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Conserved domains on  [gi|26343433|dbj|BAC35373|]
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unnamed protein product [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
65-457 0e+00

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


:

Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 789.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  65 YGPVVSFWFGRRLVVSLGTTDVLKQHFNPNKTSDPFETMLKSLLGYQSG-GGSAGEDHVRRKLYGDAVTASLHSNFPLLL 143
Cdd:cd20627   1 YGPVASFWFGRRLVVSLGSVDLLKQHINPNKTSDPFETMLKSLLGYQSGsGGDASESHVRKKLYENGVTKALQSNFPLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 144 QLSEELLDKWLSYPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEVIRFQKIHGTVWSEIGKGFLDGSLDKNTTRKKQ 223
Cdd:cd20627  81 KLSEELLDKWLSYPESQHVPLCQHMLGFAMKSVTQMVMGSTFEDDQEVIRFRKNHDAIWSEIGKGFLDGSLEKSTTRKKQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 224 YQEALMQLESTLKKIIKERKGGNFRQHTFIDSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLC 303
Cdd:cd20627 161 YEDALMEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLY 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 304 KEIDQVLGEGPITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHR 383
Cdd:cd20627 241 KEVDQVLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYR 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26343433 384 FDPDRFADEPVMKVFSSLGFSGTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVFEMKYELVTSAREEAWIT 457
Cdd:cd20627 321 FDPDRFDDESVMKSFSLLGFSGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETKYELVTSPREEAWIT 394
 
Name Accession Description Interval E-value
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
65-457 0e+00

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


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 789.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  65 YGPVVSFWFGRRLVVSLGTTDVLKQHFNPNKTSDPFETMLKSLLGYQSG-GGSAGEDHVRRKLYGDAVTASLHSNFPLLL 143
Cdd:cd20627   1 YGPVASFWFGRRLVVSLGSVDLLKQHINPNKTSDPFETMLKSLLGYQSGsGGDASESHVRKKLYENGVTKALQSNFPLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 144 QLSEELLDKWLSYPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEVIRFQKIHGTVWSEIGKGFLDGSLDKNTTRKKQ 223
Cdd:cd20627  81 KLSEELLDKWLSYPESQHVPLCQHMLGFAMKSVTQMVMGSTFEDDQEVIRFRKNHDAIWSEIGKGFLDGSLEKSTTRKKQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 224 YQEALMQLESTLKKIIKERKGGNFRQHTFIDSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLC 303
Cdd:cd20627 161 YEDALMEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLY 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 304 KEIDQVLGEGPITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHR 383
Cdd:cd20627 241 KEVDQVLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYR 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26343433 384 FDPDRFADEPVMKVFSSLGFSGTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVFEMKYELVTSAREEAWIT 457
Cdd:cd20627 321 FDPDRFDDESVMKSFSLLGFSGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETKYELVTSPREEAWIT 394
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
43-446 4.70e-36

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: 138.57  E-value: 4.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433    43 GNLPDIVNSGSLHEFLVNLHERYGPVVSFWFGRRLVVSLGTTD----VLKQHF-NPNKTSDPFetMLKSLLGYQSGGG-- 115
Cdd:pfam00067  11 GNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEavkeVLIKKGeEFSGRPDEP--WFATSRGPFLGKGiv 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   116 -SAGED-HVRRKLygdaVTASLHSN-----FPLLLQLSEELLDKWLSYPETQH-IPLSQHMLGFALKFVTRMVLGSTFE- 186
Cdd:pfam00067  89 fANGPRwRQLRRF----LTPTFTSFgklsfEPRVEEEARDLVEKLRKTAGEPGvIDITDLLFRAALNVICSILFGERFGs 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   187 -DEQEVIRFQKIHGTVWSEIGKGFLDGSLDKNTTR------KKQYQEALMQLESTLKKIIKERKG----GNFRQHTFIDS 255
Cdd:pfam00067 165 lEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKyfpgphGRKLKRARKKIKDLLDKLIEERREtldsAKKSPRDFLDA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   256 L-------TQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQ 327
Cdd:pfam00067 245 LllakeeeDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKrSPTYDDLQNMPYLD 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   328 QVLFETVRtakLTPVSARL------QDIegKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMKV--FS 399
Cdd:pfam00067 325 AVIKETLR---LHPVVPLLlprevtKDT--VIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRksFA 399
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 26343433   400 SLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVFEMKYEL 446
Cdd:pfam00067 400 FLPFGaGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDET 447
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
55-436 1.22e-17

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: 84.56  E-value: 1.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  55 HEFLVNLHErYGPVVSFWFGRR--LVVS--------LGTTDVLKQHFNPNKTSDPFETMLKSLLGyqsgggSAGEDHVR- 123
Cdd:COG2124  22 YPFYARLRE-YGPVFRVRLPGGgaWLVTryedvrevLRDPRTFSSDGGLPEVLRPLPLLGDSLLT------LDGPEHTRl 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 124 RKLYGDAVT----ASLHsnfPLLLQLSEELLDKWlsyPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEVIRfqkihg 199
Cdd:COG2124  95 RRLVQPAFTprrvAALR---PRIREIADELLDRL---AARGPVDLVEEFARPLPVIVICELLGVPEEDRDRLRR------ 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 200 tvWSEIgkgFLDGSLDKNTTRKKQYQEALMQLESTLKKIIKERkggnfRQH---TFIDSLTQ-----GKLNEQQILEDCV 271
Cdd:COG2124 163 --WSDA---LLDALGPLPPERRRRARRARAELDAYLRELIAER-----RAEpgdDLLSALLAarddgERLSDEELRDELL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 272 VFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEidqvlgegpitsekieqLSYCQQVLFETVRTAKLTPVSAR--LQDI 349
Cdd:COG2124 233 LLLLAGHETTANALAWALYALLRHPEQLARLRAE-----------------PELLPAAVEETLRLYPPVPLLPRtaTEDV 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 350 EgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRfadepvmKVFSSLGFS-GTWECPELRFAYMVTAVLVSVLLK 428
Cdd:COG2124 296 E--LGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-------PPNAHLPFGgGPHRCLGAALARLEARIALATLLR 366

                ....*...
gi 26343433 429 RLRLLAVD 436
Cdd:COG2124 367 RFPDLRLA 374
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
13-430 3.16e-14

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 74.73  E-value: 3.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   13 LALVGAVLYLYPASRQASGIPGLTPTEEKDGNLPDIVNSGSLHeFLVNLHERYGPVVSFWFGRRLVVSLGTTDVLKQHFN 92
Cdd:PLN03234  10 LVAAAAFFFLRSTTKKSLRLPPGPKGLPIIGNLHQMEKFNPQH-FLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   93 P---NKTSDPF----ETMlkSLLGYQSGGG--SAGEDHVRRKLYGDAVTASLHSNF-PLLLQLSEELLDK-WLSYPETQH 161
Cdd:PLN03234  89 TqdlNFTARPLlkgqQTM--SYQGRELGFGqyTAYYREMRKMCMVNLFSPNRVASFrPVREEECQRMMDKiYKAADQSGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  162 IPLSQHMLGFALKFVTRMVLGSTF-EDEQEVIRFQKIHGTVWSEIGKGFLD------GSLDKNTTRKKQYQEALMQLEST 234
Cdd:PLN03234 167 VDLSELLLSFTNCVVCRQAFGKRYnEYGTEMKRFIDILYETQALLGTLFFSdlfpyfGFLDNLTGLSARLKKAFKELDTY 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  235 LKKIIKERKGGNF-RQHT--FIDSLTQ-----------GKLNEQQILEDCVVFSLASciiTARLCTWTIHFLTTTGEVQK 300
Cdd:PLN03234 247 LQELLDETLDPNRpKQETesFIDLLMQiykdqpfsikfTHENVKAMILDIVVPGTDT---AAAVVVWAMTYLIKYPEAMK 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  301 KLCKEIDQVLGE-GPITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDI-EGKVGPFVIPKETLVLYALGVVLQDPSTW 378
Cdd:PLN03234 324 KAQDEVRNVIGDkGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIaDAKIGGYDIPAKTIIQVNAWAVSRDTAAW 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26343433  379 -PLPHRFDPDRFADEPVMKVFSSLGF------SGTWECPELRFAYMVTAVLVSVLLKRL 430
Cdd:PLN03234 404 gDNPNEFIPERFMKEHKGVDFKGQDFellpfgSGRRMCPAMHLGIAMVEIPFANLLYKF 462
 
Name Accession Description Interval E-value
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
65-457 0e+00

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


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 789.40  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  65 YGPVVSFWFGRRLVVSLGTTDVLKQHFNPNKTSDPFETMLKSLLGYQSG-GGSAGEDHVRRKLYGDAVTASLHSNFPLLL 143
Cdd:cd20627   1 YGPVASFWFGRRLVVSLGSVDLLKQHINPNKTSDPFETMLKSLLGYQSGsGGDASESHVRKKLYENGVTKALQSNFPLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 144 QLSEELLDKWLSYPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEVIRFQKIHGTVWSEIGKGFLDGSLDKNTTRKKQ 223
Cdd:cd20627  81 KLSEELLDKWLSYPESQHVPLCQHMLGFAMKSVTQMVMGSTFEDDQEVIRFRKNHDAIWSEIGKGFLDGSLEKSTTRKKQ 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 224 YQEALMQLESTLKKIIKERKGGNFRQHTFIDSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLC 303
Cdd:cd20627 161 YEDALMEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLY 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 304 KEIDQVLGEGPITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHR 383
Cdd:cd20627 241 KEVDQVLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYR 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26343433 384 FDPDRFADEPVMKVFSSLGFSGTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVFEMKYELVTSAREEAWIT 457
Cdd:cd20627 321 FDPDRFDDESVMKSFSLLGFSGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETKYELVTSPREEAWIT 394
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
66-448 5.82e-50

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: 174.62  E-value: 5.82e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  66 GPVVSFWFGRRLVVSLGTTDVLKQHFNPNKTSDPFETMLKSLLGYQSGGG---SAGEDH-VRRKLYGDAVT-ASLHSNFP 140
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGlltLDGPEHrRLRRLLAPAFTpRALAALRP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 141 LLLQLSEELLDKWLSYPETQhIPLSQHMLGFALKFVTRMVLGSTFEDEQEviRFQKIHGTVWSEIGKGFLdgsLDKNTTR 220
Cdd:cd00302  81 VIREIARELLDRLAAGGEVG-DDVADLAQPLALDVIARLLGGPDLGEDLE--ELAELLEALLKLLGPRLL---RPLPSPR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 221 KKQYQEALMQLESTLKKIIKERK---GGNFRQHTFIDSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGE 297
Cdd:cd00302 155 LRRLRRARARLRDYLEELIARRRaepADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLARHPE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 298 VQKKLCKEIDQVLGEGpiTSEKIEQLSYCQQVLFETVRtakLTPVSARL-----QDIEgkVGPFVIPKETLVLYALGVVL 372
Cdd:cd00302 235 VQERLRAEIDAVLGDG--TPEDLSKLPYLEAVVEETLR---LYPPVPLLprvatEDVE--LGGYTIPAGTLVLLSLYAAH 307
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26343433 373 QDPSTWPLPHRFDPDRFADEPVMKVFSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVFEMKYELVT 448
Cdd:cd00302 308 RDPEVFPDPDEFDPERFLPEREEPRYAHLPFGaGPHRCLGARLARLELKLALATLLRRFDFELVPDEELEWRPSLGT 384
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
43-446 4.70e-36

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: 138.57  E-value: 4.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433    43 GNLPDIVNSGSLHEFLVNLHERYGPVVSFWFGRRLVVSLGTTD----VLKQHF-NPNKTSDPFetMLKSLLGYQSGGG-- 115
Cdd:pfam00067  11 GNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEavkeVLIKKGeEFSGRPDEP--WFATSRGPFLGKGiv 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   116 -SAGED-HVRRKLygdaVTASLHSN-----FPLLLQLSEELLDKWLSYPETQH-IPLSQHMLGFALKFVTRMVLGSTFE- 186
Cdd:pfam00067  89 fANGPRwRQLRRF----LTPTFTSFgklsfEPRVEEEARDLVEKLRKTAGEPGvIDITDLLFRAALNVICSILFGERFGs 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   187 -DEQEVIRFQKIHGTVWSEIGKGFLDGSLDKNTTR------KKQYQEALMQLESTLKKIIKERKG----GNFRQHTFIDS 255
Cdd:pfam00067 165 lEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKyfpgphGRKLKRARKKIKDLLDKLIEERREtldsAKKSPRDFLDA 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   256 L-------TQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQ 327
Cdd:pfam00067 245 LllakeeeDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKrSPTYDDLQNMPYLD 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   328 QVLFETVRtakLTPVSARL------QDIegKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMKV--FS 399
Cdd:pfam00067 325 AVIKETLR---LHPVVPLLlprevtKDT--VIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRksFA 399
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 26343433   400 SLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVFEMKYEL 446
Cdd:pfam00067 400 FLPFGaGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDET 447
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
66-462 4.62e-34

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: 131.93  E-value: 4.62e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  66 GPVVSFWFGRRLVVSLGTTD----VLKQHfNPNKTSDPFETMLKSLLGyqsGGG--SAGEDHVR-RKL------------ 126
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHPDhiqhVLVTN-ARNYVKGGVYERLKLLLG---NGLltSEGDLWRRqRRLaqpafhrrriaa 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 127 YGDAVTASLHsnfplllqlseELLDKWLSYPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEVIR--FQKIHGTVWSE 204
Cdd:cd20620  77 YADAMVEATA-----------ALLDRWEAGARRGPVDVHAEMMRLTLRIVAKTLFGTDVEGEADEIGdaLDVALEYAARR 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 205 IGKGFLdGSLDKNTTRKKQYQEALMQLESTLKKIIKERKGGNFRQHTFIDSL-------TQGKLNEQQILEDCVVFSLAS 277
Cdd:cd20620 146 MLSPFL-LPLWLPTPANRRFRRARRRLDEVIYRLIAERRAAPADGGDLLSMLlaardeeTGEPMSDQQLRDEVMTLFLAG 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 278 CIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEKIEQLSYCQQVLFETVRtakLTP---VSAR--LQDIEgk 352
Cdd:cd20620 225 HETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRPPTAEDLPQLPYTEMVLQESLR---LYPpawIIGReaVEDDE-- 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 353 VGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMKV--FSSLGFS-GTWECPELRFAYMVTAVLVSVLLKR 429
Cdd:cd20620 300 IGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARprYAYFPFGgGPRICIGNHFAMMEAVLLLATIAQR 379
                       410       420       430
                ....*....|....*....|....*....|...
gi 26343433 430 LRLLAVDRQVFEMkyelvtsareEAWITVSKRH 462
Cdd:cd20620 380 FRLRLVPGQPVEP----------EPLITLRPKN 402
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
224-451 1.41e-26

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: 111.14  E-value: 1.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 224 YQEALMQLESTLKKIIKERKGGNFRQHT-----FIDSLTQG------KLNEQQILEDCVVFSLASCIITARLCTWTIHFL 292
Cdd:cd11055 174 GFKSFSFLEDVVKKIIEQRRKNKSSRRKdllqlMLDAQDSDedvskkKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLL 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 293 TTTGEVQKKLCKEIDQVLGE-GPITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQDIEgkVGPFVIPKETLVL---Y 366
Cdd:cd11055 254 ATNPDVQEKLIEEIDEVLPDdGSPTYDTVSKLKYLDMVINETLRLYPPAFFISRecKEDCT--INGVFIPKGVDVVipvY 331
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 367 ALGvvlQDPSTWPLPHRFDPDRFADE------PvmkvFSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQV 439
Cdd:cd11055 332 AIH---HDPEFWPDPEKFDPERFSPEnkakrhP----YAYLPFGaGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETE 404
                       250
                ....*....|..
gi 26343433 440 FEMKYELVTSAR 451
Cdd:cd11055 405 IPLKLVGGATLS 416
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
56-443 9.75e-26

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: 108.52  E-value: 9.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  56 EFLVNLHERYGPVVS-FWFGRRLVVSLGTTDV----------LKQHFNPNktsdpfetmLKSLLGYQSGGGSAGEDH-VR 123
Cdd:cd11044  12 DFIQSRYQKYGPVFKtHLLGRPTVFVIGAEAVrfilsgegklVRYGWPRS---------VRRLLGENSLSLQDGEEHrRR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 124 RKLYGDAV-TASLHSNFPLLLQLSEELLDKWLSYPEtqhIPLSQHMLGFALKFVTRMVLGSTFEDEQEVIrfqkihgtvw 202
Cdd:cd11044  83 RKLLAPAFsREALESYVPTIQAIVQSYLRKWLKAGE---VALYPELRRLTFDVAARLLLGLDPEVEAEAL---------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 203 SEIGKGFLDGS------LDKNTTRKKQyqEALMQLESTLKKIIKERKGGNfrQHTFIDSLT--------QG-KLNEQQIL 267
Cdd:cd11044 150 SQDFETWTDGLfslpvpLPFTPFGRAI--RARNKLLARLEQAIRERQEEE--NAEAKDALGllleakdeDGePLSMDELK 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 268 EDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEKIEQLSYCQQVLFETVRTakLTPVSA--R 345
Cdd:cd11044 226 DQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEPLTLESLKKMPYLDQVIKEVLRL--VPPVGGgfR 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 346 --LQDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFAD---EPVMKVFSSLGFS-GTWECPELRFAYMVT 419
Cdd:cd11044 304 kvLEDFE--LGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSParsEDKKKPFSLIPFGgGPRECLGKEFAQLEM 381
                       410       420
                ....*....|....*....|....
gi 26343433 420 AVLVSVLLKRLRLLAVDRQVFEMK 443
Cdd:cd11044 382 KILASELLRNYDWELLPNQDLEPV 405
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
66-417 8.83e-24

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: 103.06  E-value: 8.83e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  66 GPVVSFWFGRRLVVSLGTTDVLKQHF--NPNKTSDPFET-MLKSLLGYQSGGGSAGEDHVR-RKLYGDAVTASLHSNfpL 141
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEIIKEAFvkNGDNFSDRPLLpSFEIISGGKGILFSNGDYWKElRRFALSSLTKTKLKK--K 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 142 LLQLSEELLDKWLSYPET-----QHIPLSQHMLGFALKFVTRMVLGSTFEDEQEViRFQKIHGT---VWSEIGKG----F 209
Cdd:cd20617  79 MEELIEEEVNKLIESLKKhsksgEPFDPRPYFKKFVLNIINQFLFGKRFPDEDDG-EFLKLVKPieeIFKELGSGnpsdF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 210 LDGSLDKNTTRKKQYQEALMQLESTLKKIIKERK----GGNFRQHTFIDSLTQGKLNE-QQILEDCVVFSLASCII---- 280
Cdd:cd20617 158 IPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLktidPNNPRDLIDDELLLLLKEGDsGLFDDDSIISTCLDLFLagtd 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 281 -TARLCTWTIHFLTTTGEVQKKLCKEIDQVLG-EGPITSEKIEQLSYCQQVLFETVRTAKLTPVS---ARLQDIEgkVGP 355
Cdd:cd20617 238 tTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGnDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGlprVTTEDTE--IGG 315
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26343433 356 FVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADE---PVMKVFssLGFS-GTWECPELRFAYM 417
Cdd:cd20617 316 YFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENdgnKLSEQF--IPFGiGKRNCVGENLARD 379
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
66-456 1.41e-23

cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the omega-hydroxylation of the terminal carbon of fatty acids, including essential signaling molecules such as eicosanoids, prostaglandins and leukotrienes, and they are important for chemical defense. There are seven vertebrate family 4 subfamilies: CYP4A, CYP4B, CYP4F, CYP4T, CYP4V, CYP4X, and CYP4Z; three (CYP4X, CYP4A, CYP4Z) are specific to mammals. CYP4 enzymes metabolize fatty acids off various length, level of saturation, and branching. Specific subfamilies show preferences for the length of fatty acids; CYP4B, CYP4A and CYP4V, and CYP4F preferentially metabolize short (C7-C10), medium (C10-C16), and long to very long (C18-C26) fatty acid chains, respectively. CYP4 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410721 [Multi-domain]  Cd Length: 426  Bit Score: 102.60  E-value: 1.41e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  66 GPVVSFWFGRRLVVSLGTTD----VLKQHFNPNKTSDpfETMLKSLLGyqsgGG---SAGED-HVRRKLygdaVTASLHS 137
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPEdievILSSSKLITKSFL--YDFLKPWLG----DGlltSTGEKwRKRRKL----LTPAFHF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 138 N-----FPLLLQLSEELLDKWLSYPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQE--------VIRFQKIHGT---- 200
Cdd:cd20628  71 KilesfVEVFNENSKILVEKLKKKAGGGEFDIFPYISLCTLDIICETAMGVKLNAQSNedseyvkaVKRILEIILKrifs 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 201 --VWSEIgkgfldgsLDKNTTRKKQYQEALMQLESTLKKIIKERK---------------GGNFRQHTFIDSL-----TQ 258
Cdd:cd20628 151 pwLRFDF--------IFRLTSLGKEQRKALKVLHDFTNKVIKERReelkaekrnseeddeFGKKKRKAFLDLLleaheDG 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 259 GKLNEQQILEDCVVF------SLASCIitarlcTWTIHFLTTTGEVQKKLCKEIDQVLGE--GPITSEKIEQLSYCQQVL 330
Cdd:cd20628 223 GPLTDEDIREEVDTFmfaghdTTASAI------SFTLYLLGLHPEVQEKVYEELDEIFGDddRRPTLEDLNKMKYLERVI 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 331 FETVRtakL-TPVS--ARLQDIEGKVGPFVIPKET---LVLYALGvvlQDPSTWPLPHRFDPDRFADEPVMKV--FSSLG 402
Cdd:cd20628 297 KETLR---LyPSVPfiGRRLTEDIKLDGYTIPKGTtvvISIYALH---RNPEYFPDPEKFDPDRFLPENSAKRhpYAYIP 370
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 26343433 403 FS-GTWECPELRFAYMVTAVLVSVLLKRLRLLAVD-RQVFEMKYELVTSAREEAWI 456
Cdd:cd20628 371 FSaGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVPpGEDLKLIAEIVLRSKNGIRV 426
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
233-445 4.67e-23

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: 101.08  E-value: 4.67e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 233 STLKKIIKERKGGNFRQHTFIDSLTQGKLNEQQILED-------------CVVFSLASCIITARLCTWTIHFLTTTGEVQ 299
Cdd:cd11056 184 KLVRDTIEYREKNNIVRNDFIDLLLELKKKGKIEDDKsekeltdeelaaqAFVFFLAGFETSSSTLSFALYELAKNPEIQ 263
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 300 KKLCKEIDQVL--GEGPITSEKIEQLSYCQQVLFETVRtakLTPVSARL-----QDIEGKVGPFVIPKETLVL---YALG 369
Cdd:cd11056 264 EKLREEIDEVLekHGGELTYEALQEMKYLDQVVNETLR---KYPPLPFLdrvctKDYTLPGTDVVIEKGTPVIipvYALH 340
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26343433 370 vvlQDPSTWPLPHRFDPDRFADEPVMKV--FSSLGF-SGTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVFEMKYE 445
Cdd:cd11056 341 ---HDPKYYPEPEKFDPERFSPENKKKRhpYTYLPFgDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPLKLS 416
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
218-437 1.95e-22

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: 99.26  E-value: 1.95e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 218 TTRKKQYQEALMQLESTLKKIIKERK-------------------GGNFRQhTFID-----SLTQGKLNEQQILEDCVVF 273
Cdd:cd20660 162 TPDGREHKKCLKILHGFTNKVIQERKaelqksleeeeeddedadiGKRKRL-AFLDllleaSEEGTKLSDEDIREEVDTF 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 274 SLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLG--EGPITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEG 351
Cdd:cd20660 241 MFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGdsDRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDI 320
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 352 KVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMK--VFSSLGFS-GTWECPELRFAYMVTAVLVSVLLK 428
Cdd:cd20660 321 EIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGrhPYAYIPFSaGPRNCIGQKFALMEEKVVLSSILR 400

                ....*....
gi 26343433 429 RLRLLAVDR 437
Cdd:cd20660 401 NFRIESVQK 409
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
63-431 6.17e-22

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: 97.25  E-value: 6.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  63 ERYGPVvsF---WFGRRLVVSLGTtDVLKQHF-NPNK--TSDPFETMLKsLLGYQSGGGSAGEDH--VRRKLYGDAVTAS 134
Cdd:cd11043   3 KRYGPV--FktsLFGRPTVVSADP-EANRFILqNEGKlfVSWYPKSVRK-LLGKSSLLTVSGEEHkrLRGLLLSFLGPEA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 135 LHSNF-PLLLQLSEELLDKWLSYPETQHIPLSQHMlgfALKFVTRMVLGSTFEDEQEVIRfqkihgTVWSEIGKGFLDGS 213
Cdd:cd11043  79 LKDRLlGDIDELVRQHLDSWWRGKSVVVLELAKKM---TFELICKLLLGIDPEEVVEELR------KEFQAFLEGLLSFP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 214 LDKNTTRkkqYQEALM---QLESTLKKIIKERK--GGNFRQHT-FIDSL------TQGKLNEQQILEDCVVFSLASCIIT 281
Cdd:cd11043 150 LNLPGTT---FHRALKarkRIRKELKKIIEERRaeLEKASPKGdLLDVLleekdeDGDSLTDEEILDNILTLLFAGHETT 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 282 ARLCTWTIHFLTTTGEVQKKLCKEIDQVL----GEGPITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQDIEgkVGP 355
Cdd:cd11043 227 STTLTLAVKFLAENPKVLQELLEEHEEIAkrkeEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRkaLQDVE--YKG 304
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26343433 356 FVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMKVFSSLGF-SGTWECPELRFAYMVTAVLVSVLLKRLR 431
Cdd:cd11043 305 YTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGVPYTFLPFgGGPRLCPGAELAKLEILVFLHHLVTRFR 381
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
65-432 1.27e-21

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: 96.64  E-value: 1.27e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  65 YGPVVSFWFGR--RLVVSlgTTDVLKQ---HFNPNKTSDPFETMLKSLLGyqSGGGSA-GEDHVR-RKLYGDAVTA-SLH 136
Cdd:cd11052  11 YGKNFLYWYGTdpRLYVT--EPELIKEllsKKEGYFGKSPLQPGLKKLLG--RGLVMSnGEKWAKhRRIANPAFHGeKLK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 137 SNFPLLLQLSEELLDKWLSYPETQ--HIPLSQHMLGFALKFVTRMVLGSTFEDEQEVIRFQK-IHGTVWSEIGKGFLDGS 213
Cdd:cd11052  87 GMVPAMVESVSDMLERWKKQMGEEgeEVDVFEEFKALTADIISRTAFGSSYEEGKEVFKLLReLQKICAQANRDVGIPGS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 214 LDKNTTRKKQYQEALMQLESTLKKIIKERK-------GGNFrQHTF--------IDSLTQGKLNEQQILEDCVVFSLASC 278
Cdd:cd11052 167 RFLPTKGNKKIKKLDKEIEDSLLEIIKKREdslkmgrGDDY-GDDLlgllleanQSDDQNKNMTVQEIVDECKTFFFAGH 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 279 IITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEKIEQLSYCQQVLFETVRtakLTPVSARLQ-----DIegKV 353
Cdd:cd11052 246 ETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPSDSLSKLKTVSMVINESLR---LYPPAVFLTrkakeDI--KL 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 354 GPFVIPKETLVLYALGVVLQDPSTWPL-PHRFDPDRFADEPVMKVFSSLGF----SGTWECPELRFAYMVTAVLVSVLLK 428
Cdd:cd11052 321 GGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGVAKAAKHPMAFlpfgLGPRNCIGQNFATMEAKIVLAMILQ 400

                ....
gi 26343433 429 RLRL 432
Cdd:cd11052 401 RFSF 404
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
226-432 1.48e-21

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: 96.52  E-value: 1.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 226 EALMQLESTLKKIIKERKGGNFRQ-----HTFIDS-LTQG-KLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEV 298
Cdd:cd11042 166 RARAKLKEIFSEIIQKRRKSPDKDeddmlQTLMDAkYKDGrPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEH 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 299 QKKLCKEIDQVLG--EGPITSEKIEQLSYCQQVLFETVRtakLTPVSARL-----QDIEGKVGPFVIPKETLVLYALGVV 371
Cdd:cd11042 246 LEALREEQKEVLGdgDDPLTYDVLKEMPLLHACIKETLR---LHPPIHSLmrkarKPFEVEGGGYVIPKGHIVLASPAVS 322
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26343433 372 LQDPSTWPLPHRFDPDRFADE-PVMKV---FSSLGF-SGTWECPELRFAYMVTAVLVSVLLKRLRL 432
Cdd:cd11042 323 HRDPEIFKNPDEFDPERFLKGrAEDSKggkFAYLPFgAGRHRCIGENFAYLQIKTILSTLLRNFDF 388
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
56-439 1.45e-20

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: 93.42  E-value: 1.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  56 EFLVNLHERYGPVVSFWF-GRRLVVSLGTTDVLKQHF-NPNKTSD--PFETMLKSLLGYQSGGGSAGEDH-VRRKL---- 126
Cdd:cd11053   2 GFLERLRARYGDVFTLRVpGLGPVVVLSDPEAIKQIFtADPDVLHpgEGNSLLEPLLGPNSLLLLDGDRHrRRRKLlmpa 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 127 --------YGDAVTASLHSNFplllqlseellDKWlsyPETQHIPLSQHMLGFALKFVTRMVLGSTFEDE-----QEVIR 193
Cdd:cd11053  82 fhgerlraYGELIAEITEREI-----------DRW---PPGQPFDLRELMQEITLEVILRVVFGVDDGERlqelrRLLPR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 194 FQKIHGTVWSEIGKGFLD-GSLdkntTRKKQYQEALMQLESTLKKIIKERKGGNFRQHTFIDSLT------QG-KLNEQQ 265
Cdd:cd11053 148 LLDLLSSPLASFPALQRDlGPW----SPWGRFLRARRRIDALIYAEIAERRAEPDAERDDILSLLlsardeDGqPLSDEE 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 266 ILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPitSEKIEQLSYCQQVLFETVRTAKLTPVSAR 345
Cdd:cd11053 224 LRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPD--PEDIAKLPYLDAVIKETLRLYPVAPLVPR 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 346 L--QDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPvmkvFSS---LGFS-GTWECPELRFAYMVT 419
Cdd:cd11053 302 RvkEPVE--LGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRK----PSPyeyLPFGgGVRRCIGAAFALLEM 375
                       410       420
                ....*....|....*....|
gi 26343433 420 AVLVSVLLKRLRLLAVDRQV 439
Cdd:cd11053 376 KVVLATLLRRFRLELTDPRP 395
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
155-432 2.27e-20

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: 93.05  E-value: 2.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 155 SYPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEVI-RFQKIHGTVWSEIGKGFLDGSL-----DKNTTRKKQYQEAL 228
Cdd:cd11057  91 TYVGGGEFDILPDLSRCTLEMICQTTLGSDVNDESDGNeEYLESYERLFELIAKRVLNPWLhpefiYRLTGDYKEEQKAR 170
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 229 MQLESTLKKIIKERKG---------------GNFRQHTFIDSLTQGKLNE-----QQILEDCVVFSLASCIITARLCTWT 288
Cdd:cd11057 171 KILRAFSEKIIEKKLQevelesnldseedeeNGRKPQIFIDQLLELARNGeeftdEEIMDEIDTMIFAGNDTSATTVAYT 250
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 289 IHFLTTTGEVQKKLCKEIDQVLGEG--PITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQDIEGKVGpFVIPKETLV 364
Cdd:cd11057 251 LLLLAMHPEVQEKVYEEIMEVFPDDgqFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRetTADIQLSNG-VVIPKGTTI 329
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26343433 365 LYALGVVLQDPSTW-PLPHRFDPDRFADEPVMK--VFSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRL 432
Cdd:cd11057 330 VIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQrhPYAFIPFSaGPRNCIGWRYAMISMKIMLAKILRNYRL 401
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
220-443 2.62e-20

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: 92.81  E-value: 2.62e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 220 RKKQYQEALMQLESTLKKIIKERKggNFRQHTFIDSLTQGKLNE-------------------QQILEDCVVFSLASCII 280
Cdd:cd11046 178 RQRKFLRDLKLLNDTLDDLIRKRK--EMRQEEDIELQQEDYLNEddpsllrflvdmrdedvdsKQLRDDLMTMLIAGHET 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 281 TARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQDIEGKVGPFV 357
Cdd:cd11046 256 TAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRlPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRraVEDDKLPGGGVK 335
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 358 IPKETLVLYALGVVLQDPSTWPLPHRFDPDRFAD---EPVMKVFSSLGF----SGTWECPELRFAYMVTAVLVSVLLKRL 430
Cdd:cd11046 336 VPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDpfiNPPNEVIDDFAFlpfgGGPRKCLGDQFALLEATVALAMLLRRF 415
                       250
                ....*....|....
gi 26343433 431 RL-LAVDRQVFEMK 443
Cdd:cd11046 416 DFeLDVGPRHVGMT 429
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
222-432 2.21e-19

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: 89.96  E-value: 2.21e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 222 KQYQEALMQLESTLKKIIKERK----GGNFRQhtFIDSLTQGKLNEQQ--------ILEDCVVFSLASCII-----TARL 284
Cdd:cd11027 171 RELKELMKERDEILRKKLEEHKetfdPGNIRD--LTDALIKAKKEAEDegdedsglLTDDHLVMTISDIFGagtetTATT 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 285 CTWTIHFLTTTGEVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQQVLFETVRTAKLTPVS---ARLQDIEgkVGPFVIPK 360
Cdd:cd11027 249 LRWAIAYLVNYPEVQAKLHAELDDVIGRDrLPTLSDRKRLPYLEATIAEVLRLSSVVPLAlphKTTCDTT--LRGYTIPK 326
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26343433 361 ETLVLYALGVVLQDPSTWPLPHRFDPDRFADE---PVMKVFSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRL 432
Cdd:cd11027 327 GTTVLVNLWALHHDPKEWDDPDEFRPERFLDEngkLVPKPESFLPFSaGRRVCLGESLAKAELFLFLARLLQKFRF 402
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
220-392 1.54e-18

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: 87.63  E-value: 1.54e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 220 RKKQYQEALMQLESTLKKIIKERKGGNFRQH--------TFIDSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHF 291
Cdd:cd11068 177 AKRQFREDIALMRDLVDEIIAERRANPDGSPddllnlmlNGKDPETGEKLSDENIRYQMITFLIAGHETTSGLLSFALYY 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 292 LTTTGEVQKKLCKEIDQVLGEGPITSEKIEQLSYCQQVLFETVR---TAKLTPVSARLQDIEGkvGPFVIPKETLVLYAL 368
Cdd:cd11068 257 LLKNPEVLAKARAEVDEVLGDDPPPYEQVAKLRYIRRVLDETLRlwpTAPAFARKPKEDTVLG--GKYPLKKGDPVLVLL 334
                       170       180
                ....*....|....*....|....*
gi 26343433 369 GVVLQDPSTW-PLPHRFDPDRFADE 392
Cdd:cd11068 335 PALHRDPSVWgEDAEEFRPERFLPE 359
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
160-439 1.62e-18

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: 87.31  E-value: 1.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 160 QHIPLSQHMLGFALKFVTRMVLGSTFEDE-QEVIRfQKIHGTVWSEIGKGFLDGSLDKNTTR-KKQYQEALMQLESTLKK 237
Cdd:cd11049 108 RVVDVDAEMHRLTLRVVARTLFSTDLGPEaAAELR-QALPVVLAGMLRRAVPPKFLERLPTPgNRRFDRALARLRELVDE 186
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 238 IIKERKGGNFRQHTFIDSLTQ------GKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLG 311
Cdd:cd11049 187 IIAEYRASGTDRDDLLSLLLAardeegRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG 266
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 312 EGPITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFAD 391
Cdd:cd11049 267 GRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLP 346
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 26343433 392 EPVMKV--FSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRL-LAVDRQV 439
Cdd:cd11049 347 GRAAAVprGAFIPFGaGARKCIGDTFALTELTLALATIASRWRLrPVPGRPV 398
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
164-426 2.34e-18

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: 86.84  E-value: 2.34e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 164 LSQHMLGFALKFVTRMVLGSTF-----EDEQEVIRFQK-IHGTVWSeIGKG-------FLDGsLDKNTTRKKQyQEALMQ 230
Cdd:cd20618 108 LREHLSDLTLNNITRMLFGKRYfgeseKESEEAREFKElIDEAFEL-AGAFnigdyipWLRW-LDLQGYEKRM-KKLHAK 184
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 231 LESTLKKIIKERK-----GGNFRQHTFIDSLTQGKLNEQQILEDCVVfSLASCII------TARLCTWTIHFLTTTGEVQ 299
Cdd:cd20618 185 LDRFLQKIIEEHRekrgeSKKGGDDDDDLLLLLDLDGEGKLSDDNIK-ALLLDMLaagtdtSAVTIEWAMAELLRHPEVM 263
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 300 KKLCKEIDQVLGEGPITSEK-IEQLSYCQQVLFETVRtakLTPVSARL------QDIegKVGPFVIPKETLVL---YALG 369
Cdd:cd20618 264 RKAQEELDSVVGRERLVEESdLPKLPYLQAVVKETLR---LHPPGPLLlphestEDC--KVAGYDIPAGTRVLvnvWAIG 338
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26343433 370 vvlQDPSTWPLPHRFDPDRFADEPVMKV----FSSLGF-SGTWECPELRFAY-MVTAVLVSVL 426
Cdd:cd20618 339 ---RDPKVWEDPLEFKPERFLESDIDDVkgqdFELLPFgSGRRMCPGMPLGLrMVQLTLANLL 398
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
55-436 1.22e-17

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: 84.56  E-value: 1.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  55 HEFLVNLHErYGPVVSFWFGRR--LVVS--------LGTTDVLKQHFNPNKTSDPFETMLKSLLGyqsgggSAGEDHVR- 123
Cdd:COG2124  22 YPFYARLRE-YGPVFRVRLPGGgaWLVTryedvrevLRDPRTFSSDGGLPEVLRPLPLLGDSLLT------LDGPEHTRl 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 124 RKLYGDAVT----ASLHsnfPLLLQLSEELLDKWlsyPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEVIRfqkihg 199
Cdd:COG2124  95 RRLVQPAFTprrvAALR---PRIREIADELLDRL---AARGPVDLVEEFARPLPVIVICELLGVPEEDRDRLRR------ 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 200 tvWSEIgkgFLDGSLDKNTTRKKQYQEALMQLESTLKKIIKERkggnfRQH---TFIDSLTQ-----GKLNEQQILEDCV 271
Cdd:COG2124 163 --WSDA---LLDALGPLPPERRRRARRARAELDAYLRELIAER-----RAEpgdDLLSALLAarddgERLSDEELRDELL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 272 VFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEidqvlgegpitsekieqLSYCQQVLFETVRTAKLTPVSAR--LQDI 349
Cdd:COG2124 233 LLLLAGHETTANALAWALYALLRHPEQLARLRAE-----------------PELLPAAVEETLRLYPPVPLLPRtaTEDV 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 350 EgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRfadepvmKVFSSLGFS-GTWECPELRFAYMVTAVLVSVLLK 428
Cdd:COG2124 296 E--LGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-------PPNAHLPFGgGPHRCLGAALARLEARIALATLLR 366

                ....*...
gi 26343433 429 RLRLLAVD 436
Cdd:COG2124 367 RFPDLRLA 374
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
261-428 3.46e-17

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: 83.23  E-value: 3.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 261 LNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVL-GEGPITSEKIEQLSYCQQVLFETVRtakL 339
Cdd:cd20650 224 LSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLpNKAPPTYDTVMQMEYLDMVVNETLR---L 300
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 340 TPVSARL-----QDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFA----DEPVMKVFSSLGfSGTWECP 410
Cdd:cd20650 301 FPIAGRLervckKDVE--INGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSkknkDNIDPYIYLPFG-SGPRNCI 377
                       170
                ....*....|....*...
gi 26343433 411 ELRFAYMVTAVLVSVLLK 428
Cdd:cd20650 378 GMRFALMNMKLALVRVLQ 395
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
286-392 6.63e-17

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: 82.35  E-value: 6.63e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 286 TWTIHFLTTTGEVQKKLCKEIDQVLGEGPITS-EKIEQLSYCQQVLFETVRTAKLTPVS---ARLQDIEgkVGPFVIPKE 361
Cdd:cd11028 252 QWSLLYMIRYPEIQEKVQAELDRVIGRERLPRlSDRPNLPYTEAFILETMRHSSFVPFTiphATTRDTT--LNGYFIPKG 329
                        90       100       110
                ....*....|....*....|....*....|.
gi 26343433 362 TLVLYALGVVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd11028 330 TVVFVNLWSVNHDEKLWPDPSVFRPERFLDD 360
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
56-444 1.31e-16

putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of Mycobacterium tuberculosis putative cytochrome P450 136 (CYP136) and similar proteins. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 81.60  E-value: 1.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  56 EFLVNLHERYGPVVSFW-FGRRLVVSLGTTDVLKQHFNPNKtSDPFETMLKSLLG-YQSGGGSA--GEDHV-RRKLYGDA 130
Cdd:cd11045   1 EFARQRYRRYGPVSWTGmLGLRVVALLGPDANQLVLRNRDK-AFSSKQGWDPVIGpFFHRGLMLldFDEHRaHRRIMQQA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 131 VTAS-LHSNFPLLLQLSEELLDKWlsyPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEviRFQK-IHGTVWSEIGKG 208
Cdd:cd11045  80 FTRSaLAGYLDRMTPGIERALARW---PTGAGFQFYPAIKELTLDLATRVFLGVDLGPEAD--KVNKaFIDTVRASTAII 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 209 FLD--GSLDKNTTRKKQYqealmqLESTLKKIIKERKGGN----FRQHTFIDSLTQGKLNEQQILeDCVVFSL--ASCII 280
Cdd:cd11045 155 RTPipGTRWWRGLRGRRY------LEEYFRRRIPERRAGGgddlFSALCRAEDEDGDRFSDDDIV-NHMIFLMmaAHDTT 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 281 TARLCTWTiHFLTTTGEVQKKLCKEIdQVLGEGPITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQDIEgkVGPFVI 358
Cdd:cd11045 228 TSTLTSMA-YFLARHPEWQERLREES-LALGKGTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRraVKDTE--VLGYRI 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 359 PKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVM-KV--FSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLA 434
Cdd:cd11045 304 PAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEdKVhrYAWAPFGgGAHKCIGLHFAGMEVKAILHQMLRRFRWWS 383
                       410
                ....*....|
gi 26343433 435 VDRQVFEMKY 444
Cdd:cd11045 384 VPGYYPPWWQ 393
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
222-392 2.10e-16

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: 81.11  E-value: 2.10e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 222 KQYQEALMQLESTLKKIIKERKG----GNFRQhtFIDSLTQ---------GKLNEQQILEDCVVFSLASCIITARLCTWT 288
Cdd:cd20651 171 NLLVELNQKLIEFLKEEIKEHKKtydeDNPRD--LIDAYLRemkkkeppsSSFTDDQLVMICLDLFIAGSETTSNTLGFA 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 289 IHFLTTTGEVQKKLCKEIDQVLGEG--PITSEKIeQLSYCQQVLFETVRTAKLTPVS-AR--LQDIegKVGPFVIPKETL 363
Cdd:cd20651 249 FLYLLLNPEVQRKVQEEIDEVVGRDrlPTLDDRS-KLPYTEAVILEVLRIFTLVPIGiPHraLKDT--TLGGYRIPKDTT 325
                       170       180
                ....*....|....*....|....*....
gi 26343433 364 VLYALGVVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd20651 326 ILASLYSVHMDPEYWGDPEEFRPERFLDE 354
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
216-456 2.53e-16

cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is composed of family 4 cytochrome P450s from vertebrate subfamilies A (CYP4A), B (CYP4B), F (CYP4F), T (CYP4T), X (CYP4X), and Z (CYP4Z). Also included are similar proteins from lancelets, tunicates, hemichordates, echinoderms, mollusks, annelid worms, sponges, and choanoflagellates, among others. The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B and CYP4F are conserved among vertebrates. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4F enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4B_4F-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410752 [Multi-domain]  Cd Length: 423  Bit Score: 80.68  E-value: 2.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 216 KNTTRKKQYQEALMQLESTLKKIIKERK---------GGNFRQHT-FIDSLTQGK------LNEQQILEDCVVF------ 273
Cdd:cd20659 162 YLTPEGRRFKKACDYVHKFAEEIIKKRRkelednkdeALSKRKYLdFLDILLTARdedgkgLTDEEIRDEVDTFlfaghd 241
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 274 SLASCIitarlcTWTIHFLTTTGEVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEGK 352
Cdd:cd20659 242 TTASGI------SWTLYSLAKHPEHQQKCREEVDEVLGDRdDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPIT 315
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 353 VGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMKV--FSSLGFS-GTWECPELRFAYMVTAVLVSVLLKR 429
Cdd:cd20659 316 IDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRdpFAFIPFSaGPRNCIGQNFAMNEMKVVLARILRR 395
                       250       260
                ....*....|....*....|....*..
gi 26343433 430 LRLLAVDRQVFEMKYELVTSAREEAWI 456
Cdd:cd20659 396 FELSVDPNHPVEPKPGLVLRSKNGIKL 422
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
222-448 3.15e-16

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: 80.26  E-value: 3.15e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 222 KQYQEALMQLESTLKKII-------KERKGGNFRQHTFIDS-LTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLT 293
Cdd:cd11054 180 KKFVKAWDTIFDIASKYVdealeelKKKDEEDEEEDSLLEYlLSKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLA 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 294 TTGEVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQQVLFETVRtakLTPVS---ARL--QDIEgkVGPFVIPKETLVLYA 367
Cdd:cd11054 260 KNPEVQEKLYEEIRSVLPDGePITAEDLKKMPYLKACIKESLR---LYPVApgnGRIlpKDIV--LSGYHIPKGTLVVLS 334
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 368 LGVVLQDPSTWPLPHRFDPDRF-ADEPVMKV---FSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVfEM 442
Cdd:cd11054 335 NYVMGRDEEYFPDPEEFIPERWlRDDSENKNihpFASLPFGfGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHEEL-KV 413

                ....*.
gi 26343433 443 KYELVT 448
Cdd:cd11054 414 KTRLIL 419
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
221-446 3.33e-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: 80.26  E-value: 3.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 221 KKQYQEALMQLESTLKKIIKERKG-GNFRQHTFIDSLTQ--------GKLNEQQILEDCVVFSLASCIITARLCTWTIHF 291
Cdd:cd20613 181 RREVREAIKFLRETGRECIEERLEaLKRGEEVPNDILTHilkaseeePDFDMEELLDDFVTFFIAGQETTANLLSFTLLE 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 292 LTTTGEVQKKLCKEIDQVLGEGP-ITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKETLVL---YA 367
Cdd:cd20613 261 LGRHPEILKRLQAEVDEVLGSKQyVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLvstYV 340
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 368 LGvvlQDPSTWPLPHRFDPDRFADEPVMKV--FSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVFEMKY 444
Cdd:cd20613 341 MG---RMEEYFEDPLKFDPERFSPEAPEKIpsYAYFPFSlGPRSCIGQQFAQIEAKVILAKLLQNFKFELVPGQSFGILE 417

                ..
gi 26343433 445 EL 446
Cdd:cd20613 418 EV 419
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
65-426 7.23e-16

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: 79.45  E-value: 7.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  65 YGPVVSFWFGRRLVVSLGTTD----VLKQHFNP------NKTSDPFETMLKSLLGYQSGggsageDH---VR-------- 123
Cdd:cd20656   1 YGPIISVWIGSTLNVVVSSSElakeVLKEKDQQladrhrTRSAARFSRNGQDLIWADYG------PHyvkVRklctlelf 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 124 --------RKLYGDAVTASLHSNFplllqlseelLDKWLSYPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEVIRFQ 195
Cdd:cd20656  75 tpkrleslRPIREDEVTAMVESIF----------NDCMSPENEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEQ 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 196 ------------KIHG-------TVWSEIGKGFLDGSLDKNTTRKKQYQEALMQLEStlkkiIKERKGGNFRQHtFIDSL 256
Cdd:cd20656 145 gvefkaivsnglKLGAsltmaehIPWLRWMFPLSEKAFAKHGARRDRLTKAIMEEHT-----LARQKSGGGQQH-FVALL 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 257 TqgkLNEQQILEDCVVFSLASCIITARLCT------WTIHFLTTTGEVQKKLCKEIDQVLGEGPITSE-KIEQLSYCQQV 329
Cdd:cd20656 219 T---LKEQYDLSEDTVIGLLWDMITAGMDTtaisveWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEaDFPQLPYLQCV 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 330 LFETVRTAKLTPVSARLQDIEG-KVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPV-MK--VFSSLGF-S 404
Cdd:cd20656 296 VKEALRLHPPTPLMLPHKASENvKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVdIKghDFRLLPFgA 375
                       410       420
                ....*....|....*....|...
gi 26343433 405 GTWECPELRFAY-MVTAVLVSVL 426
Cdd:cd20656 376 GRRVCPGAQLGInLVTLMLGHLL 398
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
219-432 8.36e-16

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


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 79.30  E-value: 8.36e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 219 TRKKQYQEALMQLESTLKKIIKE--------RKGGNFRQHTFIDSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIH 290
Cdd:cd11070 169 SRKRAFKDVDEFLSELLDEVEAElsadskgkQGTESVVASRLKRARRSGGLTEKELLGNLFIFFIAGHETTANTLSFALY 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 291 FLTTTGEVQKKLCKEIDQVLGEGPI---TSEKIEQLSYCQQVLFETVR-------TAKLTPVSARLQDIEGKvgPFVIPK 360
Cdd:cd11070 249 LLAKHPEVQDWLREEIDSVLGDEPDdwdYEEDFPKLPYLLAVIYETLRlyppvqlLNRKTTEPVVVITGLGQ--EIVIPK 326
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 361 ETLVLYALGVVLQDPSTW-PLPHRFDPDRFaDEPVMKVFSS----------LGFS-GTWECPELRFAYMVTAVLVSVLLK 428
Cdd:cd11070 327 GTYVGYNAYATHRDPTIWgPDADEFDPERW-GSTSGEIGAAtrftpargafIPFSaGPRACLGRKFALVEFVAALAELFR 405

                ....
gi 26343433 429 RLRL 432
Cdd:cd11070 406 QYEW 409
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
218-389 1.69e-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: 78.07  E-value: 1.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 218 TTRKKQYQEALMQLESTLKKIIKER-----KGGNFRQHTFIDSLTQGKLNEQ--------QILEDCVVFSLASCIITARL 284
Cdd:cd20621 169 TKKEKKLQKRVKELRQFIEKIIQNRikqikKNKDEIKDIIIDLDLYLLQKKKleqeitkeEIIQQFITFFFAGTDTTGHL 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 285 CTWTIHFLTTTGEVQKKLCKEIDQVLG-EGPITSEKIEQLSYCQQVLFETVRtakLTPVSARL------QDIegKVGPFV 357
Cdd:cd20621 249 VGMCLYYLAKYPEIQEKLRQEIKSVVGnDDDITFEDLQKLNYLNAFIKEVLR---LYNPAPFLfprvatQDH--QIGDLK 323
                       170       180       190
                ....*....|....*....|....*....|..
gi 26343433 358 IPKETLVLYALGVVLQDPSTWPLPHRFDPDRF 389
Cdd:cd20621 324 IKKGWIVNVGYIYNHFNPKYFENPDEFNPERW 355
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
235-434 2.41e-15

cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is expressed during development of the gastrointestinal tract, is silenced after birth in the intestine and colon by epigenetic modifications, but is activated following demethylation in colorectal cancer (CRC). Its expression levels in CRC correlate with the degree of malignancy, are higher in metastases and are predictive of survival. Thus, it is an attractive tumor-specific diagnostic and therapeutic target. CYP2W1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 77.53  E-value: 2.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 235 LKKIIKERK----GGNFrqHTFIDSLTQ---------GKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKK 301
Cdd:cd20671 182 LRTLIEARRptidGNPL--HSYIEALIQkqeeddpkeTLFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKR 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 302 LCKEIDQVLGEG-PITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPL 380
Cdd:cd20671 260 VQEEIDRVLGPGcLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWET 339
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 26343433 381 PHRFDPDRF--ADEPVMKVFSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLA 434
Cdd:cd20671 340 PYQFNPNHFldAEGKFVKKEAFLPFSaGRRVCVGESLARTELFIFFTGLLQKFTFLP 396
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
260-429 1.33e-14

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: 1.33e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 260 KLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEG--PITSEKIEQLSYCQQVLFETVRTA 337
Cdd:cd20680 238 KLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSdrPVTMEDLKKLRYLECVIKESLRLF 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 338 KLTPVSARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMKV--FSSLGFS-GTWECPELRF 414
Cdd:cd20680 318 PSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRhpYAYIPFSaGPRNCIGQRF 397
                       170
                ....*....|....*
gi 26343433 415 AYMVTAVLVSVLLKR 429
Cdd:cd20680 398 ALMEEKVVLSCILRH 412
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
13-430 3.16e-14

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 74.73  E-value: 3.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   13 LALVGAVLYLYPASRQASGIPGLTPTEEKDGNLPDIVNSGSLHeFLVNLHERYGPVVSFWFGRRLVVSLGTTDVLKQHFN 92
Cdd:PLN03234  10 LVAAAAFFFLRSTTKKSLRLPPGPKGLPIIGNLHQMEKFNPQH-FLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   93 P---NKTSDPF----ETMlkSLLGYQSGGG--SAGEDHVRRKLYGDAVTASLHSNF-PLLLQLSEELLDK-WLSYPETQH 161
Cdd:PLN03234  89 TqdlNFTARPLlkgqQTM--SYQGRELGFGqyTAYYREMRKMCMVNLFSPNRVASFrPVREEECQRMMDKiYKAADQSGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  162 IPLSQHMLGFALKFVTRMVLGSTF-EDEQEVIRFQKIHGTVWSEIGKGFLD------GSLDKNTTRKKQYQEALMQLEST 234
Cdd:PLN03234 167 VDLSELLLSFTNCVVCRQAFGKRYnEYGTEMKRFIDILYETQALLGTLFFSdlfpyfGFLDNLTGLSARLKKAFKELDTY 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  235 LKKIIKERKGGNF-RQHT--FIDSLTQ-----------GKLNEQQILEDCVVFSLASciiTARLCTWTIHFLTTTGEVQK 300
Cdd:PLN03234 247 LQELLDETLDPNRpKQETesFIDLLMQiykdqpfsikfTHENVKAMILDIVVPGTDT---AAAVVVWAMTYLIKYPEAMK 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  301 KLCKEIDQVLGE-GPITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDI-EGKVGPFVIPKETLVLYALGVVLQDPSTW 378
Cdd:PLN03234 324 KAQDEVRNVIGDkGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIaDAKIGGYDIPAKTIIQVNAWAVSRDTAAW 403
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 26343433  379 -PLPHRFDPDRFADEPVMKVFSSLGF------SGTWECPELRFAYMVTAVLVSVLLKRL 430
Cdd:PLN03234 404 gDNPNEFIPERFMKEHKGVDFKGQDFellpfgSGRRMCPAMHLGIAMVEIPFANLLYKF 462
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
220-392 3.29e-14

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: 74.20  E-value: 3.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 220 RKKQYQEALMQLESTLKKIIKERK---GGNFRQHTFIDSL-----------TQGKLNEQQILEDCVVFSLASCIITARLC 285
Cdd:cd11075 172 RWKKVLELRRRQEEVLLPLIRARRkrrASGEADKDYTDFLlldlldlkeegGERKLTDEELVSLCSEFLNAGTDTTATAL 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 286 TWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEK-IEQLSYCQQVLFETVR---TAKLTPVSARLQDIegKVGPFVIPKE 361
Cdd:cd11075 252 EWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEdLPKMPYLKAVVLETLRrhpPGHFLLPHAVTEDT--VLGGYDIPAG 329
                       170       180       190
                ....*....|....*....|....*....|.
gi 26343433 362 TLVLYALGVVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd11075 330 AEVNFNVAAIGRDPKVWEDPEEFKPERFLAG 360
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
253-434 4.98e-14

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 74.00  E-value: 4.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  253 IDSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQQVLF 331
Cdd:PLN02394 281 LEAQKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGnQVTEPDTHKLPYLQAVVK 360
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  332 ETVRTAKLTPVSARLQDI-EGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEP-----VMKVFSSLGF-S 404
Cdd:PLN02394 361 ETLRLHMAIPLLVPHMNLeDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEakveaNGNDFRFLPFgV 440
                        170       180       190
                 ....*....|....*....|....*....|
gi 26343433  405 GTWECPELRFAYMVTAVLVSVLLKRLRLLA 434
Cdd:PLN02394 441 GRRSCPGIILALPILGIVLGRLVQNFELLP 470
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
257-436 6.31e-14

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: 73.12  E-value: 6.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 257 TQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLG--EGPITSEKIEQLSYCQQVLFETV 334
Cdd:cd11083 214 PDARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGgaRVPPLLEALDRLPYLEAVARETL 293
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 335 RTAKLTPVSARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRF---ADEPVMKVFSS-LGF-SGTWEC 409
Cdd:cd11083 294 RLKPVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWldgARAAEPHDPSSlLPFgAGPRLC 373
                       170       180
                ....*....|....*....|....*..
gi 26343433 410 PELRFAYMVTAVLVSVLLKRLRLLAVD 436
Cdd:cd11083 374 PGRSLALMEMKLVFAMLCRNFDIELPE 400
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
230-392 1.06e-13

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: 72.59  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 230 QLESTLKKIIKERKG----GNFRQhtFIDS----LTQGKLN------EQQILedCVVFSL--ASCIITARLCTWTIHFLT 293
Cdd:cd11026 179 EIKSFIRELVEEHREtldpSSPRD--FIDCfllkMEKEKDNpnsefhEENLV--MTVLDLffAGTETTSTTLRWALLLLM 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 294 TTGEVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQQVLFETVRTAKLTPVS---ARLQDIegKVGPFVIPKETLVLYALG 369
Cdd:cd11026 255 KYPHIQEKVQEEIDRVIGRNrTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGvphAVTRDT--KFRGYTIPKGTTVIPNLT 332
                       170       180
                ....*....|....*....|...
gi 26343433 370 VVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd11026 333 SVLRDPKQWETPEEFNPGHFLDE 355
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
232-392 1.47e-13

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: 72.35  E-value: 1.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 232 ESTLKKIIKERKGgNFRQHT---FIDSLTQGKLNEQ----QILEDCVVFS------------LASCIITARLCTWTIHFL 292
Cdd:cd20673 181 DKLLQKKLEEHKE-KFSSDSirdLLDALLQAKMNAEnnnaGPDQDSVGLSddhilmtvgdifGAGVETTTTVLKWIIAFL 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 293 TTTGEVQKKLCKEIDQVLGEG--PITSEKiEQLSYCQQVLFETVRtakLTPVSARL----QDIEGKVGPFVIPKETLVLY 366
Cdd:cd20673 260 LHNPEVQKKIQEEIDQNIGFSrtPTLSDR-NHLPLLEATIREVLR---IRPVAPLLiphvALQDSSIGEFTIPKGTRVVI 335
                       170       180
                ....*....|....*....|....*.
gi 26343433 367 ALGVVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd20673 336 NLWALHHDEKEWDQPDQFMPERFLDP 361
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
225-439 2.21e-13

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: 71.53  E-value: 2.21e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 225 QEALMQLESTLKKIIKERK-----GGNFRQHTFIDSL-------TQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFL 292
Cdd:cd11069 183 RRAKDVLRRLAREIIREKKaalleGKDDSGKDILSILlrandfaDDERLSDEELIDQILTFLAAGHETTSTALTWALYLL 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 293 TTTGEVQKKLCKEIDQVL---GEGPITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQDIegKVGPFVIPKETLVLYA 367
Cdd:cd11069 263 AKHPDVQERLREEIRAALpdpPDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSReaTKDT--VIKGVPIPKGTVVLIP 340
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 368 LGVVLQDPSTW-PLPHRFDPDRFADEPVMKVFSSLG--------FSGTWECPELRFAYMVTAVLVSVLLKRLRL-LAVDR 437
Cdd:cd11069 341 PAAINRSPEIWgPDAEEFNPERWLEPDGAASPGGAGsnyalltfLHGPRSCIGKKFALAEMKVLLAALVSRFEFeLDPDA 420

                ..
gi 26343433 438 QV 439
Cdd:cd11069 421 EV 422
PLN02290 PLN02290
cytokinin trans-hydroxylase
206-432 2.23e-13

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 72.15  E-value: 2.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  206 GKGFLDGSLDKNTTRKKqyqealMQLESTLKKIIKERK-----GgnfRQHTFIDSLTQGKLNE-------------QQIL 267
Cdd:PLN02290 248 GSRFFPSKYNREIKSLK------GEVERLLMEIIQSRRdcveiG---RSSSYGDDLLGMLLNEmekkrsngfnlnlQLIM 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  268 EDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEKIEQLSYCQQVLFETVR---TAKLTPVSA 344
Cdd:PLN02290 319 DECKTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVDHLSKLTLLNMVINESLRlypPATLLPRMA 398
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  345 rLQDIegKVGPFVIPKETLVLYALGVVLQDPSTW-PLPHRFDPDRFADEPVMKVFSSLGF-SGTWECPELRFAYMVTAVL 422
Cdd:PLN02290 399 -FEDI--KLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHFIPFaAGPRNCIGQAFAMMEAKII 475
                        250
                 ....*....|
gi 26343433  423 VSVLLKRLRL 432
Cdd:PLN02290 476 LAMLISKFSF 485
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
223-432 4.40e-13

cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The function of CYP2AB1 is unknown. CYP2AB1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 70.64  E-value: 4.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 223 QYQEALMQLesTLKKIIKERKGGNFRQHTFID----SLTQGK------LNEQQILEDCVVFSLASCIITARLCTWTIHFL 292
Cdd:cd20667 175 AYHDAVRSF--IKKEVIRHELRTNEAPQDFIDcylaQITKTKddpvstFSEENMIQVVIDLFLGGTETTATTLHWALLYM 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 293 TTTGEVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEGK-VGPFVIPKETLVLYALGV 370
Cdd:cd20667 253 VHHPEIQEKVQQELDEVLGASqLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAVRQCVTSTtMHGYYVEKGTIILPNLAS 332
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26343433 371 VLQDPSTWPLPHRFDPDRFADEP---VMKVfSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRL 432
Cdd:cd20667 333 VLYDPECWETPHKFNPGHFLDKDgnfVMNE-AFLPFSaGHRVCLGEQLARMELFIFFTTLLRTFNF 397
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
236-391 6.43e-13

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: 70.21  E-value: 6.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 236 KKIIKERKGGNFRQ-HTFIDSL---------TQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKE 305
Cdd:cd20662 186 DMIDKHREDWNPDEpRDFIDAYlkemakypdPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAE 265
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 306 IDQVLGEG--PITSEKiEQLSYCQQVLFETVRTAKLTPV-SARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPH 382
Cdd:cd20662 266 IDRVIGQKrqPSLADR-ESMPYTNAVIHEVQRMGNIIPLnVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPD 344

                ....*....
gi 26343433 383 RFDPDRFAD 391
Cdd:cd20662 345 TFNPGHFLE 353
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
286-392 1.21e-12

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: 69.26  E-value: 1.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 286 TWTIHFLTTTGEVQKKLCKEIDQVLGEGPITS-EKIEQLSYCQQVLFETVRTAKLTPVS---ARLQD--IEGkvgpFVIP 359
Cdd:cd20675 256 QWILLLLVRYPDVQARLQEELDRVVGRDRLPCiEDQPNLPYVMAFLYEAMRFSSFVPVTiphATTADtsILG----YHIP 331
                        90       100       110
                ....*....|....*....|....*....|...
gi 26343433 360 KETLVLYALGVVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd20675 332 KDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDE 364
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
176-433 1.23e-12

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: 69.36  E-value: 1.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 176 VTRMVLGSTFEDEQEvirFQKIHGTV------WSEIGKGFLDG--SLDK--NTTRKKQYQeALMQLESTLKKIIKERKGG 245
Cdd:cd20674 118 ICCLTFGDKEDKDTL---VQAFHDCVqellktWGHWSIQALDSipFLRFfpNPGLRRLKQ-AVENRDHIVESQLRQHKES 193
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 246 NFRQ--HTFIDSLTQG---KLNEQ---QILEDCVVFSLASCII-----TARLCTWTIHFLTTTGEVQKKLCKEIDQVLG- 311
Cdd:cd20674 194 LVAGqwRDMTDYMLQGlgqPRGEKgmgQLLEGHVHMAVVDLFIggtetTASTLSWAVAFLLHHPEIQDRLQEELDRVLGp 273
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 312 EGPITSEKIEQLSYCQQVLFETVRtakLTPV--------SARLQDIEGkvgpFVIPKETLVLYALGVVLQDPSTWPLPHR 383
Cdd:cd20674 274 GASPSYKDRARLPLLNATIAEVLR---LRPVvplalphrTTRDSSIAG----YDIPKGTVVIPNLQGAHLDETVWEQPHE 346
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 26343433 384 FDPDRFADePVMKVFSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLL 433
Cdd:cd20674 347 FRPERFLE-PGAANRALLPFGcGARVCLGEPLARLELFVFLARLLQAFTLL 396
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
253-434 1.36e-12

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


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 69.42  E-value: 1.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 253 IDSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGP-ITSEKIEQLSYCQQVLF 331
Cdd:cd11074 221 LDAQKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVqITEPDLHKLPYLQAVVK 300
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 332 ETVRTAKLTPVSARLQDI-EGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVmKV------FSSLGFS 404
Cdd:cd11074 301 ETLRLRMAIPLLVPHMNLhDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEES-KVeangndFRYLPFG 379
                       170       180       190
                ....*....|....*....|....*....|.
gi 26343433 405 -GTWECPELRFAYMVTAVLVSVLLKRLRLLA 434
Cdd:cd11074 380 vGRRSCPGIILALPILGITIGRLVQNFELLP 410
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
258-436 1.53e-12

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: 69.10  E-value: 1.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 258 QGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITS-EKIEQLSYCQQVLFETVRt 336
Cdd:cd20649 254 KRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDyANVQELPYLDMVIAETLR- 332
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 337 akLTPVSARL-----QDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMK--VFSSLGF-SGTWE 408
Cdd:cd20649 333 --MYPPAFRFareaaEDCV--VLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRrhPFVYLPFgAGPRS 408
                       170       180
                ....*....|....*....|....*...
gi 26343433 409 CPELRFAYMVTAVLVSVLLKRLRLLAVD 436
Cdd:cd20649 409 CIGMRLALLEIKVTLLHILRRFRFQACP 436
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
287-442 2.65e-12

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: 68.21  E-value: 2.65e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 287 WTIHFLTTTGEVQKKLCKEIDQVLGEGP-ITSEKIEQLSYCQQVLFETVRTAKLTPVS---ARLQDIEgkVGPFVIPKET 362
Cdd:cd20652 256 WFLLYMALFPKEQRRIQRELDEVVGRPDlVTLEDLSSLPYLQACISESQRIRSVVPLGiphGCTEDAV--LAGYRIPKGS 333
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 363 LVLYALGVVLQDPSTWPLPHRFDPDRFADE--PVMKVFSSLGF-SGTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQV 439
Cdd:cd20652 334 MIIPLLWAVHMDPNLWEEPEEFRPERFLDTdgKYLKPEAFIPFqTGKRMCLGDELARMILFLFTARILRKFRIALPDGQP 413

                ...
gi 26343433 440 FEM 442
Cdd:cd20652 414 VDS 416
PLN02302 PLN02302
ent-kaurenoic acid oxidase
57-410 3.46e-12

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 68.20  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   57 FLVNLHERYGPV---VSFWFGRRLVvsLGTTD-----VLKQHfNPNKTSDPFETMlkSLLGYQSGGGSAGEDHVR-RKLY 127
Cdd:PLN02302  71 FIASFISRYGRTgiyKAFMFGQPTV--LVTTPeackrVLTDD-DAFEPGWPESTV--ELIGRKSFVGITGEEHKRlRRLT 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  128 GDAVTA--SLHSNFPLLLQLSEELLDKWLSYPETQhipLSQHMLGFALKFVTRMVLGSTFEDEQEV-----------IRF 194
Cdd:PLN02302 146 AAPVNGpeALSTYIPYIEENVKSCLEKWSKMGEIE---FLTELRKLTFKIIMYIFLSSESELVMEAlereyttlnygVRA 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  195 QKIH--GTVWSEIGKGfldgsldknttRKKqyqealmqLESTLKKIIKER----KGGNFRQHT-----FIDSLTQG--KL 261
Cdd:PLN02302 223 MAINlpGFAYHRALKA-----------RKK--------LVALFQSIVDERrnsrKQNISPRKKdmldlLLDAEDENgrKL 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  262 NEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVL-----GEGPITSEKIEQLSYCQQVLFETVRT 336
Cdd:PLN02302 284 DDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAkkrppGQKGLTLKDVRKMEYLSQVIDETLRL 363
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26343433  337 AKLTPVSAR--LQDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVmKVFSSLGFS-GTWECP 410
Cdd:PLN02302 364 INISLTVFReaKTDVE--VNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTP-KAGTFLPFGlGSRLCP 437
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
256-429 5.45e-12

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: 67.38  E-value: 5.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 256 LTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPI-TSEKIEQLSYCQQVLFETV 334
Cdd:cd20646 224 LSSGKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIpTAEDIAKMPLLKAVIKETL 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 335 RTAKLTPVSARL-QDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMK--VFSSLGFS-GTWECP 410
Cdd:cd20646 304 RLYPVVPGNARViVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKhhPFGSIPFGyGVRACV 383
                       170
                ....*....|....*....
gi 26343433 411 ELRFAYMVTAVLVSVLLKR 429
Cdd:cd20646 384 GRRIAELEMYLALSRLIKR 402
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
208-392 7.08e-12

cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and amphibians. CYP2K6 from zebrafish has been shown to catalyze the conversion of aflatoxin B1 (AFB1) to its cytotoxic derivative AFB1 exo-8,9-epoxide, while its ortholog in rainbow trout CYP2K1 is also capable of oxidizing lauric acid. In birds, CYP2K is one of the largest CYP2 subfamilies. The CYP2K subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 67.14  E-value: 7.08e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 208 GFLDGSLDKNTTRKKQYQEALMQ-LESTLKkiIKERkggnFRQHTFIDSLtqgkLNEQQILED------------CVVFS 274
Cdd:cd20664 163 GPFPGDINKLLRNTKELNDFLMEtFMKHLD--VLEP----NDQRGFIDAF----LVKQQEEEEssdsffhddnltCSVGN 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 275 L--ASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEKIEQLSYCQQVLFETVRTAKLTPVS---ARLQDI 349
Cdd:cd20664 233 LfgAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVEHRKNMPYTDAVIHEIQRFANIVPMNlphATTRDV 312
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 26343433 350 EGKvGPFvIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd20664 313 TFR-GYF-IPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDS 353
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
151-428 8.46e-12

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: 66.93  E-value: 8.46e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 151 DKWLSYPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQE----VIRFQKIHGTVWSEIGK--GFLDGSLDKNTTRKKQY 224
Cdd:cd11041  97 EELGSCTEWTEVNLYDTVLRIVARVSARVFVGPPLCRNEEwldlTINYTIDVFAAAAALRLfpPFLRPLVAPFLPEPRRL 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 225 QEALMQLESTLKKIIKER----------KGGNFRQHTFIDSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTT 294
Cdd:cd11041 177 RRLLRRARPLIIPEIERRrklkkgpkedKPNDLLQWLIEAAKGEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAA 256
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 295 TGEVQKKLCKEIDQVLGE-GPITSEKIEQLSYCQQVLFETVRTAKLTPVSAR---LQDIeGKVGPFVIPKETLVLYALGV 370
Cdd:cd11041 257 HPEYIEPLREEIRSVLAEhGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRrkvLKDV-TLSDGLTLPKGTRIAVPAHA 335
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26343433 371 VLQDPSTWPLPHRFDPDRFA----DEPVMKVF-------SSLGFS-GTWECPElRF--AYMVTAVLVSVLLK 428
Cdd:cd11041 336 IHRDPDIYPDPETFDGFRFYrlreQPGQEKKHqfvstspDFLGFGhGRHACPG-RFfaSNEIKLILAHLLLN 406
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
176-426 1.05e-11

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: 66.47  E-value: 1.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 176 VTRMVLGSTF-EDEQEVIRFQKIHGTVwSEIGKGFLDGSLDKNTTR------KKQYQEALMQLESTLKKIIKER------ 242
Cdd:cd20655 120 ICRMIMGRSCsEENGEAEEVRKLVKES-AELAGKFNASDFIWPLKKldlqgfGKRIMDVSNRFDELLERIIKEHeekrkk 198
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 243 -KGGNFRQhtFIDSL--------TQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEG 313
Cdd:cd20655 199 rKEGGSKD--LLDILldayedenAEYKITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKT 276
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 314 PITSEK-IEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKETLVL---YALGvvlQDPSTWPLPHRFDPDRF 389
Cdd:cd20655 277 RLVQESdLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKTTLFvnvYAIM---RDPNYWEDPLEFKPERF 353
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 26343433 390 --------ADEPVMKVFSSLGF-SGTWECPELRFAYMVTAVLVSVL 426
Cdd:cd20655 354 lassrsgqELDVRGQHFKLLPFgSGRRGCPGASLAYQVVGTAIAAM 399
PLN02966 PLN02966
cytochrome P450 83A1
6-427 1.22e-11

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 66.69  E-value: 1.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433    6 IFAVTFLLALVGAVLYLYPASRQASGIPGLTPteekdgnLPDIVNSGSLHE-----FLVNLHERYGPVVSFWFGRRLVVS 80
Cdd:PLN02966   5 IIGVVALAAVLLFFLYQKPKTKRYKLPPGPSP-------LPVIGNLLQLQKlnpqrFFAGWAKKYGPILSYRIGSRTMVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   81 LGTTDVLKQHFN---------PNKTSDPF------ETMLKSLLGYQSGGGSAGEDHvrrkLYGDAVTASLHSNFPLLLQL 145
Cdd:PLN02966  78 ISSAELAKELLKtqdvnfadrPPHRGHEFisygrrDMALNHYTPYYREIRKMGMNH----LFSPTRVATFKHVREEEARR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  146 SEELLDKwlSYPETQHIPLSQHMLGFALKFVTRMVLGSTF-EDEQEVIRFQKIHGTVWSEIGKGFLD------GSLDKNT 218
Cdd:PLN02966 154 MMDKINK--AADKSEVVDISELMLTFTNSVVCRQAFGKKYnEDGEEMKRFIKILYGTQSVLGKIFFSdffpycGFLDDLS 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  219 TRKKQYQEALMQLESTLKKIIKERKG----------------GNFRQHTFIDSLTQGklNEQQILEDCVVfslASCIITA 282
Cdd:PLN02966 232 GLTAYMKECFERQDTYIQEVVNETLDpkrvkpetesmidllmEIYKEQPFASEFTVD--NVKAVILDIVV---AGTDTAA 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  283 RLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGP---ITSEKIEQLSYCQQVLFETVRTAKLTPV---SARLQDIegKVGPF 356
Cdd:PLN02966 307 AAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGstfVTEDDVKNLPYFRALVKETLRIEPVIPLlipRACIQDT--KIAGY 384
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26343433  357 VIPKETLVLYALGVVLQDPSTW-PLPHRFDPDRFADEPVMKVFSSLGF----SGTWECPELRFAYMVTAVLVSVLL 427
Cdd:PLN02966 385 DIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKGTDYEFipfgSGRRMCPGMRLGAAMLEVPYANLL 460
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
297-426 2.97e-11

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: 65.25  E-value: 2.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 297 EVQKKLCKEIDQVLGEGPITSEK-IEQLSYCQQVLFETVRtakLTPVSARL------QDIEgkVGPFVIPKETLVL---Y 366
Cdd:cd11073 263 EKMAKARAELDEVIGKDKIVEESdISKLPYLQAVVKETLR---LHPPAPLLlprkaeEDVE--VMGYTIPKGTQVLvnvW 337
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26343433 367 ALGvvlQDPSTWPLPHRFDPDRFADEPVM---KVFSSLGF-SGTWECPELRFAY-MVTAVLVSVL 426
Cdd:cd11073 338 AIG---RDPSVWEDPLEFKPERFLGSEIDfkgRDFELIPFgSGRRICPGLPLAErMVHLVLASLL 399
PLN02687 PLN02687
flavonoid 3'-monooxygenase
259-389 3.84e-11

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 64.83  E-value: 3.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  259 GKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSE-KIEQLSYCQQVLFETVRTA 337
Cdd:PLN02687 291 GRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSEsDLPQLTYLQAVIKETFRLH 370
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 26343433  338 KLTPVS-ARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRF 389
Cdd:PLN02687 371 PSTPLSlPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRF 423
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
281-459 4.45e-11

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: 64.50  E-value: 4.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 281 TARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGP-ITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQD--------I 349
Cdd:cd11063 232 TASLLSFLFYELARHPEVWAKLREEVLSLFGPEPtPTYEDLKNMKYLRAVINETLRLYPPVPLNSRvaVRDttlprgggP 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 350 EGKvGPFVIPKETLVLYALGVVLQDPSTW-PLPHRFDPDRFADEPvmkvfsslgfSGTWE----------CPELRFAYMV 418
Cdd:cd11063 312 DGK-SPIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWEDLK----------RPGWEylpfnggpriCLGQQFALTE 380
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 26343433 419 TA-VLVsvllkrlRLLavdrQVFE-MKYELVTSAREEAWITVS 459
Cdd:cd11063 381 ASyVLV-------RLL----QTFDrIESRDVRPPEERLTLTLS 412
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
226-438 5.46e-11

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 64.19  E-value: 5.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  226 EALMQLESTLKKIIKERKGGNFRQHTFIDSLTQGK--LNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLC 303
Cdd:PLN02196 223 KARKELAQILAKILSKRRQNGSSHNDLLGSFMGDKegLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVT 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  304 KEIDQVLG----EGPITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQDIEGKvgPFVIPKETLVLYALGVVLQDPST 377
Cdd:PLN02196 303 EEQMAIRKdkeeGESLTWEDTKKMPLTSRVIQETLRVASILSFTFReaVEDVEYE--GYLIPKGWKVLPLFRNIHHSADI 380
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26343433  378 WPLPHRFDPDRFADEPVMKVFSSLGfSGTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQ 438
Cdd:PLN02196 381 FSDPGKFDPSRFEVAPKPNTFMPFG-NGTHSCPGNELAKLEISVLIHHLTTKYRWSIVGTS 440
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
231-392 6.26e-11

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: 64.03  E-value: 6.26e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 231 LESTLKKIIKERKGG--NFRQHTFID------SLTQGKLNEQQILEDCVVFSLASCII-----TARLCTWTIHFLTTTGE 297
Cdd:cd20666 181 ITAFLKKIIADHRETldPANPRDFIDmyllhiEEEQKNNAESSFNEDYLFYIIGDLFIagtdtTTNTLLWCLLYMSLYPE 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 298 VQKKLCKEIDQVLGEG--PITSEKiEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKV-GPFVIPKETLVLYALGVVLQD 374
Cdd:cd20666 261 VQEKVQAEIDTVIGPDraPSLTDK-AQMPFTEATIMEVQRMTVVVPLSIPHMASENTVlQGYTIPKGTVIVPNLWSVHRD 339
                       170
                ....*....|....*...
gi 26343433 375 PSTWPLPHRFDPDRFADE 392
Cdd:cd20666 340 PAIWEKPDDFMPSRFLDE 357
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
164-394 6.62e-11

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: 64.02  E-value: 6.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 164 LSQHMLGFALKFVTRMVLGSTFEDEQEvIRFQKIHGTVWSEIGKGFLD------GSLDKNTTRKKQYQEALMQLESTLKK 237
Cdd:cd11072 110 LSELLFSLTNDIVCRAAFGRKYEGKDQ-DKFKELVKEALELLGGFSVGdyfpslGWIDLLTGLDRKLEKVFKELDAFLEK 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 238 IIKERKGGNFRQHTFIDSLTQGKLNEQQ---------------ILEDcvVFsLASCIITARLCTWTIHFLTTTGEVQKKL 302
Cdd:cd11072 189 IIDEHLDKKRSKDEDDDDDDLLDLRLQKegdlefpltrdnikaIILD--MF-LAGTDTSATTLEWAMTELIRNPRVMKKA 265
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 303 CKEIDQVLGE-GPITSEKIEQLSYCQQVLFETVRtakLTPVSARL------QDIegKVGPFVIPKETLVL---YALGvvl 372
Cdd:cd11072 266 QEEVREVVGGkGKVTEEDLEKLKYLKAVIKETLR---LHPPAPLLlprecrEDC--KINGYDIPAKTRVIvnaWAIG--- 337
                       250       260
                ....*....|....*....|..
gi 26343433 373 QDPSTWPLPHRFDPDRFADEPV 394
Cdd:cd11072 338 RDPKYWEDPEEFRPERFLDSSI 359
PLN02738 PLN02738
carotene beta-ring hydroxylase
264-461 1.23e-10

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 63.78  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  264 QQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEKIEQLSYCQQVLFETVRTAKLTPVS 343
Cdd:PLN02738 390 KQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQPPVL 469
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  344 ARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFA-DEP----VMKVFSSLGF-SGTWECPELRFAYM 417
Cdd:PLN02738 470 IRRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWPlDGPnpneTNQNFSYLPFgGGPRKCVGDMFASF 549
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 26343433  418 VTAVLVSVLLKRLRL-LAVDRQVFEMKYELVTSAREEAWITVSKR 461
Cdd:PLN02738 550 ENVVATAMLVRRFDFqLAPGAPPVKMTTGATIHTTEGLKMTVTRR 594
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
222-393 1.35e-10

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: 62.98  E-value: 1.35e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 222 KQYQEALMQLESTLKKIIKERKGGNFRQHTFIDSLTQGKLNEQQILEDCVVFSLASCII-----TARLCTWTIHFLTTTG 296
Cdd:cd11065 175 RELRELTRRLYEGPFEAAKERMASGTATPSFVKDLLEELDKEGGLSEEEIKYLAGSLYEagsdtTASTLQTFILAMALHP 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 297 EVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQQVLFETVRTAKLTPVS---ARLQDIE--GkvgpFVIPKETLVLYALGV 370
Cdd:cd11065 255 EVQKKAQEELDRVVGPDrLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGiphALTEDDEyeG----YFIPKGTTVIPNAWA 330
                       170       180
                ....*....|....*....|...
gi 26343433 371 VLQDPSTWPLPHRFDPDRFADEP 393
Cdd:cd11065 331 IHHDPEVYPDPEEFDPERYLDDP 353
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
235-397 1.64e-10

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: 62.82  E-value: 1.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 235 LKKIIKERKGGNFRQHTFIDSLTQ-----------GKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLC 303
Cdd:cd20657 187 LTKILEEHKATAQERKGKPDFLDFvllenddngegERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQ 266
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 304 KEIDQVLGEGPITSEK-IEQLSYCQQVLFETVRTAKLTPVS-ARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTWPLP 381
Cdd:cd20657 267 EEMDQVIGRDRRLLESdIPNLPYLQAICKETFRLHPSTPLNlPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENP 346
                       170
                ....*....|....*.
gi 26343433 382 HRFDPDRFADEPVMKV 397
Cdd:cd20657 347 LEFKPERFLPGRNAKV 362
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
221-388 1.69e-10

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: 62.66  E-value: 1.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 221 KKQYQEALMQLESTLKKIIKERkggnFRQHTFIDSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQK 300
Cdd:cd11062 184 AKQVDEVLRQVSAGDPPSIVTS----LFHALLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILE 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 301 KLCKEIDQVLGE--GPITSEKIEQLSYCQQVLFETVRTAklTPVSARLQDI---EG-KVGPFVIPKETLVLYALGVVLQD 374
Cdd:cd11062 260 RLREELKTAMPDpdSPPSLAELEKLPYLTAVIKEGLRLS--YGVPTRLPRVvpdEGlYYKGWVIPPGTPVSMSSYFVHHD 337
                       170
                ....*....|....
gi 26343433 375 PSTWPLPHRFDPDR 388
Cdd:cd11062 338 EEIFPDPHEFRPER 351
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
162-429 2.10e-10

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


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 62.43  E-value: 2.10e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 162 IPLSQHMLGFALKFVTRMVLGSTFEDEQEVirFQKIHgTVWSEIGKGF----LDGSLDKNTTRKKQYQEALMQLESTLKK 237
Cdd:cd20640 118 IVVDEDLRAFSADVISRACFGSSYSKGKEI--FSKLR-ELQKAVSKQSvlfsIPGLRHLPTKSNRKIWELEGEIRSLILE 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 238 IIKERK-----GGNFRQhTFIDSLTQGKLNEQQ----ILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQ 308
Cdd:cd20640 195 IVKEREeecdhEKDLLQ-AILEGARSSCDKKAEaedfIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLE 273
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 309 VLGEGPITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQDIegKVGPFVIPKETLVLYALGVVLQDPSTW-PLPHRFD 385
Cdd:cd20640 274 VCKGGPPDADSLSRMKTVTMVIQETLRLYPPAAFVSReaLRDM--KLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFN 351
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 26343433 386 PDRFAD---EPVMKVFSSLGF-SGTWECPELRFAYMVTAVLVSVLLKR 429
Cdd:cd20640 352 PERFSNgvaAACKPPHSYMPFgAGARTCLGQNFAMAELKVLVSLILSK 399
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
176-432 3.70e-10

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


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 61.70  E-value: 3.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 176 VTRMVLGSTFEDEQEVIRFQK-IHGTVWSEIGKGFLDGSLDKNTTRKKQYQEALMQLESTLKKIIKER---KGGNFRQHT 251
Cdd:cd20641 131 IATTAFGSSYAEGIEVFLSQLeLQKCAAASLTNLYIPGTQYLPTPRNLRVWKLEKKVRNSIKRIIDSRltsEGKGYGDDL 210
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 252 FIDSLTQGKLNEQ-----------QILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEI-DQVLGEGPITSEK 319
Cdd:cd20641 211 LGLMLEAASSNEGgrrterkmsidEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVfRECGKDKIPDADT 290
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 320 IEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKETLVLYALGVVLQDPSTW-PLPHRFDPDRFAD---EPVM 395
Cdd:cd20641 291 LSKLKLMNMVLMETLRLYGPVINIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANgvsRAAT 370
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 26343433 396 KVFSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRL 432
Cdd:cd20641 371 HPNALLSFSlGPRACIGQNFAMIEAKTVLAMILQRFSF 408
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
64-429 5.32e-10

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


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 61.31  E-value: 5.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  64 RYGPVVSFWFGR--RLVVSlgttdvlkqhfnpnktsDPfeTMLKSLLGYQSGGGSAGEDH-VRRKLYGDA---------- 130
Cdd:cd20639  10 IYGKTFLYWFGPtpRLTVA-----------------DP--ELIREILLTRADHFDRYEAHpLVRQLEGDGlvslrgekwa 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 131 -----VTASLHSNF-----PLLLQLSEELLDKW---LSYPETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEVIRFQKI 197
Cdd:cd20639  71 hhrrvITPAFHMENlkrlvPHVVKSVADMLDKWeamAEAGGEGEVDVAEWFQNLTEDVISRTAFGSSYEDGKAVFRLQAQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 198 HGTVWSEI-------GKGFLDGSldKNTTR---KKQYQEALMQL-ESTLKKIIKERKGGNFRQ--HTFIDSLTQG---KL 261
Cdd:cd20639 151 QMLLAAEAfrkvyipGYRFLPTK--KNRKSwrlDKEIRKSLLKLiERRQTAADDEKDDEDSKDllGLMISAKNARngeKM 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 262 NEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPI-TSEKIEQLSYCQQVLFETVRtakLT 340
Cdd:cd20639 229 TVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVpTKDHLPKLKTLGMILNETLR---LY 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 341 PVSARLQ-----DIegKVGPFVIPKETLVLYALGVVLQDPSTW-PLPHRFDPDRFADEPVMKVFSSLGFS----GTWECP 410
Cdd:cd20639 306 PPAVATIrrakkDV--KLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARAAKHPLAFIpfglGPRTCV 383
                       410
                ....*....|....*....
gi 26343433 411 ELRFAYMVTAVLVSVLLKR 429
Cdd:cd20639 384 GQNLAILEAKLTLAVILQR 402
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
222-447 7.53e-10

cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana cytochrome P450s (CYP86A1, CYP86A2, CYP86A4, among others), Petunia x hybrida CYP86A22, and Vicia sativa CYP94A1 and CYP94A2. They are P450-dependent fatty acid omega-hydroxylases that catalyze the omega-hydroxylation of various fatty acids. CYP86A2 acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18; CYP86A22 prefers substrates with chain lengths of C16 and C18; and CYP94A1 acts on various fatty acids from 10 to 18 carbons. They play roles in the biosynthesis of extracellular lipids, cutin synthesis, and plant defense. The CYP86A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410687 [Multi-domain]  Cd Length: 432  Bit Score: 60.68  E-value: 7.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 222 KQYQEALMQLESTLKKIIKERK-----GGNFRQHT------FIDS-LTQGKLNEQQILED-CVVFSLASCIITARLCTWT 288
Cdd:cd11064 174 KKLREAIRVIDDFVYEVISRRReelnsREEENNVRedllsrFLASeEEEGEPVSDKFLRDiVLNFILAGRDTTAAALTWF 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 289 IHFLTTTGEVQKKLCKEIDQVL------GEGPITSEKIEQLSYCQQVLFETVRtakLTPVSArlqdIEGKV--------- 353
Cdd:cd11064 254 FWLLSKNPRVEEKIREELKSKLpklttdESRVPTYEELKKLVYLHAALSESLR---LYPPVP----FDSKEavnddvlpd 326
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 354 GPFViPKETLVL---YALGVVlqdPSTW-PLPHRFDPDRFADE-PVMKVFSSLGFS----GTWECPELRFAYMVTAVLVS 424
Cdd:cd11064 327 GTFV-KKGTRIVysiYAMGRM---ESIWgEDALEFKPERWLDEdGGLRPESPYKFPafnaGPRICLGKDLAYLQMKIVAA 402
                       250       260
                ....*....|....*....|...
gi 26343433 425 VLLKRLRLLAVDRQVFEMKYELV 447
Cdd:cd11064 403 AILRRFDFKVVPGHKVEPKMSLT 425
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
281-402 9.53e-10

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: 60.42  E-value: 9.53e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 281 TARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEK-IEQLSYCQQVLFETVRtakLTP----VS-ARLQDIEGKVG 354
Cdd:cd11076 240 VAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSdVAKLPYLQAVVKETLR---LHPpgplLSwARLAIHDVTVG 316
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 26343433 355 PFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMKVFSSLG 402
Cdd:cd11076 317 GHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGADVSVLG 364
PLN00168 PLN00168
Cytochrome P450; Provisional
8-389 1.74e-09

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 59.96  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433    8 AVTFLLALVGAVLYLYPASRQASG--IPGLTPTEEKDGNLPDIVNSGSLHEFLVN-LHERYGPVVSFWFGRRLVVSLGTT 84
Cdd:PLN00168  10 AALLLLPLLLLLLGKHGGRGGKKGrrLPPGPPAVPLLGSLVWLTNSSADVEPLLRrLIARYGPVVSLRVGSRLSVFVADR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   85 DVLKQHFNPNKTS--DPFETMLKSLLGYQSGGGS-AGEDHVRRKLYGDAVTASLHSN-----FPLLLQLSEELLDKWLSY 156
Cdd:PLN00168  90 RLAHAALVERGAAlaDRPAVASSRLLGESDNTITrSSYGPVWRLLRRNLVAETLHPSrvrlfAPARAWVRRVLVDKLRRE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  157 PETQHIPLSQHMLGFALKFVTRMVLGSTFEDEQEV------IRFQKIHGT-------VWSEIGKGFLDGSLDKNTTRKKQ 223
Cdd:PLN00168 170 AEDAAAPRVVETFQYAMFCLLVLMCFGERLDEPAVraiaaaQRDWLLYVSkkmsvfaFFPAVTKHLFRGRLQKALALRRR 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  224 YQEALMQL-------ESTLKKIIKERKGGNFRQHTFIDSLTQGKLNEQ--------QILEDCVVFSLASCIITARLCTWT 288
Cdd:PLN00168 250 QKELFVPLidarreyKNHLGQGGEPPKKETTFEHSYVDTLLDIRLPEDgdraltddEIVNLCSEFLNAGTDTTSTALQWI 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  289 IHFLTTTGEVQKKLCKEIDQVLGEGP--ITSEKIEQLSYCQQVLFETVRtaKLTPVSARL-----QDIEgkVGPFVIPKE 361
Cdd:PLN00168 330 MAELVKNPSIQSKLHDEIKAKTGDDQeeVSEEDVHKMPYLKAVVLEGLR--KHPPAHFVLphkaaEDME--VGGYLIPKG 405
                        410       420
                 ....*....|....*....|....*...
gi 26343433  362 TLVLYALGVVLQDPSTWPLPHRFDPDRF 389
Cdd:PLN00168 406 ATVNFMVAEMGRDEREWERPMEFVPERF 433
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
252-392 3.17e-09

cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, reptiles, and amphibians. The hominin CYP2D subfamily consists of a functional CYP2D6 and two paralogs, CYP2D7 and CYP2D8, that are often not functional in some species. Human CYP2D6 has a high affinity for alkaloids and can detoxify them. It is also responsible for metabolizing about 25% of commonly used drugs, such as antidepressants, beta-blockers, and antiarrhythmics. The CYP2D subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 58.55  E-value: 3.17e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 252 FIDSLTQGKLNEQQILED----CVVFSL--ASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEG--PITSEKIeQL 323
Cdd:cd20663 211 FLAEMEKAKGNPESSFNDenlrLVVADLfsAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVrrPEMADQA-RM 289
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26343433 324 SYCQQVLFETVRTAKLTPVSA---RLQDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd20663 290 PYTNAVIHEVQRFGDIVPLGVphmTSRDIE--VQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDA 359
PLN02936 PLN02936
epsilon-ring hydroxylase
264-461 4.95e-09

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 58.26  E-value: 4.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  264 QQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEKIEQLSYCQQVLFETVRTAKLTPVS 343
Cdd:PLN02936 277 VQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDIKELKYLTRCINESMRLYPHPPVL 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  344 ARLQDIEGKV-GPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFA-DEPVMKV----FSSLGFS-GTWECPELRFAY 416
Cdd:PLN02936 357 IRRAQVEDVLpGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDlDGPVPNEtntdFRYIPFSgGPRKCVGDQFAL 436
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 26343433  417 MVTAVLVSVLLKRLRLLAVDRQVFEMKYELVTSAREEAWITVSKR 461
Cdd:PLN02936 437 LEAIVALAVLLQRLDLELVPDQDIVMTTGATIHTTNGLYMTVSRR 481
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
176-391 5.45e-09

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: 58.06  E-value: 5.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 176 VTRMVLGSTFEDEQEVIRFQKIHGT-VWSEIGKGFLDGSLDKNTTRKKQYQEALMQLESTLKKII----KERKGG----- 245
Cdd:cd20642 127 ISRTAFGSSYEEGKKIFELQKEQGElIIQALRKVYIPGWRFLPTKRNRRMKEIEKEIRSSLRGIInkreKAMKAGeatnd 206
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 246 ---------NFRQHTFIDSLTQGkLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPIT 316
Cdd:cd20642 207 dllgillesNHKEIKEQGNKNGG-MSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKPD 285
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26343433 317 SEKIEQLSYCQQVLFETVRtakLTPVSARLQDI---EGKVGPFVIPKETLVLYALGVVLQDPSTW-PLPHRFDPDRFAD 391
Cdd:cd20642 286 FEGLNHLKVVTMILYEVLR---LYPPVIQLTRAihkDTKLGDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFAE 361
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
217-389 7.38e-09

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: 57.72  E-value: 7.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 217 NTTRKKqYQEALMQLESTLKKIIKER----KGGNFRQHTfiDSLTQ----GKLNEQ---QILEDCVV------FSLASCI 279
Cdd:cd20676 176 NPAMKR-FKDINKRFNSFLQKIVKEHyqtfDKDNIRDIT--DSLIEhcqdKKLDENaniQLSDEKIVnivndlFGAGFDT 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 280 ITARLCtWTIHFLTTTGEVQKKLCKEIDQVLGE--GPITSEKIeQLSYCQQVLFETVRTAKLTPV-----SARLQDIEGk 352
Cdd:cd20676 253 VTTALS-WSLMYLVTYPEIQKKIQEELDEVIGRerRPRLSDRP-QLPYLEAFILETFRHSSFVPFtiphcTTRDTSLNG- 329
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 26343433 353 vgpFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRF 389
Cdd:cd20676 330 ---YYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERF 363
PLN02655 PLN02655
ent-kaurene oxidase
233-405 8.34e-09

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 57.44  E-value: 8.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  233 STLKKIIKERKGGNFRQHT---FIDSLTQGK--LNEQQILedcvvFSLASCIITARLCT-----WTIHFLTTTGEVQKKL 302
Cdd:PLN02655 225 AVMKALIKQQKKRIARGEErdcYLDFLLSEAthLTDEQLM-----MLVWEPIIEAADTTlvtteWAMYELAKNPDKQERL 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  303 CKEIDQVLGEGPITSEKIEQLSYCQQVLFETVRT---AKLTPVSARLQDIEgkVGPFVIPKETLVLYALGVVLQDPSTWP 379
Cdd:PLN02655 300 YREIREVCGDERVTEEDLPNLPYLNAVFHETLRKyspVPLLPPRFVHEDTT--LGGYDIPAGTQIAINIYGCNMDKKRWE 377
                        170       180
                 ....*....|....*....|....*...
gi 26343433  380 LPHRFDPDRFADEP--VMKVFSSLGFSG 405
Cdd:PLN02655 378 NPEEWDPERFLGEKyeSADMYKTMAFGA 405
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
66-392 1.29e-08

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: 56.84  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  66 GPVVSFWFGRRLVVSLGTTDVLKQHFNPNKT--SDPFETMLKSLLGYQS---GGGSAGED--HVRRKLYGDAV-TASLHS 137
Cdd:cd20653   1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIvlANRPRFLTGKHIGYNYttvGSAPYGDHwrNLRRITTLEIFsSHRLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 138 NFPLLLQLSEELLDKWL--SYPETQHIPLSQHMLGFALKFVTRMVLGSTF-----EDEQEVIRFQKIHGTVWSEIGKG-- 208
Cdd:cd20653  81 FSSIRRDEIRRLLKRLArdSKGGFAKVELKPLFSELTFNNIMRMVAGKRYygedvSDAEEAKLFRELVSEIFELSGAGnp 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 209 --------FLD-GSLDKNTTRKKQYQEALMQlestlkKIIKE-RKGGNFRQHTFIDSLTqgKLNEQQ--------ILEDC 270
Cdd:cd20653 161 adflpilrWFDfQGLEKRVKKLAKRRDAFLQ------GLIDEhRKNKESGKNTMIDHLL--SLQESQpeyytdeiIKGLI 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 271 VVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEK-IEQLSYCQQVLFETVRtakLTPVSARL--- 346
Cdd:cd20653 233 LVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESdLPKLPYLQNIISETLR---LYPAAPLLvph 309
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 26343433 347 ---QDIegKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd20653 310 essEDC--KIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGE 356
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
297-392 1.76e-08

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: 56.34  E-value: 1.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 297 EVQKKLCKEIDQVLGEGpiTSEKIE---QLSYCQQVLFETVRTAKLTPVS-ARLQDIEGKVGPFVIPKETLVLYALGVVL 372
Cdd:cd20668 258 EVEAKVHEEIDRVIGRN--RQPKFEdraKMPYTEAVIHEIQRFGDVIPMGlARRVTKDTKFRDFFLPKGTEVFPMLGSVL 335
                        90       100
                ....*....|....*....|
gi 26343433 373 QDPSTWPLPHRFDPDRFADE 392
Cdd:cd20668 336 KDPKFFSNPKDFNPQHFLDD 355
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
241-389 2.00e-08

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: 56.08  E-value: 2.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 241 ERKGGNFRQHTFIDSltqgKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEG-PITSEK 319
Cdd:cd20647 217 EEVKGGLLTYLLVSK----ELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRvVPTAED 292
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26343433 320 IEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKET---LVLYALGVvlqDPSTWPLPHRFDPDRF 389
Cdd:cd20647 293 VPKLPLIRALLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTqlaLCHYSTSY---DEENFPRAEEFRPERW 362
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
217-442 2.06e-08

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: 55.97  E-value: 2.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 217 NTTRKKQYQEALMQLESTLKKIIKER--KGGNFRQHTFI-DSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLT 293
Cdd:cd20645 175 NTKVWQDHTEAWDNIFKTAKHCIDKRlqRYSQGPANDFLcDIYHDNELSKKELYAAITELQIGGVETTANSLLWILYNLS 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 294 TTGEVQKKLCKEIDQVLGEGPI-TSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKETLVL---YALG 369
Cdd:cd20645 255 RNPQAQQKLLQEIQSVLPANQTpRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMinsQALG 334
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 26343433 370 VvlqDPSTWPLPHRFDPDRF-ADEPVMKVFSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVFEM 442
Cdd:cd20645 335 S---SEEYFEDGRQFKPERWlQEKHSINPFAHVPFGiGKRMCIGRRLAELQLQLALCWIIQKYQIVATDNEPVEM 406
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
281-393 2.19e-08

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: 56.11  E-value: 2.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 281 TARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGP--------ITSEKIEQLSYCQQVLFETVR------TAKLTPVSARL 346
Cdd:cd11051 201 TSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPsaaaellrEGPELLNQLPYTTAVIKETLRlfppagTARRGPPGVGL 280
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 26343433 347 QDIEGKVgpfvIPKETLVLYALGVVLQ-DPSTWPLPHRFDPDRFADEP 393
Cdd:cd11051 281 TDRDGKE----YPTDGCIVYVCHHAIHrDPEYWPRPDEFIPERWLVDE 324
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
297-392 3.33e-08

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: 55.35  E-value: 3.33e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 297 EVQKKLCKEIDQVLG--EGPITSEKIeQLSYCQQVLFETVRTAKLTPVS---ARLQDIegKVGPFVIPKETLVLYALGVV 371
Cdd:cd20665 258 EVTAKVQEEIDRVIGrhRSPCMQDRS-HMPYTDAVIHEIQRYIDLVPNNlphAVTCDT--KFRNYLIPKGTTVITSLTSV 334
                        90       100
                ....*....|....*....|.
gi 26343433 372 LQDPSTWPLPHRFDPDRFADE 392
Cdd:cd20665 335 LHDDKEFPNPEKFDPGHFLDE 355
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
251-432 3.65e-08

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: 55.59  E-value: 3.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 251 TFIDSLTQGKLN-EQQILEDCVVFSLASCII-----TARLCTWTIHFLTTTGEVQKKLCKEIDQVLGE-GPITSEKIEQL 323
Cdd:cd20661 218 AYLDEMDQNKNDpESTFSMENLIFSVGELIIagtetTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPnGMPSFEDKCKM 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 324 SYCQQVLFETVRTAKLTPVS---ARLQDieGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADE--PVMKVF 398
Cdd:cd20661 298 PYTEAVLHEVLRFCNIVPLGifhATSKD--AVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSngQFAKKE 375
                       170       180       190
                ....*....|....*....|....*....|....*
gi 26343433 399 SSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRL 432
Cdd:cd20661 376 AFVPFSlGRRHCLGEQLARMEMFLFFTALLQRFHL 410
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
238-414 3.87e-08

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: 55.45  E-value: 3.87e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 238 IIKER-----KGGNFRQHTFIDSL-----TQGK--LNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKE 305
Cdd:cd20658 198 IIDERikqwrEGKKKEEEDWLDVFitlkdENGNplLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEE 277
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 306 IDQVLGEGPITSEK-IEQLSYCQQVLFETVRtakLTPVSA------RLQDIegKVGPFVIPKETLVL---YALGvvlQDP 375
Cdd:cd20658 278 LDRVVGKERLVQESdIPNLNYVKACAREAFR---LHPVAPfnvphvAMSDT--TVGGYFIPKGSHVLlsrYGLG---RNP 349
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 26343433 376 STWPLPHRFDPDRFADEPVMKVFSSlgfsgtwecPELRF 414
Cdd:cd20658 350 KVWDDPLKFKPERHLNEDSEVTLTE---------PDLRF 379
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
252-456 6.75e-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: 54.70  E-value: 6.75e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 252 FIDSLTQGK------LNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVL-GEGP--ITSEKIEQ 322
Cdd:cd20679 225 FIDVLLLSKdedgkeLSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLkDREPeeIEWDDLAQ 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 323 LSYCQQVLFETVRTAKLTPVSAR--LQDI---EGKVgpfvIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVmKV 397
Cdd:cd20679 305 LPFLTMCIKESLRLHPPVTAISRccTQDIvlpDGRV----IPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENS-QG 379
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26343433 398 FSSLGF----SGTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVfEMKYELVTSAREEAWI 456
Cdd:cd20679 380 RSPLAFipfsAGPRNCIGQTFAMAEMKVVLALTLLRFRVLPDDKEP-RRKPELILRAEGGLWL 441
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
256-403 1.55e-07

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: 53.60  E-value: 1.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 256 LTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITS-EKIEQLSYCQQVLFETV 334
Cdd:cd20648 225 LAREKLPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSaADVARMPLLKAVVKEVL 304
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26343433 335 RTAKLTPVSARL---QDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADE-PVMKVFSSLGF 403
Cdd:cd20648 305 RLYPVIPGNARVipdRDIQ--VGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKgDTHHPYASLPF 375
PTZ00404 PTZ00404
cytochrome P450; Provisional
43-415 2.29e-07

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 53.19  E-value: 2.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433   43 GNLPdivnsgslHEFLVNLHERYGPVVSFWFGRRLVVSLGTTDVLKQHF---NPNKTSDPFETMLKSLLGYQSGGGSAGE 119
Cdd:PTZ00404  47 GNLP--------HRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFvdnFDNFSDRPKIPSIKHGTFYHGIVTSSGE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  120 DHVR-RKLYGDAVTaslHSNFPLLLQLSEELLD---KWLSYPETQHIPLSQHMlgfalkFVTRMVLGSTF-----ED--E 188
Cdd:PTZ00404 119 YWKRnREIVGKAMR---KTNLKHIYDLLDDQVDvliESMKKIESSGETFEPRY------YLTKFTMSAMFkyifnEDisF 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  189 QEVI---RFQKIHG---TVWSEIGKGFLDGSLDKNTTRKKQYQEALMQLESTLKKIIKERkggnFRQH--TF-------- 252
Cdd:PTZ00404 190 DEDIhngKLAELMGpmeQVFKDLGSGSLFDVIEITQPLYYQYLEHTDKNFKKIKKFIKEK----YHEHlkTIdpevprdl 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  253 IDSL-----TQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGP-ITSEKIEQLSYC 326
Cdd:PTZ00404 266 LDLLikeygTNTDDDILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNkVLLSDRQSTPYT 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  327 QQVLFETVRTAKLTPVS---ARLQDIEGKVGPFvIPKETLVL---YALGvvlQDPSTWPLPHRFDPDRFADEPVMKVFss 400
Cdd:PTZ00404 346 VAIIKETLRYKPVSPFGlprSTSNDIIIGGGHF-IPKDAQILinyYSLG---RNEKYFENPEQFDPSRFLNPDSNDAF-- 419
                        410
                 ....*....|....*.
gi 26343433  401 LGFS-GTWECPELRFA 415
Cdd:PTZ00404 420 MPFSiGPRNCVGQQFA 435
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
287-436 3.19e-07

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: 52.31  E-value: 3.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 287 WTIHFLTTTGEVQKKLCKEIDQVLGEG-----PITSEKIEQLSYCQQVLFETVR-------TAKLT-PVsarlqdiegKV 353
Cdd:cd20635 232 WTLAFILSHPSVYKKVMEEISSVLGKAgkdkiKISEDDLKKMPYIKRCVLEAIRlrspgaiTRKVVkPI---------KI 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 354 GPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMKVFSSLGF----SGTWECPELRFAYMVTAVLVSVLLKR 429
Cdd:cd20635 303 KNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEGFvafgGGRYQCPGRWFALMEIQMFVAMFLYK 382

                ....*..
gi 26343433 430 LRLLAVD 436
Cdd:cd20635 383 YDFTLLD 389
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
286-443 3.41e-07

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: 52.23  E-value: 3.41e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 286 TWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEK-IEQLSYCQQVLFETVRTAKLTPVSARLQDIEG-KVGPFVIPKETL 363
Cdd:cd20654 262 TWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESdIKNLVYLQAIVKETLRLYPPGPLLGPREATEDcTVGGYHVPKGTR 341
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 364 VLYALGVVLQDPSTWPLPHRFDPDRF----ADEPVMKV-FSSLGF-SGTWECPELRFAY-MVTAVLVsvllkrlRLLavd 436
Cdd:cd20654 342 LLVNVWKIQRDPNVWSDPLEFKPERFltthKDIDVRGQnFELIPFgSGRRSCPGVSFGLqVMHLTLA-------RLL--- 411

                ....*..
gi 26343433 437 rQVFEMK 443
Cdd:cd20654 412 -HGFDIK 417
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
280-458 4.10e-07

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: 51.90  E-value: 4.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 280 ITARLCTWTIHFLTTTGEVQKKLCKEIDQVLGE-GPITSEKIEQ----LSYCqqvLFETVRtakLTPV--------SARL 346
Cdd:cd20615 230 VTTGVLSWNLVFLAANPAVQEKLREEISAAREQsGYPMEDYILStdtlLAYC---VLESLR---LRPLlafsvpesSPTD 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 347 QDIEGkvgpFVIPKETLVL---YALGVvlQDPSTWPLPHRFDPDRFADEPVMKV---FSSLGFsGTWECPELRFAYMVTA 420
Cdd:cd20615 304 KIIGG----YRIPANTPVVvdtYALNI--NNPFWGPDGEAYRPERFLGISPTDLrynFWRFGF-GPRKCLGQHVADVILK 376
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 26343433 421 VLVSVLLKRLRLLAVDRQvfemkyELVTSARE-EAWITV 458
Cdd:cd20615 377 ALLAHLLEQYELKLPDQG------ENEEDTFEgLPWIWV 409
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
286-417 5.17e-07

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: 51.84  E-value: 5.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 286 TWTIHFLTTTGEVQKKLCKEIDQVL--GEGPITSEKIEQLSYCQQVLFETVRtakLTP-VSARLQDI---EGK-VGPFVI 358
Cdd:cd11061 237 SAIFYYLARNPEAYEKLRAELDSTFpsDDEIRLGPKLKSLPYLRACIDEALR---LSPpVPSGLPREtppGGLtIDGEYI 313
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26343433 359 PKETLV---LYALGvvlQDPSTWPLPHRFDPDR-FADEPVMK----VFSSlgFS-GTWECPELRFAYM 417
Cdd:cd11061 314 PGGTTVsvpIYSIH---RDERYFPDPFEFIPERwLSRPEELVrarsAFIP--FSiGPRGCIGKNLAYM 376
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
220-433 7.72e-07

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: 51.12  E-value: 7.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 220 RKKQYQEalmqlESTLKKIIKERkggnfrqH-TFIDSLTQGKLNEQQILEDCVV------FSLASCIITARLCTWTIHFL 292
Cdd:cd20678 199 RKEQLQD-----EGELEKIKKKR-------HlDFLDILLFAKDENGKSLSDEDLraevdtFMFEGHDTTASGISWILYCL 266
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 293 TTTGEVQKKLCKEIDQVLGEG-PITSEKIEQLSYCQQVLFETVRtakLTP----VSARLQdiegKVGPFV----IPKETL 363
Cdd:cd20678 267 ALHPEHQQRCREEIREILGDGdSITWEHLDQMPYTTMCIKEALR---LYPpvpgISRELS----KPVTFPdgrsLPAGIT 339
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26343433 364 V---LYALGvvlQDPSTWPLPHRFDPDRFADEPVMKV--FSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLL 433
Cdd:cd20678 340 VslsIYGLH---HNPAVWPNPEVFDPLRFSPENSSKRhsHAFLPFSaGPRNCIGQQFAMNEMKVAVALTLLRFELL 412
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
171-393 1.03e-06

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: 50.76  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 171 FALKFVTRMVLGSTF--------EDEQEVIRFQKIHGT--------VWSEIgKGFLDGSLDKNTTRKKQYQEALMQLEST 234
Cdd:cd11059 110 LAMDVVSHLLFGESFgtlllgdkDSRERELLRRLLASLapwlrwlpRYLPL-ATSRLIIGIYFRAFDEIEEWALDLCARA 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 235 LKKIIKERKGGNFRQHTFIDSLTQGK--LNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQVLG- 311
Cdd:cd11059 189 ESSLAESSDSESLTVLLLEKLKGLKKqgLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGp 268
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 312 -EGPITSEKIEQLSYCQQVLFETVRTAKLTPVSA-RLQDIEGKVGP-FVIPKETLVL---YALGvvlQDPSTWPLPHRFD 385
Cdd:cd11059 269 fRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLpRVVPEGGATIGgYYIPGGTIVStqaYSLH---RDPEVFPDPEEFD 345

                ....*...
gi 26343433 386 PDRFADEP 393
Cdd:cd11059 346 PERWLDPS 353
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
107-453 1.20e-06

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: 50.60  E-value: 1.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 107 LLGYQSGGGSAGEDHVRRKLYGDAV--TASLHSNFPLLLQLSEELLDKWLSYPEtqhiPLSQHMLGFALKF--VTRMVLG 182
Cdd:cd20636  66 LLGSNTLLNSVGELHRQRRKVLARVfsRAALESYLPRIQDVVRSEVRGWCRGPG----PVAVYTAAKSLTFriAVRILLG 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 183 STFEDEQevirFQKIHGTvWSEIGKGFLDGSLDKNTTRKKQYQEALMQLESTLKKIIKERKGGNfRQHTFIDSLT----- 257
Cdd:cd20636 142 LRLEEQQ----FTYLAKT-FEQLVENLFSLPLDVPFSGLRKGIKARDILHEYMEKAIEEKLQRQ-QAAEYCDALDymihs 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 258 ---QGK-LNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQV-LGE------GPITSEKIEQLSYC 326
Cdd:cd20636 216 areNGKeLTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVSHgLIDqcqccpGALSLEKLSRLRYL 295
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 327 QQVLFETVRTakLTPVSA----RLQDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFA---DEPVMKVFS 399
Cdd:cd20636 296 DCVVKEVLRL--LPPVSGgyrtALQTFE--LDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGverEESKSGRFN 371
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26343433 400 SLGF-SGTWECPELRFAYMVtavlvsvllkrLRLLAVdrqvfemkyELVTSAREE 453
Cdd:cd20636 372 YIPFgGGVRSCIGKELAQVI-----------LKTLAV---------ELVTTARWE 406
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
291-392 2.44e-06

cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of rats and rabbits and may have important functions for the olfactory chemosensory system. It is involved in the metabolism of sex steroids and xenobiotic compounds. In cynomolgus monkeys, CYP2G2 is a functional drug-metabolizing enzyme in nasal mucosa. In humans, two different CYP2G genes, CYP2GP1 and CYP2GP2, are pseudogenes because of loss-of-function deletions/mutations. The CYP2G subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 49.54  E-value: 2.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 291 FLTTTGEVQKKLCKEIDQVLGEG--PITSEKIeQLSYCQQVLFETVRTAKLTPVSARLQDI-EGKVGPFVIPKETLVLYA 367
Cdd:cd20670 252 LLMKYPEVEAKIHEEINQVIGPHrlPSVDDRV-KMPYTDAVIHEIQRLTDIVPLGVPHNVIrDTQFRGYLLPKGTDVFPL 330
                        90       100
                ....*....|....*....|....*
gi 26343433 368 LGVVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd20670 331 LGSVLKDPKYFRYPEAFYPQHFLDE 355
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
296-432 2.73e-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: 2.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 296 GEVQKKLCKEIDQVLGEGPITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQD--IEGkvgpFVIPKETLVLYALGVV 371
Cdd:cd20616 255 PEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRkaLEDdvIDG----YPVKKGTNIILNIGRM 330
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26343433 372 LQDPsTWPLPHRFDPDRFADEPVMKVFSSLGFsGTWECPELRFA-YMVTAVLVSvLLKRLRL 432
Cdd:cd20616 331 HRLE-FFPKPNEFTLENFEKNVPSRYFQPFGF-GPRSCVGKYIAmVMMKAILVT-LLRRFQV 389
PLN03018 PLN03018
homomethionine N-hydroxylase
238-388 2.86e-06

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 49.62  E-value: 2.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  238 IIKER------KGGNFRQHTFIDSLTQGK-------LNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCK 304
Cdd:PLN03018 274 IIDERvelwreKGGKAAVEDWLDTFITLKdqngkylVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALK 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  305 EIDQVLGEGPITSEK-IEQLSYCQQVLFETVR---TAKLTPVSARLQDIegKVGPFVIPKETLVLYALGVVLQDPSTWPL 380
Cdd:PLN03018 354 ELDEVVGKDRLVQESdIPNLNYLKACCRETFRihpSAHYVPPHVARQDT--TLGGYFIPKGSHIHVCRPGLGRNPKIWKD 431

                 ....*...
gi 26343433  381 PHRFDPDR 388
Cdd:PLN03018 432 PLVYEPER 439
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
281-392 3.72e-06

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: 49.17  E-value: 3.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 281 TARLcTWTIHFLTTTGEVQKKLCKEIDQVLG--EGPITSEKIEQLSYCQQVLFETVR---TAKLTP--VSARLQDIEGkv 353
Cdd:cd11082 237 TSSL-VWALQLLADHPDVLAKVREEQARLRPndEPPLTLDLLEEMKYTRQVVKEVLRyrpPAPMVPhiAKKDFPLTED-- 313
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 26343433 354 gpFVIPKETLVLyalgvvlqdPSTW-------PLPHRFDPDRFADE 392
Cdd:cd11082 314 --YTVPKGTIVI---------PSIYdscfqgfPEPDKFDPDRFSPE 348
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
231-391 5.13e-06

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: 48.59  E-value: 5.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 231 LESTLKKIIKERKGGNFRQhTFIDSLTQGK------LNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCK 304
Cdd:cd20614 169 IDARLSQLVATARANGART-GLVAALIRARddngagLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCD 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 305 EIdQVLGEGPITSEKIEQLSYCQQVLFETVRTAKLTPVSAR--LQDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPH 382
Cdd:cd20614 248 EA-AAAGDVPRTPAELRRFPLAEALFRETLRLHPPVPFVFRrvLEEIE--LGGRRIPAGTHLGIPLLLFSRDPELYPDPD 324

                ....*....
gi 26343433 383 RFDPDRFAD 391
Cdd:cd20614 325 RFRPERWLG 333
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
321-436 6.99e-06

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: 48.07  E-value: 6.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 321 EQLSYCQQVLFeTVRTAkltpvsarLQDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRfadepvmKVFSS 400
Cdd:cd20629 242 EGLRWEPPVAS-VPRMA--------LRDVE--LDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR-------KPKPH 303
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 26343433 401 LGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLAVD 436
Cdd:cd20629 304 LVFGgGAHRCLGEHLARVELREALNALLDRLPNLRLD 340
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
252-393 7.30e-06

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: 47.96  E-value: 7.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 252 FIDSLTQGK-----LNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEI-DQVLGEGPITSEKIEQLSY 325
Cdd:cd11058 199 FMSYILRNKdekkgLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIrSAFSSEDDITLDSLAQLPY 278
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26343433 326 CQQVLFETVRtakLTP-VSARLQ--------DIEGKvgpFViPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEP 393
Cdd:cd11058 279 LNAVIQEALR---LYPpVPAGLPrvvpaggaTIDGQ---FV-PGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDP 348
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
297-392 9.56e-06

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: 47.83  E-value: 9.56e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 297 EVQKKLCKEIDQVLGEGPI-TSEKIEQLSYCQQVLFETVRTAKLTPVS---ARLQDIEGKvgPFVIPKETLVLYALGVVL 372
Cdd:cd20669 258 KVAARVQEEIDRVVGRNRLpTLEDRARMPYTDAVIHEIQRFADIIPMSlphAVTRDTNFR--GFLIPKGTDVIPLLNSVH 335
                        90       100
                ....*....|....*....|
gi 26343433 373 QDPSTWPLPHRFDPDRFADE 392
Cdd:cd20669 336 YDPTQFKDPQEFNPEHFLDD 355
PLN02183 PLN02183
ferulate 5-hydroxylase
287-410 1.19e-05

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 47.54  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  287 WTIHFLTTTGEVQKKLCKEIDQVLG-EGPITSEKIEQLSYCQQVLFETVRTAKLTPVSARLQDIEGKVGPFVIPKETLVL 365
Cdd:PLN02183 326 WAMAELMKSPEDLKRVQQELADVVGlNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVM 405
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 26343433  366 ---YALGvvlQDPSTWPLPHRFDPDRF--ADEPVMK--VFSSLGF-SGTWECP 410
Cdd:PLN02183 406 inaWAIG---RDKNSWEDPDTFKPSRFlkPGVPDFKgsHFEFIPFgSGRRSCP 455
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
287-397 1.53e-05

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 47.15  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  287 WTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEK-IEQLSYCQQVLFETVRTAKLTPVS-ARLQDIEGKVGPFVIPKETLV 364
Cdd:PLN00110 311 WSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESdLPKLPYLQAICKESFRKHPSTPLNlPRVSTQACEVNGYYIPKNTRL 390
                         90       100       110
                 ....*....|....*....|....*....|...
gi 26343433  365 LYALGVVLQDPSTWPLPHRFDPDRFADEPVMKV 397
Cdd:PLN00110 391 SVNIWAIGRDPDVWENPEEFRPERFLSEKNAKI 423
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
275-436 1.65e-05

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: 46.87  E-value: 1.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 275 LASCIitARLCTwtihfltTTGEVQKKLCKEIDQVLGE-GPITSEKIEQLSYCQQVLFETVRTAklTPVS-----ARlQD 348
Cdd:cd11071 245 LPSLL--ARLGL-------AGEELHARLAEEIRSALGSeGGLTLAALEKMPLLKSVVYETLRLH--PPVPlqygrAR-KD 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 349 --IEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVmKVFSSLGFSG---TWE-------CPELRFAY 416
Cdd:cd11071 313 fvIESHDASYKIKKGELLVGYQPLATRDPKVFDNPDEFVPDRFMGEEG-KLLKHLIWSNgpeTEEptpdnkqCPGKDLVV 391
                       170       180
                ....*....|....*....|
gi 26343433 417 MVTAVLVSVLLKRLRLLAVD 436
Cdd:cd11071 392 LLARLFVAELFLRYDTFTIE 411
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
298-391 1.79e-05

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


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 47.08  E-value: 1.79e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 298 VQKKLCKEIDQVLG-EGPITSEKIEQLSYCQQVLFETVRTAKLTPVSAR---LQDIEGKvgPFVIPKETLVLYALGVVLQ 373
Cdd:cd20672 259 VAEKVQKEIDQVIGsHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPhrvTKDTLFR--GYLLPKNTEVYPILSSALH 336
                        90
                ....*....|....*...
gi 26343433 374 DPSTWPLPHRFDPDRFAD 391
Cdd:cd20672 337 DPQYFEQPDTFNPDHFLD 354
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
279-392 3.80e-05

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


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 45.86  E-value: 3.80e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 279 IITARLctWTIHFLTTTGEVQKKLCKEIDQVLGEGPITS-EKIEQLSYCQQVLFETVRTAKLTPVS-ARLQDIEGKVGPF 356
Cdd:cd20677 252 ISTALQ--WSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRfEDRKSLHYTEAFINEVFRHSSFVPFTiPHCTTADTTLNGY 329
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26343433 357 VIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADE 392
Cdd:cd20677 330 FIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDE 365
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
281-429 4.10e-05

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: 45.82  E-value: 4.10e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 281 TARLCTWTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEKI---EQLSYC---QQVLFETVRTAkLTPVSARL--QDIEGk 352
Cdd:cd11040 239 TIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILdltDLLTSCpllDSTYLETLRLH-SSSTSVRLvtEDTVL- 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 353 VGPFVIPKETLVLYALGVVLQDPSTW-PLPHRFDPDRFADEP-------VMKVFSSLGfSGTWECPELRFAYMVTAVLVS 424
Cdd:cd11040 317 GGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDgdkkgrgLPGAFRPFG-GGASLCPGRHFAKNEILAFVA 395

                ....*
gi 26343433 425 VLLKR 429
Cdd:cd11040 396 LLLSR 400
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
232-447 4.88e-05

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: 45.60  E-value: 4.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 232 ESTLKKIIKERKGGNFRQHTFI--DSLTQGKLNEQQILEDCVVFSLASCIITARLCTWTIHFLTTTGEVQKKLCKEIDQV 309
Cdd:cd20644 197 DNCIQKIYQELAFGRPQHYTGIvaELLLQAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAA 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 310 LGEGPITSEKIEQ-LSYCQQVLFETVRtakLTPVSARLQDIEGK---VGPFVIPKETLV---LYALGvvlQDPSTWPLPH 382
Cdd:cd20644 277 AAQISEHPQKALTeLPLLKAALKETLR---LYPVGITVQRVPSSdlvLQNYHIPAGTLVqvfLYSLG---RSAALFPRPE 350
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26343433 383 RFDPDRF-ADEPVMKVFSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRLLAVDRQVFEMKYELV 447
Cdd:cd20644 351 RYDPQRWlDIRGSGRNFKHLAFGfGMRQCLGRRLAEAEMLLLLMHVLKNFLVETLSQEDIKTVYSFI 417
PLN02971 PLN02971
tryptophan N-hydroxylase
287-392 5.31e-05

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 45.41  E-value: 5.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  287 WTIHFLTTTGEVQKKLCKEIDQVLGEGPITSEK-IEQLSYCQQVLFETVRtakLTPVSA------RLQDIegKVGPFVIP 359
Cdd:PLN02971 349 WAMAEMINKPEILHKAMEEIDRVVGKERFVQESdIPKLNYVKAIIREAFR---LHPVAAfnlphvALSDT--TVAGYHIP 423
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 26343433  360 KETLVL---YALGvvlQDPSTWPLPHRFDPDRFADE 392
Cdd:PLN02971 424 KGSQVLlsrYGLG---RNPKVWSDPLSFKPERHLNE 456
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
170-430 7.54e-05

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 45.20  E-value: 7.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  170 GFALKFVTRMVLGSTF-----EDEQEVIRFQKIHGTVWSEIGKGFLD------GSLDKNTTRKKQYqEALMQLESTLKKI 238
Cdd:PLN03112 178 AFSMNNVTRMLLGKQYfgaesAGPKEAMEFMHITHELFRLLGVIYLGdylpawRWLDPYGCEKKMR-EVEKRVDEFHDKI 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  239 IKER------KGGNFRQHTFIDSL-TQGKLNEQQILEDCVVFSLASCIITARLCT------WTIHFLTTTGEVQKKLCKE 305
Cdd:PLN03112 257 IDEHrrarsgKLPGGKDMDFVDVLlSLPGENGKEHMDDVEIKALMQDMIAAATDTsavtneWAMAEVIKNPRVLRKIQEE 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  306 IDQVLGEGPITSEK-IEQLSYCQQVLFETVRTAKLTPV-----SARLQDIEGkvgpFVIPKETLVL---YALGvvlQDPS 376
Cdd:PLN03112 337 LDSVVGRNRMVQESdLVHLNYLRCVVRETFRMHPAGPFlipheSLRATTING----YYIPAKTRVFintHGLG---RNTK 409
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26343433  377 TWPLPHRFDPDRF--ADEPVMKV-----FSSLGFS-GTWECPelrfAYMVTAVLVSVLLKRL 430
Cdd:PLN03112 410 IWDDVEEFRPERHwpAEGSRVEIshgpdFKILPFSaGKRKCP----GAPLGVTMVLMALARL 467
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
56-392 8.45e-05

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


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 44.84  E-value: 8.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  56 EFLVNLHERYGPVV-SFWFGRRLVVSLGTTDVLKQHFNPN---KTSDPFETmlKSLLGYQSGGGSAGEDHV-RRKLYGDA 130
Cdd:cd20637  12 GFQSSRREKYGNVFkTHLLGRPLIRVTGAENVRKILMGEHslvSTEWPRST--RMLLGPNSLVNSIGDIHRhKRKVFSKL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 131 VT-ASLHSNFPLLLQLSEELLDKWLSYPETQHIPLSQHMLGFalKFVTRMVLGSTFEDEQEVIRFQkihgtVWSEIGKGF 209
Cdd:cd20637  90 FShEALESYLPKIQQVIQDTLRVWSSNPEPINVYQEAQKLTF--RMAIRVLLGFRVSEEELSHLFS-----VFQQFVENV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 210 LDGSLDKNTTRKKQYQEALMQLESTLKKIIKERKGGNfRQHTFIDSL--------TQGK-LNEQQILEDCVVFSLASCII 280
Cdd:cd20637 163 FSLPLDLPFSGYRRGIRARDSLQKSLEKAIREKLQGT-QGKDYADALdiliesakEHGKeLTMQELKDSTIELIFAAFAT 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 281 TARLCTWTIHFLTTTGEVQKKLCKEI-------DQVLGEGPITSEKIEQLSYCQQVLFETVRTakLTPVSA----RLQDI 349
Cdd:cd20637 242 TASASTSLIMQLLKHPGVLEKLREELrsngilhNGCLCEGTLRLDTISSLKYLDCVIKEVLRL--FTPVSGgyrtALQTF 319
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 26343433 350 EgkVGPFVIPKETLVLYAL------GVVLQDPSTwplphrFDPDRFADE 392
Cdd:cd20637 320 E--LDGFQIPKGWSVLYSIrdthdtAPVFKDVDA------FDPDRFGQE 360
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
346-436 6.60e-04

cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces coelicolor CYP158A1 and CYP158A2, Streptomyces natalensis PimD (also known as CYP107E), Mycobacterium tuberculosis CYP121, and Micromonospora griseorubida MycG (also known as CYP107B). CYP158A1 and CYP158A2 catalyze an unusual oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments; CYP158A2 produces three isomers of biflaviolin and one triflaviolin while CYP158A1 produces only two isomers of biflaviolin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. CYP121 is essential for the viability of M. tuberculosis and is a novel drug target for the inhibition of mycobacterial growth. MycG catalyzes both hydroxylation and epoxidation reactions in the biosynthesis of the 16-membered ring macrolide antibiotic mycinamicin II. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 41.78  E-value: 6.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 346 LQDIEgkVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRfADEPvmkvfsSLGFS-GTWECPELRFAYMVTAVLVS 424
Cdd:cd11031 274 TEDVE--LGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDR-EPNP------HLAFGhGPHHCLGAPLARLELQVALG 344
                        90
                ....*....|....*
gi 26343433 425 VLLKR---LRlLAVD 436
Cdd:cd11031 345 ALLRRlpgLR-LAVP 358
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
358-394 1.98e-03

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: 40.21  E-value: 1.98e-03
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 26343433 358 IPKETLVLyaLGV--VLQDPSTWPLPHRFDPDRFADEPV 394
Cdd:cd11067 297 FPKGQRVL--LDLygTNHDPRLWEDPDRFRPERFLGWEG 333
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
229-432 4.44e-03

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: 39.31  E-value: 4.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 229 MQLESTLKKIIKE--RKGGNFRQHTFIDS--LTQGKLNEQQIlEDCVVFSLASCIITARLCT-WTIHFLTTTGEVQKKLC 303
Cdd:cd20643 194 NHADKCIQNIYRDlrQKGKNEHEYPGILAnlLLQDKLPIEDI-KASVTELMAGGVDTTSMTLqWTLYELARNPNVQEMLR 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 304 KEI--DQVLGEGPItSEKIEQLSYCQQVLFETVRtakLTPVSARLQ-----DIegKVGPFVIPKETLV---LYALGvvlQ 373
Cdd:cd20643 273 AEVlaARQEAQGDM-VKMLKSVPLLKAAIKETLR---LHPVAVSLQryiteDL--VLQNYHIPAGTLVqvgLYAMG---R 343
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 374 DPSTWPLPHRFDPDRFAdEPVMKVFSSLGFS-GTWECPELRFAYMVTAVLVSVLLKRLRL 432
Cdd:cd20643 344 DPTVFPKPEKYDPERWL-SKDITHFRNLGFGfGPRQCLGRRIAETEMQLFLIHMLENFKI 402
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
217-335 4.81e-03

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 39.29  E-value: 4.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433  217 NTTRKKQYQEALMQLESTLKKIIKERKGGNFRQHTFIDSLTQGKLNEQQILEDCVV-FSLASCIITARLCTWTIHFLTTT 295
Cdd:PLN02426 244 NIGSERKLKEAIKLVDELAAEVIRQRRKLGFSASKDLLSRFMASINDDKYLRDIVVsFLLAGRDTVASALTSFFWLLSKH 323
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 26343433  296 GEVQKKLCKEIDQVLG--EGPITSEKIEQLSYCQQVLFETVR 335
Cdd:PLN02426 324 PEVASAIREEADRVMGpnQEAASFEEMKEMHYLHAALYESMR 365
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
327-437 6.47e-03

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: 38.86  E-value: 6.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26343433 327 QQVLFETVRTAKLTPVSARL--QD---IEGKVGPFVIPKETLVLYALGVVLQDPSTWPLPHRFDPDRFADEPVMkvfssL 401
Cdd:cd20612 241 RGYVLEALRLNPIAPGLYRRatTDttvADGGGRTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDRPLESYIH-----F 315
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 26343433 402 GFsGTWECPElrfAYMVTAVLVSVLLKRLRLLAVDR 437
Cdd:cd20612 316 GH-GPHQCLG---EEIARAALTEMLRVVLRLPNLRR 347
 
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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