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Conserved domains on  [gi|1707919355|ref|NP_001358632|]
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cytochrome P450 20A1 isoform 5 [Homo sapiens]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
1-229 3.05e-171

cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs with > 40% sequence identity are members of the same family. There are approximately 2250 CYP families: mammals, insects, plants, fungi, bacteria, and archaea have around 18, 208, 277, 805, 591, and 14 families, respectively. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle. CYPs use a variety of redox partners, such as the eukaryotic diflavin enzyme NADPH-cytochrome P450 oxidoreductase and the bacterial/mitochondrial NAD(P)H-ferredoxin reductase and ferredoxin partners. Some CYPs are naturally linked to their redox partners and others have evolved to bypass requirements for redox partners, and instead react directly with hydrogen peroxide or NAD(P)H to facilitate oxidative or reductive catalysis.


The actual alignment was detected with superfamily member cd20627:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 394  Bit Score: 476.62  E-value: 3.05e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQ 80
Cdd:cd20627   166 MEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQ 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  81 VFGNGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDR 160
Cdd:cd20627   246 VLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYRFDPDR 325
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707919355 161 FDDELVMKTFSSLGFSGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVTSSREEAWIT 229
Cdd:cd20627   326 FDDESVMKSFSLLGFSGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETKYELVTSPREEAWIT 394
 
Name Accession Description Interval E-value
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
1-229 3.05e-171

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: 476.62  E-value: 3.05e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQ 80
Cdd:cd20627   166 MEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQ 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  81 VFGNGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDR 160
Cdd:cd20627   246 VLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYRFDPDR 325
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707919355 161 FDDELVMKTFSSLGFSGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVTSSREEAWIT 229
Cdd:cd20627   326 FDDESVMKSFSLLGFSGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETKYELVTSPREEAWIT 394
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
1-218 2.19e-25

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: 103.13  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERKgRNFSQHI-----FIDSLV-------QGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSE 68
Cdd:pfam00067 214 KKIKDLLDKLIEERR-ETLDSAKksprdFLDALLlakeeedGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHP 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  69 EVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL------QDIegKIDRFIIPRETLVLYALG 141
Cdd:pfam00067 293 EVQEKLREEIDEVIGDKrSPTYDDLQNMPYLDAVIKETLR---LHPVVPLLlprevtKDT--VIPGYLIPKGTLVIVNLY 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 142 VVLQDPNTWPSPHKFDPDRFDDELVM--KTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYEL 218
Cdd:pfam00067 368 ALHRDPEVFPNPEEFDPERFLDENGKfrKSFAFLPFGaGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDET 447
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
59-210 5.52e-15

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 73.23  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDI-EGKIDRFIIPRETLV 136
Cdd:PLN02394  315 WGIAELVNHPEIQKKLRDELDTVLGPGnQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLeDAKLGGYDIPAESKI 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 137 LYALGVVLQDPNTWPSPHKFDPDRF-----DDELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 210
Cdd:PLN02394  395 LVNAWWLANNPELWKNPEEFRPERFleeeaKVEANGNDFRFLPFgVGRRSCPGIILALPILGIVLGRLVQNFELLPPPGQ 474
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
1-233 1.03e-11

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: 63.37  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERKGRnfSQHIFIDSLVQ-----GNLNDQQILedSMIFSLascII-----TAKLCTWAICFLTTSEEV 70
Cdd:COG2124   187 AELDAYLRELIAERRAE--PGDDLLSALLAarddgERLSDEELR--DELLLL---LLaghetTANALAWALYALLRHPEQ 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  71 QKKLYEEinqvfgngpvtPEKIEQ-----LRYCQHVLCeTVRTAKltpvsaqlQDIEgkIDRFIIPRETLVLYALGVVLQ 145
Cdd:COG2124   260 LARLRAE-----------PELLPAaveetLRLYPPVPL-LPRTAT--------EDVE--LGGVTIPAGDRVLLSLAAANR 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 146 DPNTWPSPHKFDPDRfddelvmKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLS-VEGQVIETKYELVTSSR 223
Cdd:COG2124   318 DPRVFPDPDRFDPDR-------PPNAHLPFGgGPHRCLGAALARLEARIALATLLRRFPDLRlAPPEELRWRPSLTLRGP 390
                         250
                  ....*....|
gi 1707919355 224 EEAWITVSKR 233
Cdd:COG2124   391 KSLPVRLRPR 400
 
Name Accession Description Interval E-value
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
1-229 3.05e-171

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: 476.62  E-value: 3.05e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQ 80
Cdd:cd20627   166 MEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQ 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  81 VFGNGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDR 160
Cdd:cd20627   246 VLGKGPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYRFDPDR 325
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707919355 161 FDDELVMKTFSSLGFSGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVTSSREEAWIT 229
Cdd:cd20627   326 FDDESVMKSFSLLGFSGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETKYELVTSPREEAWIT 394
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
1-220 1.21e-40

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: 143.04  E-value: 1.21e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERK---GRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEE 77
Cdd:cd00302   163 ARLRDYLEELIARRRaepADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLARHPEVQERLRAE 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  78 INQVFGNGpvTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPS 152
Cdd:cd00302   243 IDAVLGDG--TPEDLSKLPYLEAVVEETLR---LYPPVPLLprvatEDVE--LGGYTIPAGTLVLLSLYAAHRDPEVFPD 315
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707919355 153 PHKFDPDRFDDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVT 220
Cdd:cd00302   316 PDEFDPERFLPEREEPRYAHLPFGaGPHRCLGARLARLELKLALATLLRRFDFELVPDEELEWRPSLGT 384
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
8-228 1.68e-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: 113.77  E-value: 1.68e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   8 RNIIKERK------------GRNFSQ---HIFIDSLVQ-----GNLNDQQILE--DSMIF----SLASCIitaklcTWAI 61
Cdd:cd20628   180 NKVIKERReelkaekrnseeDDEFGKkkrKAFLDLLLEahedgGPLTDEDIREevDTFMFaghdTTASAI------SFTL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  62 CFLTTSEEVQKKLYEEINQVFGN--GPVTPEKIEQLRYCQHVLCETVRtakLTP----VSAQL-QDIegKIDRFIIPRET 134
Cdd:cd20628   254 YLLGLHPEVQEKVYEELDEIFGDddRRPTLEDLNKMKYLERVIKETLR---LYPsvpfIGRRLtEDI--KLDGYTIPKGT 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 135 ---LVLYALGvvlQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVE 208
Cdd:cd20628   329 tvvISIYALH---RNPEYFPDPEKFDPDRFLPENSAKrhPYAYIPFSaGPRNCIGQKFAMLEMKTLLAKILRNFRVLPVP 405
                         250       260
                  ....*....|....*....|.
gi 1707919355 209 -GQVIETKYELVTSSREEAWI 228
Cdd:cd20628   406 pGEDLKLIAEIVLRSKNGIRV 426
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
1-218 2.19e-25

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: 103.13  E-value: 2.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERKgRNFSQHI-----FIDSLV-------QGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSE 68
Cdd:pfam00067 214 KKIKDLLDKLIEERR-ETLDSAKksprdFLDALLlakeeedGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHP 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  69 EVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL------QDIegKIDRFIIPRETLVLYALG 141
Cdd:pfam00067 293 EVQEKLREEIDEVIGDKrSPTYDDLQNMPYLDAVIKETLR---LHPVVPLLlprevtKDT--VIPGYLIPKGTLVIVNLY 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 142 VVLQDPNTWPSPHKFDPDRFDDELVM--KTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYEL 218
Cdd:pfam00067 368 ALHRDPEVFPNPEEFDPERFLDENGKfrKSFAFLPFGaGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDET 447
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
2-213 5.00e-25

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: 101.50  E-value: 5.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNIIKERKGRNFSQHIFIDSLVQ-------GNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKL 74
Cdd:cd20620   170 RLDEVIYRLIAERRAAPADGGDLLSMLLAardeetgEPMSDQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARL 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  75 YEEINQVFGNGPVTPEKIEQLRYCQHVLCETVR---TAKLTPVSAqLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWP 151
Cdd:cd20620   250 RAEVDRVLGGRPPTAEDLPQLPYTEMVLQESLRlypPAWIIGREA-VEDDE--IGGYRIPAGSTVLISPYVTHRDPRFWP 326
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707919355 152 SPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIE 213
Cdd:cd20620   327 DPEAFDPERFTPEREAArpRYAYFPFGgGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPGQPVE 391
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
5-217 3.22e-24

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: 99.54  E-value: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   5 SVLRNIIKERKGRNFSQHIFIDSLVQ-------------GNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQ 71
Cdd:cd11056   184 KLVRDTIEYREKNNIVRNDFIDLLLElkkkgkieddkseKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQ 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  72 KKLYEEINQVF--GNGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIEGKIDRFIIPRETLVL---YALG 141
Cdd:cd11056   264 EKLREEIDEVLekHGGELTYEALQEMKYLDQVVNETLR---KYPPLPFLdrvctKDYTLPGTDVVIEKGTPVIipvYALH 340
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707919355 142 vvlQDPNTWPSPHKFDPDRFDDELV--MKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYE 217
Cdd:cd11056   341 ---HDPKYYPEPEKFDPERFSPENKkkRHPYTYLPFgDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPLKLS 416
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
3-223 8.00e-24

cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes vertebrate CYP3A subfamily enzymes and CYP5a1, and similar proteins. CYP5A1, also called thromboxane-A synthase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid. CYP3A enzymes are drug-metabolizing enzymes embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. The CYP3A-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410678 [Multi-domain]  Cd Length: 422  Bit Score: 98.43  E-value: 8.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERKGRNFSQH-----IFIDSLVQGN------LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQ 71
Cdd:cd11055   181 LEDVVKKIIEQRRKNKSSRRkdllqLMLDAQDSDEdvskkkLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQ 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  72 KKLYEEINQVFGN-GPVTPEKIEQLRYCQHVLCETVRtakL-TPVSAQ----LQDIEgkIDRFIIPRETLVL---YALGv 142
Cdd:cd11055   261 EKLIEEIDEVLPDdGSPTYDTVSKLKYLDMVINETLR---LyPPAFFIsrecKEDCT--INGVFIPKGVDVVipvYAIH- 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 143 vlQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEgqviETKYELV 219
Cdd:cd11055   335 --HDPEFWPDPEKFDPERFSPENKAKrhPYAYLPFGaGPRNCIGMRFALLEVKLALVKILQKFRFVPCK----ETEIPLK 408

                  ....
gi 1707919355 220 TSSR 223
Cdd:cd11055   409 LVGG 412
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
3-221 2.43e-22

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: 94.21  E-value: 2.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERKGRNFSQ-HIFIDSLVQG------NLNDQQILedSMIFSL------ASCIITAklctWAICFLTTSEE 69
Cdd:cd11042   171 LKEIFSEIIQKRRKSPDKDeDDMLQTLMDAkykdgrPLTDDEIA--GLLIALlfagqhTSSATSA----WTGLELLRNPE 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  70 VQKKLYEEINQVFG--NGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIEGKIDRFIIPRETLVLYALGV 142
Cdd:cd11042   245 HLEALREEQKEVLGdgDDPLTYDVLKEMPLLHACIKETLR---LHPPIHSLmrkarKPFEVEGGGYVIPKGHIVLASPAV 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 143 VLQDPNTWPSPHKFDPDRFDD---ELVMKTFSS-LGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYE 217
Cdd:cd11042   322 SHRDPEIFKNPDEFDPERFLKgraEDSKGGKFAyLPFgAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSPFPEPDYT 401

                  ....
gi 1707919355 218 LVTS 221
Cdd:cd11042   402 TMVV 405
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
53-208 2.55e-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: 94.25  E-value: 2.55e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  53 TAKLCTWAICFLTTSEEVQKKLYEEINQVFG--NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFII 130
Cdd:cd20660   248 TAAAINWALYLIGSHPEVQEKVHEELDRIFGdsDRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTI 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 131 PRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSV 207
Cdd:cd20660   328 PKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGrhPYAYIPFSaGPRNCIGQKFALMEEKVVLSSILRNFRIESV 407

                  .
gi 1707919355 208 E 208
Cdd:cd20660   408 Q 408
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
5-211 3.36e-22

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: 3.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   5 SVLRNIIKERKGRNFSQHI--FIDSLVQG-------NLNDQQILEDSMIFSLASCII------TAKLCTWAICFLTTSEE 69
Cdd:cd11027   182 EILRKKLEEHKETFDPGNIrdLTDALIKAkkeaedeGDEDSGLLTDDHLVMTISDIFgagtetTATTLRWAIAYLVNYPE 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  70 VQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEgkIDRFIIPRETLVLYALGVVLQ 145
Cdd:cd11027   262 VQAKLHAELDDVIGRDrLPTLSDRKRLPYLEATIAEVLRLSSVVPLAlphKTTCDTT--LRGYTIPKGTTVLVNLWALHH 339
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 146 DPNTWPSPHKFDPDRFDDE---LVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQV 211
Cdd:cd11027   340 DPKEWDDPDEFRPERFLDEngkLVPKPESFLPFSaGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEP 409
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
2-204 4.42e-22

cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect cytochrome P450s from families 313 (CYP313) and 318 (CYP318), and similar proteins. These proteins may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. Their specific function is yet unknown. They belong to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410680 [Multi-domain]  Cd Length: 427  Bit Score: 93.44  E-value: 4.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNIIKERKGR---------------NFSQHIFIDSLVQ-----GNLNDQQILE--DSMIFslASCIITAKLCTW 59
Cdd:cd11057   172 ILRAFSEKIIEKKLQEvelesnldseedeenGRKPQIFIDQLLElarngEEFTDEEIMDeiDTMIF--AGNDTSATTVAY 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  60 AICFLTTSEEVQKKLYEEINQVFGNG--PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQ--LQDIEgkIDR-FIIPRET 134
Cdd:cd11057   250 TLLLLAMHPEVQEKVYEEIMEVFPDDgqFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRetTADIQ--LSNgVVIPKGT 327
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707919355 135 LVLYALGVVLQDPNTW-PSPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHL 204
Cdd:cd11057   328 TIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQrhPYAFIPFSaGPRNCIGWRYAMISMKIMLAKILRNYRL 401
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
1-214 5.38e-21

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: 90.35  E-value: 5.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERKGRNFSQHI--FIDSLVQ----GNLNDQQILEDSMIFSLASCII-----TAKLCTWAICFLTTSEE 69
Cdd:cd20651   178 QKLIEFLKEEIKEHKKTYDEDNPrdLIDAYLRemkkKEPPSSSFTDDQLVMICLDLFIagsetTSNTLGFAFLYLLLNPE 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  70 VQKKLYEEINQVFGNG--PVTPEKIeQLRYCQHVLCETVRTAKLTPVSAQ---LQDIegKIDRFIIPRETLVLYALGVVL 144
Cdd:cd20651   258 VQRKVQEEIDEVVGRDrlPTLDDRS-KLPYTEAVILEVLRIFTLVPIGIPhraLKDT--TLGGYRIPKDTTILASLYSVH 334
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707919355 145 QDPNTWPSPHKFDPDRF--DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIET 214
Cdd:cd20651   335 MDPEYWGDPEEFRPERFldEDGKLLKDEWFLPFGaGKRRCLGESLARNELFLFFTGLLQNFTFSPPNGSLPDL 407
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
2-210 6.27e-21

cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate cytochrome P450 family 26 enzymes, and similar cytochrome P450s; This family includes cyanobacterial CYP120A1 and vertebrate cytochrome P450s 26A1 (CYP26A1), 26B1 (CYP26B1), and 26C1 (CYP26C1). These are retinoic acid-metabolizing cytochromes that play key roles in retinoic acid (RA) metabolism. Human and zebrafish CYP26a1, as well as Synechocystis CYP120A1 are characterized as RA hydroxylases. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 90.03  E-value: 6.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNIIKERKGRNfsQHIFIDSL--------VQGN-LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQK 72
Cdd:cd11044   181 KLLARLEQAIRERQEEE--NAEAKDALgllleakdEDGEpLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLE 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  73 KLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRTakLTPVSA----QLQDIEgkIDRFIIPRETLVLYALGVVLQDPN 148
Cdd:cd11044   259 KLRQEQDALGLEEPLTLESLKKMPYLDQVIKEVLRL--VPPVGGgfrkVLEDFE--LGGYQIPKGWLVYYSIRDTHRDPE 334
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707919355 149 TWPSPHKFDPDRF---DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 210
Cdd:cd11044   335 LYPDPERFDPERFspaRSEDKKKPFSLIPFGgGPRECLGKEFAQLEMKILASELLRNYDWELLPNQ 400
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
6-201 1.02e-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: 89.55  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   6 VLRNIIKERK--GRNFSQHI-FIDSLVQGNLNDQQILEDSMIFSLASCII------TAKLCTWAICFLTTSEEVQKKLYE 76
Cdd:cd11043   170 ELKKIIEERRaeLEKASPKGdLLDVLLEEKDEDGDSLTDEEILDNILTLLfaghetTSTTLTLAVKFLAENPKVLQELLE 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  77 E----INQVFGNGPVTPEKIEQLRYCQHVLCETVRTAklTPVSA----QLQDIEgkIDRFIIPRETLVLYALGVVLQDPN 148
Cdd:cd11043   250 EheeiAKRKEEGEGLTWEDYKSMKYTWQVINETLRLA--PIVPGvfrkALQDVE--YKGYTIPKGWKVLWSARATHLDPE 325
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1707919355 149 TWPSPHKFDPDRFDDELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKR 201
Cdd:cd11043   326 YFPDPLKFNPWRWEGKGKGVPYTFLPFgGGPRLCPGAELAKLEILVFLHHLVTR 379
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
33-195 1.87e-20

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: 89.01  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  33 LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGN-GPVTPEKIEQLRYCQHVLCETVRtakL 111
Cdd:cd20650   224 LSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNkAPPTYDTVMQMEYLDMVVNETLR---L 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 112 TPVSAQL-----QDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF----DDELVMKTFSSLGfSGTQECP 182
Cdd:cd20650   301 FPIAGRLervckKDVE--INGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFskknKDNIDPYIYLPFG-SGPRNCI 377
                         170
                  ....*....|...
gi 1707919355 183 ELRFAYMVTTVLL 195
Cdd:cd20650   378 GMRFALMNMKLAL 390
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
32-218 1.95e-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: 88.96  E-value: 1.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  32 NLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAK 110
Cdd:cd11046   235 DVDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRlPPTYEDLKKLKYTRRVLNESLRLYP 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 111 LTPVSAQLQDIEGKID--RFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDD------ELVMKTFSSLGFS-GTQEC 181
Cdd:cd11046   315 QPPVLIRRAVEDDKLPggGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDpfinppNEVIDDFAFLPFGgGPRKC 394
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1707919355 182 PELRFAYMVTTVLLSVLVKRL---------HLLSVEGQVIETKYEL 218
Cdd:cd11046   395 LGDQFALLEATVALAMLLRRFdfeldvgprHVGMTTGATIHTKNGL 440
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
32-210 2.72e-20

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: 88.51  E-value: 2.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  32 NLNDQQILEDSMIFSLASCIITAKLCT------WAICFLTTSEEVQKKLYEEINQVFGNGPV-TPEKIEQLRYCQHVLCE 104
Cdd:cd11028   220 EEKPEVGLTDEHIISTVQDLFGAGFDTisttlqWSLLYMIRYPEIQEKVQAELDRVIGRERLpRLSDRPNLPYTEAFILE 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 105 TVRTAKLTPVS---AQLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF--DDELVMKTFSS--LGFS- 176
Cdd:cd11028   300 TMRHSSFVPFTiphATTRDTT--LNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFldDNGLLDKTKVDkfLPFGa 377
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1707919355 177 GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 210
Cdd:cd11028   378 GRRRCLGEELARMELFLFFATLLQQCEFSVKPGE 411
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
1-204 2.48e-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: 82.76  E-value: 2.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQ 80
Cdd:cd11070   187 EVEAELSADSKGKQGTESVVASRLKRARRSGGLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDS 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  81 VFGNGP---VTPEKIEQLRYCQHVLCETVR-------TAKLTPVSAQLQDIEGKidRFIIPRETLVLYALGVVLQDPNTW 150
Cdd:cd11070   267 VLGDEPddwDYEEDFPKLPYLLAVIYETLRlyppvqlLNRKTTEPVVVITGLGQ--EIVIPKGTYVGYNAYATHRDPTIW 344
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1707919355 151 -PSPHKFDPDRFDDElVMKTFSS----------LGFS-GTQECPELRFAYMVTTVLLSVLVKRLHL 204
Cdd:cd11070   345 gPDADEFDPERWGST-SGEIGAAtrftpargafIPFSaGPRACLGRKFALVEFVAALAELFRQYEW 409
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
3-209 2.51e-18

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: 82.75  E-value: 2.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERKGRN----FSQHIFIDSLVQGNLNDQQILeDSMIFSL--ASCIITAKLCTWAIcFLTTSEEVQKKLYE 76
Cdd:cd11045   173 LEEYFRRRIPERRAGGgddlFSALCRAEDEDGDRFSDDDIV-NHMIFLMmaAHDTTTSTLTSMAY-FLARHPEWQERLRE 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  77 EInQVFGNGPVTPEKIEQLRYCQHVLCETVRTakLTPVSA----QLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPS 152
Cdd:cd11045   251 ES-LALGKGTLDYEDLGQLEVTDWVFKEALRL--VPPVPTlprrAVKDTE--VLGYRIPAGTLVAVSPGVTHYMPEYWPN 325
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1707919355 153 PHKFDPDRFDDEL----VMKtFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEG 209
Cdd:cd11045   326 PERFDPERFSPERaedkVHR-YAWAPFGgGAHKCIGLHFAGMEVKAILHQMLRRFRWWSVPG 386
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
53-222 5.26e-18

cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome P450 families 1 (CYP1) and 2 (CYP2), CYP17A1, and CYP21 in vertebrates, as well as insect and crustacean CYPs similar to CYP15A1 and CYP306A1. CYP1 and CYP2 enzymes are involved in the metabolism of endogenous and exogenous compounds such as hormones, xenobiotics, and drugs. CYP17A1 catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products, while CYP21 catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. Members of this group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410710 [Multi-domain]  Cd Length: 419  Bit Score: 81.88  E-value: 5.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  53 TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEgkIDRF 128
Cdd:cd20617   239 TSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDrRVTLSDRSKLPYLNAVIKEVLRLRPILPLGlprVTTEDTE--IGGY 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 129 IIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF-DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLS 206
Cdd:cd20617   317 FIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFlENDGNKLSEQFIPFGiGKRNCVGENLARDELFLFFANLLLNFKFKS 396
                         170
                  ....*....|....*..
gi 1707919355 207 VEGQVI-ETKYELVTSS 222
Cdd:cd20617   397 SDGLPIdEKEVFGLTLK 413
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
11-220 6.39e-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: 81.80  E-value: 6.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  11 IKERKGRNFSQHIFIDSLV-QGNLNDQQILedSMIFSL--ASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-P 86
Cdd:cd11054   204 LKKKDEEDEEEDSLLEYLLsKPGLSKKEIV--TMALDLllAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGeP 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  87 VTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF 161
Cdd:cd11054   282 ITAEDLKKMPYLKACIKESLR---LYPVAPGNgrilpKDIV--LSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERW 356
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707919355 162 ----DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQvIETKYELVT 220
Cdd:cd11054   357 lrddSENKNIHPFASLPFGfGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHEE-LKVKTRLIL 419
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
9-228 2.17e-16

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


Pssm-ID: 410752 [Multi-domain]  Cd Length: 423  Bit Score: 77.21  E-value: 2.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   9 NIIKERK---------GRNFSQHI-FIDSLVQ-----GN-LNDQQILE--DSMIF----SLASCIitaklcTWAICFLTT 66
Cdd:cd20659   183 EIIKKRRkelednkdeALSKRKYLdFLDILLTardedGKgLTDEEIRDevDTFLFaghdTTASGI------SWTLYSLAK 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  67 SEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQ 145
Cdd:cd20659   257 HPEHQQKCREEVDEVLGDRdDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHH 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 146 DPNTWPSPHKFDPDRFDDELV--MKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVTSS 222
Cdd:cd20659   337 NPTVWEDPEEFDPERFLPENIkkRDPFAFIPFSaGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNHPVEPKPGLVLRS 416

                  ....*.
gi 1707919355 223 REEAWI 228
Cdd:cd20659   417 KNGIKL 422
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
2-199 4.21e-16

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: 76.44  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNIIKERK------GRNFSQHIFIDSLVQgnLNDQQILEDSMIFSLASCII------TAKLCTWAICFLTTSEE 69
Cdd:cd20618   184 KLDRFLQKIIEEHRekrgesKKGGDDDDDLLLLLD--LDGEGKLSDDNIKALLLDMLaagtdtSAVTIEWAMAELLRHPE 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  70 VQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL------QDIegKIDRFIIPRETLVL---YA 139
Cdd:cd20618   262 VMRKAQEELDSVVGRErLVEESDLPKLPYLQAVVKETLR---LHPPGPLLlphestEDC--KVAGYDIPAGTRVLvnvWA 336
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707919355 140 LGvvlQDPNTWPSPHKFDPDRFDDELVMKT----FSSLGF-SGTQECPELRFAYMVTTVLLSVLV 199
Cdd:cd20618   337 IG---RDPKVWEDPLEFKPERFLESDIDDVkgqdFELLPFgSGRRMCPGMPLGLRMVQLTLANLL 398
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
33-220 5.69e-16

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: 76.08  E-value: 5.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  33 LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPvtPEKIEQLRYCQHVLCETVRtakLT 112
Cdd:cd11053   219 LSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPD--PEDIAKLPYLDAVIKETLR---LY 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 113 PVSAQL-----QDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDElvmkTFSS---LGFS-GTQECPE 183
Cdd:cd11053   294 PVAPLVprrvkEPVE--LGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGR----KPSPyeyLPFGgGVRRCIG 367
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1707919355 184 LRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVT 220
Cdd:cd11053   368 AAFALLEMKVVLATLLRRFRLELTDPRPERPVRRGVT 404
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
3-161 6.93e-16

cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is composed of CYPs from unicellular ciliates similar to Tetrahymena thermophila CYP5011A1, whose function is still unknown. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410714 [Multi-domain]  Cd Length: 427  Bit Score: 75.75  E-value: 6.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERKGR-------------NFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEE 69
Cdd:cd20621   182 LRQFIEKIIQNRIKQikknkdeikdiiiDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPE 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  70 VQKKLYEEINQVFGNGP-VTPEKIEQLRYCQHVLCETVRtakLTPVSAQL------QDIegKIDRFIIPRETLVLYALGV 142
Cdd:cd20621   262 IQEKLRQEIKSVVGNDDdITFEDLQKLNYLNAFIKEVLR---LYNPAPFLfprvatQDH--QIGDLKIKKGWIVNVGYIY 336
                         170
                  ....*....|....*....
gi 1707919355 143 VLQDPNTWPSPHKFDPDRF 161
Cdd:cd20621   337 NHFNPKYFENPDEFNPERW 355
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
33-230 7.28e-16

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: 75.76  E-value: 7.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  33 LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRtakLT 112
Cdd:cd11049   216 LSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLGGRPATFEDLPRLTYTRRVVTEALR---LY 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 113 PVSAQL-----QDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDE--LVMKTFSSLGFS-GTQECPEL 184
Cdd:cd11049   293 PPVWLLtrrttADVE--LGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGraAAVPRGAFIPFGaGARKCIGD 370
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1707919355 185 RFAYMVTTVLLSVLVKRLHLLSVEGqvietkyelvTSSREEAWITV 230
Cdd:cd11049   371 TFALTELTLALATIASRWRLRPVPG----------RPVRPRPLATL 406
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
8-202 1.13e-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: 75.36  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   8 RNIIKERKGRNFSQHIFIDSLVQGNLNDQQI-LEDSMIFSLASCIITAKLCT------WAICFLTTSEEVQKKLYEEINQ 80
Cdd:cd11075   195 RKRRASGEADKDYTDFLLLDLLDLKEEGGERkLTDEELVSLCSEFLNAGTDTtataleWAMAELVKNPEIQEKLYEEIKE 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  81 VFG-NGPVTPEKIEQLRYCQHVLCETVR---TAKLTPVSAQLQDIegKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKF 156
Cdd:cd11075   275 VVGdEAVVTEEDLPKMPYLKAVVLETLRrhpPGHFLLPHAVTEDT--VLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEF 352
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1707919355 157 DPDRF--DDELVMKTFSSLGFS------GTQECPELRFAymvtTVLLSVLVKRL 202
Cdd:cd11075   353 KPERFlaGGEAADIDTGSKEIKmmpfgaGRRICPGLGLA----TLHLELFVARL 402
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
40-216 5.25e-15

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: 5.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  40 EDSMI-----FSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTP 113
Cdd:cd20667   223 EENMIqvvidLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASqLICYEDRKRLPYTNAVIHEVQRLSNVVS 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 114 VSAQLQDIEGK-IDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF---DDELVMKTfSSLGFS-GTQECPELRFAY 188
Cdd:cd20667   303 VGAVRQCVTSTtMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFldkDGNFVMNE-AFLPFSaGHRVCLGEQLAR 381
                         170       180
                  ....*....|....*....|....*....
gi 1707919355 189 MVTTVLLSVLVKRLHLLSVEG-QVIETKY 216
Cdd:cd20667   382 MELFIFFTTLLRTFNFQLPEGvQELNLEY 410
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
59-210 5.52e-15

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 73.23  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDI-EGKIDRFIIPRETLV 136
Cdd:PLN02394  315 WGIAELVNHPEIQKKLRDELDTVLGPGnQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLeDAKLGGYDIPAESKI 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 137 LYALGVVLQDPNTWPSPHKFDPDRF-----DDELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 210
Cdd:PLN02394  395 LVNAWWLANNPELWKNPEEFRPERFleeeaKVEANGNDFRFLPFgVGRRSCPGIILALPILGIVLGRLVQNFELLPPPGQ 474
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
24-204 7.16e-15

cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 (CYP4V2) is the most characterized member of the CYP4V subfamily. It is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410773 [Multi-domain]  Cd Length: 440  Bit Score: 72.87  E-value: 7.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  24 FIDSLV-----QGN-LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG--PVTPEKIEQL 95
Cdd:cd20680   224 FLDMLLsvtdeEGNkLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSdrPVTMEDLKKL 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  96 RYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMK--TFSSL 173
Cdd:cd20680   304 RYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGrhPYAYI 383
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1707919355 174 GFS-GTQECPELRFAYMVTTVLLSVLVKRLHL 204
Cdd:cd20680   384 PFSaGPRNCIGQRFALMEEKVVLSCILRHFWV 415
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
4-210 8.02e-15

cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or Cyp17a1), also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. It is a dual enzyme that catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reactions. Severe mutations on the enzyme cause combined 17-hydroxylase/17,20-lyase deficiency (17OHD); patients with 17OHD synthesize 11-deoxycorticosterone (DOC) which causes hypertension and hypokalemia. Loss of 17,20-lyase activity precludes sex steroid synthesis and leads to sexual infantilism. Included in this group is a second 17A P450 from teleost fish, CYP17A2, that is more efficient in pregnenolone 17-alpha-hydroxylation than CYP17A1, but does not catalyze the lyase reaction. CYP17A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 72.74  E-value: 8.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   4 ESVLRNIIKERKgRNFSQHI---FIDSLVQGNLN----------DQQILEDSMIFSLASCIITAKLCT------WAICFL 64
Cdd:cd20673   181 DKLLQKKLEEHK-EKFSSDSirdLLDALLQAKMNaennnagpdqDSVGLSDDHILMTVGDIFGAGVETtttvlkWIIAFL 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  65 TTSEEVQKKLYEEINQV--FGNGPVTPEKiEQLRYCQHVLCETVRtakLTPVSAQL----QDIEGKIDRFIIPRETLVLY 138
Cdd:cd20673   260 LHNPEVQKKIQEEIDQNigFSRTPTLSDR-NHLPLLEATIREVLR---IRPVAPLLiphvALQDSSIGEFTIPKGTRVVI 335
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707919355 139 ALGVVLQDPNTWPSPHKFDPDRFDDE----LVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 210
Cdd:cd20673   336 NLWALHHDEKEWDQPDQFMPERFLDPtgsqLISPSLSYLPFgAGPRVCLGEALARQELFLFMAWLLQRFDLEVPDGG 412
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
3-164 8.45e-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: 72.60  E-value: 8.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERKgRNFSQHIfiDSLVQGNLN------DQQILEDSMIFSLASCII-----TAKLCTWAICFLTTSEEVQ 71
Cdd:cd11068   188 MRDLVDEIIAERR-ANPDGSP--DDLLNLMLNgkdpetGEKLSDENIRYQMITFLIaghetTSGLLSFALYYLLKNPEVL 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  72 KKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVR---TAKLTPVSAqLQD--IEGKIDrfiIPRETLVLYALGVVLQD 146
Cdd:cd11068   265 AKARAEVDEVLGDDPPPYEQVAKLRYIRRVLDETLRlwpTAPAFARKP-KEDtvLGGKYP---LKKGDPVLVLLPALHRD 340
                         170
                  ....*....|....*....
gi 1707919355 147 PNTW-PSPHKFDPDRFDDE 164
Cdd:cd11068   341 PSVWgEDAEEFRPERFLPE 359
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
6-209 1.15e-14

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: 72.14  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   6 VLRNIIKERKgRNFSQ---HIFIDSLVQ---------GNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKK 73
Cdd:cd20671   181 ILRTLIEARR-PTIDGnplHSYIEALIQkqeeddpkeTLFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKR 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  74 LYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPS 152
Cdd:cd20671   260 VQEEIDRVLGPGcLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWET 339
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 153 PHKFDPDRFDDE--LVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEG 209
Cdd:cd20671   340 PYQFNPNHFLDAegKFVKKEAFLPFSaGRRVCVGESLARTELFIFFTGLLQKFTFLPPPG 399
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
22-210 1.75e-14

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: 71.73  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  22 HIfIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPE-KIEQLRYCQH 100
Cdd:cd11074   219 HI-LDAQKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEpDLHKLPYLQA 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 101 VLCETVRTAKLTPVSAQLQDI-EGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDE-----LVMKTFSSLG 174
Cdd:cd11074   298 VVKETLRLRMAIPLLVPHMNLhDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEeskveANGNDFRYLP 377
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1707919355 175 FS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 210
Cdd:cd11074   378 FGvGRRSCPGIILALPILGITIGRLVQNFELLPPPGQ 414
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
59-210 2.69e-14

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: 2.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFGnGP--VTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEgkIDRFIIPRE 133
Cdd:cd20652   256 WFLLYMALFPKEQRRIQRELDEVVG-RPdlVTLEDLSSLPYLQACISESQRIRSVVPLGiphGCTEDAV--LAGYRIPKG 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 134 TLVLYALGVVLQDPNTWPSPHKFDPDRF--DDELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 210
Cdd:cd20652   333 SMIIPLLWAVHMDPNLWEEPEEFRPERFldTDGKYLKPEAFIPFqTGKRMCLGDELARMILFLFTARILRKFRIALPDGQ 412
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
59-164 4.66e-14

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: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIE--GkidrFIIPR 132
Cdd:cd11026   248 WALLLLMKYPHIQEKVQEEIDRVIGrNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGvphAVTRDTKfrG----YTIPK 323
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1707919355 133 ETLVLYALGVVLQDPNTWPSPHKFDPDRFDDE 164
Cdd:cd11026   324 GTTVIPNLTSVLRDPKQWETPEEFNPGHFLDE 355
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
1-202 7.36e-14

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: 70.06  E-value: 7.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERK-------GRNFSqHIFIDSLVQGNLND--------QQILEDSMIFSLASCIITAKLCTWAICFLT 65
Cdd:cd11052   182 KEIEDSLLEIIKKREdslkmgrGDDYG-DDLLGLLLEANQSDdqnknmtvQEIVDECKTFFFAGHETTALLLTWTTMLLA 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  66 TSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQLQ-----DIegKIDRFIIPRETLVLYAL 140
Cdd:cd11052   261 IHPEWQEKAREEVLEVCGKDKPPSDSLSKLKTVSMVINESLR---LYPPAVFLTrkakeDI--KLGGLVIPKGTSIWIPV 335
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707919355 141 GVVLQDPNTWPS-PHKFDPDRFDDELVMKTFSSLGF----SGTQECPELRFAYMVTTVLLSVLVKRL 202
Cdd:cd11052   336 LALHHDEEIWGEdANEFNPERFADGVAKAAKHPMAFlpfgLGPRNCIGQNFATMEAKIVLAMILQRF 402
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
3-222 7.37e-14

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: 69.99  E-value: 7.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERK-----GRNFSQHIFIDSLVQGN-------LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEV 70
Cdd:cd11069   189 LRRLAREIIREKKaalleGKDDSGKDILSILLRANdfadderLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDV 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  71 QKKLYEEINQVF---GNGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL-----QDIegKIDRFIIPRETLVLYALGV 142
Cdd:cd11069   269 QERLREEIRAALpdpPDGDLSYDDLDRLPYLNAVCRETLR---LYPPVPLTsreatKDT--VIKGVPIPKGTVVLIPPAA 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 143 VLQDPNTW-PSPHKFDPDRFDDELV------------MKTFSslgfSGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEG 209
Cdd:cd11069   344 INRSPEIWgPDAEEFNPERWLEPDGaaspggagsnyaLLTFL----HGPRSCIGKKFALAEMKVLLAALVSRFEFELDPD 419
                         250
                  ....*....|...
gi 1707919355 210 QVIETKYELVTSS 222
Cdd:cd11069   420 AEVERPIGIITRP 432
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
59-198 1.23e-13

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: 69.10  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRtakLTPVSAQL------QDIEgkIDRFIIP 131
Cdd:cd11073   253 WAMAELLRNPEKMAKARAELDEVIGKDKIVEESdISKLPYLQAVVKETLR---LHPPAPLLlprkaeEDVE--VMGYTIP 327
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707919355 132 RETLVL---YALGvvlQDPNTWPSPHKFDPDRF-DDELVMK--TFSSLGF-SGTQECPELRFAY-MVTTVLLSVL 198
Cdd:cd11073   328 KGTQVLvnvWAIG---RDPSVWEDPLEFKPERFlGSEIDFKgrDFELIPFgSGRRICPGLPLAErMVHLVLASLL 399
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
33-208 1.24e-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: 69.48  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  33 LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINqVFGNGPVTPE--KIEQLRYCQHVLCETVR--- 107
Cdd:cd20649   257 LTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVD-EFFSKHEMVDyaNVQELPYLDMVIAETLRmyp 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 108 -TAKLTPVSAQLQDIEGKIdrfiIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGF-SGTQECPE 183
Cdd:cd20649   336 pAFRFAREAAEDCVVLGQR----IPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRrhPFVYLPFgAGPRSCIG 411
                         170       180
                  ....*....|....*....|....*
gi 1707919355 184 LRFAYMVTTVLLSVLVKRLHLLSVE 208
Cdd:cd20649   412 MRLALLEIKVTLLHILRRFRFQACP 436
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
2-178 1.59e-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: 69.03  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLAS--CII----------TAKLCTWAICFLTTSEE 69
Cdd:cd11072   181 ELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEFPLTRDNikAIIldmflagtdtSATTLEWAMTELIRNPR 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  70 VQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQL------QDIegKIDRFIIPRETLVL---YA 139
Cdd:cd11072   261 VMKKAQEEVREVVGgKGKVTEEDLEKLKYLKAVIKETLR---LHPPAPLLlprecrEDC--KINGYDIPAKTRVIvnaWA 335
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1707919355 140 LGvvlQDPNTWPSPHKFDPDRFDDelvmktfSSLGFSGT 178
Cdd:cd11072   336 IG---RDPKYWEDPEEFRPERFLD-------SSIDFKGQ 364
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
8-218 1.67e-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: 68.70  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   8 RNIIKER-----KGRNFSQ----HIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEI 78
Cdd:cd20613   196 RECIEERlealkRGEEVPNdiltHILKASEEEPDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEV 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  79 NQVFGNGP-VTPEKIEQLRYCQHVLCETVRtakLTPVSAQLQDI---EGKIDRFIIPRETLVL---YALGvvlQDPNTWP 151
Cdd:cd20613   276 DEVLGSKQyVEYEDLGKLEYLSQVLKETLR---LYPPVPGTSREltkDIELGGYKIPAGTTVLvstYVMG---RMEEYFE 349
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 152 SPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYEL 218
Cdd:cd20613   350 DPLKFDPERFSPEAPEKipSYAYFPFSlGPRSCIGQQFAQIEAKVILAKLLQNFKFELVPGQSFGILEEV 419
PLN02302 PLN02302
ent-kaurenoic acid oxidase
33-182 2.41e-13

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 68.59  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  33 LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-----IEQLRYCQHVLCETVR 107
Cdd:PLN02302  283 LDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKKRPPGQKGltlkdVRKMEYLSQVIDETLR 362
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707919355 108 TAKLTPVSAQ--LQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVmKTFSSLGFS-GTQECP 182
Cdd:PLN02302  363 LINISLTVFReaKTDVE--VNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTP-KAGTFLPFGlGSRLCP 437
PLN02290 PLN02290
cytokinin trans-hydroxylase
1-201 6.79e-13

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 67.15  E-value: 6.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERK-----GRNFS----------QHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLT 65
Cdd:PLN02290  265 GEVERLLMEIIQSRRdcveiGRSSSygddllgmllNEMEKKRSNGFNLNLQLIMDECKTFFFAGHETTALLLTWTLMLLA 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  66 TSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVR---TAKLTPVSAqLQDIegKIDRFIIPRETLVLYALGV 142
Cdd:PLN02290  345 SNPTWQDKVRAEVAEVCGGETPSVDHLSKLTLLNMVINESLRlypPATLLPRMA-FEDI--KLGDLHIPKGLSIWIPVLA 421
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707919355 143 VLQDPNTW-PSPHKFDPDRFddelVMKTFSSLGF-----SGTQECPELRFAYMVTTVLLSVLVKR 201
Cdd:PLN02290  422 IHHSEELWgKDANEFNPDRF----AGRPFAPGRHfipfaAGPRNCIGQAFAMMEAKIILAMLISK 482
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
30-208 7.22e-13

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: 7.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  30 QGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTP--EKIEQLRYCQHVLCETVR 107
Cdd:cd11083   215 DARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPllEALDRLPYLEAVARETLR 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 108 takLTPVSAQL-----QDieGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF---DDELVMKTFSS-LGF-SG 177
Cdd:cd11083   295 ---LKPVAPLLflepnED--TVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWldgARAAEPHDPSSlLPFgAG 369
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1707919355 178 TQECPELRFAYMVTTVLLSVLVKRLHLLSVE 208
Cdd:cd11083   370 PRLCPGRSLALMEMKLVFAMLCRNFDIELPE 400
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
19-164 7.47e-13

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


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 67.14  E-value: 7.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  19 FSQHIFIDSLvqgnLNDQQILEDSM---------IFSLASCI-----ITAKLCTWAICFLTTSEEVQKKLYEEINQVFGN 84
Cdd:cd20664   197 NDQRGFIDAF----LVKQQEEEESSdsffhddnlTCSVGNLFgagtdTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGS 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  85 GPVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIegKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF 161
Cdd:cd20664   273 RQPQVEHRKNMPYTDAVIHEIQRFANIVPMNlphATTRDV--TFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHF 350

                  ...
gi 1707919355 162 DDE 164
Cdd:cd20664   351 LDS 353
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
59-199 9.07e-13

cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in flowering plants and could be classified into ten subfamilies, CYP93A-K. CYP93A appears to be the ancestor that was derived in flowering plants, and the remaining subfamiles show lineage-specific distribution: CYP93B and CYP93C are present in dicots; CYP93F is distributed only in Poaceae; CYP93G and CYP93J are monocot-specific; CYP93E is unique to legumes; CYP93H and CYP93K are only found in Aquilegia coerulea; and CYP93D is Brassicaceae-specific. Members of this family include: Glycyrrhiza echinata CYP93B1, also called licodione synthase (EC 1.14.14.140), that catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively; and Glycine max CYP93A1, also called 3,9-dihydroxypterocarpan 6A-monooxygenase (EC 1.14.14.93), that is involved in the biosynthesis of the phytoalexin glyceollin. CYP93 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 66.85  E-value: 9.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVL 137
Cdd:cd20655   250 WAMAELINNPEVLEKAREEIDSVVGKTRLVQESdLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKTTLF 329
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707919355 138 ---YALGvvlQDPNTWPSPHKFDPDRF--------DDELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLV 199
Cdd:cd20655   330 vnvYAIM---RDPNYWEDPLEFKPERFlassrsgqELDVRGQHFKLLPFgSGRRGCPGASLAYQVVGTAIAAMV 400
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
4-198 2.55e-12

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: 65.58  E-value: 2.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   4 ESVLRNIIKE----RKGRNFSQHiFIDSLVqgNLNDQQILEDSMIFSLASCIITAKLCT------WAICFLTTSEEVQKK 73
Cdd:cd20656   190 DRLTKAIMEEhtlaRQKSGGGQQ-HFVALL--TLKEQYDLSEDTVIGLLWDMITAGMDTtaisveWAMAEMIRNPRVQEK 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  74 LYEEINQVFGNGPVTPE-KIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEG-KIDRFIIPRETLVLYALGVVLQDPNTWP 151
Cdd:cd20656   267 AQEELDRVVGSDRVMTEaDFPQLPYLQCVVKEALRLHPPTPLMLPHKASENvKIGGYDIPKGANVHVNVWAIARDPAVWK 346
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1707919355 152 SPHKFDPDRFDDELV-MK--TFSSLGF-SGTQECPELRFAY-MVTTVLLSVL 198
Cdd:cd20656   347 NPLEFRPERFLEEDVdIKghDFRLLPFgAGRRVCPGAQLGInLVTLMLGHLL 398
PLN02687 PLN02687
flavonoid 3'-monooxygenase
53-161 3.73e-12

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 65.22  E-value: 3.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  53 TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVS-AQLQDIEGKIDRFII 130
Cdd:PLN02687  313 TSSTVEWAIAELIRHPDILKKAQEELDAVVGRDrLVSESDLPQLTYLQAVIKETFRLHPSTPLSlPRMAAEECEINGYHI 392
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1707919355 131 PRETLVLYALGVVLQDPNTWPSPHKFDPDRF 161
Cdd:PLN02687  393 PKGATLLVNVWAIARDPEQWPDPLEFRPDRF 423
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
3-219 6.22e-12

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: 64.15  E-value: 6.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERKGRNF----SQHI---FIDS-LVQGNLNDQQILEDSMI-FSLASCIITAKLCTWAICFLTTSEEVQKK 73
Cdd:cd11064   187 VYEVISRRREELNSREEennvREDLlsrFLASeEEEGEPVSDKFLRDIVLnFILAGRDTTAAALTWFFWLLSKNPRVEEK 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  74 LYEEINQV----FGNGPV--TPEKIEQLRYCQHVLCETVRtakLTPVSAqlqdIEGKI--------DRFIIPRETLVL-- 137
Cdd:cd11064   267 IREELKSKlpklTTDESRvpTYEELKKLVYLHAALSESLR---LYPPVP----FDSKEavnddvlpDGTFVKKGTRIVys 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 138 -YALGVVlqdPNTW-PSPHKFDPDRF-DDELVMKTFSSLGFS----GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 210
Cdd:cd11064   340 iYAMGRM---ESIWgEDALEFKPERWlDEDGGLRPESPYKFPafnaGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGH 416

                  ....*....
gi 1707919355 211 VIETKYELV 219
Cdd:cd11064   417 KVEPKMSLT 425
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
23-177 8.75e-12

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: 63.73  E-value: 8.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  23 IFIDSLVQgNLNDQQILEDSM--IFsLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGP-VTPEKIEQLRYCQ 99
Cdd:cd11063   202 VFLDELAK-ETRDPKELRDQLlnIL-LAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPtPTYEDLKNMKYLR 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 100 HVLCETVRtakLTPVSAQ-----LQD--------IEGKIDRFiIPRETLVLYALGVVLQDPNTW-PSPHKFDPDRFDDeL 165
Cdd:cd11063   280 AVINETLR---LYPPVPLnsrvaVRDttlprgggPDGKSPIF-VPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWED-L 354
                         170
                  ....*....|..
gi 1707919355 166 VMKTFSSLGFSG 177
Cdd:cd11063   355 KRPGWEYLPFNG 366
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
10-181 8.83e-12

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: 63.66  E-value: 8.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  10 IIKERKGRNFSQ-HIFIDSLVQGNLNDQQ----ILEDSMIFS-----LASCIITAKLCTWAICFLTTSEEVQKKLYEEIN 79
Cdd:cd20662   188 IDKHREDWNPDEpRDFIDAYLKEMAKYPDpttsFNEENLICStldlfFAGTETTSTTLRWALLYMALYPEIQEKVQAEID 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  80 QVFGNG--PVTPEKiEQLRYCQHVLCETVRTAKLTPVSAQLQ-DIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKF 156
Cdd:cd20662   268 RVIGQKrqPSLADR-ESMPYTNAVIHEVQRMGNIIPLNVPREvAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTF 346
                         170       180
                  ....*....|....*....|....*..
gi 1707919355 157 DPDRF-DDELVMKTFSSLGFS-GTQEC 181
Cdd:cd20662   347 NPGHFlENGQFKKREAFLPFSmGKRAC 373
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
3-189 9.55e-12

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: 63.64  E-value: 9.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERKGR--NFSQHIFIDSLV------QGNLNDQQILEDSMIFSLASCII-----TAKLCTWAICFLTTSEE 69
Cdd:cd20666   181 ITAFLKKIIADHRETldPANPRDFIDMYLlhieeeQKNNAESSFNEDYLFYIIGDLFIagtdtTTNTLLWCLLYMSLYPE 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  70 VQKKLYEEINQVFGNG--PVTPEKiEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDR-FIIPRETLVLYALGVVLQD 146
Cdd:cd20666   261 VQEKVQAEIDTVIGPDraPSLTDK-AQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQgYTIPKGTVIVPNLWSVHRD 339
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1707919355 147 PNTWPSPHKFDPDRFDDE--LVMKTFSSLGFS-GTQECPELRFAYM 189
Cdd:cd20666   340 PAIWEKPDDFMPSRFLDEngQLIKKEAFIPFGiGRRVCMGEQLAKM 385
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
1-233 1.03e-11

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: 63.37  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERKGRnfSQHIFIDSLVQ-----GNLNDQQILedSMIFSLascII-----TAKLCTWAICFLTTSEEV 70
Cdd:COG2124   187 AELDAYLRELIAERRAE--PGDDLLSALLAarddgERLSDEELR--DELLLL---LLaghetTANALAWALYALLRHPEQ 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  71 QKKLYEEinqvfgngpvtPEKIEQ-----LRYCQHVLCeTVRTAKltpvsaqlQDIEgkIDRFIIPRETLVLYALGVVLQ 145
Cdd:COG2124   260 LARLRAE-----------PELLPAaveetLRLYPPVPL-LPRTAT--------EDVE--LGGVTIPAGDRVLLSLAAANR 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 146 DPNTWPSPHKFDPDRfddelvmKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLS-VEGQVIETKYELVTSSR 223
Cdd:COG2124   318 DPRVFPDPDRFDPDR-------PPNAHLPFGgGPHRCLGAALARLEARIALATLLRRFPDLRlAPPEELRWRPSLTLRGP 390
                         250
                  ....*....|
gi 1707919355 224 EEAWITVSKR 233
Cdd:COG2124   391 KSLPVRLRPR 400
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
4-182 1.55e-11

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: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   4 ESVLRNIIKERK--GRNFSQHIFIDSLVQGNLNDQQILEDS-MIFSLASCII-----TAKLCTWAICFLTTSEEVQKKLY 75
Cdd:cd11076   183 NTFVGKIIEEHRakRSNRARDDEDDVDVLLSLQGEEKLSDSdMIAVLWEMIFrgtdtVAILTEWIMARMVLHPDIQSKAQ 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  76 EEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRtakLTP----VS-AQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNT 149
Cdd:cd11076   263 AEIDAAVGgSRRVADSDVAKLPYLQAVVKETLR---LHPpgplLSwARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHV 339
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1707919355 150 WPSPHKFDPDRFDDELVMKTFSSLG-------F-SGTQECP 182
Cdd:cd11076   340 WEDPLEFKPERFVAAEGGADVSVLGsdlrlapFgAGRRVCP 380
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
2-206 1.93e-11

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 63.03  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNIIKERKGRNFSQHIFIDSLV--QGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEIN 79
Cdd:PLN02196  227 ELAQILAKILSKRRQNGSSHNDLLGSFMgdKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQM 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  80 QVFGNGP----VTPEKIEQLRYCQHVLCETVRTAKLTPVSAQ--LQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSP 153
Cdd:PLN02196  307 AIRKDKEegesLTWEDTKKMPLTSRVIQETLRVASILSFTFReaVEDVE--YEGYLIPKGWKVLPLFRNIHHSADIFSDP 384
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1707919355 154 HKFDPDRFDDELVMKTFSSLGfSGTQECPELRFAYMVTTVLLSVLVK--RLHLLS 206
Cdd:PLN02196  385 GKFDPSRFEVAPKPNTFMPFG-NGTHSCPGNELAKLEISVLIHHLTTkyRWSIVG 438
PLN02738 PLN02738
carotene beta-ring hydroxylase
32-201 2.20e-11

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 63.01  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  32 NLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRTAKL 111
Cdd:PLN02738  386 DVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTRVINESLRLYPQ 465
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 112 TPV----SAQlQDIEGKidrFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF-----DDELVMKTFSSLGF-SGTQEC 181
Cdd:PLN02738  466 PPVlirrSLE-NDMLGG---YPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpldgpNPNETNQNFSYLPFgGGPRKC 541
                         170       180
                  ....*....|....*....|
gi 1707919355 182 PELRFAYMVTTVLLSVLVKR 201
Cdd:PLN02738  542 VGDMFASFENVVATAMLVRR 561
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
7-161 2.98e-11

cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the biosynthesis of colored class of flavonoids, anthocyanins, which confer a diverse range of colors to flowers from orange to red to violet and blue. The number of hydroxyl groups on the B-ring of anthocyanidins, the chromophores and precursors of anthocyanins, impact the anthocyanin color - the more the bluer. The hydroxylation pattern is determined by CYP75 proteins: flavonoid 3'-hydroxylase (F3'H, EC 1.14.14.82) and and flavonoid 3',5'-hydroxylase (F3'5'H, EC 1.14.14.81), which belong to CYP75B and CYP75A subfamilies, respectively. Both enzymes have broad substrate specificity and catalyze the hydroxylation of flavanones, dihydroflavonols, flavonols and flavones. F3'H catalyzes the 3'-hydroxylation of the flavonoid B-ring to the 3',4'-hydroxylated state. F3'5'H catalysis leads to trihydroxylated delphinidin-based anthocyanins that tend to have violet/blue colours. CYP75 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 62.44  E-value: 2.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   7 LRNIIKERKGRNFSQHI---FIDSLVQGNL--NDQQILEDSMIFSLASCIITAKLCT------WAICFLTTSEEVQKKLY 75
Cdd:cd20657   187 LTKILEEHKATAQERKGkpdFLDFVLLENDdnGEGERLTDTNIKALLLNLFTAGTDTssstveWALAELIRHPDILKKAQ 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  76 EEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEG-KIDRFIIPRETLVLYALGVVLQDPNTWPSP 153
Cdd:cd20657   267 EEMDQVIGrDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEAcEVDGYYIPKGTRLLVNIWAIGRDPDVWENP 346

                  ....*...
gi 1707919355 154 HKFDPDRF 161
Cdd:cd20657   347 LEFKPERF 354
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
58-164 5.02e-11

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: 5.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  58 TWAICFLTTSEEVQKKLYEEINQVFGNGPV-TPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEgkIDRFIIPRE 133
Cdd:cd20675   256 QWILLLLVRYPDVQARLQEELDRVVGRDRLpCIEDQPNLPYVMAFLYEAMRFSSFVPVTiphATTADTS--ILGYHIPKD 333
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1707919355 134 TLVLYALGVVLQDPNTWPSPHKFDPDRFDDE 164
Cdd:cd20675   334 TVVFVNQWSVNHDPQKWPNPEVFDPTRFLDE 364
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
2-208 7.23e-11

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: 61.12  E-value: 7.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNiiKERKGRNFSQHIFIDSLVQGNLN-----DQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYE 76
Cdd:cd11062   186 QVDEVLRQ--VSAGDPPSIVTSLFHALLNSDLPpsektLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLRE 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  77 EINQVF--GNGPVTPEKIEQLRYCQHVLCETVRTAklTPVSAQLQDI---EG-KIDRFIIPRETLVLYALGVVLQDPNTW 150
Cdd:cd11062   264 ELKTAMpdPDSPPSLAELEKLPYLTAVIKEGLRLS--YGVPTRLPRVvpdEGlYYKGWVIPPGTPVSMSSYFVHHDEEIF 341
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1707919355 151 PSPHKFDPDRF---DDELVMKTFsSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVE 208
Cdd:cd11062   342 PDPHEFRPERWlgaAEKGKLDRY-LVPFSkGSRSCLGINLAYAELYLALAALFRRFDLELYE 402
PLN02655 PLN02655
ent-kaurene oxidase
5-164 9.12e-11

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 60.91  E-value: 9.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   5 SVLRNIIKERKGRNFS---QHIFIDSLVQGN--LNDQQI---LEDSMIFSLASCIITAKlctWAICFLTTSEEVQKKLYE 76
Cdd:PLN02655  225 AVMKALIKQQKKRIARgeeRDCYLDFLLSEAthLTDEQLmmlVWEPIIEAADTTLVTTE---WAMYELAKNPDKQERLYR 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  77 EINQVFGNGPVTPEKIEQLRYCQHVLCETVRT---AKLTPVSAQLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSP 153
Cdd:PLN02655  302 EIREVCGDERVTEEDLPNLPYLNAVFHETLRKyspVPLLPPRFVHEDTT--LGGYDIPAGTQIAINIYGCNMDKKRWENP 379
                         170
                  ....*....|.
gi 1707919355 154 HKFDPDRFDDE 164
Cdd:PLN02655  380 EEWDPERFLGE 390
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
59-199 9.21e-11

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: 60.70  E-value: 9.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRtakLTPVSAQL------QDIegKIDRFIIP 131
Cdd:cd20653   249 WAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESdLPKLPYLQNIISETLR---LYPAAPLLvphessEDC--KIGGYDIP 323
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707919355 132 RETLVLYALGVVLQDPNTWPSPHKFDPDRFDDElVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLV 199
Cdd:cd20653   324 RGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGE-EREGYKLIPFgLGRRACPGAGLAQRVVGLALGSLI 391
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
41-218 9.30e-11

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: 60.98  E-value: 9.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  41 DSMIFSLASCII-----TAKLCTWAICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPV 114
Cdd:cd20661   237 ENLIFSVGELIIagtetTTNVLRWAILFMALYPNIQGQVQKEIDLVVGpNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPL 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 115 SAQLQDIEGKIDR-FIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDE--LVMKTFSSLGFS-GTQECPELRFAYMV 190
Cdd:cd20661   317 GIFHATSKDAVVRgYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSngQFAKKEAFVPFSlGRRHCLGEQLARME 396
                         170       180
                  ....*....|....*....|....*...
gi 1707919355 191 TTVLLSVLVKRLHLLSVEGQVIETKYEL 218
Cdd:cd20661   397 MFLFFTALLQRFHLHFPHGLIPDLKPKL 424
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
7-164 1.08e-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: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   7 LRNIIKE-RKGRNFSQHI--FIDSLV------QGN----LNDQQI-LEDSMIFSlASCIITAKLCTWAICFLTTSEEVQK 72
Cdd:cd20663   187 LDELLTEhRTTWDPAQPPrdLTDAFLaemekaKGNpessFNDENLrLVVADLFS-AGMVTTSTTLSWALLLMILHPDVQR 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  73 KLYEEINQVFGNGPvTPEKIEQLR--YCQHVLCETVRTAKLTPVSA---QLQDIEgkIDRFIIPRETLVLYALGVVLQDP 147
Cdd:cd20663   266 RVQQEIDEVIGQVR-RPEMADQARmpYTNAVIHEVQRFGDIVPLGVphmTSRDIE--VQGFLIPKGTTLITNLSSVLKDE 342
                         170
                  ....*....|....*..
gi 1707919355 148 NTWPSPHKFDPDRFDDE 164
Cdd:cd20663   343 TVWEKPLRFHPEHFLDA 359
PLN02936 PLN02936
epsilon-ring hydroxylase
36-233 1.09e-10

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 60.58  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  36 QQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRTAKLTPV- 114
Cdd:PLN02936  277 VQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDIKELKYLTRCINESMRLYPHPPVl 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 115 --SAQLQDIEGKidRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMKTFSSLGF------SGTQECPELRF 186
Cdd:PLN02936  357 irRAQVEDVLPG--GYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETNTDFryipfsGGPRKCVGDQF 434
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1707919355 187 AYMVTTVLLSVLVKRLHLLSVEGQVIETKYELVTSSREEAWITVSKR 233
Cdd:PLN02936  435 ALLEAIVALAVLLQRLDLELVPDQDIVMTTGATIHTTNGLYMTVSRR 481
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
28-201 1.16e-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: 60.44  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  28 LVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPV-TPEKIEQLRYCQHVLCETV 106
Cdd:cd20646   224 LSSGKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIpTAEDIAKMPLLKAVIKETL 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 107 RTAKLTPVSAQL-QDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF--DDELVMKTFSSLGFS-GTQECP 182
Cdd:cd20646   304 RLYPVVPGNARViVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWlrDGGLKHHPFGSIPFGyGVRACV 383
                         170
                  ....*....|....*....
gi 1707919355 183 ELRFAYMVTTVLLSVLVKR 201
Cdd:cd20646   384 GRRIAELEMYLALSRLIKR 402
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
3-161 1.24e-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: 60.28  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERKGRNFSQHifidsLVQGNLNDQQILEDSMIFSLASCII-----TAKLCTWAICFLTTSEEVQKKLYEE 77
Cdd:cd11065   189 FEAAKERMASGTATPSFVKD-----LLEELDKEGGLSEEEIKYLAGSLYEagsdtTASTLQTFILAMALHPEVQKKAQEE 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  78 INQVFGNG-PVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSP 153
Cdd:cd11065   264 LDRVVGPDrLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGiphALTEDDE--YEGYFIPKGTTVIPNAWAIHHDPEVYPDP 341

                  ....*...
gi 1707919355 154 HKFDPDRF 161
Cdd:cd11065   342 EEFDPERY 349
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
30-182 2.45e-10

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: 59.61  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  30 QGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFGN-GPVTPEKIEQLRYCQHVLCETVRT 108
Cdd:cd11041   220 EGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEhGGWTKAALNKLKKLDSFMKESQRL 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 109 AKLTPVSAQ---LQDIeGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF------DDELVMKTFSS-----LG 174
Cdd:cd11041   300 NPLSLVSLRrkvLKDV-TLSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFyrlreqPGQEKKHQFVStspdfLG 378

                  ....*....
gi 1707919355 175 FS-GTQECP 182
Cdd:cd11041   379 FGhGRHACP 387
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
2-230 2.54e-10

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: 2.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNIIKERKGRNFSQHI--FIDSLVQGNLNDQQILE--DSMIFslASCIITAKLCTWAICFLTTSEEVQKKLYEE 77
Cdd:cd20615   178 RWRAFNLKIYNRARQRGQSTPIvkLYEAVEKGDITFEELLQtlDEMLF--ANLDVTTGVLSWNLVFLAANPAVQEKLREE 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  78 INQVFGN-GPVTPEKIEQ----LRYCqhvLCETVRTAKLTPVS-AQLQDIEGKIDRFIIPRETLVL---YALGVvlQDPN 148
Cdd:cd20615   256 ISAAREQsGYPMEDYILStdtlLAYC---VLESLRLRPLLAFSvPESSPTDKIIGGYRIPANTPVVvdtYALNI--NNPF 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 149 TWPSPHKFDPDRFDDEL---VMKTFSSLGFsGTQECPELRFAYMVTTVLLSVLVKRLHL-LSVEGQVIETKYElvtssrE 224
Cdd:cd20615   331 WGPDGEAYRPERFLGISptdLRYNFWRFGF-GPRKCLGQHVADVILKALLAHLLEQYELkLPDQGENEEDTFE------G 403

                  ....*.
gi 1707919355 225 EAWITV 230
Cdd:cd20615   404 LPWIWV 409
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
3-224 3.63e-10

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: 59.17  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKE-RKGRNFSQ-----HIFIDSL-------VQGNLNDQQILEDSMIFS--LASCIITAKLCTWAICFLTTS 67
Cdd:cd20654   192 LDSILEEWLEEhRQKRSSSGkskndEDDDDVMmlsiledSQISGYDADTVIKATCLEliLGGSDTTAVTLTWALSLLLNN 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  68 EEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRTAKLTPVSAQLQDIEG-KIDRFIIPRETLVLYALGVVLQ 145
Cdd:cd20654   272 PHVLKKAQEELDTHVGKDRWVEESdIKNLVYLQAIVKETLRLYPPGPLLGPREATEDcTVGGYHVPKGTRLLVNVWKIQR 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 146 DPNTWPSPHKFDPDRF-----DDELVMKTFSSLGF-SGTQECPELRFAYMVttVLLsVLVKRLHllsvegqvietKYELV 219
Cdd:cd20654   352 DPNVWSDPLEFKPERFltthkDIDVRGQNFELIPFgSGRRSCPGVSFGLQV--MHL-TLARLLH-----------GFDIK 417

                  ....*
gi 1707919355 220 TSSRE 224
Cdd:cd20654   418 TPSNE 422
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
25-205 5.11e-10

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: 58.58  E-value: 5.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  25 IDSLVQGnLNDQ-------QILEDSMIFSLASCII-----TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEK 91
Cdd:cd20674   203 TDYMLQG-LGQPrgekgmgQLLEGHVHMAVVDLFIggtetTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGaSPSYKD 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  92 IEQLRYCQHVLCETVRTAKLTPVSAQLQDI-EGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDElVMKTF 170
Cdd:cd20674   282 RARLPLLNATIAEVLRLRPVVPLALPHRTTrDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEP-GAANR 360
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1707919355 171 SSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLL 205
Cdd:cd20674   361 ALLPFGcGARVCLGEPLARLELFVFLARLLQAFTLL 396
PLN02183 PLN02183
ferulate 5-hydroxylase
59-182 1.58e-09

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 57.17  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRETLVL 137
Cdd:PLN02183  326 WAMAELMKSPEDLKRVQQELADVVGlNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVM 405
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1707919355 138 ---YALGvvlQDPNTWPSPHKFDPDRFDDELVM----KTFSSLGF-SGTQECP 182
Cdd:PLN02183  406 inaWAIG---RDKNSWEDPDTFKPSRFLKPGVPdfkgSHFEFIPFgSGRRSCP 455
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
2-207 1.89e-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: 56.92  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNIIKERKGRNFSQ--HIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEIN 79
Cdd:cd11059   184 LCARAESSLAESSDSESLTVllLEKLKGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELA 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  80 QVFGN--GPVTPEKIEQLRYCQHVLCETVRTAklTPVSAQLQ---DIEGK-IDRFIIPRETLVL---YALGvvlQDPNTW 150
Cdd:cd11059   264 GLPGPfrGPPDLEDLDKLPYLNAVIRETLRLY--PPIPGSLPrvvPEGGAtIGGYYIPGGTIVStqaYSLH---RDPEVF 338
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1707919355 151 PSPHKFDPDRF-----DDELVMKT-FSSLGfSGTQECPELRFAYMVTTVLLSVLVKRLHLLSV 207
Cdd:cd11059   339 PDPEEFDPERWldpsgETAREMKRaFWPFG-SGSRMCIGMNLALMEMKLALAAIYRNYRTSTT 400
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
53-161 2.97e-09

cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus nidulans cytochrome P450 59 (CYP59), also called sterigmatocystin biosynthesis P450 monooxygenase stcS, and similar fungal proteins. CYP59 is required for the conversion of versicolorin A to sterigmatocystin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410674 [Multi-domain]  Cd Length: 403  Bit Score: 56.11  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  53 TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGP--------VTPEKIEQLRYCQHVLCETVR------TAKLTPVSAQL 118
Cdd:cd11051   201 TSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPsaaaellrEGPELLNQLPYTTAVIKETLRlfppagTARRGPPGVGL 280
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1707919355 119 QDIEGKIdrfiIPRETLVLYALGVVLQ-DPNTWPSPHKFDPDRF 161
Cdd:cd11051   281 TDRDGKE----YPTDGCIVYVCHHAIHrDPEYWPRPDEFIPERW 320
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
1-201 3.37e-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: 56.27  E-value: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   1 MQLESVLRNIIKERK-----GRNFSQHIfIDSlVQGNLNDQQILEDsmiFSLASCI--------ITAKLCTWAICFLTTS 67
Cdd:cd20640   186 GEIRSLILEIVKEREeecdhEKDLLQAI-LEG-ARSSCDKKAEAED---FIVDNCKniyfagheTTAVTAAWCLMLLALH 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  68 EEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRtakLTPVSA-----QLQDIegKIDRFIIPRETLVLYALGV 142
Cdd:cd20640   261 PEWQDRVRAEVLEVCKGGPPDADSLSRMKTVTMVIQETLR---LYPPAAfvsreALRDM--KLGGLVVPKGVNIWVPVST 335
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707919355 143 VLQDPNTW-PSPHKFDPDRFDD---ELVMKTFSSLGF-SGTQECPELRFAYMVTTVLLSVLVKR 201
Cdd:cd20640   336 LHLDPEIWgPDANEFNPERFSNgvaAACKPPHSYMPFgAGARTCLGQNFAMAELKVLVSLILSK 399
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
7-204 4.50e-09

cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3,4-desaturase; Cytochrome P450 27C1 (CYP27C1) is also called all-trans retinol 3,4-desaturase. It catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-didehydroretinal). CYP27C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410740 [Multi-domain]  Cd Length: 433  Bit Score: 55.70  E-value: 4.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   7 LRNIIKE-RKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFG-N 84
Cdd:cd20647   206 LREIQKQmDRGEEVKGGLLTYLLVSKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGkR 285
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  85 GPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDRFIIPRET-LVLYALGVVLQDPNtWPSPHKFDPDRF-- 161
Cdd:cd20647   286 VVPTAEDVPKLPLIRALLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTqLALCHYSTSYDEEN-FPRAEEFRPERWlr 364
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1707919355 162 -DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHL 204
Cdd:cd20647   365 kDALDRVDNFGSIPFGyGIRSCIGRRIAELEIHLALIQLLQNFEI 409
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
4-219 6.92e-09

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: 55.23  E-value: 6.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   4 ESVLRNIIKE---RKGRNFSQhIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQ 80
Cdd:cd20644   197 DNCIQKIYQElafGRPQHYTG-IVAELLLQAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLA 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  81 VFGNGPVTPEKIEQ-LRYCQHVLCETVRtakLTPVSAQLQDIEGK---IDRFIIPRETLV---LYALGvvlQDPNTWPSP 153
Cdd:cd20644   276 AAAQISEHPQKALTeLPLLKAALKETLR---LYPVGITVQRVPSSdlvLQNYHIPAGTLVqvfLYSLG---RSAALFPRP 349
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1707919355 154 HKFDPDRF-DDELVMKTFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYELV 219
Cdd:cd20644   350 ERYDPQRWlDIRGSGRNFKHLAFGfGMRQCLGRRLAEAEMLLLLMHVLKNFLVETLSQEDIKTVYSFI 417
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
69-164 8.47e-09

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: 8.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  69 EVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVS-AQLQDIEGKIDRFIIPRETLVLYALGVVLQD 146
Cdd:cd20668   258 EVEAKVHEEIDRVIGrNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGlARRVTKDTKFRDFFLPKGTEVFPMLGSVLKD 337
                          90
                  ....*....|....*...
gi 1707919355 147 PNTWPSPHKFDPDRFDDE 164
Cdd:cd20668   338 PKFFSNPKDFNPQHFLDD 355
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
59-164 1.35e-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: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFGNG--PVTPEKIeQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDR-FIIPRETL 135
Cdd:cd20670   248 YGFLLLMKYPEVEAKIHEEINQVIGPHrlPSVDDRV-KMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFRgYLLPKGTD 326
                          90       100
                  ....*....|....*....|....*....
gi 1707919355 136 VLYALGVVLQDPNTWPSPHKFDPDRFDDE 164
Cdd:cd20670   327 VFPLLGSVLKDPKYFRYPEAFYPQHFLDE 355
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
52-161 1.90e-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: 53.86  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  52 ITAKLCtWAICFLTTSEEVQKKLYEEINQVFG--NGPVTPEKIeQLRYCQHVLCETVRTAKLTPVS---AQLQDIegKID 126
Cdd:cd20676   253 VTTALS-WSLMYLVTYPEIQKKIQEELDEVIGreRRPRLSDRP-QLPYLEAFILETFRHSSFVPFTiphCTTRDT--SLN 328
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1707919355 127 RFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF 161
Cdd:cd20676   329 GYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERF 363
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
69-164 2.33e-08

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


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 53.80  E-value: 2.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  69 EVQKKLYEEINQVFG--NGPVTPEKIeQLRYCQHVLCETVRTAKLTPVS---AQLQDIegKIDRFIIPRETLVLYALGVV 143
Cdd:cd20665   258 EVTAKVQEEIDRVIGrhRSPCMQDRS-HMPYTDAVIHEIQRYIDLVPNNlphAVTCDT--KFRNYLIPKGTTVITSLTSV 334
                          90       100
                  ....*....|....*....|.
gi 1707919355 144 LQDPNTWPSPHKFDPDRFDDE 164
Cdd:cd20665   335 LHDDKEFPNPEKFDPGHFLDE 355
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
37-204 4.25e-08

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: 52.84  E-value: 4.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  37 QILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEI-NQVFGNGPVTPEKIEQLRYCQHVLCETVR-------T 108
Cdd:cd20641   235 EIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVfRECGKDKIPDADTLSKLKLMNMVLMETLRlygpvinI 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 109 AKLTPVSAQLQDIEgkidrfiIPRETLVLYALGVVLQDPNTWPS-PHKFDPDRFDDELVMKTF---SSLGFS-GTQECPE 183
Cdd:cd20641   315 ARRASEDMKLGGLE-------IPKGTTIIIPIAKLHRDKEVWGSdADEFNPLRFANGVSRAAThpnALLSFSlGPRACIG 387
                         170       180
                  ....*....|....*....|.
gi 1707919355 184 LRFAYMVTTVLLSVLVKRLHL 204
Cdd:cd20641   388 QNFAMIEAKTVLAMILQRFSF 408
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
59-199 4.67e-08

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 52.93  E-value: 4.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTP-----VSAQLQDIEGkidrFIIPR 132
Cdd:PLN00110  311 WSLAEMLKNPSILKRAHEEMDQVIGrNRRLVESDLPKLPYLQAICKESFRKHPSTPlnlprVSTQACEVNG----YYIPK 386
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1707919355 133 ETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMKT------FSSLGF-SGTQECPELRFAYMVTTVLLSVLV 199
Cdd:PLN00110  387 NTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIdprgndFELIPFgAGRRICAGTRMGIVLVEYILGTLV 460
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
2-201 5.92e-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: 52.28  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNII----KERKGRNFSQHIFIDSLVQGNLND-------------QQILEDSMIFSLASCIITAKLCTWAICFL 64
Cdd:cd20642   182 EIRSSLRGIInkreKAMKAGEATNDDLLGILLESNHKEikeqgnknggmstEDVIEECKLFYFAGQETTSVLLVWTMVLL 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  65 TTSEEVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRtakLTPVSAQLQDI---EGKIDRFIIPRETLVLYALG 141
Cdd:cd20642   262 SQHPDWQERAREEVLQVFGNNKPDFEGLNHLKVVTMILYEVLR---LYPPVIQLTRAihkDTKLGDLTLPAGVQVSLPIL 338
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707919355 142 VVLQDPNTW-PSPHKFDPDRFDDELVMKT---FSSLGFS-GTQECPELRFAYMVTTVLLSVLVKR 201
Cdd:cd20642   339 LVHRDPELWgDDAKEFNPERFAEGISKATkgqVSYFPFGwGPRICIGQNFALLEAKMALALILQR 403
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
67-164 1.20e-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: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  67 SEEVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAklTPVSAQLQ------DIEGKIDRFIIPRETLVLYA 139
Cdd:cd11071   256 GEELHARLAEEIRSALGsEGGLTLAALEKMPLLKSVVYETLRLH--PPVPLQYGrarkdfVIESHDASYKIKKGELLVGY 333
                          90       100
                  ....*....|....*....|....*
gi 1707919355 140 LGVVLQDPNTWPSPHKFDPDRFDDE 164
Cdd:cd11071   334 QPLATRDPKVFDNPDEFVPDRFMGE 358
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
9-219 1.22e-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: 51.62  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   9 NIIKERKGRNFSqhiFIDSLV-----QGN-LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVF 82
Cdd:cd20679   213 FLKAKAKSKTLD---FIDVLLlskdeDGKeLSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELL 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  83 -GNGPvtpEKIE-----QLRYCQHVLCETVRTAKLTPVSAQ--LQDIEGKIDRfIIPRETLVLYALGVVLQDPNTWPSPH 154
Cdd:cd20679   290 kDREP---EEIEwddlaQLPFLTMCIKESLRLHPPVTAISRccTQDIVLPDGR-VIPKGIICLISIYGTHHNPTVWPDPE 365
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707919355 155 KFDPDRFDDELVmKTFSSLGF----SGTQECPELRFAYMVTTVLLSVLVKRLHLLSvEGQVIETKYELV 219
Cdd:cd20679   366 VYDPFRFDPENS-QGRSPLAFipfsAGPRNCIGQTFAMAEMKVVLALTLLRFRVLP-DDKEPRRKPELI 432
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
12-203 1.45e-07

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 51.36  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  12 KERKGRNFSQHIFIDSLVQ-GNLNDQQILEDSMIFSLASCIITAKLCT------WAICFLTTSEEVQKKLYEEINQVFG- 83
Cdd:PLN03112  264 RSGKLPGGKDMDFVDVLLSlPGENGKEHMDDVEIKALMQDMIAAATDTsavtneWAMAEVIKNPRVLRKIQEELDSVVGr 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  84 NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEG-KIDRFIIPRETLVL---YALGvvlQDPNTWPSPHKFDPD 159
Cdd:PLN03112  344 NRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRAtTINGYYIPAKTRVFintHGLG---RNTKIWDDVEEFRPE 420
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1707919355 160 RF--DDELVMKT-----FSSLGFS-GTQECPElrfAYMVTTVLLSVLVKRLH 203
Cdd:PLN03112  421 RHwpAEGSRVEIshgpdFKILPFSaGKRKCPG---APLGVTMVLMALARLFH 469
PLN02971 PLN02971
tryptophan N-hydroxylase
59-224 2.12e-07

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 50.81  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRtakLTPVSA------QLQDIegKIDRFIIP 131
Cdd:PLN02971  349 WAMAEMINKPEILHKAMEEIDRVVGKERFVQESdIPKLNYVKAIIREAFR---LHPVAAfnlphvALSDT--TVAGYHIP 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 132 RETLVL---YALGvvlQDPNTWPSPHKFDPDRFDDEL--VMKTFSSLGF----SGTQECPELRFAYMVTTVLLSVLVKRL 202
Cdd:PLN02971  424 KGSQVLlsrYGLG---RNPKVWSDPLSFKPERHLNECseVTLTENDLRFisfsTGKRGCAAPALGTAITTMMLARLLQGF 500
                         170       180
                  ....*....|....*....|..
gi 1707919355 203 HLLSVEGqviETKYELVTSSRE 224
Cdd:PLN02971  501 KWKLAGS---ETRVELMESSHD 519
PLN00168 PLN00168
Cytochrome P450; Provisional
12-161 2.46e-07

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 50.72  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  12 KERKGRNFSQHIFIDSLVQGNLNDQ--QILEDSMIFSLASCIITAKLCT------WAICFLTTSEEVQKKLYEEINQVFG 83
Cdd:PLN00168  273 EPPKKETTFEHSYVDTLLDIRLPEDgdRALTDDEIVNLCSEFLNAGTDTtstalqWIMAELVKNPSIQSKLHDEIKAKTG 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  84 NGP--VTPEKIEQLRYCQHVLCETVRtaKLTPVSAQL-----QDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKF 156
Cdd:PLN00168  353 DDQeeVSEEDVHKMPYLKAVVLEGLR--KHPPAHFVLphkaaEDME--VGGYLIPKGATVNFMVAEMGRDEREWERPMEF 428

                  ....*
gi 1707919355 157 DPDRF 161
Cdd:PLN00168  429 VPERF 433
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
59-215 2.66e-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: 50.48  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEI----NQVFGNgPVTPEKIEQLRYCqhVLCETVRtakLTPVSAQLQ-----DIegKIDRFI 129
Cdd:cd20643   256 WTLYELARNPNVQEMLRAEVlaarQEAQGD-MVKMLKSVPLLKA--AIKETLR---LHPVAVSLQryiteDL--VLQNYH 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 130 IPRETLV---LYALGvvlQDPNTWPSPHKFDPDRFddeLVMKT--FSSLGFS-GTQECPELRFAYMVTTVLLsvlvkrLH 203
Cdd:cd20643   328 IPAGTLVqvgLYAMG---RDPTVFPKPEKYDPERW---LSKDIthFRNLGFGfGPRQCLGRRIAETEMQLFL------IH 395
                         170
                  ....*....|..
gi 1707919355 204 LLsvEGQVIETK 215
Cdd:cd20643   396 ML--ENFKIETQ 405
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
53-199 2.86e-07

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: 2.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  53 TAKLcTWAICFLTTSEEVQKKLYEEINQVFGNG--PVTPEKIEQLRYCQHVLCETVR---TAKLTP--VSAQLQDIEGki 125
Cdd:cd11082   237 TSSL-VWALQLLADHPDVLAKVREEQARLRPNDepPLTLDLLEEMKYTRQVVKEVLRyrpPAPMVPhiAKKDFPLTED-- 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 126 drFIIPRETLVLYALGVVLQDPntWPSPHKFDPDRFD-----DELVMKTFSSLGfSGTQECPELRFA---YMVTTVLLSV 197
Cdd:cd11082   314 --YTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSperqeDRKYKKNFLVFG-AGPHQCVGQEYAinhLMLFLALFST 388

                  ..
gi 1707919355 198 LV 199
Cdd:cd11082   389 LV 390
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
53-164 4.00e-07

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: 50.06  E-value: 4.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  53 TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKI---EQLRYCQH---VLCETVRTAkLTPVSA--QLQDIEGk 124
Cdd:cd11040   239 TIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILdltDLLTSCPLldsTYLETLRLH-SSSTSVrlVTEDTVL- 316
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1707919355 125 IDRFIIPRETLVLYALGVVLQDPNTW-PSPHKFDPDRFDDE 164
Cdd:cd11040   317 GGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKK 357
PTZ00404 PTZ00404
cytochrome P450; Provisional
7-233 5.64e-07

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 49.72  E-value: 5.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   7 LRNIIKERkgrnFSQHIF-IDSLVQGNLNDQQILE-----DSMIFSLASCII---------TAKLCTWAICFLTTSEEVQ 71
Cdd:PTZ00404  242 IKKFIKEK----YHEHLKtIDPEVPRDLLDLLIKEygtntDDDILSILATILdfflagvdtSATSLEWMVLMLCNYPEIQ 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  72 KKLYEEINQVFGNGP-VTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEGKIDRFIiPRETLVL---YALGvvl 144
Cdd:PTZ00404  318 EKAYNEIKSTVNGRNkVLLSDRQSTPYTVAIIKETLRYKPVSPFGlprSTSNDIIIGGGHFI-PKDAQILinyYSLG--- 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 145 QDPNTWPSPHKFDPDRFDDELVMKTFssLGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEG-QVIETKYELVTSS 222
Cdd:PTZ00404  394 RNEKYFENPEQFDPSRFLNPDSNDAF--MPFSiGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGkKIDETEEYGLTLK 471
                         250
                  ....*....|.
gi 1707919355 223 REEAWITVSKR 233
Cdd:PTZ00404  472 PNKFKVLLEKR 482
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
33-203 1.65e-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: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  33 LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVfGNGPVTPEKIEQLRYCQHVLCETVRTAKLT 112
Cdd:cd20614   204 LSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA-GDVPRTPAELRRFPLAEALFRETLRLHPPV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 113 PVSAQ--LQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRF-DDELVMKTFSSLGF-SGTQECPELRFAY 188
Cdd:cd20614   283 PFVFRrvLEEIE--LGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWlGRDRAPNPVELLQFgGGPHFCLGYHVAC 360
                         170
                  ....*....|....*
gi 1707919355 189 MVTTVLLSVLVKRLH 203
Cdd:cd20614   361 VELVQFIVALARELG 375
PLN02966 PLN02966
cytochrome P450 83A1
2-187 2.92e-06

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 47.43  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNIIKERKGRNFSQHIFIDslvqgnlNDQQILEDSMIfslASCIITAKLCTWAICFLTTSEEVQKKLYEEINQV 81
Cdd:PLN02966  264 ETESMIDLLMEIYKEQPFASEFTVD-------NVKAVILDIVV---AGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREY 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  82 F---GNGPVTPEKIEQLRYCQHVLCETVRTAKLTPV---SAQLQDIegKIDRFIIPRETLVLYALGVVLQDPNTW-PSPH 154
Cdd:PLN02966  334 MkekGSTFVTEDDVKNLPYFRALVKETLRIEPVIPLlipRACIQDT--KIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPD 411
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1707919355 155 KFDPDRFDDELVMKTFSSLGF----SGTQECPELRFA 187
Cdd:PLN02966  412 EFRPERFLEKEVDFKGTDYEFipfgSGRRMCPGMRLG 448
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
58-187 3.05e-06

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: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  58 TWAICFLTTSEEVQKKLYEEINQVFGNGPV-TPEKIEQLRYCQHVLCETVRTAKLTPVSAQL---QDIEgkIDRFIIPRE 133
Cdd:cd20648   255 SWSLYELSRHPDVQTALHREITAALKDNSVpSAADVARMPLLKAVVKEVLRLYPVIPGNARVipdRDIQ--VGEYIIPKK 332
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1707919355 134 TLVLYALGVVLQDPNTWPSPHKFDPDRF-DDELVMKTFSSLGFS-GTQECPELRFA 187
Cdd:cd20648   333 TLITLCHYATSRDENQFPDPNSFRPERWlGKGDTHHPYASLPFGfGKRSCIGRRIA 388
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
70-163 3.62e-06

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: 3.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  70 VQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKIDR-FIIPRETLVLYALGVVLQDP 147
Cdd:cd20672   259 VAEKVQKEIDQVIGsHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTLFRgYLLPKNTEVYPILSSALHDP 338
                          90
                  ....*....|....*.
gi 1707919355 148 NTWPSPHKFDPDRFDD 163
Cdd:cd20672   339 QYFEQPDTFNPDHFLD 354
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
59-189 4.83e-06

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: 4.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFGNG-----PVTPEKIEQLRYCQHVLCETVR-------TAKLT-PVsaqlqdiegKI 125
Cdd:cd20635   232 WTLAFILSHPSVYKKVMEEISSVLGKAgkdkiKISEDDLKKMPYIKRCVLEAIRlrspgaiTRKVVkPI---------KI 302
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707919355 126 DRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDD-----ELVMKTFSSLGfSGTQECPELRFAYM 189
Cdd:cd20635   303 KNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKadlekNVFLEGFVAFG-GGRYQCPGRWFALM 370
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
2-177 6.60e-06

cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It effectively metabolizes all-trans retinoic acid (atRA), 9-cis-retinoic acid (9-cis-RA), 13-cis-retinoic acid, and 4-oxo-atRA with the highest intrinsic clearance toward 9-cis-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. Loss of function mutations in the CYP26C1 gene cause type IV focal facial dermal dysplasia (FFDD), a rare syndrome characterized by facial lesions resembling aplasia cutis. CYP26C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 46.37  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   2 QLESVLRNIIKERKGRNFSQH------IFIDSLVQGN--LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKK 73
Cdd:cd20636   184 ILHEYMEKAIEEKLQRQQAAEycdaldYMIHSARENGkeLTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEK 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  74 LYEEINQ-----VFGNGP--VTPEKIEQLRYCQHVLCETVRTakLTPVSA----QLQDIEgkIDRFIIPRETLVLYALGV 142
Cdd:cd20636   264 IRQELVShglidQCQCCPgaLSLEKLSRLRYLDCVVKEVLRL--LPPVSGgyrtALQTFE--LDGYQIPKGWSVMYSIRD 339
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1707919355 143 VLQDPNTWPSPHKFDPDRFD---DELVMKTFSSLGFSG 177
Cdd:cd20636   340 THETAAVYQNPEGFDPDRFGverEESKSGRFNYIPFGG 377
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
59-199 6.88e-06

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: 6.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  59 WAICFLTTSEEVQKKLYEEINQVFGNGPVTPEK-IEQLRYCQHVLCETVRtakLTPVSA------QLQDIegKIDRFIIP 131
Cdd:cd20658   259 WALAEMLNQPEILRKATEELDRVVGKERLVQESdIPNLNYVKACAREAFR---LHPVAPfnvphvAMSDT--TVGGYFIP 333
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1707919355 132 RETLVL---YALGvvlQDPNTWPSPHKFDPDRF--DDELVMKTFSSLGF----SGTQECPELRFAYMVTTVLLSVLV 199
Cdd:cd20658   334 KGSHVLlsrYGLG---RNPKVWDDPLKFKPERHlnEDSEVTLTEPDLRFisfsTGRRGCPGVKLGTAMTVMLLARLL 407
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
4-164 7.35e-06

cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 46.04  E-value: 7.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   4 ESVLRNIIKERKGRNFSQHIFIDSLVQGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFG 83
Cdd:cd11058   184 EKVDRRLAKGTDRPDFMSYILRNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFS 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  84 N-GPVTPEKIEQLRYCQHVLCETVRtakLT-PVSAQLQDI---EGK-IDRFIIPRETLVLYALGVVLQDPNTWPSPHKFD 157
Cdd:cd11058   264 SeDDITLDSLAQLPYLNAVIQEALR---LYpPVPAGLPRVvpaGGAtIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFI 340

                  ....*..
gi 1707919355 158 PDRFDDE 164
Cdd:cd11058   341 PERWLGD 347
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
93-210 8.40e-06

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


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 45.75  E-value: 8.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  93 EQLRYCQHVLCeTVRTAkltpvsaqLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRfddelvmKTFSS 172
Cdd:cd20629   242 EGLRWEPPVAS-VPRMA--------LRDVE--LDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR-------KPKPH 303
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1707919355 173 LGFS-GTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQ 210
Cdd:cd20629   304 LVFGgGAHRCLGEHLARVELREALNALLDRLPNLRLDPD 342
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
37-213 9.68e-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: 45.86  E-value: 9.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  37 QILEDSMIFSLASCIITAKLCT------WAICFLTTSEEVQKKLYEEINQVFGNGPVTP-EKIEQLRYCQHVLCETVRTA 109
Cdd:cd20677   230 AVLSDEQIISTVNDIFGAGFDTistalqWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRfEDRKSLHYTEAFINEVFRHS 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 110 KLTPVS-AQLQDIEGKIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDE-------LVMKTfssLGFS-GTQE 180
Cdd:cd20677   310 SFVPFTiPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDEngqlnksLVEKV---LIFGmGVRK 386
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1707919355 181 CPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIE 213
Cdd:cd20677   387 CLGEDVARNEIFVFLTTILQQLKLEKPPGQKLD 419
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
69-214 1.37e-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: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  69 EVQKKLYEEINQVFGNGPVTPEKIEQLRYCQHVLCETVRT---AKLTPVSAQLQDIegkIDRFIIPRETLVLYALGVVLQ 145
Cdd:cd20616   256 EVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYqpvVDFVMRKALEDDV---IDGYPVKKGTNIILNIGRMHR 332
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1707919355 146 DPNtWPSPHKFDPDRFDDELVMKTFSSLGFsGTQECPELRFAYMVTTVLLSVLVKRLHLLSVEGQVIET 214
Cdd:cd20616   333 LEF-FPKPNEFTLENFEKNVPSRYFQPFGF-GPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVEN 399
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
30-224 3.04e-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: 44.41  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  30 QGNLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQV-FGNGPVTPEKIEQLRYCQHVLCETVRT 108
Cdd:cd20645   219 DNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVlPANQTPRAEDLKNMPYLKACLKESMRL 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 109 AKLTPVSAQLQDIEGKIDRFIIPRETLVL---YALGVvlqDPNTWPSPHKFDPDRF-DDELVMKTFSSLGFS-GTQECPE 183
Cdd:cd20645   299 TPSVPFTSRTLDKDTVLGDYLLPKGTVLMinsQALGS---SEEYFEDGRQFKPERWlQEKHSINPFAHVPFGiGKRMCIG 375
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1707919355 184 LRFAYMVTTVLLSVLVKRLHLLSVEGQVIETKYE-LVTSSRE 224
Cdd:cd20645   376 RRLAELQLQLALCWIIQKYQIVATDNEPVEMLHSgILVPSRE 417
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
69-164 3.82e-05

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: 3.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  69 EVQKKLYEEINQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAKLTPVS---AQLQDIEGKidRFIIPRETLVLYALGVVL 144
Cdd:cd20669   258 KVAARVQEEIDRVVGrNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSlphAVTRDTNFR--GFLIPKGTDVIPLLNSVH 335
                          90       100
                  ....*....|....*....|
gi 1707919355 145 QDPNTWPSPHKFDPDRFDDE 164
Cdd:cd20669   336 YDPTQFKDPQEFNPEHFLDD 355
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
32-201 4.15e-05

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 43.81  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  32 NLNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEINQVFG----NGPVTPEKIEQLRYCQHVLCETVR 107
Cdd:PLN02987  262 GFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAmksdSYSLEWSDYKSMPFTQCVVNETLR 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 108 TAKLTP--VSAQLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVM----KTFSSLGfSGTQEC 181
Cdd:PLN02987  342 VANIIGgiFRRAMTDIE--VKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTtvpsNVFTPFG-GGPRLC 418
                         170       180
                  ....*....|....*....|
gi 1707919355 182 PELRFAYMVTTVLLSVLVKR 201
Cdd:PLN02987  419 PGYELARVALSVFLHRLVTR 438
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
17-212 4.24e-05

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 43.96  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  17 RNFSQHIfIDSLVQGNLNDQQIL-EDSMifslasciitAKLCTWAICFLTTSEEVQKKLYEEINQVFGNGPVTPEKIE-- 93
Cdd:PLN03141  241 RDGSDEL-TDDLISDNMIDMMIPgEDSV----------PVLMTLAVKFLSDCPVALQQLTEENMKLKRLKADTGEPLYwt 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  94 ---QLRYCQHVLCETVRTAKLTP--VSAQLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDElVMK 168
Cdd:PLN03141  310 dymSLPFTQNVITETLRMGNIINgvMRKAMKDVE--IKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEK-DMN 386
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1707919355 169 TFSSLGFSGTQE-CPELRFAYMVTTVLLSVLVKRLHLLSVEGQVI 212
Cdd:PLN03141  387 NSSFTPFGGGQRlCPGLDLARLEASIFLHHLVTRFRWVAEEDTIV 431
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
3-222 6.98e-05

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


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 43.30  E-value: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERKGRNFSQ--HIFIDSLVQGN--LNDQQILEDSMIFSLASCIITAKLCTWAICFLTTSEEVQKKLYEEI 78
Cdd:cd20637   188 LEKAIREKLQGTQGKDYADalDILIESAKEHGkeLTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREEL 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  79 -------NQVFGNGPVTPEKIEQLRYCQHVLCETVRTakLTPVSA----QLQDIEgkIDRFIIPRETLVLYAL------G 141
Cdd:cd20637   268 rsngilhNGCLCEGTLRLDTISSLKYLDCVIKEVLRL--FTPVSGgyrtALQTFE--LDGFQIPKGWSVLYSIrdthdtA 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 142 VVLQDPNTwpsphkFDPDRFDDElvmktfsslgfsgTQECPELRFAYM-----VTTVLLSVLVKR-LHLLSVEgQVIETK 215
Cdd:cd20637   344 PVFKDVDA------FDPDRFGQE-------------RSEDKDGRFHYLpfgggVRTCLGKQLAKLfLKVLAVE-LASTSR 403

                  ....*..
gi 1707919355 216 YELVTSS 222
Cdd:cd20637   404 FELATRT 410
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
29-164 9.67e-05

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: 9.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  29 VQGNL--NDQQILEDSMIFSLASCIITAKLCT------WAICFLTTS--EEVQKKLYEEINQVFGNG------PVTPEKI 92
Cdd:cd11066   212 IVGNIlkDKESKLTDAELQSICLTMVSAGLDTvplnlnHLIGHLSHPpgQEIQEKAYEEILEAYGNDedawedCAAEEKC 291
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1707919355  93 EqlrYCQHVLCETVR---TAKLTPVSAQLQDIEgkIDRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDE 164
Cdd:cd11066   292 P---YVVALVKETLRyftVLPLGLPRKTTKDIV--YNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDA 361
PLN02774 PLN02774
brassinosteroid-6-oxidase
3-182 1.97e-04

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 42.07  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355   3 LESVLRNIIKERKGRNFSQHIFIDSL--VQGN---LNDQQILED--SMIFSLASCIITAKLCtwAICFLTTSEEVQKKLY 75
Cdd:PLN02774  225 IVRMLRQLIQERRASGETHTDMLGYLmrKEGNrykLTDEEIIDQiiTILYSGYETVSTTSMM--AVKYLHDHPKALQELR 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  76 EE---INQVFG-NGPVTPEKIEQLRYCQHVLCETVRTAklTPVSAQL----QDIEgkIDRFIIPRETLVLYALGVVLQDP 147
Cdd:PLN02774  303 KEhlaIRERKRpEDPIDWNDYKSMRFTRAVIFETSRLA--TIVNGVLrkttQDME--LNGYVIPKGWRIYVYTREINYDP 378
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1707919355 148 NTWPSPHKFDPDRF-DDELVMKTFSSLGFSGTQECP 182
Cdd:PLN02774  379 FLYPDPMTFNPWRWlDKSLESHNYFFLFGGGTRLCP 414
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
53-202 6.19e-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: 40.18  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  53 TAKLCTWAICFLTTSEEVQKKLYEEIN-QVFGNGPVTPEK------IEQLRYCQHVLCETVRTAKLTPVSAQLQDIEGKI 125
Cdd:cd20638   246 TASAATSLIMFLGLHPEVLQKVRKELQeKGLLSTKPNENKelsmevLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFEL 325
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 126 DRFIIPRETLVLYALGVVLQDPNTWPSPHKFDPDRFDDELVMKT--FSSLGF-SGTQECPELRFAymvtTVLLSVLVKRL 202
Cdd:cd20638   326 NGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSsrFSFIPFgGGSRSCVGKEFA----KVLLKIFTVEL 401
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
53-205 4.88e-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: 37.64  E-value: 4.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355  53 TAKLCTWAICFLTTSEEVQKKLYEEINQVFGNG-PVTPEKIEQLRYCQHVLCETVRtakLTP----VSAQLQDIEGKIDR 127
Cdd:cd20678   255 TASGISWILYCLALHPEHQQRCREEIREILGDGdSITWEHLDQMPYTTMCIKEALR---LYPpvpgISRELSKPVTFPDG 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1707919355 128 FIIPRETLV---LYALGvvlQDPNTWPSPHKFDPDRFDDELVMK--TFSSLGFS-GTQECPELRFAYMVTTVLLSVLVKR 201
Cdd:cd20678   332 RSLPAGITVslsIYGLH---HNPAVWPNPEVFDPLRFSPENSSKrhSHAFLPFSaGPRNCIGQQFAMNEMKVAVALTLLR 408

                  ....
gi 1707919355 202 LHLL 205
Cdd:cd20678   409 FELL 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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