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Conserved domains on  [gi|29171730|ref|NP_803882|]
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cytochrome P450 20A1 isoform 2 [Homo sapiens]

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: 814.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  65 YGPVVSFWFGRRLVVSLGTVDVLKQHINPNKTSDPFETMLKSLLRYQSG-GGSVSENHMRKKLYENGVTDSLKSNFALLL 143
Cdd:cd20627   1 YGPVASFWFGRRLVVSLGSVDLLKQHINPNKTSDPFETMLKSLLGYQSGsGGDASESHVRKKLYENGVTKALQSNFPLLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 144 KLSEELLDKWLSYPETQHVPLSQHMLGFAMKSVTQMVMGSTFEDDQEVIRFQKNHGTVWSEIGKGFLDGSLDKNMTRKKQ 223
Cdd:cd20627  81 KLSEELLDKWLSYPESQHVPLCQHMLGFAMKSVTQMVMGSTFEDDQEVIRFRKNHDAIWSEIGKGFLDGSLEKSTTRKKQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 224 YEDALMQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLY 303
Cdd:cd20627 161 YEDALMEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLY 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 304 EEINQVFGNGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHK 383
Cdd:cd20627 241 KEVDQVLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYR 320

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29171730 384 FDPDRFDDELVMKTFSSLGFSGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVTSSREEAWIT 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: 814.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  65 YGPVVSFWFGRRLVVSLGTVDVLKQHINPNKTSDPFETMLKSLLRYQSG-GGSVSENHMRKKLYENGVTDSLKSNFALLL 143
Cdd:cd20627   1 YGPVASFWFGRRLVVSLGSVDLLKQHINPNKTSDPFETMLKSLLGYQSGsGGDASESHVRKKLYENGVTKALQSNFPLLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 144 KLSEELLDKWLSYPETQHVPLSQHMLGFAMKSVTQMVMGSTFEDDQEVIRFQKNHGTVWSEIGKGFLDGSLDKNMTRKKQ 223
Cdd:cd20627  81 KLSEELLDKWLSYPESQHVPLCQHMLGFAMKSVTQMVMGSTFEDDQEVIRFRKNHDAIWSEIGKGFLDGSLEKSTTRKKQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 224 YEDALMQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLY 303
Cdd:cd20627 161 YEDALMEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLY 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 304 EEINQVFGNGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHK 383
Cdd:cd20627 241 KEVDQVLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYR 320

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29171730 384 FDPDRFDDELVMKTFSSLGFSGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVTSSREEAWIT 457
Cdd:cd20627 321 FDPDRFDDESVMKSFSLLGFSGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETKYELVTSPREEAWIT 394
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 43-446 7.72e-33

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: 129.71  E-value: 7.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730    43 GNLPDIVNSGSLHEFLVNLHERYGPVVSFWFGRRLVVSLGTVD----VLKQH-INPNKTSDPFetMLKSLLRYQSGGGSV 117
Cdd:pfam00067  11 GNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEavkeVLIKKgEEFSGRPDEP--WFATSRGPFLGKGIV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   118 SENHMRKK----LYENGVTDSLKSNF-ALLLKLSEELLDKWLSYPETQHV-PLSQHMLGFAMKSVTQMVMGSTFE--DDQ 189
Cdd:pfam00067  89 FANGPRWRqlrrFLTPTFTSFGKLSFePRVEEEARDLVEKLRKTAGEPGViDITDLLFRAALNVICSILFGERFGslEDP 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   190 EVIRFQKNHGTVWSEIGKGFLDGSLDKNMTR------KKQYEDALMQLESVLRNIIKERKgRNFSQHI-----FIDSLV- 257
Cdd:pfam00067 169 KFLELVKAVQELSSLLSSPSPQLLDLFPILKyfpgphGRKLKRARKKIKDLLDKLIEERR-ETLDSAKksprdFLDALLl 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   258 ------QGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVL 330
Cdd:pfam00067 248 akeeedGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKrSPTYDDLQNMPYLDAVI 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   331 CETVRtakLTPVSAQL------QDIegKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVM--KTFSSLG 402
Cdd:pfam00067 328 KETLR---LHPVVPLLlprevtKDT--VIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKfrKSFAFLP 402

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 29171730   403 FS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYEL 446
Cdd:pfam00067 403 FGaGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDET 447
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 151-461 7.65e-14

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: 73.00  E-value: 7.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 151 DKWlsyPETQHVPLSQHMLGFAMKSVTQMVMGSTFEDDQEVIRfqknhgtvWSEIgkgFLDGSLDKNMTRKKQYEDALMQ 230
Cdd:COG2124 123 DRL---AARGPVDLVEEFARPLPVIVICELLGVPEEDRDRLRR--------WSDA---LLDALGPLPPERRRRARRARAE 188

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 231 LESVLRNIIKERKGRnfSQHIFIDSLVQ-----GNLNDQQILedSMIFSLascII-----TAKLCTWAICFLTTSEEVQK 300
Cdd:COG2124 189 LDAYLRELIAERRAE--PGDDLLSALLAarddgERLSDEELR--DELLLL---LLaghetTANALAWALYALLRHPEQLA 261

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 301 KLYEEinqvfgngpvtPEKIEQ-----LRYCQHVLCeTVRTAKltpvsaqlQDIEgkIDRFIIPRETLVLYALGVVLQDP 375
Cdd:COG2124 262 RLRAE-----------PELLPAaveetLRLYPPVPL-LPRTAT--------EDVE--LGGVTIPAGDRVLLSLAAANRDP 319

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 376 NTWPSPHKFDPDRfddelvmKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLS-VEGQVIETKYELVTSSREE 453
Cdd:COG2124 320 RVFPDPDRFDPDR-------PPNAHLPFGgGPHRCLGAALARLEARIALATLLRRFPDLRlAPPEELRWRPSLTLRGPKS 392


                ....*...
gi 29171730 454 AWITVSKR 461
Cdd:COG2124 393 LPVRLRPR 400
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 287-438 8.87e-14

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 73.23  E-value: 8.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  287 WAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDI-EGKIDRFIIPRETLV 364
Cdd:PLN02394 315 WGIAELVNHPEIQKKLRDELDTVLGPGnQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLeDAKLGGYDIPAESKI 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  365 LYALGVVLQDPNTWPSPHKFDPDRF-----DDELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 438
Cdd:PLN02394 395 LVNAWWLANNPELWKNPEEFRPERFleeeaKVEANGNDFRFLPFgVGRRSCPGIILALPILGIVLGRLVQNFELLPPPGQ 474
 
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: 814.44  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  65 YGPVVSFWFGRRLVVSLGTVDVLKQHINPNKTSDPFETMLKSLLRYQSG-GGSVSENHMRKKLYENGVTDSLKSNFALLL 143
Cdd:cd20627   1 YGPVASFWFGRRLVVSLGSVDLLKQHINPNKTSDPFETMLKSLLGYQSGsGGDASESHVRKKLYENGVTKALQSNFPLLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 144 KLSEELLDKWLSYPETQHVPLSQHMLGFAMKSVTQMVMGSTFEDDQEVIRFQKNHGTVWSEIGKGFLDGSLDKNMTRKKQ 223
Cdd:cd20627  81 KLSEELLDKWLSYPESQHVPLCQHMLGFAMKSVTQMVMGSTFEDDQEVIRFRKNHDAIWSEIGKGFLDGSLEKSTTRKKQ 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 224 YEDALMQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLY 303
Cdd:cd20627 161 YEDALMEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLY 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 304 EEINQVFGNGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHK 383
Cdd:cd20627 241 KEVDQVLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYR 320

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29171730 384 FDPDRFDDELVMKTFSSLGFSGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVTSSREEAWIT 457
Cdd:cd20627 321 FDPDRFDDESVMKSFSLLGFSGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETKYELVTSPREEAWIT 394
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 66-448 3.18e-49

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: 172.70  E-value: 3.18e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  66 GPVVSFWFGRRLVVSLGTVDVLKQHINPNKTSDPFETMLKSLLRYQSGGG---SVSENHMR-KKLYENGVTDS-LKSNFA 140
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGlltLDGPEHRRlRRLLAPAFTPRaLAALRP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 141 LLLKLSEELLDKWLSYPETQhVPLSQHMLGFAMKSVTQMVMGSTFEDDQEviRFQKNHGTVWSEIGKGFLdgsLDKNMTR 220
Cdd:cd00302  81 VIREIARELLDRLAAGGEVG-DDVADLAQPLALDVIARLLGGPDLGEDLE--ELAELLEALLKLLGPRLL---RPLPSPR 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 221 KKQYEDALMQLESVLRNIIKERK---GRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEE 297
Cdd:cd00302 155 LRRLRRARARLRDYLEELIARRRaepADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLARHPE 234

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 298 VQKKLYEEINQVFGNGpvTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIEgkIDRFIIPRETLVLYALGVVL 372
Cdd:cd00302 235 VQERLRAEIDAVLGDG--TPEDLSKLPYLEAVVEETLR---LYPPVPLLprvatEDVE--LGGYTIPAGTLVLLSLYAAH 307

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29171730 373 QDPNTWPSPHKFDPDRFDDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVT 448
Cdd:cd00302 308 RDPEVFPDPDEFDPERFLPEREEPRYAHLPFGaGPHRCLGARLARLELKLALATLLRRFDFELVPDEELEWRPSLGT 384
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 43-446 7.72e-33

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: 129.71  E-value: 7.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730    43 GNLPDIVNSGSLHEFLVNLHERYGPVVSFWFGRRLVVSLGTVD----VLKQH-INPNKTSDPFetMLKSLLRYQSGGGSV 117
Cdd:pfam00067  11 GNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEavkeVLIKKgEEFSGRPDEP--WFATSRGPFLGKGIV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   118 SENHMRKK----LYENGVTDSLKSNF-ALLLKLSEELLDKWLSYPETQHV-PLSQHMLGFAMKSVTQMVMGSTFE--DDQ 189
Cdd:pfam00067  89 FANGPRWRqlrrFLTPTFTSFGKLSFePRVEEEARDLVEKLRKTAGEPGViDITDLLFRAALNVICSILFGERFGslEDP 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   190 EVIRFQKNHGTVWSEIGKGFLDGSLDKNMTR------KKQYEDALMQLESVLRNIIKERKgRNFSQHI-----FIDSLV- 257
Cdd:pfam00067 169 KFLELVKAVQELSSLLSSPSPQLLDLFPILKyfpgphGRKLKRARKKIKDLLDKLIEERR-ETLDSAKksprdFLDALLl 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   258 ------QGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVL 330
Cdd:pfam00067 248 akeeedGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKrSPTYDDLQNMPYLDAVI 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   331 CETVRtakLTPVSAQL------QDIegKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVM--KTFSSLG 402
Cdd:pfam00067 328 KETLR---LHPVVPLLlprevtKDT--VIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKfrKSFAFLP 402

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 29171730   403 FS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYEL 446
Cdd:pfam00067 403 FGaGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDET 447
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 221-456 1.55e-29

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: 119.55  E-value: 1.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 221 KKQYEDALMQLESVLRNIIKERK------------GRNFSQ---HIFIDSLVQ-----GNLNDQQILE--DSMIF----S 274
Cdd:cd20628 165 GKEQRKALKVLHDFTNKVIKERReelkaekrnseeDDEFGKkkrKAFLDLLLEahedgGPLTDEDIREevDTFMFaghdT 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 275 LASCIitaklcTWAICFLTTSEEVQKKLYEEINQVFGN--GPVTPEKIEQLRYCQHVLCETVRtakLTP----VSAQL-Q 347
Cdd:cd20628 245 TASAI------SFTLYLLGLHPEVQEKVYEELDEIFGDddRRPTLEDLNKMKYLERVIKETLR---LYPsvpfIGRRLtE 315

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 348 DIegKIDRFIIPRET---LVLYALGvvlQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTV 421
Cdd:cd20628 316 DI--KLDGYTIPKGTtvvISIYALH---RNPEYFPDPEKFDPDRFLPENSAKrhPYAYIPFSaGPRNCIGQKFAMLEMKT 390

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 29171730 422 LLSVLVKRLHLLSVE-GQVIETKYELVTSSREEAWI 456
Cdd:cd20628 391 LLAKILRNFRVLPVPpGEDLKLIAEIVLRSKNGIRV 426
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 151-441 3.15e-26

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: 109.98  E-value: 3.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 151 DKWLSYPETQHVPLSQHMLGFAMKSVTQMVMGSTFEDDQEVIRFQKNHGTVWSE-IGKGFLDGSLDKNMTRKKQYEDALM 229
Cdd:cd20620  90 DRWEAGARRGPVDVHAEMMRLTLRIVAKTLFGTDVEGEADEIGDALDVALEYAArRMLSPFLLPLWLPTPANRRFRRARR 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 230 QLESVLRNIIKERKGRNFSQHIFIDSLVQ-------GNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKL 302
Cdd:cd20620 170 RLDEVIYRLIAERRAAPADGGDLLSMLLAardeetgEPMSDQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARL 249

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 303 YEEINQVFGNGPVTPEKIEQLRYCQHVLCETVR---TAKLTPVSAqLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWP 379
Cdd:cd20620 250 RAEVDRVLGGRPPTAEDLPQLPYTEMVLQESLRlypPAWIIGREA-VEDDE--IGGYRIPAGSTVLISPYVTHRDPRFWP 326

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29171730 380 SPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIE 441
Cdd:cd20620 327 DPEAFDPERFTPEREAArpRYAYFPFGgGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPGQPVE 391
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 164-432 1.90e-23

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: 101.91  E-value: 1.90e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 164 LSQHMLGFAMKSVTQMVMGSTFEDDQEVI-RFQKNHGTVWSEIGKGFLDGSLDKNMTRK-----KQYEDALMQLESVLRN 237
Cdd:cd11057 100 ILPDLSRCTLEMICQTTLGSDVNDESDGNeEYLESYERLFELIAKRVLNPWLHPEFIYRltgdyKEEQKARKILRAFSEK 179

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 238 IIKERKGR---------------NFSQHIFIDSLVQ-----GNLNDQQILE--DSMIFslASCIITAKLCTWAICFLTTS 295
Cdd:cd11057 180 IIEKKLQEvelesnldseedeenGRKPQIFIDQLLElarngEEFTDEEIMDeiDTMIF--AGNDTSATTVAYTLLLLAMH 257

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 296 EEVQKKLYEEINQVFGNG--PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQ--LQDIEgkIDR-FIIPRETLVLYALGV 370
Cdd:cd11057 258 PEVQEKVYEEIMEVFPDDgqFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRetTADIQ--LSNgVVIPKGTTIVIDIFN 335

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29171730 371 VLQDPNTW-PSPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHL 432
Cdd:cd11057 336 MHRRKDIWgPDADQFDPDNFLPERSAQrhPYAFIPFSaGPRNCIGWRYAMISMKIMLAKILRNYRL 401
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 66-450 2.52e-23

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: 101.52  E-value: 2.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  66 GPVVSFWFGRRLVVSLGTVDVLKQHI--NPNKTSDPFETmlKSLLRYQSGGGSVSEN-------------HMRKklyeNG 130
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEIIKEAFvkNGDNFSDRPLL--PSFEIISGGKGILFSNgdywkelrrfalsSLTK----TK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 131 VTDSLKSNFALLLKLSEELLDKWLSypETQHVPLSQHMLGFAMKSVTQMVMGSTF--EDDQEVIRFQKNHGTVWSEIGKG 208
Cdd:cd20617  75 LKKKMEELIEEEVNKLIESLKKHSK--SGEPFDPRPYFKKFVLNIINQFLFGKRFpdEDDGEFLKLVKPIEEIFKELGSG 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 209 ----FLDGSLDKNMTRKKQYEDALMQLESVLRNIIKERK-------GRNFSQHIFIDSLVQGNlnDQQILEDSMIFSLAS 277
Cdd:cd20617 153 npsdFIPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLktidpnnPRDLIDDELLLLLKEGD--SGLFDDDSIISTCLD 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 278 CII-----TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQD 348
Cdd:cd20617 231 LFLagtdtTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDrRVTLSDRSKLPYLNAVIKEVLRLRPILPLGlprVTTED 310

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 349 IEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF-DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVL 426
Cdd:cd20617 311 TE--IGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFlENDGNKLSEQFIPFGiGKRNCVGENLARDELFLFFANL 388

                       410       420
                ....*....|....*....|....*
gi 29171730 427 VKRLHLLSVEGQVI-ETKYELVTSS 450
Cdd:cd20617 389 LLNFKFKSSDGLPIdEKEVFGLTLK 413
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 226-451 3.97e-23

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: 101.12  E-value: 3.97e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 226 DALMQLESVLRNIIKERKGRNFSQH-----IFIDSLVQGN------LNDQQILEDSMIFSLASCIITAKLCTWAICFLTT 294
Cdd:cd11055 176 KSFSFLEDVVKKIIEQRRKNKSSRRkdllqLMLDAQDSDEdvskkkLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLAT 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 295 SEEVQKKLYEEINQVFGN-GPVTPEKIEQLRYCQHVLCETVRtakL-TPVSAQ----LQDIEgkIDRFIIPRETLVL--- 365
Cdd:cd11055 256 NPDVQEKLIEEIDEVLPDdGSPTYDTVSKLKYLDMVINETLR---LyPPAFFIsrecKEDCT--INGVFIPKGVDVVipv 330

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 366 YALGvvlQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEgqviET 442
Cdd:cd11055 331 YAIH---HDPEFWPDPEKFDPERFSPENKAKrhPYAYLPFgAGPRNCIGMRFALLEVKLALVKILQKFRFVPCK----ET 403


                ....*....
gi 29171730 443 KYELVTSSR 451
Cdd:cd11055 404 EIPLKLVGG 412
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 221-445 9.54e-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: 99.92  E-value: 9.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 221 KKQYEDALMqleSVLRNIIKERKGRNFSQHIFIDSLVQ-------------GNLNDQQILEDSMIFSLASCIITAKLCTW 287
Cdd:cd11056 175 PKEVEDFFR---KLVRDTIEYREKNNIVRNDFIDLLLElkkkgkieddkseKELTDEELAAQAFVFFLAGFETSSSTLSF 251

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 288 AICFLTTSEEVQKKLYEEINQVF--GNGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIEGKIDRFIIPR 360
Cdd:cd11056 252 ALYELAKNPEIQEKLREEIDEVLekHGGELTYEALQEMKYLDQVVNETLR---KYPPLPFLdrvctKDYTLPGTDVVIEK 328

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 361 ETLVL---YALGvvlQDPNTWPSPHKFDPDRFDDELV--MKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLS 434
Cdd:cd11056 329 GTPVIipvYALH---HDPKYYPEPEKFDPERFSPENKkkRHPYTYLPFgDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEP 405

                       250
                ....*....|.
gi 29171730 435 VEGQVIETKYE 445
Cdd:cd11056 406 SSKTKIPLKLS 416
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 222-436 9.82e-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: 96.95  E-value: 9.82e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 222 KQYEDALMQLESVLRNIIKERKG-RNFSQHI-----------------FIDSLVQ-----GNLNDQQILEDSMIFSLASC 278
Cdd:cd20660 166 REHKKCLKILHGFTNKVIQERKAeLQKSLEEeeeddedadigkrkrlaFLDLLLEaseegTKLSDEDIREEVDTFMFEGH 245

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 279 IITAKLCTWAICFLTTSEEVQKKLYEEINQVFG--NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRF 356
Cdd:cd20660 246 DTTAAAINWALYLIGSHPEVQEKVHEELDRIFGdsDRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGY 325

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 357 IIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLL 433
Cdd:cd20660 326 TIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGrhPYAYIPFSaGPRNCIGQKFALMEEKVVLSSILRNFRIE 405


                ...
gi 29171730 434 SVE 436
Cdd:cd20660 406 SVQ 408
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 226-449 1.17e-20

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: 93.82  E-value: 1.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 226 DALMQLESVLRNIIKERKGRNFSQ-HIFIDSLVQG------NLNDQQILedSMIFSL------ASCIITAklctWAICFL 292
Cdd:cd11042 166 RARAKLKEIFSEIIQKRRKSPDKDeDDMLQTLMDAkykdgrPLTDDEIA--GLLIALlfagqhTSSATSA----WTGLEL 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 293 TTSEEVQKKLYEEINQVFG--NGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIEGKIDRFIIPRETLVL 365
Cdd:cd11042 240 LRNPEHLEALREEQKEVLGdgDDPLTYDVLKEMPLLHACIKETLR---LHPPIHSLmrkarKPFEVEGGGYVIPKGHIVL 316

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 366 YALGVVLQDPNTWPSPHKFDPDRFDD---ELVMKTFSS-LGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVI 440
Cdd:cd11042 317 ASPAVSHRDPEIFKNPDEFDPERFLKgraEDSKGGKFAyLPFgAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSPFP 396


                ....*....
gi 29171730 441 ETKYELVTS 449
Cdd:cd11042 397 EPDYTTMVV 405
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 233-439 1.33e-20

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: 93.81  E-value: 1.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 233 SVLRNIIKERKGRNFSQHI--FIDSLVQG-------NLNDQQILEDSMIFSLASCIITAKLCT------WAICFLTTSEE 297
Cdd:cd11027 182 EILRKKLEEHKETFDPGNIrdLTDALIKAkkeaedeGDEDSGLLTDDHLVMTISDIFGAGTETtattlrWAIAYLVNYPE 261

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 298 VQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEgkIDRFIIPRETLVLYALGVVLQ 373
Cdd:cd11027 262 VQAKLHAELDDVIGRDrLPTLSDRKRLPYLEATIAEVLRLSSVVPLAlphKTTCDTT--LRGYTIPKGTTVLVNLWALHH 339

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 374 DPNTWPSPHKFDPDRFDDE---LVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQV 439
Cdd:cd11027 340 DPKEWDDPDEFRPERFLDEngkLVPKPESFLPFSaGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEP 409
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 220-446 1.53e-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: 93.58  E-value: 1.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 220 RKKQYEDALMQLESVLRNIIKERK-----------GRNFSQ----HIfIDSLVQGNLND---QQILEDSMIFSLASCIIT 281
Cdd:cd11046 178 RQRKFLRDLKLLNDTLDDLIRKRKemrqeedielqQEDYLNeddpSL-LRFLVDMRDEDvdsKQLRDDLMTMLIAGHETT 256

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 282 AKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKID--RFII 358
Cdd:cd11046 257 AAVLTWTLYELSQNPELMAKVQAEVDAVLGDRlPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPggGVKV 336

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 359 PRETLVLYALGVVLQDPNTWPSPHKFDPDRFDD------ELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRL- 430
Cdd:cd11046 337 PAGTDIFISVYNLHRSPELWEDPEEFDPERFLDpfinppNEVIDDFAFLPFGgGPRKCLGDQFALLEATVALAMLLRRFd 416

                       250       260
                ....*....|....*....|....
gi 29171730 431 --------HLLSVEGQVIETKYEL 446
Cdd:cd11046 417 feldvgprHVGMTTGATIHTKNGL 440
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 171-429 3.81e-20

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: 92.24  E-value: 3.81e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 171 FAMKSVTQMVMGSTFEDDQEVIRfqknhgTVWSEIGKGFLDGSLDKNMTRkkqYEDALM---QLESVLRNIIKERK--GR 245
Cdd:cd11043 113 MTFELICKLLLGIDPEEVVEELR------KEFQAFLEGLLSFPLNLPGTT---FHRALKarkRIRKELKKIIEERRaeLE 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 246 NFSQHI-FIDSLVQGNLNDQQILEDSMIFSLASCII------TAKLCTWAICFLTTSEEVQKKLYEE----INQVFGNGP 314
Cdd:cd11043 184 KASPKGdLLDVLLEEKDEDGDSLTDEEILDNILTLLfaghetTSTTLTLAVKFLAENPKVLQELLEEheeiAKRKEEGEG 263

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 315 VTPEKIEQLRYCQHVLCETVRTAklTPVSA----QLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFD 390
Cdd:cd11043 264 LTWEDYKSMKYTWQVINETLRLA--PIVPGvfrkALQDVE--YKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWE 339

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 29171730 391 DELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKR 429
Cdd:cd11043 340 GKGKGVPYTFLPFgGGPRLCPGAELAKLEILVFLHHLVTR 379
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 226-442 4.54e-20

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: 91.90  E-value: 4.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 226 DALMQLESVLRNIIKERKGRNFSQHI--FIDSLVQ----GNLNDQQILEDSMIFSLASCII-----TAKLCTWAICFLTT 294
Cdd:cd20651 175 ELNQKLIEFLKEEIKEHKKTYDEDNPrdLIDAYLRemkkKEPPSSSFTDDQLVMICLDLFIagsetTSNTLGFAFLYLLL 254

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 295 SEEVQKKLYEEINQVFGNG--PVTPEKIeQLRYCQHVLCETVRTAKLTPVSAQ---LQDIegKIDRFIIPRETLVLYALG 369
Cdd:cd20651 255 NPEVQRKVQEEIDEVVGRDrlPTLDDRS-KLPYTEAVILEVLRIFTLVPIGIPhraLKDT--TLGGYRIPKDTTILASLY 331

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29171730 370 VVLQDPNTWPSPHKFDPDRF--DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIET 442
Cdd:cd20651 332 SVHMDPEYWGDPEEFRPERFldEDGKLLKDEWFLPFGaGKRRCLGESLARNELFLFFTGLLQNFTFSPPNGSLPDL 407
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 230-438 1.41e-19

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: 90.42  E-value: 1.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 230 QLESVLRNIIKERKGRNfsQHIFIDSLV--------QGN-LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQK 300
Cdd:cd11044 181 KLLARLEQAIRERQEEE--NAEAKDALGllleakdeDGEpLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLE 258

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 301 KLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRTakLTPVSA----QLQDIEgkIDRFIIPRETLVLYALGVVLQDPN 376
Cdd:cd11044 259 KLRQEQDALGLEEPLTLESLKKMPYLDQVIKEVLRL--VPPVGGgfrkVLEDFE--LGGYQIPKGWLVYYSIRDTHRDPE 334

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29171730 377 TWPSPHKFDPDRF---DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 438
Cdd:cd11044 335 LYPDPERFDPERFspaRSEDKKKPFSLIPFGgGPRECLGKEFAQLEMKILASELLRNYDWELLPNQ 400
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 261-423 3.41e-19

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: 89.40  E-value: 3.41e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 261 LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGN-GPVTPEKIEQLRYCQHVLCETVRtakL 339
Cdd:cd20650 224 LSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNkAPPTYDTVMQMEYLDMVVNETLR---L 300

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 340 TPVSAQL-----QDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF----DDELVMKTFSSLGfSGTQECP 410
Cdd:cd20650 301 FPIAGRLervckKDVE--INGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFskknKDNIDPYIYLPFG-SGPRNCI 377

                       170
                ....*....|...
gi 29171730 411 ELRFAYMVTTVLL 423
Cdd:cd20650 378 GMRFALMNMKLAL 390
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 222-438 5.48e-19

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: 88.89  E-value: 5.48e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 222 KQYEDALMQLESVLRNIIKERKgRNFSQ----HIfIDSLV------QGNLNDQQILEDSMIFSLASCIITAKLCT----- 286
Cdd:cd11028 174 QKFKELLNRLNSFILKKVKEHL-DTYDKghirDI-TDALIkaseekPEEEKPEVGLTDEHIISTVQDLFGAGFDTisttl 251

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 -WAICFLTTSEEVQKKLYEEINQVFGNGPV-TPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEgkIDRFIIPRE 361
Cdd:cd11028 252 qWSLLYMIRYPEIQEKVQAELDRVIGRERLpRLSDRPNLPYTEAFILETMRHSSFVPFTiphATTRDTT--LNGYFIPKG 329

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 362 TLVLYALGVVLQDPNTWPSPHKFDPDRF--DDELVMKTFSS--LGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVE 436
Cdd:cd11028 330 TVVFVNLWSVNHDEKLWPDPSVFRPERFldDNGLLDKTKVDkfLPFGaGRRRCLGEELARMELFLFFATLLQQCEFSVKP 409


                ..
gi 29171730 437 GQ 438
Cdd:cd11028 410 GE 411
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 219-432 1.84e-18

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: 87.38  E-value: 1.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 219 TRKKQYEDALMQLESVLRNIIKE--------RKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAIC 290
Cdd:cd11070 169 SRKRAFKDVDEFLSELLDEVEAElsadskgkQGTESVVASRLKRARRSGGLTEKELLGNLFIFFIAGHETTANTLSFALY 248

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 291 FLTTSEEVQKKLYEEINQVFGNGP---VTPEKIEQLRYCQHVLCETVR-------TAKLTPVSAQLQDIEGKidRFIIPR 360
Cdd:cd11070 249 LLAKHPEVQDWLREEIDSVLGDEPddwDYEEDFPKLPYLLAVIYETLRlyppvqlLNRKTTEPVVVITGLGQ--EIVIPK 326

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 361 ETLVLYALGVVLQDPNTW-PSPHKFDPDRFDDElVMKTFSS----------LGFS-GTQECPELRFAYMVTTVLLSVLVK 428
Cdd:cd11070 327 GTYVGYNAYATHRDPTIWgPDADEFDPERWGST-SGEIGAAtrftpargafIPFSaGPRACLGRKFALVEFVAALAELFR 405


                ....
gi 29171730 429 RLHL 432
Cdd:cd11070 406 QYEW 409
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 222-448 5.84e-18

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: 85.66  E-value: 5.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 222 KQYEDALMQLESVLRNIIKERKGRNFSQHIFID---SLVQgNLNDQQILEDSMIFSLASCII------TAKLCTWAICFL 292
Cdd:cd11054 180 KKFVKAWDTIFDIASKYVDEALEELKKKDEEDEeedSLLE-YLLSKPGLSKKEIVTMALDLLlagvdtTSNTLAFLLYHL 258

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 293 TTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIEgkIDRFIIPRETLVLY 366
Cdd:cd11054 259 AKNPEVQEKLYEEIRSVLPDGePITAEDLKKMPYLKACIKESLR---LYPVAPGNgrilpKDIV--LSGYHIPKGTLVVL 333

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 367 ALGVVLQDPNTWPSPHKFDPDRF----DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQvIE 441
Cdd:cd11054 334 SNYVMGRDEEYFPDPEEFIPERWlrddSENKNIHPFASLPFGfGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHEE-LK 412


                ....*..
gi 29171730 442 TKYELVT 448
Cdd:cd11054 413 VKTRLIL 419
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 162-427 1.59e-17

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: 84.53  E-value: 1.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 162 VPLSQHMLGFAMKSVTQMVMGSTF-----EDDQEVIRFQKnhgtVWSEIGK--GFLDGS--------LDKNMTRKKQYeD 226
Cdd:cd20618 106 VNLREHLSDLTLNNITRMLFGKRYfgeseKESEEAREFKE----LIDEAFElaGAFNIGdyipwlrwLDLQGYEKRMK-K 180

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 227 ALMQLESVLRNIIKERK------GRNFSQHIFIDSLVQgnLNDQQILEDSMIFSLASCII------TAKLCTWAICFLTT 294
Cdd:cd20618 181 LHAKLDRFLQKIIEEHRekrgesKKGGDDDDDLLLLLD--LDGEGKLSDDNIKALLLDMLaagtdtSAVTIEWAMAELLR 258

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 295 SEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL------QDIegKIDRFIIPRETLVL-- 365
Cdd:cd20618 259 HPEVMRKAQEELDSVVGRErLVEESDLPKLPYLQAVVKETLR---LHPPGPLLlphestEDC--KVAGYDIPAGTRVLvn 333

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29171730 366 -YALGvvlQDPNTWPSPHKFDPDRFDDELVMKT----FSSLGF-SGTQECPELRFAYMVTTVLLSVLV 427
Cdd:cd20618 334 vWAIG---RDPKVWEDPLEFKPERFLESDIDDVkgqdFELLPFgSGRRMCPGMPLGLRMVQLTLANLL 398
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 65-430 2.52e-17

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: 83.93  E-value: 2.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  65 YGPVVSFWFGR--RLVVSlgTVDVLKQ---HINPNKTSDPFETMLKSLLryqsGGGSVSEN-----HMRKKLYENGVTDS 134
Cdd:cd11052  11 YGKNFLYWYGTdpRLYVT--EPELIKEllsKKEGYFGKSPLQPGLKKLL----GRGLVMSNgekwaKHRRIANPAFHGEK 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 135 LKSNFALLLKLSEELLDKWLSYPETQ--HVPLSQHMLGFAMKSVTQMVMGSTFEDDQEVIRFQKNHGTVWSEIG-KGFLD 211
Cdd:cd11052  85 LKGMVPAMVESVSDMLERWKKQMGEEgeEVDVFEEFKALTADIISRTAFGSSYEEGKEVFKLLRELQKICAQANrDVGIP 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 212 GSLDKNMTRKKQYEDALMQLESVLRNIIKERK-------GRNFSqHIFIDSLVQGNLND--------QQILEDSMIFSLA 276
Cdd:cd11052 165 GSRFLPTKGNKKIKKLDKEIEDSLLEIIKKREdslkmgrGDDYG-DDLLGLLLEANQSDdqnknmtvQEIVDECKTFFFA 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 277 SCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQLQ-----DIeg 351
Cdd:cd11052 244 GHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPSDSLSKLKTVSMVINESLR---LYPPAVFLTrkakeDI-- 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 352 KIDRFIIPRETLVLYALGVVLQDPNTWPS-PHKFDPDRFDDELVMKTFSSLGF----SGTQECPELRFAYMVTTVLLSVL 426
Cdd:cd11052 319 KLGGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGVAKAAKHPMAFlpfgLGPRNCIGQNFATMEAKIVLAMI 398


                ....
gi 29171730 427 VKRL 430
Cdd:cd11052 399 LQRF 402
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 56-437 2.53e-17

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: 83.52  E-value: 2.53e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  56 EFLVNLHERYGPVVSFW-FGRRLVVSLG-----TVDVLKQHINPNKTS-----DPFET---MLKSLlryqsgggsvsENH 121
Cdd:cd11045   1 EFARQRYRRYGPVSWTGmLGLRVVALLGpdanqLVLRNRDKAFSSKQGwdpviGPFFHrglMLLDF-----------DEH 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 122 M--RKKLYENGVTDSLKSNFALLLKLSEELLDKWlsyPETQHVPLSQHMLGFAMKSVTQMVMGSTFEDdqEVIRFQKN-H 198
Cdd:cd11045  70 RahRRIMQQAFTRSALAGYLDRMTPGIERALARW---PTGAGFQFYPAIKELTLDLATRVFLGVDLGP--EADKVNKAfI 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 199 GTVWSEIGKGFLD--GSLDKNMTRKKQYedalmqLESVLRNIIKERKGRN----FSQHIFIDSLVQGNLNDQQILeDSMI 272
Cdd:cd11045 145 DTVRASTAIIRTPipGTRWWRGLRGRRY------LEEYFRRRIPERRAGGgddlFSALCRAEDEDGDRFSDDDIV-NHMI 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 273 FSL--ASCIITAKLCTWAIcFLTTSEEVQKKLYEEInQVFGNGPVTPEKIEQLRYCQHVLCETVRTakLTPVSA----QL 346
Cdd:cd11045 218 FLMmaAHDTTTSTLTSMAY-FLARHPEWQERLREES-LALGKGTLDYEDLGQLEVTDWVFKEALRL--VPPVPTlprrAV 293

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 347 QDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDEL----VMKtFSSLGFS-GTQECPELRFAYMVTTV 421
Cdd:cd11045 294 KDTE--VLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERaedkVHR-YAWAPFGgGAHKCIGLHFAGMEVKA 370

                       410
                ....*....|....*.
gi 29171730 422 LLSVLVKRLHLLSVEG 437
Cdd:cd11045 371 ILHQMLRRFRWWSVPG 386
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 217-456 1.29e-15

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


Pssm-ID: 410752 [Multi-domain]  Cd Length: 423  Bit Score: 78.37  E-value: 1.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 217 NMTRK-KQYEDALMQLESVLRNIIKERK---------GRNFSQHI-FIDSLVQ-----GN-LNDQQILE--DSMIF---- 273
Cdd:cd20659 162 YLTPEgRRFKKACDYVHKFAEEIIKKRRkelednkdeALSKRKYLdFLDILLTardedGKgLTDEEIRDevDTFLFaghd 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 274 SLASCIitaklcTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGK 352
Cdd:cd20659 242 TTASGI------SWTLYSLAKHPEHQQKCREEVDEVLGDRdDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPIT 315

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 353 IDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELV--MKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKR 429
Cdd:cd20659 316 IDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIkkRDPFAFIPFSaGPRNCIGQNFAMNEMKVVLARILRR 395

                       250       260
                ....*....|....*....|....*..
gi 29171730 430 LHLLSVEGQVIETKYELVTSSREEAWI 456
Cdd:cd20659 396 FELSVDPNHPVEPKPGLVLRSKNGIKL 422
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 213-389 1.31e-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: 78.45  E-value: 1.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 213 SLDKNMTRKKQYEDALMQ-LESVLRNIIKERKGR-------------NFSQHIFIDSLVQGNLNDQQILEDSMIFSLASC 278
Cdd:cd20621 163 SWKLFPTKKEKKLQKRVKeLRQFIEKIIQNRIKQikknkdeikdiiiDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGT 242

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 279 IITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGP-VTPEKIEQLRYCQHVLCETVRtakLTPVSAQL------QDIeg 351
Cdd:cd20621 243 DTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDdITFEDLQKLNYLNAFIKEVLR---LYNPAPFLfprvatQDH-- 317

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 29171730 352 KIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF 389
Cdd:cd20621 318 QIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERW 355
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 219-430 3.57e-15

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: 77.28  E-value: 3.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 219 TRKKQyEDALMQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQI-LEDSMIFSLASCIITAKLCT------WAICF 291
Cdd:cd11075 179 LRRRQ-EEVLLPLIRARRKRRASGEADKDYTDFLLLDLLDLKEEGGERkLTDEELVSLCSEFLNAGTDTtataleWAMAE 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 292 LTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVR---TAKLTPVSAQLQDIegKIDRFIIPRETLVLYA 367
Cdd:cd11075 258 LVKNPEIQEKLYEEIKEVVGdEAVVTEEDLPKMPYLKAVVLETLRrhpPGHFLLPHAVTEDT--VLGGYDIPAGAEVNFN 335

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29171730 368 LGVVLQDPNTWPSPHKFDPDRF--DDELVMKTFSSLGFS------GTQECPELRFAymvtTVLLSVLVKRL 430
Cdd:cd11075 336 VAAIGRDPKVWEDPEEFKPERFlaGGEAADIDTGSKEIKmmpfgaGRRICPGLGLA----TLHLELFVARL 402
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 160-458 4.62e-15

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: 76.91  E-value: 4.62e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 160 QHVPLSQHMLGFAMKSVTQMVMGSTFeDDQEVIRFQK-----NHGTVWSEIGKGFLDgSLDKNMTRkkQYEDALMQLESV 234
Cdd:cd11049 108 RVVDVDAEMHRLTLRVVARTLFSTDL-GPEAAAELRQalpvvLAGMLRRAVPPKFLE-RLPTPGNR--RFDRALARLREL 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 235 LRNIIKERkgRNFSQH------IFIDSLVQGN--LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEI 306
Cdd:cd11049 184 VDEIIAEY--RASGTDrddllsLLLAARDEEGrpLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAEL 261

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 307 NQVFGNGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSP 381
Cdd:cd11049 262 DAVLGGRPATFEDLPRLTYTRRVVTEALR---LYPPVWLLtrrttADVE--LGGHRLPAGTEVAFSPYALHRDPEVYPDP 336

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 382 HKFDPDRFDDE--LVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGqvietkyelvTSSREEAWITV 458
Cdd:cd11049 337 ERFDPDRWLPGraAAVPRGAFIPFGaGARKCIGDTFALTELTLALATIASRWRLRPVPG----------RPVRPRPLATL 406
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 218-448 6.03e-15

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: 76.47  E-value: 6.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 218 MTRKKQYEDALMQLesvlrniIKERKGRNFSQHIFIDSLV------QGN-LNDQQILEDSMIFSLASCIITAKLCTWAIC 290
Cdd:cd11053 176 LRARRRIDALIYAE-------IAERRAEPDAERDDILSLLlsardeDGQpLSDEELRDELMTLLFAGHETTATALAWAFY 248

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 291 FLTTSEEVQKKLYEEINQVFGNGPvtPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIEgkIDRFIIPRETLVL 365
Cdd:cd11053 249 WLHRHPEVLARLLAELDALGGDPD--PEDIAKLPYLDAVIKETLR---LYPVAPLVprrvkEPVE--LGGYTLPAGTTVA 321

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 366 YALGVVLQDPNTWPSPHKFDPDRFDDElvmkTFSS---LGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIE 441
Cdd:cd11053 322 PSIYLTHHRPDLYPDPERFRPERFLGR----KPSPyeyLPFGgGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPER 397


                ....*..
gi 29171730 442 TKYELVT 448
Cdd:cd11053 398 PVRRGVT 404
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 220-392 7.68e-15

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: 76.07  E-value: 7.68e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 220 RKKQYEDALMQLESVLRNIIKERKgRNFSQHIfiDSLVQGNLN------DQQILEDSMIFSLASCII-----TAKLCTWA 288
Cdd:cd11068 177 AKRQFREDIALMRDLVDEIIAERR-ANPDGSP--DDLLNLMLNgkdpetGEKLSDENIRYQMITFLIaghetTSGLLSFA 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 289 ICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVR---TAKLTPVSAqLQD--IEGKIDrfiIPRETL 363
Cdd:cd11068 254 LYYLLKNPEVLAKARAEVDEVLGDDPPPYEQVAKLRYIRRVLDETLRlwpTAPAFARKP-KEDtvLGGKYP---LKKGDP 329

                       170       180       190
                ....*....|....*....|....*....|
gi 29171730 364 VLYALGVVLQDPNTW-PSPHKFDPDRFDDE 392
Cdd:cd11068 330 VLVLLPALHRDPSVWgEDAEEFRPERFLPE 359
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 65-426 1.79e-14

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: 75.21  E-value: 1.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  65 YGPVVSFWFGRRLVVSLGTVD----VLKQHINP------NKTSDPFETMLKSLLRYQSGGGSVSenhMRK---------- 124
Cdd:cd20656   1 YGPIISVWIGSTLNVVVSSSElakeVLKEKDQQladrhrTRSAARFSRNGQDLIWADYGPHYVK---VRKlctlelftpk 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 125 ------KLYENGVTDSLKSNFalllklseelLDKWLSYPETQHVPLSQHMLGFAMKSVTQMVMGSTFEDDQEVIRFQknh 198
Cdd:cd20656  78 rleslrPIREDEVTAMVESIF----------NDCMSPENEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEQ--- 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 199 GTVWSEI-GKGF-LDGSLD--------------------KNMTRKKQYEDALMQLESvlrniiKERKGRNFSQHiFIDSL 256
Cdd:cd20656 145 GVEFKAIvSNGLkLGASLTmaehipwlrwmfplsekafaKHGARRDRLTKAIMEEHT------LARQKSGGGQQ-HFVAL 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 257 VqgNLNDQQILEDSMIFSLASCIITAKLCT------WAICFLTTSEEVQKKLYEEINQVFGNGPVTPE-KIEQLRYCQHV 329
Cdd:cd20656 218 L--TLKEQYDLSEDTVIGLLWDMITAGMDTtaisveWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEaDFPQLPYLQCV 295

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 330 LCETVRTAKLTPVSAQLQDIEG-KIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELV-MK--TFSSLGF-S 404
Cdd:cd20656 296 VKEALRLHPPTPLMLPHKASENvKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVdIKghDFRLLPFgA 375

                       410       420
                ....*....|....*....|...
gi 29171730 405 GTQECPELRFAY-MVTTVLLSVL 426
Cdd:cd20656 376 GRRVCPGAQLGInLVTLMLGHLL 398
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 268-444 5.55e-14

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: 73.33  E-value: 5.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 268 EDSMI-----FSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTP 341
Cdd:cd20667 223 EENMIqvvidLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASqLICYEDRKRLPYTNAVIHEVQRLSNVVS 302

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 342 VSAQLQDIEGK-IDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF---DDELVMKTfSSLGFS-GTQECPELRFAY 416
Cdd:cd20667 303 VGAVRQCVTSTtMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFldkDGNFVMNE-AFLPFSaGHRVCLGEQLAR 381

                       170       180
                ....*....|....*....|....*....
gi 29171730 417 MVTTVLLSVLVKRLHLLSVEG-QVIETKY 444
Cdd:cd20667 382 MELFIFFTTLLRTFNFQLPEGvQELNLEY 410
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 252-432 5.58e-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: 73.64  E-value: 5.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 252 FIDSLV-----QGN-LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG--PVTPEKIEQL 323
Cdd:cd20680 224 FLDMLLsvtdeEGNkLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSdrPVTMEDLKKL 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 324 RYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMK--TFSSL 401
Cdd:cd20680 304 RYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGrhPYAYI 383

                       170       180       190
                ....*....|....*....|....*....|..
gi 29171730 402 GFS-GTQECPELRFAYMVTTVLLSVLVKRLHL 432
Cdd:cd20680 384 PFSaGPRNCIGQRFALMEEKVVLSCILRHFWV 415
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 151-461 7.65e-14

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: 73.00  E-value: 7.65e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 151 DKWlsyPETQHVPLSQHMLGFAMKSVTQMVMGSTFEDDQEVIRfqknhgtvWSEIgkgFLDGSLDKNMTRKKQYEDALMQ 230
Cdd:COG2124 123 DRL---AARGPVDLVEEFARPLPVIVICELLGVPEEDRDRLRR--------WSDA---LLDALGPLPPERRRRARRARAE 188

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 231 LESVLRNIIKERKGRnfSQHIFIDSLVQ-----GNLNDQQILedSMIFSLascII-----TAKLCTWAICFLTTSEEVQK 300
Cdd:COG2124 189 LDAYLRELIAERRAE--PGDDLLSALLAarddgERLSDEELR--DELLLL---LLaghetTANALAWALYALLRHPEQLA 261

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 301 KLYEEinqvfgngpvtPEKIEQ-----LRYCQHVLCeTVRTAKltpvsaqlQDIEgkIDRFIIPRETLVLYALGVVLQDP 375
Cdd:COG2124 262 RLRAE-----------PELLPAaveetLRLYPPVPL-LPRTAT--------EDVE--LGGVTIPAGDRVLLSLAAANRDP 319

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 376 NTWPSPHKFDPDRfddelvmKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLS-VEGQVIETKYELVTSSREE 453
Cdd:COG2124 320 RVFPDPDRFDPDR-------PPNAHLPFGgGPHRCLGAALARLEARIALATLLRRFPDLRlAPPEELRWRPSLTLRGPKS 392


                ....*...
gi 29171730 454 AWITVSKR 461
Cdd:COG2124 393 LPVRLRPR 400
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 232-438 8.34e-14

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: 73.12  E-value: 8.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 232 ESVLRNIIKERKgRNFSQHI---FIDSLVQGNLN----------DQQILEDSMIFSLASCIITAKLCT------WAICFL 292
Cdd:cd20673 181 DKLLQKKLEEHK-EKFSSDSirdLLDALLQAKMNaennnagpdqDSVGLSDDHILMTVGDIFGAGVETtttvlkWIIAFL 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 293 TTSEEVQKKLYEEINQV--FGNGPVTPEKiEQLRYCQHVLCETVRtakLTPVSAQL----QDIEGKIDRFIIPRETLVLY 366
Cdd:cd20673 260 LHNPEVQKKIQEEIDQNigFSRTPTLSDR-NHLPLLEATIREVLR---IRPVAPLLiphvALQDSSIGEFTIPKGTRVVI 335

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29171730 367 ALGVVLQDPNTWPSPHKFDPDRFDDE----LVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 438
Cdd:cd20673 336 NLWALHHDEKEWDQPDQFMPERFLDPtgsqLISPSLSYLPFgAGPRVCLGEALARQELFLFMAWLLQRFDLEVPDGG 412
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 287-438 8.87e-14

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 73.23  E-value: 8.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  287 WAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDI-EGKIDRFIIPRETLV 364
Cdd:PLN02394 315 WGIAELVNHPEIQKKLRDELDTVLGPGnQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLeDAKLGGYDIPAESKI 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  365 LYALGVVLQDPNTWPSPHKFDPDRF-----DDELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 438
Cdd:PLN02394 395 LVNAWWLANNPELWKNPEEFRPERFleeeaKVEANGNDFRFLPFgVGRRSCPGIILALPILGIVLGRLVQNFELLPPPGQ 474
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 225-450 1.06e-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: 72.69  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 225 EDALMQLESVLRNIIKERK-----GRNFSQHIFIDSLVQGN-------LNDQQILEDSMIFSLASCIITAKLCTWAICFL 292
Cdd:cd11069 183 RRAKDVLRRLAREIIREKKaalleGKDDSGKDILSILLRANdfadderLSDEELIDQILTFLAAGHETTSTALTWALYLL 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 293 TTSEEVQKKLYEEINQVF---GNGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIegKIDRFIIPRETLV 364
Cdd:cd11069 263 AKHPDVQERLREEIRAALpdpPDGDLSYDDLDRLPYLNAVCRETLR---LYPPVPLTsreatKDT--VIKGVPIPKGTVV 337

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 365 LYALGVVLQDPNTW-PSPHKFDPDRFDDELV------------MKTFSslgfSGTQECPELRFAYMVTTVLLSVLVKRLH 431
Cdd:cd11069 338 LIPPAAINRSPEIWgPDAEEFNPERWLEPDGaaspggagsnyaLLTFL----HGPRSCIGKKFALAEMKVLLAALVSRFE 413

                       250
                ....*....|....*....
gi 29171730 432 LLSVEGQVIETKYELVTSS 450
Cdd:cd11069 414 FELDPDAEVERPIGIITRP 432
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 234-437 1.32e-13

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: 72.52  E-value: 1.32e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 234 VLRNIIKERKgRNFSQ---HIFIDSLVQ---------GNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKK 301
Cdd:cd20671 181 ILRTLIEARR-PTIDGnplHSYIEALIQkqeeddpkeTLFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKR 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 302 LYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPS 380
Cdd:cd20671 260 VQEEIDRVLGPGcLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWET 339

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 381 PHKFDPDRFDDE--LVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEG 437
Cdd:cd20671 340 PYQFNPNHFLDAegKFVKKEAFLPFSaGRRVCVGESLARTELFIFFTGLLQKFTFLPPPG 399
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 250-438 1.83e-13

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: 72.12  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 250 HIfIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPE-KIEQLRYCQH 328
Cdd:cd11074 219 HI-LDAQKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEpDLHKLPYLQA 297

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 329 VLCETVRTAKLTPVSAQLQDI-EGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDE-----LVMKTFSSLG 402
Cdd:cd11074 298 VVKETLRLRMAIPLLVPHMNLhDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEeskveANGNDFRYLP 377

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 29171730 403 FS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 438
Cdd:cd11074 378 FGvGRRSCPGIILALPILGITIGRLVQNFELLPPPGQ 414
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 287-438 3.34e-13

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: 71.29  E-value: 3.34e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEINQVFGnGP--VTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEgkIDRFIIPRE 361
Cdd:cd20652 256 WFLLYMALFPKEQRRIQRELDEVVG-RPdlVTLEDLSSLPYLQACISESQRIRSVVPLGiphGCTEDAV--LAGYRIPKG 332

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 362 TLVLYALGVVLQDPNTWPSPHKFDPDRF--DDELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 438
Cdd:cd20652 333 SMIIPLLWAVHMDPNLWEEPEEFRPERFldTDGKYLKPEAFIPFqTGKRMCLGDELARMILFLFTARILRKFRIALPDGQ 412
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 221-406 3.86e-13

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: 70.95  E-value: 3.86e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 221 KKQYEDALMQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLAS--CII----------TAKLCTWA 288
Cdd:cd11072 172 DRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEFPLTRDNikAIIldmflagtdtSATTLEWA 251

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 289 ICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL------QDIegKIDRFIIPRE 361
Cdd:cd11072 252 MTELIRNPRVMKKAQEEVREVVGgKGKVTEEDLEKLKYLKAVIKETLR---LHPPAPLLlprecrEDC--KINGYDIPAK 326

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 29171730 362 TLVL---YALGvvlQDPNTWPSPHKFDPDRFDDelvmktfSSLGFSGT 406
Cdd:cd11072 327 TRVIvnaWAIG---RDPKYWEDPEEFRPERFLD-------SSIDFKGQ 364
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 221-446 4.53e-13

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: 70.63  E-value: 4.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 221 KKQYEDALMQLESVLRNIIKER-----KGRNFSQ----HIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICF 291
Cdd:cd20613 181 RREVREAIKFLRETGRECIEERlealkRGEEVPNdiltHILKASEEEPDFDMEELLDDFVTFFIAGQETTANLLSFTLLE 260

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 292 LTTSEEVQKKLYEEINQVFGNGP-VTPEKIEQLRYCQHVLCETVRtakLTPVSAQLQDI---EGKIDRFIIPRETLVL-- 365
Cdd:cd20613 261 LGRHPEILKRLQAEVDEVLGSKQyVEYEDLGKLEYLSQVLKETLR---LYPPVPGTSREltkDIELGGYKIPAGTTVLvs 337

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 366 -YALGvvlQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIE 441
Cdd:cd20613 338 tYVMG---RMEEYFEDPLKFDPERFSPEAPEKipSYAYFPFSlGPRSCIGQQFAQIEAKVILAKLLQNFKFELVPGQSFG 414


                ....*
gi 29171730 442 TKYEL 446
Cdd:cd20613 415 ILEEV 419
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 287-392 5.19e-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: 70.67  E-value: 5.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIE--GkidrFIIPR 360
Cdd:cd11026 248 WALLLLMKYPHIQEKVQEEIDRVIGrNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGvphAVTRDTKfrG----YTIPK 323

                        90       100       110
                ....*....|....*....|....*....|..
gi 29171730 361 ETLVLYALGVVLQDPNTWPSPHKFDPDRFDDE 392
Cdd:cd11026 324 GTTVIPNLTSVLRDPKQWETPEEFNPGHFLDE 355
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 261-436 5.90e-13

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


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 70.64  E-value: 5.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 261 LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINqVFGNGPVTPE--KIEQLRYCQHVLCETVR--- 335
Cdd:cd20649 257 LTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVD-EFFSKHEMVDyaNVQELPYLDMVIAETLRmyp 335

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 336 -TAKLTPVSAQLQDIEGKIdrfiIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGF-SGTQECPE 411
Cdd:cd20649 336 pAFRFAREAAEDCVVLGQR----IPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRrhPFVYLPFgAGPRSCIG 411

                       170       180
                ....*....|....*....|....*
gi 29171730 412 LRFAYMVTTVLLSVLVKRLHLLSVE 436
Cdd:cd20649 412 MRLALLEIKVTLLHILRRFRFQACP 436
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 220-392 1.57e-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: 69.06  E-value: 1.57e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 220 RKKQYEDALMQLESVLRNIIKERKGRN-FSQHIFIDSLvqgnLNDQQILEDSM---------IFSLASCI-----ITAKL 284
Cdd:cd20664 169 INKLLRNTKELNDFLMETFMKHLDVLEpNDQRGFIDAF----LVKQQEEEESSdsffhddnlTCSVGNLFgagtdTTGTT 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 285 CTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQ---DIegKIDRFIIPRE 361
Cdd:cd20664 245 LRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVEHRKNMPYTDAVIHEIQRFANIVPMNLPHAttrDV--TFRGYFIPKG 322

                       170       180       190
                ....*....|....*....|....*....|.
gi 29171730 362 TLVLYALGVVLQDPNTWPSPHKFDPDRFDDE 392
Cdd:cd20664 323 TYVIPLLTSVLQDKTEWEKPEEFNPEHFLDS 353
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 287-426 2.00e-12

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: 68.71  E-value: 2.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRtakLTPVSAQL------QDIEgkIDRFIIP 359
Cdd:cd11073 253 WAMAELLRNPEKMAKARAELDEVIGKDKIVEESdISKLPYLQAVVKETLR---LHPPAPLLlprkaeEDVE--VMGYTIP 327

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29171730 360 RETLVL---YALGvvlQDPNTWPSPHKFDPDRF-DDELVMK--TFSSLGF-SGTQECPELRFAY-MVTTVLLSVL 426
Cdd:cd11073 328 KGTQVLvnvWAIG---RDPSVWEDPLEFKPERFlGSEIDFKgrDFELIPFgSGRRICPGLPLAErMVHLVLASLL 399
PLN02290 PLN02290
cytokinin trans-hydroxylase
 206-429 2.57e-12

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 68.69  E-value: 2.57e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  206 GKGFLDGSLDKNMTRKKqyedalMQLESVLRNIIKERK-----GRNFS----------QHIFIDSLVQGNLNDQQILEDS 270
Cdd:PLN02290 248 GSRFFPSKYNREIKSLK------GEVERLLMEIIQSRRdcveiGRSSSygddllgmllNEMEKKRSNGFNLNLQLIMDEC 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  271 MIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVR---TAKLTPVSAqLQ 347
Cdd:PLN02290 322 KTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVDHLSKLTLLNMVINESLRlypPATLLPRMA-FE 400

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  348 DIegKIDRFIIPRETLVLYALGVVLQDPNTW-PSPHKFDPDRFddelVMKTFSSLGF-----SGTQECPELRFAYMVTTV 421
Cdd:PLN02290 401 DI--KLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRF----AGRPFAPGRHfipfaAGPRNCIGQAFAMMEAKI 474


                 ....*...
gi 29171730  422 LLSVLVKR 429
Cdd:PLN02290 475 ILAMLISK 482
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 261-410 3.43e-12

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 68.20  E-value: 3.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  261 LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-----IEQLRYCQHVLCETVR 335
Cdd:PLN02302 283 LDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKKRPPGQKGltlkdVRKMEYLSQVIDETLR 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29171730  336 TAKLTPVSAQ--LQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVmKTFSSLGFS-GTQECP 410
Cdd:PLN02302 363 LINISLTVFReaKTDVE--VNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTP-KAGTFLPFGlGSRLCP 437
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 287-427 5.85e-12

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: 67.24  E-value: 5.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRtakLTPVSAQL--QDIEG-KIDRFIIPRET 362
Cdd:cd20655 250 WAMAELINNPEVLEKAREEIDSVVGKTRLVQESdLPNLPYLQAVVKETLR---LHPPGPLLvrESTEGcKINGYDIPEKT 326

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29171730 363 LVL---YALGvvlQDPNTWPSPHKFDPDRF--------DDELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLV 427
Cdd:cd20655 327 TLFvnvYAIM---RDPNYWEDPLEFKPERFlassrsgqELDVRGQHFKLLPFgSGRRGCPGASLAYQVVGTAIAAMV 400
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 220-436 6.28e-12

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: 66.96  E-value: 6.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 220 RKKQYEDALMQLESVLRNII---KER---------KGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTW 287
Cdd:cd11083 165 ADRALDRALVEVRALVLDIIaaaRARlaanpalaeAPETLLAMMLAEDDPDARLTDDEIYANVLTLLLAGEDTTANTLAW 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 288 AICFLTTSEEVQKKLYEEINQVFGNGPVTP--EKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDieGKIDRFIIPR 360
Cdd:cd11083 245 MLYYLASRPDVQARVREEVDAVLGGARVPPllEALDRLPYLEAVARETLR---LKPVAPLLflepnED--TVVGDIALPA 319

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 361 ETLVLYALGVVLQDPNTWPSPHKFDPDRF---DDELVMKTFSS-LGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSV 435
Cdd:cd11083 320 GTPVFLLTRAAGLDAEHFPDPEEFDPERWldgARAAEPHDPSSlLPFgAGPRLCPGRSLALMEMKLVFAMLCRNFDIELP 399


                .
gi 29171730 436 E 436
Cdd:cd11083 400 E 400
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 151-410 7.34e-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: 7.34e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 151 DKWLSYPETQHVPLSQHMLGFAMKSVTQMVMGSTFEDDQE----VIRFQKNHGTVWSEIGK--GFLDGSLDKNMTRKKQY 224
Cdd:cd11041  97 EELGSCTEWTEVNLYDTVLRIVARVSARVFVGPPLCRNEEwldlTINYTIDVFAAAAALRLfpPFLRPLVAPFLPEPRRL 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 225 EDALMQLESVLRNIIKERKGRNFS----------QHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTT 294
Cdd:cd11041 177 RRLLRRARPLIIPEIERRRKLKKGpkedkpndllQWLIEAAKGEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAA 256

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 295 SEEVQKKLYEEINQVFGN-GPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQ---LQDIeGKIDRFIIPRETLVLYALGV 370
Cdd:cd11041 257 HPEYIEPLREEIRSVLAEhGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRrkvLKDV-TLSDGLTLPKGTRIAVPAHA 335

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 29171730 371 VLQDPNTWPSPHKFDPDRF------DDELVMKTFSS-----LGFS-GTQECP 410
Cdd:cd11041 336 IHRDPDIYPDPETFDGFRFyrlreqPGQEKKHQFVStspdfLGFGhGRHACP 387
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 209-405 1.15e-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: 66.43  E-value: 1.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 209 FLDGSLDKNMTRKKQYEDalmqlesvlrniiKERKGRNfsqhIFIDSLVQgNLNDQQILEDSM--IFsLASCIITAKLCT 286
Cdd:cd11063 177 FVDPYVDKALARKEESKD-------------EESSDRY----VFLDELAK-ETRDPKELRDQLlnIL-LAGRDTTASLLS 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEINQVFGNGP-VTPEKIEQLRYCQHVLCETVRtakLTPVSAQ-----LQD--------IEGK 352
Cdd:cd11063 238 FLFYELARHPEVWAKLREEVLSLFGPEPtPTYEDLKNMKYLRAVINETLR---LYPPVPLnsrvaVRDttlprgggPDGK 314

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 29171730 353 IDRFiIPRETLVLYALGVVLQDPNTW-PSPHKFDPDRFDDeLVMKTFSSLGFSG 405
Cdd:cd11063 315 SPIF-VPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWED-LKRPGWEYLPFNG 366
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 176-452 3.31e-11

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: 64.94  E-value: 3.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 176 VTQMVMGSTF------EDDQEVIRFQKN-----HGTVWSEIGK-----GFLD-GSLDKNMtrKKQYEDalmqLESVLRNI 238
Cdd:cd20654 126 ILRMVVGKRYfggtavEDDEEAERYKKAirefmRLAGTFVVSDaipflGWLDfGGHEKAM--KRTAKE----LDSILEEW 199

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 239 IKE-RKGRNFSQ-----HIFIDSL-------VQGNLNDQQILEDSMIFS--LASCIITAKLCTWAICFLTTSEEVQKKLY 303
Cdd:cd20654 200 LEEhRQKRSSSGkskndEDDDDVMmlsiledSQISGYDADTVIKATCLEliLGGSDTTAVTLTWALSLLLNNPHVLKKAQ 279

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 304 EEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRTAKLTPVSAQLQDIEG-KIDRFIIPRETLVLYALGVVLQDPNTWPSP 381
Cdd:cd20654 280 EELDTHVGKDRWVEESdIKNLVYLQAIVKETLRLYPPGPLLGPREATEDcTVGGYHVPKGTRLLVNVWKIQRDPNVWSDP 359

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29171730 382 HKFDPDRF-----DDELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLvkrLHllsvegqvietKYELVTSSRE 452
Cdd:cd20654 360 LEFKPERFltthkDIDVRGQNFELIPFgSGRRSCPGVSFGLQVMHLTLARL---LH-----------GFDIKTPSNE 422
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 281-389 3.64e-11

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 65.22  E-value: 3.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  281 TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVS-AQLQDIEGKIDRFII 358
Cdd:PLN02687 313 TSSTVEWAIAELIRHPDILKKAQEELDAVVGRDrLVSESDLPQLTYLQAVIKETFRLHPSTPLSlPRMAAEECEINGYHI 392

                         90       100       110
                 ....*....|....*....|....*....|.
gi 29171730  359 PRETLVLYALGVVLQDPNTWPSPHKFDPDRF 389
Cdd:PLN02687 393 PKGATLLVNVWAIARDPEQWPDPLEFRPDRF 423
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 238-409 5.32e-11

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: 64.43  E-value: 5.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 238 IIKERKGRNFSQ-HIFIDSLVQGNLNDQQ----ILEDSMIFS-----LASCIITAKLCTWAICFLTTSEEVQKKLYEEIN 307
Cdd:cd20662 188 IDKHREDWNPDEpRDFIDAYLKEMAKYPDpttsFNEENLICStldlfFAGTETTSTTLRWALLYMALYPEIQEKVQAEID 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 308 QVFGNG--PVTPEKiEQLRYCQHVLCETVRTAKLTPVSAQLQ-DIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKF 384
Cdd:cd20662 268 RVIGQKrqPSLADR-ESMPYTNAVIHEVQRMGNIIPLNVPREvAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTF 346

                       170       180
                ....*....|....*....|....*..
gi 29171730 385 DPDRF-DDELVMKTFSSLGFS-GTQEC 409
Cdd:cd20662 347 NPGHFlENGQFKKREAFLPFSmGKRAC 373
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 231-417 6.15e-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: 6.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 231 LESVLRNIIKERKGR--NFSQHIFIDSLV------QGNLNDQQILEDSMIFSLASCII-----TAKLCTWAICFLTTSEE 297
Cdd:cd20666 181 ITAFLKKIIADHRETldPANPRDFIDMYLlhieeeQKNNAESSFNEDYLFYIIGDLFIagtdtTTNTLLWCLLYMSLYPE 260

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 298 VQKKLYEEINQVFGNG--PVTPEKiEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDR-FIIPRETLVLYALGVVLQD 374
Cdd:cd20666 261 VQEKVQAEIDTVIGPDraPSLTDK-AQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQgYTIPKGTVIVPNLWSVHRD 339

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 29171730 375 PNTWPSPHKFDPDRFDDE--LVMKTFSSLGFS-GTQECPELRFAYM 417
Cdd:cd20666 340 PAIWEKPDDFMPSRFLDEngQLIKKEAFIPFGiGRRVCMGEQLAKM 385
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 210-434 9.21e-11

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 63.80  E-value: 9.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  210 LDGSL-DKNMTRKKQyedalmqLESVLRNIIKERKGRNFSQHIFIDSLV--QGNLNDQQILEDSMIFSLASCIITAKLCT 286
Cdd:PLN02196 213 LPGTLfHKSMKARKE-------LAQILAKILSKRRQNGSSHNDLLGSFMgdKEGLTDEQIADNIIGVIFAARDTTASVLT 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  287 WAICFLTTSEEVQKKLYEEINQVFGNGP----VTPEKIEQLRYCQHVLCETVRTAKLTPVSAQ--LQDIEgkIDRFIIPR 360
Cdd:PLN02196 286 WILKYLAENPSVLEAVTEEQMAIRKDKEegesLTWEDTKKMPLTSRVIQETLRVASILSFTFReaVEDVE--YEGYLIPK 363

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29171730  361 ETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMKTFSSLGfSGTQECPELRFAYMVTTVLLSVLVK--RLHLLS 434
Cdd:PLN02196 364 GWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAPKPNTFMPFG-NGTHSCPGNELAKLEISVLIHHLTTkyRWSIVG 438
PLN02655 PLN02655
ent-kaurene oxidase
 222-392 9.29e-11

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 63.61  E-value: 9.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  222 KQYEDALMQLE----SVLRNIIKERKGRNFS---QHIFIDSLVQGN--LNDQQI---LEDSMIFSLASCIITAKlctWAI 289
Cdd:PLN02655 210 KSFETRVQTTEfrrtAVMKALIKQQKKRIARgeeRDCYLDFLLSEAthLTDEQLmmlVWEPIIEAADTTLVTTE---WAM 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  290 CFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRT---AKLTPVSAQLQDIEgkIDRFIIPRETLVLY 366
Cdd:PLN02655 287 YELAKNPDKQERLYREIREVCGDERVTEEDLPNLPYLNAVFHETLRKyspVPLLPPRFVHEDTT--LGGYDIPAGTQIAI 364

                        170       180
                 ....*....|....*....|....*.
gi 29171730  367 ALGVVLQDPNTWPSPHKFDPDRFDDE 392
Cdd:PLN02655 365 NIYGCNMDKKRWENPEEWDPERFLGE 390
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 231-447 1.05e-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: 63.38  E-value: 1.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 231 LESVLRNIIKERKGRNF----SQHI---FIDS-LVQGNLNDQQILEDSMI-FSLASCIITAKLCTWAICFLTTSEEVQKK 301
Cdd:cd11064 187 VYEVISRRREELNSREEennvREDLlsrFLASeEEEGEPVSDKFLRDIVLnFILAGRDTTAAALTWFFWLLSKNPRVEEK 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 302 LYEEINQV----FGNGPV--TPEKIEQLRYCQHVLCETVRtakLTPVSAqlqdIEGKI--------DRFIIPRETLVL-- 365
Cdd:cd11064 267 IREELKSKlpklTTDESRvpTYEELKKLVYLHAALSESLR---LYPPVP----FDSKEavnddvlpDGTFVKKGTRIVys 339

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 366 -YALGVVlqdPNTW-PSPHKFDPDRF-DDELVMKTFSSLGFS----GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 438
Cdd:cd11064 340 iYAMGRM---ESIWgEDALEFKPERWlDEDGGLRPESPYKFPafnaGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGH 416


                ....*....
gi 29171730 439 VIETKYELV 447
Cdd:cd11064 417 KVEPKMSLT 425
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 232-410 1.25e-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: 63.12  E-value: 1.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 232 ESVLRNIIKERK--GRNFSQHIFIDSLVQGNLNDQQILEDS-MIFSLASCII-----TAKLCTWAICFLTTSEEVQKKLY 303
Cdd:cd11076 183 NTFVGKIIEEHRakRSNRARDDEDDVDVLLSLQGEEKLSDSdMIAVLWEMIFrgtdtVAILTEWIMARMVLHPDIQSKAQ 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 304 EEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRtakLTP----VS-AQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNT 377
Cdd:cd11076 263 AEIDAAVGgSRRVADSDVAKLPYLQAVVKETLR---LHPpgplLSwARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHV 339

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 29171730 378 WPSPHKFDPDRFDDELVMKTFSSLG-------F-SGTQECP 410
Cdd:cd11076 340 WEDPLEFKPERFVAAEGGADVSVLGsdlrlapFgAGRRVCP 380
PLN02966 PLN02966
cytochrome P450 83A1
 6-415 1.82e-10

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 62.84  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730    6 IFAVTFLLALVGAVLYLYPASRQAAGIPGITPteekdgnLPDIVNSGSLHE-----FLVNLHERYGPVVSFWFGRRLVVS 80
Cdd:PLN02966   5 IIGVVALAAVLLFFLYQKPKTKRYKLPPGPSP-------LPVIGNLLQLQKlnpqrFFAGWAKKYGPILSYRIGSRTMVV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   81 LGTVDVLK-----QHIN----PNKTSDPF------ETMLKSLLRYQSGGGSVSENHMRKKLYENGVTDSLKSNFALLLKL 145
Cdd:PLN02966  78 ISSAELAKellktQDVNfadrPPHRGHEFisygrrDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  146 SEELLDKwlsypeTQHVPLSQHMLGFAMKSVTQMVMGSTF-EDDQEVIRFQKNHGTVWSEIGK----------GFLDGSL 214
Cdd:PLN02966 158 INKAADK------SEVVDISELMLTFTNSVVCRQAFGKKYnEDGEEMKRFIKILYGTQSVLGKiffsdffpycGFLDDLS 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  215 DKNMTRKKQYEDALMQLESVLRNIIKERKGRNFSQHIfIDsLVQGNLNDQQILEDSMIFSLASCII---------TAKLC 285
Cdd:PLN02966 232 GLTAYMKECFERQDTYIQEVVNETLDPKRVKPETESM-ID-LLMEIYKEQPFASEFTVDNVKAVILdivvagtdtAAAAV 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  286 TWAICFLTTSEEVQKKLYEEINQVF---GNGPVTPEKIEQLRYCQHVLCETVRTAKLTPV---SAQLQDIegKIDRFIIP 359
Cdd:PLN02966 310 VWGMTYLMKYPQVLKKAQAEVREYMkekGSTFVTEDDVKNLPYFRALVKETLRIEPVIPLlipRACIQDT--KIAGYDIP 387

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29171730  360 RETLVLYALGVVLQDPNTW-PSPHKFDPDRFDDELVMKTFSSLGF----SGTQECPELRFA 415
Cdd:PLN02966 388 AGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKGTDYEFipfgSGRRMCPGMRLG 448
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 216-389 1.96e-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: 62.44  E-value: 1.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 216 KNMTRKKQYEDALMQlesvlrNIIKERKGRNFSQHI---FIDSLVQGNL--NDQQILEDSMIFSLASCIITAKLCT---- 286
Cdd:cd20657 174 KKMKRLHKRFDALLT------KILEEHKATAQERKGkpdFLDFVLLENDdnGEGERLTDTNIKALLLNLFTAGTDTssst 247

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 --WAICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEG-KIDRFIIPRET 362
Cdd:cd20657 248 veWALAELIRHPDILKKAQEEMDQVIGrDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEAcEVDGYYIPKGT 327

                       170       180
                ....*....|....*....|....*..
gi 29171730 363 LVLYALGVVLQDPNTWPSPHKFDPDRF 389
Cdd:cd20657 328 RLLVNIWAIGRDPDVWENPLEFKPERF 354
PLN02738 PLN02738
carotene beta-ring hydroxylase
 260-429 2.06e-10

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 63.01  E-value: 2.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  260 NLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRTAKL 339
Cdd:PLN02738 386 DVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQ 465

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  340 TPV----SAQlQDIEGKidrFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF-----DDELVMKTFSSLGF-SGTQEC 409
Cdd:PLN02738 466 PPVlirrSLE-NDMLGG---YPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpldgpNPNETNQNFSYLPFgGGPRKC 541

                        170       180
                 ....*....|....*....|
gi 29171730  410 PELRFAYMVTTVLLSVLVKR 429
Cdd:PLN02738 542 VGDMFASFENVVATAMLVRR 561
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 209-436 2.26e-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: 62.27  E-value: 2.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 209 FLDGSLDKNMTRKKQY-EDALMQLESVLRNiiKERKGRNFSQHIFIDSLVQGNLN-----DQQILEDSMIFSLASCIITA 282
Cdd:cd11062 164 SLLKRLNPGLAVFLDFqESIAKQVDEVLRQ--VSAGDPPSIVTSLFHALLNSDLPpsektLERLADEAQTLIGAGTETTA 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 283 KLCTWAICFLTTSEEVQKKLYEEINQVF--GNGPVTPEKIEQLRYCQHVLCETVRTAklTPVSAQLQDI---EG-KIDRF 356
Cdd:cd11062 242 RTLSVATFHLLSNPEILERLREELKTAMpdPDSPPSLAELEKLPYLTAVIKEGLRLS--YGVPTRLPRVvpdEGlYYKGW 319

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 357 IIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF---DDELVMKTFsSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHL 432
Cdd:cd11062 320 VIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWlgaAEKGKLDRY-LVPFSkGSRSCLGINLAYAELYLALAALFRRFDL 398


                ....
gi 29171730 433 LSVE 436
Cdd:cd11062 399 ELYE 402
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 286-392 4.52e-10

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: 61.56  E-value: 4.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 286 TWAICFLTTSEEVQKKLYEEINQVFGNGPV-TPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEgkIDRFIIPRE 361
Cdd:cd20675 256 QWILLLLVRYPDVQARLQEELDRVVGRDRLpCIEDQPNLPYVMAFLYEAMRFSSFVPVTiphATTADTS--ILGYHIPKD 333

                        90       100       110
                ....*....|....*....|....*....|.
gi 29171730 362 TLVLYALGVVLQDPNTWPSPHKFDPDRFDDE 392
Cdd:cd20675 334 TVVFVNQWSVNHDPQKWPNPEVFDPTRFLDE 364
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 287-427 5.29e-10

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: 61.08  E-value: 5.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRtakLTPVSAQL------QDIegKIDRFIIP 359
Cdd:cd20653 249 WAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESdLPKLPYLQNIISETLR---LYPAAPLLvphessEDC--KIGGYDIP 323

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29171730 360 RETLVLYALGVVLQDPNTWPSPHKFDPDRFDDElVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLV 427
Cdd:cd20653 324 RGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGE-EREGYKLIPFgLGRRACPGAGLAQRVVGLALGSLI 391
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 222-389 6.14e-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: 61.05  E-value: 6.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 222 KQYEDALMQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCII-----TAKLCTWAICFLTTSE 296
Cdd:cd11065 175 RELRELTRRLYEGPFEAAKERMASGTATPSFVKDLLEELDKEGGLSEEEIKYLAGSLYEagsdtTASTLQTFILAMALHP 254

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 297 EVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEgkIDRFIIPRETLVLYALGVVL 372
Cdd:cd11065 255 EVQKKAQEELDRVVGPDrLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGiphALTEDDE--YEGYFIPKGTTVIPNAWAIH 332

                       170
                ....*....|....*..
gi 29171730 373 QDPNTWPSPHKFDPDRF 389
Cdd:cd11065 333 HDPEVYPDPEEFDPERY 349
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 256-429 6.42e-10

cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; Cytochrome P450 27A1 (CYP27A1, EC 1.14.15.15) is also called CYP27, cholestanetriol 26-monooxygenase, sterol 26-hydroxylase, 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase, cytochrome P-450C27/25, sterol 27-hydroxylase, or vitamin D(3) 25-hydroxylase. It catalyzes the first step in the oxidation of the side chain of sterol intermediates, the 27-hydroxylation of 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol, and the first three sterol side chain oxidations in bile acid biosynthesis via the neutral (classic) pathway. It also hydroxylates vitamin D3 at the 25-position, as well as cholesterol at positions 24 and 25. CYP27A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 60.83  E-value: 6.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 256 LVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPV-TPEKIEQLRYCQHVLCETV 334
Cdd:cd20646 224 LSSGKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIpTAEDIAKMPLLKAVIKETL 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 335 RTAKLTPVSAQL-QDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF--DDELVMKTFSSLGFS-GTQECP 410
Cdd:cd20646 304 RLYPVVPGNARViVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWlrDGGLKHHPFGSIPFGyGVRACV 383

                       170
                ....*....|....*....
gi 29171730 411 ELRFAYMVTTVLLSVLVKR 429
Cdd:cd20646 384 GRRIAELEMYLALSRLIKR 402
PLN02936 PLN02936
epsilon-ring hydroxylase
 264-461 7.08e-10

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 60.96  E-value: 7.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  264 QQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRTAKLTPV- 342
Cdd:PLN02936 277 VQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDIKELKYLTRCINESMRLYPHPPVl 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  343 --SAQLQDIEGKidRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMKTFSSLGF------SGTQECPELRF 414
Cdd:PLN02936 357 irRAQVEDVLPG--GYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETNTDFryipfsGGPRKCVGDQF 434

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 29171730  415 AYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVTSSREEAWITVSKR 461
Cdd:PLN02936 435 ALLEAIVALAVLLQRLDLELVPDQDIVMTTGATIHTTNGLYMTVSRR 481
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 235-392 7.77e-10

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: 60.48  E-value: 7.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 235 LRNIIKE-RKGRNFSQHI--FIDSLV------QGN----LNDQQI-LEDSMIFSlASCIITAKLCTWAICFLTTSEEVQK 300
Cdd:cd20663 187 LDELLTEhRTTWDPAQPPrdLTDAFLaemekaKGNpessFNDENLrLVVADLFS-AGMVTTSTTLSWALLLMILHPDVQR 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 301 KLYEEINQVFGNGPvTPEKIEQLR--YCQHVLCETVRTAKLTPVSA---QLQDIEgkIDRFIIPRETLVLYALGVVLQDP 375
Cdd:cd20663 266 RVQQEIDEVIGQVR-RPEMADQARmpYTNAVIHEVQRFGDIVPLGVphmTSRDIE--VQGFLIPKGTTLITNLSSVLKDE 342

                       170
                ....*....|....*..
gi 29171730 376 NTWPSPHKFDPDRFDDE 392
Cdd:cd20663 343 TVWEKPLRFHPEHFLDA 359
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 269-446 8.13e-10

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: 60.60  E-value: 8.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 269 DSMIFSLASCII-----TAKLCTWAICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPV 342
Cdd:cd20661 237 ENLIFSVGELIIagtetTTNVLRWAILFMALYPNIQGQVQKEIDLVVGpNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPL 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 343 SAQLQDIEGKIDR-FIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDE--LVMKTFSSLGFS-GTQECPELRFAYMV 418
Cdd:cd20661 317 GIFHATSKDAVVRgYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSngQFAKKEAFVPFSlGRRHCLGEQLARME 396

                       170       180
                ....*....|....*....|....*...
gi 29171730 419 TTVLLSVLVKRLHLLSVEGQVIETKYEL 446
Cdd:cd20661 397 MFLFFTALLQRFHLHFPHGLIPDLKPKL 424
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 176-433 1.26e-09

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: 60.12  E-value: 1.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 176 VTQMVMGSTFEDDQEVIRFqknHGTV------WSEIGKGFLDG--SLDK--NMTRKKqYEDALMQLESVLRNIIKERKGR 245
Cdd:cd20674 118 ICCLTFGDKEDKDTLVQAF---HDCVqellktWGHWSIQALDSipFLRFfpNPGLRR-LKQAVENRDHIVESQLRQHKES 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 246 NFSQHI--FIDSLVQGnLNDQ-------QILEDSMIFSLASCII-----TAKLCTWAICFLTTSEEVQKKLYEEINQVFG 311
Cdd:cd20674 194 LVAGQWrdMTDYMLQG-LGQPrgekgmgQLLEGHVHMAVVDLFIggtetTASTLSWAVAFLLHHPEIQDRLQEELDRVLG 272

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 312 NG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDI-EGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF 389
Cdd:cd20674 273 PGaSPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTrDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERF 352

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 29171730 390 DDElVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLL 433
Cdd:cd20674 353 LEP-GAANRALLPFGcGARVCLGEPLARLELFVFLARLLQAFTLL 396
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 230-458 1.58e-09

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: 59.61  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 230 QLESVLRNIIKERKGRNFSQHI--FIDSLVQGNLNDQQILE--DSMIFslASCIITAKLCTWAICFLTTSEEVQKKLYEE 305
Cdd:cd20615 178 RWRAFNLKIYNRARQRGQSTPIvkLYEAVEKGDITFEELLQtlDEMLF--ANLDVTTGVLSWNLVFLAANPAVQEKLREE 255

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 306 INQVFGN-GPVTPEKIEQ----LRYCqhvLCETVRTAKLTPVS-AQLQDIEGKIDRFIIPRETLVL---YALGVvlQDPN 376
Cdd:cd20615 256 ISAAREQsGYPMEDYILStdtlLAYC---VLESLRLRPLLAFSvPESSPTDKIIGGYRIPANTPVVvdtYALNI--NNPF 330

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 377 TWPSPHKFDPDRFDDEL---VMKTFSSLGFsGTQECPELRFAYMVTTVLLSVLVKRLHL-LSVEGQVIETKYElvtssrE 452
Cdd:cd20615 331 WGPDGEAYRPERFLGISptdLRYNFWRFGF-GPRKCLGQHVADVILKALLAHLLEQYELkLPDQGENEEDTFE------G 403


                ....*.
gi 29171730 453 EAWITV 458
Cdd:cd20615 404 LPWIWV 409
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 57-429 4.92e-09

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: 58.19  E-value: 4.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  57 FLVNLHERYGPVVSFWFGRRLVVSLGTVDVLKQhINPNKTSD---PFETM--LKSLLryqsGGGSVSEN-----HMRKKL 126
Cdd:cd20640   3 YFDKWRKQYGPIFTYSTGNKQFLYVSRPEMVKE-INLCVSLDlgkPSYLKktLKPLF----GGGILTSNgphwaHQRKII 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 127 YENGVTDSLKSNFALLLKLSEELLDKWLSYPE-----TQHVPLSQHMLGFAMKSVTQMVMGSTFEDDQEV-IRFQKNHGT 200
Cdd:cd20640  78 APEFFLDKVKGMVDLMVDSAQPLLSSWEERIDraggmAADIVVDEDLRAFSADVISRACFGSSYSKGKEIfSKLRELQKA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 201 VwSEIGKGFLDGSLDKNMTRKKQYEDAL-MQLESVLRNIIKERK-----GRNFSQHIfIDSlVQGNLNDQQILEDsmiFS 274
Cdd:cd20640 158 V-SKQSVLFSIPGLRHLPTKSNRKIWELeGEIRSLILEIVKEREeecdhEKDLLQAI-LEG-ARSSCDKKAEAED---FI 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 275 LASCI--------ITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRtakLTPVSA-- 344
Cdd:cd20640 232 VDNCKniyfagheTTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPPDADSLSRMKTVTMVIQETLR---LYPPAAfv 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 345 ---QLQDIegKIDRFIIPRETLVLYALGVVLQDPNTW-PSPHKFDPDRFDD---ELVMKTFSSLGF-SGTQECPELRFAY 416
Cdd:cd20640 309 sreALRDM--KLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNgvaAACKPPHSYMPFgAGARTCLGQNFAM 386

                       410
                ....*....|...
gi 29171730 417 MVTTVLLSVLVKR 429
Cdd:cd20640 387 AELKVLVSLILSK 399
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 227-435 7.11e-09

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: 57.69  E-value: 7.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 227 ALMQLESVLRNIIKERKGRNFSQ--HIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYE 304
Cdd:cd11059 181 ALDLCARAESSLAESSDSESLTVllLEKLKGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLRE 260

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 305 EINQVFGN--GPVTPEKIEQLRYCQHVLCETVRTAklTPVSAQLQ---DIEGK-IDRFIIPRETLVL---YALGvvlQDP 375
Cdd:cd11059 261 ELAGLPGPfrGPPDLEDLDKLPYLNAVIRETLRLY--PPIPGSLPrvvPEGGAtIGGYYIPGGTIVStqaYSLH---RDP 335

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29171730 376 NTWPSPHKFDPDRF-----DDELVMKT-FSSLGfSGTQECPELRFAYMVTTVLLSVLVKRLHLLSV 435
Cdd:cd11059 336 EVFPDPEEFDPERWldpsgETAREMKRaFWPFG-SGSRMCIGMNLALMEMKLALAAIYRNYRTSTT 400
PLN02183 PLN02183
ferulate 5-hydroxylase
 287-410 1.24e-08

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 57.17  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  287 WAICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVL 365
Cdd:PLN02183 326 WAMAELMKSPEDLKRVQQELADVVGlNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVM 405

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 29171730  366 ---YALGvvlQDPNTWPSPHKFDPDRFDDELVM----KTFSSLGF-SGTQECP 410
Cdd:PLN02183 406 inaWAIG---RDKNSWEDPDTFKPSRFLKPGVPdfkgSHFEFIPFgSGRRSCP 455
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 224-447 1.54e-08

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: 56.39  E-value: 1.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 224 YEDALMQLESVLRNIIKE---RKGRNFSQhIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQK 300
Cdd:cd20644 189 WDCIFQYADNCIQKIYQElafGRPQHYTG-IVAELLLQAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQ 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 301 KLYEEINQVFGNGPVTPEKIEQ-LRYCQHVLCETVRtakLTPVSAQLQDIEGK---IDRFIIPRETLV---LYALGvvlQ 373
Cdd:cd20644 268 ILRQESLAAAAQISEHPQKALTeLPLLKAALKETLR---LYPVGITVQRVPSSdlvLQNYHIPAGTLVqvfLYSLG---R 341

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29171730 374 DPNTWPSPHKFDPDRF-DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELV 447
Cdd:cd20644 342 SAALFPRPERYDPQRWlDIRGSGRNFKHLAFGfGMRQCLGRRLAEAEMLLLLMHVLKNFLVETLSQEDIKTVYSFI 417
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 281-389 1.77e-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: 1.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 281 TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGP--------VTPEKIEQLRYCQHVLCETVR------TAKLTPVSAQL 346
Cdd:cd11051 201 TSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPsaaaellrEGPELLNQLPYTTAVIKETLRlfppagTARRGPPGVGL 280

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 29171730 347 QDIEGKIdrfiIPRETLVLYALGVVLQ-DPNTWPSPHKFDPDRF 389
Cdd:cd11051 281 TDRDGKE----YPTDGCIVYVCHHAIHrDPEYWPRPDEFIPERW 320
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 235-432 1.80e-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: 56.47  E-value: 1.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 235 LRNIIKE-RKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFG-N 312
Cdd:cd20647 206 LREIQKQmDRGEEVKGGLLTYLLVSKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGkR 285

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 313 GPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRET-LVLYALGVVLQDPNtWPSPHKFDPDRF-- 389
Cdd:cd20647 286 VVPTAEDVPKLPLIRALLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTqLALCHYSTSYDEEN-FPRAEEFRPERWlr 364

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 29171730 390 -DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHL 432
Cdd:cd20647 365 kDALDRVDNFGSIPFGyGIRSCIGRRIAELEIHLALIQLLQNFEI 409
PLN00168 PLN00168
Cytochrome P450; Provisional
 8-389 2.15e-08

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 56.50  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730    8 AVTFLLALVGAVLYLYPASRQAAG--IPGITPTEEKDGNLPDIVNSGSLHEFLVN-LHERYGPVVSFWFGRRLVVSLGTV 84
Cdd:PLN00168  10 AALLLLPLLLLLLGKHGGRGGKKGrrLPPGPPAVPLLGSLVWLTNSSADVEPLLRrLIARYGPVVSLRVGSRLSVFVADR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   85 DVLKQHI---------NPNKTSDPFETMLKSLLRyQSGGGSVSENHMRKKLYENGVTDSLKSNFALLLKLSEELLDKWLS 155
Cdd:PLN00168  90 RLAHAALvergaaladRPAVASSRLLGESDNTIT-RSSYGPVWRLLRRNLVAETLHPSRVRLFAPARAWVRRVLVDKLRR 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  156 YPETQHVPLSQHMLGFAMKSV-TQMVMGSTFEDD---------QEVIRFQKNHGTV---WSEIGKGFLDGSLDKNMT-RK 221
Cdd:PLN00168 169 EAEDAAAPRVVETFQYAMFCLlVLMCFGERLDEPavraiaaaqRDWLLYVSKKMSVfafFPAVTKHLFRGRLQKALAlRR 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  222 KQYE------DALMQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQ--QILEDSMIFSLASCIITAKLCT------W 287
Cdd:PLN00168 249 RQKElfvpliDARREYKNHLGQGGEPPKKETTFEHSYVDTLLDIRLPEDgdRALTDDEIVNLCSEFLNAGTDTtstalqW 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  288 AICFLTTSEEVQKKLYEEINQVFGNGP--VTPEKIEQLRYCQHVLCETVRtaKLTPVSAQL-----QDIEgkIDRFIIPR 360
Cdd:PLN00168 329 IMAELVKNPSIQSKLHDEIKAKTGDDQeeVSEEDVHKMPYLKAVVLEGLR--KHPPAHFVLphkaaEDME--VGGYLIPK 404

                        410       420
                 ....*....|....*....|....*....
gi 29171730  361 ETLVLYALGVVLQDPNTWPSPHKFDPDRF 389
Cdd:PLN00168 405 GATVNFMVAEMGRDEREWERPMEFVPERF 433
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 182-429 2.40e-08

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: 56.13  E-value: 2.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 182 GSTFEDDQEVIRFQKNHGT-VWSEIGKGFLDGSL---DKNMTRKKQYEdalMQLESVLRNII----KERKGRNFSQHIFI 253
Cdd:cd20642 133 GSSYEEGKKIFELQKEQGElIIQALRKVYIPGWRflpTKRNRRMKEIE---KEIRSSLRGIInkreKAMKAGEATNDDLL 209

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 254 DSLVQGNLND-------------QQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKI 320
Cdd:cd20642 210 GILLESNHKEikeqgnknggmstEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKPDFEGL 289

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 321 EQLRYCQHVLCETVRtakLTPVSAQLQDI---EGKIDRFIIPRETLVLYALGVVLQDPNTW-PSPHKFDPDRFDDELVMK 396
Cdd:cd20642 290 NHLKVVTMILYEVLR---LYPPVIQLTRAihkDTKLGDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFAEGISKA 366

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 29171730 397 T---FSSLGFS-GTQECPELRFAYMVTTVLLSVLVKR 429
Cdd:cd20642 367 TkgqVSYFPFGwGPRICIGQNFALLEAKMALALILQR 403
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 222-389 4.12e-08

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: 55.41  E-value: 4.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 222 KQYEDALMQLESVLRNIIKERKgRNFSQ-HI--FIDSLVQ--------GNLNDQqiLEDSMIFSLASCI-------ITAK 283
Cdd:cd20676 180 KRFKDINKRFNSFLQKIVKEHY-QTFDKdNIrdITDSLIEhcqdkkldENANIQ--LSDEKIVNIVNDLfgagfdtVTTA 256

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 284 LCtWAICFLTTSEEVQKKLYEEINQVFG--NGPVTPEKIeQLRYCQHVLCETVRTAKLTPVS---AQLQDIegKIDRFII 358
Cdd:cd20676 257 LS-WSLMYLVTYPEIQKKIQEELDEVIGreRRPRLSDRP-QLPYLEAFILETFRHSSFVPFTiphCTTRDT--SLNGYYI 332

                       170       180       190
                ....*....|....*....|....*....|.
gi 29171730 359 PRETLVLYALGVVLQDPNTWPSPHKFDPDRF 389
Cdd:cd20676 333 PKDTCVFINQWQVNHDEKLWKDPSSFRPERF 363
PTZ00404 PTZ00404
cytochrome P450; Provisional
 43-461 5.54e-08

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 55.11  E-value: 5.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   43 GNLPdivnsgslHEFLVNLHERYGPVVSFWFGRRLVVSLGTVDVLKQ-HIN--PNKTSDPFETMLKSLLRYQSGGGSVSE 119
Cdd:PTZ00404  47 GNLP--------HRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREmFVDnfDNFSDRPKIPSIKHGTFYHGIVTSSGE 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  120 NHMRKKlyeNGVTDSL-KSNFALLLKLSEELLD---KWLSYPETQHVPLSQHML--GFAMKSVTQMVMGSTFEDDQEVIR 193
Cdd:PTZ00404 119 YWKRNR---EIVGKAMrKTNLKHIYDLLDDQVDvliESMKKIESSGETFEPRYYltKFTMSAMFKYIFNEDISFDEDIHN 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  194 FQ-----KNHGTVWSEIGKGFLDGSLDKNMTRKKQYedaLMQLESVLRNIIKERKGRnFSQHI-FIDSLVQGNLNDQQIL 267
Cdd:PTZ00404 196 GKlaelmGPMEQVFKDLGSGSLFDVIEITQPLYYQY---LEHTDKNFKKIKKFIKEK-YHEHLkTIDPEVPRDLLDLLIK 271

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  268 E-----DSMIFSLASCII---------TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGP-VTPEKIEQLRYCQHVLCE 332
Cdd:PTZ00404 272 EygtntDDDILSILATILdfflagvdtSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNkVLLSDRQSTPYTVAIIKE 351

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  333 TVRTAKLTPVS---AQLQDIEGKIDRFiIPRETLVL---YALGvvlQDPNTWPSPHKFDPDRFDDELVMKTFssLGFS-G 405
Cdd:PTZ00404 352 TLRYKPVSPFGlprSTSNDIIIGGGHF-IPKDAQILinyYSLG---RNEKYFENPEQFDPSRFLNPDSNDAF--MPFSiG 425

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 29171730  406 TQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVI-ETKYELVTSSREEAWITVSKR 461
Cdd:PTZ00404 426 PRNCVGQQFAQDELYLAFSNIILNFKLKSIDGKKIdETEEYGLTLKPNKFKVLLEKR 482
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 4-431 5.84e-08

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 54.83  E-value: 5.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730    4 FAIFAVTFLLALVGAVLYLYPAsRQAAGIPGITPTEEKDGNLpdiVNSGSL-HEFLVNLHERYGPVVsfwfgrrlVVSLG 82
Cdd:PLN03112   6 LSLLFSVLIFNVLIWRWLNASM-RKSLRLPPGPPRWPIVGNL---LQLGPLpHRDLASLCKKYGPLV--------YLRLG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730   83 TVDVLKqhinpnkTSDPfETMLKSLLRYQS----------------GGGSVSE-------NHMRKKLYENGVTDSLKSNF 139
Cdd:PLN03112  74 SVDAIT-------TDDP-ELIREILLRQDDvfasrprtlaavhlayGCGDVALaplgphwKRMRRICMEHLLTTKRLESF 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  140 AL--LLKLSEELLDKWLSYPETQHVPLSQHMLGFAMKSVTQMVMGSTF-----EDDQEVIRFQK-NHGTVWSeIGKGFLD 211
Cdd:PLN03112 146 AKhrAEEARHLIQDVWEAAQTGKPVNLREVLGAFSMNNVTRMLLGKQYfgaesAGPKEAMEFMHiTHELFRL-LGVIYLG 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  212 ------GSLDKNMTRKKQYEdALMQLESVLRNIIKER------KGRNFSQHIFIDSLVQ-GNLNDQQILEDSMIFSLASC 278
Cdd:PLN03112 225 dylpawRWLDPYGCEKKMRE-VEKRVDEFHDKIIDEHrrarsgKLPGGKDMDFVDVLLSlPGENGKEHMDDVEIKALMQD 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  279 IITAKLCT------WAICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEG 351
Cdd:PLN03112 304 MIAAATDTsavtneWAMAEVIKNPRVLRKIQEELDSVVGrNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRA 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  352 -KIDRFIIPRETLVL---YALGvvlQDPNTWPSPHKFDPDRF--DDELVMKT-----FSSLGFS-GTQECPElrfAYMVT 419
Cdd:PLN03112 384 tTINGYYIPAKTRVFintHGLG---RNTKIWDDVEEFRPERHwpAEGSRVEIshgpdFKILPFSaGKRKCPG---APLGV 457

                        490
                 ....*....|..
gi 29171730  420 TVLLSVLVKRLH 431
Cdd:PLN03112 458 TMVLMALARLFH 469
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 297-392 6.17e-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: 54.80  E-value: 6.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 297 EVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVS-AQLQDIEGKIDRFIIPRETLVLYALGVVLQD 374
Cdd:cd20668 258 EVEAKVHEEIDRVIGrNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGlARRVTKDTKFRDFFLPKGTEVFPMLGSVLKD 337

                        90
                ....*....|....*...
gi 29171730 375 PNTWPSPHKFDPDRFDDE 392
Cdd:cd20668 338 PKFFSNPKDFNPQHFLDD 355
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 287-392 7.55e-08

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: 54.55  E-value: 7.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEINQVFGNG--PVTPEKIeQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDR-FIIPRETL 363
Cdd:cd20670 248 YGFLLLMKYPEVEAKIHEEINQVIGPHrlPSVDDRV-KMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFRgYLLPKGTD 326

                        90       100
                ....*....|....*....|....*....
gi 29171730 364 VLYALGVVLQDPNTWPSPHKFDPDRFDDE 392
Cdd:cd20670 327 VFPLLGSVLKDPKYFRYPEAFYPQHFLDE 355
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 155-432 1.09e-07

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: 53.99  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 155 SYPETQHVPLSQHMLGF-AMKSVTQM-VMGSTFEDDQEVIRFQKNHGTVWSEIgKGFLDGSLDKNmtrKKQYEDALMQLe 232
Cdd:cd20641 139 SYAEGIEVFLSQLELQKcAAASLTNLyIPGTQYLPTPRNLRVWKLEKKVRNSI-KRIIDSRLTSE---GKGYGDDLLGL- 213

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 233 sVLRNIIKERKGRNFSQHIFIDslvqgnlndqQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEI-NQVFG 311
Cdd:cd20641 214 -MLEAASSNEGGRRTERKMSID----------EIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVfRECGK 282

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 312 NGPVTPEKIEQLRYCQHVLCETVR-------TAKLTPVSAQLQDIEgkidrfiIPRETLVLYALGVVLQDPNTWPS-PHK 383
Cdd:cd20641 283 DKIPDADTLSKLKLMNMVLMETLRlygpvinIARRASEDMKLGGLE-------IPKGTTIIIPIAKLHRDKEVWGSdADE 355

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 29171730 384 FDPDRFDDELVMKTF---SSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHL 432
Cdd:cd20641 356 FNPLRFANGVSRAAThpnALLSFSlGPRACIGQNFAMIEAKTVLAMILQRFSF 408
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 297-392 1.10e-07

cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group includes CYP2C, and similar CYPs including mammalian CYP2E1, also called 4-nitrophenol 2-hydroxylase, as well as chicken CYP2H1 and CYP2H2. The CYP2C subfamily is composed of four human members (CYP2C8, CYP2C9, CYP2C18, CYP2C19) that metabolize approximately 20% of clinically used drugs, and all four exhibit genetic polymorphisms that results in toxicity or altered efficacy of some drugs in affected individuals. CYP2E1 participates in the metabolism of endogenous substrates, including acetone and fatty acids, and exogenous compounds such as anesthetics, ethanol, nicotine, acetaminophen, aspartame, and chlorzoxazone, among others. The CYP2C-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 53.80  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 297 EVQKKLYEEINQVFG--NGPVTPEKIeQLRYCQHVLCETVRTAKLTPVS---AQLQDIegKIDRFIIPRETLVLYALGVV 371
Cdd:cd20665 258 EVTAKVQEEIDRVIGrhRSPCMQDRS-HMPYTDAVIHEIQRYIDLVPNNlphAVTCDT--KFRNYLIPKGTTVITSLTSV 334

                        90       100
                ....*....|....*....|.
gi 29171730 372 LQDPNTWPSPHKFDPDRFDDE 392
Cdd:cd20665 335 LHDDKEFPNPEKFDPGHFLDE 355
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 223-447 3.34e-07

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: 52.39  E-value: 3.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 223 QYEDALMQL-------ESVLRNIIKERKGRNFSqhiFIDSLV-----QGN-LNDQQILEDSMIFSLASCIITAKLCTWAI 289
Cdd:cd20679 192 DFTDAVIQErrrtlpsQGVDDFLKAKAKSKTLD---FIDVLLlskdeDGKeLSDEDIRAEADTFMFEGHDTTASGLSWIL 268

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 290 CFLTTSEEVQKKLYEEINQVF-GNGPvtpEKIE-----QLRYCQHVLCETVRTAKLTPVSAQ--LQDIEGKIDRfIIPRE 361
Cdd:cd20679 269 YNLARHPEYQERCRQEVQELLkDREP---EEIEwddlaQLPFLTMCIKESLRLHPPVTAISRccTQDIVLPDGR-VIPKG 344

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 362 TLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVmKTFSSLGF----SGTQECPELRFAYMVTTVLLSVLVKRLHLLSvEG 437
Cdd:cd20679 345 IICLISIYGTHHNPTVWPDPEVYDPFRFDPENS-QGRSPLAFipfsAGPRNCIGQTFAMAEMKVVLALTLLRFRVLP-DD 422

                       250
                ....*....|
gi 29171730 438 QVIETKYELV 447
Cdd:cd20679 423 KEPRRKPELI 432
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 287-427 3.55e-07

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 52.55  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  287 WAICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTP-----VSAQLQDIEGkidrFIIPR 360
Cdd:PLN00110 311 WSLAEMLKNPSILKRAHEEMDQVIGrNRRLVESDLPKLPYLQAICKESFRKHPSTPlnlprVSTQACEVNG----YYIPK 386

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29171730  361 ETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMKT------FSSLGF-SGTQECPELRFAYMVTTVLLSVLV 427
Cdd:PLN00110 387 NTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIdprgndFELIPFgAGRRICAGTRMGIVLVEYILGTLV 460
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 295-392 7.12e-07

cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic conversions of fatty acid hydroperoxides to bioactive oxylipins in plants, some invertebrates, and bacteria. It includes two dehydrases, namely allene oxide synthase (AOS) and divinyl ether synthase (DES), and two isomerases, hydroperoxide lyase (HPL) and epoxyalcohol synthase (EAS). AOS (EC 4.2.1.92, also called hydroperoxide dehydratase), such as Arabidopsis thaliana CYP74A acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. DES (EC 4.2.1.121), also called colneleate synthase or CYP74D, catalyzes the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid. The linolenate HPL, Arabidopsis thaliana CYP74B2, is required for the synthesis of the green leaf volatiles (GLVs) hexanal and trans-2-hexenal. The fatty acid HPL, Solanum lycopersicum CYP74B, is involved in the biosynthesis of traumatin and C6 aldehydes. The epoxyalcohol synthase Ranunculus japonicus CYP74A88 (also known as RjEAS) specifically converts linoleic acid 9- and 13-hydroperoxides to oxiranyl carbinols 9,10-epoxy-11-hydroxy-12-octadecenoic acid and 11-hydroxy-12,13-epoxy-9-octadecenoic acid, respectively. The CYP74 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 51.49  E-value: 7.12e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 295 SEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAklTPVSAQLQ------DIEGKIDRFIIPRETLVLYA 367
Cdd:cd11071 256 GEELHARLAEEIRSALGsEGGLTLAALEKMPLLKSVVYETLRLH--PPVPLQYGrarkdfVIESHDASYKIKKGELLVGY 333

                        90       100
                ....*....|....*....|....*
gi 29171730 368 LGVVLQDPNTWPSPHKFDPDRFDDE 392
Cdd:cd11071 334 QPLATRDPKVFDNPDEFVPDRFMGE 358
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 287-443 8.16e-07

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: 51.25  E-value: 8.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEI----NQVFGNgPVTPEKIEQLRYCqhVLCETVRtakLTPVSAQLQ-----DIegKIDRFI 357
Cdd:cd20643 256 WTLYELARNPNVQEMLRAEVlaarQEAQGD-MVKMLKSVPLLKA--AIKETLR---LHPVAVSLQryiteDL--VLQNYH 327

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 358 IPRETLV---LYALGvvlQDPNTWPSPHKFDPDRFddeLVMKT--FSSLGFS-GTQECPELRFAYMVTTVLLsvlvkrLH 431
Cdd:cd20643 328 IPAGTLVqvgLYAMG---RDPTVFPKPEKYDPERW---LSKDIthFRNLGFGfGPRQCLGRRIAETEMQLFL------IH 395

                       170
                ....*....|..
gi 29171730 432 LLsvEGQVIETK 443
Cdd:cd20643 396 ML--ENFKIETQ 405
PLN02971 PLN02971
tryptophan N-hydroxylase
 287-452 9.45e-07

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 51.19  E-value: 9.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  287 WAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRtakLTPVSA------QLQDIegKIDRFIIP 359
Cdd:PLN02971 349 WAMAEMINKPEILHKAMEEIDRVVGKERFVQESdIPKLNYVKAIIREAFR---LHPVAAfnlphvALSDT--TVAGYHIP 423

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  360 RETLVL---YALGvvlQDPNTWPSPHKFDPDRFDDEL--VMKTFSSLGF----SGTQECPELRFAYMVTTVLLSVLVKRL 430
Cdd:PLN02971 424 KGSQVLlsrYGLG---RNPKVWSDPLSFKPERHLNECseVTLTENDLRFisfsTGKRGCAAPALGTAITTMMLARLLQGF 500

                        170       180
                 ....*....|....*....|..
gi 29171730  431 HLLSVEGqviETKYELVTSSRE 452
Cdd:PLN02971 501 KWKLAGS---ETRVELMESSHD 519
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 281-427 1.38e-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: 50.32  E-value: 1.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 281 TAKLcTWAICFLTTSEEVQKKLYEEINQVFGNG--PVTPEKIEQLRYCQHVLCETVR---TAKLTP--VSAQLQDIEGki 353
Cdd:cd11082 237 TSSL-VWALQLLADHPDVLAKVREEQARLRPNDepPLTLDLLEEMKYTRQVVKEVLRyrpPAPMVPhiAKKDFPLTED-- 313

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 354 drFIIPRETLVLYALGVVLQDPntWPSPHKFDPDRFD-----DELVMKTFSSLGfSGTQECPELRFA---YMVTTVLLSV 425
Cdd:cd11082 314 --YTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSperqeDRKYKKNFLVFG-AGPHQCVGQEYAinhLMLFLALFST 388


                ..
gi 29171730 426 LV 427
Cdd:cd11082 389 LV 390
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 281-392 2.96e-06

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: 49.29  E-value: 2.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 281 TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKI---EQLRYCQH---VLCETVRTAkLTPVSA--QLQDIEGk 352
Cdd:cd11040 239 TIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILdltDLLTSCPLldsTYLETLRLH-SSSTSVrlVTEDTVL- 316

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 29171730 353 IDRFIIPRETLVLYALGVVLQDPNTW-PSPHKFDPDRFDDE 392
Cdd:cd11040 317 GGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKK 357
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 261-431 7.23e-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: 48.21  E-value: 7.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 261 LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVfGNGPVTPEKIEQLRYCQHVLCETVRTAKLT 340
Cdd:cd20614 204 LSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA-GDVPRTPAELRRFPLAEALFRETLRLHPPV 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 341 PVSAQ--LQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF-DDELVMKTFSSLGF-SGTQECPELRFAY 416
Cdd:cd20614 283 PFVFRrvLEEIE--LGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWlGRDRAPNPVELLQFgGGPHFCLGYHVAC 360

                       170
                ....*....|....*
gi 29171730 417 MVTTVLLSVLVKRLH 431
Cdd:cd20614 361 VELVQFIVALARELG 375
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 213-441 7.53e-06

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: 48.17  E-value: 7.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 213 SLDKNMTRkkQYEDALMQLesvlrniIKERKGRNFSQhifidslvqgNLNDQQILED-SMIFSLASCIITAKLcTWAICF 291
Cdd:cd20677 203 TYDKNHIR--DITDALIAL-------CQERKAEDKSA----------VLSDEQIISTvNDIFGAGFDTISTAL-QWSLLY 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 292 LTTSEEVQKKLYEEINQVFGNGPVTP-EKIEQLRYCQHVLCETVRTAKLTPVS-AQLQDIEGKIDRFIIPRETLVLYALG 369
Cdd:cd20677 263 LIKYPEIQDKIQEEIDEKIGLSRLPRfEDRKSLHYTEAFINEVFRHSSFVPFTiPHCTTADTTLNGYFIPKDTCVFINMY 342

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 370 VVLQDPNTWPSPHKFDPDRFDDE-------LVMKTfssLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIE 441
Cdd:cd20677 343 QVNHDETLWKDPDLFMPERFLDEngqlnksLVEKV---LIFGmGVRKCLGEDVARNEIFVFLTTILQQLKLEKPPGQKLD 419
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 286-415 1.07e-05

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: 47.44  E-value: 1.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 286 TWAICFLTTSEEVQKKLYEEINQVFGNGPV-TPEKIEQLRYCQHVLCETVRTAKLTPVSAQL---QDIEgkIDRFIIPRE 361
Cdd:cd20648 255 SWSLYELSRHPDVQTALHREITAALKDNSVpSAADVARMPLLKAVVKEVLRLYPVIPGNARVipdRDIQ--VGEYIIPKK 332

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 29171730 362 TLVLYALGVVLQDPNTWPSPHKFDPDRF-DDELVMKTFSSLGFS-GTQECPELRFA 415
Cdd:cd20648 333 TLITLCHYATSRDENQFPDPNSFRPERWlGKGDTHHPYASLPFGfGKRSCIGRRIA 388
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
 298-391 1.40e-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: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 298 VQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDR-FIIPRETLVLYALGVVLQDP 375
Cdd:cd20672 259 VAEKVQKEIDQVIGsHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTLFRgYLLPKNTEVYPILSSALHDP 338

                        90
                ....*....|....*.
gi 29171730 376 NTWPSPHKFDPDRFDD 391
Cdd:cd20672 339 QYFEQPDTFNPDHFLD 354
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 230-450 1.59e-05

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: 47.14  E-value: 1.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 230 QLESVLRNIIKERKGRNFSQH------IFIDSLVQGN--LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKK 301
Cdd:cd20636 184 ILHEYMEKAIEEKLQRQQAAEycdaldYMIHSARENGkeLTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEK 263

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 302 LYEEINQ-----VFGNGP--VTPEKIEQLRYCQHVLCETVRTakLTPVSA----QLQDIEgkIDRFIIPRETLVLYALGV 370
Cdd:cd20636 264 IRQELVShglidQCQCCPgaLSLEKLSRLRYLDCVVKEVLRL--LPPVSGgyrtALQTFE--LDGYQIPKGWSVMYSIRD 339

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 371 VLQDPNTWPSPHKFDPDRFD---DELVMKTFSSLGF-SGTQECPELRFAYMVttvllsvlvkrLHLLSVEgQVIETKYEL 446
Cdd:cd20636 340 THETAAVYQNPEGFDPDRFGverEESKSGRFNYIPFgGGVRSCIGKELAQVI-----------LKTLAVE-LVTTARWEL 407


                ....
gi 29171730 447 VTSS 450
Cdd:cd20636 408 ATPT 411
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 287-417 2.11e-05

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: 46.54  E-value: 2.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEINQVFGNG-----PVTPEKIEQLRYCQHVLCETVR-------TAKLT-PVsaqlqdiegKI 353
Cdd:cd20635 232 WTLAFILSHPSVYKKVMEEISSVLGKAgkdkiKISEDDLKKMPYIKRCVLEAIRlrspgaiTRKVVkPI---------KI 302

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29171730 354 DRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDD-----ELVMKTFSSLGfSGTQECPELRFAYM 417
Cdd:cd20635 303 KNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKadlekNVFLEGFVAFG-GGRYQCPGRWFALM 370
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 287-427 2.89e-05

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: 46.21  E-value: 2.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRtakLTPVSA------QLQDIegKIDRFIIP 359
Cdd:cd20658 259 WALAEMLNQPEILRKATEELDRVVGKERLVQESdIPNLNYVKACAREAFR---LHPVAPfnvphvAMSDT--TVGGYFIP 333

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29171730 360 RETLVL---YALGvvlQDPNTWPSPHKFDPDRF--DDELVMKTFSSLGF----SGTQECPELRFAYMVTTVLLSVLV 427
Cdd:cd20658 334 KGSHVLlsrYGLG---RNPKVWDDPLKFKPERHlnEDSEVTLTEPDLRFisfsTGRRGCPGVKLGTAMTVMLLARLL 407
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 232-392 3.05e-05

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: 46.04  E-value: 3.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 232 ESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFG 311
Cdd:cd11058 184 EKVDRRLAKGTDRPDFMSYILRNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFS 263

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 312 N-GPVTPEKIEQLRYCQHVLCETVRtakLT-PVSAQLQDI---EGK-IDRFIIPRETLVLYALGVVLQDPNTWPSPHKFD 385
Cdd:cd11058 264 SeDDITLDSLAQLPYLNAVIQEALR---LYpPVPAGLPRVvpaGGAtIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFI 340


                ....*..
gi 29171730 386 PDRFDDE 392
Cdd:cd11058 341 PERWLGD 347
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 321-438 3.29e-05

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


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 45.75  E-value: 3.29e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 321 EQLRYCQHVLCeTVRTAkltpvsaqLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRfddelvmKTFSS 400
Cdd:cd20629 242 EGLRWEPPVAS-VPRMA--------LRDVE--LDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR-------KPKPH 303

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 29171730 401 LGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 438
Cdd:cd20629 304 LVFGgGAHRCLGEHLARVELREALNALLDRLPNLRLDPD 342
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 297-442 4.57e-05

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: 45.43  E-value: 4.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 297 EVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRT---AKLTPVSAQLQDIegkIDRFIIPRETLVLYALGVVLQ 373
Cdd:cd20616 256 EVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYqpvVDFVMRKALEDDV---IDGYPVKKGTNIILNIGRMHR 332

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29171730 374 DPNtWPSPHKFDPDRFDDELVMKTFSSLGFsGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIET 442
Cdd:cd20616 333 LEF-FPKPNEFTLENFEKNVPSRYFQPFGF-GPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVEN 399
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 168-452 6.03e-05

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: 45.18  E-value: 6.03e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 168 MLGFAMKSVTQMVMGSTFEDdqeviRFQKNHGTVWSEIGKGfLDGSLDKNMTRKKQyedalmqlesvlrniikeRKGRNF 247
Cdd:cd20645 157 MSTFGKMMVTPVELHKRLNT-----KVWQDHTEAWDNIFKT-AKHCIDKRLQRYSQ------------------GPANDF 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 248 SQHIFIDslvqGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQV-FGNGPVTPEKIEQLRYC 326
Cdd:cd20645 213 LCDIYHD----NELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVlPANQTPRAEDLKNMPYL 288

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 327 QHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVL---YALGVvlqDPNTWPSPHKFDPDRF-DDELVMKTFSSLG 402
Cdd:cd20645 289 KACLKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMinsQALGS---SEEYFEDGRQFKPERWlQEKHSINPFAHVP 365

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 29171730 403 FS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYE-LVTSSRE 452
Cdd:cd20645 366 FGiGKRMCIGRRLAELQLQLALCWIIQKYQIVATDNEPVEMLHSgILVPSRE 417
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 245-440 1.46e-04

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 43.96  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  245 RNFSQHIfIDSLVQGNLNDQQIL-EDSMifslasciitAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIE-- 321
Cdd:PLN03141 241 RDGSDEL-TDDLISDNMIDMMIPgEDSV----------PVLMTLAVKFLSDCPVALQQLTEENMKLKRLKADTGEPLYwt 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  322 ---QLRYCQHVLCETVRTAKLTP--VSAQLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDElVMK 396
Cdd:PLN03141 310 dymSLPFTQNVITETLRMGNIINgvMRKAMKDVE--IKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEK-DMN 386

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 29171730  397 TFSSLGFSGTQE-CPELRFAYMVTTVLLSVLVKRLHLLSVEGQVI 440
Cdd:PLN03141 387 NSSFTPFGGGQRlCPGLDLARLEASIFLHHLVTRFRWVAEEDTIV 431
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 260-429 1.61e-04

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 43.81  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  260 NLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFG----NGPVTPEKIEQLRYCQHVLCETVR 335
Cdd:PLN02987 262 GFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAmksdSYSLEWSDYKSMPFTQCVVNETLR 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  336 TAKLTP--VSAQLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVM----KTFSSLGfSGTQEC 409
Cdd:PLN02987 342 VANIIGgiFRRAMTDIE--VKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTtvpsNVFTPFG-GGPRLC 418

                        170       180
                 ....*....|....*....|
gi 29171730  410 PELRFAYMVTTVLLSVLVKR 429
Cdd:PLN02987 419 PGYELARVALSVFLHRLVTR 438
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 297-392 1.70e-04

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: 43.98  E-value: 1.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 297 EVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEGKidRFIIPRETLVLYALGVVL 372
Cdd:cd20669 258 KVAARVQEEIDRVVGrNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSlphAVTRDTNFR--GFLIPKGTDVIPLLNSVH 335

                        90       100
                ....*....|....*....|
gi 29171730 373 QDPNTWPSPHKFDPDRFDDE 392
Cdd:cd20669 336 YDPTQFKDPQEFNPEHFLDD 355
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 231-450 1.97e-04

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: 43.68  E-value: 1.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 231 LESVLRNIIKERKGRNFSQ--HIFIDSLVQGN--LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEI 306
Cdd:cd20637 188 LEKAIREKLQGTQGKDYADalDILIESAKEHGkeLTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREEL 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 307 -------NQVFGNGPVTPEKIEQLRYCQHVLCETVRTakLTPVSA----QLQDIEgkIDRFIIPRETLVLYAL------G 369
Cdd:cd20637 268 rsngilhNGCLCEGTLRLDTISSLKYLDCVIKEVLRL--FTPVSGgyrtALQTFE--LDGFQIPKGWSVLYSIrdthdtA 343

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 370 VVLQDPNTwpsphkFDPDRFDDElvmktfsslgfsgTQECPELRFAYM-----VTTVLLSVLVKR-LHLLSVEgQVIETK 443
Cdd:cd20637 344 PVFKDVDA------FDPDRFGQE-------------RSEDKDGRFHYLpfgggVRTCLGKQLAKLfLKVLAVE-LASTSR 403


                ....*..
gi 29171730 444 YELVTSS 450
Cdd:cd20637 404 FELATRT 410
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 257-392 3.59e-04

fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This group includes Aspergillus nidulans phenylacetate 2-hydroxylase (encoded by the phacA gene) and similar fungal cytochrome P450s. PhacA catalyzes the ortho-hydroxylation of phenylacetate, the first step of A. nidulans phenylacetate catabolism. The PhacA-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 42.69  E-value: 3.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 257 VQGNL--NDQQILEDSMIFSLASCIITAKLCT------WAICFLTTS--EEVQKKLYEEINQVFGNG------PVTPEKI 320
Cdd:cd11066 212 IVGNIlkDKESKLTDAELQSICLTMVSAGLDTvplnlnHLIGHLSHPpgQEIQEKAYEEILEAYGNDedawedCAAEEKC 291

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29171730 321 EqlrYCQHVLCETVR---TAKLTPVSAQLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDE 392
Cdd:cd11066 292 P---YVVALVKETLRyftVLPLGLPRKTTKDIV--YNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDA 361
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 207-430 6.42e-04

cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is the main all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. CYP26A1 has been shown to upregulate fascin and promote the malignant behavior of breast carcinoma cells. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 42.11  E-value: 6.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 207 KGFLDGSLDKNMTRKKQYEDALMQLESVLRNIIkERKGRNFSQhifidslvqgnLNDQQILEDSMIFSLASCIITAKLCT 286
Cdd:cd20638 184 RNLIHAKIEENIRAKIQREDTEQQCKDALQLLI-EHSRRNGEP-----------LNLQALKESATELLFGGHETTASAAT 251

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 287 WAICFLTTSEEVQKKLYEEIN-QVFGNGPVTPEK------IEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIP 359
Cdd:cd20638 252 SLIMFLGLHPEVLQKVRKELQeKGLLSTKPNENKelsmevLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIP 331

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29171730 360 RETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMKT--FSSLGF-SGTQECPELRFAymvtTVLLSVLVKRL 430
Cdd:cd20638 332 KGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSsrFSFIPFgGGSRSCVGKEFA----KVLLKIFTVEL 401
PLN02774 PLN02774
brassinosteroid-6-oxidase
 231-410 8.78e-04

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 41.68  E-value: 8.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  231 LESVLRNIIKERKGRNFSQHIFIDSL--VQGN---LNDQQILED--SMIFSLASCIITAKLCtwAICFLTTSEEVQKKLY 303
Cdd:PLN02774 225 IVRMLRQLIQERRASGETHTDMLGYLmrKEGNrykLTDEEIIDQiiTILYSGYETVSTTSMM--AVKYLHDHPKALQELR 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730  304 EE---INQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAklTPVSAQL----QDIEgkIDRFIIPRETLVLYALGVVLQDP 375
Cdd:PLN02774 303 KEhlaIRERKRpEDPIDWNDYKSMRFTRAVIFETSRLA--TIVNGVLrkttQDME--LNGYVIPKGWRIYVYTREINYDP 378

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 29171730  376 NTWPSPHKFDPDRF-DDELVMKTFSSLGFSGTQECP 410
Cdd:PLN02774 379 FLYPDPMTFNPWRWlDKSLESHNYFFLFGGGTRLCP 414
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 220-433 8.32e-03

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: 38.41  E-value: 8.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 220 RKKQyedalMQLESVLRNIIKERkgrnfsqHI-FIDSLVQGNLNDQQILEDSMI------FSLASCIITAKLCTWAICFL 292
Cdd:cd20678 199 RKEQ-----LQDEGELEKIKKKR-------HLdFLDILLFAKDENGKSLSDEDLraevdtFMFEGHDTTASGISWILYCL 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29171730 293 TTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRtakLTP----VSAQLQDIEGKIDRFIIPRETLV--- 364
Cdd:cd20678 267 ALHPEHQQRCREEIREILGDGdSITWEHLDQMPYTTMCIKEALR---LYPpvpgISRELSKPVTFPDGRSLPAGITVsls 343

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29171730 365 LYALGvvlQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLL 433
Cdd:cd20678 344 IYGLH---HNPAVWPNPEVFDPLRFSPENSSKrhSHAFLPFSaGPRNCIGQQFAMNEMKVAVALTLLRFELL 412
 
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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