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Conserved domains on  [gi|2462608768|ref|XP_054211551|]
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24-hydroxycholesterol 7-alpha-hydroxylase isoform X6 [Homo sapiens]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
49-397 0e+00

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.


The actual alignment was detected with superfamily member cd20635:

Pssm-ID: 477761  Cd Length: 410  Bit Score: 602.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  49 PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYHT--------------------GKMG 108
Cdd:cd20635     1 PLEFIEKARQKLGPVFTVKAAGERMTFVTDEEDFHVFFKSKDVDFQKAVQDPVQNTasiskesffeyhtkihdmmkGKLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 109 TVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLP 188
Cdd:cd20635    81 SSNLAPLSDKLCEEFKEQLELLGSEGTGDLNDLVRHVMYPAVVNNLFGKGLLPTSEEEIKEFEEHFVKFDEQFEYGSQLP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 189 ECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVEtetsKENSPNYGLLLLWASLSNAVPVAFWTLAY 268
Cdd:cd20635   161 EFFLRDWSSSKQWLLSLFEKVVPDAEKTKPLENNSKTLLQHLLDTVD----KENAPNYSLLLLWASLANAIPITFWTLAF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 269 VLSHPDIHKAIMEGISSVFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLS 348
Cdd:cd20635   237 ILSHPSVYKKVMEEISSVLGKAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSPGAITRKVVKPIKIKNYTIPAGDMLMLS 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462608768 349 PFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPAR 397
Cdd:cd20635   317 PYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEGFVAFGGGRYQCPGR 365
 
Name Accession Description Interval E-value
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
49-397 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: 602.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  49 PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYHT--------------------GKMG 108
Cdd:cd20635     1 PLEFIEKARQKLGPVFTVKAAGERMTFVTDEEDFHVFFKSKDVDFQKAVQDPVQNTasiskesffeyhtkihdmmkGKLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 109 TVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLP 188
Cdd:cd20635    81 SSNLAPLSDKLCEEFKEQLELLGSEGTGDLNDLVRHVMYPAVVNNLFGKGLLPTSEEEIKEFEEHFVKFDEQFEYGSQLP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 189 ECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVEtetsKENSPNYGLLLLWASLSNAVPVAFWTLAY 268
Cdd:cd20635   161 EFFLRDWSSSKQWLLSLFEKVVPDAEKTKPLENNSKTLLQHLLDTVD----KENAPNYSLLLLWASLANAIPITFWTLAF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 269 VLSHPDIHKAIMEGISSVFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLS 348
Cdd:cd20635   237 ILSHPSVYKKVMEEISSVLGKAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSPGAITRKVVKPIKIKNYTIPAGDMLMLS 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462608768 349 PFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPAR 397
Cdd:cd20635   317 PYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEGFVAFGGGRYQCPGR 365
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
35-397 3.32e-37

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: 140.49  E-value: 3.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  35 WIPWIGVGFEFGKA--PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFE----LAV----------Q 98
Cdd:pfam00067   6 PLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSgrpdEPWfatsrgpflgK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  99 NIVYHTG-------KMGTVNLHQFTG--------QLTEELHEQL-ENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFST 162
Cdd:pfam00067  86 GIVFANGprwrqlrRFLTPTFTSFGKlsfeprveEEARDLVEKLrKTAGEPGVIDITDLLFRAALNVICSILFGERFGSL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 163 NKKKIKEFHQYFQVYDEDFEYGSQ--------LPECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNS----MTLLQAT 230
Cdd:pfam00067 166 EDPKFLELVKAVQELSSLLSSPSPqlldlfpiLKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAkkspRDFLDAL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 231 LDIVETET----SKENSPNYGLLLLWAS---LSNAVpvaFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLE 303
Cdd:pfam00067 246 LLAKEEEDgsklTDEELRATVLELFFAGtdtTSSTL---SWALYELAKHPEVQEKLREEIDEVIG----DKRSPTYDDLQ 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 304 NLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE-KHSF 380
Cdd:pfam00067 319 NMPYLDAVIKETLRLHpvVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKfRKSF 398
                         410
                  ....*....|....*..
gi 2462608768 381 ldCFMAFGSGKFQCPAR 397
Cdd:pfam00067 399 --AFLPFGAGPRNCLGE 413
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
44-395 4.72e-16

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: 79.17  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  44 EFGKAPLEFIEKARiKYGPIFTVFAMGNRMTFVTEEEGINVFLK-----SKKVDFELAVQNIVYHTGKMGTVN--LHQ-- 114
Cdd:COG2124    16 AFLRDPYPFYARLR-EYGPVFRVRLPGGGAWLVTRYEDVREVLRdprtfSSDGGLPEVLRPLPLLGDSLLTLDgpEHTrl 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 115 -------FTGQLTEELH--------EQLENLGTHGTMDLNNLVRHLLyPVTVNMlfnkSLFSTNKKKIKEFHQYFQVYde 179
Cdd:COG2124    95 rrlvqpaFTPRRVAALRprireiadELLDRLAARGPVDLVEEFARPL-PVIVIC----ELLGVPEEDRDRLRRWSDAL-- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 180 dFEYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKAckSAKDNSMT-LLQATLDivETETSKENSPNYGLLLLWASL--- 255
Cdd:COG2124   168 -LDALGPLPPERRRRARRARAELDAYLRELIAERRA--EPGDDLLSaLLAARDD--GERLSDEELRDELLLLLLAGHett 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 256 SNAVPVAFWTLayvLSHPDIHKAIMEGISsvfgkagkdkikvseddlenllLIKWCVLETIRLKAPG-VITRKVVKPVEI 334
Cdd:COG2124   243 ANALAWALYAL---LRHPEQLARLRAEPE----------------------LLPAAVEETLRLYPPVpLLPRTATEDVEL 297
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462608768 335 LNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAnlekhsfldcFMAFGSGKFQCP 395
Cdd:COG2124   298 GGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDRPPNA----------HLPFGGGPHRCL 348
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
23-396 6.14e-16

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 79.35  E-value: 6.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  23 RKNLRRPPCIKGwIPWIGVGFEFGK-APLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFE----LAV 97
Cdd:PLN03234   24 KKSLRLPPGPKG-LPIIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTarplLKG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  98 QNIVYHTG----------------KMGTVNLHQ------FTGQLTEELHEQLENL----GTHGTMDLNNLVRHLLYPVTV 151
Cdd:PLN03234  103 QQTMSYQGrelgfgqytayyremrKMCMVNLFSpnrvasFRPVREEECQRMMDKIykaaDQSGTVDLSELLLSFTNCVVC 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 152 NMLFNKSL--FSTNKKKIKEFHQYFQVYDEDFEYGSQLP-----ECLLRNWSKSKKWFLEL---FEKNIPDIKACKSAKD 221
Cdd:PLN03234  183 RQAFGKRYneYGTEMKRFIDILYETQALLGTLFFSDLFPyfgflDNLTGLSARLKKAFKELdtyLQELLDETLDPNRPKQ 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 222 NSMTLLQATLDIVETET-----SKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIK 296
Cdd:PLN03234  263 ETESFIDLLMQIYKDQPfsikfTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIG----DKGY 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 297 VSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPE-PELFKPERWkka 373
Cdd:PLN03234  339 VSEEDIPNLPYLKAVIKESLRLEPviPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERF--- 415
                         410       420
                  ....*....|....*....|....*....
gi 2462608768 374 nLEKHSFLDC------FMAFGSGKFQCPA 396
Cdd:PLN03234  416 -MKEHKGVDFkgqdfeLLPFGSGRRMCPA 443
 
Name Accession Description Interval E-value
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
49-397 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: 602.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  49 PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFELAVQNIVYHT--------------------GKMG 108
Cdd:cd20635     1 PLEFIEKARQKLGPVFTVKAAGERMTFVTDEEDFHVFFKSKDVDFQKAVQDPVQNTasiskesffeyhtkihdmmkGKLA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 109 TVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLP 188
Cdd:cd20635    81 SSNLAPLSDKLCEEFKEQLELLGSEGTGDLNDLVRHVMYPAVVNNLFGKGLLPTSEEEIKEFEEHFVKFDEQFEYGSQLP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 189 ECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVEtetsKENSPNYGLLLLWASLSNAVPVAFWTLAY 268
Cdd:cd20635   161 EFFLRDWSSSKQWLLSLFEKVVPDAEKTKPLENNSKTLLQHLLDTVD----KENAPNYSLLLLWASLANAIPITFWTLAF 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 269 VLSHPDIHKAIMEGISSVFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLS 348
Cdd:cd20635   237 ILSHPSVYKKVMEEISSVLGKAGKDKIKISEDDLKKMPYIKRCVLEAIRLRSPGAITRKVVKPIKIKNYTIPAGDMLMLS 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2462608768 349 PFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPAR 397
Cdd:cd20635   317 PYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEGFVAFGGGRYQCPGR 365
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
53-397 6.21e-75

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: 239.57  E-value: 6.21e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  53 IEKARIKY---GPIFTVFAMGNRMTFVTEEEGINVFLKSKKV-DFELAVQNIVYHTGKM--------------------- 107
Cdd:cd11040     1 LLRNGKKYfsgGPIFTIRLGGQKIYVITDPELISAVFRNPKTlSFDPIVIVVVGRVFGSpesakkkegepggkglirllh 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 108 --------GTVNLHQFTGQLTEELHEQLENLGTHG-----TMDLNNLVRHLLYPVTVNMLFNKSLFSTNkkkiKEFHQYF 174
Cdd:cd11040    81 dlhkkalsGGEGLDRLNEAMLENLSKLLDELSLSGgtstvEVDLYEWLRDVLTRATTEALFGPKLPELD----PDLVEDF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 175 QVYDEDFEYG-SQLPECLLRNWSKSKKWFLELFEKNIPDIKAcksAKDNSMTLLQATLDI-VETETSKENSPNYGLLLLW 252
Cdd:cd11040   157 WTFDRGLPKLlLGLPRLLARKAYAARDRLLKALEKYYQAARE---ERDDGSELIRARAKVlREAGLSEEDIARAELALLW 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 253 ASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKA-GKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKP 331
Cdd:cd11040   234 AINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDsGTNAILDLTDLLTSCPLLDSTYLETLRLHSSSTSVRLVTED 313
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 332 -VEILNYIIPSGDLLMLSPFWLHRNPKYF-PEPELFKPERWKKANLEK--HSFLDCFMAFGSGKFQCPAR 397
Cdd:cd11040   314 tVLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKkgRGLPGAFRPFGGGASLCPGR 383
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
35-397 3.32e-37

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: 140.49  E-value: 3.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  35 WIPWIGVGFEFGKA--PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFE----LAV----------Q 98
Cdd:pfam00067   6 PLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSgrpdEPWfatsrgpflgK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  99 NIVYHTG-------KMGTVNLHQFTG--------QLTEELHEQL-ENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFST 162
Cdd:pfam00067  86 GIVFANGprwrqlrRFLTPTFTSFGKlsfeprveEEARDLVEKLrKTAGEPGVIDITDLLFRAALNVICSILFGERFGSL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 163 NKKKIKEFHQYFQVYDEDFEYGSQ--------LPECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNS----MTLLQAT 230
Cdd:pfam00067 166 EDPKFLELVKAVQELSSLLSSPSPqlldlfpiLKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAkkspRDFLDAL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 231 LDIVETET----SKENSPNYGLLLLWAS---LSNAVpvaFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLE 303
Cdd:pfam00067 246 LLAKEEEDgsklTDEELRATVLELFFAGtdtTSSTL---SWALYELAKHPEVQEKLREEIDEVIG----DKRSPTYDDLQ 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 304 NLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE-KHSF 380
Cdd:pfam00067 319 NMPYLDAVIKETLRLHpvVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKfRKSF 398
                         410
                  ....*....|....*..
gi 2462608768 381 ldCFMAFGSGKFQCPAR 397
Cdd:pfam00067 399 --AFLPFGAGPRNCLGE 413
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
61-398 6.57e-34

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: 129.94  E-value: 6.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  61 GPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDF----ELAVQNIVYHTGKMGTVN-------------------LHQFTG 117
Cdd:cd00302     1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSsdagPGLPALGDFLGDGLLTLDgpehrrlrrllapaftpraLAALRP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 118 QLTEELHEQLENLGTHGTMDLNnlVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEYGSQLPECLLRNWS- 196
Cdd:cd00302    81 VIREIARELLDRLAAGGEVGDD--VADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLKLLGPRLLRPLPSPRLRRl 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 197 -KSKKWFLELFEKNIpdiKACKSAKDNSMTLLQATLDIVETETSKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDI 275
Cdd:cd00302   159 rRARARLRDYLEELI---ARRRAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLARHPEV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 276 HKAIMEGISSVFGKAgkdkikvSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHR 354
Cdd:cd00302   236 QERLRAEIDAVLGDG-------TPEDLSKLPYLEAVVEETLRLYPPvPLLPRVATEDVELGGYTIPAGTLVLLSLYAAHR 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2462608768 355 NPKYFPEPELFKPERWKKANLEKHSfldCFMAFGSGKFQCPARK 398
Cdd:cd00302   309 DPEVFPDPDEFDPERFLPEREEPRY---AHLPFGAGPHRCLGAR 349
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
56-395 6.23e-29

cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 116.55  E-value: 6.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  56 ARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKK--VDFELAVQN--------IVYHTGKMG-------------TVNL 112
Cdd:cd11042     1 CRKKYGDVFTFNLLGKKVTVLLGPEANEFFFNGKDedLSAEEVYGFltppfgggVVYYAPFAEqkeqlkfglnilrRGKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 113 HQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNkkkikeFHQYFQVYdEDFEYGSQLPECLL 192
Cdd:cd11042    81 RGYVPLIVEEVEKYFAKWGESGEVDLFEEMSELTILTASRCLLGKEVRELL------DDEFAQLY-HDLDGGFTPIAFFF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 193 RNWS--------KSKKWFLELFEKNIPDIKACKSAKDNSMtlLQATLDIV---ETETSKENSPNYGLLLLWASLSNAVPV 261
Cdd:cd11042   154 PPLPlpsfrrrdRARAKLKEIFSEIIQKRRKSPDKDEDDM--LQTLMDAKykdGRPLTDDEIAGLLIALLFAGQHTSSAT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 262 AFWTLAYVLSHPDIHKAIMEGISSVFGKAGKDkikVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILN--YI 338
Cdd:cd11042   232 SAWTGLELLRNPEHLEALREEQKEVLGDGDDP---LTYDVLKEMPLLHACIKETLRLHPPIHsLMRKARKPFEVEGggYV 308
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 339 IPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE---KHSFldCFMAFGSGKFQCP 395
Cdd:cd11042   309 IPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEdskGGKF--AYLPFGAGRHRCI 366
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
52-397 2.22e-24

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: 103.92  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  52 FIEKARIKYGPIFTVFAMGNRMTFVTEE-EGINVFLKSKKVDFELAVQNIVYHTGKMGTVNLHQFTGqLTEELH------ 124
Cdd:cd20632     1 FLLALQKKHGDVFTVLIAGKYITFIMDPfLYPYVIKHGKQLDFHEFSDRLASKTFGYPPLRSPKFPG-LNEQIHrsyqyl 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 125 --EQLENLGTHGTMDLNNLVRH-------------------LLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEY 183
Cdd:cd20632    80 qgENLDILTESMMGNLQLVLRQqflgetdweteelyefcsrIMFEATFLTLYGKPPDDDRHKVISELRKKFRKFDAMFPY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 184 -GSQLPECLLRNWSKSKKWFLELFEKNipdikacKSAK-DNSMTLLQATLDIVEtetskenspNYGLL-----------L 250
Cdd:cd20632   160 lVANIPIELLGATKSIREKLIKYFLPQ-------KMAKwSNPSEVIQARQELLE---------QYDVLqdydkaahhfaF 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 251 LWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKDK-----IKVSEDDLENLLLIKWCVLETIRLKAPGVIT 325
Cdd:cd20632   224 LWASVGNTIPATFWAMYYLLRHPEALAAVRDEIDHVLQSTGQELgpdfdIHLTREQLDSLVYLESAINESLRLSSASMNI 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 326 RkVVKPVEILN------YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSF------LDCF-MAFGSGKF 392
Cdd:cd20632   304 R-VVQEDFTLKlesdgsVNLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKKTTFykrgqkLKYYlMPFGSGSS 382

                  ....*
gi 2462608768 393 QCPAR 397
Cdd:cd20632   383 KCPGR 387
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
53-397 3.88e-23

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: 100.52  E-value: 3.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  53 IEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLK-SK-KVDFELAVQNIVyhtgkmgtvnLHQFTGQLTEELHEQLENL 130
Cdd:cd20633     1 LQKMQKKHGDIFTVQIGGHYFTFVMDPLSFGAIVKeSKsKLDFGKFASELV----------LRVFGYQPTENDHKMLQTL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 131 GT------------HGTMD-LNNLVRHL--------------LYPVTVNMLFNK---SLFST-------NKKKIKE---- 169
Cdd:cd20633    71 STkhlmgdglvvlnQAMMEnLQNLMLHSkgsgdggrewqqdgLFHYSYNIVFRAgylALFGNepdkeagNKEKAKEqdll 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 170 -----FHQyFQVYDEDFE---YGSQLPecllRNWSKSKKwfLELFEKNIPDIKACkSAKDN------SMTLLQATLDIVE 235
Cdd:cd20633   151 hseelFEE-FRKFDQLFPrlaYSVLPP----KDKLEAER--LKRLFWDMLSVSKM-SQKENisgwisEQQRQLAEHGMPE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 236 TETSKenspnYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKD-KIKVSEDDLENLLLIKWCVL- 313
Cdd:cd20633   223 YMQDR-----FMFLLLWASQGNTGPASFWLLLYLLKHPEAMKAVREEVEQVLKETGQEvKPGGPLINLTRDMLLKTPVLd 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 314 ----ETIRLKAPGVITRKVVKPVEIL-----NYIIPSGDLLMLSPFW-LHRNPKYFPEPELFK------PERWKKANLEK 377
Cdd:cd20633   298 saveETLRLTAAPVLIRAVVQDMTLKmangrEYALRKGDRLALFPYLaVQMDPEIHPEPHTFKydrflnPDGGKKKDFYK 377
                         410       420
                  ....*....|....*....|..
gi 2462608768 378 H--SFLDCFMAFGSGKFQCPAR 397
Cdd:cd20633   378 NgkKLKYYNMPWGAGVSICPGR 399
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
111-398 1.45e-22

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: 98.75  E-value: 1.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 111 NLHQFTGQL---TEELHEQLENLGTHGTMDLNNLvRHLLY----PVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFEY 183
Cdd:cd11054    82 SVASYLPAInevADDFVERIRRLRDEDGEEVPDL-EDELYkwslESIGTVLFGKRLGCLDDNPDSDAQKLIEAVKDIFES 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 184 GSQL----PEC----------LLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLdiveteTSKENSPN--YG 247
Cdd:cd11054   161 SAKLmfgpPLWkyfptpawkkFVKAWDTIFDIASKYVDEALEELKKKDEEDEEEDSLLEYLL------SKPGLSKKeiVT 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 248 LL--LLWASL---SNAVPVAFWTLAyvlSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLK--A 320
Cdd:cd11054   235 MAldLLLAGVdttSNTLAFLLYHLA---KNPEVQEKLYEEIRSVLP----DGEPITAEDLKKMPYLKACIKESLRLYpvA 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 321 PGvITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW---KKANLEKHSFLdcFMAFGSGKFQCPAR 397
Cdd:cd11054   308 PG-NGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlrdDSENKNIHPFA--SLPFGFGPRMCIGR 384

                  .
gi 2462608768 398 K 398
Cdd:cd11054   385 R 385
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
264-394 3.99e-21

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: 94.18  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLaYVLS-HPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPS 341
Cdd:cd20620   234 WTW-YLLAqHPEVAARLRAEVDRVLGGR-----PPTAEDLPQLPYTEMVLQESLRLYPPAwIIGREAVEDDEIGGYRIPA 307
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSGKFQC 394
Cdd:cd20620   308 GSTVLISPYVTHRDPRFWPDPEAFDPERFtPEREAARPRY--AYFPFGGGPRIC 359
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
249-395 1.49e-20

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: 92.71  E-value: 1.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 249 LLLWASLSNAVPVAfWTLaYVLS-HPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRLKAPG-VITR 326
Cdd:cd11049   228 LLTAGTETTASTLA-WAF-HLLArHPEVERRLHAELDAVLGGR-----PATFEDLPRLTYTRRVVTEALRLYPPVwLLTR 300
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462608768 327 KVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW---KKANLEKHSFLdcfmAFGSGKFQCP 395
Cdd:cd11049   301 RTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWlpgRAAAVPRGAFI----PFGAGARKCI 368
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
264-390 4.32e-20

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: 91.43  E-value: 4.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLaYVLS-HPDIHKAIMEGISSVFGKagkDKIKVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPS 341
Cdd:cd20628   251 FTL-YLLGlHPEVQEKVYEELDEIFGD---DDRRPTLEDLNKMKYLERVIKETLRLYPSVpFIGRRLTEDIKLDGYTIPK 326
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSG 390
Cdd:cd20628   327 GTTVVISIYALHRNPEYFPDPEKFDPDRFlPENSAKRHPY--AYIPFSAG 374
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
127-396 5.56e-20

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: 91.08  E-value: 5.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 127 LENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKKIKEFHQYFQVYDEDFE------YGSQLP--ECLLRNWSKS 198
Cdd:cd20618    97 LEESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEAREFKELIDEAFElagafnIGDYIPwlRWLDLQGYEK 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 199 K-----KWFLELFEKNIPDIKACKSAKDNSMTLLQaTLDIVETETSKENSPN---YGLL---LLWASLSNAVPVAfWTLA 267
Cdd:cd20618   177 RmkklhAKLDRFLQKIIEEHREKRGESKKGGDDDD-DLLLLLDLDGEGKLSDdniKALLldmLAAGTDTSAVTIE-WAMA 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 268 YVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPG--VITRKVVKPVEILNYIIPSGDLL 345
Cdd:cd20618   255 ELLRHPEVMRKAQEELDSV---VGRERL-VEESDLPKLPYLQAVVKETLRLHPPGplLLPHESTEDCKVAGYDIPAGTRV 330
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 346 MLSPFWLHRNPKYFPEPELFKPERWKKANLEK---HSFldCFMAFGSGKFQCPA 396
Cdd:cd20618   331 LVNVWAIGRDPKVWEDPLEFKPERFLESDIDDvkgQDF--ELLPFGSGRRMCPG 382
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
52-397 2.14e-19

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: 89.36  E-value: 2.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  52 FIEKARIKYGPIFTVFAMGNRMTFVTEEEGI-NVFLKSKKVDFE---LAVQNIVYHTGKM------GTVNLHQF------ 115
Cdd:cd20631     1 FLRSRQKKYGHIFTCKIAGKYVHFITDPFSYhSVIRHGKHLDWKkfhFATSAKAFGHVSFdpsdgnTTENIHDTfiktlq 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 116 ---TGQLTEELHEQLE-----------NLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFS--TNKKKIKEFHQYFQVYDE 179
Cdd:cd20631    81 gsaLDSLTESMMENLQyvmlqdkssssSTKAWVTEGLYSFCYRVMFEAGYLTLFGKELTAreDKNARLEAQRALILNALE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 180 DF-EYGSQLPE-------CLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLD-IVETETSKENspnygLLL 250
Cdd:cd20631   161 NFkEFDKVFPAlvaglpiHMFKTAKSAREALAERLLHENLQKRENISELISLRMLLNDTLStLDEMEKARTH-----VAM 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 251 LWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGK------DKIKVSEDDLENLLLIKWCVLETIRLKAPGVI 324
Cdd:cd20631   236 LWASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEKTGQkvsdggNPIVLTREQLDDMPVLGSIIKEALRLSSASLN 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 325 TRKVVKPVEIL-----NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDC--------FMAFGSGK 391
Cdd:cd20631   316 IRVAKEDFTLHldsgeSYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTFYKngrklkyyYMPFGSGT 395

                  ....*.
gi 2462608768 392 FQCPAR 397
Cdd:cd20631   396 SKCPGR 401
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
266-394 8.52e-19

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: 87.64  E-value: 8.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 266 LAYVLS-HPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILNYIIPSGD 343
Cdd:cd11055   249 ASYLLAtNPDVQEKLIEEIDEVLPDDGS----PTYDTVSKLKYLDMVINETLRLYPPAfFISRECKEDCTINGVFIPKGV 324
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462608768 344 LLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSGKFQC 394
Cdd:cd11055   325 DVVIPVYAIHHDPEFWPDPEKFDPERFsPENKAKRHPY--AYLPFGAGPRNC 374
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
211-396 1.91e-18

cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes cytochrome P450 families 73 (CYP77) and 89 (CYP89), which are sister families that share a common ancestor. CYP89, present only in angiosperms, is younger than CYP77, which is already found in lycopods; thus, CYP89 may have evolved from CYP77 after duplication and divergence. Also included in this group is ent-kaurene oxidase, called CYP701A3 in Arabidopsis thaliana and CYP701B1 in Physcomitrella patens, that catalyzes the oxidation of ent-kaurene to form ent-kaurenoic acid. CYP701A3 is sensitive to inhibitor uniconazole-P while CYP701B1 is not. This CYP77/89 group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410698 [Multi-domain]  Cd Length: 433  Bit Score: 86.53  E-value: 1.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 211 PDIKACK-------SAKDNSMTLLQATLDIVETEtsKENSPNYG--LLLLWASLSNA---VPVAF-WTLAYVLSHPDIHK 277
Cdd:cd11075   189 PLIRARRkrrasgeADKDYTDFLLLDLLDLKEEG--GERKLTDEelVSLCSEFLNAGtdtTATALeWAMAELVKNPEIQE 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 278 AIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKAPG--VITRKVVKPVEILNYIIPSGDLLMLSPFWLHRN 355
Cdd:cd11075   267 KLYEEIKEVVGDEAV----VTEEDLPKMPYLKAVVLETLRRHPPGhfLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRD 342
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2462608768 356 PKYFPEPELFKPERWkkANLEKHSFLDC------FMAFGSGKFQCPA 396
Cdd:cd11075   343 PKVWEDPEEFKPERF--LAGGEAADIDTgskeikMMPFGAGRRICPG 387
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
152-395 2.31e-18

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: 86.11  E-value: 2.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 152 NMLFNKSLFSTNKKKIKEFHQYFqvyDEDFEYGSQLPEC---------LLRNWSKSKKWF---LELFEKNIPDIKAcKSA 219
Cdd:cd20617   120 QFLFGKRFPDEDDGEFLKLVKPI---EEIFKELGSGNPSdfipillpfYFLYLKKLKKSYdkiKDFIEKIIEEHLK-TID 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 220 KDNSMTLLQATLDIVETETSKENSPNYGLLLLWASL--------SNAVpvaFWTLAYVLSHPDIHKAIMEGISSVFGKAG 291
Cdd:cd20617   196 PNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLDLflagtdttSTTL---EWFLLYLANNPEIQEKIYEEIDNVVGNDR 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 292 KDKIKvsedDLENLLLIKWCVLETIRLKAPGVIT--RKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER 369
Cdd:cd20617   273 RVTLS----DRSKLPYLNAVIKEVLRLRPILPLGlpRVTTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPER 348
                         250       260
                  ....*....|....*....|....*.
gi 2462608768 370 WKKANLEKHSflDCFMAFGSGKFQCP 395
Cdd:cd20617   349 FLENDGNKLS--EQFIPFGIGKRNCV 372
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
264-394 4.62e-18

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: 85.38  E-value: 4.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLA----YVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDDLENLLLIKWCVLETIRLkAPGVITR--KVV--KPVEIL 335
Cdd:cd11062   242 RTLSvatfHLLSNPEILERLREELKTAMPD---PDSPPSLAELEKLPYLTAVIKEGLRL-SYGVPTRlpRVVpdEGLYYK 317
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462608768 336 NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW----KKANLEKhsfldCFMAFGSGKFQC 394
Cdd:cd11062   318 GWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWlgaaEKGKLDR-----YLVPFSKGSRSC 375
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
44-394 5.20e-18

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: 85.03  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  44 EFGKAPLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFL----KSKKVDFELAVQ------NIVYHTGK------- 106
Cdd:cd11044     5 EFLRDPEDFIQSRYQKYGPVFKTHLLGRPTVFVIGAEAVRFILsgegKLVRYGWPRSVRrllgenSLSLQDGEehrrrrk 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 107 -----MGTVNLHQFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLfnksLFSTNKKKIKEFHQYFQVYDED- 180
Cdd:cd11044    85 llapaFSREALESYVPTIQAIVQSYLRKWLKAGEVALYPELRRLTFDVAARLL----LGLDPEVEAEALSQDFETWTDGl 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 181 FEYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKAC--KSAKDNSMTLLQATLDIVE---TETSKENSpnygLLLLWASL 255
Cdd:cd11044   161 FSLPVPLPFTPFGRAIRARNKLLARLEQAIRERQEEenAEAKDALGLLLEAKDEDGEplsMDELKDQA----LLLLFAGH 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 256 SNAVPVAFWTLAYVLSHPDIHKAImegissvfgKAGKDKIKVSED-DLENLLLIKW--CVL-ETIRLKAP-GVITRKVVK 330
Cdd:cd11044   237 ETTASALTSLCFELAQHPDVLEKL---------RQEQDALGLEEPlTLESLKKMPYldQVIkEVLRLVPPvGGGFRKVLE 307
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 331 PVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQC 394
Cdd:cd11044   308 DFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPFSLIPFGGGPREC 371
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
199-395 5.60e-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: 84.96  E-value: 5.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 199 KKWFLELFEKNIPDI-----------------KACKSAKDNSMTLLQATLDIVETETS-----KENSPNYGLLLLWASLS 256
Cdd:cd20655   163 KKLDLQGFGKRIMDVsnrfdelleriikeheeKRKKRKEGGSKDLLDILLDAYEDENAeykitRNHIKAFILDLFIAGTD 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 257 NAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEIL 335
Cdd:cd20655   243 TSAATTEWAMAELINNPEVLEKAREEIDSV---VGKTRL-VQESDLPNLPYLQAVVKETLRLHPPGpLLVRESTEGCKIN 318
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462608768 336 NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWkKANLEKHSFLDC------FMAFGSGKFQCP 395
Cdd:cd20655   319 GYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERF-LASSRSGQELDVrgqhfkLLPFGSGRRGCP 383
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
118-398 1.32e-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: 83.96  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 118 QLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNKSLFSTNKKK----IKEFHQYFQVYDE-DFEYGSQLPECL- 191
Cdd:cd20658    91 NLVAYVYNMCKKSNGGGLVNVRDAARHYCGNVIRKLMFGTRYFGKGMEDggpgLEEVEHMDAIFTAlKCLYAFSISDYLp 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 192 -LRNWSkskkwfLELFEKNIPD----IKAC---------KSAKDNSMTLLQATLDIVETETSKENSPnygLL-------- 249
Cdd:cd20658   171 fLRGLD------LDGHEKIVREamriIRKYhdpiideriKQWREGKKKEEEDWLDVFITLKDENGNP---LLtpdeikaq 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 250 ---LLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVI 324
Cdd:cd20658   242 ikeLMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRV---VGKERL-VQESDIPNLNYVKACAREAFRLHpvAPFNV 317
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462608768 325 TRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE----KHSFLdcFMAFGSGKFQCPARK 398
Cdd:cd20658   318 PHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEvtltEPDLR--FISFSTGRRGCPGVK 393
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
264-390 4.99e-17

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: 82.25  E-value: 4.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGkdkikvsEDDLENLLLIKWCVLETIRLKAPGVIT-RKVVKPVEILNYIIPSG 342
Cdd:cd11053   245 WAFYWLHRHPEVLARLLAELDALGGDPD-------PEDIAKLPYLDAVIKETLRLYPVAPLVpRRVKEPVELGGYTLPAG 317
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462608768 343 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSfldcFMAFGSG 390
Cdd:cd11053   318 TTVAPSIYLTHHRPDLYPDPERFRPERFLGRKPSPYE----YLPFGGG 361
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
264-395 6.71e-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: 6.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDI-HKAIMEgISSvfgKAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIP 340
Cdd:cd20653   249 WAMSNLLNHPEVlKKAREE-IDT---QVGQDRL-IEESDLPKLPYLQNIISETLRLYpaAPLLVPHESSEDCKIGGYDIP 323
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462608768 341 SGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSfldcFMAFGSGKFQCP 395
Cdd:cd20653   324 RGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEEREGYK----LIPFGLGRRACP 374
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
265-396 1.25e-16

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: 81.05  E-value: 1.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLAYVL----SHPDIHKAIMEGISSVFGKAGKdkiKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEI--LNY 337
Cdd:cd11056   248 TLSFALyelaKNPEIQEKLREEIDEVLEKHGG---ELTYEALQEMKYLDQVVNETLRKYPPlPFLDRVCTKDYTLpgTDV 324
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 338 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQCPA 396
Cdd:cd11056   325 VIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKrHPY--TYLPFGDGPRNCIG 382
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
264-394 1.62e-16

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: 80.77  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDDLENLLLIKWCVLETIRLkAPGV--ITRKVVKPVEILNYIIPS 341
Cdd:cd20660   254 WALYLIGSHPEVQEKVHEELDRIFGD---SDRPATMDDLKEMKYLECVIKEALRL-FPSVpmFGRTLSEDIEIGGYTIPK 329
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQC 394
Cdd:cd20660   330 GTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGrHPY--AYIPFSAGPRNC 381
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
262-379 2.87e-16

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: 79.87  E-value: 2.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 262 AFwTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLlliKW--CVL-ETIRLKAP-GVITRKVVKPVEILNY 337
Cdd:cd20613   255 SF-TLLELGRHPEILKRLQAEVDEVLG----SKQYVEYEDLGKL---EYlsQVLkETLRLYPPvPGTSRELTKDIELGGY 326
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462608768 338 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHS 379
Cdd:cd20613   327 KIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIP 368
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
44-395 4.72e-16

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: 79.17  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  44 EFGKAPLEFIEKARiKYGPIFTVFAMGNRMTFVTEEEGINVFLK-----SKKVDFELAVQNIVYHTGKMGTVN--LHQ-- 114
Cdd:COG2124    16 AFLRDPYPFYARLR-EYGPVFRVRLPGGGAWLVTRYEDVREVLRdprtfSSDGGLPEVLRPLPLLGDSLLTLDgpEHTrl 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 115 -------FTGQLTEELH--------EQLENLGTHGTMDLNNLVRHLLyPVTVNMlfnkSLFSTNKKKIKEFHQYFQVYde 179
Cdd:COG2124    95 rrlvqpaFTPRRVAALRprireiadELLDRLAARGPVDLVEEFARPL-PVIVIC----ELLGVPEEDRDRLRRWSDAL-- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 180 dFEYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKAckSAKDNSMT-LLQATLDivETETSKENSPNYGLLLLWASL--- 255
Cdd:COG2124   168 -LDALGPLPPERRRRARRARAELDAYLRELIAERRA--EPGDDLLSaLLAARDD--GERLSDEELRDELLLLLLAGHett 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 256 SNAVPVAFWTLayvLSHPDIHKAIMEGISsvfgkagkdkikvseddlenllLIKWCVLETIRLKAPG-VITRKVVKPVEI 334
Cdd:COG2124   243 ANALAWALYAL---LRHPEQLARLRAEPE----------------------LLPAAVEETLRLYPPVpLLPRTATEDVEL 297
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462608768 335 LNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAnlekhsfldcFMAFGSGKFQCP 395
Cdd:COG2124   298 GGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDRPPNA----------HLPFGGGPHRCL 348
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
264-394 5.41e-16

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: 79.33  E-value: 5.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRL-KAPGVITRKVVKPVEI--LNYIIP 340
Cdd:cd11046   262 WTLYELSQNPELMAKVQAEVDAVLG----DRLPPTYEDLKKLKYTRRVLNESLRLyPQPPVLIRRAVEDDKLpgGGVKVP 337
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462608768 341 SGDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFLD-CFMAFGSGKFQC 394
Cdd:cd11046   338 AGTDIFISVYNLHRSPELWEDPEEFDPERFldPFINPPNEVIDDfAFLPFGGGPRKC 394
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
23-396 6.14e-16

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 79.35  E-value: 6.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  23 RKNLRRPPCIKGwIPWIGVGFEFGK-APLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFE----LAV 97
Cdd:PLN03234   24 KKSLRLPPGPKG-LPIIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTarplLKG 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  98 QNIVYHTG----------------KMGTVNLHQ------FTGQLTEELHEQLENL----GTHGTMDLNNLVRHLLYPVTV 151
Cdd:PLN03234  103 QQTMSYQGrelgfgqytayyremrKMCMVNLFSpnrvasFRPVREEECQRMMDKIykaaDQSGTVDLSELLLSFTNCVVC 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 152 NMLFNKSL--FSTNKKKIKEFHQYFQVYDEDFEYGSQLP-----ECLLRNWSKSKKWFLEL---FEKNIPDIKACKSAKD 221
Cdd:PLN03234  183 RQAFGKRYneYGTEMKRFIDILYETQALLGTLFFSDLFPyfgflDNLTGLSARLKKAFKELdtyLQELLDETLDPNRPKQ 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 222 NSMTLLQATLDIVETET-----SKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGkagkDKIK 296
Cdd:PLN03234  263 ETESFIDLLMQIYKDQPfsikfTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIG----DKGY 338
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 297 VSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPE-PELFKPERWkka 373
Cdd:PLN03234  339 VSEEDIPNLPYLKAVIKESLRLEPviPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERF--- 415
                         410       420
                  ....*....|....*....|....*....
gi 2462608768 374 nLEKHSFLDC------FMAFGSGKFQCPA 396
Cdd:PLN03234  416 -MKEHKGVDFkgqdfeLLPFGSGRRMCPA 443
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
57-395 8.36e-16

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: 78.38  E-value: 8.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  57 RIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFEL----AVQNIVyhtGK--MGTVN--LH--------------- 113
Cdd:cd11043     2 IKRYGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSwypkSVRKLL---GKssLLTVSgeEHkrlrglllsflgpea 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 114 ---QFTGQLTEELHEQLENLGTHGTMDLNNLVRHLLYPVTVNMLFNkslfSTNKKKIKEFHQYFQvydeDFEYGS-QLPE 189
Cdd:cd11043    79 lkdRLLGDIDELVRQHLDSWWRGKSVVVLELAKKMTFELICKLLLG----IDPEEVVEELRKEFQ----AFLEGLlSFPL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 190 CLL-----RNWsKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVETETSK---ENSPNYGLLLLWASLSNAVPV 261
Cdd:cd11043   151 NLPgttfhRAL-KARKRIRKELKKIIEERRAELEKASPKGDLLDVLLEEKDEDGDSltdEEILDNILTLLFAGHETTSTT 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 262 AFWTLAYVLSHPDI-------HKAIMegissvfgKAGKDKIKVSEDDLENLlliK--WCV-LETIRLK--APGVItRKVV 329
Cdd:cd11043   230 LTLAVKFLAENPKVlqelleeHEEIA--------KRKEEGEGLTWEDYKSM---KytWQViNETLRLApiVPGVF-RKAL 297
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462608768 330 KPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKhSFldCFMAFGSGKFQCP 395
Cdd:cd11043   298 QDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGV-PY--TFLPFGGGPRLCP 360
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
60-395 8.37e-16

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: 78.41  E-value: 8.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  60 YGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDF-----------------ELAVQN----------IVYHTGKMGTVNL 112
Cdd:cd11027     1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFagrpklftfdlfsrggkDIAFGDysptwklhrkLAHSALRLYASGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 113 HQFTGQLTEELHEQLENLGTHG--TMDLNNLVRHLLYPVTVNMLFNKSlFSTNKKKIKEFHQYFQVYDEDFEYGSQ---- 186
Cdd:cd11027    81 PRLEEKIAEEAEKLLKRLASQEgqPFDPKDELFLAVLNVICSITFGKR-YKLDDPEFLRLLDLNDKFFELLGAGSLldif 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 187 -----LPECLLRNWSKSKKWFLELFEK------------NIPDIkacksakdnSMTLLQATLDIvetetSKENSPNYGLL 249
Cdd:cd11027   160 pflkyFPNKALRELKELMKERDEILRKkleehketfdpgNIRDL---------TDALIKAKKEA-----EDEGDEDSGLL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 250 -----------LLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKvSEDDLENLLLIKWCVLETIRL 318
Cdd:cd11027   226 tddhlvmtisdIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGR---DRLP-TLSDRKRLPYLEATIAEVLRL 301
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462608768 319 K--APGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCP 395
Cdd:cd11027   302 SsvVPLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVPKPESFLPFSAGRRVCL 380
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
264-395 1.02e-15

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: 78.22  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVfgkaGKDKIKVSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 341
Cdd:cd20652   256 WFLLYMALFPKEQRRIQRELDEV----VGRPDLVTLEDLSSLPYLQACISESQRIRSvvPLGIPHGCTEDAVLAGYRIPK 331
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFldcFMAFGSGKFQCP 395
Cdd:cd20652   332 GSMIIPLLWAVHMDPNLWEEPEEFRPERFldTDGKYLKPEA---FIPFQTGKRMCL 384
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
3-395 1.39e-15

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 78.33  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768   3 LISPTVIIILGCLALFLLLQRKNLRRPPCIKGWiPWIGVGFEFGKAPLEFIEKARIKYGPIFTVfAMGNRMTFVTEEEGI 82
Cdd:PLN03112    8 LLFSVLIFNVLIWRWLNASMRKSLRLPPGPPRW-PIVGNLLQLGPLPHRDLASLCKKYGPLVYL-RLGSVDAITTDDPEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  83 ---------NVFLKSKKV-----------DFELA--------VQNIVYHTgKMGTVNLHQFTGQLTEELHEQLENLGTHG 134
Cdd:PLN03112   86 ireillrqdDVFASRPRTlaavhlaygcgDVALAplgphwkrMRRICMEH-LLTTKRLESFAKHRAEEARHLIQDVWEAA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 135 -TMDLNNLvRHLLYPVTVN----MLFNKSLF---STNKKKIKEF----HQYFQ----VYDEDF--EYGSQLPECLLRNWS 196
Cdd:PLN03112  165 qTGKPVNL-REVLGAFSMNnvtrMLLGKQYFgaeSAGPKEAMEFmhitHELFRllgvIYLGDYlpAWRWLDPYGCEKKMR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 197 KSKKWFLELFEKNIPDIKACKSAKDNS---MTLLQATLDIvETETSKENSPNYGL------LLLWASLSNAVpVAFWTLA 267
Cdd:PLN03112  244 EVEKRVDEFHDKIIDEHRRARSGKLPGgkdMDFVDVLLSL-PGENGKEHMDDVEIkalmqdMIAAATDTSAV-TNEWAMA 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 268 YVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPSGDLL 345
Cdd:PLN03112  322 EVIKNPRVLRKIQEELDSV---VGRNRM-VQESDLVHLNYLRCVVRETFRMHpaGPFLIPHESLRATTINGYYIPAKTRV 397
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 346 MLSPFWLHRNPKYFPEPELFKPER-W--KKANLEKHSFLDC-FMAFGSGKFQCP 395
Cdd:PLN03112  398 FINTHGLGRNTKIWDDVEEFRPERhWpaEGSRVEISHGPDFkILPFSAGKRKCP 451
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
264-398 2.70e-15

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: 76.92  E-value: 2.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLaYVLS-HPDIHKAIMEGISSVfgKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPS 341
Cdd:cd11069   257 WAL-YLLAkHPDVQERLREEIRAA--LPDPPDGDLSYDDLDRLPYLNAVCRETLRLYPPvPLTSREATKDTVIKGVPIPK 333
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462608768 342 GDLLMLSPFWLHRNPK-YFPEPELFKPERW-----KKANLEKHSFlDCFMAFGSGKFQCPARK 398
Cdd:cd11069   334 GTVVLIPPAAINRSPEiWGPDAEEFNPERWlepdgAASPGGAGSN-YALLTFLHGPRSCIGKK 395
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
264-396 2.85e-15

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: 77.12  E-value: 2.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDI-HKAIMEgISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIP 340
Cdd:cd11072   250 WAMTELIRNPRVmKKAQEE-VREVVG----GKGKVTEEDLEKLKYLKAVIKETLRLHppAPLLLPRECREDCKINGYDIP 324
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462608768 341 SGDLLMLSPFWLHRNPKYFPEPELFKPERwkkanlekhsFLDC----------FMAFGSGKFQCPA 396
Cdd:cd11072   325 AKTRVIVNAWAIGRDPKYWEDPEEFRPER----------FLDSsidfkgqdfeLIPFGAGRRICPG 380
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
264-396 4.14e-15

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: 76.50  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSvfgKAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPGVIT--RKVVKPVEILNYIIPS 341
Cdd:cd20654   263 WALSLLLNNPHVLKKAQEELDT---HVGKDRW-VEESDIKNLVYLQAIVKETLRLYPPGPLLgpREATEDCTVGGYHVPK 338
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW----KKANLEKHSFLdcFMAFGSGKFQCPA 396
Cdd:cd20654   339 GTRLLVNVWKIQRDPNVWSDPLEFKPERFltthKDIDVRGQNFE--LIPFGSGRRSCPG 395
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
264-395 4.86e-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: 76.42  E-value: 4.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd11073   253 WAMAELLRNPEKMAKARAELDEVIGK---DKI-VEESDISKLPYLQAVVKETLRLHppAPLLLPRKAEEDVEVMGYTIPK 328
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERwkkanlekhsFLDC----------FMAFGSGKFQCP 395
Cdd:cd11073   329 GTQVLVNVWAIGRDPSVWEDPLEFKPER----------FLGSeidfkgrdfeLIPFGSGRRICP 382
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
265-394 4.89e-15

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: 76.30  E-value: 4.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLAYVL----SHPDIHKAIMEGISSVFgkagKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKP-VEILNYII 339
Cdd:cd20650   247 TLSFLLyelaTHPDVQQKLQEEIDAVL----PNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKdVEINGVFI 322
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462608768 340 PSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdCFMAFGSGKFQC 394
Cdd:cd20650   323 PKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPY-IYLPFGSGPRNC 376
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
264-398 6.03e-15

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: 75.82  E-value: 6.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAgkdKIKVSEDDLENLLLIKWCVLETIRLK--APgVITRKVVKPVEILNYIIPS 341
Cdd:cd11083   244 WMLYYLASRPDVQARVREEVDAVLGGA---RVPPLLEALDRLPYLEAVARETLRLKpvAP-LLFLEPNEDTVVGDIALPA 319
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462608768 342 GD--LLMLSPFWLhrNPKYFPEPELFKPERW--KKANLEKHSFLDcFMAFGSGKFQCPARK 398
Cdd:cd11083   320 GTpvFLLTRAAGL--DAEHFPDPEEFDPERWldGARAAEPHDPSS-LLPFGAGPRLCPGRS 377
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
265-394 6.16e-15

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: 75.82  E-value: 6.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLAYVLS-HPDIHKAIMEGISSVfgkagkDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSG 342
Cdd:cd11045   233 SMAYFLArHPEWQERLREESLAL------GKGTLDYEDLGQLEVTDWVFKEALRLVPPvPTLPRRAVKDTEVLGYRIPAG 306
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 343 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE--KHSFLdcFMAFGSGKFQC 394
Cdd:cd11045   307 TLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEdkVHRYA--WAPFGGGAHKC 358
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
264-394 7.08e-15

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: 75.75  E-value: 7.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFgkagKDKIKVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd20621   251 MCLYYLAKYPEIQEKLRQEIKSVV----GNDDDITFEDLQKLNYLNAFIKEVLRLYnpAPFLFPRVATQDHQIGDLKIKK 326
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFLdcFMAFGSGKFQC 394
Cdd:cd20621   327 GWIVNVGYIYNHFNPKYFENPDEFNPERWlNQNNIEDNPFV--FIPFSAGPRNC 378
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
264-394 7.43e-15

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: 75.57  E-value: 7.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkiKVSEDDLENLLLIKWCVLETIRLkAPGV--ITRKVVKPVEILNYIIPS 341
Cdd:cd20680   265 WSLYLLGSHPEVQRKVHKELDEVFGKSDR---PVTMEDLKKLRYLECVIKESLRL-FPSVplFARSLCEDCEIRGFKVPK 340
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQC 394
Cdd:cd20680   341 GVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGrHPY--AYIPFSAGPRNC 392
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
118-395 1.35e-14

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: 74.95  E-value: 1.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 118 QLTEELHEQLENLgthgtmdLNNLVRHLLYPVTVNMLFNKSL------------FSTNKKKIKE----FHQYFQVYDEDF 181
Cdd:cd20651    79 SMEEVIQEEAEEL-------IDLLKKGEKGPIQMPDLFNVSVlnvlwamvagerYSLEDQKLRKllelVHLLFRNFDMSG 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 182 EYGSQLPecLLR----NWSK------SKKWFLELFEKNIPDIKAcKSAKDNSMTLLQATLDIVETETSKENSPNY----- 246
Cdd:cd20651   152 GLLNQFP--WLRfiapEFSGynllveLNQKLIEFLKEEIKEHKK-TYDEDNPRDLIDAYLREMKKKEPPSSSFTDdqlvm 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 247 GLL-LLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKvSEDDLENLLLIKWCVLETIRLK--APGV 323
Cdd:cd20651   229 ICLdLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGR---DRLP-TLDDRSKLPYTEAVILEVLRIFtlVPIG 304
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462608768 324 ITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANlEKHSFLDCFMAFGSGKFQCP 395
Cdd:cd20651   305 IPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDED-GKLLKDEWFLPFGAGKRRCL 375
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
248-398 2.57e-14

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: 74.02  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 248 LLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKDK---IKVSEDDLENLLLIKWCVLETIRLKAPGVI 324
Cdd:cd20634   227 LLQLWATQGNAGPAAFWLLLFLLKHPEAMAAVRGEIQRIKHQRGQPVsqtLTINQELLDNTPVFDSVLSETLRLTAAPFI 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 325 TRKVVKPVEIL-----NYIIPSGDLLMLSPFWL-HRNPKYFPEPELFKPERWKKA-NLEKHSF------LDCF-MAFGSG 390
Cdd:cd20634   307 TREVLQDMKLRladgqEYNLRRGDRLCLFPFLSpQMDPEIHQEPEVFKYDRFLNAdGTEKKDFykngkrLKYYnMPWGAG 386

                  ....*...
gi 2462608768 391 KFQCPARK 398
Cdd:cd20634   387 DNVCIGRH 394
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
264-397 3.00e-14

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: 73.90  E-value: 3.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKAPGVI---TRKVVKPVEILNYIIP 340
Cdd:cd11076   246 WIMARMVLHPDIQSKAQAEIDAAVGGSRR----VADSDVAKLPYLQAVVKETLRLHPPGPLlswARLAIHDVTVGGHVVP 321
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462608768 341 SGDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFL--DCFMA-FGSGKFQCPAR 397
Cdd:cd11076   322 AGTTAMVNMWAITHDPHVWEDPLEFKPERFvAAEGGADVSVLgsDLRLApFGAGRRVCPGK 382
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
265-394 7.27e-14

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: 72.72  E-value: 7.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLAY----VLSHPDIHKAIMEGISSVFGKAGKDkikVSEDDLENLLLIKWCVLETIRLKA--PGVITRkVVKP--VEILN 336
Cdd:cd11059   240 TLTYliweLSRPPNLQEKLREELAGLPGPFRGP---PDLEDLDKLPYLNAVIRETLRLYPpiPGSLPR-VVPEggATIGG 315
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462608768 337 YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN----LEKHSFldcFMAFGSGKFQC 394
Cdd:cd11059   316 YYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSgetaREMKRA---FWPFGSGSRMC 374
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
245-394 7.35e-14

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: 72.47  E-value: 7.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 245 NYGLLLLWASLSNAVPVAfWTLAYVLSHPDIHKAIMEGISSVfgkagkDKIKVSEDDLENLLLIKWCVLETIRLKAP-GV 323
Cdd:cd20614   212 NLRLLVLAGHETTASIMA-WMVIMLAEHPAVWDALCDEAAAA------GDVPRTPAELRRFPLAEALFRETLRLHPPvPF 284
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462608768 324 ITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANlEKHSFLDcFMAFGSGKFQC 394
Cdd:cd20614   285 VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRD-RAPNPVE-LLQFGGGPHFC 353
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
187-397 1.16e-13

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: 71.84  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 187 LPECLLRNW-SKSKKWF---LELFEKNIPDIK---ACKSAKDNSMTLLQATLDIVETETSKENSPNYGLLLLWASLSNAV 259
Cdd:cd11065   162 LPSWLGAPWkRKARELReltRRLYEGPFEAAKermASGTATPSFVKDLLEELDKEGGLSEEEIKYLAGSLYEAGSDTTAS 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 260 PVAFWTLAYVLsHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNY 337
Cdd:cd11065   242 TLQTFILAMAL-HPEVQKKAQEELDRV---VGPDRL-PTFEDRPNLPYVNAIVKEVLRWRpvAPLGIPHALTEDDEYEGY 316
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462608768 338 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDC-FMAFGSGKFQCPAR 397
Cdd:cd11065   317 FIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPDPpHFAFGFGRRICPGR 377
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
29-395 1.54e-13

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 71.89  E-value: 1.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  29 PPCIKGWiPWIGVGFE-FGKAPLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFE----------LAV 97
Cdd:PLN02196   37 PPGTMGW-PYVGETFQlYSQDPNVFFASKQKRYGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLFKptfpaskermLGK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  98 QNIVYHTG----KMGTVNLHQFTGQLTEELHEQLENLGTH------GTMdLNNLVRHLLYPVTVNMLfnkSLFSTNKKKI 167
Cdd:PLN02196  116 QAIFFHQGdyhaKLRKLVLRAFMPDAIRNMVPDIESIAQEslnsweGTQ-INTYQEMKTYTFNVALL---SIFGKDEVLY 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 168 KE-FHQYFQVYDEDfeYGS---QLPECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNsmtLLQATLDIVETETSKENS 243
Cdd:PLN02196  192 REdLKRCYYILEKG--YNSmpiNLPGTLFHKSMKARKELAQILAKILSKRRQNGSSHND---LLGSFMGDKEGLTDEQIA 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 244 PNYgLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFgKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGV 323
Cdd:PLN02196  267 DNI-IGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIR-KDKEEGESLTWEDTKKMPLTSRVIQETLRVASILS 344
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462608768 324 IT-RKVVKPVEILNYIIPSGDLLMlsPFW--LHRNPKYFPEPELFKPERWKKANLEkhsflDCFMAFGSGKFQCP 395
Cdd:PLN02196  345 FTfREAVEDVEYEGYLIPKGWKVL--PLFrnIHHSADIFSDPGKFDPSRFEVAPKP-----NTFMPFGNGTHSCP 412
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
256-398 1.79e-13

cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes catalyze the final steps in the production of glucocorticoids and mineralocorticoids that takes place in the adrenal gland. There are two human CYP11B isoforms: Cyb11B1 (11-beta-hydroxylase or P45011beta), which catalyzes the final step of cortisol synthesis by a one-step reaction from 11-deoxycortisol; and CYP11B2 (aldosterone synthase or P450aldo), which catalyzes three steps in the synthesis of aldosterone. The CYP11B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 71.41  E-value: 1.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 256 SNAVPVAFwTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKVseddLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEI 334
Cdd:cd20644   247 TTAFPLLF-TLFELARNPDVQQILRQESLAAAAQISEHPQKA----LTELPLLKAALKETLRLYPVGItVQRVPSSDLVL 321
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 335 LNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDcfMAFGSGKFQCPARK 398
Cdd:cd20644   322 QNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKH--LAFGFGMRQCLGRR 383
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
265-397 2.08e-13

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: 71.10  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLAYVLSHPDIHKAIMEGISSVFgkAGKDKIKvSEDDLENLLLIKWCVLETIRLK--APGVITRKVVK-PVEILNYIIPS 341
Cdd:cd11061   239 IFYYLARNPEAYEKLRAELDSTF--PSDDEIR-LGPKLKSLPYLRACIDEALRLSppVPSGLPRETPPgGLTIDGEYIPG 315
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHsfLDCFMAFGSGKFQCPAR 397
Cdd:cd11061   316 GTTVSVPIYSIHRDERYFPDPFEFIPERWlsRPEELVRA--RSAFIPFSIGPRGCIGK 371
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
264-381 2.14e-13

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: 71.05  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSG 342
Cdd:cd20659   249 WTLYSLAKHPEHQQKCREEVDEVLG----DRDDIEWDDLSKLPYLTMCIKESLRLYPPvPFIARTLTKPITIDGVTLPAG 324
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462608768 343 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK---HSFL 381
Cdd:cd20659   325 TLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKrdpFAFI 366
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
264-395 2.87e-13

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 70.92  E-value: 2.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 341
Cdd:PLN02394  315 WGIAELVNHPEIQKKLRDELDTVLGPGNQ----VTEPDTHKLPYLQAVVKETLRLHMaiPLLVPHMNLEDAKLGGYDIPA 390
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFLDCFMAFGSGKFQCP 395
Cdd:PLN02394  391 ESKILVNAWWLANNPELWKNPEEFRPERFleEEAKVEANGNDFRFLPFGVGRRSCP 446
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
201-398 5.34e-13

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: 70.05  E-value: 5.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 201 WFLELFEKniPDIKACKSAKDNSMTLLQATLDIVETETSKENSPNYGLLLLWAS----------------LSNAVpvaFW 264
Cdd:cd11070   157 PFLDRLPW--VLFPSRKRAFKDVDEFLSELLDEVEAELSADSKGKQGTESVVASrlkrarrsggltekelLGNLF---IF 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLA-------------YVLS-HPDIHKAIMEGISSVFGKAGKDKIKvsEDDLENLLLIKWCVLETIRLKAP-GVITRKVV 329
Cdd:cd11070   232 FIAghettantlsfalYLLAkHPEVQDWLREEIDSVLGDEPDDWDY--EEDFPKLPYLLAVIYETLRLYPPvQLLNRKTT 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 330 KPVEILN-----YIIPSGDLLMLSPFWLHRNPKY-FPEPELFKPERW-----KKANLEKHSFLDC-FMAFGSGKFQCPAR 397
Cdd:cd11070   310 EPVVVITglgqeIVIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWgstsgEIGAATRFTPARGaFIPFSAGPRACLGR 389

                  .
gi 2462608768 398 K 398
Cdd:cd11070   390 K 390
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
264-395 1.58e-12

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: 68.48  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd11028   253 WSLLYMIRYPEIQEKVQAELDRVIGRERLPRL----SDRPNLPYTEAFILETMRHSsfVPFTIPHATTRDTTLNGYFIPK 328
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKhSFLDCFMAFGSGKFQCP 395
Cdd:cd11028   329 GTVVFVNLWSVNHDEKLWPDPSVFRPERFldDNGLLDK-TKVDKFLPFGAGRRRCL 383
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
264-398 1.68e-12

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: 68.63  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLaYVLS-HPDIHKAIMEGISSVFgkagKDKIKVSEDDLENLLLIKWCVLETIRLKA--PG---VITRKvvkPVEILNY 337
Cdd:cd20648   256 WSL-YELSrHPDVQTALHREITAAL----KDNSVPSAADVARMPLLKAVVKEVLRLYPviPGnarVIPDR---DIQVGEY 327
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462608768 338 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDcfMAFGSGKFQCPARK 398
Cdd:cd20648   328 IIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGDTHHPYAS--LPFGFGKRSCIGRR 386
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
265-398 3.44e-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: 67.63  E-value: 3.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLAYVL----SHPDIHKAIMEGISSVFGKAGkdkIKVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILN-YI 338
Cdd:cd11057   246 TVAYTLlllaMHPEVQEKVYEEIMEVFPDDG---QFITYEDLQQLVYLEMVLKETMRLFPVGpLVGRETTADIQLSNgVV 322
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462608768 339 IPSGDLLMLSPFWLHRNPKYF-PEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQCPARK 398
Cdd:cd11057   323 IPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQrHPY--AFIPFSAGPRNCIGWR 382
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
265-397 4.54e-12

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: 67.22  E-value: 4.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLAYVLSHPDIHKAIMEGISSvFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKP--VEILNYIIPS 341
Cdd:cd11060   245 ILYYLLKNPRVYAKLRAEIDA-AVAEGKLSSPITFAEAQKLPYLQAVIKEALRLHPPvGLPLERVVPPggATICGRFIPG 323
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462608768 342 GDLLMLSPFWLHRNPKYF-PEPELFKPERWKKANLEKHSFLD-CFMAFGSGKFQCPAR 397
Cdd:cd11060   324 GTIVGVNPWVIHRDKEVFgEDADVFRPERWLEADEEQRRMMDrADLTFGAGSRTCLGK 381
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
264-398 4.69e-12

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: 67.05  E-value: 4.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKVseddLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILNYIIPSG 342
Cdd:cd20643   256 WTLYELARNPNVQEMLRAEVLAARQEAQGDMVKM----LKSVPLLKAAIKETLRLHPVAVsLQRYITEDLVLQNYHIPAG 331
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462608768 343 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdcfmAFGSGKFQCPARK 398
Cdd:cd20643   332 TLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRNL----GFGFGPRQCLGRR 383
PLN02966 PLN02966
cytochrome P450 83A1
236-398 8.65e-12

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 66.69  E-value: 8.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 236 TETSKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKdkIKVSEDDLENLLLIKWCVLET 315
Cdd:PLN02966  283 SEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGS--TFVTEDDVKNLPYFRALVKET 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 316 IRLKA--PGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPK-YFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKF 392
Cdd:PLN02966  361 LRIEPviPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKeWGPNPDEFRPERFLEKEVDFKGTDYEFIPFGSGRR 440

                  ....*.
gi 2462608768 393 QCPARK 398
Cdd:PLN02966  441 MCPGMR 446
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
264-395 1.25e-11

cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called trans-cinnamate 4-monooxygenase (EC 1.14.14.91) or cinnamic acid 4-hydroxylase, catalyzes the regiospecific 4-hydroxylation of cinnamic acid to form precursors of lignin and many other phenolic compounds. It controls the general phenylpropanoid pathway, and controls carbon flux to pigments essential for pollination or UV protection. CYP73 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 65.96  E-value: 1.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAgkdkIKVSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 341
Cdd:cd11074   255 WGIAELVNHPEIQKKLRDELDTVLGPG----VQITEPDLHKLPYLQAVVKETLRLRMaiPLLVPHMNLHDAKLGGYDIPA 330
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWkkanLEKHSFLDC------FMAFGSGKFQCP 395
Cdd:cd11074   331 ESKILVNAWWLANNPAHWKKPEEFRPERF----LEEESKVEAngndfrYLPFGVGRRSCP 386
PLN02183 PLN02183
ferulate 5-hydroxylase
264-395 1.61e-11

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 65.64  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkdKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSG 342
Cdd:PLN02183  326 WAMAELMKSPEDLKRVQQELADVVGL----NRRVEESDLEKLTYLKCTLKETLRLHPPiPLLLHETAEDAEVAGYFIPKR 401
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462608768 343 DLLMLSPFWLHRNPKYFPEPELFKPERWKKANLE--KHSFLDcFMAFGSGKFQCP 395
Cdd:PLN02183  402 SRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVPdfKGSHFE-FIPFGSGRRSCP 455
PLN02655 PLN02655
ent-kaurene oxidase
248-394 1.65e-11

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 65.53  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 248 LLLLWASLSNAVPVAF----WTLAYVLSHPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRL--KAP 321
Cdd:PLN02655  264 MMLVWEPIIEAADTTLvtteWAMYELAKNPDKQERLYREIREVCGDE-----RVTEEDLPNLPYLNAVFHETLRKysPVP 338
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462608768 322 GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER-----WKKANLEKhsfldcFMAFGSGKFQC 394
Cdd:PLN02655  339 LLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERflgekYESADMYK------TMAFGAGKRVC 410
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
253-398 2.26e-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: 2.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 253 ASLSNAVpvafWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKP 331
Cdd:cd11082   235 ASTSSLV----WALQLLADHPDVLAKVREEQARL---RPNDEPPLTLDLLEEMKYTRQVVKEVLRYRPPAPmVPHIAKKD 307
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462608768 332 VEIL-NYIIPSGDLLMLSPFWLHRNPkyFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQCPARK 398
Cdd:cd11082   308 FPLTeDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQEDRKYKKNFLVFGAGPHQCVGQE 373
PLN02774 PLN02774
brassinosteroid-6-oxidase
23-398 2.27e-11

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 65.18  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  23 RKNLrrPPCIKGWiPWIGVGFEFGKAPLEFIEKARIKYGPIF--------TVFAMG---NRMTFVTEEEGINVFLKSKKV 91
Cdd:PLN02774   29 KKGL--PPGTMGW-PLFGETTEFLKQGPDFMKNQRLRYGSFFkshilgcpTIVSMDpelNRYILMNEGKGLVPGYPQSML 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  92 DFeLAVQNIV--------YHTGKM-GTVNLHQFTGQLTEELHE----QLENLGTHGTMDLNNLVRH--LLYPVTVNMLFN 156
Cdd:PLN02774  106 DI-LGTCNIAavhgsthrYMRGSLlSLISPTMIRDHLLPKIDEfmrsHLSGWDGLKTIDIQEKTKEmaLLSALKQIAGTL 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 157 KSLFSTNKKKikefhQYFQVYDEDFEYGSQLPECLLRNWSKSKKWFLELFEKNIPDIKACKSAKDNSMTLLQATLDIVET 236
Cdd:PLN02774  185 SKPISEEFKT-----EFFKLVLGTLSLPIDLPGTNYRSGVQARKNIVRMLRQLIQERRASGETHTDMLGYLMRKEGNRYK 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 237 ETSKEnSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDI-------HKAIMEGissvfgKAGKDKIKVseDDLENLLLIK 309
Cdd:PLN02774  260 LTDEE-IIDQIITILYSGYETVSTTSMMAVKYLHDHPKAlqelrkeHLAIRER------KRPEDPIDW--NDYKSMRFTR 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 310 WCVLETIRLKA--PGVItRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFldcFMAF 387
Cdd:PLN02774  331 AVIFETSRLATivNGVL-RKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKSLESHNY---FFLF 406
                         410
                  ....*....|.
gi 2462608768 388 GSGKFQCPARK 398
Cdd:PLN02774  407 GGGTRLCPGKE 417
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
210-397 7.13e-11

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: 63.47  E-value: 7.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 210 IPDIKACKSAK-----DNSMTLLQATLDIVETETskENSPN---YGLLLLW-ASLSNAVPVAFWTLAYVLSHPDIHKAIM 280
Cdd:cd11041   188 IPEIERRRKLKkgpkeDKPNDLLQWLIEAAKGEG--ERTPYdlaDRQLALSfAAIHTTSMTLTHVLLDLAAHPEYIEPLR 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 281 EGISSVFGKAGKdkikVSEDDLENLLL----IKwcvlETIRLKAPGVIT--RKVVKPVEILN-YIIPSGDLLMLSPFWLH 353
Cdd:cd11041   266 EEIRSVLAEHGG----WTKAALNKLKKldsfMK----ESQRLNPLSLVSlrRKVLKDVTLSDgLTLPKGTRIAVPAHAIH 337
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462608768 354 RNPKYFPEPELFKPERW-----KKANLEKHSFLDC---FMAFGSGKFQCPAR 397
Cdd:cd11041   338 RDPDIYPDPETFDGFRFyrlreQPGQEKKHQFVSTspdFLGFGHGRHACPGR 389
PLN02687 PLN02687
flavonoid 3'-monooxygenase
264-370 1.14e-10

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 62.91  E-value: 1.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPS 341
Cdd:PLN02687  319 WAIAELIRHPDILKKAQEELDAV---VGRDRL-VSESDLPQLTYLQAVIKETFRLhpSTPLSLPRMAAEECEINGYHIPK 394
                          90       100
                  ....*....|....*....|....*....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW 370
Cdd:PLN02687  395 GATLLVNVWAIARDPEQWPDPLEFRPDRF 423
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
264-394 1.59e-10

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: 62.29  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGkagkDKIKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILN-YIIPS 341
Cdd:cd20678   261 WILYCLALHPEHQQRCREEIREILG----DGDSITWEHLDQMPYTTMCIKEALRLYPPVPgISRELSKPVTFPDgRSLPA 336
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEK-HSFldCFMAFGSGKFQC 394
Cdd:cd20678   337 GITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKrHSH--AFLPFSAGPRNC 388
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
256-398 4.86e-10

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: 61.01  E-value: 4.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 256 SNAVPVAFWTLAyvlSHPDIHKAIMEGISSVFGKagkdKIKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEI 334
Cdd:cd20649   278 TNTLSFATYLLA---THPECQKKLLREVDEFFSK----HEMVDYANVQELPYLDMVIAETLRMYPPAFrFAREAAEDCVV 350
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462608768 335 LNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFLdcFMAFGSGKFQCPARK 398
Cdd:cd20649   351 LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFtAEAKQRRHPFV--YLPFGAGPRSCIGMR 413
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
264-398 5.85e-10

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: 60.59  E-value: 5.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDdLENLLLIKWCVLETIRLkAPGV--ITRKVVKPVEILNYIIPS 341
Cdd:cd20645   248 WILYNLSRNPQAQQKLLQEIQSVLPA---NQTPRAED-LKNMPYLKACLKESMRL-TPSVpfTSRTLDKDTVLGDYLLPK 322
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKanlEKHSfLDCF--MAFGSGKFQCPARK 398
Cdd:cd20645   323 GTVLMINSQALGSSEEYFEDGRQFKPERWLQ---EKHS-INPFahVPFGIGKRMCIGRR 377
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
250-396 6.33e-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: 60.58  E-value: 6.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 250 LLW----ASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRLKAPG--V 323
Cdd:cd20656   234 LLWdmitAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRV---VGSDRV-MTEADFPQLPYLQCVVKEALRLHPPTplM 309
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462608768 324 ITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW--KKANLEKHSFLdcFMAFGSGKFQCPA 396
Cdd:cd20656   310 LPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFleEDVDIKGHDFR--LLPFGAGRRVCPG 382
PLN02971 PLN02971
tryptophan N-hydroxylase
238-396 7.41e-10

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 60.44  E-value: 7.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 238 TSKENSPNYGLLLLWA--SLSNAVPvafWTLAYVLSHPDIHKAIMEGISSVFGKagkdKIKVSEDDLENLLLIKWCVLET 315
Cdd:PLN02971  324 TADEIKPTIKELVMAApdNPSNAVE---WAMAEMINKPEILHKAMEEIDRVVGK----ERFVQESDIPKLNYVKAIIREA 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 316 IRLK--APGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER----WKKANLEKHSFLdcFMAFGS 389
Cdd:PLN02971  397 FRLHpvAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERhlneCSEVTLTENDLR--FISFST 474

                  ....*..
gi 2462608768 390 GKFQCPA 396
Cdd:PLN02971  475 GKRGCAA 481
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
264-394 1.27e-09

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: 59.74  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKiKVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPS 341
Cdd:cd20657   250 WALAELIRHPDILKKAQEEMDQVIGR---DR-RLLESDIPNLPYLQAICKETFRLhpSTPLNLPRIASEACEVDGYYIPK 325
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKanlEKHSFLDC------FMAFGSGKFQC 394
Cdd:cd20657   326 GTRLLVNIWAIGRDPDVWENPLEFKPERFLP---GRNAKVDVrgndfeLIPFGAGRRIC 381
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
264-398 1.88e-09

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: 59.16  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKVSEDdLENLLLIKWCVLETIRLKA--PGViTRKVVKPVEILNYIIPS 341
Cdd:cd20647   259 WATYLLARHPEVQQQVYEEIVRNLGK---RVVPTAED-VPKLPLIRALLKETLRLFPvlPGN-GRVTQDDLIVGGYLIPK 333
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKhsfLDCF--MAFGSGKFQCPARK 398
Cdd:cd20647   334 GTQLALCHYSTSYDEENFPRAEEFRPERWlRKDALDR---VDNFgsIPFGYGIRSCIGRR 390
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
264-394 3.62e-09

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: 58.12  E-value: 3.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAgkdkiKVSEDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILNYIIPSG 342
Cdd:cd11052   254 WTTMLLAIHPEWQEKAREEVLEVCGKD-----KPPSDSLSKLKTVSMVINESLRLYPPAVfLTRKAKEDIKLGGLVIPKG 328
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462608768 343 DLLMLSPFWLHRNPKYFPE-PELFKPERWKK--ANLEKHSflDCFMAFGSGKFQC 394
Cdd:cd11052   329 TSIWIPVLALHHDEEIWGEdANEFNPERFADgvAKAAKHP--MAFLPFGLGPRNC 381
PLN03018 PLN03018
homomethionine N-hydroxylase
253-369 9.68e-09

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 56.94  E-value: 9.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 253 ASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIkVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVK 330
Cdd:PLN03018  325 AAIDNPANNMEWTLGEMLKNPEILRKALKELDEV---VGKDRL-VQESDIPNLNYLKACCRETFRIhpSAHYVPPHVARQ 400
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2462608768 331 PVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER 369
Cdd:PLN03018  401 DTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPER 439
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
24-395 1.02e-08

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 56.91  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  24 KNLRRPPCIKGwIPWIGVGFEFGKA-----PLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDFELAVQ 98
Cdd:PLN02987   27 RRMRLPPGSLG-LPLVGETLQLISAyktenPEPFIDERVARYGSLFMTHLFGEPTVFSADPETNRFILQNEGKLFECSYP 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  99 NIVyhTGKMGTVNLHQFTGQLTEELHEQLENLGT------HGTMDLNNLVRHLLYPVTVNMLF----NKSLFSTNKKKIK 168
Cdd:PLN02987  106 GSI--SNLLGKHSLLLMKGNLHKKMHSLTMSFANssiikdHLLLDIDRLIRFNLDSWSSRVLLmeeaKKITFELTVKQLM 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 169 EF----------HQYFQVYDEDFEYGSQLPECLLRNWSKSKKWFLE-----LFEKNIPDIKACKSAKDnsmtLLQATLDi 233
Cdd:PLN02987  184 SFdpgewteslrKEYVLVIEGFFSVPLPLFSTTYRRAIQARTKVAEaltlvVMKRRKEEEEGAEKKKD----MLAALLA- 258
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 234 VETETSKENSPNYGLLLLWASLSNAVPVAFWTLAYVLSHPDIHKAIMEGISSVFGKAGkDKIKVSEDDLENLLLIKWCVL 313
Cdd:PLN02987  259 SDDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKS-DSYSLEWSDYKSMPFTQCVVN 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 314 ETIRL-KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKaNLEKHSFLDCFMAFGSGKF 392
Cdd:PLN02987  338 ETLRVaNIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQS-NSGTTVPSNVFTPFGGGPR 416

                  ...
gi 2462608768 393 QCP 395
Cdd:PLN02987  417 LCP 419
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
264-394 1.09e-08

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: 56.62  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFgkAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVEILN-YIIPS 341
Cdd:cd20679   266 WILYNLARHPEYQERCRQEVQELL--KDREPEEIEWDDLAQLPFLTMCIKESLRLHPPvTAISRCCTQDIVLPDgRVIPK 343
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdCFMAFGSGKFQC 394
Cdd:cd20679   344 GIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPL-AFIPFSAGPRNC 395
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
23-394 1.12e-08

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 56.78  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  23 RKNLRR-PPCIKGWiPWIGVGFEFGKAPLEFIEKARIKYGPIFTVFAMGNRMTFVTEEEGINVFLKSKKVDF-----ELA 96
Cdd:PLN00110   26 PKPSRKlPPGPRGW-PLLGALPLLGNMPHVALAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFsnrppNAG 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  97 VQNIVYHTGKM-------------GTVNLHQFTGQlteelheQLENLGTHGTMDLNNLVRHLLY------PVTV------ 151
Cdd:PLN00110  105 ATHLAYGAQDMvfadygprwkllrKLSNLHMLGGK-------ALEDWSQVRTVELGHMLRAMLElsqrgePVVVpemltf 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 152 ---NMLFNKSL----FSTNKKKIKEFHQY---FQVYDEDFEYGSQLP-------ECLLRNWSKSKKWFLELFEKNIPDIK 214
Cdd:PLN00110  178 smaNMIGQVILsrrvFETKGSESNEFKDMvveLMTTAGYFNIGDFIPsiawmdiQGIERGMKHLHKKFDKLLTRMIEEHT 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 215 ACKSAKDNSMTLLqatlDIVETEtsKENSP-------NYGLLLL---WASLSNAVPVAFWTLAYVLSHPDIHKAIMEGIS 284
Cdd:PLN00110  258 ASAHERKGNPDFL----DVVMAN--QENSTgekltltNIKALLLnlfTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMD 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 285 SVFGKAGKdkikVSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEP 362
Cdd:PLN00110  332 QVIGRNRR----LVESDLPKLPYLQAICKESFRKhpSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENP 407
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 2462608768 363 ELFKPERWKKanlEKHSFLDC------FMAFGSGKFQC 394
Cdd:PLN00110  408 EEFRPERFLS---EKNAKIDPrgndfeLIPFGAGRRIC 442
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
265-398 1.42e-08

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: 56.21  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLAYVLSH----PDIHKAIMEGISSVfgkAGKDKIKVSEDdLENLLLIKWCVLETIRLkAPGVIT--RKVV-KPVEILNY 337
Cdd:cd20646   252 TLSWALYHlardPEIQERLYQEVISV---CPGDRIPTAED-IAKMPLLKAVIKETLRL-YPVVPGnaRVIVeKEVVVGDY 326
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462608768 338 IIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW-KKANLEKHSFldCFMAFGSGKFQCPARK 398
Cdd:cd20646   327 LFPKNTLFHLCHYAVSHDETNFPEPERFKPERWlRDGGLKHHPF--GSIPFGYGVRACVGRR 386
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
262-394 2.89e-08

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: 55.27  E-value: 2.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 262 AFwTLAYVLSHPDIHKAIMEGISSVFGKAGkdkikVSEDDLENLLLIKWCVLETIRLKAPG-VITRKVVKPVEILN-YII 339
Cdd:cd11068   251 SF-ALYYLLKNPEVLAKARAEVDEVLGDDP-----PPYEQVAKLRYIRRVLDETLRLWPTApAFARKPKEDTVLGGkYPL 324
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462608768 340 PSGD-LLMLSPFwLHRNPK-YFPEPELFKPERWKKANLEKHSfLDCFMAFGSGKFQC 394
Cdd:cd11068   325 KKGDpVLVLLPA-LHRDPSvWGEDAEEFRPERFLPEEFRKLP-PNAWKPFGNGQRAC 379
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
264-394 6.70e-08

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: 54.25  E-value: 6.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd20673   254 WIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTL----SDRNHLPLLEATIREVLRIRpvAPLLIPHVALQDSSIGEFTIPK 329
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERwkkanlekhsFLD-----------CFMAFGSGKFQC 394
Cdd:cd20673   330 GTRVVINLWALHHDEKEWDQPDQFMPER----------FLDptgsqlispslSYLPFGAGPRVC 383
PTZ00404 PTZ00404
cytochrome P450; Provisional
264-394 7.38e-08

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 54.34  E-value: 7.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGkaGKDKIKVSedDLENLLLIKWCVLETIRLKAPGV--ITRKVVKPVEILN-YIIP 340
Cdd:PTZ00404  305 WMVLMLCNYPEIQEKAYNEIKSTVN--GRNKVLLS--DRQSTPYTVAIIKETLRYKPVSPfgLPRSTSNDIIIGGgHFIP 380
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 341 SGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEkhsflDCFMAFGSGKFQC 394
Cdd:PTZ00404  381 KDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDSN-----DAFMPFSIGPRNC 429
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
264-395 1.11e-07

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: 53.33  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLaYVLS-HPDIHKAIMEGISSVFGKAGKDKikvsEDDLENLLLIKWCVLETIRLkAPGVI--TRKVVK---------- 330
Cdd:cd11063   238 FLF-YELArHPEVWAKLREEVLSLFGPEPTPT----YEDLKNMKYLRAVINETLRL-YPPVPlnSRVAVRdttlprgggp 311
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 331 ----PVeilnyIIPSGDLLMLSPFWLHRNPK-YFPEPELFKPERWkkANLEKHSFLdcFMAFGSGKFQCP 395
Cdd:cd11063   312 dgksPI-----FVPKGTRVLYSVYAMHRRKDiWGPDAEEFRPERW--EDLKRPGWE--YLPFNGGPRICL 372
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
264-398 1.37e-07

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: 53.24  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKagkDKIKvSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 341
Cdd:cd20666   250 WCLLYMSLYPEVQEKVQAEIDTVIGP---DRAP-SLTDKAQMPFTEATIMEVQRMTVvvPLSIPHMASENTVLQGYTIPK 325
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN---LEKHSfldcFMAFGSGKFQCPARK 398
Cdd:cd20666   326 GTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENgqlIKKEA----FIPFGIGRRVCMGEQ 381
PLN02738 PLN02738
carotene beta-ring hydroxylase
250-394 1.54e-07

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 53.38  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 250 LLWASLSNAVPVAFWTLaYVLS-HPDIHKAIMEGISSVFGkagkDKIKVSEDdLENLLLIKWCVLETIRL-KAPGVITRK 327
Cdd:PLN02738  399 MLIAGHETSAAVLTWTF-YLLSkEPSVVAKLQEEVDSVLG----DRFPTIED-MKKLKYTTRVINESLRLyPQPPVLIRR 472
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462608768 328 VVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW----KKANLEKHSFldCFMAFGSGKFQC 394
Cdd:PLN02738  473 SLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpldgPNPNETNQNF--SYLPFGGGPRKC 541
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
264-394 2.01e-07

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: 52.80  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKvsedDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd20674   248 WAVAFLLHHPEIQDRLQEELDRVLGPGASPSYK----DRARLPLLNATIAEVLRLRpvVPLALPHRTTRDSSIAGYDIPK 323
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLdcfmAFGSGKFQC 394
Cdd:cd20674   324 GTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAANRALL----PFGCGARVC 372
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
68-400 2.40e-07

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: 52.41  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768  68 AMGNRMTFVTEEEginvflkSKKVDFELAVQNIVYHTGKmgtvNLHQFTGQLTEELhEQLENLGTHGTMDLNNLVRHLLY 147
Cdd:cd20626    63 AFGITNAFTSPDT-------SVHKDFVKKARGLINLSAA----DWELLTQAIQATL-RRWISHATGGCVNLAELVQALTL 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 148 PVTVNMLFNKSLfstnkkkikefhqyfQVYDEDFEYGSQLPECLLRNWSKSKKWFLEL-FEKNIpdikacksakdnsmtL 226
Cdd:cd20626   131 RVVLVGLFQSDT---------------DALSLPDESLLDLAEAINELWISSKSGPDPPpFSDNI---------------D 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 227 LQATLDIVETETSKENSPNYGLLLL---WASLSNAVPVAFWTLAY----VLSHPDIHKAIMEGISSVFGKAGKDKIKVSE 299
Cdd:cd20626   181 LQDALRRVFPDLNDIDPFENPLNLIlpaFETMWRVVLRTFLEIHYlkgsPTLRDPTHPEWREANADFAKSATKDGISAKN 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 300 ddlenllLIKwcvlETIRLKAPgviTRKVVK--------PVEILNYIIPSgdllmlspfwLHRNPKYF-PEPELFKPERW 370
Cdd:cd20626   261 -------LVK----EALRLYPP---TRRIYRafqrpgssKPEIIAADIEA----------CHRSESIWgPDALEFNPSRW 316
                         330       340       350
                  ....*....|....*....|....*....|
gi 2462608768 371 KKANLEKHsflDCFMAFGSGKFQCPARKGF 400
Cdd:cd20626   317 SKLTPTQK---EAFLPFGSGPFRCPAKPVF 343
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
265-370 2.64e-07

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: 52.20  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLAYVLSHPDIHKAIMEGISSVFGkagkdkikvSEDD-----LENLLLIKWCVLETIRL--KAPGVITRKVVKP-VEILN 336
Cdd:cd11058   240 LTYYLLKNPEVLRKLVDEIRSAFS---------SEDDitldsLAQLPYLNAVIQEALRLypPVPAGLPRVVPAGgATIDG 310
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462608768 337 YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW 370
Cdd:cd11058   311 QFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERW 344
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
191-394 5.34e-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: 51.34  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 191 LLRNWSKSKKWFLELFEKNIPDIKAcksakDNSMTLLQATLdiveTETSKENSPNYG----------LLLLWASLSNAVP 260
Cdd:cd20662   173 VFSNWKKLKLFVSDMIDKHREDWNP-----DEPRDFIDAYL----KEMAKYPDPTTSfneenlicstLDLFFAGTETTST 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 261 VAFWTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYI 338
Cdd:cd20662   244 TLRWALLYMALYPEIQEKVQAEIDRVIGQKRQ----PSLADRESMPYTNAVIHEVQRMGniIPLNVPREVAVDTKLAGFH 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462608768 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 8.79e-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: 50.64  E-value: 8.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKdkikVSEDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd11026   248 WALLLLMKYPHIQEKVQEEIDRVIGRNRT----PSLEDRAKMPYTDAVIHEVQRFGdiVPLGVPHAVTRDTKFRGYTIPK 323
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462608768 342 GD--LLMLSPfwLHRNPKYFPEPELFKPERW--KKANLEKHsflDCFMAFGSGKFQCP 395
Cdd:cd11026   324 GTtvIPNLTS--VLRDPKQWETPEEFNPGHFldEQGKFKKN---EAFMPFSAGKRVCL 376
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
252-369 1.39e-06

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: 49.95  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 252 WASLSNAVPVAFWTLAyvLSHPDIHKAIMEGISSVFGKAGKDKIKVseddLENLLLIKWCVLETIRLKAP-GVITRKVVK 330
Cdd:cd11071   238 FGGFSALLPSLLARLG--LAGEELHARLAEEIRSALGSEGGLTLAA----LEKMPLLKSVVYETLRLHPPvPLQYGRARK 311
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2462608768 331 PVEILN----YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPER 369
Cdd:cd11071   312 DFVIEShdasYKIKKGELLVGYQPLATRDPKVFDNPDEFVPDR 354
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
263-398 1.59e-06

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: 49.90  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 263 FWTLAyvlSHPDIHKAIMEGISSVFGKAGKDKIKV-SEDDLENLLLIKWCVLETIRLKAP-GVITRKVVKPVeIL--NYI 338
Cdd:cd11064   254 FWLLS---KNPRVEEKIREELKSKLPKLTTDESRVpTYEELKKLVYLHAALSESLRLYPPvPFDSKEAVNDD-VLpdGTF 329
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462608768 339 IPSGDLLMLSPFWLHRNPKYF-PEPELFKPERWkkanLEKHSFLDC-----FMAFGSGKFQCPARK 398
Cdd:cd11064   330 VKKGTRIVYSIYAMGRMESIWgEDALEFKPERW----LDEDGGLRPespykFPAFNAGPRICLGKD 391
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
263-394 2.33e-06

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: 49.28  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 263 FWTLAYVLSHPDIHKAIMEGISSVFGkaGKDkikVSEDDLENLLLIKWCVLETIRLKaPGV--ITRKVVKPVEILNYIIP 340
Cdd:cd20616   245 FFMLLLIAQHPEVEEAILKEIQTVLG--ERD---IQNDDLQKLKVLENFINESMRYQ-PVVdfVMRKALEDDVIDGYPVK 318
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462608768 341 SGDLLMLSPFWLHRNPkYFPEPELFKPErwkkaNLEKHSFLDCFMAFGSGKFQC 394
Cdd:cd20616   319 KGTNIILNIGRMHRLE-FFPKPNEFTLE-----NFEKNVPSRYFQPFGFGPRSC 366
PLN02302 PLN02302
ent-kaurenoic acid oxidase
261-395 2.47e-06

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 49.33  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 261 VAFWTLAYVLSHPDIH---KAIMEGISSvfgKAGKDKIKVSEDDLENLLLIKWCVLETIRL-KAPGVITRKVVKPVEILN 336
Cdd:PLN02302  306 LTMWATIFLQEHPEVLqkaKAEQEEIAK---KRPPGQKGLTLKDVRKMEYLSQVIDETLRLiNISLTVFREAKTDVEVNG 382
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462608768 337 YIIPSGDLLMLspfWL---HRNPKYFPEPELFKPERWKKANLEKHSFLdcfmAFGSGKFQCP 395
Cdd:PLN02302  383 YTIPKGWKVLA---WFrqvHMDPEVYPNPKEFDPSRWDNYTPKAGTFL----PFGLGSRLCP 437
PLN00168 PLN00168
Cytochrome P450; Provisional
264-370 3.45e-06

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 49.18  E-value: 3.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSvfgKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPG--VITRKVVKPVEILNYIIPS 341
Cdd:PLN00168  328 WIMAELVKNPSIQSKLHDEIKA---KTGDDQEEVSEEDVHKMPYLKAVVLEGLRKHPPAhfVLPHKAAEDMEVGGYLIPK 404
                          90       100
                  ....*....|....*....|....*....
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERW 370
Cdd:PLN00168  405 GATVNFMVAEMGRDEREWERPMEFVPERF 433
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
314-395 3.69e-06

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 48.97  E-value: 3.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 314 ETIRL-KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKhsflDCFMAFGSGKF 392
Cdd:PLN03141  323 ETLRMgNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEKDMNN----SSFTPFGGGQR 398

                  ...
gi 2462608768 393 QCP 395
Cdd:PLN03141  399 LCP 401
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
314-390 3.81e-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: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 314 ETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLspfWL---HRNPKYFPEPELFKPERwkKANleKHsfldcfMAFGS 389
Cdd:cd11032   248 EVLRYRPPvQRTARVTTEDVELGGVTIPAGQLVIA---WLasaNRDERQFEDPDTFDIDR--NPN--PH------LSFGH 314

                  .
gi 2462608768 390 G 390
Cdd:cd11032   315 G 315
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
236-394 3.88e-06

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: 48.80  E-value: 3.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 236 TETSkENSPNYGLLLLwaslsnavpvafwtlayvLSHPDIHKAIMEGISSVFGK----AGKDKIKVSEDDlenlllikwC 311
Cdd:cd20665   239 TETT-STTLRYGLLLL------------------LKHPEVTAKVQEEIDRVIGRhrspCMQDRSHMPYTD---------A 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 312 VLETIRLKA---PGVITRKVVKPVEILNYIIPSGD--LLMLSPFwLHrNPKYFPEPELFKPERW--KKANLEKHsflDCF 384
Cdd:cd20665   291 VIHEIQRYIdlvPNNLPHAVTCDTKFRNYLIPKGTtvITSLTSV-LH-DDKEFPNPEKFDPGHFldENGNFKKS---DYF 365
                         170
                  ....*....|
gi 2462608768 385 MAFGSGKFQC 394
Cdd:cd20665   366 MPFSAGKRIC 375
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
314-395 4.87e-06

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: 48.37  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 314 ETIRLKAPGVIT-RKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERwkkANLEKHsfldcfMAFGSGKF 392
Cdd:cd11078   259 ETLRYDSPVQGLrRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR---PNARKH------LTFGHGIH 329

                  ...
gi 2462608768 393 QCP 395
Cdd:cd11078   330 FCL 332
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
312-397 7.00e-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: 47.72  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 312 VLETIRLK--APGVItRKVVKPVEIL-----NYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERwkkaNLEKhsfldcF 384
Cdd:cd20612   244 VLEALRLNpiAPGLY-RRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR----PLES------Y 312
                          90
                  ....*....|...
gi 2462608768 385 MAFGSGKFQCPAR 397
Cdd:cd20612   313 IHFGHGPHQCLGE 325
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
264-390 7.70e-06

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: 47.66  E-value: 7.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKikvseDDLENLLLIKWCVLETIRLKAPGV-ITRKVVKPVEILNYIIPSG 342
Cdd:cd20642   256 WTMVLLSQHPDWQERAREEVLQVFGNNKPDF-----EGLNHLKVVTMILYEVLRLYPPVIqLTRAIHKDTKLGDLTLPAG 330
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462608768 343 DLLMLSPFWLHRNPKYFPE-PELFKPERWK----KANLEKHSFLdcfmAFGSG 390
Cdd:cd20642   331 VQVSLPILLVHRDPELWGDdAKEFNPERFAegisKATKGQVSYF----PFGWG 379
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
248-396 9.33e-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: 47.31  E-value: 9.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 248 LLLLWASLSNAVPVAFWTLAYvLSHPD-------IHKAIMEgissvfgkAGKDKIKVSEDDLEN------LLLIKwcvlE 314
Cdd:cd11066   234 LTMVSAGLDTVPLNLNHLIGH-LSHPPgqeiqekAYEEILE--------AYGNDEDAWEDCAAEekcpyvVALVK----E 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 315 TIR------LKAPgvitRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFmAFG 388
Cdd:cd11066   301 TLRyftvlpLGLP----RKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHF-SFG 375

                  ....*...
gi 2462608768 389 SGKFQCPA 396
Cdd:cd11066   376 AGSRMCAG 383
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
307-395 2.71e-05

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: 45.75  E-value: 2.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 307 LIKWCVLETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLekhsfldcfm 385
Cdd:cd20629   235 LIPAAIEEGLRWEPPvASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDRKPKPHL---------- 304
                          90
                  ....*....|
gi 2462608768 386 AFGSGKFQCP 395
Cdd:cd20629   305 VFGGGAHRCL 314
PLN02936 PLN02936
epsilon-ring hydroxylase
300-370 4.09e-05

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 45.55  E-value: 4.09e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462608768 300 DDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERW 370
Cdd:PLN02936  331 EDIKELKYLTRCINESMRLypHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERF 403
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
264-370 5.99e-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: 44.94  E-value: 5.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLaYVLS-HPDIHKAIMEGISSVFG---KAGKDKIKVSEDDLENLLLIKWCVLETIRLKAPGVITRKVVKPVeilNYII 339
Cdd:cd11051   207 WAF-YLLSkHPEVLAKVRAEHDEVFGpdpSAAAELLREGPELLNQLPYTTAVIKETLRLFPPAGTARRGPPGV---GLTD 282
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462608768 340 PSGDLLMLSPF--W-----LHRNPKYFPEPELFKPERW 370
Cdd:cd11051   283 RDGKEYPTDGCivYvchhaIHRDPEYWPRPDEFIPERW 320
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
261-397 8.48e-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: 44.37  E-value: 8.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 261 VAFWTLAYVLSHPDIHKAIMEGISSVFGKAgkdkikvsedDLENLlliKWCVLETIRL--KAPgVITRKVVKPVEILNYI 338
Cdd:cd20624   210 ALLRALALLAAHPEQAARAREEAAVPPGPL----------ARPYL---RACVLDAVRLwpTTP-AVLRESTEDTVWGGRT 275
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 339 IPSGD-LLMLSPFWlHRNPKYFPEPELFKPERWKKANLEKHSFLdcfMAFGSGKFQCPAR 397
Cdd:cd20624   276 VPAGTgFLIFAPFF-HRDDEALPFADRFVPEIWLDGRAQPDEGL---VPFSAGPARCPGE 331
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
327-381 1.02e-04

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: 44.06  E-value: 1.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462608768 327 KVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFL 381
Cdd:cd11067   285 RARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGDPFDFI 339
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
264-394 1.48e-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: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVfgkAGKDKIKvSEDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYIIPS 341
Cdd:cd20675   257 WILLLLVRYPDVQARLQEELDRV---VGRDRLP-CIEDQPNLPYVMAFLYEAMRFSSfvPVTIPHATTADTSILGYHIPK 332
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWkkanLEKHSFLD-----CFMAFGSGKFQC 394
Cdd:cd20675   333 DTVVFVNQWSVNHDPQKWPNPEVFDPTRF----LDENGFLNkdlasSVMIFSVGKRRC 386
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
202-394 1.55e-04

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: 43.76  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 202 FLELFEKNIPDIKACKSAKDNSMTLLQATLDIVETETSKENSP-NYGLLLLwaslsnavpvafwtlayvLSHPDIHKAIM 280
Cdd:cd20670   203 FIDCFLIKMHQDKNNPHTEFNLKNLVLTTLNLFFAGTETVSSTlRYGFLLL------------------MKYPEVEAKIH 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 281 EGISSVFGK----AGKDKIKVSEDDLenlllikwCVLETIRLK--APGVITRKVVKPVEILNYIIPSG-DLLMLSPFWLh 353
Cdd:cd20670   265 EEINQVIGPhrlpSVDDRVKMPYTDA--------VIHEIQRLTdiVPLGVPHNVIRDTQFRGYLLPKGtDVFPLLGSVL- 335
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462608768 354 RNPKYFPEPELFKPERW--KKANLEKHsflDCFMAFGSGKFQC 394
Cdd:cd20670   336 KDPKYFRYPEAFYPQHFldEQGRFKKN---EAFVPFSSGKRVC 375
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
264-394 2.20e-04

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: 43.04  E-value: 2.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKVSEDdleNLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYIIPS 341
Cdd:cd20615   237 WNLVFLAANPAVQEKLREEISAAREQSGYPMEDYILS---TDTLLAYCVLESLRLRplLAFSVPESSPTDKIIGGYRIPA 313
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462608768 342 GDLLMLSPFWL-HRNPKYFPEPELFKPERW---KKANLEKHsfldcFMAFGSGKFQC 394
Cdd:cd20615   314 NTPVVVDTYALnINNPFWGPDGEAYRPERFlgiSPTDLRYN-----FWRFGFGPRKC 365
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
264-394 4.78e-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: 42.11  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDkikvSEDDLENLLLIKWCVLETIRL--KAPGVITRKVVKPVEILNYIIPS 341
Cdd:cd20661   260 WAILFMALYPNIQGQVQKEIDLVVGPNGMP----SFEDKCKMPYTEAVLHEVLRFcnIVPLGIFHATSKDAVVRGYSIPK 335
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462608768 342 GDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN--LEKHsflDCFMAFGSGKFQC 394
Cdd:cd20661   336 GTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNgqFAKK---EAFVPFSLGRRHC 387
PLN02500 PLN02500
cytochrome P450 90B1
296-394 5.05e-04

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 42.16  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 296 KVSEDDLENLLLIKWCVLETIRL-KAPGVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKAN 374
Cdd:PLN02500  334 ELNWEDYKKMEFTQCVINETLRLgNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNN 413
                          90       100
                  ....*....|....*....|....*.
gi 2462608768 375 LEKHS------FLDCFMAFGSGKFQC 394
Cdd:PLN02500  414 NRGGSsgsssaTTNNFMPFGGGPRLC 439
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
265-394 5.26e-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: 42.09  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 265 TLAY----VLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLK--APGVITRKVVKPVEILNYI 338
Cdd:cd20668   245 TLRYgfllLMKHPEVEAKVHEEIDRVIGRNRQPKF----EDRAKMPYTEAVIHEIQRFGdvIPMGLARRVTKDTKFRDFF 320
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 339 IPSGDLL--MLSPfwLHRNPKYFPEPELFKPERW--KKANLEKHsflDCFMAFGSGKFQC 394
Cdd:cd20668   321 LPKGTEVfpMLGS--VLKDPKFFSNPKDFNPQHFldDKGQFKKS---DAFVPFSIGKRYC 375
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
264-394 5.69e-04

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: 41.92  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 264 WTLAYVLSHPDIHKAIMEGISSVFGKAGKDKIKvsedDLENLLLIKWCVLETIR------LKAPGVITRKVvkpveILN- 336
Cdd:cd20676   259 WSLMYLVTYPEIQKKIQEELDEVIGRERRPRLS----DRPQLPYLEAFILETFRhssfvpFTIPHCTTRDT-----SLNg 329
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 337 YIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDC--FMAFGSGKFQC 394
Cdd:cd20676   330 YYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEINKTESekVMLFGLGKRRC 389
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
314-395 1.03e-03

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 40.95  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 314 ETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLekhsfldcfmAFGSGKF 392
Cdd:cd11039   252 EGLRWISPiGMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFDVFRPKSPHV----------SFGAGPH 321

                  ...
gi 2462608768 393 QCP 395
Cdd:cd11039   322 FCA 324
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
303-397 1.43e-03

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: 40.42  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 303 ENLLLIKWCVLETIRLKAPGVITRKVVK-PVEILNYIIPSGDLLMLSpfWL--HRNPKYFPEPELFKPERWKKANLekhs 379
Cdd:cd11079   222 ANPALLPAAIDEILRLDDPFVANRRITTrDVELGGRTIPAGSRVTLN--WAsaNRDERVFGDPDEFDPDRHAADNL---- 295
                          90
                  ....*....|....*...
gi 2462608768 380 fldcfmAFGSGKFQCPAR 397
Cdd:cd11079   296 ------VYGRGIHVCPGA 307
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
325-395 2.16e-03

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: 39.72  E-value: 2.16e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462608768 325 TRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLekhsfldcfmAFGSGKFQCP 395
Cdd:cd20630   266 ARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRRDPNANI----------AFGYGPHFCI 326
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
272-394 2.97e-03

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: 39.41  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 272 HPDIHKAIMEGISS--VFGKAGKDKIKVSEDDLENLLLIKWCVLETIRLKAP---GVitRKVVKPVEILNYIIPSGDLLM 346
Cdd:cd20638   260 HPEVLQKVRKELQEkgLLSTKPNENKELSMEVLEQLKYTGCVIKETLRLSPPvpgGF--RVALKTFELNGYQIPKGWNVI 337
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2462608768 347 LSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDcFMAFGSGKFQC 394
Cdd:cd20638   338 YSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFS-FIPFGGGSRSC 384
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
250-394 3.74e-03

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: 39.43  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 250 LLWASLSNAVPVAFWTLAYVLSHPD-IHKAIMEGISSVFGKA-GKDKIKVSEDDLENLLLIKWCVLETIRLKAP---GVi 324
Cdd:cd20636   235 LIFAAFSTTASASTSLVLLLLQHPSaIEKIRQELVSHGLIDQcQCCPGALSLEKLSRLRYLDCVVKEVLRLLPPvsgGY- 313
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 325 tRKVVKPVEILNYIIPSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANLEKHSFLDCFMAFGSGKFQC 394
Cdd:cd20636   314 -RTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGRFNYIPFGGGVRSC 382
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
314-397 7.00e-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: 38.34  E-value: 7.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 314 ETIRLKAPGVITRKVVKPVEILNYIIPSGDLLMLsPFWLH-RNPKYFPEPELFKPERwkKANleKHsfldcfMAFGSGKF 392
Cdd:cd11035   240 ELLRRYPLVNVARIVTRDVEFHGVQLKAGDMVLL-PLALAnRDPREFPDPDTVDFDR--KPN--RH------LAFGAGPH 308

                  ....*....
gi 2462608768 393 QCP----AR 397
Cdd:cd11035   309 RCLgshlAR 317
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
196-394 8.00e-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: 38.20  E-value: 8.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 196 SKSKKWFLELFEKNIP-DIKAC---KSAKD--------NSMTLLQATLDIV--ETETSKeNSPNYGLLLLwaslsnavpv 261
Cdd:cd20669   185 AESVREHQESLDPNSPrDFIDCfltKMAEEkqdplshfNMETLVMTTHNLLfgGTETVS-TTLRYGFLIL---------- 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 262 afwtlayvLSHPDIHKAIMEGISSVFGKAGKDKIkvseDDLENLLLIKWCVLETIRLKA--PGVITRKVVKPVEILNYII 339
Cdd:cd20669   254 --------MKYPKVAARVQEEIDRVVGRNRLPTL----EDRARMPYTDAVIHEIQRFADiiPMSLPHAVTRDTNFRGFLI 321
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462608768 340 PSGDLLMLSPFWLHRNPKYFPEPELFKPERWKKANlekHSFL--DCFMAFGSGKFQC 394
Cdd:cd20669   322 PKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDN---GSFKknDAFMPFSAGKRIC 375
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
312-394 9.77e-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: 37.92  E-value: 9.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462608768 312 VLETIRLKAP-GVITRKVVKPVEILNYIIPSGDLLMLspfwL----HRNPKYFPEPELFKPERwkKANleKHsfldcfMA 386
Cdd:cd20625   249 VEELLRYDSPvQLTARVALEDVEIGGQTIPAGDRVLL----LlgaaNRDPAVFPDPDRFDITR--APN--RH------LA 314

                  ....*...
gi 2462608768 387 FGSGKFQC 394
Cdd:cd20625   315 FGAGIHFC 322
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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