLEFIEKARQKLGPVFTVKAAGERMTFVTDEEDFHVFFKSKDVDFQKAVQDPVQNTasiskesffeyhtkihdmmkGKLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 109 TVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLP 188
Cdd:cd20635   81 SSNLAPLSDKLCEEFKEQLELLGSEGTGDLNDLVRHVMYPAVVNNLFGKGLLPTSEEEIKEFEEHFVKFDEQFEYGSQLP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 189 ECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVEtetsKENSPNYGLLLLWASLSNAVPVAFWTLAY 268
Cdd:cd20635  161 EFFLRDWSSSKQWLLSLFEKVVPDAEKTKPLENNSKTLLQHLLDTVD----KENAPNYSLLLLWASLANAIPITFWTLAF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 269 VLSHPDIHKAIMEGISSVFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLS 348
Cdd:cd20635  237 ILSHPSVYKKVMEEISSVLGKAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSPGAITRKVVKPIKIKNYTIPAGDMLMLS 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 349 PFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLLDPLPKQSY 428
Cdd:cd20635  317 PYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFTLLDPVPKPSP 396

                        410
                 ....*....|....
gi 525313655 429 LHLVGVPQPEGQCR 442
Cdd:cd20635  397 LHLVGTQQPEGPCR 410
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 35-440 9.01e-41

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: 151.28  E-value: 9.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655   35 WIPWIGVGFEFGKA--PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFE----LAV----------Q 98
Cdd:pfam00067   6 PLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSgrpdEPWfatsrgpflgK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655   99 NIVYRTG-------KMGTVNLHQFTG--------QLTEELHEQL-ENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFST 162
Cdd:pfam00067  86 GIVFANGprwrqlrRFLTPTFTSFGKlsfeprveEEARDLVEKLrKTAGEPGVIDITDLLFRAALNVICSILFGERFGSL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  163 NKKKIKEFHQYFQVYDEDFEYGSQ--------LPECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNS----MTLLQAT 230
Cdd:pfam00067 166 EDPKFLELVKAVQELSSLLSSPSPqlldlfpiLKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAkkspRDFLDAL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  231 LDIVETET----SKENSPNYGLLLLWAS---LSNAVpvaFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLE 303
Cdd:pfam00067 246 LLAKEEEDgsklTDEELRATVLELFFAGtdtTSSTL---SWALYELAKHPEVQEKLREEIDEVIG----DKRSPTYDDLQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  304 NLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE-KHSF 380
Cdd:pfam00067 319 NMPYLDAVIKETLRLHpvVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKfRKSF 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313655  381 ldCFMAFGSGKFQCPARWFALLEVQMCIILILYKYD---CSLLDPLPKQSyLHLVGVPQPEGQ 440
Cdd:pfam00067 399 --AFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEvelPPGTDPPDIDE-TPGLLLPPKPYK 458
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 44-406 1.73e-19

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: 89.95  E-value: 1.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  44 EFGKAPLEFIEKARiKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKV------------DFELAVQNIV---------Y 102
Cdd:COG2124   16 AFLRDPYPFYARLR-EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTfssdgglpevlrPLPLLGDSLLtldgpehtrL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 103 R-------TGKmgtvNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLyPVTVNMlfnkSLFSTNKKKIKEFHQYFQ 175
Cdd:COG2124   95 RrlvqpafTPR----RVAALRPRIREIADELLDRLAARGPVDLVEEFARPL-PVIVIC----ELLGVPEEDRDRLRRWSD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 176 VYdedFEYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKAckSAKDNSMT-LLQATLDivETETSKENSPNYGLLLLWAS 254
Cdd:COG2124  166 AL---LDALGPLPPERRRRARRARAELDAYLRELIAERRA--EPGDDLLSaLLAARDD--GERLSDEELRDELLLLLLAG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 255 L---SNAVPVAFWTLayvLSHPDIHKAIMEGISsvfgkagkdkikvseddlenllLIKWCVLETIRLKAPG-VITRKVVK 330
Cdd:COG2124  239 HettANALAWALYAL---LRHPEQLARLRAEPE----------------------LLPAAVEETLRLYPPVpLLPRTATE 293

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313655 331 PVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAnlekhsfldcFMAFGSGKFQCPARWFALLEVQM 406
Cdd:COG2124  294 DVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDRPPNA----------HLPFGGGPHRCLGAALARLEARI 359
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 23-419 1.34e-18

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 87.82  E-value: 1.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  23 RKNLRRPPCIKGwIPWIGVGFEFGK-APLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFE----LAV 97
Cdd:PLN03234  24 KKSLRLPPGPKG-LPIIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTarplLKG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  98 QNIVYRTG----------------KMGTVNLHQ------FTGQLTEELHEQLENL----GTHGTMDLNNLVRHLLYPVTV 151
Cdd:PLN03234 103 QQTMSYQGrelgfgqytayyremrKMCMVNLFSpnrvasFRPVREEECQRMMDKIykaaDQSGTVDLSELLLSFTNCVVC 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 152 NMLFNKSL--FSTNKKKIKEFHQYFQVYDEDFEYGSQLP-----ECLLRNWSKSKKWFLEL---FEKNIPDIKACKSAKD 221
Cdd:PLN03234 183 RQAFGKRYneYGTEMKRFIDILYETQALLGTLFFSDLFPyfgflDNLTGLSARLKKAFKELdtyLQELLDETLDPNRPKQ 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 222 NSMTLLQATLDIVETET-----SKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIK 296
Cdd:PLN03234 263 ETESFIDLLMQIYKDQPfsikfTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIG----DKGY 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 297 VSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPE-PELFKPERWkka 373
Cdd:PLN03234 339 VSEEDIPNLPYLKAVIKESLRLEPviPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERF--- 415

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525313655 374 nLEKHSFLDC------FMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSL 419
Cdd:PLN03234 416 -MKEHKGVDFkgqdfeLLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSL 466
 
Name Accession Description Interval E-value
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 49-442 0e+00

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: 693.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  49 PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYRT--------------------GKMG 108
Cdd:cd20635    1 PLEFIEKARQKLGPVFTVKAAGERMTFVTDEEDFHVFFKSKDVDFQKAVQDPVQNTasiskesffeyhtkihdmmkGKLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 109 TVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLP 188
Cdd:cd20635   81 SSNLAPLSDKLCEEFKEQLELLGSEGTGDLNDLVRHVMYPAVVNNLFGKGLLPTSEEEIKEFEEHFVKFDEQFEYGSQLP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 189 ECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVEtetsKENSPNYGLLLLWASLSNAVPVAFWTLAY 268
Cdd:cd20635  161 EFFLRDWSSSKQWLLSLFEKVVPDAEKTKPLENNSKTLLQHLLDTVD----KENAPNYSLLLLWASLANAIPITFWTLAF 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 269 VLSHPDIHKAIMEGISSVFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLS 348
Cdd:cd20635  237 ILSHPSVYKKVMEEISSVLGKAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSPGAITRKVVKPIKIKNYTIPAGDMLMLS 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 349 PFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLLDPLPKQSY 428
Cdd:cd20635  317 PYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFTLLDPVPKPSP 396

                        410
                 ....*....|....
gi 525313655 429 LHLVGVPQPEGQCR 442
Cdd:cd20635  397 LHLVGTQQPEGPCR 410
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 53-442 9.63e-89

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: 276.94  E-value: 9.63e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  53 IEKARIKY---GPIFTVFAMGNRMTFVTEEEGINVFLKSKKV-DFELAVQNIVYRTGKM--------------------- 107
Cdd:cd11040    1 LLRNGKKYfsgGPIFTIRLGGQKIYVITDPELISAVFRNPKTlSFDPIVIVVVGRVFGSpesakkkegepggkglirllh 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 108 --------GTVNLHQFTGQLTEELHEQLENLGTHG-----TMDLNNLVRHLLYPVTVNMLFNKSLFSTNkkkiKEFHQYF 174
Cdd:cd11040   81 dlhkkalsGGEGLDRLNEAMLENLSKLLDELSLSGgtstvEVDLYEWLRDVLTRATTEALFGPKLPELD----PDLVEDF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 175 QVYDEDFEYG-SQLPECLLRNWSKSKKWFLELFEKNIPDIKAcksAKDNSMTLLQATLDI-VETETSKENSPNYGLLLLW 252
Cdd:cd11040  157 WTFDRGLPKLlLGLPRLLARKAYAARDRLLKALEKYYQAARE---ERDDGSELIRARAKVlREAGLSEEDIARAELALLW 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 253 ASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKA-GKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKP 331
Cdd:cd11040  234 AINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDsGTNAILDLTDLLTSCPLLDSTYLETLRLHSSSTSVRLVTED 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 332 -VEILNYIIPSGDLLMLSPFWLHRNPKYF-PEPELFKPERWKKANLEK--HSFLDCFMAFGSGKFQCPARWFALLEVQMC 407
Cdd:cd11040  314 tVLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKkgRGLPGAFRPFGGGASLCPGRHFAKNEILAF 393

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 525313655 408 IILILYKYDCSLLD----PLPKQSYLHLVGVPQPEGQCR 442
Cdd:cd11040  394 VALLLSRFDVEPVGggdwKVPGMDESPGLGILPPKRDVR 432
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 35-440 9.01e-41

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: 151.28  E-value: 9.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655   35 WIPWIGVGFEFGKA--PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFE----LAV----------Q 98
Cdd:pfam00067   6 PLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSgrpdEPWfatsrgpflgK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655   99 NIVYRTG-------KMGTVNLHQFTG--------QLTEELHEQL-ENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFST 162
Cdd:pfam00067  86 GIVFANGprwrqlrRFLTPTFTSFGKlsfeprveEEARDLVEKLrKTAGEPGVIDITDLLFRAALNVICSILFGERFGSL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  163 NKKKIKEFHQYFQVYDEDFEYGSQ--------LPECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNS----MTLLQAT 230
Cdd:pfam00067 166 EDPKFLELVKAVQELSSLLSSPSPqlldlfpiLKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAkkspRDFLDAL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  231 LDIVETET----SKENSPNYGLLLLWAS---LSNAVpvaFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLE 303
Cdd:pfam00067 246 LLAKEEEDgsklTDEELRATVLELFFAGtdtTSSTL---SWALYELAKHPEVQEKLREEIDEVIG----DKRSPTYDDLQ 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  304 NLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE-KHSF 380
Cdd:pfam00067 319 NMPYLDAVIKETLRLHpvVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKfRKSF 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313655  381 ldCFMAFGSGKFQCPARWFALLEVQMCIILILYKYD---CSLLDPLPKQSyLHLVGVPQPEGQ 440
Cdd:pfam00067 399 --AFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEvelPPGTDPPDIDE-TPGLLLPPKPYK 458
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 61-439 2.11e-39

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: 146.12  E-value: 2.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  61 GPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDF-----ELAVQNIVYRTGKMGTV------------------NLHQFTG 117
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSsdagpGLPALGDFLGDGLLTLDgpehrrlrrllapaftprALAALRP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 118 QLTEELHEQLENLGTHGTMDLNnlVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLPECLLRNWS- 196
Cdd:cd00302   81 VIREIARELLDRLAAGGEVGDD--VADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLKLLGPRLLRPLPSPRLRRl 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 197 -KSKKWFLELFEKNIpdiKACKSAKDNSMTLLQATLDIVETETSKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDI 275
Cdd:cd00302  159 rRARARLRDYLEELI---ARRRAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLARHPEV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 276 HKAIMEGISSVFGKAgkdkikvSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHR 354
Cdd:cd00302  236 QERLRAEIDAVLGDG-------TPEDLSKLPYLEAVVEETLRLYPPvPLLPRVATEDVELGGYTIPAGTLVLLSLYAAHR 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 355 NPKYFPEPELFKPERWKKANLEKHSfldCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDcSLLDPLPKQSYLHLVGV 434
Cdd:cd00302  309 DPEVFPDPDEFDPERFLPEREEPRY---AHLPFGAGPHRCLGARLARLELKLALATLLRRFD-FELVPDEELEWRPSLGT 384


                 ....*
gi 525313655 435 PQPEG 439
Cdd:cd00302  385 LGPAS 389
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 56-446 4.67e-36

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: 137.35  E-value: 4.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  56 ARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKK---------------------VDFELAVQNIVYRTGK--MGTVNL 112
Cdd:cd11042    1 CRKKYGDVFTFNLLGKKVTVLLGPEANEFFFNGKDedlsaeevygfltppfgggvvYYAPFAEQKEQLKFGLniLRRGKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 113 HQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNkkkikeFHQYFQVYdEDFEYGSQLPECLL 192
Cdd:cd11042   81 RGYVPLIVEEVEKYFAKWGESGEVDLFEEMSELTILTASRCLLGKEVRELL------DDEFAQLY-HDLDGGFTPIAFFF 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 193 RNWS--------KSKKWFLELFEKNIPDIKACKSAKDNSMtlLQATLDIV---ETETSKENSPNYGLLLLWASLSNAVPV 261
Cdd:cd11042  154 PPLPlpsfrrrdRARAKLKEIFSEIIQKRRKSPDKDEDDM--LQTLMDAKykdGRPLTDDEIAGLLIALLFAGQHTSSAT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 262 AFWTLAYVLSHPDIHKAIMEGISSVFGKAGKDkikVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILN--YI 338
Cdd:cd11042  232 SAWTGLELLRNPEHLEALREEQKEVLGDGDDP---LTYDVLKEMPLLHACIKETLRLHPPIHsLMRKARKPFEVEGggYV 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 339 IPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE---KHSFldCFMAFGSGKFQCPARWFALLevQMCIIL--ILY 413
Cdd:cd11042  309 IPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEdskGGKF--AYLPFGAGRHRCIGENFAYL--QIKTILstLLR 384

                        410       420       430
                 ....*....|....*....|....*....|....
gi 525313655 414 KYDCSLLD-PLPKQSYLHLVGVPQpeGQCRIEYK 446
Cdd:cd11042  385 NFDFELVDsPFPEPDYTTMVVWPK--GPARVRYK 416
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 53-422 8.67e-32

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: 126.33  E-value: 8.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  53 IEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLK-SK-KVDFELAVQNIVYRTgkmgtvnlhqFTGQLTEELHEQLENL 130
Cdd:cd20633    1 LQKMQKKHGDIFTVQIGGHYFTFVMDPLSFGAIVKeSKsKLDFGKFASELVLRV----------FGYQPTENDHKMLQTL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 131 G------------THGTMD-LNNLVRHL--------------LYPVTVNMLFNK---SLFST-------NKKKIKE---- 169
Cdd:cd20633   71 StkhlmgdglvvlNQAMMEnLQNLMLHSkgsgdggrewqqdgLFHYSYNIVFRAgylALFGNepdkeagNKEKAKEqdll 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 170 -----FHQyFQVYDEDFE---YGSQLPecllRNWSKSKKwfLELFEKNIPDIKACkSAKDN------SMTLLQATLDIVE 235
Cdd:cd20633  151 hseelFEE-FRKFDQLFPrlaYSVLPP----KDKLEAER--LKRLFWDMLSVSKM-SQKENisgwisEQQRQLAEHGMPE 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 236 TETSKenspnYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKD-KIKVSEDDLENLLLIKWCVL- 313
Cdd:cd20633  223 YMQDR-----FMFLLLWASQGNTGPASFWLLLYLLKHPEAMKAVREEVEQVLKETGQEvKPGGPLINLTRDMLLKTPVLd 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 314 ----ETIRLKAPGVITRKVVKPVEIL-----NYIIPSGDLLMLSPFW-LHRNPKYFPEPELFK------PERWKKANLEK 377
Cdd:cd20633  298 saveETLRLTAAPVLIRAVVQDMTLKmangrEYALRKGDRLALFPYLaVQMDPEIHPEPHTFKydrflnPDGGKKKDFYK 377

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 525313655 378 H--SFLDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLLDP 422
Cdd:cd20633  378 NgkKLKYYNMPWGAGVSICPGRFFAVNEMKQFVFLMLTYFDLELVNP 424
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 52-420 1.05e-30

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: 122.79  E-value: 1.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  52 FIEKARIKYGPIFTVFAMGNRMTFVTEE-EGINVFLKSKKVDFELAVQNIVYRTGKMGTVNLHQFTGqLTEELH------ 124
Cdd:cd20632    1 FLLALQKKHGDVFTVLIAGKYITFIMDPfLYPYVIKHGKQLDFHEFSDRLASKTFGYPPLRSPKFPG-LNEQIHrsyqyl 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 125 --EQLENLGTHGTMDLNNLVRH-------------------LLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEY 183
Cdd:cd20632   80 qgENLDILTESMMGNLQLVLRQqflgetdweteelyefcsrIMFEATFLTLYGKPPDDDRHKVISELRKKFRKFDAMFPY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 184 -GSQLPECLLRNWSKSKKWFLELFEKNipdikacKSAK-DNSMTLLQATLDIVEtetskenspNYGLL-----------L 250
Cdd:cd20632  160 lVANIPIELLGATKSIREKLIKYFLPQ-------KMAKwSNPSEVIQARQELLE---------QYDVLqdydkaahhfaF 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 251 LWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKDK-----IKVSEDDLENLLLIKWCVLETIRLKAPGVIT 325
Cdd:cd20632  224 LWASVGNTIPATFWAMYYLLRHPEALAAVRDEIDHVLQSTGQELgpdfdIHLTREQLDSLVYLESAINESLRLSSASMNI 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 326 RkVVKPVEILN------YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSF------LDCF-MAFGSGKF 392
Cdd:cd20632  304 R-VVQEDFTLKlesdgsVNLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKKTTFykrgqkLKYYlMPFGSGSS 382

                        410       420
                 ....*....|....*....|....*...
gi 525313655 393 QCPARWFALLEVQMCIILILYKYDCSLL 420
Cdd:cd20632  383 KCPGRFFAVNEIKQFLSLLLLYFDLELL 410
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 111-416 1.56e-27

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: 113.78  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 111 NLHQFTGQL---TEELHEQLENLGTHGTMDLNNLvRHLLY----PVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEY 183
Cdd:cd11054   82 SVASYLPAInevADDFVERIRRLRDEDGEEVPDL-EDELYkwslESIGTVLFGKRLGCLDDNPDSDAQKLIEAVKDIFES 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 184 GSQL----PEC----------LLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLdiveteTSKENSPN--YG 247
Cdd:cd11054  161 SAKLmfgpPLWkyfptpawkkFVKAWDTIFDIASKYVDEALEELKKKDEEDEEEDSLLEYLL------SKPGLSKKeiVT 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 248 LL--LLWASL---SNAVPVAFWTLAyvlSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLK--A 320
Cdd:cd11054  235 MAldLLLAGVdttSNTLAFLLYHLA---KNPEVQEKLYEEIRSVLP----DGEPITAEDLKKMPYLKACIKESLRLYpvA 307

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 321 PGvITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW---KKANLEKHSFLdcFMAFGSGKFQCPAR 397
Cdd:cd11054  308 PG-NGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlrdDSENKNIHPFA--SLPFGFGPRMCIGR 384

                        330
                 ....*....|....*....
gi 525313655 398 WFALLEVQMCIILILYKYD 416
Cdd:cd11054  385 RFAELEMYLLLAKLLQNFK 403
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 52-422 1.44e-25

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: 108.23  E-value: 1.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  52 FIEKARIKYGPIFTVFAMGNRMTFVTEEEGI-NVFLKSKKVDFE---LAVQNIVYRTGKM------GTVNLHQF------ 115
Cdd:cd20631    1 FLRSRQKKYGHIFTCKIAGKYVHFITDPFSYhSVIRHGKHLDWKkfhFATSAKAFGHVSFdpsdgnTTENIHDTfiktlq 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 116 ---TGQLTEELHEQLE-----------NLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFS--TNKKKIKEFHQYFQVYDE 179
Cdd:cd20631   81 gsaLDSLTESMMENLQyvmlqdkssssSTKAWVTEGLYSFCYRVMFEAGYLTLFGKELTAreDKNARLEAQRALILNALE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 180 DF-EYGSQLPE-------CLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLD-IVETETSKENspnygLLL 250
Cdd:cd20631  161 NFkEFDKVFPAlvaglpiHMFKTAKSAREALAERLLHENLQKRENISELISLRMLLNDTLStLDEMEKARTH-----VAM 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 251 LWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGK------DKIKVSEDDLENLLLIKWCVLETIRLKAPGVI 324
Cdd:cd20631  236 LWASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEKTGQkvsdggNPIVLTREQLDDMPVLGSIIKEALRLSSASLN 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 325 TRKVVKPVEIL-----NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDC--------FMAFGSGK 391
Cdd:cd20631  316 IRVAKEDFTLHldsgeSYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTFYKngrklkyyYMPFGSGT 395

                        410       420       430
                 ....*....|....*....|....*....|.
gi 525313655 392 FQCPARWFALLEVQMCIILILYKYDCSLLDP 422
Cdd:cd20631  396 SKCPGRFFAINEIKQFLSLMLCYFDMELLDG 426
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 264-427 1.82e-24

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: 104.58  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLaYVLS-HPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPS 341
Cdd:cd20620  234 WTW-YLLAqHPEVAARLRAEVDRVLGGR-----PPTAEDLPQLPYTEMVLQESLRLYPPAwIIGREAVEDDEIGGYRIPA 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDcslL 420
Cdd:cd20620  308 GSTVLISPYVTHRDPRFWPDPEAFDPERFtPEREAARPRY--AYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFR---L 382


                 ....*..
gi 525313655 421 DPLPKQS 427
Cdd:cd20620  383 RLVPGQP 389
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 266-415 5.36e-24

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: 103.43  E-value: 5.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 266 LAYVLS-HPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPSGD 343
Cdd:cd11055  249 ASYLLAtNPDVQEKLIEEIDEVLPDDGS----PTYDTVSKLKYLDMVINETLRLYPPAfFISRECKEDCTINGVFIPKGV 324

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313655 344 LLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSGKFQCPARWFALLEVQMCIILILYKY 415
Cdd:cd11055  325 DVVIPVYAIHHDPEFWPDPEKFDPERFsPENKAKRHPY--AYLPFGAGPRNCIGMRFALLEVKLALVKILQKF 395
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 264-415 7.66e-24

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: 102.99  E-value: 7.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLaYVLS-HPDIHKAIMEGISSVFGKagkDKIKVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPS 341
Cdd:cd20628  251 FTL-YLLGlHPEVQEKVYEELDEIFGD---DDRRPTLEDLNKMKYLERVIKETLRLYPSVpFIGRRLTEDIKLDGYTIPK 326

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSGKFQCPARWFALLEVQMCIILILYKY 415
Cdd:cd20628  327 GTTVVISIYALHRNPEYFPDPEKFDPDRFlPENSAKRHPY--AYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNF 399
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 249-424 5.46e-23

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: 100.41  E-value: 5.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 249 LLLWASLSNAVPVAfWTLaYVLS-HPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRLKAPG-VITR 326
Cdd:cd11049  228 LLTAGTETTASTLA-WAF-HLLArHPEVERRLHAELDAVLGGR-----PATFEDLPRLTYTRRVVTEALRLYPPVwLLTR 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 327 KVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW---KKANLEKHSFLdcfmAFGSGKFQCPARWFALLE 403
Cdd:cd11049  301 RTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWlpgRAAAVPRGAFI----PFGAGARKCIGDTFALTE 376

                        170       180
                 ....*....|....*....|.
gi 525313655 404 VQMCIILILYKYDcslLDPLP 424
Cdd:cd11049  377 LTLALATIASRWR---LRPVP 394
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 127-425 4.54e-22

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: 98.01  E-value: 4.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 127 LENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFE------YGSQLP--ECLLRNWSKS 198
Cdd:cd20618   97 LEESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEAREFKELIDEAFElagafnIGDYIPwlRWLDLQGYEK 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 199 K-----KWFLELFEKNIPDIKACKSAKDNSMTLLQaTLDIVETETSKENSPN---YGLL---LLWASLSNAVPVAfWTLA 267
Cdd:cd20618  177 RmkklhAKLDRFLQKIIEEHREKRGESKKGGDDDD-DLLLLLDLDGEGKLSDdniKALLldmLAAGTDTSAVTIE-WAMA 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 268 YVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPG--VITRKVVKPVEILNYIIPSGDLL 345
Cdd:cd20618  255 ELLRHPEVMRKAQEELDSV---VGRERL-VEESDLPKLPYLQAVVKETLRLHPPGplLLPHESTEDCKVAGYDIPAGTRV 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 346 MLSPFWLHRNPKYFPEPELFKPERWKKANLEK---HSFldCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLLDP 422
Cdd:cd20618  331 LVNVWAIGRDPKVWEDPLEFKPERFLESDIDDvkgQDF--ELLPFGSGRRMCPGMPLGLRMVQLTLANLLHGFDWSLPGP 408


                 ...
gi 525313655 423 LPK 425
Cdd:cd20618  409 KPE 411
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 44-437 1.05e-21

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: 96.58  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  44 EFGKAPLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFL----KSKKVDFELAVQ------NIVYRTGK------- 106
Cdd:cd11044    5 EFLRDPEDFIQSRYQKYGPVFKTHLLGRPTVFVIGAEAVRFILsgegKLVRYGWPRSVRrllgenSLSLQDGEehrrrrk 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 107 -----MGTVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLfnksLFSTNKKKIKEFHQYFQVYDED- 180
Cdd:cd11044   85 llapaFSREALESYVPTIQAIVQSYLRKWLKAGEVALYPELRRLTFDVAARLL----LGLDPEVEAEALSQDFETWTDGl 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 181 FEYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKAC--KSAKDNSMTLLQATLDIVE---TETSKENSpnygLLLLWASL 255
Cdd:cd11044  161 FSLPVPLPFTPFGRAIRARNKLLARLEQAIRERQEEenAEAKDALGLLLEAKDEDGEplsMDELKDQA----LLLLFAGH 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 256 SNAVPVAFWTLAYVLSHPDIHKAImegissvfgKAGKDKIKVSED-DLENLLLIKW--CVL-ETIRLKAP-GVITRKVVK 330
Cdd:cd11044  237 ETTASALTSLCFELAQHPDVLEKL---------RQEQDALGLEEPlTLESLKKMPYldQVIkEVLRLVPPvGGGFRKVLE 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 331 PVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARWFALLEVQMCIIL 410
Cdd:cd11044  308 DFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPFSLIPFGGGPRECLGKEFAQLEMKILASE 387

                        410       420
                 ....*....|....*....|....*...
gi 525313655 411 ILYKYDCSLldpLPKQSY-LHLVGVPQP 437
Cdd:cd11044  388 LLRNYDWEL---LPNQDLePVVVPTPRP 412
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 265-416 1.18e-21

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: 96.45  E-value: 1.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLAYVL----SHPDIHKAIMEGISSVFGKAGKdkiKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEI--LNY 337
Cdd:cd11056  248 TLSFALyelaKNPEIQEKLREEIDEVLEKHGG---ELTYEALQEMKYLDQVVNETLRKYPPlPFLDRVCTKDYTLpgTDV 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 338 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQCPARWFALLEVQMCIILILYKYD 416
Cdd:cd11056  325 VIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKrHPY--TYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFR 402
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 152-424 1.59e-21

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: 96.13  E-value: 1.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 152 NMLFNKSLFSTNKKKIKEFHQYFqvyDEDFEYGSQLPEC---------LLRNWSKSKKWF---LELFEKNIPDIKAcKSA 219
Cdd:cd20617  120 QFLFGKRFPDEDDGEFLKLVKPI---EEIFKELGSGNPSdfipillpfYFLYLKKLKKSYdkiKDFIEKIIEEHLK-TID 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 220 KDNSMTLLQATLDIVETETSKENSPNYGLLLLWASL--------SNAVpvaFWTLAYVLSHPDIHKAIMEGISSVFGKAG 291
Cdd:cd20617  196 PNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDLflagtdttSTTL---EWFLLYLANNPEIQEKIYEEIDNVVGNDR 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 292 KDKIKvsedDLENLLLIKWCVLETIRLKAPGVIT--RKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER 369
Cdd:cd20617  273 RVTLS----DRSKLPYLNAVIKEVLRLRPILPLGlpRVTTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPER 348

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 525313655 370 WKKANLEKHSflDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLLDPLP 424
Cdd:cd20617  349 FLENDGNKLS--EQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKFKSSDGLP 401
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 264-419 4.79e-21

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: 95.12  E-value: 4.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRL-KAPGVITRKVVKPVEI--LNYIIP 340
Cdd:cd11046  262 WTLYELSQNPELMAKVQAEVDAVLG----DRLPPTYEDLKKLKYTRRVLNESLRLyPQPPVLIRRAVEDDKLpgGGVKVP 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 341 SGDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFLD-CFMAFGSGKFQCPARWFALLEVQMCIILILYKYDC 417
Cdd:cd11046  338 AGTDIFISVYNLHRSPELWEDPEEFDPERFldPFINPPNEVIDDfAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDF 417


                 ..
gi 525313655 418 SL 419
Cdd:cd11046  418 EL 419
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 264-416 1.02e-19

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: 90.78  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLA----YVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDDLENLLLIKWCVLETIRLkAPGVITR--KVV--KPVEIL 335
Cdd:cd11062  242 RTLSvatfHLLSNPEILERLREELKTAMPD---PDSPPSLAELEKLPYLTAVIKEGLRL-SYGVPTRlpRVVpdEGLYYK 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 336 NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW----KKANLEKhsfldCFMAFGSGKFQCPARWFALLEVQMCIILI 411
Cdd:cd11062  318 GWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWlgaaEKGKLDR-----YLVPFSKGSRSCLGINLAYAELYLALAAL 392


                 ....*
gi 525313655 412 LYKYD 416
Cdd:cd11062  393 FRRFD 397
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 264-424 1.20e-19

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: 90.72  E-value: 1.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGkdkikvsEDDLENLLLIKWCVLETIRLKAPGVIT-RKVVKPVEILNYIIPSG 342
Cdd:cd11053  245 WAFYWLHRHPEVLARLLAELDALGGDPD-------PEDIAKLPYLDAVIKETLRLYPVAPLVpRRVKEPVELGGYTLPAG 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 343 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSfldcFMAFGSGKFQCPARWFALLEvqMCIIL--ILYKYDCSLL 420
Cdd:cd11053  318 TTVAPSIYLTHHRPDLYPDPERFRPERFLGRKPSPYE----YLPFGGGVRRCIGAAFALLE--MKVVLatLLRRFRLELT 391


                 ....
gi 525313655 421 DPLP 424
Cdd:cd11053  392 DPRP 395
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 44-406 1.73e-19

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: 89.95  E-value: 1.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  44 EFGKAPLEFIEKARiKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKV------------DFELAVQNIV---------Y 102
Cdd:COG2124   16 AFLRDPYPFYARLR-EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTfssdgglpevlrPLPLLGDSLLtldgpehtrL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 103 R-------TGKmgtvNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLyPVTVNMlfnkSLFSTNKKKIKEFHQYFQ 175
Cdd:COG2124   95 RrlvqpafTPR----RVAALRPRIREIADELLDRLAARGPVDLVEEFARPL-PVIVIC----ELLGVPEEDRDRLRRWSD 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 176 VYdedFEYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKAckSAKDNSMT-LLQATLDivETETSKENSPNYGLLLLWAS 254
Cdd:COG2124  166 AL---LDALGPLPPERRRRARRARAELDAYLRELIAERRA--EPGDDLLSaLLAARDD--GERLSDEELRDELLLLLLAG 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 255 L---SNAVPVAFWTLayvLSHPDIHKAIMEGISsvfgkagkdkikvseddlenllLIKWCVLETIRLKAPG-VITRKVVK 330
Cdd:COG2124  239 HettANALAWALYAL---LRHPEQLARLRAEPE----------------------LLPAAVEETLRLYPPVpLLPRTATE 293

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313655 331 PVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAnlekhsfldcFMAFGSGKFQCPARWFALLEVQM 406
Cdd:COG2124  294 DVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDRPPNA----------HLPFGGGPHRCLGAALARLEARI 359
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 210-447 1.74e-19

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: 90.43  E-value: 1.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 210 IPDIKACKSAK-----DNSMTLLQATLDIVETETskENSPN---YGLLLLW-ASLSNAVPVAFWTLAYVLSHPDIHKAIM 280
Cdd:cd11041  188 IPEIERRRKLKkgpkeDKPNDLLQWLIEAAKGEG--ERTPYdlaDRQLALSfAAIHTTSMTLTHVLLDLAAHPEYIEPLR 265

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 281 EGISSVFGKAGKdkikVSEDDLENLLL----IKwcvlETIRLKAPGVIT--RKVVKPVEILN-YIIPSGDLLMLSPFWLH 353
Cdd:cd11041  266 EEIRSVLAEHGG----WTKAALNKLKKldsfMK----ESQRLNPLSLVSlrRKVLKDVTLSDgLTLPKGTRIAVPAHAIH 337

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 354 RNPKYFPEPELFKPERW-----KKANLEKHSFLDC---FMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLLDPL-- 423
Cdd:cd11041  338 RDPDIYPDPETFDGFRFyrlreQPGQEKKHQFVSTspdFLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGer 417

                        250       260
                 ....*....|....*....|....
gi 525313655 424 PKQSYLHLVGVPQPEGQCRIEYKQ 447
Cdd:cd11041  418 PKNIWFGEFIMPDPNAKVLVRRRE 441
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 211-406 2.18e-19

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: 89.99  E-value: 2.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 211 PDIKACK-------SAKDNSMTLLQATLDIVETEtsKENSPNYG--LLLLWASLSNA---VPVAF-WTLAYVLSHPDIHK 277
Cdd:cd11075  189 PLIRARRkrrasgeADKDYTDFLLLDLLDLKEEG--GERKLTDEelVSLCSEFLNAGtdtTATALeWAMAELVKNPEIQE 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 278 AIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKAPG--VITRKVVKPVEILNYIIPSGDLLMLSPFWLHRN 355
Cdd:cd11075  267 KLYEEIKEVVGDEAV----VTEEDLPKMPYLKAVVLETLRRHPPGhfLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRD 342

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 525313655 356 PKYFPEPELFKPERWkkANLEKHSFLDC------FMAFGSGKFQCPARWFALLEVQM 406
Cdd:cd11075  343 PKVWEDPEEFKPERF--LAGGEAADIDTgskeikMMPFGAGRRICPGLGLATLHLEL 397
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 264-410 4.72e-19

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: 88.86  E-value: 4.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDDLENLLLIKWCVLETIRLkAPGV--ITRKVVKPVEILNYIIPS 341
Cdd:cd20660  254 WALYLIGSHPEVQEKVHEELDRIFGD---SDRPATMDDLKEMKYLECVIKEALRL-FPSVpmFGRTLSEDIEIGGYTIPK 329

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQCPARWFALLE--VQMCIIL 410
Cdd:cd20660  330 GTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGrHPY--AYIPFSAGPRNCIGQKFALMEekVVLSSIL 399
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 23-419 1.34e-18

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 87.82  E-value: 1.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  23 RKNLRRPPCIKGwIPWIGVGFEFGK-APLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFE----LAV 97
Cdd:PLN03234  24 KKSLRLPPGPKG-LPIIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTarplLKG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  98 QNIVYRTG----------------KMGTVNLHQ------FTGQLTEELHEQLENL----GTHGTMDLNNLVRHLLYPVTV 151
Cdd:PLN03234 103 QQTMSYQGrelgfgqytayyremrKMCMVNLFSpnrvasFRPVREEECQRMMDKIykaaDQSGTVDLSELLLSFTNCVVC 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 152 NMLFNKSL--FSTNKKKIKEFHQYFQVYDEDFEYGSQLP-----ECLLRNWSKSKKWFLEL---FEKNIPDIKACKSAKD 221
Cdd:PLN03234 183 RQAFGKRYneYGTEMKRFIDILYETQALLGTLFFSDLFPyfgflDNLTGLSARLKKAFKELdtyLQELLDETLDPNRPKQ 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 222 NSMTLLQATLDIVETET-----SKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIK 296
Cdd:PLN03234 263 ETESFIDLLMQIYKDQPfsikfTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIG----DKGY 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 297 VSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPE-PELFKPERWkka 373
Cdd:PLN03234 339 VSEEDIPNLPYLKAVIKESLRLEPviPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERF--- 415

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525313655 374 nLEKHSFLDC------FMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSL 419
Cdd:PLN03234 416 -MKEHKGVDFkgqdfeLLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSL 466
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 248-422 1.42e-18

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: 87.51  E-value: 1.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 248 LLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKDK---IKVSEDDLENLLLIKWCVLETIRLKAPGVI 324
Cdd:cd20634  227 LLQLWATQGNAGPAAFWLLLFLLKHPEAMAAVRGEIQRIKHQRGQPVsqtLTINQELLDNTPVFDSVLSETLRLTAAPFI 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 325 TRKVVKPVEIL-----NYIIPSGDLLMLSPFWL-HRNPKYFPEPELFKPERWKKA-NLEKHSF------LDCF-MAFGSG 390
Cdd:cd20634  307 TREVLQDMKLRladgqEYNLRRGDRLCLFPFLSpQMDPEIHQEPEVFKYDRFLNAdGTEKKDFykngkrLKYYnMPWGAG 386

                        170       180       190
                 ....*....|....*....|....*....|..
gi 525313655 391 KFQCPARWFALLEVQMCIILILYKYDCSLLDP 422
Cdd:cd20634  387 DNVCIGRHFAVNSIKQFVFLILTHFDVELKDP 418
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 199-405 1.76e-18

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: 87.27  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 199 KKWFLELFEKNIPDI-----------------KACKSAKDNSMTLLQATLDIVETETS-----KENSPNYGLLLLWASLS 256
Cdd:cd20655  163 KKLDLQGFGKRIMDVsnrfdelleriikeheeKRKKRKEGGSKDLLDILLDAYEDENAeykitRNHIKAFILDLFIAGTD 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 257 NAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEIL 335
Cdd:cd20655  243 TSAATTEWAMAELINNPEVLEKAREEIDSV---VGKTRL-VQESDLPNLPYLQAVVKETLRLHPPGpLLVRESTEGCKIN 318

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313655 336 NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER-----WKKANLEK--HSFLdcFMAFGSGKFQCPARWFALLEVQ 405
Cdd:cd20655  319 GYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERflassRSGQELDVrgQHFK--LLPFGSGRRGCPGASLAYQVVG 393
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 265-427 1.85e-18

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: 86.89  E-value: 1.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLAYVLSHPDIHKAIMEGISSVFgkAGKDKIKvSEDDLENLLLIKWCVLETIRLK--APGVITRKVVK-PVEILNYIIPS 341
Cdd:cd11061  239 IFYYLARNPEAYEKLRAELDSTF--PSDDEIR-LGPKLKSLPYLRACIDEALRLSppVPSGLPRETPPgGLTIDGEYIPG 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHsfLDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSL 419
Cdd:cd11061  316 GTTVSVPIYSIHRDERYFPDPFEFIPERWlsRPEELVRA--RSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRL 393


                 ....*...
gi 525313655 420 LDPLPKQS 427
Cdd:cd11061  394 APGEDGEA 401
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 264-424 1.98e-18

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: 86.99  E-value: 1.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAgkdKIKVSEDDLENLLLIKWCVLETIRLK--APgVITRKVVKPVEILNYIIPS 341
Cdd:cd11083  244 WMLYYLASRPDVQARVREEVDAVLGGA---RVPPLLEALDRLPYLEAVARETLRLKpvAP-LLFLEPNEDTVVGDIALPA 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GD--LLMLSPFWLhrNPKYFPEPELFKPERW--KKANLEKHSFLDcFMAFGSGKFQCPARWFALLEVQMCIILILYKYDC 417
Cdd:cd11083  320 GTpvFLLTRAAGL--DAEHFPDPEEFDPERWldGARAAEPHDPSS-LLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDI 396


                 ....*..
gi 525313655 418 SLLDPLP 424
Cdd:cd11083  397 ELPEPAP 403
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 264-417 2.81e-18

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: 86.54  E-value: 2.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFgkagKDKIKVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd20621  251 MCLYYLAKYPEIQEKLRQEIKSVV----GNDDDITFEDLQKLNYLNAFIKEVLRLYnpAPFLFPRVATQDHQIGDLKIKK 326

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFLdcFMAFGSGKFQCPARWFALLEVQMCIILILYKYDC 417
Cdd:cd20621  327 GWIVNVGYIYNHFNPKYFENPDEFNPERWlNQNNIEDNPFV--FIPFSAGPRNCIGQHLALMEAKIILIYILKNFEI 401
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 264-416 5.64e-18

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: 85.75  E-value: 5.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSvfgKAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPGVIT--RKVVKPVEILNYIIPS 341
Cdd:cd20654  263 WALSLLLNNPHVLKKAQEELDT---HVGKDRW-VEESDIKNLVYLQAIVKETLRLYPPGPLLgpREATEDCTVGGYHVPK 338

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW----KKANLEKHSFLdcFMAFGSGKFQCPARWFALLEVQMCIILILYKYD 416
Cdd:cd20654  339 GTRLLVNVWKIQRDPNVWSDPLEFKPERFltthKDIDVRGQNFE--LIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFD 415
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 264-416 5.91e-18

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: 85.58  E-value: 5.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkiKVSEDDLENLLLIKWCVLETIRLkAPGV--ITRKVVKPVEILNYIIPS 341
Cdd:cd20680  265 WSLYLLGSHPEVQRKVHKELDEVFGKSDR---PVTMEDLKKLRYLECVIKESLRL-FPSVplFARSLCEDCEIRGFKVPK 340

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQCPARWFALLEVQMCIILILYKYD 416
Cdd:cd20680  341 GVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGrHPY--AYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFW 414
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 262-428 6.39e-18

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: 85.65  E-value: 6.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 262 AFwTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLlliKW--CVL-ETIRLKAP-GVITRKVVKPVEILNY 337
Cdd:cd20613  255 SF-TLLELGRHPEILKRLQAEVDEVLG----SKQYVEYEDLGKL---EYlsQVLkETLRLYPPvPGTSRELTKDIELGGY 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 338 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDC 417
Cdd:cd20613  327 KIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIPSY-AYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKF 405

                        170
                 ....*....|.
gi 525313655 418 SLldpLPKQSY 428
Cdd:cd20613  406 EL---VPGQSF 413
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 265-415 8.48e-18

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: 85.16  E-value: 8.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLAYVL----SHPDIHKAIMEGISSVFgkagKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKP-VEILNYII 339
Cdd:cd20650  247 TLSFLLyelaTHPDVQQKLQEEIDAVL----PNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKdVEINGVFI 322

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313655 340 PSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdCFMAFGSGKFQCPARWFALLEVQMCIILILYKY 415
Cdd:cd20650  323 PKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPY-IYLPFGSGPRNCIGMRFALMNMKLALVRVLQNF 397
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 264-409 9.01e-18

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: 85.01  E-value: 9.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLaYVLS-HPDIHKAIMEGISSVfgKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPS 341
Cdd:cd11069  257 WAL-YLLAkHPDVQERLREEIRAA--LPDPPDGDLSYDDLDRLPYLNAVCRETLRLYPPvPLTSREATKDTVIKGVPIPK 333

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313655 342 GDLLMLSPFWLHRNPK-YFPEPELFKPERW-----KKANLEKHSFlDCFMAFGSGKFQCPARWFALLEVQmCII 409
Cdd:cd11069  334 GTVVLIPPAAINRSPEiWGPDAEEFNPERWlepdgAASPGGAGSN-YALLTFLHGPRSCIGKKFALAEMK-VLL 405
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 264-437 1.02e-17

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: 84.77  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVfgkaGKDKIKVSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 341
Cdd:cd20652  256 WFLLYMALFPKEQRRIQRELDEV----VGRPDLVTLEDLSSLPYLQACISESQRIRSvvPLGIPHGCTEDAVLAGYRIPK 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFldcFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSL 419
Cdd:cd20652  332 GSMIIPLLWAVHMDPNLWEEPEEFRPERFldTDGKYLKPEA---FIPFQTGKRMCLGDELARMILFLFTARILRKFRIAL 408

                        170       180
                 ....*....|....*....|.
gi 525313655 420 LDPLPKQSYLHLVGV---PQP 437
Cdd:cd20652  409 PDGQPVDSEGGNVGItltPPP 429
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 264-422 1.15e-17

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: 84.82  E-value: 1.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDI-HKAIMEgISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIP 340
Cdd:cd11072  250 WAMTELIRNPRVmKKAQEE-VREVVG----GKGKVTEEDLEKLKYLKAVIKETLRLHppAPLLLPRECREDCKINGYDIP 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 341 SGDLLMLSPFWLHRNPKYFPEPELFKPERwkkanlekhsFLDC----------FMAFGSGKFQCPARWFALLEVQMCIIL 410
Cdd:cd11072  325 AKTRVIVNAWAIGRDPKYWEDPEEFRPER----------FLDSsidfkgqdfeLIPFGAGRRICPGITFGLANVELALAN 394

                        170
                 ....*....|..
gi 525313655 411 ILYKYDCSLLDP 422
Cdd:cd11072  395 LLYHFDWKLPDG 406
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 57-410 1.41e-17

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: 84.15  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  57 RIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFEL----AVQNIVYRTGkMGTVN--LH----------------- 113
Cdd:cd11043    2 IKRYGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSwypkSVRKLLGKSS-LLTVSgeEHkrlrglllsflgpealk 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 114 -QFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNkslfSTNKKKIKEFHQYFQvydeDFEYGS-QLPECL 191
Cdd:cd11043   81 dRLLGDIDELVRQHLDSWWRGKSVVVLELAKKMTFELICKLLLG----IDPEEVVEELRKEFQ----AFLEGLlSFPLNL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 192 L-----RNWsKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVETETSK---ENSPNYGLLLLWASLSNAVPVAF 263
Cdd:cd11043  153 PgttfhRAL-KARKRIRKELKKIIEERRAELEKASPKGDLLDVLLEEKDEDGDSltdEEILDNILTLLFAGHETTSTTLT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDI-------HKAIMegissvfgKAGKDKIKVSEDDLENLlliK--WCV-LETIRLK--APGVItRKVVKP 331
Cdd:cd11043  232 LAVKFLAENPKVlqelleeHEEIA--------KRKEEGEGLTWEDYKSM---KytWQViNETLRLApiVPGVF-RKALQD 299

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313655 332 VEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKhSFldCFMAFGSGKFQCPARWFALLEvqMCIIL 410
Cdd:cd11043  300 VEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGV-PY--TFLPFGGGPRLCPGAELAKLE--ILVFL 373
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 118-396 1.78e-17

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


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 84.34  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 118 QLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKK----IKEFHQYFQVYDE-DFEYGSQLPECL- 191
Cdd:cd20658   91 NLVAYVYNMCKKSNGGGLVNVRDAARHYCGNVIRKLMFGTRYFGKGMEDggpgLEEVEHMDAIFTAlKCLYAFSISDYLp 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 192 -LRNWSkskkwfLELFEKNIPD----IKAC---------KSAKDNSMTLLQATLDIVETETSKENSPnygLL-------- 249
Cdd:cd20658  171 fLRGLD------LDGHEKIVREamriIRKYhdpiideriKQWREGKKKEEEDWLDVFITLKDENGNP---LLtpdeikaq 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 250 ---LLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVI 324
Cdd:cd20658  242 ikeLMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRV---VGKERL-VQESDIPNLNYVKACAREAFRLHpvAPFNV 317

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313655 325 TRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE----KHSFLdcFMAFGSGKFQCPA 396
Cdd:cd20658  318 PHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEvtltEPDLR--FISFSTGRRGCPG 391
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 60-424 2.58e-17

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: 83.80  E-value: 2.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  60 YGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDF-----------------ELAVQN----------IVYRTGKMGTVNL 112
Cdd:cd11027    1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFagrpklftfdlfsrggkDIAFGDysptwklhrkLAHSALRLYASGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 113 HQFTGQLTEELHEQLENLGTHG--TMDLNNLVRHLLYPVTVNMLFNKSlFSTNKKKIKEFHQYFQVYDEDFEYGSQ---- 186
Cdd:cd11027   81 PRLEEKIAEEAEKLLKRLASQEgqPFDPKDELFLAVLNVICSITFGKR-YKLDDPEFLRLLDLNDKFFELLGAGSLldif 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 187 -----LPECLLRNWSKSKKWFLELFEK------------NIPDIkacksakdnSMTLLQATLDIvetetSKENSPNYGLL 249
Cdd:cd11027  160 pflkyFPNKALRELKELMKERDEILRKkleehketfdpgNIRDL---------TDALIKAKKEA-----EDEGDEDSGLL 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 250 -----------LLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKvSEDDLENLLLIKWCVLETIRL 318
Cdd:cd11027  226 tddhlvmtisdIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGR---DRLP-TLSDRKRLPYLEATIAEVLRL 301

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 319 K--APGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPA 396
Cdd:cd11027  302 SsvVPLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVPKPESFLPFSAGRRVCLG 381

                        410       420       430
                 ....*....|....*....|....*....|
gi 525313655 397 RWFALLEVQMCIILILYKYD--CSLLDPLP 424
Cdd:cd11027  382 ESLAKAELFLFLARLLQKFRfsPPEGEPPP 411
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 264-395 8.79e-17

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: 81.88  E-value: 8.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDI-HKAIMEgISSvfgKAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIP 340
Cdd:cd20653  249 WAMSNLLNHPEVlKKAREE-IDT---QVGQDRL-IEESDLPKLPYLQNIISETLRLYpaAPLLVPHESSEDCKIGGYDIP 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 525313655 341 SGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSfldcFMAFGSGKFQCP 395
Cdd:cd20653  324 RGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEEREGYK----LIPFGLGRRACP 374
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 265-437 1.32e-16

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: 81.21  E-value: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLAYVLS-HPDIHKAIMEGISSVfgkagkDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSG 342
Cdd:cd11045  233 SMAYFLArHPEWQERLREESLAL------GKGTLDYEDLGQLEVTDWVFKEALRLVPPvPTLPRRAVKDTEVLGYRIPAG 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 343 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE--KHSFLdcFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLL 420
Cdd:cd11045  307 TLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEdkVHRYA--WAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWSV 384

                        170       180
                 ....*....|....*....|
gi 525313655 421 D---PLPKQSYLhlvgvPQP 437
Cdd:cd11045  385 PgyyPPWWQSPL-----PAP 399
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 265-422 4.31e-16

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: 79.93  E-value: 4.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLAYVLSHPDIHKAIMEGISSvFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKP--VEILNYIIPS 341
Cdd:cd11060  245 ILYYLLKNPRVYAKLRAEIDA-AVAEGKLSSPITFAEAQKLPYLQAVIKEALRLHPPvGLPLERVVPPggATICGRFIPG 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWLHRNPKYF-PEPELFKPERWKKANLEKHSFLD-CFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSL 419
Cdd:cd11060  324 GTIVGVNPWVIHRDKEVFgEDADVFRPERWLEADEEQRRMMDrADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFEL 403


                 ...
gi 525313655 420 LDP 422
Cdd:cd11060  404 VDP 406
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 245-412 6.09e-16

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: 79.41  E-value: 6.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 245 NYGLLLLWASLSNAVPVAfWTLAYVLSHPDIHKAIMEGISSVfgkagkDKIKVSEDDLENLLLIKWCVLETIRLKAP-GV 323
Cdd:cd20614  212 NLRLLVLAGHETTASIMA-WMVIMLAEHPAVWDALCDEAAAA------GDVPRTPAELRRFPLAEALFRETLRLHPPvPF 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 324 ITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANlEKHSFLDcFMAFGSGKFQCPARWFALLE 403
Cdd:cd20614  285 VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRD-RAPNPVE-LLQFGGGPHFCLGYHVACVE 362

                        170
                 ....*....|
gi 525313655 404 -VQMCIILIL 412
Cdd:cd20614  363 lVQFIVALAR 372
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 201-425 6.11e-16

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: 79.68  E-value: 6.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 201 WFLELFEKniPDIKACKSAKDNSMTLLQATLDIVETETSKENSPNYGLLLLWAS----------------LSNAVpvaFW 264
Cdd:cd11070  157 PFLDRLPW--VLFPSRKRAFKDVDEFLSELLDEVEAELSADSKGKQGTESVVASrlkrarrsggltekelLGNLF---IF 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLA-------------YVLS-HPDIHKAIMEGISSVFGKAGKDKIKvsEDDLENLLLIKWCVLETIRLKAP-GVITRKVV 329
Cdd:cd11070  232 FIAghettantlsfalYLLAkHPEVQDWLREEIDSVLGDEPDDWDY--EEDFPKLPYLLAVIYETLRLYPPvQLLNRKTT 309

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 330 KPVEILN-----YIIPSGDLLMLSPFWLHRNPKY-FPEPELFKPERW-----KKANLEKHSFLDC-FMAFGSGKFQCPAR 397
Cdd:cd11070  310 EPVVVITglgqeIVIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWgstsgEIGAATRFTPARGaFIPFSAGPRACLGR 389

                        250       260       270
                 ....*....|....*....|....*....|
gi 525313655 398 WFALLEvqMCIIL--ILYKYDCSlLDPLPK 425
Cdd:cd11070  390 KFALVE--FVAALaeLFRQYEWR-VDPEWE 416
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 264-430 8.86e-16

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: 79.03  E-value: 8.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLaYVLS-HPDIHKAIMEGISSVFgkagKDKIKVSEDDLENLLLIKWCVLETIRLKA--PG---VITRKvvkPVEILNY 337
Cdd:cd20648  256 WSL-YELSrHPDVQTALHREITAAL----KDNSVPSAADVARMPLLKAVVKEVLRLYPviPGnarVIPDR---DIQVGEY 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 338 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDcfMAFGSGKFQCPARWFALLEVQMCIILILYKYDc 417
Cdd:cd20648  328 IIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGDTHHPYAS--LPFGFGKRSCIGRRIAELEVYLALARILTHFE- 404

                        170
                 ....*....|...
gi 525313655 418 slLDPLPKQSYLH 430
Cdd:cd20648  405 --VRPEPGGSPVK 415
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 264-422 9.05e-16

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: 78.75  E-value: 9.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSG 342
Cdd:cd20659  249 WTLYSLAKHPEHQQKCREEVDEVLG----DRDDIEWDDLSKLPYLTMCIKESLRLYPPvPFIARTLTKPITIDGVTLPAG 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 343 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSlLD 421
Cdd:cd20659  325 TLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKrDPF--AFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELS-VD 401


                 .
gi 525313655 422 P 422
Cdd:cd20659  402 P 402
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 265-415 1.37e-15

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: 78.50  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLAY----VLSHPDIHKAIMEGISSVFGKAGKDkikVSEDDLENLLLIKWCVLETIRLKA--PGVITRkVVKP--VEILN 336
Cdd:cd11059  240 TLTYliweLSRPPNLQEKLREELAGLPGPFRGP---PDLEDLDKLPYLNAVIRETLRLYPpiPGSLPR-VVPEggATIGG 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 337 YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN----LEKHSFldcFMAFGSGKFQCPARWFALLEVQMCIILIL 412
Cdd:cd11059  316 YYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSgetaREMKRA---FWPFGSGSRMCIGMNLALMEMKLALAAIY 392


                 ...
gi 525313655 413 YKY 415
Cdd:cd11059  393 RNY 395
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 3-423 1.62e-15

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 78.71  E-value: 1.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655   3 LISPTVIIILGCLALFLLLQRKNLRRPPCIKGWiPWIGVGFEFGKAPLEFIEKARIKYGPIFTVfAMGNRMTFVTEEEGI 82
Cdd:PLN03112   8 LLFSVLIFNVLIWRWLNASMRKSLRLPPGPPRW-PIVGNLLQLGPLPHRDLASLCKKYGPLVYL-RLGSVDAITTDDPEL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  83 ---------NVFLKSKKVdfeLAVQNIVYRTGKMG---------------------TVNLHQFTGQLTEELHEQLENLGT 132
Cdd:PLN03112  86 ireillrqdDVFASRPRT---LAAVHLAYGCGDVAlaplgphwkrmrricmehlltTKRLESFAKHRAEEARHLIQDVWE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 133 HG-TMDLNNLvRHLLYPVTVN----MLFNKSLF---STNKKKIKEF----HQYFQ----VYDEDF--EYGSQLPECLLRN 194
Cdd:PLN03112 163 AAqTGKPVNL-REVLGAFSMNnvtrMLLGKQYFgaeSAGPKEAMEFmhitHELFRllgvIYLGDYlpAWRWLDPYGCEKK 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 195 WSKSKKWFLELFEKNIPDIKACKSAKDNS---MTLLQATLDIvETETSKENSPNYGL------LLLWASLSNAVpVAFWT 265
Cdd:PLN03112 242 MREVEKRVDEFHDKIIDEHRRARSGKLPGgkdMDFVDVLLSL-PGENGKEHMDDVEIkalmqdMIAAATDTSAV-TNEWA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 266 LAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPSGD 343
Cdd:PLN03112 320 MAEVIKNPRVLRKIQEELDSV---VGRNRM-VQESDLVHLNYLRCVVRETFRMHpaGPFLIPHESLRATTINGYYIPAKT 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 344 LLMLSPFWLHRNPKYFPEPELFKPER-W--KKANLEKHSFLDC-FMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSL 419
Cdd:PLN03112 396 RVFINTHGLGRNTKIWDDVEEFRPERhWpaEGSRVEISHGPDFkILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSP 475


                 ....
gi 525313655 420 LDPL 423
Cdd:PLN03112 476 PDGL 479
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 264-416 2.87e-15

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


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 77.37  E-value: 2.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKAPGVI---TRKVVKPVEILNYIIP 340
Cdd:cd11076  246 WIMARMVLHPDIQSKAQAEIDAAVGGSRR----VADSDVAKLPYLQAVVKETLRLHPPGPLlswARLAIHDVTVGGHVVP 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 341 SGDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFL--DCFMA-FGSGKFQCPARWFALLEVQMCIILILYKYD 416
Cdd:cd11076  322 AGTTAMVNMWAITHDPHVWEDPLEFKPERFvAAEGGADVSVLgsDLRLApFGAGRRVCPGKALGLATVHLWVAQLLHEFE 401
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 264-395 4.65e-15

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: 76.80  E-value: 4.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd11073  253 WAMAELLRNPEKMAKARAELDEVIGK---DKI-VEESDISKLPYLQAVVKETLRLHppAPLLLPRKAEEDVEVMGYTIPK 328

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERwkkanlekhsFLDC----------FMAFGSGKFQCP 395
Cdd:cd11073  329 GTQVLVNVWAIGRDPSVWEDPLEFKPER----------FLGSeidfkgrdfeLIPFGSGRRICP 382
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 118-412 5.07e-15

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: 76.49  E-value: 5.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 118 QLTEELHEQLENLgthgtmdLNNLVRHLLYPVTVNMLFNKSL------------FSTNKKKIKE----FHQYFQVYDEDF 181
Cdd:cd20651   79 SMEEVIQEEAEEL-------IDLLKKGEKGPIQMPDLFNVSVlnvlwamvagerYSLEDQKLRKllelVHLLFRNFDMSG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 182 EYGSQLPecLLR----NWSK------SKKWFLELFEKNIPDIKAcKSAKDNSMTLLQATLDIVETETSKENSPNY----- 246
Cdd:cd20651  152 GLLNQFP--WLRfiapEFSGynllveLNQKLIEFLKEEIKEHKK-TYDEDNPRDLIDAYLREMKKKEPPSSSFTDdqlvm 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 247 GLL-LLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKvSEDDLENLLLIKWCVLETIRLK--APGV 323
Cdd:cd20651  229 ICLdLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGR---DRLP-TLDDRSKLPYTEAVILEVLRIFtlVPIG 304

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 324 ITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANlEKHSFLDCFMAFGSGKFQCPARWFAlle 403
Cdd:cd20651  305 IPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDED-GKLLKDEWFLPFGAGKRRCLGESLA--- 380


                 ....*....
gi 525313655 404 vQMCIILIL 412
Cdd:cd20651  381 -RNELFLFF 388
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 29-422 5.20e-15

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 76.90  E-value: 5.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  29 PPCIKGWiPWIGVGFE-FGKAPLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFE----------LAV 97
Cdd:PLN02196  37 PPGTMGW-PYVGETFQlYSQDPNVFFASKQKRYGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLFKptfpaskermLGK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  98 QNIVYRTG----KMGTVNLHQFTGQLTEELHEQLENLGTH------GTMdLNNLVRHLLYPVTVNMLfnkSLFSTNKKKI 167
Cdd:PLN02196 116 QAIFFHQGdyhaKLRKLVLRAFMPDAIRNMVPDIESIAQEslnsweGTQ-INTYQEMKTYTFNVALL---SIFGKDEVLY 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 168 KE-FHQYFQVYDEDfeYGS---QLPECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNsmtLLQATLDIVETETSKENS 243
Cdd:PLN02196 192 REdLKRCYYILEKG--YNSmpiNLPGTLFHKSMKARKELAQILAKILSKRRQNGSSHND---LLGSFMGDKEGLTDEQIA 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 244 PNYgLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFgKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGV 323
Cdd:PLN02196 267 DNI-IGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIR-KDKEEGESLTWEDTKKMPLTSRVIQETLRVASILS 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 324 IT-RKVVKPVEILNYIIPSGDLLMlsPFW--LHRNPKYFPEPELFKPERWKKANLEkhsflDCFMAFGSGKFQCPARWFA 400
Cdd:PLN02196 345 FTfREAVEDVEYEGYLIPKGWKVL--PLFrnIHHSADIFSDPGKFDPSRFEVAPKP-----NTFMPFGNGTHSCPGNELA 417

                        410       420
                 ....*....|....*....|..
gi 525313655 401 LLEVQMCIILILYKYDCSLLDP 422
Cdd:PLN02196 418 KLEISVLIHHLTTKYRWSIVGT 439
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 187-416 1.13e-14

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: 75.69  E-value: 1.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 187 LPECLLRNW-SKSKKWF---LELFEKNIPDIK---ACKSAKDNSMTLLQATLDIVETETSKENSPNYGLLLLWASLSNAV 259
Cdd:cd11065  162 LPSWLGAPWkRKARELReltRRLYEGPFEAAKermASGTATPSFVKDLLEELDKEGGLSEEEIKYLAGSLYEAGSDTTAS 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 260 PVAFWTLAYVLsHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNY 337
Cdd:cd11065  242 TLQTFILAMAL-HPEVQKKAQEELDRV---VGPDRL-PTFEDRPNLPYVNAIVKEVLRWRpvAPLGIPHALTEDDEYEGY 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 338 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDC-FMAFGSGKFQCPARWFALLEVQMCIILILYKYD 416
Cdd:cd11065  317 FIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPDPpHFAFGFGRRICPGRHLAENSLFIAIARLLWAFD 396
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 264-412 2.80e-14

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: 74.37  E-value: 2.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKVseddLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILNYIIPSG 342
Cdd:cd20643  256 WTLYELARNPNVQEMLRAEVLAARQEAQGDMVKM----LKSVPLLKAAIKETLRLHPVAVsLQRYITEDLVLQNYHIPAG 331

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 343 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdcfmAFGSGKFQCPARWFALLEVQMCIILIL 412
Cdd:cd20643  332 TLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRNL----GFGFGPRQCLGRRIAETEMQLFLIHML 397
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 256-412 3.22e-14

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: 74.11  E-value: 3.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 256 SNAVPVAFwTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKVseddLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEI 334
Cdd:cd20644  247 TTAFPLLF-TLFELARNPDVQQILRQESLAAAAQISEHPQKA----LTELPLLKAALKETLRLYPVGItVQRVPSSDLVL 321

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313655 335 LNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDcfMAFGSGKFQCPARWFALLEVQMCIILIL 412
Cdd:cd20644  322 QNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKH--LAFGFGMRQCLGRRLAEAEMLLLLMHVL 397
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 264-432 5.21e-14

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: 73.46  E-value: 5.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILN-YIIPS 341
Cdd:cd20678  261 WILYCLALHPEHQQRCREEIREILG----DGDSITWEHLDQMPYTTMCIKEALRLYPPVPgISRELSKPVTFPDgRSLPA 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSlL 420
Cdd:cd20678  337 GITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKrHSH--AFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFELL-P 413

                        170
                 ....*....|....
gi 525313655 421 DP--LPKQSyLHLV 432
Cdd:cd20678  414 DPtrIPIPI-PQLV 426
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 256-415 1.47e-13

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: 72.18  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 256 SNAVPVAFWTLAyvlSHPDIHKAIMEGISSVFGKagkdKIKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEI 334
Cdd:cd20649  278 TNTLSFATYLLA---THPECQKKLLREVDEFFSK----HEMVDYANVQELPYLDMVIAETLRMYPPAFrFAREAAEDCVV 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 335 LNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFLdcFMAFGSGKFQCPARWFALLEVQMCIILILY 413
Cdd:cd20649  351 LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFtAEAKQRRHPFV--YLPFGAGPRSCIGMRLALLEIKVTLLHILR 428


                 ..
gi 525313655 414 KY 415
Cdd:cd20649  429 RF 430
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 264-401 2.62e-13

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 71.69  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 341
Cdd:PLN02394 315 WGIAELVNHPEIQKKLRDELDTVLGPGNQ----VTEPDTHKLPYLQAVVKETLRLHMaiPLLVPHMNLEDAKLGGYDIPA 390

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFLDCFMAFGSGKFQCPARWFAL 401
Cdd:PLN02394 391 ESKILVNAWWLANNPELWKNPEEFRPERFleEEAKVEANGNDFRFLPFGVGRRSCPGIILAL 452
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 262-416 2.63e-13

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: 71.45  E-value: 2.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 262 AFwTLAYVLSHPDIHKAIMEGISSVFGKAGkdkikVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILN-YII 339
Cdd:cd11068  251 SF-ALYYLLKNPEVLAKARAEVDEVLGDDP-----PPYEQVAKLRYIRRVLDETLRLWPTApAFARKPKEDTVLGGkYPL 324

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313655 340 PSGD-LLMLSPFwLHRNPK-YFPEPELFKPERWKKANLEKHSfLDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYD 416
Cdd:cd11068  325 KKGDpVLVLLPA-LHRDPSvWGEDAEEFRPERFLPEEFRKLP-PNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFD 401
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 264-407 3.36e-13

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: 71.17  E-value: 3.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd11028  253 WSLLYMIRYPEIQEKVQAELDRVIGRERLPRL----SDRPNLPYTEAFILETMRHSsfVPFTIPHATTRDTTLNGYFIPK 328

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKhSFLDCFMAFGSGKFQCP----ARW-----FALLeVQMC 407
Cdd:cd11028  329 GTVVFVNLWSVNHDEKLWPDPSVFRPERFldDNGLLDK-TKVDKFLPFGAGRRRCLgeelARMelflfFATL-LQQC 403
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 264-430 5.15e-13

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: 70.22  E-value: 5.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDdLENLLLIKWCVLETIRLkAPGV--ITRKVVKPVEILNYIIPS 341
Cdd:cd20645  248 WILYNLSRNPQAQQKLLQEIQSVLPA---NQTPRAED-LKNMPYLKACLKESMRL-TPSVpfTSRTLDKDTVLGDYLLPK 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKanlEKHSfLDCF--MAFGSGKFQCPARWFALLEVQMCIILILYKYDCSL 419
Cdd:cd20645  323 GTVLMINSQALGSSEEYFEDGRQFKPERWLQ---EKHS-INPFahVPFGIGKRMCIGRRLAELQLQLALCWIIQKYQIVA 398

                        170
                 ....*....|.
gi 525313655 420 LDPLPKQSyLH 430
Cdd:cd20645  399 TDNEPVEM-LH 408
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 264-419 8.86e-13

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: 69.68  E-value: 8.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILNYIIPSG 342
Cdd:cd11052  254 WTTMLLAIHPEWQEKAREEVLEVCGKD-----KPPSDSLSKLKTVSMVINESLRLYPPAVfLTRKAKEDIKLGGLVIPKG 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 343 DLLMLSPFWLHRNPKYFPE-PELFKPERWKK--ANLEKHSflDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSL 419
Cdd:cd11052  329 TSIWIPVLALHHDEEIWGEdANEFNPERFADgvAKAAKHP--MAFLPFGLGPRNCIGQNFATMEAKIVLAMILQRFSFTL 406
PLN02183 PLN02183
ferulate 5-hydroxylase
 264-441 1.27e-12

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 69.49  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkdKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSG 342
Cdd:PLN02183 326 WAMAELMKSPEDLKRVQQELADVVGL----NRRVEESDLEKLTYLKCTLKETLRLHPPiPLLLHETAEDAEVAGYFIPKR 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 343 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE--KHSFLDcFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLL 420
Cdd:PLN02183 402 SRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVPdfKGSHFE-FIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWELP 480

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 525313655 421 DPLpKQSYL--------------HLVGVPQPEGQC 441
Cdd:PLN02183 481 DGM-KPSELdmndvfgltapratRLVAVPTYRLQC 514
PLN02966 PLN02966
cytochrome P450 83A1
 36-415 1.31e-12

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 69.39  E-value: 1.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  36 IPWIGVGFEFGKA-PLEFIEKARIKYGPIFTvFAMGNR-MTFVTEEEGINVFLKSKKVDF-----------------ELA 96
Cdd:PLN02966  37 LPVIGNLLQLQKLnPQRFFAGWAKKYGPILS-YRIGSRtMVVISSAELAKELLKTQDVNFadrpphrghefisygrrDMA 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  97 VQNIV--YR-TGKMGTVNLHQFTGQLT------EELHEQLENLGTHG----TMDLNNLVRHLLYPVTVNMLFNKSlFSTN 163
Cdd:PLN02966 116 LNHYTpyYReIRKMGMNHLFSPTRVATfkhvreEEARRMMDKINKAAdkseVVDISELMLTFTNSVVCRQAFGKK-YNED 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 164 KKKIKEFHQYF--------QVYDEDFeygsqLPEC-LLRNWSKSKKWFLELFEKNIPDIKAC-------KSAKDNSMTLL 227
Cdd:PLN02966 195 GEEMKRFIKILygtqsvlgKIFFSDF-----FPYCgFLDDLSGLTAYMKECFERQDTYIQEVvnetldpKRVKPETESMI 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 228 QATLDIVE-----TETSKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKdkIKVSEDDL 302
Cdd:PLN02966 270 DLLMEIYKeqpfaSEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGS--TFVTEDDV 347

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 303 ENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPK-YFPEPELFKPERWKKANLEKHS 379
Cdd:PLN02966 348 KNLPYFRALVKETLRIEPviPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKeWGPNPDEFRPERFLEKEVDFKG 427

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 525313655 380 FLDCFMAFGSGKFQCPARWF--ALLEVQMCIILILYKY 415
Cdd:PLN02966 428 TDYEFIPFGSGRRMCPGMRLgaAMLEVPYANLLLNFNF 465
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 265-415 1.68e-12

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: 68.78  E-value: 1.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLAYVL----SHPDIHKAIMEGISSVFGKAGkdkIKVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILN-YI 338
Cdd:cd11057  246 TVAYTLlllaMHPEVQEKVYEEIMEVFPDDG---QFITYEDLQQLVYLEMVLKETMRLFPVGpLVGRETTADIQLSNgVV 322

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313655 339 IPSGDLLMLSPFWLHRNPKYF-PEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQCPARWFALLEVQMCIILILYKY 415
Cdd:cd11057  323 IPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQrHPY--AFIPFSAGPRNCIGWRYAMISMKIMLAKILRNY 399
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 264-416 6.99e-12

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: 66.87  E-value: 6.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDdLENLLLIKWCVLETIRLKA--PGViTRKVVKPVEILNYIIPS 341
Cdd:cd20647  259 WATYLLARHPEVQQQVYEEIVRNLGK---RVVPTAED-VPKLPLIRALLKETLRLFPvlPGN-GRVTQDDLIVGGYLIPK 333

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKhsfLDCF--MAFGSGKFQCPARWFALLEVQMCIILILYKYD 416
Cdd:cd20647  334 GTQLALCHYSTSYDEENFPRAEEFRPERWlRKDALDR---VDNFgsIPFGYGIRSCIGRRIAELEIHLALIQLLQNFE 408
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 264-401 7.06e-12

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: 67.11  E-value: 7.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAgkdkIKVSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 341
Cdd:cd11074  255 WGIAELVNHPEIQKKLRDELDTVLGPG----VQITEPDLHKLPYLQAVVKETLRLRMaiPLLVPHMNLHDAKLGGYDIPA 330

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWkkanLEKHSFLDC------FMAFGSGKFQCPARWFAL 401
Cdd:cd11074  331 ESKILVNAWWLANNPAHWKKPEEFRPERF----LEEESKVEAngndfrYLPFGVGRRSCPGIILAL 392
PLN02774 PLN02774
brassinosteroid-6-oxidase
 23-404 1.09e-11

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 66.34  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  23 RKNLrrPPCIKGWiPWIGVGFEFGKAPLEFIEKARIKYGPIF--------TVFAMG---NRMTFVTEEEGINVFLKSKKV 91
Cdd:PLN02774  29 KKGL--PPGTMGW-PLFGETTEFLKQGPDFMKNQRLRYGSFFkshilgcpTIVSMDpelNRYILMNEGKGLVPGYPQSML 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  92 DFeLAVQNIVYRTGK---------MGTVNLHQFTGQLTEELHE----QLENLGTHGTMDLNNLVRH--LLYPVTVNMLFN 156
Cdd:PLN02774 106 DI-LGTCNIAAVHGSthrymrgslLSLISPTMIRDHLLPKIDEfmrsHLSGWDGLKTIDIQEKTKEmaLLSALKQIAGTL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 157 KSLFSTNKKKikefhQYFQVYDEDFEYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVET 236
Cdd:PLN02774 185 SKPISEEFKT-----EFFKLVLGTLSLPIDLPGTNYRSGVQARKNIVRMLRQLIQERRASGETHTDMLGYLMRKEGNRYK 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 237 ETSKEnSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDI-------HKAIMEGissvfgKAGKDKIKVseDDLENLLLIK 309
Cdd:PLN02774 260 LTDEE-IIDQIITILYSGYETVSTTSMMAVKYLHDHPKAlqelrkeHLAIRER------KRPEDPIDW--NDYKSMRFTR 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 310 WCVLETIRLKA--PGVItRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFldcFMAF 387
Cdd:PLN02774 331 AVIFETSRLATivNGVL-RKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKSLESHNY---FFLF 406

                        410
                 ....*....|....*..
gi 525313655 388 GSGKFQCPARWFALLEV 404
Cdd:PLN02774 407 GGGTRLCPGKELGIVEI 423
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 264-422 2.12e-11

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: 65.52  E-value: 2.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKiKVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPS 341
Cdd:cd20657  250 WALAELIRHPDILKKAQEEMDQVIGR---DR-RLLESDIPNLPYLQAICKETFRLhpSTPLNLPRIASEACEVDGYYIPK 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKanlEKHSFLDC------FMAFGSGKFQCPARWFALLEVQMCIILILYKY 415
Cdd:cd20657  326 GTRLLVNIWAIGRDPDVWENPLEFKPERFLP---GRNAKVDVrgndfeLIPFGAGRRICAGTRMGIRMVEYILATLVHSF 402


                 ....*..
gi 525313655 416 DCSLLDP 422
Cdd:cd20657  403 DWKLPAG 409
PLN02655 PLN02655
ent-kaurene oxidase
 248-394 2.16e-11

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 65.53  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 248 LLLLWASLSNAVPVAF----WTLAYVLSHPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRL--KAP 321
Cdd:PLN02655 264 MMLVWEPIIEAADTTLvtteWAMYELAKNPDKQERLYREIREVCGDE-----RVTEEDLPNLPYLNAVFHETLRKysPVP 338

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313655 322 GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER-----WKKANLEKhsfldcFMAFGSGKFQC 394
Cdd:PLN02655 339 LLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERflgekYESADMYK------TMAFGAGKRVC 410
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 264-421 2.16e-11

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 65.60  E-value: 2.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPS 341
Cdd:PLN02687 319 WAIAELIRHPDILKKAQEELDAV---VGRDRL-VSESDLPQLTYLQAVIKETFRLhpSTPLSLPRMAAEECEINGYHIPK 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANleKHSFLDC------FMAFGSGKFQCPARWFALLEVQMCIILILYKY 415
Cdd:PLN02687 395 GATLLVNVWAIARDPEQWPDPLEFRPDRFLPGG--EHAGVDVkgsdfeLIPFGAGRRICAGLSWGLRMVTLLTATLVHAF 472


                 ....*.
gi 525313655 416 DCSLLD 421
Cdd:PLN02687 473 DWELAD 478
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 264-415 2.42e-11

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: 65.48  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFgkAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILN-YIIPS 341
Cdd:cd20679  266 WILYNLARHPEYQERCRQEVQELL--KDREPEEIEWDDLAQLPFLTMCIKESLRLHPPvTAISRCCTQDIVLPDgRVIPK 343

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdCFMAFGSGKFQCPARWFALLEVQMCIILILYKY 415
Cdd:cd20679  344 GIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPL-AFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRF 416
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 253-401 2.59e-11

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: 64.96  E-value: 2.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 253 ASLSNAVpvafWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKP 331
Cdd:cd11082  235 ASTSSLV----WALQLLADHPDVLAKVREEQARL---RPNDEPPLTLDLLEEMKYTRQVVKEVLRYRPPAPmVPHIAKKD 307

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313655 332 VEIL-NYIIPSGDLLMLSPFWLHRNPkyFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARWFAL 401
Cdd:cd11082  308 FPLTeDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQEDRKYKKNFLVFGAGPHQCVGQEYAI 376
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 264-430 6.42e-11

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: 63.84  E-value: 6.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKikvseDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILNYIIPSG 342
Cdd:cd20642  256 WTMVLLSQHPDWQERAREEVLQVFGNNKPDF-----EGLNHLKVVTMILYEVLRLYPPVIqLTRAIHKDTKLGDLTLPAG 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 343 DLLMLSPFWLHRNPKYFPE-PELFKPERWK----KANLEKHSFLdcfmAFGSGKFQCPARWFALLEVQMCIILILYKYDC 417
Cdd:cd20642  331 VQVSLPILLVHRDPELWGDdAKEFNPERFAegisKATKGQVSYF----PFGWGPRICIGQNFALLEAKMALALILQRFSF 406

                        170
                 ....*....|...
gi 525313655 418 SLldplpKQSYLH 430
Cdd:cd20642  407 EL-----SPSYVH 414
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 263-416 1.36e-10

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: 62.99  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 263 FWTLAyvlSHPDIHKAIMEGISSVFGKAGKDKIKV-SEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVeIL--NYI 338
Cdd:cd11064  254 FWLLS---KNPRVEEKIREELKSKLPKLTTDESRVpTYEELKKLVYLHAALSESLRLYPPvPFDSKEAVNDD-VLpdGTF 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 339 IPSGDLLMLSPFWLHRNPKYF-PEPELFKPERWkkanLEKHSFLDC-----FMAFGSGKFQCPARWFALLEVQMCIILIL 412
Cdd:cd11064  330 VKKGTRIVYSIYAMGRMESIWgEDALEFKPERW----LDEDGGLRPespykFPAFNAGPRICLGKDLAYLQMKIVAAAIL 405


                 ....
gi 525313655 413 YKYD 416
Cdd:cd11064  406 RRFD 409
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 264-416 1.78e-10

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: 62.57  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLaYVLS-HPDIHKAIMEGISSVFGKAGKDKikvsEDDLENLLLIKWCVLETIRLkAPGVI--TRKVVK---------- 330
Cdd:cd11063  238 FLF-YELArHPEVWAKLREEVLSLFGPEPTPT----YEDLKNMKYLRAVINETLRL-YPPVPlnSRVAVRdttlprgggp 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 331 ----PVeilnyIIPSGDLLMLSPFWLHRNPK-YFPEPELFKPERWkkANLEKHSFLdcFMAFGSGKFQCPARWFALLEVQ 405
Cdd:cd11063  312 dgksPI-----FVPKGTRVLYSVYAMHRRKDiWGPDAEEFRPERW--EDLKRPGWE--YLPFNGGPRICLGQQFALTEAS 382

                        170
                 ....*....|.
gi 525313655 406 MCIILILYKYD 416
Cdd:cd11063  383 YVLVRLLQTFD 393
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 265-416 2.37e-10

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: 61.98  E-value: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLAYVLSH----PDIHKAIMEGISSVfgkAGKDKIKVSEDdLENLLLIKWCVLETIRLkAPGVIT--RKVV-KPVEILNY 337
Cdd:cd20646  252 TLSWALYHlardPEIQERLYQEVISV---CPGDRIPTAED-IAKMPLLKAVIKETLRL-YPVVPGnaRVIVeKEVVVGDY 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 338 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSGKFQCPARWFALLEVQMCIILILYKYD 416
Cdd:cd20646  327 LFPKNTLFHLCHYAVSHDETNFPEPERFKPERWlRDGGLKHHPF--GSIPFGYGVRACVGRRIAELEMYLALSRLIKRFE 404
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 250-424 3.15e-10

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: 61.73  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 250 LLW----ASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPG--V 323
Cdd:cd20656  234 LLWdmitAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRV---VGSDRV-MTEADFPQLPYLQCVVKEALRLHPPTplM 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 324 ITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFLdcFMAFGSGKFQCPARWFAL 401
Cdd:cd20656  310 LPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFleEDVDIKGHDFR--LLPFGAGRRVCPGAQLGI 387

                        170       180
                 ....*....|....*....|...
gi 525313655 402 LEVQMCIILILYKYDCSLLDPLP 424
Cdd:cd20656  388 NLVTLMLGHLLHHFSWTPPEGTP 410
PTZ00404 PTZ00404
cytochrome P450; Provisional
 264-421 4.01e-10

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 61.66  E-value: 4.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGkaGKDKIKVSedDLENLLLIKWCVLETIRLKAPGV--ITRKVVKPVEILN-YIIP 340
Cdd:PTZ00404 305 WMVLMLCNYPEIQEKAYNEIKSTVN--GRNKVLLS--DRQSTPYTVAIIKETLRYKPVSPfgLPRSTSNDIIIGGgHFIP 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 341 SGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEkhsflDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLL 420
Cdd:PTZ00404 381 KDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSN-----DAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSI 455


                 .
gi 525313655 421 D 421
Cdd:PTZ00404 456 D 456
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 265-422 4.85e-10

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: 61.06  E-value: 4.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLAYVLSHPDIHKAIMEGISSVFGkagkdkikvSEDD-----LENLLLIKWCVLETIRL--KAPGVITRKVVKP-VEILN 336
Cdd:cd11058  240 LTYYLLKNPEVLRKLVDEIRSAFS---------SEDDitldsLAQLPYLNAVIQEALRLypPVPAGLPRVVPAGgATIDG 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 337 YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW---KKANLEKHSfLDCFMAFGSGKFQCPARWFALLEvqMCIIL--I 411
Cdd:cd11058  311 QFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWlgdPRFEFDNDK-KEAFQPFSVGPRNCIGKNLAYAE--MRLILakL 387

                        170
                 ....*....|.
gi 525313655 412 LYKYDCSLLDP 422
Cdd:cd11058  388 LWNFDLELDPE 398
PLN02971 PLN02971
tryptophan N-hydroxylase
 238-396 8.10e-10

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 60.82  E-value: 8.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 238 TSKENSPNYGLLLLWA--SLSNAVPvafWTLAYVLSHPDIHKAIMEGISSVFGKagkdKIKVSEDDLENLLLIKWCVLET 315
Cdd:PLN02971 324 TADEIKPTIKELVMAApdNPSNAVE---WAMAEMINKPEILHKAMEEIDRVVGK----ERFVQESDIPKLNYVKAIIREA 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 316 IRLK--APGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER----WKKANLEKHSFLdcFMAFGS 389
Cdd:PLN02971 397 FRLHpvAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERhlneCSEVTLTENDLR--FISFST 474


                 ....*..
gi 525313655 390 GKFQCPA 396
Cdd:PLN02971 475 GKRGCAA 481
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 261-441 1.42e-09

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 59.73  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 261 VAFWTLAYVLSHPDIH---KAIMEGISSvfgKAGKDKIKVSEDDLENLLLIKWCVLETIRL-KAPGVITRKVVKPVEILN 336
Cdd:PLN02302 306 LTMWATIFLQEHPEVLqkaKAEQEEIAK---KRPPGQKGLTLKDVRKMEYLSQVIDETLRLiNISLTVFREAKTDVEVNG 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 337 YIIPSGDLLMLspfWL---HRNPKYFPEPELFKPERWKKANLEKHSFLdcfmAFGSGKFQCPARWFALLEVqmCIIL--I 411
Cdd:PLN02302 383 YTIPKGWKVLA---WFrqvHMDPEVYPNPKEFDPSRWDNYTPKAGTFL----PFGLGSRLCPGNDLAKLEI--SIFLhhF 453

                        170       180       190
                 ....*....|....*....|....*....|.
gi 525313655 412 LYKYDCSLLDPLPKQSYL-HlvgvPQPEGQC 441
Cdd:PLN02302 454 LLGYRLERLNPGCKVMYLpH----PRPKDNC 480
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 264-435 2.48e-09

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: 58.87  E-value: 2.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd20673  254 WIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTL----SDRNHLPLLEATIREVLRIRpvAPLLIPHVALQDSSIGEFTIPK 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERwkkanlekhsFLD-----------CFMAFGSGKFQCPARWFALLEVQMCIIL 410
Cdd:cd20673  330 GTRVVINLWALHHDEKEWDQPDQFMPER----------FLDptgsqlispslSYLPFGAGPRVCLGEALARQELFLFMAW 399

                        170       180
                 ....*....|....*....|....*..
gi 525313655 411 ILYKYDCSLLD--PLPkqsylHLVGVP 435
Cdd:cd20673  400 LLQRFDLEVPDggQLP-----SLEGKF 421
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 24-410 4.06e-09

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 58.45  E-value: 4.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  24 KNLRRPPCIKGwIPWIGVGFEFGKA-----PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFELAVQ 98
Cdd:PLN02987  27 RRMRLPPGSLG-LPLVGETLQLISAyktenPEPFIDERVARYGSLFMTHLFGEPTVFSADPETNRFILQNEGKLFECSYP 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  99 NIVyrTGKMGTVNLHQFTGQLTEELHEQLENLGT------HGTMDLNNLVRHLLYPVTVNMLF----NKSLFSTNKKKIK 168
Cdd:PLN02987 106 GSI--SNLLGKHSLLLMKGNLHKKMHSLTMSFANssiikdHLLLDIDRLIRFNLDSWSSRVLLmeeaKKITFELTVKQLM 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 169 EF----------HQYFQVYDEDFEYGSQLPECLLRNWSKSKKWFLE-----LFEKNIPDIKACKSAKDnsmtLLQATLDi 233
Cdd:PLN02987 184 SFdpgewteslrKEYVLVIEGFFSVPLPLFSTTYRRAIQARTKVAEaltlvVMKRRKEEEEGAEKKKD----MLAALLA- 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 234 VETETSKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGkDKIKVSEDDLENLLLIKWCVL 313
Cdd:PLN02987 259 SDDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKS-DSYSLEWSDYKSMPFTQCVVN 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 314 ETIRL-KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKaNLEKHSFLDCFMAFGSGKF 392
Cdd:PLN02987 338 ETLRVaNIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQS-NSGTTVPSNVFTPFGGGPR 416

                        410
                 ....*....|....*...
gi 525313655 393 QCPArwFALLEVQMCIIL 410
Cdd:PLN02987 417 LCPG--YELARVALSVFL 432
PLN02738 PLN02738
carotene beta-ring hydroxylase
 250-419 4.61e-09

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 58.39  E-value: 4.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 250 LLWASLSNAVPVAFWTLaYVLS-HPDIHKAIMEGISSVFGkagkDKIKVSEDdLENLLLIKWCVLETIRL-KAPGVITRK 327
Cdd:PLN02738 399 MLIAGHETSAAVLTWTF-YLLSkEPSVVAKLQEEVDSVLG----DRFPTIED-MKKLKYTTRVINESLRLyPQPPVLIRR 472

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 328 VVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW----KKANLEKHSFldCFMAFGSGKFQCPARWFALLE 403
Cdd:PLN02738 473 SLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpldgPNPNETNQNF--SYLPFGGGPRKCVGDMFASFE 550

                        170
                 ....*....|....*.
gi 525313655 404 VQMCIILILYKYDCSL 419
Cdd:PLN02738 551 NVVATAMLVRRFDFQL 566
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 23-421 7.92e-09

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 57.55  E-value: 7.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  23 RKNLRR-PPCIKGWiPWIGVGFEFGKAPLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDF-----ELA 96
Cdd:PLN00110  26 PKPSRKlPPGPRGW-PLLGALPLLGNMPHVALAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFsnrppNAG 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655  97 VQNIVYRTGKM-------------GTVNLHQFTGQlteelheQLENLGTHGTMDLNNLVRHLLY------PVTV------ 151
Cdd:PLN00110 105 ATHLAYGAQDMvfadygprwkllrKLSNLHMLGGK-------ALEDWSQVRTVELGHMLRAMLElsqrgePVVVpemltf 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 152 ---NMLFNKSL----FSTNKKKIKEFHQY---FQVYDEDFEYGSQLP-------ECLLRNWSKSKKWFLELFEKNIPDIK 214
Cdd:PLN00110 178 smaNMIGQVILsrrvFETKGSESNEFKDMvveLMTTAGYFNIGDFIPsiawmdiQGIERGMKHLHKKFDKLLTRMIEEHT 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 215 ACKSAKDNSMTLLqatlDIVETEtsKENSP-------NYGLLLL---WASLSNAVPVAFWTLAYVLSHPDIHKAIMEGIS 284
Cdd:PLN00110 258 ASAHERKGNPDFL----DVVMAN--QENSTgekltltNIKALLLnlfTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMD 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 285 SVFGKAGKdkikVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEP 362
Cdd:PLN00110 332 QVIGRNRR----LVESDLPKLPYLQAICKESFRKhpSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENP 407

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525313655 363 ELFKPERWKKanlEKHSFLDC------FMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLLD 421
Cdd:PLN00110 408 EEFRPERFLS---EKNAKIDPrgndfeLIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPD 469
PLN03018 PLN03018
homomethionine N-hydroxylase
 253-369 1.23e-08

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 56.94  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 253 ASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVK 330
Cdd:PLN03018 325 AAIDNPANNMEWTLGEMLKNPEILRKALKELDEV---VGKDRL-VQESDIPNLNYLKACCRETFRIhpSAHYVPPHVARQ 400

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 525313655 331 PVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER 369
Cdd:PLN03018 401 DTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPER 439
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 256-419 1.65e-08

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: 56.27  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 256 SNAVPVAfWTLAYVLSHPDIHKAIMEGISSVFGKAGKDkikvsEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEI 334
Cdd:cd20640  245 TTAVTAA-WCLMLLALHPEWQDRVRAEVLEVCKGGPPD-----ADSLSRMKTVTMVIQETLRLYPPAaFVSREALRDMKL 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 335 LNYIIPSGDLLMLSPFWLHRNPKYF-PEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARWFALLEVQMCIILILY 413
Cdd:cd20640  319 GGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLILS 398


                 ....*.
gi 525313655 414 KYDCSL 419
Cdd:cd20640  399 KFSFTL 404
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 263-411 2.17e-08

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: 55.83  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 263 FWTLAYVLSHPDIHKAIMEGISSVFGkaGKDkikVSEDDLENLLLIKWCVLETIRLKaPGV--ITRKVVKPVEILNYIIP 340
Cdd:cd20616  245 FFMLLLIAQHPEVEEAILKEIQTVLG--ERD---IQNDDLQKLKVLENFINESMRYQ-PVVdfVMRKALEDDVIDGYPVK 318

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525313655 341 SGDLLMLSPFWLHRNPkYFPEPELFKPErwkkaNLEKHSFLDCFMAFGSGKFQCPARWFALleVQMCIILI 411
Cdd:cd20616  319 KGTNIILNIGRMHRLE-FFPKPNEFTLE-----NFEKNVPSRYFQPFGFGPRSCVGKYIAM--VMMKAILV 381
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 264-427 3.02e-08

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: 55.55  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKvSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 341
Cdd:cd20666  250 WCLLYMSLYPEVQEKVQAEIDTVIGP---DRAP-SLTDKAQMPFTEATIMEVQRMTVvvPLSIPHMASENTVLQGYTIPK 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN---LEKHSfldcFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCS 418
Cdd:cd20666  326 GTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENgqlIKKEA----FIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFL 401


                 ....*....
gi 525313655 419 LLDPLPKQS 427
Cdd:cd20666  402 LPPNAPKPS 410
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 264-430 3.77e-08

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: 55.15  E-value: 3.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDkikvSEDDLENLLLIKWCVLETIRLKAPGVIT-RKVVKPVEILNYIIPSG 342
Cdd:cd20639  254 WTTVLLAMHPEWQERARREVLAVCGKGDVP----TKDHLPKLKTLGMILNETLRLYPPAVATiRRAKKDVKLGGLDIPAG 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 343 DLLMLSPFWLHRNPKYF-PEPELFKPERWK--KANLEKHsfLDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSL 419
Cdd:cd20639  330 TELLIPIMAIHHDAELWgNDAAEFNPARFAdgVARAAKH--PLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRL 407

                        170
                 ....*....|.
gi 525313655 420 ldplpKQSYLH 430
Cdd:cd20639  408 -----SPSYAH 413
PLN02936 PLN02936
epsilon-ring hydroxylase
 300-419 6.82e-08

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 54.80  E-value: 6.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 300 DDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN-LE 376
Cdd:PLN02936 331 EDIKELKYLTRCINESMRLypHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGpVP 410

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 525313655 377 KHSFLDC-FMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSL 419
Cdd:PLN02936 411 NETNTDFrYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLEL 454
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 264-404 9.42e-08

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: 53.96  E-value: 9.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKvsedDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd20674  248 WAVAFLLHHPEIQDRLQEELDRVLGPGASPSYK----DRARLPLLNATIAEVLRLRpvVPLALPHRTTRDSSIAGYDIPK 323

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdcfmAFGSGKFQCPARWFALLEV 404
Cdd:cd20674  324 GTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAANRALL----PFGCGARVCLGEPLARLEL 382
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 307-440 1.22e-07

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: 53.46  E-value: 1.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 307 LIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLekhsfldcfm 385
Cdd:cd20629  235 LIPAAIEEGLRWEPPvASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDRKPKPHL---------- 304

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525313655 386 AFGSGKFQCPARWFALLEVQMCIILilykydcsLLDPLPKqsyLHLVG-VPQPEGQ 440
Cdd:cd20629  305 VFGGGAHRCLGEHLARVELREALNA--------LLDRLPN---LRLDPdAPAPEIS 349
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 252-416 1.32e-07

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: 53.42  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 252 WASLSNAVPVAFWTLAyvLSHPDIHKAIMEGISSVFGKAGKDKIKVseddLENLLLIKWCVLETIRLKAP-GVITRKVVK 330
Cdd:cd11071  238 FGGFSALLPSLLARLG--LAGEELHARLAEEIRSALGSEGGLTLAA----LEKMPLLKSVVYETLRLHPPvPLQYGRARK 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 331 PVEILN----YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFldcfmaFGSGKF---------QCP 395
Cdd:cd11071  312 DFVIEShdasYKIKKGELLVGYQPLATRDPKVFDNPDEFVPDRFmgEEGKLLKHLI------WSNGPEteeptpdnkQCP 385

                        170       180
                 ....*....|....*....|.
gi 525313655 396 ARWFALLEVQMCIILILYKYD 416
Cdd:cd11071  386 GKDLVVLLARLFVAELFLRYD 406
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 314-410 3.20e-07

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: 52.22  E-value: 3.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 314 ETIRLKAPGVIT-RKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERwkkANLEKHsfldcfMAFGSGKF 392
Cdd:cd11078  259 ETLRYDSPVQGLrRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR---PNARKH------LTFGHGIH 329

                         90
                 ....*....|....*...
gi 525313655 393 QCPArwFALLEVQMCIIL 410
Cdd:cd11078  330 FCLG--AALARMEARIAL 345
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 191-394 4.86e-07

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: 51.72  E-value: 4.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 191 LLRNWSKSKKWFLELFEKNIPDIKAcksakDNSMTLLQATLdiveTETSKENSPNYG----------LLLLWASLSNAVP 260
Cdd:cd20662  173 VFSNWKKLKLFVSDMIDKHREDWNP-----DEPRDFIDAYL----KEMAKYPDPTTSfneenlicstLDLFFAGTETTST 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 261 VAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYI 338
Cdd:cd20662  244 TLRWALLYMALYPEIQEKVQAEIDRVIGQKRQ----PSLADRESMPYTNAVIHEVQRMGniIPLNVPREVAVDTKLAGFH 319

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525313655 339 IPSGDLLMLSPFWLHRNPKYFPEPELFKPERWkkanLEKHSF--LDCFMAFGSGKFQC 394
Cdd:cd20662  320 LPKGTMILTNLTALHRDPKEWATPDTFNPGHF----LENGQFkkREAFLPFSMGKRAC 373
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 264-395 8.08e-07

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: 51.02  E-value: 8.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd11026  248 WALLLLMKYPHIQEKVQEEIDRVIGRNRT----PSLEDRAKMPYTDAVIHEVQRFGdiVPLGVPHAVTRDTKFRGYTIPK 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525313655 342 GD--LLMLSPfwLHRNPKYFPEPELFKPERW--KKANLEKHsflDCFMAFGSGKFQCP 395
Cdd:cd11026  324 GTtvIPNLTS--VLRDPKQWETPEEFNPGHFldEQGKFKKN---EAFMPFSAGKRVCL 376
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 236-422 9.48e-07

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: 50.72  E-value: 9.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 236 TETSkENSPNYGLLLLwaslsnavpvafwtlayvLSHPDIHKAIMEGISSVFGK----AGKDKIKVSEDDlenlllikwC 311
Cdd:cd20665  239 TETT-STTLRYGLLLL------------------LKHPEVTAKVQEEIDRVIGRhrspCMQDRSHMPYTD---------A 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 312 VLETIRLKA---PGVITRKVVKPVEILNYIIPSGD--LLMLSPFwLHrNPKYFPEPELFKPERW--KKANLEKHsflDCF 384
Cdd:cd20665  291 VIHEIQRYIdlvPNNLPHAVTCDTKFRNYLIPKGTtvITSLTSV-LH-DDKEFPNPEKFDPGHFldENGNFKKS---DYF 365

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 525313655 385 MAFGSGKFQCPARWFALLEVQMCIILILYKYDC-SLLDP 422
Cdd:cd20665  366 MPFSAGKRICAGEGLARMELFLFLTTILQNFNLkSLVDP 404
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 314-404 1.30e-06

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 50.51  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 314 ETIRL-KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKhsflDCFMAFGSGKF 392
Cdd:PLN03141 323 ETLRMgNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEKDMNN----SSFTPFGGGQR 398

                         90
                 ....*....|..
gi 525313655 393 QCPARWFALLEV 404
Cdd:PLN03141 399 LCPGLDLARLEA 410
PLN00168 PLN00168
Cytochrome P450; Provisional
 264-405 1.42e-06

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 50.33  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSvfgKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPG--VITRKVVKPVEILNYIIPS 341
Cdd:PLN00168 328 WIMAELVKNPSIQSKLHDEIKA---KTGDDQEEVSEEDVHKMPYLKAVVLEGLRKHPPAhfVLPHKAAEDMEVGGYLIPK 404

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERwkkanlekhsFL--------DC-------FMAFGSGKFQCPARWFALLEVQ 405
Cdd:PLN00168 405 GATVNFMVAEMGRDEREWERPMEFVPER----------FLaggdgegvDVtgsreirMMPFGVGRRICAGLGIAMLHLE 473
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 264-419 2.46e-06

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: 49.75  E-value: 2.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEgisSVFGKAGKDKIKVSeDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILNYIIPSG 342
Cdd:cd20641  257 WTMFLLSLHPDWQEKLRE---EVFRECGKDKIPDA-DTLSKLKLMNMVLMETLRLYGPVInIARRASEDMKLGGLEIPKG 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 343 DLLMLSPFWLHRNPKYF-PEPELFKPERWK----KANLEKHSFLdcfmAFGSGKFQCPARWFALLEVQMCIILILYKYDC 417
Cdd:cd20641  333 TTIIIPIAKLHRDKEVWgSDADEFNPLRFAngvsRAATHPNALL----SFSLGPRACIGQNFAMIEAKTVLAMILQRFSF 408


                 ..
gi 525313655 418 SL 419
Cdd:cd20641  409 SL 410
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 248-413 2.88e-06

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: 49.23  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 248 LLLLWASLSNAVPVAFWTLAYvLSHPD-------IHKAIMEgissvfgkAGKDKIKVSEDDLEN------LLLIKwcvlE 314
Cdd:cd11066  234 LTMVSAGLDTVPLNLNHLIGH-LSHPPgqeiqekAYEEILE--------AYGNDEDAWEDCAAEekcpyvVALVK----E 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 315 TIR------LKAPgvitRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFmAFG 388
Cdd:cd11066  301 TLRyftvlpLGLP----RKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHF-SFG 375

                        170       180
                 ....*....|....*....|....*.
gi 525313655 389 SGKFQCPARWFALLEVQMCII-LILY 413
Cdd:cd11066  376 AGSRMCAGSHLANRELYTAICrLILL 401
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 264-422 3.10e-06

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: 49.21  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKVSEDdleNLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd20615  237 WNLVFLAANPAVQEKLREEISAAREQSGYPMEDYILS---TDTLLAYCVLESLRLRplLAFSVPESSPTDKIIGGYRIPA 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 342 GDLLMLSPFWL-HRNPKYFPEPELFKPERW---KKANLEKHsfldcFMAFGSGKFQCPARWFALLEVQMCIILILYKYDC 417
Cdd:cd20615  314 NTPVVVDTYALnINNPFWGPDGEAYRPERFlgiSPTDLRYN-----FWRFGFGPRKCLGQHVADVILKALLAHLLEQYEL 388


                 ....*
gi 525313655 418 SLLDP 422
Cdd:cd20615  389 KLPDQ 393
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 312-410 4.11e-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: 48.88  E-value: 4.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 312 VLETIRLK--APGVItRKVVKPVEIL-----NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERwkkaNLEKhsfldcF 384
Cdd:cd20612  244 VLEALRLNpiAPGLY-RRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR----PLES------Y 312

                         90       100
                 ....*....|....*....|....*.
gi 525313655 385 MAFGSGKFQCPARWFALleVQMCIIL 410
Cdd:cd20612  313 IHFGHGPHQCLGEEIAR--AALTEML 336
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 314-390 4.62e-06

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 48.36  E-value: 4.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 314 ETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLspfWL---HRNPKYFPEPELFKPERwkKANleKHsfldcfMAFGS 389
Cdd:cd11032  248 EVLRYRPPvQRTARVTTEDVELGGVTIPAGQLVIA---WLasaNRDERQFEDPDTFDIDR--NPN--PH------LSFGH 314


                 .
gi 525313655 390 G 390
Cdd:cd11032  315 G 315
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 202-424 5.95e-06

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: 48.38  E-value: 5.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 202 FLELFEKNIPDIKACKSAKDNSMTLLQATLDIVETETSKENSP-NYGLLLLwaslsnavpvafwtlayvLSHPDIHKAIM 280
Cdd:cd20670  203 FIDCFLIKMHQDKNNPHTEFNLKNLVLTTLNLFFAGTETVSSTlRYGFLLL------------------MKYPEVEAKIH 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 281 EGISSVFGK----AGKDKIKVSEDDLenlllikwCVLETIRLK--APGVITRKVVKPVEILNYIIPSG-DLLMLSPFWLh 353
Cdd:cd20670  265 EEINQVIGPhrlpSVDDRVKMPYTDA--------VIHEIQRLTdiVPLGVPHNVIRDTQFRGYLLPKGtDVFPLLGSVL- 335

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525313655 354 RNPKYFPEPELFKPERW--KKANLEKHsflDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYdcSLLDPLP 424
Cdd:cd20670  336 KDPKYFRYPEAFYPQHFldEQGRFKKN---EAFVPFSSGKRVCLGEAMARMELFLYFTSILQNF--SLRSLVP 403
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
 118-396 7.09e-06

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: 48.17  E-value: 7.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 118 QLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLfstnkkkikefhqyfQVYDEDFEYGSQLPECLLRNWSK 197
Cdd:cd20626  101 QAIQATLRRWISHATGGCVNLAELVQALTLRVVLVGLFQSDT---------------DALSLPDESLLDLAEAINELWIS 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 198 SKKWFLEL-FEKNIpdikacksakdnsmtLLQATLDIVETETSKENSPNYGLLLL---WASLSNAVPVAFWTLAY----V 269
Cdd:cd20626  166 SKSGPDPPpFSDNI---------------DLQDALRRVFPDLNDIDPFENPLNLIlpaFETMWRVVLRTFLEIHYlkgsP 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 270 LSHPDIHKAIMEGISSVFGKAGKDKIKVSEddlenllLIKwcvlETIRLKAPgviTRKVVK--------PVEILNYIIPS 341
Cdd:cd20626  231 TLRDPTHPEWREANADFAKSATKDGISAKN-------LVK----EALRLYPP---TRRIYRafqrpgssKPEIIAADIEA 296

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525313655 342 gdllmlspfwLHRNPKYF-PEPELFKPERWKKANLEKHsflDCFMAFGSGKFQCPA 396
Cdd:cd20626  297 ----------CHRSESIWgPDALEFNPSRWSKLTPTQK---EAFLPFGSGPFRCPA 339
PLN02500 PLN02500
cytochrome P450 90B1
 296-422 1.40e-05

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 47.17  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 296 KVSEDDLENLLLIKWCVLETIRL-KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN 374
Cdd:PLN02500 334 ELNWEDYKKMEFTQCVINETLRLgNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNN 413

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 525313655 375 LEKHS------FLDCFMAFGSGKFQCPARWFALLEVQMCIILILYKYDCSLLDP 422
Cdd:PLN02500 414 NRGGSsgsssaTTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELAEA 467
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 264-416 1.83e-05

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: 46.86  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLaYVLS-HPDIHKAIMEGISSVFG---KAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVeilNYII 339
Cdd:cd11051  207 WAF-YLLSkHPEVLAKVRAEHDEVFGpdpSAAAELLREGPELLNQLPYTTAVIKETLRLFPPAGTARRGPPGV---GLTD 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 340 PSGDLLMLSPF--W-----LHRNPKYFPEPELFKPERW-KKANLEKHSFLDCFMAFGSGKFQCPARWFALLEVQMCIILI 411
Cdd:cd11051  283 RDGKEYPTDGCivYvchhaIHRDPEYWPRPDEFIPERWlVDEGHELYPPKSAWRPFERGPRNCIGQELAMLELKIILAMT 362


                 ....*
gi 525313655 412 LYKYD 416
Cdd:cd11051  363 VRRFD 367
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 261-424 1.86e-05

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: 46.69  E-value: 1.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 261 VAFWTLAYVLSHPDIHKAIMEGISSVFGKAgkdkikvsedDLENLlliKWCVLETIRL--KAPgVITRKVVKPVEILNYI 338
Cdd:cd20624  210 ALLRALALLAAHPEQAARAREEAAVPPGPL----------ARPYL---RACVLDAVRLwpTTP-AVLRESTEDTVWGGRT 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 339 IPSGD-LLMLSPFWlHRNPKYFPEPELFKPERWKKANLEKHSFLdcfMAFGSGKFQCPARWFALLEVQMCIILILYKYDC 417
Cdd:cd20624  276 VPAGTgFLIFAPFF-HRDDEALPFADRFVPEIWLDGRAQPDEGL---VPFSAGPARCPGENLVLLVASTALAALLRRAEI 351


                 ....*..
gi 525313655 418 SLLDPLP 424
Cdd:cd20624  352 DPLESPR 358
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
 314-400 2.40e-05

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 46.34  E-value: 2.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 314 ETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLekhsfldcfmAFGSGKF 392
Cdd:cd11039  252 EGLRWISPiGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFDVFRPKSPHV----------SFGAGPH 321


                 ....*...
gi 525313655 393 QCPARWFA 400
Cdd:cd11039  322 FCAGAWAS 329
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 327-404 6.91e-05

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: 44.83  E-value: 6.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 327 KVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAnlEKHSFldCFMAFGSGKFQ----CPARWF--A 400
Cdd:cd11067  285 RARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGW--EGDPF--DFIPQGGGDHAtghrCPGEWItiA 360


                 ....
gi 525313655 401 LLEV 404
Cdd:cd11067  361 LMKE 364
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 303-405 7.14e-05

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 44.65  E-value: 7.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 303 ENLLLIKWCVLETIRLKAPGVITRKVVK-PVEILNYIIPSGDLLMLSpfWL--HRNPKYFPEPELFKPERWKKANLekhs 379
Cdd:cd11079  222 ANPALLPAAIDEILRLDDPFVANRRITTrDVELGGRTIPAGSRVTLN--WAsaNRDERVFGDPDEFDPDRHAADNL---- 295

                         90       100
                 ....*....|....*....|....*.
gi 525313655 380 fldcfmAFGSGKFQCPARWFALLEVQ 405
Cdd:cd11079  296 ------VYGRGIHVCPGAPLARLELR 315
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 264-398 7.71e-05

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: 45.00  E-value: 7.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKvsedDLENLLLIKWCVLETIR------LKAPGVITRKVvkpveILN- 336
Cdd:cd20676  259 WSLMYLVTYPEIQKKIQEELDEVIGRERRPRLS----DRPQLPYLEAFILETFRhssfvpFTIPHCTTRDT-----SLNg 329

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313655 337 YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDC--FMAFGSGKFQC----PARW 398
Cdd:cd20676  330 YYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEINKTESekVMLFGLGKRRCigesIARW 397
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 264-415 1.39e-04

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: 44.03  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDkikvSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPS 341
Cdd:cd20661  260 WAILFMALYPNIQGQVQKEIDLVVGPNGMP----SFEDKCKMPYTEAVLHEVLRFcnIVPLGIFHATSKDAVVRGYSIPK 335

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN--LEKHsflDCFMAFGSGKFQCPARWFALLEVQMCIILILYKY 415
Cdd:cd20661  336 GTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNgqFAKK---EAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRF 408
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 246-408 1.54e-04

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: 43.86  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 246 YGLLLLWASL---SNAVPVAFWTLAyvlSHPDIHKAImegissvfgkagkdkikvseddLENLLLIKWCVLETIRLKAPG 322
Cdd:cd11034  194 FLTLLLLGGTdttSSALSGALLWLA---QHPEDRRRL----------------------IADPSLIPNAVEEFLRFYSPV 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 323 V-ITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKanleKHsfldcfMAFGSGKFQCPARWFAL 401
Cdd:cd11034  249 AgLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRTPN----RH------LAFGSGVHRCLGSHLAR 318


                 ....*..
gi 525313655 402 LEVQMCI 408
Cdd:cd11034  319 VEARVAL 325
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 264-394 1.77e-04

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: 43.84  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIKvSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 341
Cdd:cd20675  257 WILLLLVRYPDVQARLQEELDRV---VGRDRLP-CIEDQPNLPYVMAFLYEAMRFSSfvPVTIPHATTADTSILGYHIPK 332

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525313655 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWkkanLEKHSFLD-----CFMAFGSGKFQC 394
Cdd:cd20675  333 DTVVFVNQWSVNHDPQKWPNPEVFDPTRF----LDENGFLNkdlasSVMIFSVGKRRC 386
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 254-421 1.81e-04

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 43.84  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 254 SLSNAVPVAFWTLAyvlSHPDIHKAIMEGISSvfgkagkdkiKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVE 333
Cdd:PLN02169 316 TTSSALTWFFWLLS---KHPQVMAKIRHEINT----------KFDNEDLEKLVYLHAALSESMRLYPPLPFNHKAPAKPD 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 334 IL--NYIIPSGDLLMLSPFWLHRNPKYFPEPEL-FKPERWKKANLE-KHSFLDCFMAFGSGKFQCPARWFALLEVQMCII 409
Cdd:PLN02169 383 VLpsGHKVDAESKIVICIYALGRMRSVWGEDALdFKPERWISDNGGlRHEPSYKFMAFNSGPRTCLGKHLALLQMKIVAL 462

                        170
                 ....*....|..
gi 525313655 410 LILYKYDCSLLD 421
Cdd:PLN02169 463 EIIKNYDFKVIE 474
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 325-406 1.90e-04

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: 43.57  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 325 TRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLekhsfldcfmAFGSGKFQCPARWFALLEV 404
Cdd:cd20630  266 ARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRRDPNANI----------AFGYGPHFCIGAALARLEL 335


                 ..
gi 525313655 405 QM 406
Cdd:cd20630  336 EL 337
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 250-422 2.14e-04

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: 43.28  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 250 LLWASLSNAVPVAFWTLAYVLSHPD-IHKAIMEGISSVFGKA-GKDKIKVSEDDLENLLLIKWCVLETIRLKAP---GVi 324
Cdd:cd20636  235 LIFAAFSTTASASTSLVLLLLQHPSaIEKIRQELVSHGLIDQcQCCPGALSLEKLSRLRYLDCVVKEVLRLLPPvsgGY- 313

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 325 tRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARWFALLEV 404
Cdd:cd20636  314 -RTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGRFNYIPFGGGVRSCIGKELAQVIL 392

                        170
                 ....*....|....*...
gi 525313655 405 QMCIILILYKYDCSLLDP 422
Cdd:cd20636  393 KTLAVELVTTARWELATP 410
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 265-412 3.07e-04

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: 42.86  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 265 TLAY----VLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYI 338
Cdd:cd20668  245 TLRYgfllLMKHPEVEAKVHEEIDRVIGRNRQPKF----EDRAKMPYTEAVIHEIQRFGdvIPMGLARRVTKDTKFRDFF 320

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313655 339 IPSGDLL--MLSPfwLHRNPKYFPEPELFKPERW--KKANLEKHsflDCFMAFGSGKFQCPARWFALLEVQMCIILIL 412
Cdd:cd20668  321 LPKGTEVfpMLGS--VLKDPKFFSNPKDFNPQHFldDKGQFKKS---DAFVPFSIGKRYCFGEGLARMELFLFFTTIM 393
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 272-404 4.49e-04

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: 42.49  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 272 HPDIHKAIMEGISS--VFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP---GVitRKVVKPVEILNYIIPSGDLLM 346
Cdd:cd20638  260 HPEVLQKVRKELQEkgLLSTKPNENKELSMEVLEQLKYTGCVIKETLRLSPPvpgGF--RVALKTFELNGYQIPKGWNVI 337

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 347 LSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDcFMAFGSGKFQCPARWFA--LLEV 404
Cdd:cd20638  338 YSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFS-FIPFGGGSRSCVGKEFAkvLLKI 396
PLN02290 PLN02290
cytokinin trans-hydroxylase
 264-430 6.45e-04

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 42.11  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikvSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPSG 342
Cdd:PLN02290 338 WTLMLLASNPTWQDKVRAEVAEVCGGETP-----SVDHLSKLTLLNMVINESLRLYPPAtLLPRMAFEDIKLGDLHIPKG 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 343 dllmLSpFWL------HRNPKYFPEPELFKPERW--KKANLEKHsfldcFMAFGSGKFQCPARWFALLEVQMCIILILYK 414
Cdd:PLN02290 413 ----LS-IWIpvlaihHSEELWGKDANEFNPDRFagRPFAPGRH-----FIPFAAGPRNCIGQAFAMMEAKIILAMLISK 482

                        170
                 ....*....|....*.
gi 525313655 415 YDCSLLDplpkqSYLH 430
Cdd:PLN02290 483 FSFTISD-----NYRH 493
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 312-405 6.73e-04

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: 41.78  E-value: 6.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 312 VLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERwkKANleKHsfldcfMAFGSGK 391
Cdd:cd11031  257 LLRYIPLGAGGGFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDR--EPN--PH------LAFGHGP 326

                         90
                 ....*....|....
gi 525313655 392 FQCPARWFALLEVQ 405
Cdd:cd11031  327 HHCLGAPLARLELQ 340
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 307-406 9.14e-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: 41.41  E-value: 9.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 307 LIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERwkkaNLEKHsfldcfM 385
Cdd:cd11037  245 LAPNAFEEAVRLESPvQTFSRTTTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR----NPSGH------V 314

                         90       100
                 ....*....|....*....|.
gi 525313655 386 AFGSGKFQCPARWFALLEVQM 406
Cdd:cd11037  315 GFGHGVHACVGQHLARLEGEA 335
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 312-405 1.51e-03

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: 40.61  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 312 VLETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLspfwL----HRNPKYFPEPELFKPERwkKANleKHsfldcfMA 386
Cdd:cd20625  249 VEELLRYDSPvQLTARVALEDVEIGGQTIPAGDRVLL----LlgaaNRDPAVFPDPDRFDITR--APN--RH------LA 314

                         90
                 ....*....|....*....
gi 525313655 387 FGSGKFQCPARWFALLEVQ 405
Cdd:cd20625  315 FGAGIHFCLGAPLARLEAE 333
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 314-412 1.60e-03

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: 40.53  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 314 ETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKF 392
Cdd:cd11080  243 ETLRYHPPvQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREDLGIRSAFSGAADHLAFGSGRH 322

                         90       100
                 ....*....|....*....|
gi 525313655 393 QCPARWFALLEVQMCIILIL 412
Cdd:cd11080  323 FCVGAALAKREIEIVANQVL 342
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 314-404 1.93e-03

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: 40.27  E-value: 1.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 314 ETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLsPFWLH-RNPKYFPEPELFKPERwkKANleKHsfldcfMAFGSGKF 392
Cdd:cd11035  240 ELLRRYPLVNVARIVTRDVEFHGVQLKAGDMVLL-PLALAnRDPREFPDPDTVDFDR--KPN--RH------LAFGAGPH 308

                         90
                 ....*....|..
gi 525313655 393 QCPARWFALLEV 404
Cdd:cd11035  309 RCLGSHLARLEL 320
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 196-415 2.28e-03

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: 40.13  E-value: 2.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 196 SKSKKWFLELFEKNIP-DIKAC---KSAKD--------NSMTLLQATLDIV--ETETSKeNSPNYGLLLLwaslsnavpv 261
Cdd:cd20669  185 AESVREHQESLDPNSPrDFIDCfltKMAEEkqdplshfNMETLVMTTHNLLfgGTETVS-TTLRYGFLIL---------- 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 262 afwtlayvLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYII 339
Cdd:cd20669  254 --------MKYPKVAARVQEEIDRVVGRNRLPTL----EDRARMPYTDAVIHEIQRFADiiPMSLPHAVTRDTNFRGFLI 321

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525313655 340 PSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANlekHSFL--DCFMAFGSGKFQCPARWFALLEVQMCIILILYKY 415
Cdd:cd20669  322 PKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDN---GSFKknDAFMPFSAGKRICLGESLARMELFLYLTAILQNF 396
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 191-404 7.77e-03

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: 38.63  E-value: 7.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 191 LLRNWSKSKKWFLELFEKNIpDIKAcksaKDNSMTLLQATLdiVETETSKENSPNY----GLLLLWASLSNA-----VPV 261
Cdd:cd20664  172 LLRNTKELNDFLMETFMKHL-DVLE----PNDQRGFIDAFL--VKQQEEEESSDSFfhddNLTCSVGNLFGAgtdttGTT 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525313655 262 AFWTLAYVLSHPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYII 339
Cdd:cd20664  245 LRWGLLLMMKYPEIQKKVQEEIDRVIGSR-----QPQVEHRKNMPYTDAVIHEIQRFAniVPMNLPHATTRDVTFRGYFI 319

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525313655 340 PSGDLLMLSPFWLHRNPKYFPEPELFKPERWkkANLEKHsFL--DCFMAFGSGKFQCPARWFALLEV 404
Cdd:cd20664  320 PKGTYVIPLLTSVLQDKTEWEKPEEFNPEHF--LDSQGK-FVkrDAFMPFSAGRRVCIGETLAKMEL 383
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH