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Conserved domains on  [gi|193083117|ref|NP_001122387|]
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1,25-dihydroxyvitamin D(3) 24-hydroxylase, mitochondrial isoform 2 precursor [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 ...
 90-442 0e+00

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


The actual alignment was detected with superfamily member cd20645:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 419  Bit Score: 729.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  90 HKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKP 169
Cdd:cd20645    1 HKKFGKIFRMKLGSFESVHIGSPCLLEALYRKESAYPQRLEIKPWKAYRDYRDEAYGLLILEGQEWQRVRSAFQKKLMKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 170 GEVMKLDNKINEVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTF 249
Cdd:cd20645   81 KEVMKLDGKINEVLADFMGRIDELCDETGRVEDLYSELNKWSFETICLVLYDKRFGLLQQNVEEEALNFIKAIKTMMSTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 250 GRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQNRLSKKELYAAVTELQLAAVE 329
Cdd:cd20645  161 GKMMVTPVELHKRLNTKVWQDHTEAWDNIFKTAKHCIDKRLQRYSQGPANDFLCDIYHDNELSKKELYAAITELQIGGVE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 330 TTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYAL 409
Cdd:cd20645  241 TTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGDYLL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 410 PKG------------------------------------------------------------------IVRKYDIQATD 423
Cdd:cd20645  321 PKGtvlminsqalgsseeyfedgrqfkperwlqekhsinpfahvpfgigkrmcigrrlaelqlqlalcwIIQKYQIVATD 400

                        410
                 ....*....|....*....
gi 193083117 424 NEPVEMLHSGTLVPSRELP 442
Cdd:cd20645  401 NEPVEMLHSGILVPSRELP 419
 
Name Accession Description Interval E-value
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 90-442 0e+00

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: 729.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  90 HKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKP 169
Cdd:cd20645    1 HKKFGKIFRMKLGSFESVHIGSPCLLEALYRKESAYPQRLEIKPWKAYRDYRDEAYGLLILEGQEWQRVRSAFQKKLMKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 170 GEVMKLDNKINEVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTF 249
Cdd:cd20645   81 KEVMKLDGKINEVLADFMGRIDELCDETGRVEDLYSELNKWSFETICLVLYDKRFGLLQQNVEEEALNFIKAIKTMMSTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 250 GRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQNRLSKKELYAAVTELQLAAVE 329
Cdd:cd20645  161 GKMMVTPVELHKRLNTKVWQDHTEAWDNIFKTAKHCIDKRLQRYSQGPANDFLCDIYHDNELSKKELYAAITELQIGGVE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 330 TTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYAL 409
Cdd:cd20645  241 TTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGDYLL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 410 PKG------------------------------------------------------------------IVRKYDIQATD 423
Cdd:cd20645  321 PKGtvlminsqalgsseeyfedgrqfkperwlqekhsinpfahvpfgigkrmcigrrlaelqlqlalcwIIQKYQIVATD 400

                        410
                 ....*....|....*....
gi 193083117 424 NEPVEMLHSGTLVPSRELP 442
Cdd:cd20645  401 NEPVEMLHSGILVPSRELP 419
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 59-414 1.29e-79

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: 254.13  E-value: 1.29e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117   59 PGPTSWPLLGSLLQIlwkGGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYR 138
Cdd:pfam00067   2 PGPPPLPLFGNLLQL---GRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  139 DYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGeVMKLDNKINEVLADFMGRIDELCDERGHVeDLYSELNKWSFESICLV 218
Cdd:pfam00067  79 RGPFLGKGIVFANGPRWRQLRRFLTPTFTSFG-KLSFEPRVEEEARDLVEKLRKTAGEPGVI-DITDLLFRAALNVICSI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  219 LYEKRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPS 298
Cdd:pfam00067 157 LFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  299 -----ADFLC---DIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAED 370
Cdd:pfam00067 237 sprdfLDALLlakEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDD 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 193083117  371 LRNMPYLKACLKESMRLTPSVPFT-TRTLDKATVLGEYALPKGIV 414
Cdd:pfam00067 317 LQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTL 361
PTZ00404 PTZ00404
cytochrome P450; Provisional
 58-412 2.41e-25

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 107.89  E-value: 2.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  58 LPGPTSWPLLGSLLQILwkgglKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALY-RTESAYPQRLEIKPWKA 136
Cdd:PTZ00404  31 LKGPIPIPILGNLHQLG-----NLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFvDNFDNFSDRPKIPSIKH 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 137 YRDYRkegyGLLILEGEDWQRVRSAFQKklmkpgeVMKLDN--KINEVLADfmgridelcdergHVEDLYSELNKW--SF 212
Cdd:PTZ00404 106 GTFYH----GIVTSSGEYWKRNREIVGK-------AMRKTNlkHIYDLLDD-------------QVDVLIESMKKIesSG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 213 ESICLVLYEKRFGL--LQKNAGDEAVNF------------IMAIKTMMSTFGRMMVTPV-ELHKSLNTKvWQDHTlawDT 277
Cdd:PTZ00404 162 ETFEPRYYLTKFTMsaMFKYIFNEDISFdedihngklaelMGPMEQVFKDLGSGSLFDViEITQPLYYQ-YLEHT---DK 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 278 IFKSVKACIDNRLEKY-------SQQPSADFLCDIY----HQNRLSkkeLYAAVTELQLAAVETTANSLMWILYNLSRNP 346
Cdd:PTZ00404 238 NFKKIKKFIKEKYHEHlktidpeVPRDLLDLLIKEYgtntDDDILS---ILATILDFFLAGVDTSATSLEWMVLMLCNYP 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193083117 347 QVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPF--TTRTLDKATVLGEYALPKG 412
Cdd:PTZ00404 315 EIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFglPRSTSNDIIIGGGHFIPKD 382
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 92-412 1.01e-21

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: 96.50  E-value: 1.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  92 KYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWkaYRDYRKEGYGLLILEGEDWQRVRSAFQKkLMKPGE 171
Cdd:COG2124   30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEV--LRPLPLLGDSLLTLDGPEHTRLRRLVQP-AFTPRR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 172 VMKLDNKINEVladfmgrIDELCDE---RGHVeDLYSELNKWSFESICLVLyekrFGLlqknAGDEAVNFIMAIKTMMST 248
Cdd:COG2124  107 VAALRPRIREI-------ADELLDRlaaRGPV-DLVEEFARPLPVIVICEL----LGV----PEEDRDRLRRWSDALLDA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 249 FGRmmvtpvelhksLNTKVWQDHTLAWDTIFKSVKACIDNRLekysQQPSADFLCDI----YHQNRLSKKELYAAVTELQ 324
Cdd:COG2124  171 LGP-----------LPPERRRRARRARAELDAYLRELIAERR----AEPGDDLLSALlaarDDGERLSDEELRDELLLLL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 325 LAAVETTANSLMWILYNLSRNPQVQQKLlkeiqsvlpenqvpRAEDlrnmPYLKACLKESMRLTPSVPFTTRTLDKATVL 404
Cdd:COG2124  236 LAGHETTANALAWALYALLRHPEQLARL--------------RAEP----ELLPAAVEETLRLYPPVPLLPRTATEDVEL 297


                 ....*...
gi 193083117 405 GEYALPKG 412
Cdd:COG2124  298 GGVTIPAG 305
 
Name Accession Description Interval E-value
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 90-442 0e+00

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: 729.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  90 HKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKP 169
Cdd:cd20645    1 HKKFGKIFRMKLGSFESVHIGSPCLLEALYRKESAYPQRLEIKPWKAYRDYRDEAYGLLILEGQEWQRVRSAFQKKLMKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 170 GEVMKLDNKINEVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTF 249
Cdd:cd20645   81 KEVMKLDGKINEVLADFMGRIDELCDETGRVEDLYSELNKWSFETICLVLYDKRFGLLQQNVEEEALNFIKAIKTMMSTF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 250 GRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQNRLSKKELYAAVTELQLAAVE 329
Cdd:cd20645  161 GKMMVTPVELHKRLNTKVWQDHTEAWDNIFKTAKHCIDKRLQRYSQGPANDFLCDIYHDNELSKKELYAAITELQIGGVE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 330 TTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYAL 409
Cdd:cd20645  241 TTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGDYLL 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 410 PKG------------------------------------------------------------------IVRKYDIQATD 423
Cdd:cd20645  321 PKGtvlminsqalgsseeyfedgrqfkperwlqekhsinpfahvpfgigkrmcigrrlaelqlqlalcwIIQKYQIVATD 400

                        410
                 ....*....|....*....
gi 193083117 424 NEPVEMLHSGTLVPSRELP 442
Cdd:cd20645  401 NEPVEMLHSGILVPSRELP 419
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 90-412 8.19e-133

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: 389.19  E-value: 8.19e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  90 HKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKP 169
Cdd:cd11054    1 HKKYGPIVREKLGGRDIVHLFDPDDIEKVFRNEGKYPIRPSLEPLEKYRKKRGKPLGLLNSNGEEWHRLRSAVQKPLLRP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 170 GEVMKLDNKINEVLADFMGRIDELCDERGH-VEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMST 248
Cdd:cd11054   81 KSVASYLPAINEVADDFVERIRRLRDEDGEeVPDLEDELYKWSLESIGTVLFGKRLGCLDDNPDSDAQKLIEAVKDIFES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 249 FGRMMVTPVeLHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSAD-----FLCDIYHQNRLSKKELYAAVTEL 323
Cdd:cd11054  161 SAKLMFGPP-LWKYFPTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEEDeeedsLLEYLLSKPGLSKKEIVTMALDL 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 324 QLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATV 403
Cdd:cd11054  240 LLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKDIV 319


                 ....*....
gi 193083117 404 LGEYALPKG 412
Cdd:cd11054  320 LSGYHIPKG 328
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 91-411 1.75e-89

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: 278.47  E-value: 1.75e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  91 KKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPG 170
Cdd:cd20646    2 KIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKPK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 171 EVMKLDNKINEVLADFMGRIDELCDERGH---VEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMS 247
Cdd:cd20646   82 EVSLYADAINEVVSDLMKRIEYLRERSGSgvmVSDLANELYKFAFEGISSILFETRIGCLEKEIPEETQKFIDSIGEMFK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 248 TFGRMMVTPVELHKSLntKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSAD------FLCDIYHQNRLSKKELYAAVT 321
Cdd:cd20646  162 LSEIVTLLPKWTRPYL--PFWKRYVDAWDTIFSFGKKLIDKKMEEIEERVDRGepvegeYLTYLLSSGKLSPKEVYGSLT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 322 ELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTL-DK 400
Cdd:cd20646  240 ELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIvEK 319

                        330
                 ....*....|.
gi 193083117 401 ATVLGEYALPK 411
Cdd:cd20646  320 EVVVGDYLFPK 330
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 59-414 1.29e-79

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: 254.13  E-value: 1.29e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117   59 PGPTSWPLLGSLLQIlwkGGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYR 138
Cdd:pfam00067   2 PGPPPLPLFGNLLQL---GRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  139 DYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGeVMKLDNKINEVLADFMGRIDELCDERGHVeDLYSELNKWSFESICLV 218
Cdd:pfam00067  79 RGPFLGKGIVFANGPRWRQLRRFLTPTFTSFG-KLSFEPRVEEEARDLVEKLRKTAGEPGVI-DITDLLFRAALNVICSI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  219 LYEKRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPS 298
Cdd:pfam00067 157 LFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  299 -----ADFLC---DIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAED 370
Cdd:pfam00067 237 sprdfLDALLlakEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDD 316

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 193083117  371 LRNMPYLKACLKESMRLTPSVPFT-TRTLDKATVLGEYALPKGIV 414
Cdd:pfam00067 317 LQNMPYLDAVIKETLRLHPVVPLLlPREVTKDTVIPGYLIPKGTL 361
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 92-426 9.70e-77

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: 245.40  E-value: 9.70e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  92 KYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGE 171
Cdd:cd20643    3 KYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAPKV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 172 VMKLDNKINEVLADFMGRIDELCDERGH---VEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMST 248
Cdd:cd20643   83 IDNFVPLLNEVSQDFVSRLHKRIKKSGSgkwTADLSNDLFRFALESICNVLYGERLGLLQDYVNPEAQRFIDAITLMFHT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 249 FGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDN-----RLEKYSQQPSADFLCDIYHQNRLSKKELYAAVTEL 323
Cdd:cd20643  163 TSPMLYIPPDLLRLINTKIWRDHVEAWDVIFNHADKCIQNiyrdlRQKGKNEHEYPGILANLLLQDKLPIEDIKASVTEL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 324 QLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATV 403
Cdd:cd20643  243 MAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITEDLV 322

                        330       340
                 ....*....|....*....|...
gi 193083117 404 LGEYALPKGIVRKYDIQATDNEP 426
Cdd:cd20643  323 LQNYHIPAGTLVQVGLYAMGRDP 345
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 92-411 3.50e-74

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: 238.88  E-value: 3.50e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  92 KYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGE 171
Cdd:cd20648    4 KYGPVWKASFGPILTVHVADPALIEQVLRQEGKHPVRSDLSSWKDYRQLRGHAYGLLTAEGEEWQRLRSLLAKHMLKPKA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 172 VMKLDNKINEVLADFMGRIDEL--CDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTF 249
Cdd:cd20648   84 VEAYAGVLNAVVTDLIRRLRRQrsRSSPGVVKDIAGEFYKFGLEGISSVLFESRIGCLEANVPEETETFIQSINTMFVMT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 250 GRMMVTPVELHKsLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQ------PSADFLCDIYHQNRLSKKELYAAVTEL 323
Cdd:cd20648  164 LLTMAMPKWLHR-LFPKPWQRFCRSWDQMFAFAKGHIDRRMAEVAAKlprgeaIEGKYLTYFLAREKLPMKSIYGNVTEL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 324 QLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATV 403
Cdd:cd20648  243 LLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPDRDI 322


                 ....*....
gi 193083117 404 -LGEYALPK 411
Cdd:cd20648  323 qVGEYIIPK 331
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 91-412 3.16e-65

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: 215.94  E-value: 3.16e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  91 KKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPG 170
Cdd:cd20647    2 REYGKIFKSHFGPQFVVSIADRDMVAQVLRAEGAAPQRANMESWQEYRDLRGRSTGLISAEGEQWLKMRSVLRQKILRPR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 171 EVMKLDNKINEVLADFMGRIDELcdeRGHVEDLYSELN------KWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKT 244
Cdd:cd20647   82 DVAVYSGGVNEVVADLIKRIKTL---RSQEDDGETVTNvndlffKYSMEGVATILYECRLGCLENEIPKQTVEYIEALEL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 245 MMSTFGRMM---VTPVELhKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKY------SQQPSADFLCDIYHQNRLSKKE 315
Cdd:cd20647  159 MFSMFKTTMyagAIPKWL-RPFIPKPWEEFCRSWDGLFKFSQIHVDNRLREIqkqmdrGEEVKGGLLTYLLVSKELTLEE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 316 LYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTT 395
Cdd:cd20647  238 IYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLPGNG 317

                        330
                 ....*....|....*..
gi 193083117 396 RTLDKATVLGEYALPKG 412
Cdd:cd20647  318 RVTQDDLIVGGYLIPKG 334
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 91-412 9.38e-59

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: 198.53  E-value: 9.38e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  91 KKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPG 170
Cdd:cd20644    2 QELGPIYRENLGGPNMVNVMLPEDVEKLFQSEGLHPRRMTLEPWVAHRQHRGHKCGVFLLNGPEWRFDRLRLNPEVLSPA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 171 EVMKLDNKINEVLADFMGRIDE--LCDERGHVE-DLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMS 247
Cdd:cd20644   82 AVQRFLPMLDAVARDFSQALKKrvLQNARGSLTlDVQPDLFRFTLEASNLALYGERLGLVGHSPSSASLRFISAVEVMLK 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 248 TFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSADF---LCDIYHQNRLSKKELYAAVTELQ 324
Cdd:cd20644  162 TTVPLLFMPRSLSRWISPKLWKEHFEAWDCIFQYADNCIQKIYQELAFGRPQHYtgiVAELLLQAELSLEAIKANITELT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 325 LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVlpENQVPR--AEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKAT 402
Cdd:cd20644  242 AGGVDTTAFPLLFTLFELARNPDVQQILRQESLAA--AAQISEhpQKALTELPLLKAALKETLRLYPVGITVQRVPSSDL 319

                        330
                 ....*....|
gi 193083117 403 VLGEYALPKG 412
Cdd:cd20644  320 VLQNYHIPAG 329
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 94-412 4.94e-45

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: 161.14  E-value: 4.94e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  94 GKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAYRDYrkeGYGLLILEGEDWQRVRSAFQKkLMKPGEVM 173
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFL---GDGLLTLDGPEHRRLRRLLAP-AFTPRALA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 174 KLDNKINEVLADFMGRIDELCDERghvEDLYSELNKWSFESICLVLyekrFGllqKNAGDEAVNFIMAIKTMMSTFGRMM 253
Cdd:cd00302   77 ALRPVIREIARELLDRLAAGGEVG---DDVADLAQPLALDVIARLL----GG---PDLGEDLEELAELLEALLKLLGPRL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 254 VTPvelhksLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQNRLSKKELYAAVTELQLAAVETTAN 333
Cdd:cd00302  147 LRP------LPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTAS 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193083117 334 SLMWILYNLSRNPQVQQKLLKEIQSVLPENQvprAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd00302  221 LLAWALYLLARHPEVQERLRAEIDAVLGDGT---PEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAG 296
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 94-412 1.43e-36

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: 138.88  E-value: 1.43e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  94 GKIFRMKLGSFESVHLGSPCLLEALYRTESAY----PQRLEikpwkayRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKP 169
Cdd:cd20617    1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNfsdrPLLPS-------FEIISGGKGILFSNGDYWKELRRFALSSLTKT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 170 GEVMKLDNKINEVLADFMGRIDELCDeRGHVEDLYSELNKWSFESICLVLYEKRFGLLQKnagDEAVNFIMAIKTMMSTF 249
Cdd:cd20617   74 KLKKKMEELIEEEVNKLIESLKKHSK-SGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDD---GEFLKLVKPIEEIFKEL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 250 GRMMVTPV-----ELHKSLNTKVWQDHtlawDTIFKSVKACIDNRLEKYSQQPSADFLCDI-------YHQNRLSKKELY 317
Cdd:cd20617  150 GSGNPSDFipillPFYFLYLKKLKKSY----DKIKDFIEKIIEEHLKTIDPNNPRDLIDDElllllkeGDSGLFDDDSII 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 318 AAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFT-TR 396
Cdd:cd20617  226 STCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGlPR 305

                        330
                 ....*....|....*.
gi 193083117 397 TLDKATVLGEYALPKG 412
Cdd:cd20617  306 VTTEDTEIGGYFIPKG 321
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 94-412 3.80e-33

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: 129.24  E-value: 3.80e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  94 GKIFRMKLGSFESVHLGSPCLLEALYRTESA-YPQRLEIKPWKayrdyRKEGYGLLILEGEDWQRvrsafQKKLMKP--- 169
Cdd:cd20620    1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARnYVKGGVYERLK-----LLLGNGLLTSEGDLWRR-----QRRLAQPafh 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 170 -------GEVMKldnkinEVLADFMGRIDELcDERGHVeDLYSELNKWSFESICLVLyekrFGLlqkNAGDEAVNFIMAI 242
Cdd:cd20620   71 rrriaayADAMV------EATAALLDRWEAG-ARRGPV-DVHAEMMRLTLRIVAKTL----FGT---DVEGEADEIGDAL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 243 KTMMSTFGRMMVTPVELHKSL----NTKVWQdhtlAWDTIFKSVKACIDNRLEkySQQPSADFLC------DIYHQNRLS 312
Cdd:cd20620  136 DVALEYAARRMLSPFLLPLWLptpaNRRFRR----ARRRLDEVIYRLIAERRA--APADGGDLLSmllaarDEETGEPMS 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 313 KKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLpENQVPRAEDLRNMPYLKACLKESMRLTPSVP 392
Cdd:cd20620  210 DQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVL-GGRPPTAEDLPQLPYTEMVLQESLRLYPPAW 288

                        330       340
                 ....*....|....*....|
gi 193083117 393 FTTRTLDKATVLGEYALPKG 412
Cdd:cd20620  289 IIGREAVEDDEIGGYRIPAG 308
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 94-412 2.39e-32

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: 127.25  E-value: 2.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  94 GKIFRMKLGSFESVHLGSPCLLEALYRTesayPQRLE-------IKPWKayrdyrkeGYGLLILEGEDWQRVR----SAF 162
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIEVILSS----SKLITksflydfLKPWL--------GDGLLTSTGEKWRKRRklltPAF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 163 QKKLMKP-GEVMkldnkiNEVLADFMGRIDELCDerGHVEDLYSELNKWSFESIClvlyEKRFGLLQKNAGDEAVNFIMA 241
Cdd:cd20628   69 HFKILESfVEVF------NENSKILVEKLKKKAG--GGEFDIFPYISLCTLDIIC----ETAMGVKLNAQSNEDSEYVKA 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 242 IKTMMstfgRMMVTPVelhkslnTKVWqdhtLAWDTIF----------KSVKAC-------IDNRLEKYSQQPSA----- 299
Cdd:cd20628  137 VKRIL----EIILKRI-------FSPW----LRFDFIFrltslgkeqrKALKVLhdftnkvIKERREELKAEKRNseedd 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 300 -----------DFLCDIYHQNR-LSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVL-PENQVP 366
Cdd:cd20628  202 efgkkkrkaflDLLLEAHEDGGpLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFgDDDRRP 281

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 193083117 367 RAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd20628  282 TLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKG 327
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 92-412 1.11e-31

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: 125.39  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  92 KYGKIFRMKLGSFESVHLGSPCLLEALYRTE-SAYPQR----LEIKPWKAyrdyrkegyGLLILEGEDWQRVRSAF---- 162
Cdd:cd11055    1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKEfSNFTNRplfiLLDEPFDS---------SLLFLKGERWKRLRTTLsptf 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 163 --QK-KLMKPgevmkldnKINEVLADFMGRIDELCDERGHVE--DLYSELnkwSFESICLVLyekrFGL---LQKNAGDE 234
Cdd:cd11055   72 ssGKlKLMVP--------IINDCCDELVEKLEKAAETGKPVDmkDLFQGF---TLDVILSTA----FGIdvdSQNNPDDP 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 235 avnFIMAIKTMM--STFGRMMVT--PVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPsADFL---CDIYH 307
Cdd:cd11055  137 ---FLKAAKKIFrnSIIRLFLLLllFPLRLFLFLLFPFVFGFKSFSFLEDVVKKIIEQRRKNKSSRR-KDLLqlmLDAQD 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 308 QN------RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACL 381
Cdd:cd11055  213 SDedvskkKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVI 292

                        330       340       350
                 ....*....|....*....|....*....|.
gi 193083117 382 KESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd11055  293 NETLRLYPPAFFISRECKEDCTINGVFIPKG 323
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 93-412 1.35e-31

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: 125.46  E-value: 1.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  93 YGKIFRMK-LGSFESVHLGSPCLLEALYRTESAYPqrleiKPWKAYRDYRKE--GYGLLILEGEDWQRvrsafQKKLMKP 169
Cdd:cd11069    1 YGGLIRYRgLFGSERLLVTDPKALKHILVTNSYDF-----EKPPAFRRLLRRilGDGLLAAEGEEHKR-----QRKILNP 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 170 G----EVMKLDNKINEVLADFMGRIDELCDERGHVEDlYSELNKW----SFESICLVLYEKRFGLLQkNAGDEavnFIMA 241
Cdd:cd11069   71 AfsyrHVKELYPIFWSKAEELVDKLEEEIEESGDESI-SIDVLEWlsraTLDIIGLAGFGYDFDSLE-NPDNE---LAEA 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 242 IKTMMST-------FGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQP---SADFLCDIYHQN-- 309
Cdd:cd11069  146 YRRLFEPtllgsllFILLLFLPRWLVRILPWKANREIRRAKDVLRRLAREIIREKKAALLEGKddsGKDILSILLRANdf 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 310 ----RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPE--NQVPRAEDLRNMPYLKACLKE 383
Cdd:cd11069  226 addeRLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDppDGDLSYDDLDRLPYLNAVCRE 305

                        330       340
                 ....*....|....*....|....*....
gi 193083117 384 SMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd11069  306 TLRLYPPVPLTSREATKDTVIKGVPIPKG 334
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 144-404 7.39e-29

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: 117.69  E-value: 7.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 144 GYGLLILEGEDWQRVR----SAFQKKLMKpgEVMklDNKINEVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVL 219
Cdd:cd11064   48 GDGIFNVDGELWKFQRktasHEFSSRALR--EFM--ESVVREKVEKLLVPLLDHAAESGKVVDLQDVLQRFTFDVICKIA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 220 yekrFGL-LQKNAGDEAVN-FIMAIKTMMSTFGRMMVTPV---ELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKY- 293
Cdd:cd11064  124 ----FGVdPGSLSPSLPEVpFAKAFDDASEAVAKRFIVPPwlwKLKRWLNIGSEKKLREAIRVIDDFVYEVISRRREELn 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 294 ----SQQPSADFL-----CDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLP--- 361
Cdd:cd11064  200 sreeENNVREDLLsrflaSEEEEGEPVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPklt 279

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 193083117 362 --ENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVL 404
Cdd:cd11064  280 tdESRVPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVL 324
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 161-393 9.97e-29

cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Nectria haematococca cytochrome P450 57A1 (CYP57A1), also called pisatin demethylase, which detoxifies the phytoalexin pisatin; Penicillium aethiopicum P450 monooxygenase gsfF, also called griseofulvin synthesis protein F, which catalyzes the coupling of orcinol and phloroglucinol rings in griseophenone B to form desmethyl-dehydrogriseofulvin A during the biosynthesis of griseofulvin, a spirocyclic fungal natural product used to treat dermatophyte infections; and Penicillium aethiopicum P450 monooxygenase vrtE, also called viridicatumtoxin synthesis protein E, which catalyzes hydroxylation at C5 of the polyketide backbone during the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP57A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410683 [Multi-domain]  Cd Length: 425  Bit Score: 116.91  E-value: 9.97e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 161 AFQKKLMKPG----EVMKLDNKINEVLADFMGRIDELCDERGHVEdlyseLNKW----SFESICLVLYEKRFGLLqKNAG 232
Cdd:cd11060   58 AALRRKVASGysmsSLLSLEPFVDECIDLLVDLLDEKAVSGKEVD-----LGKWlqyfAFDVIGEITFGKPFGFL-EAGT 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 233 DEAvNFIMAIKTMMSTFGRMMVTPvELHKSLNTK----VWQDHTlAWDTIFKSVKACIDNRLEKYSQQPSA--DFLcDIY 306
Cdd:cd11060  132 DVD-GYIASIDKLLPYFAVVGQIP-WLDRLLLKNplgpKRKDKT-GFGPLMRFALEAVAERLAEDAESAKGrkDML-DSF 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 307 HQNRLSKKEL---YAAVTELQ---LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRA---EDLRNMPYL 377
Cdd:cd11060  208 LEAGLKDPEKvtdREVVAEALsniLAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGKLSSPitfAEAQKLPYL 287

                        250
                 ....*....|....*.
gi 193083117 378 KACLKESMRLTPSVPF 393
Cdd:cd11060  288 QAVIKEALRLHPPVGL 303
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 83-412 1.07e-27

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: 114.15  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  83 HDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLL-EALyrTESAYPqrleikpwKAYRDY---------RKEGYGLL-ILE 151
Cdd:cd20613    1 HDLLLEWAKEYGPVFVFWILHRPIVVVSDPEAVkEVL--ITLNLP--------KPPRVYsrlaflfgeRFLGNGLVtEVD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 152 GEDWQRVRS----AFQKKLMkpgevMKLDNKINEVLADFMGRIDELCDERGHVeDLYSELNKWSFESICLVLyekrFGLL 227
Cdd:cd20613   71 HEKWKKRRAilnpAFHRKYL-----KNLMDEFNESADLLVEKLSKKADGKTEV-NMLDEFNRVTLDVIAKVA----FGMD 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 228 QKNAGDEAVNFIMAIKTMMSTFGRMMVTPVelhkslntkvWQDHTLAWDTIfKSVKA-----------CIDNRLE--KYS 294
Cdd:cd20613  141 LNSIEDPDSPFPKAISLVLEGIQESFRNPL----------LKYNPSKRKYR-REVREaikflretgreCIEERLEalKRG 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 295 QQPSADFLCDIYhqnRLSKKELYAAVTELQ-------LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPR 367
Cdd:cd20613  210 EEVPNDILTHIL---KASEEEPDFDMEELLddfvtffIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVE 286

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 193083117 368 AEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd20613  287 YEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAG 331
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 95-413 1.52e-26

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: 110.72  E-value: 1.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  95 KIFRMKLGSFE-SVHLGSPCLLEALYRTESAYP---QRLeIKPWKayrdyrkeGYGLLILEGEDWQRVRsafqkKLMKPG 170
Cdd:cd20659    2 RAYVFWLGPFRpILVLNHPDTIKAVLKTSEPKDrdsYRF-LKPWL--------GDGLLLSNGKKWKRNR-----RLLTPA 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 171 ---EVMKLDNKI-NEVLADFMGRIDELCDERGHVEdLYSELNKWSFESI--CLVLYEKRfgLLQKNAGDEavnFIMAIKT 244
Cdd:cd20659   68 fhfDILKPYVPVyNECTDILLEKWSKLAETGESVE-VFEDISLLTLDIIlrCAFSYKSN--CQQTGKNHP---YVAAVHE 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 245 MMSTFGRMMVTPVELHKSL-----NTKVWQD-----HTLAWDTIFKSVKACIDNRLEKYSQQPSADFLcDIYHQ------ 308
Cdd:cd20659  142 LSRLVMERFLNPLLHFDWIyyltpEGRRFKKacdyvHKFAEEIIKKRRKELEDNKDEALSKRKYLDFL-DILLTardedg 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 309 NRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLT 388
Cdd:cd20659  221 KGLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLY 300

                        330       340
                 ....*....|....*....|....*
gi 193083117 389 PSVPFTTRTLDKATVLGEYALPKGI 413
Cdd:cd20659  301 PPVPFIARTLTKPITIDGVTLPAGT 325
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 178-414 5.46e-26

cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces viciae-fabae cytochrome P450 67 (CYP67), also called planta-induced rust protein 16, Cystobasidium minutum (Rhodotorula minuta) cytochrome P450rm, and other fungal cytochrome P450s. P450rm catalyzes the formation of isobutene and 4-hydroxylation of benzoate. The gene encoding CYP67 is a planta-induced gene that is expressed in haustoria and rust-infected leaves. The CYP67-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410684 [Multi-domain]  Cd Length: 418  Bit Score: 109.23  E-value: 5.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 178 KINEVLADFMGRIDELCDERGHVEDLYSELNKW-SFESICLVLYEKRFGLLQKnaGDEAVNFIMAIKTMM--STFGRMM- 253
Cdd:cd11061   76 RILSHVEQLCEQLDDRAGKPVSWPVDMSDWFNYlSFDVMGDLAFGKSFGMLES--GKDRYILDLLEKSMVrlGVLGHAPw 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 254 VTPVELHKSLNTKVWQDhtlaWDTIFKSVKACIDNRLEkySQQPSADflcDIYH----------QNRLSKKELYAAVTEL 323
Cdd:cd11061  154 LRPLLLDLPLFPGATKA----RKRFLDFVRAQLKERLK--AEEEKRP---DIFSylleakdpetGEGLDLEELVGEARLL 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 324 QLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRA-EDLRNMPYLKACLKESMRLTPSVPFTT--RTLDK 400
Cdd:cd11061  225 IVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLgPKLKSLPYLRACIDEALRLSPPVPSGLprETPPG 304

                        250
                 ....*....|....*
gi 193083117 401 -ATVLGEYaLPKGIV 414
Cdd:cd11061  305 gLTIDGEY-IPGGTT 318
PTZ00404 PTZ00404
cytochrome P450; Provisional
 58-412 2.41e-25

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 107.89  E-value: 2.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  58 LPGPTSWPLLGSLLQILwkgglKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALY-RTESAYPQRLEIKPWKA 136
Cdd:PTZ00404  31 LKGPIPIPILGNLHQLG-----NLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFvDNFDNFSDRPKIPSIKH 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 137 YRDYRkegyGLLILEGEDWQRVRSAFQKklmkpgeVMKLDN--KINEVLADfmgridelcdergHVEDLYSELNKW--SF 212
Cdd:PTZ00404 106 GTFYH----GIVTSSGEYWKRNREIVGK-------AMRKTNlkHIYDLLDD-------------QVDVLIESMKKIesSG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 213 ESICLVLYEKRFGL--LQKNAGDEAVNF------------IMAIKTMMSTFGRMMVTPV-ELHKSLNTKvWQDHTlawDT 277
Cdd:PTZ00404 162 ETFEPRYYLTKFTMsaMFKYIFNEDISFdedihngklaelMGPMEQVFKDLGSGSLFDViEITQPLYYQ-YLEHT---DK 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 278 IFKSVKACIDNRLEKY-------SQQPSADFLCDIY----HQNRLSkkeLYAAVTELQLAAVETTANSLMWILYNLSRNP 346
Cdd:PTZ00404 238 NFKKIKKFIKEKYHEHlktidpeVPRDLLDLLIKEYgtntDDDILS---ILATILDFFLAGVDTSATSLEWMVLMLCNYP 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193083117 347 QVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPF--TTRTLDKATVLGEYALPKG 412
Cdd:PTZ00404 315 EIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFglPRSTSNDIIIGGGHFIPKD 382
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 93-412 1.21e-24

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: 105.37  E-value: 1.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  93 YGKIFRMKLGSFESVHLGSPCLL-EALYRTESAYPQRleikPWKAYRDYRKEGYGLLILE--GEDWQRVRSAFQKKL-MK 168
Cdd:cd11027    1 YGDVFSLYLGSRLVVVLNSGAAIkEALVKKSADFAGR----PKLFTFDLFSRGGKDIAFGdySPTWKLHRKLAHSALrLY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 169 PGEVMKLDNKINEVLADFMGRIDElCDERGHveDLYSELNKWSFESICLVLYEKRFGLlqknaGDEAVNFIMAI------ 242
Cdd:cd11027   77 ASGGPRLEEKIAEEAEKLLKRLAS-QEGQPF--DPKDELFLAVLNVICSITFGKRYKL-----DDPEFLRLLDLndkffe 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 243 -------------------------KTMMSTFGRMMVTPVELHK-SLNTKVWQDHTlawDTIFKSVKACIDNRLEKYSQq 296
Cdd:cd11027  149 llgagslldifpflkyfpnkalrelKELMKERDEILRKKLEEHKeTFDPGNIRDLT---DALIKAKKEAEDEGDEDSGL- 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 297 psadflcdiyhqnrLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPY 376
Cdd:cd11027  225 --------------LTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPY 290

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 193083117 377 LKACLKESMRLTPSVP-----FTTRtlDkaTVLGEYALPKG 412
Cdd:cd11027  291 LEATIAEVLRLSSVVPlalphKTTC--D--TTLRGYTIPKG 327
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 144-419 9.54e-24

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: 102.68  E-value: 9.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 144 GYGLLILEGEDWQRVRsafqkKLMKPGevmkLDNKI--------NEVLADFMGRIDELCDerGHVEDLYSELNKWSFESI 215
Cdd:cd11057   44 GRGLFSAPYPIWKLQR-----KALNPS----FNPKIllsflpifNEEAQKLVQRLDTYVG--GGEFDILPDLSRCTLEMI 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 216 CLVLyekrFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVTPvELHK---SLNTKVWQDHTLAWDTIFKSVKACID---NR 289
Cdd:cd11057  113 CQTT----LGSDVNDESDGNEEYLESYERLFELIAKRVLNP-WLHPefiYRLTGDYKEEQKARKILRAFSEKIIEkklQE 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 290 LEKYSQQPSADF-------------LCDIYHQ-NRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKE 355
Cdd:cd11057  188 VELESNLDSEEDeengrkpqifidqLLELARNgEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEE 267

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193083117 356 IQSVLPE-NQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLG-EYALPKGIVRKYDI 419
Cdd:cd11057  268 IMEVFPDdGQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDI 333
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 296-412 2.53e-23

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: 101.55  E-value: 2.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 296 QPSADFLCDIYH-------QNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRA 368
Cdd:cd11075  205 KDYTDFLLLDLLdlkeeggERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTE 284

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 193083117 369 EDLRNMPYLKACLKESMRLTPSVPFT-TRTLDKATVLGEYALPKG 412
Cdd:cd11075  285 EDLPKMPYLKAVVLETLRRHPPGHFLlPHAVTEDTVLGGYDIPAG 329
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 312-412 3.44e-23

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: 101.09  E-value: 3.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 312 SKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSV 391
Cdd:cd11063  213 DPKELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPV 292

                         90       100
                 ....*....|....*....|.
gi 193083117 392 PFTTRTLDKATVlgeyaLPKG 412
Cdd:cd11063  293 PLNSRVAVRDTT-----LPRG 308
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 146-426 5.20e-23

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: 100.79  E-value: 5.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 146 GLLILEGEDWQRVR----SAF---QKKLMKPgevmkldnKINEVLADFmgrIDELCDERGHVEDLY-------------- 204
Cdd:cd20621   50 GLLFSEGEEWKKQRkllsNSFhfeKLKSRLP--------MINEITKEK---IKKLDNQNVNIIQFLqkitgevvirsffg 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 205 SELNKWSFE----SICLVLYEKRFGLLQKNagdeavNFIMAIKTMMstFGRMMVT--PVELHKSLNTKVwqdhtlawDTI 278
Cdd:cd20621  119 EEAKDLKINgkeiQVELVEILIESFLYRFS------SPYFQLKRLI--FGRKSWKlfPTKKEKKLQKRV--------KEL 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 279 FKSVKACIDNRLEKYSQQPSADF----------LCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQV 348
Cdd:cd20621  183 RQFIEKIIQNRIKQIKKNKDEIKdiiidldlylLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEI 262

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193083117 349 QQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFT-TRTLDKATVLGEYALPKGIVRKYDIQATDNEP 426
Cdd:cd20621  263 QEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLfPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNP 341
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 144-414 2.36e-22

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: 98.89  E-value: 2.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 144 GYGLLILEGEDWqrvrsaFQ-KKLMKPG---EVMKLDNKInevLAD----FMGRIDELCDERGHVEdLYSELNKWSFESI 215
Cdd:cd20678   57 GKGLLVLNGQKW------FQhRRLLTPAfhyDILKPYVKL---MADsvrvMLDKWEKLATQDSSLE-IFQHVSLMTLDTI 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 216 --CLVLYEkrfGLLQKNAGDEavNFIMAIKTMMS-TFGRMMVTP--------VELHKSLNTKVWQ---DHTlawDTIFKS 281
Cdd:cd20678  127 mkCAFSHQ---GSCQLDGRSN--SYIQAVSDLSNlIFQRLRNFFyhndfiykLSPHGRRFRRACQlahQHT---DKVIQQ 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 282 VKACIDN--RLEKYSQQPSADFLcDIY------HQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLL 353
Cdd:cd20678  199 RKEQLQDegELEKIKKKRHLDFL-DILlfakdeNGKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCR 277

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193083117 354 KEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKA-TVLGEYALPKGIV 414
Cdd:cd20678  278 EEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPvTFPDGRSLPAGIT 339
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 181-412 9.18e-22

Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is considerably larger than in other taxa. In individual plant genomes, CYPs form the third largest family of plant genes; the two largest gene families code for F-box proteins and receptor-like kinases. CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. However, there is a phenomenon called family creep, where a sequence (below 40% identity) is absorbed into a large family; this is seen in the plant CYP71 and CYP89 families. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP71 clan has expanded dramatically and represents 50% of all plant CYPs; it includes several families including CYP71, CYP73, CYP76, CYP81, CYP82, CYP89, and CYP93, among others. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410711 [Multi-domain]  Cd Length: 429  Bit Score: 96.85  E-value: 9.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 181 EVLADFMGRIDELCdERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVT---P- 256
Cdd:cd20618   87 EELSHLVKSLLEES-ESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEAREFKELIDEAFELAGAFNIGdyiPw 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 257 -------------VELHKSLN---TKVWQDHtlawdtifksvKACIDNRLEKYSQQPSADFLCDIYHQNRLSKKELYAAV 320
Cdd:cd20618  166 lrwldlqgyekrmKKLHAKLDrflQKIIEEH-----------REKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALL 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 321 TELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTT-RTLD 399
Cdd:cd20618  235 LDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLpHEST 314

                        250
                 ....*....|...
gi 193083117 400 KATVLGEYALPKG 412
Cdd:cd20618  315 EDCKVAGYDIPAG 327
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 92-412 1.01e-21

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: 96.50  E-value: 1.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  92 KYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWkaYRDYRKEGYGLLILEGEDWQRVRSAFQKkLMKPGE 171
Cdd:COG2124   30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEV--LRPLPLLGDSLLTLDGPEHTRLRRLVQP-AFTPRR 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 172 VMKLDNKINEVladfmgrIDELCDE---RGHVeDLYSELNKWSFESICLVLyekrFGLlqknAGDEAVNFIMAIKTMMST 248
Cdd:COG2124  107 VAALRPRIREI-------ADELLDRlaaRGPV-DLVEEFARPLPVIVICEL----LGV----PEEDRDRLRRWSDALLDA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 249 FGRmmvtpvelhksLNTKVWQDHTLAWDTIFKSVKACIDNRLekysQQPSADFLCDI----YHQNRLSKKELYAAVTELQ 324
Cdd:COG2124  171 LGP-----------LPPERRRRARRARAELDAYLRELIAERR----AEPGDDLLSALlaarDDGERLSDEELRDELLLLL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 325 LAAVETTANSLMWILYNLSRNPQVQQKLlkeiqsvlpenqvpRAEDlrnmPYLKACLKESMRLTPSVPFTTRTLDKATVL 404
Cdd:COG2124  236 LAGHETTANALAWALYALLRHPEQLARL--------------RAEP----ELLPAAVEETLRLYPPVPLLPRTATEDVEL 297


                 ....*...
gi 193083117 405 GEYALPKG 412
Cdd:COG2124  298 GGVTIPAG 305
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 179-414 2.75e-21

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: 95.44  E-value: 2.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 179 INEVLADFMGRIDElCDERGHVEDLYSELNKWSFESICLVLYEKRFG--LLQKNAGDEAVN-----FIMAIKTM-MSTFG 250
Cdd:cd11059   80 IRERVLPLIDRIAK-EAGKSGSVDVYPLFTALAMDVVSHLLFGESFGtlLLGDKDSRERELlrrllASLAPWLRwLPRYL 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 251 RMMVTPVelhkslntkVWQDHTLAWDTIFKSVKACIDnRLEKYSQQPSADFL--------CDIYHQNRLSKKELYAAVTE 322
Cdd:cd11059  159 PLATSRL---------IIGIYFRAFDEIEEWALDLCA-RAESSLAESSDSESltvlllekLKGLKKQGLDDLEIASEALD 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 323 LQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSV-LPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFT-TRTLDK 400
Cdd:cd11059  229 HIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLpGPFRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSlPRVVPE 308

                        250
                 ....*....|....*
gi 193083117 401 A-TVLGEYALPKGIV 414
Cdd:cd11059  309 GgATIGGYYIPGGTI 323
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 85-412 3.80e-21

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: 94.96  E-value: 3.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  85 TLVEYHKKYGKIFRMKLGSFESVH-LGSPCLLEALYRTESAYPQRLE----IKPWkayrdyrkEG-YGLLILEGEDWQRv 158
Cdd:cd11053    3 FLERLRARYGDVFTLRVPGLGPVVvLSDPEAIKQIFTADPDVLHPGEgnslLEPL--------LGpNSLLLLDGDRHRR- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 159 rsafQKKLMKP---GEVMKldnkineVLADFMGRI-DELCDE--RGHVEDLYSELNKWSFESICLVLyekrFGLlqkNAG 232
Cdd:cd11053   74 ----RRKLLMPafhGERLR-------AYGELIAEItEREIDRwpPGQPFDLRELMQEITLEVILRVV----FGV---DDG 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 233 DEAVNFIMAIKTMMSTFGRMMVT-PVELHKSLNTKVWQdhtlawdtIFKSVKACIDNRLEKYSQQPSADFLC---DI--- 305
Cdd:cd11053  136 ERLQELRRLLPRLLDLLSSPLASfPALQRDLGPWSPWG--------RFLRARRRIDALIYAEIAERRAEPDAerdDIlsl 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 306 -----YHQ-NRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPEnqvPRAEDLRNMPYLKA 379
Cdd:cd11053  208 llsarDEDgQPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGD---PDPEDIAKLPYLDA 284

                        330       340       350
                 ....*....|....*....|....*....|...
gi 193083117 380 CLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd11053  285 VIKETLRLYPVAPLVPRRVKEPVELGGYTLPAG 317
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 93-412 7.63e-21

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: 94.25  E-value: 7.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  93 YGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIkpWKAYRDYRkeGYGLLILEGEDWQRvrsafQKKLMKP--- 169
Cdd:cd11049   12 HGDLVRIRLGPRPAYVVTSPELVRQVLVNDRVFDKGGPL--FDRARPLL--GNGLATCPGEDHRR-----QRRLMQPafh 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 170 -------GEVMkldnkinevlADfmgRIDELCD--ERGHVEDLYSELNKWSFESICLVLYEKRFGllqknagDEAVNFIM 240
Cdd:cd11049   83 rsripayAEVM----------RE---EAEALAGswRPGRVVDVDAEMHRLTLRVVARTLFSTDLG-------PEAAAELR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 241 -AIKTMMSTFGRMMVTPVELHKsLNTKVWQDHTLAWDTIFKSVKACIDNRLEkySQQPSADFL------CDiYHQNRLSK 313
Cdd:cd11049  143 qALPVVLAGMLRRAVPPKFLER-LPTPGNRRFDRALARLRELVDEIIAEYRA--SGTDRDDLLslllaaRD-EEGRPLSD 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 314 KELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPeNQVPRAEDLRNMPYLKACLKESMRLTPSVPF 393
Cdd:cd11049  219 EELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWL 297

                        330
                 ....*....|....*....
gi 193083117 394 TTRTLDKATVLGEYALPKG 412
Cdd:cd11049  298 LTRRTTADVELGGHRLPAG 316
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 92-422 8.64e-21

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: 94.32  E-value: 8.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  92 KYGKIFRMKLGSFEsVHLGSPCLLEALYRTESAYPQRLEIKPWKAYrdyrkegYGLLIL--EGEDWQRVRsafqkKLMKP 169
Cdd:cd11070    1 KLGAVKILFVSRWN-ILVTKPEYLTQIFRRRDDFPKPGNQYKIPAF-------YGPNVIssEGEDWKRYR-----KIVAP 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 170 G---EVMKLDnkINEVLADFMGRIDELCDERGHVEDLYSE----LNKWSFESICLVLYEKRFGLLQKNAGDEAVnFIMAI 242
Cdd:cd11070   68 AfneRNNALV--WEESIRQAQRLIRYLLEEQPSAKGGGVDvrdlLQRLALNVIGEVGFGFDLPALDEEESSLHD-TLNAI 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 243 KTMMSTFGRMMVTPVElhkSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPS---------ADFLCDIYHQNRLSK 313
Cdd:cd11070  145 KLAIFPPLFLNFPFLD---RLPWVLFPSRKRAFKDVDEFLSELLDEVEAELSADSKgkqgtesvvASRLKRARRSGGLTE 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 314 KELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLP--ENQVPRAEDLRNMPYLKACLKESMRLTPSV 391
Cdd:cd11070  222 KELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGdePDDWDYEEDFPKLPYLLAVIYETLRLYPPV 301

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 193083117 392 PFTTRTLDKATVL-----GEYALPKGIVRKYDIQAT 422
Cdd:cd11070  302 QLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYAT 337
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 59-412 1.55e-20

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 94.12  E-value: 1.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  59 PGPTSWPLLGSLLQIlwkGGLKkqHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLL-EALYRTESAYPQRleikPWKAY 137
Cdd:PLN03112  35 PGPPRWPIVGNLLQL---GPLP--HRDLASLCKKYGPLVYLRLGSVDAITTDDPELIrEILLRQDDVFASR----PRTLA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 138 RDYRKEGYGLLILE--GEDWQRVRSAFQKKLMKPgevMKLDNKINEVL--ADFMGRIDELCDERGHVEDLYSELNKWSFE 213
Cdd:PLN03112 106 AVHLAYGCGDVALAplGPHWKRMRRICMEHLLTT---KRLESFAKHRAeeARHLIQDVWEAAQTGKPVNLREVLGAFSMN 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 214 SICLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMV---TPV--------------ELHKSLN---TKVWQDHTl 273
Cdd:PLN03112 183 NVTRMLLGKQYFGAESAGPKEAMEFMHITHELFRLLGVIYLgdyLPAwrwldpygcekkmrEVEKRVDefhDKIIDEHR- 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 274 awdtifksvkaciDNRLEKYSQQPSADF---LCDIYHQN---RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQ 347
Cdd:PLN03112 262 -------------RARSGKLPGGKDMDFvdvLLSLPGENgkeHMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPR 328

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193083117 348 VQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTT-RTLDKATVLGEYALPKG 412
Cdd:PLN03112 329 VLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIpHESLRATTINGYYIPAK 394
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 330-412 2.40e-20

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: 92.71  E-value: 2.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 330 TTANSLMWILYNLSRNPQVQQKLLKEIQSVL-PENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYA 408
Cdd:cd20660  247 TTAAAINWALYLIGSHPEVQEKVHEELDRIFgDSDRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYT 326


                 ....
gi 193083117 409 LPKG 412
Cdd:cd20660  327 IPKG 330
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 107-412 3.02e-20

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: 92.32  E-value: 3.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 107 VHLGSPCLLEALYRTESaypqRLEIKPWKAYRDYRKEGYGLLILEGEDWQRVRSA----FQKKlmkpgEVMKLDNKINEV 182
Cdd:cd11062   11 LHISDPDFYDEIYAGGS----RRRKDPPYFYGAFGAPGSTFSTVDHDLHRLRRKAlspfFSKR-----SILRLEPLIQEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 183 LADFMGRIDELCdERGHVEDLYSELNKWSFESICLVLYEKRFGLLqknagdEAVNFIMAIKTMMSTFGRMMVT----PVe 258
Cdd:cd11062   82 VDKLVSRLREAK-GTGEPVNLDDAFRALTADVITEYAFGRSYGYL------DEPDFGPEFLDALRALAEMIHLlrhfPW- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 259 LHKSLN------TKVWQDHTLAWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYH--------QNRLSKKELYAAVTELQ 324
Cdd:cd11062  154 LLKLLRslpeslLKRLNPGLAVFLDFQESIAKQVDEVLRQVSAGDPPSIVTSLFHallnsdlpPSEKTLERLADEAQTLI 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 325 LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPE-NQVPRAEDLRNMPYLKACLKESMRLTPSVPftTR----TLD 399
Cdd:cd11062  234 GAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDpDSPPSLAELEKLPYLTAVIKEGLRLSYGVP--TRlprvVPD 311

                        330
                 ....*....|...
gi 193083117 400 KATVLGEYALPKG 412
Cdd:cd11062  312 EGLYYKGWVIPPG 324
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 147-412 5.01e-20

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: 91.83  E-value: 5.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 147 LLILEGEDWQRVRS----AFQKKLMKpgevmKLDNKINEVLADFMGRIDELCDERGHVE--DLYSelnKWSFESICLVLy 220
Cdd:cd11056   53 LFSLDGEKWKELRQkltpAFTSGKLK-----NMFPLMVEVGDELVDYLKKQAEKGKELEikDLMA---RYTTDVIASCA- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 221 ekrFGL----LQKN------AGDEAV--NFIMAIKTMMSTFGRmmvtpvELHKSLNTKVW-QDHTlawDTIFKSVKACID 287
Cdd:cd11056  124 ---FGLdansLNDPenefreMGRRLFepSRLRGLKFMLLFFFP------KLARLLRLKFFpKEVE---DFFRKLVRDTIE 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 288 NRLEKYSQQPsaDF---LCDIYHQNRLSKKELYAAVTELQLAAV---------ETTANSLMWILYNLSRNPQVQQKLLKE 355
Cdd:cd11056  192 YREKNNIVRN--DFidlLLELKKKGKIEDDKSEKELTDEELAAQafvfflagfETSSSTLSFALYELAKNPEIQEKLREE 269

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 356 IQSVLPE-NQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGE--YALPKG 412
Cdd:cd11056  270 IDEVLEKhGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGtdVVIEKG 329
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 94-412 5.26e-20

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: 91.61  E-value: 5.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  94 GKIFRMKLGSFESVHLGSPCLLEALYRtesaypQRleikPwKAYRDYR------KE--GYGLLILEGEDWQRVR----SA 161
Cdd:cd11083    1 GSAYRFRLGRQPVLVISDPELIREVLR------RR----P-DEFRRISslesvfREmgINGVFSAEGDAWRRQRrlvmPA 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 162 FQkklmkPGEVMKLDNKINEVLADFMGRIDELCDErGHVEDLYSELNKWSFESICLV-------LYEKRFGLLQKNagde 234
Cdd:cd11083   70 FS-----PKHLRYFFPTLRQITERLRERWERAAAE-GEAVDVHKDLMRYTVDVTTSLafgydlnTLERGGDPLQEH---- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 235 avnfimaIKTMMSTFGRMMVTPVELHKSLNTKvwQDHTL--AWDTIFKSVKACID---NRLEKYSQQPSADFLCDIY--- 306
Cdd:cd11083  140 -------LERVFPMLNRRVNAPFPYWRYLRLP--ADRALdrALVEVRALVLDIIAaarARLAANPALAEAPETLLAMmla 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 307 ---HQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVL--PENQVPRaEDLRNMPYLKACL 381
Cdd:cd11083  211 eddPDARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLggARVPPLL-EALDRLPYLEAVA 289

                        330       340       350
                 ....*....|....*....|....*....|.
gi 193083117 382 KESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd11083  290 RETLRLKPVAPLLFLEPNEDTVVGDIALPAG 320
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 132-412 5.57e-18

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: 85.71  E-value: 5.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 132 KPWKAYRDYRKEGYGLLILEGEDWQRVRS----AFQKKLMKPGEVMkldnkINEVLADFMGRIDELCDERGHVEdlyseL 207
Cdd:cd11058   35 KDPRFYPPAPNGPPSISTADDEDHARLRRllahAFSEKALREQEPI-----IQRYVDLLVSRLRERAGSGTPVD-----M 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 208 NKW----SFESIC-LVLYEkRFGLLQKNAGDEAVNFIM-AIK--TMMSTFGRMMVTPVELHKSLNTKVWQDhtlaWDTIF 279
Cdd:cd11058  105 VKWfnftTFDIIGdLAFGE-SFGCLENGEYHPWVALIFdSIKalTIIQALRRYPWLLRLLRLLIPKSLRKK----RKEHF 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 280 KSVKACIDNRLEKYSQQPsaDFlcdIYH-------QNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKL 352
Cdd:cd11058  180 QYTREKVDRRLAKGTDRP--DF---MSYilrnkdeKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKL 254

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193083117 353 LKEIQSvlpenQVPRAED-----LRNMPYLKACLKESMRLTPSVP-FTTRTLDK--ATVLGEYaLPKG 412
Cdd:cd11058  255 VDEIRS-----AFSSEDDitldsLAQLPYLNAVIQEALRLYPPVPaGLPRVVPAggATIDGQF-VPGG 316
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 329-412 8.49e-18

cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome P450/NADPH--P450 reductase; Cytochrome P450 102A1, also called cytochrome P450(BM-3) or P450BM-3, is a bifunctional cytochrome P450/NADPH--P450 reductase. These proteins fuse an N-terminal cytochrome p450 with a C-terminal cytochrome p450 reductase (CYPOR). It functions as a fatty acid monooxygenase, catalyzing the hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, with activity towards fatty acids with a chain length of 9-18 carbons. Its NADPH-dependent reductase activity (via the C-terminal domain) allows electron transfer from NADPH to the heme iron of the N-terminal cytochrome P450. CYP120A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 84.93  E-value: 8.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 329 ETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPeNQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVL-GEY 407
Cdd:cd11068  244 ETTSGLLSFALYYLLKNPEVLAKARAEVDEVLG-DDPPPYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLgGKY 322


                 ....*
gi 193083117 408 ALPKG 412
Cdd:cd11068  323 PLKKG 327
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 286-426 1.53e-17

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: 84.36  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 286 IDNRLEKYSQQPSADFLcDIY------HQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSV 359
Cdd:cd20679  210 VDDFLKAKAKSKTLDFI-DVLllskdeDGKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQEL 288

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 360 LPENQVPRAE--DLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVL-GEYALPKGIVRKYDIQATDNEP 426
Cdd:cd20679  289 LKDREPEEIEwdDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIYGTHHNP 358
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 282-412 1.99e-17

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: 83.81  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 282 VKACIDNRLEKYSQQPSADFLcDIYHQNRLSKKELYAAVTELQL---------AAVETTANSLMWILYNLSRNPQVQQKL 352
Cdd:cd20651  184 LKEEIKEHKKTYDEDNPRDLI-DAYLREMKKKEPPSSSFTDDQLvmicldlfiAGSETTSNTLGFAFLYLLLNPEVQRKV 262

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193083117 353 LKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTT--RTLdKATVLGEYALPKG 412
Cdd:cd20651  263 QEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIGIphRAL-KDTTLGGYRIPKD 323
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 152-412 3.01e-17

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: 83.40  E-value: 3.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 152 GEDWQRVRSAFQKkLMKPGEVMKL----DNKINEVLADFMGRIDelcderghveDLYSELNKWSFESICLVLYEKRFgll 227
Cdd:cd11065   59 GPRWRLHRRLFHQ-LLNPSAVRKYrplqELESKQLLRDLLESPD----------DFLDHIRRYAASIILRLAYGYRV--- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 228 qKNAGDEavnFIMAIKTMMSTFGRMMV---TPVELHKSLN--------------TKVWQDHTLAWDTIFKSVKAcidnRL 290
Cdd:cd11065  125 -PSYDDP---LLRDAEEAMEGFSEAGSpgaYLVDFFPFLRylpswlgapwkrkaRELRELTRRLYEGPFEAAKE----RM 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 291 EKYSQQPS--ADFLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRA 368
Cdd:cd11065  197 ASGTATPSfvKDLLEELDKEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTF 276

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 193083117 369 EDLRNMPYLKACLKESMRLTPSVPF-TTRTLDKATVLGEYALPKG 412
Cdd:cd11065  277 EDRPNLPYVNAIVKEVLRWRPVAPLgIPHALTEDDEYEGYFIPKG 321
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 90-422 3.06e-17

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: 83.49  E-value: 3.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  90 HKKYGKIFRMKLgsfesvhLGSPCLlealYRTESAYPQRL---EIKPWKA--YRDYRK--EGYGLLILEGEDWQRVRS-- 160
Cdd:cd11044   18 YQKYGPVFKTHL-------LGRPTV----FVIGAEAVRFIlsgEGKLVRYgwPRSVRRllGENSLSLQDGEEHRRRRKll 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 161 --AFQKKLMKpGEVMKLDNKINEVLADFMGRiDELCderghvedLYSELNKWSFESICLVLyekrfglLQKNAGDEAVNF 238
Cdd:cd11044   87 apAFSREALE-SYVPTIQAIVQSYLRKWLKA-GEVA--------LYPELRRLTFDVAARLL-------LGLDPEVEAEAL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 239 IMAIKTMMSTfgrMMVTPVELHKSLNTKVWQdhtlAWDTIFKSVKACIDNRLEKySQQPSADFLcDIY------HQNRLS 312
Cdd:cd11044  150 SQDFETWTDG---LFSLPVPLPFTPFGRAIR----ARNKLLARLEQAIRERQEE-ENAEAKDAL-GLLleakdeDGEPLS 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 313 KKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEiQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVP 392
Cdd:cd11044  221 MDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQE-QDALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVG 299

                        330       340       350
                 ....*....|....*....|....*....|
gi 193083117 393 FTTRTLDKATVLGEYALPKGIVRKYDIQAT 422
Cdd:cd11044  300 GGFRKVLEDFELGGYQIPKGWLVYYSIRDT 329
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 308-414 4.29e-17

cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three functional human members: CYP1A1, CYP1A2 and CYP1B1, which are regulated by the aryl hydrocarbon receptor (AhR), ligand-activated transcriptional factor that dimerizes with AhR nuclear translocator (ARNT). CYP1 enzymes are involved in the metabolism of endogenous hormones, xenobiotics, and drugs. Included in the CYP1 family is CYP1D1 (cytochrome P450 family 1, subfamily D, polypeptide 1), which is not expressed in humans as its gene is pseudogenized due to five nonsense mutations in the putative coding region, but is functional in in other organisms including cynomolgus monkey. Zebrafish CYP1D1 expression is not regulated by AhR. The CYP1 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 83.12  E-value: 4.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 308 QNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRL 387
Cdd:cd11028  224 EVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRH 303

                         90       100
                 ....*....|....*....|....*...
gi 193083117 388 TPSVPFTT-RTLDKATVLGEYALPKGIV 414
Cdd:cd11028  304 SSFVPFTIpHATTRDTTLNGYFIPKGTV 331
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 309-413 2.02e-16

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: 80.96  E-value: 2.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 309 NRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVP-RAEDLRNMPYLKACLKESMRL 387
Cdd:cd20680  237 NKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDRPvTMEDLKKLRYLECVIKESLRL 316

                         90       100
                 ....*....|....*....|....*.
gi 193083117 388 TPSVPFTTRTLDKATVLGEYALPKGI 413
Cdd:cd20680  317 FPSVPLFARSLCEDCEIRGFKVPKGV 342
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 59-410 2.14e-16

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 81.28  E-value: 2.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  59 PGPTSWPLLGSLLQIlwkGGLKKQHdTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTE----SAYPQrLEIKPW 134
Cdd:PLN03234  31 PGPKGLPIIGNLHQM---EKFNPQH-FLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQdlnfTARPL-LKGQQT 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 135 KAYRDyRKEGYGLLILEgedWQRVRSAFQKKLMKPGEVMKLDNKINEVLADFMGRIDELCDERGHVeDLYSELNKWSFES 214
Cdd:PLN03234 106 MSYQG-RELGFGQYTAY---YREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTV-DLSELLLSFTNCV 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 215 ICLVLYEKRFgllqKNAGDEAVNFIMAIKTMMSTFGRMMVTPV------------------ELHKSLNTKVWQ--DHTLA 274
Cdd:PLN03234 181 VCRQAFGKRY----NEYGTEMKRFIDILYETQALLGTLFFSDLfpyfgfldnltglsarlkKAFKELDTYLQEllDETLD 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 275 WDTIFKSVKACIDNRLEKYSQQPsadFLCDIYHQNrlskkeLYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLK 354
Cdd:PLN03234 257 PNRPKQETESFIDLLMQIYKDQP---FSIKFTHEN------VKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQD 327

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 355 EIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFttrTLDKATV----LGEYALP 410
Cdd:PLN03234 328 EVRNVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPI---LLHRETIadakIGGYDIP 384
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 325-412 4.04e-16

fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 monooxygenase TRI13, also called core trichothecene cluster (CTC) protein 13, and similar proteins. The tri13 gene is located in the trichothecene biosynthesis gene cluster in Fusarium species, which produce a great diversity of agriculturally important trichothecene toxins that differ from each other in their pattern of oxygenation and esterification. Trichothecenes comprise a large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including the T2-toxin; TRI13 is required for the addition of the C-4 oxygen of T-2 toxin. The TRI13-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: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 80.42  E-value: 4.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 325 LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLP----ENQVPRAEDLRNM--PYLKACLKESMRLTPSVPFTTR-T 397
Cdd:cd20622  272 IAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPeavaEGRLPTAQEIAQAriPYLDAVIEEILRCANTAPILSReA 351

                         90
                 ....*....|....*
gi 193083117 398 LDKATVLGeYALPKG 412
Cdd:cd20622  352 TVDTQVLG-YSIPKG 365
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 93-428 6.01e-16

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: 79.46  E-value: 6.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  93 YGKIFRMKLGSFESVHL-GSPCLLEALYRTESAYPQRleikPWKAYRDYRKEGYGLLILEGEDWQRVRSAFQKKLMKPGE 171
Cdd:cd20662    1 YGNIFSLQLGSISSVIVtGLPLIKEALVTQEQNFMNR----PETPLRERIFNKNGLIFSSGQTWKEQRRFALMTLRNFGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 172 VMK-LDNKINEVlADFMgrIDELCDERGHVEDLYSELNKWSFESICLVLYEKRF--------GLLQKNagDEAVNFIMAI 242
Cdd:cd20662   77 GKKsLEERIQEE-CRHL--VEAIREEKGNPFNPHFKINNAVSNIICSVTFGERFeyhdewfqELLRLL--DETVYLEGSP 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 243 KTMM-STFGRMMVTPVELHKSLNTKvwqdhtlaWDTIFKSVKACIDNRLEKYSQQPSADFLcDIYHQNRLSKKE------ 315
Cdd:cd20662  152 MSQLyNAFPWIMKYLPGSHQTVFSN--------WKKLKLFVSDMIDKHREDWNPDEPRDFI-DAYLKEMAKYPDpttsfn 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 316 ---LYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVP 392
Cdd:cd20662  223 eenLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIP 302

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 193083117 393 FTT-RTLDKATVLGEYALPKGIVRKYDIQATDNEPVE 428
Cdd:cd20662  303 LNVpREVAVDTKLAGFHLPKGTMILTNLTALHRDPKE 339
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 326-412 8.03e-16

cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including insect cytochrome P450 306A1 (CYP306A1 or Cyp306a1) and CYP18A1. CYP306A1 functions as a carbon 25-hydroxylase and has an essential role in ecdysteroid biosynthesis during insect development. CYP18A1 is a 26-hydroxylase and plays a key role in steroid hormone inactivation. The CYP306A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 78.99  E-value: 8.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 326 AAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPF-TTRTLDKATVL 404
Cdd:cd20652  245 AGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPLgIPHGCTEDAVL 324


                 ....*...
gi 193083117 405 GEYALPKG 412
Cdd:cd20652  325 AGYRIPKG 332
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 286-412 1.18e-15

cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant cytochrome P450 family 76 (CYP76 or Cyp76) include: Catharanthus roseus CYP76B6, a multifunctional enzyme catalyzing two sequential oxidation steps leading to the formation of 8-oxogeraniol from geraniol; the Brassicaceae-specific CYP76C subfamily of enzymes that are involved in the metabolism of monoterpenols and phenylurea herbicides; and two P450s from Lamiaceae, CYP76AH and CYP76AK, that are involved in the oxidation of abietane diterpenes. CYP76AH produces ferruginol and 11-hydroxyferruginol, while CYP76AK catalyzes oxidations at the C20 position. Also included in this group is Berberis stolonifera Cyp80, also called berbamunine synthase or (S)-N-methylcoclaurine oxidase [C-O phenol-coupling], that catalyzes the phenol oxidation of N-methylcoclaurine to form the bisbenzylisoquinoline alkaloid berbamunine. The CYP76-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 78.73  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 286 IDNRLEKYSQQPSA--DFLCDIY------HQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQ 357
Cdd:cd11073  194 IDERLAEREAGGDKkkDDDLLLLldleldSESELTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELD 273

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 193083117 358 SVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPF-TTRTLDKATVLGEYALPKG 412
Cdd:cd11073  274 EVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLlLPRKAEEDVEVMGYTIPKG 329
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 276-414 2.20e-15

cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most abundant CYP subfamily in the liver, consists of drug-metabolizing enzymes. In humans, there are at least four isoforms: CYP3A4, 3A5, 3A7, and 3A3. CYP3A enzymes are embedded in the endoplasmic reticulum, where they can catalyze a wide variety of biochemical reactions including hydroxylation, N-demethylation, O-dealkylation, S-oxidation, deamination, or epoxidation of substrates. They oxidize a variety of structurally unrelated compounds including steroids, fatty acids, and xenobiotics. The CYP3A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 77.84  E-value: 2.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 276 DTIFKSVKACIDNRLEKySQQPSADFLCDIYHQNRLSKKELYAAVTELQL---------AAVETTANSLMWILYNLSRNP 346
Cdd:cd20650  181 NFFYKSVKKIKESRLDS-TQKHRVDFLQLMIDSQNSKETESHKALSDLEIlaqsiififAGYETTSSTLSFLLYELATHP 259

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193083117 347 QVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGIV 414
Cdd:cd20650  260 DVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEINGVFIPKGTV 327
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 311-412 5.79e-15

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: 76.64  E-value: 5.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 311 LSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPS 390
Cdd:cd20658  233 LTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPV 312

                         90       100
                 ....*....|....*....|...
gi 193083117 391 VPFTTRTLDKA-TVLGEYALPKG 412
Cdd:cd20658  313 APFNVPHVAMSdTTVGGYFIPKG 335
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 300-412 6.69e-15

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: 76.10  E-value: 6.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 300 DFLCDIYHQ----NRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMP 375
Cdd:cd20655  209 DILLDAYEDenaeYKITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLP 288

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 193083117 376 YLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd20655  289 YLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEK 325
PLN02655 PLN02655
ent-kaurene oxidase
 56-441 8.48e-15

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 76.32  E-value: 8.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  56 AALPGptsWPLLGSLLQIlwkgGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLL-EALYRTESAYPQRleiKPW 134
Cdd:PLN02655   2 PAVPG---LPVIGNLLQL----KEKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAkEAMVTKFSSISTR---KLS 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 135 KA---------------YRDYRK--EGYGLLILEGEDWQRvrsafQKKLMKpgevmklDNKINEVLADFMGRIDELCDER 197
Cdd:PLN02655  72 KAltvltrdksmvatsdYGDFHKmvKRYVMNNLLGANAQK-----RFRDTR-------DMLIENMLSGLHALVKDDPHSP 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 198 GHVEDLY-SELnkwsFesiclvlyekRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVTPVELHKSLNTKVWQDH--TLA 274
Cdd:PLN02655 140 VNFRDVFeNEL----F----------GLSLIQALGEDVESVYVEELGTEISKEEIFDVLVHDMMMCAIEVDWRDFfpYLS 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 275 W------DTIFKSV--------KACIDNRLEKYSQQPSADFLCDIY--HQNRLSKKELYAAVTELQLAAVETTANSLMWI 338
Cdd:PLN02655 206 WipnksfETRVQTTefrrtavmKALIKQQKKRIARGEERDCYLDFLlsEATHLTDEQLMMLVWEPIIEAADTTLVTTEWA 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 339 LYNLSRNPQVQQKLLKEIQSVLPENQVPRaEDLRNMPYLKACLKESMRLTPSVPFT-TRTLDKATVLGEYALPKGIVRKY 417
Cdd:PLN02655 286 MYELAKNPDKQERLYREIREVCGDERVTE-EDLPNLPYLNAVFHETLRKYSPVPLLpPRFVHEDTTLGGYDIPAGTQIAI 364

                        410       420
                 ....*....|....*....|....
gi 193083117 418 DIQATDNEPVEMLHSGTLVPSREL 441
Cdd:PLN02655 365 NIYGCNMDKKRWENPEEWDPERFL 388
PLN03018 PLN03018
homomethionine N-hydroxylase
 257-412 1.06e-14

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 76.20  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 257 VELHKSLNTKVWQDHTLAWDTifKSVKACIDNRLEKYSQqpsadfLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLM 336
Cdd:PLN03018 264 VNLVRSYNNPIIDERVELWRE--KGGKAAVEDWLDTFIT------LKDQNGKYLVTPDEIKAQCVEFCIAAIDNPANNME 335

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193083117 337 WILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKA-TVLGEYALPKG 412
Cdd:PLN03018 336 WTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQdTTLGGYFIPKG 412
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 93-412 1.20e-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: 75.60  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  93 YGKIFRMKLGSFESVHL-GSPCLLEALYRTESAYPQRLEIKPWKAYrdyrKEGYGLLILEGEDWQRVRSaFQKKLMKPGE 171
Cdd:cd20671    1 YGPVFTIHLGMQKTVVLtGYEAVKEALVGTGDEFADRPPIPIFQAI----QHGNGVFFSSGERWRTTRR-FTVRSMKSLG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 172 VMK--LDNKINEVLADFMGRIDELcdeRGHVEDLySELNkWSFESICL-VLYEKRFgllqkNAGDEA-VNFIMAIKTMMS 247
Cdd:cd20671   76 MGKrtIEDKILEELQFLNGQIDSF---NGKPFPL-RLLG-WAPTNITFaMLFGRRF-----DYKDPTfVSLLDLIDEVMV 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 248 TFGRMMVTPVELHKSLNTkVWQDHTLAWDTIfKSVKACIDNRLEKYSQQPSADFLCD-----IYHQNRLSKKE------- 315
Cdd:cd20671  146 LLGSPGLQLFNLYPVLGA-FLKLHKPILDKV-EEVCMILRTLIEARRPTIDGNPLHSyiealIQKQEEDDPKEtlfhdan 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 316 LYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTT 395
Cdd:cd20671  224 VLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVP 303

                        330
                 ....*....|....*..
gi 193083117 396 RTLDKATVLGEYALPKG 412
Cdd:cd20671  304 RCTAADTQFKGYLIPKG 320
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 286-412 1.45e-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: 75.29  E-value: 1.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 286 ID---NRLEKYSQQPSADFlcdiyhqnrlSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPE 362
Cdd:cd11026  204 IDcflLKMEKEKDNPNSEF----------HEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGR 273

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 193083117 363 NQVPRAEDLRNMPYLKACLKESMRLTPSVPFT-TRTLDKATVLGEYALPKG 412
Cdd:cd11026  274 NRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGvPHAVTRDTKFRGYTIPKG 324
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 310-414 1.60e-14

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: 75.04  E-value: 1.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 310 RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTP 389
Cdd:cd20675  230 GLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSS 309

                         90       100
                 ....*....|....*....|....*..
gi 193083117 390 SVPFTT--RTLDKATVLGeYALPKGIV 414
Cdd:cd20675  310 FVPVTIphATTADTSILG-YHIPKDTV 335
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 325-412 2.77e-14

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: 74.32  E-value: 2.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 325 LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVL 404
Cdd:cd11046  250 IAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKL 329

                         90
                 ....*....|
gi 193083117 405 --GEYALPKG 412
Cdd:cd11046  330 pgGGVKVPAG 339
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 59-442 2.98e-14

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 74.46  E-value: 2.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  59 PGPTSWPLLGSLLQIlwkGGlkKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTE----SAYP-------- 126
Cdd:PLN02687  37 PGPRGWPVLGNLPQL---GP--KPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHdanfSNRPpnsgaehm 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 127 ----QRLEIKP----WKAYR--------------DYRKegygllILEGEDWQRVRSAFQKKLMKPgevMKLDNKINEVLA 184
Cdd:PLN02687 112 aynyQDLVFAPygprWRALRkicavhlfsakaldDFRH------VREEEVALLVRELARQHGTAP---VNLGQLVNVCTT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 185 DFMGRI-----------DELCDErghvedlyselnkwsFESICLVLYEKRfGLLqkNAGDeavnFIMAI----------- 242
Cdd:PLN02687 183 NALGRAmvgrrvfagdgDEKARE---------------FKEMVVELMQLA-GVF--NVGD----FVPALrwldlqgvvgk 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 243 -KTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKacidnrlekySQQPSADflcdiyhQNRLSKKELYAAVT 321
Cdd:PLN02687 241 mKRLHRRFDAMMNGIIEEHKAAGQTGSEEHKDLLSTLLALKR----------EQQADGE-------GGRITDTEIKALLL 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 322 ELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFT-TRTLDK 400
Cdd:PLN02687 304 NLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSlPRMAAE 383

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 193083117 401 ATVLGEYALPKGIVRKYDIQATDNEPVEMLHSGTLVPSRELP 442
Cdd:PLN02687 384 ECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLP 425
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 211-426 3.19e-14

cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the meta-hydroxylation step in the phenylpropanoid biosynthetic pathway. CYP98A3, also called p-coumaroylshikimate/quinate 3'-hydroxylase, catalyzes 3'-hydroxylation of p-coumaric esters of shikimic/quinic acids to form lignin monomers. CYP98A8, also called p-coumarate 3-hydroxylase, acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. CYP98 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 74.06  E-value: 3.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 211 SFESICLVLYEKRFGLLQKNAGDEAVNF--IMAIKTMMSTFGRMMVTPVELHK--SLNTKVWQDHTLAWDTIFKsvKACI 286
Cdd:cd20656  121 AFNNITRLAFGKRFVNAEGVMDEQGVEFkaIVSNGLKLGASLTMAEHIPWLRWmfPLSEKAFAKHGARRDRLTK--AIME 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 287 DNRLEKYSQQPSADF---LCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPEN 363
Cdd:cd20656  199 EHTLARQKSGGGQQHfvaLLTLKEQYDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSD 278

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193083117 364 QVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATV-LGEYALPKGIVRKYDIQATDNEP 426
Cdd:cd20656  279 RVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHKASENVkIGGYDIPKGANVHVNVWAIARDP 342
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 275-412 3.21e-14

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: 74.04  E-value: 3.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 275 WDTIFKSVkacIDNRLEKYSQQPS---ADFLCDIYHQN------RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRN 345
Cdd:cd11072  182 LDAFLEKI---IDEHLDKKRSKDEdddDDDLLDLRLQKegdlefPLTRDNIKAIILDMFLAGTDTSATTLEWAMTELIRN 258

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193083117 346 PQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTT-RTLDKATVLGEYALPKG 412
Cdd:cd11072  259 PRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLpRECREDCKINGYDIPAK 326
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 86-412 6.97e-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: 73.14  E-value: 6.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  86 LVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRleikpwKAYRDYRK--EGYGLLILEGEDWQRvrsafQ 163
Cdd:cd11052    4 YYHWIKQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEGYFGK------SPLQPGLKklLGRGLVMSNGEKWAK-----H 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 164 KKLMKPGEVM-KLDNKINEVLADFMGRIDELCDERGHVE---DLYSELNKWSFESICLVL----YEKrfgllqknaGDEA 235
Cdd:cd11052   73 RRIANPAFHGeKLKGMVPAMVESVSDMLERWKKQMGEEGeevDVFEEFKALTADIISRTAfgssYEE---------GKEV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 236 VNFIMAIKTMMSTFGRMMVTPVELHKSL--NTKVWQ-DHTlawdtIFKSVKACIDNRLEKYSQQPSADFLCDIY------ 306
Cdd:cd11052  144 FKLLRELQKICAQANRDVGIPGSRFLPTkgNKKIKKlDKE-----IEDSLLEIIKKREDSLKMGRGDDYGDDLLglllea 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 307 HQNRLSKKELYAA--VTELQL---AAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPrAEDLRNMPYLKACL 381
Cdd:cd11052  219 NQSDDQNKNMTVQeiVDECKTfffAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPP-SDSLSKLKTVSMVI 297

                        330       340       350
                 ....*....|....*....|....*....|.
gi 193083117 382 KESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd11052  298 NESLRLYPPAVFLTRKAKEDIKLGGLVIPKG 328
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 155-412 9.51e-14

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: 72.78  E-value: 9.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 155 WQRVRSAFQKKLMKPGEVMKLDN---KINEVLAdfmgRIDELCDERGHVEDLyselnkwsfesiclvlyekrfGLLQKna 231
Cdd:cd20616   70 WKKVRPFFAKALTGPGLVRMVTVcveSTNTHLD----NLEEVTNESGYVDVL---------------------TLMRR-- 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 232 gdeavnfimaikTMMSTFGRMMVTPVELHKSLNTKV------WQDHTLAWDTIFK----------SVKACID-------- 287
Cdd:cd20616  123 ------------IMLDTSNRLFLGVPLNEKAIVLKIqgyfdaWQALLIKPDIFFKiswlykkyekAVKDLKDaieilieq 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 288 -----NRLEKYSQQpsADFLCD-IYHQNR--LSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSV 359
Cdd:cd20616  191 krrriSTAEKLEDH--MDFATElIFAQKRgeLTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTV 268

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193083117 360 LPENQvPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd20616  269 LGERD-IQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 93-412 1.28e-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: 72.15  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  93 YGKIFRMKLGSFESVHL-GSPCLLEALYRTESAYPQRlEIKPwkAYRDYRKeGYGLLILEGEDWQRVRSafqkklmkpge 171
Cdd:cd20664    1 YGSIFTVQMGTKKVVVLaGYKTVKEALVNHAEAFGGR-PIIP--IFEDFNK-GYGILFSNGENWKEMRR----------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 172 vMKLDNkinevLADF-MGRI---DELCDERGHVEDLYSELNKWSFES-----------ICLVLYEKRFgllqKNAGDEAV 236
Cdd:cd20664   66 -FTLTT-----LRDFgMGKKtseDKILEEIPYLIEVFEKHKGKPFETtlsmnvavsniIASIVLGHRF----EYTDPTLL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 237 NFIMAIKTMMSTFGRMMVTPVELHKSLNTKVWQDHTLAWDTifKSVKACIDNRLEKYSQQPSADF---LCDIYHQNRLSK 313
Cdd:cd20664  136 RMVDRINENMKLTGSPSVQLYNMFPWLGPFPGDINKLLRNT--KELNDFLMETFMKHLDVLEPNDqrgFIDAFLVKQQEE 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 314 KE----------LYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQvPRAEDLRNMPYLKACLKE 383
Cdd:cd20664  214 EEssdsffhddnLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQ-PQVEHRKNMPYTDAVIHE 292

                        330       340       350
                 ....*....|....*....|....*....|
gi 193083117 384 SMRLTPSVPFTT-RTLDKATVLGEYALPKG 412
Cdd:cd20664  293 IQRFANIVPMNLpHATTRDVTFRGYFIPKG 322
PLN02966 PLN02966
cytochrome P450 83A1
 59-412 1.47e-13

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 72.47  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  59 PGPTSWPLLGSLLQIlwkGGLKKQHdTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTesaypQRLEIKPWKAYR 138
Cdd:PLN02966  32 PGPSPLPVIGNLLQL---QKLNPQR-FFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKT-----QDVNFADRPPHR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 139 DYRKEGYG----LLILEGEDWQRVRSAFQKKLMKPGEVMKLDNKINEVLADFMGRIDELCDeRGHVEDLYSELNKWSFES 214
Cdd:PLN02966 103 GHEFISYGrrdmALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAAD-KSEVVDISELMLTFTNSV 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 215 IClvlyEKRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVTPVELHKSLN------TKVWQDHTLAWDT-IFKSVKACID 287
Cdd:PLN02966 182 VC----RQAFGKKYNEDGEEMKRFIKILYGTQSVLGKIFFSDFFPYCGFLddlsglTAYMKECFERQDTyIQEVVNETLD 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 288 NRLEKYSQQPSADFLCDIYHQNRLSKK----ELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPEN 363
Cdd:PLN02966 258 PKRVKPETESMIDLLMEIYKEQPFASEftvdNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEK 337

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193083117 364 QVP--RAEDLRNMPYLKACLKESMRLTPSVP-FTTRTLDKATVLGEYALPKG 412
Cdd:PLN02966 338 GSTfvTEDDVKNLPYFRALVKETLRIEPVIPlLIPRACIQDTKIAGYDIPAG 389
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 144-412 1.58e-13

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: 71.93  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 144 GYGLLILEGEDWQRVRSAFQKKLMKPGEVMKLDNKINEVLADFMGRIDELCDERGHVEDLYSELNKWSFESICLVLYEKr 223
Cdd:cd20615   49 GQCVGLLSGTDWKRVRKVFDPAFSHSAAVYYIPQFSREARKWVQNLPTNSGDGRRFVIDPAQALKFLPFRVIAEILYGE- 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 224 fgllqknAGDEAVNFIMAIktmmstfgrmmvtpVELHKSLNTKVWQDHTLAWdTIFKSVKACIDNRLEKYSQQpSADFLC 303
Cdd:cd20615  128 -------LSPEEKEELWDL--------------APLREELFKYVIKGGLYRF-KISRYLPTAANRRLREFQTR-WRAFNL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 304 DIYHQNRLSKKE-----LYAAVT--------------ELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLpENQ 364
Cdd:cd20615  185 KIYNRARQRGQStpivkLYEAVEkgditfeellqtldEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAR-EQS 263

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 193083117 365 VPRAED--LRNMPYLKACLKESMRLTPSVPFTT-RTLDKATVLGEYALPKG 412
Cdd:cd20615  264 GYPMEDyiLSTDTLLAYCVLESLRLRPLLAFSVpESSPTDKIIGGYRIPAN 314
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 316-414 2.62e-13

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: 71.35  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 316 LYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTT 395
Cdd:cd20666  229 LFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSI 308

                         90       100
                 ....*....|....*....|
gi 193083117 396 -RTLDKATVLGEYALPKGIV 414
Cdd:cd20666  309 pHMASENTVLQGYTIPKGTV 328
PLN02936 PLN02936
epsilon-ring hydroxylase
 323-412 4.13e-13

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 70.98  E-value: 4.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 323 LQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLpENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKAT 402
Cdd:PLN02936 286 MLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVL-QGRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVED 364

                         90
                 ....*....|.
gi 193083117 403 VL-GEYALPKG 412
Cdd:PLN02936 365 VLpGGYKVNAG 375
PLN02183 PLN02183
ferulate 5-hydroxylase
 59-411 5.84e-13

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 70.65  E-value: 5.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  59 PGPTSWPLLGSLLQILwkgglKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTE----SAYPQRLEIKpw 134
Cdd:PLN02183  39 PGPKGLPIIGNMLMMD-----QLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQdsvfSNRPANIAIS-- 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 135 kaYRDYRKEGYGLLILeGEDWQRVRSAFQKKLMKPGEVMKLDNKINEVlaDFMGR-IDELCDERGHVEDLYSELNKwsfe 213
Cdd:PLN02183 112 --YLTYDRADMAFAHY-GPFWRQMRKLCVMKLFSRKRAESWASVRDEV--DSMVRsVSSNIGKPVNIGELIFTLTR---- 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 214 sicLVLYEKRFGLLQKNAGDEAVNFIMAIKTMMSTFGRMMVTP--------------VELHKSLN---TKVWQDH----- 271
Cdd:PLN02183 183 ---NITYRAAFGSSSNEGQDEFIKILQEFSKLFGAFNVADFIPwlgwidpqglnkrlVKARKSLDgfiDDIIDDHiqkrk 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 272 -TLAWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQ 350
Cdd:PLN02183 260 nQNADNDSEEAETDMVDDLLAFYSEEAKVNESDDLQNSIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLK 339

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193083117 351 KLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPK 411
Cdd:PLN02183 340 RVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPK 400
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 311-414 6.39e-13

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: 70.16  E-value: 6.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 311 LSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVlpeNQVPR-AEDLRNMPYLKACLKESMRLTP 389
Cdd:cd20614  204 LSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA---GDVPRtPAELRRFPLAEALFRETLRLHP 280

                         90       100
                 ....*....|....*....|....*
gi 193083117 390 SVPFTTRTLDKATVLGEYALPKGIV 414
Cdd:cd20614  281 PVPFVFRRVLEEIELGGRRIPAGTH 305
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 307-412 8.10e-13

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


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 69.66  E-value: 8.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 307 HQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMR 386
Cdd:cd20673  224 DSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLR 303

                         90       100       110
                 ....*....|....*....|....*....|.
gi 193083117 387 LTPSVPfttrTL--DKA---TVLGEYALPKG 412
Cdd:cd20673  304 IRPVAP----LLipHVAlqdSSIGEFTIPKG 330
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 312-412 9.44e-13

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: 69.84  E-value: 9.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 312 SKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSV 391
Cdd:cd20661  235 SMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIV 314

                         90       100
                 ....*....|....*....|..
gi 193083117 392 PFTT-RTLDKATVLGEYALPKG 412
Cdd:cd20661  315 PLGIfHATSKDAVVRGYSIPKG 336
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 233-412 1.17e-12

cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of predominantly fungal cytochrome P450s (CYPs) with similarity to Fusarium fujikuroi Cytochrome P450 503A1 (CYP503A1, also called ent-kaurene oxidase or cytochrome P450-4), Aspergillus nidulans austinol synthesis protein I (ausI), Alternaria alternata tentoxin synthesis protein 1 (TES1), and Acanthamoeba polyphaga mimivirus cytochrome P450 51 (CYP51, also called P450-LIA1 or sterol 14-alpha demethylase). Ent-kaurene oxidase catalyzes three successive oxidations of the 4-methyl group of ent-kaurene to form kaurenoic acid, an intermediate in gibberellin biosynthesis. AusI and TES1 are cytochrome P450 monooxygenases that mediate the biosynthesis of the meroterpenoids, austinol and dehydroaustinol, and the phytotoxin tentoxin, respectively. P450-LIA1 catalyzes the 14-alpha demethylation of obtusifoliol and functions in steroid biosynthesis. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 69.24  E-value: 1.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 233 DEAVNFIMAIkTMMSTFGRMMvtPVELHK---SLNTKVWQDHTLAWDT--IFKSVKACIDNRLEKYSQQPSADFLCDIYH 307
Cdd:cd11041  139 DLTINYTIDV-FAAAAALRLF--PPFLRPlvaPFLPEPRRLRRLLRRArpLIIPEIERRRKLKKGPKEDKPNDLLQWLIE 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 308 QNRLSKKELYAAVTELQL----AAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKE 383
Cdd:cd11041  216 AAKGEGERTPYDLADRQLalsfAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKE 295

                        170       180       190
                 ....*....|....*....|....*....|.
gi 193083117 384 SMRLTPSVPFTT-RTLDKATVLGE-YALPKG 412
Cdd:cd11041  296 SQRLNPLSLVSLrRKVLKDVTLSDgLTLPKG 326
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 89-412 1.29e-12

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


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 69.02  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  89 YH---KKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPQRLEIKPWKAyrdyRKEGYGLLILEGEDWqrvrsAFQKK 165
Cdd:cd20639    4 YHhwrKIYGKTFLYWFGPTPRLTVADPELIREILLTRADHFDRYEAHPLVR----QLEGDGLVSLRGEKW-----AHHRR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 166 LMKPGEVM-KLDNKINEVLADFMGRIDELCDERGHVEDLYSELNKWsFESICL-VLYEKRFGllqKNAGDEAVNFIMAik 243
Cdd:cd20639   75 VITPAFHMeNLKRLVPHVVKSVADMLDKWEAMAEAGGEGEVDVAEW-FQNLTEdVISRTAFG---SSYEDGKAVFRLQ-- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 244 tmmstfGRMMVTPVELHKSL------------NTKVWQDHTlawdTIFKSVKACIDNRLEKYSQQPSADFLCDIYH--QN 309
Cdd:cd20639  149 ------AQQMLLAAEAFRKVyipgyrflptkkNRKSWRLDK----EIRKSLLKLIERRQTAADDEKDDEDSKDLLGlmIS 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 310 RLSKKELYAAVTE--------LQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACL 381
Cdd:cd20639  219 AKNARNGEKMTVEeiieecktFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMIL 298

                        330       340       350
                 ....*....|....*....|....*....|.
gi 193083117 382 KESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd20639  299 NETLRLYPPAVATIRRAKKDVKLGGLDIPAG 329
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 91-431 1.39e-12

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: 68.98  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  91 KKYGKIFRMKLGSFESVHLGSPCLLEALYRTESaypqrLEIKPWKAYRDYRKE--GYGLLILEGEDWqrvrsAFQKKLMK 168
Cdd:cd20640    9 KQYGPIFTYSTGNKQFLYVSRPEMVKEINLCVS-----LDLGKPSYLKKTLKPlfGGGILTSNGPHW-----AHQRKIIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 169 P--------GEVMKLDNKINEVLADFMGRIDelcDERGHVEDLY--SELNKWSFESICLVLYEKRFgllqkNAGDEAVNF 238
Cdd:cd20640   79 PeffldkvkGMVDLMVDSAQPLLSSWEERID---RAGGMAADIVvdEDLRAFSADVISRACFGSSY-----SKGKEIFSK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 239 IMAIKTMMSTFGRMMVTPVELH--KSLNTKVW----QDHTLAWDTIFKSVKACIDNR------LEKYSQQPSA-----DF 301
Cdd:cd20640  151 LRELQKAVSKQSVLFSIPGLRHlpTKSNRKIWelegEIRSLILEIVKEREEECDHEKdllqaiLEGARSSCDKkaeaeDF 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 302 LCDiyhqnrlSKKELYaavtelqLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLpENQVPRAEDLRNMPYLKACL 381
Cdd:cd20640  231 IVD-------NCKNIY-------FAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVC-KGGPPDADSLSRMKTVTMVI 295

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 193083117 382 KESMRLTPSVPFTTRTLDKATVLGEYALPKGIvrkyDIQAtdnePVEMLH 431
Cdd:cd20640  296 QETLRLYPPAAFVSREALRDMKLGGLVVPKGV----NIWV----PVSTLH 337
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 91-412 2.25e-12

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: 68.36  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  91 KKYGKIFRMKLgsfesvhLGSPCLL----EALYR--------TESAYPQ---RLEIKpwkayrdyrkegYGLLILEGEDW 155
Cdd:cd11043    3 KRYGPVFKTSL-------FGRPTVVsadpEANRFilqnegklFVSWYPKsvrKLLGK------------SSLLTVSGEEH 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 156 QRVRSAFQKkLMKPgEVMKldnkinevlADFMGRIDELCDE------RGHVEDLYSELNKWSFESICLVLyekrFGLLQK 229
Cdd:cd11043   64 KRLRGLLLS-FLGP-EALK---------DRLLGDIDELVRQhldswwRGKSVVVLELAKKMTFELICKLL----LGIDPE 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 230 NAGDEavnfimaIKTMMSTFGR-MMVTPVEL-----HKSLNtkvwqdhtlAWDTIFKSVKACIDNRL-EKYSQQPSADFL 302
Cdd:cd11043  129 EVVEE-------LRKEFQAFLEgLLSFPLNLpgttfHRALK---------ARKRIRKELKKIIEERRaELEKASPKGDLL 192

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 303 C-----DIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKE---IQSVLPENQVPRAEDLRNM 374
Cdd:cd11043  193 DvlleeKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEheeIAKRKEEGEGLTWEDYKSM 272

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 193083117 375 PYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd11043  273 KYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKG 310
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 59-412 2.91e-12

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 68.22  E-value: 2.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  59 PGPTSWPLLGSLLQIlwkgGLKKQHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLlealyRTESAYPQRLEI--KPWKA 136
Cdd:PLN02394  33 PGPAAVPIFGNWLQV----GDDLNHRNLAEMAKKYGDVFLLRMGQRNLVVVSSPEL-----AKEVLHTQGVEFgsRTRNV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 137 YRD-YRKEGYGLLILE-GEDWQRVRSA-----FQKKLMKPGEVM---KLDNKINEVLAD--------------------F 186
Cdd:PLN02394 104 VFDiFTGKGQDMVFTVyGDHWRKMRRImtvpfFTNKVVQQYRYGweeEADLVVEDVRANpeaategvvirrrlqlmmynI 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 187 MGRIdeLCDERGHVED--LYSELNKW---------SFE------------------SICLVLYEKRFGLLQKNAGDEAvn 237
Cdd:PLN02394 184 MYRM--MFDRRFESEDdpLFLKLKALngersrlaqSFEynygdfipilrpflrgylKICQDVKERRLALFKDYFVDER-- 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 238 fimaiKTMMSTfgrmmvTPVELHKslntkvwqdhtlawdtifksVKACIDNRLEkySQQPSadflcDIYHQNrlskkELY 317
Cdd:PLN02394 260 -----KKLMSA------KGMDKEG--------------------LKCAIDHILE--AQKKG-----EINEDN-----VLY 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 318 AaVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTT-- 395
Cdd:PLN02394 297 I-VENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVph 375

                        410
                 ....*....|....*..
gi 193083117 396 RTLDKATvLGEYALPKG 412
Cdd:PLN02394 376 MNLEDAK-LGGYDIPAE 391
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 93-412 5.21e-12

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: 67.26  E-value: 5.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  93 YGKIFRMKLGSFESVHL-GSPCLLEALYRTESAYPQRLEIkpwkAYRDYRKEGYGLLILEGEDWQRVRSaFQKKLMKPGE 171
Cdd:cd20670    1 YGPVFTVYMGPRPVVVLcGHEAVKEALVDQADEFSGRGEL----ATIERNFQGHGVALANGERWRILRR-FSLTILRNFG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 172 VMK--LDNKINEVlADFMgrIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLlqknagdEAVNFIMAIKTMMSTF 249
Cdd:cd20670   76 MGKrsIEERIQEE-AGYL--LEEFRKTKGAPIDPTFFLSRTVSNVISSVVFGSRFDY-------EDKQFLSLLRMINESF 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 250 GRMMVTPVELHkSLNTKVWQ----DHTLAWDTIfKSVKACIDNRLE----KYSQQPSADFLcDIY----HQNR------L 311
Cdd:cd20670  146 IEMSTPWAQLY-DMYSGIMQylpgRHNRIYYLI-EELKDFIASRVKineaSLDPQNPRDFI-DCFlikmHQDKnnphteF 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 312 SKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSV 391
Cdd:cd20670  223 NLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIV 302

                        330       340
                 ....*....|....*....|..
gi 193083117 392 PF-TTRTLDKATVLGEYALPKG 412
Cdd:cd20670  303 PLgVPHNVIRDTQFRGYLLPKG 324
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 59-426 5.75e-12

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 67.57  E-value: 5.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  59 PGPTSWPLLGSLLQIlwkGGLKkqHDTLVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRT---------ESAYPQRL 129
Cdd:PLN00110  34 PGPRGWPLLGALPLL---GNMP--HVALAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTldinfsnrpPNAGATHL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 130 ----------EIKP-WKAYRDYRKegygLLILEG---EDWQRVRSAFQKKLMKP-------GEVMKLDNKINEVLADFMG 188
Cdd:PLN00110 109 aygaqdmvfaDYGPrWKLLRKLSN----LHMLGGkalEDWSQVRTVELGHMLRAmlelsqrGEPVVVPEMLTFSMANMIG 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 189 RIdelCDERGHVEDLYSELNKWSFESICLVLYEKRFgllqkNAGDeavnFIMAIKTM-MSTFGRMMVtpvELHKSLN--- 264
Cdd:PLN00110 185 QV---ILSRRVFETKGSESNEFKDMVVELMTTAGYF-----NIGD----FIPSIAWMdIQGIERGMK---HLHKKFDkll 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 265 TKVWQDHTlawdtifksvkACIDNRLEKysqqpsADFLcDIYHQN-------RLSKKELYAAVTELQLAAVETTANSLMW 337
Cdd:PLN00110 250 TRMIEEHT-----------ASAHERKGN------PDFL-DVVMANqenstgeKLTLTNIKALLLNLFTAGTDTSSSVIEW 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 338 ILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFT-TRTLDKATVLGEYALPKGIVRK 416
Cdd:PLN00110 312 SLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNlPRVSTQACEVNGYYIPKNTRLS 391

                        410
                 ....*....|
gi 193083117 417 YDIQATDNEP 426
Cdd:PLN00110 392 VNIWAIGRDP 401
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 311-412 7.46e-12

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: 67.04  E-value: 7.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 311 LSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPS 390
Cdd:cd20677  232 LSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSF 311

                         90       100
                 ....*....|....*....|....*
gi 193083117 391 VPFTT---RTLDkaTVLGEYALPKG 412
Cdd:cd20677  312 VPFTIphcTTAD--TTLNGYFIPKD 334
PLN02738 PLN02738
carotene beta-ring hydroxylase
 86-412 1.25e-11

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 66.47  E-value: 1.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  86 LVEYHKKYGKIFRMKLGSFESVHLGSPCLLEALYRTES-AYPQRL--EIKPWKAyrdyrkeGYGLLILEGEDWQRVRSAF 162
Cdd:PLN02738 157 LYELFLTYGGIFRLTFGPKSFLIVSDPSIAKHILRDNSkAYSKGIlaEILEFVM-------GKGLIPADGEIWRVRRRAI 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 163 qkklmkpgeVMKLDNKINEVLADFMGRI-DELCD---------ERGHVEDLYSELnkwSFESICLVLYEKRFGLLQKNAG 232
Cdd:PLN02738 230 ---------VPALHQKYVAAMISLFGQAsDRLCQkldaaasdgEDVEMESLFSRL---TLDIIGKAVFNYDFDSLSNDTG 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 233 D-EAVNFIMAIKTMMStfgrmmVTPVELhksLNTKVWQDHTLAWDTIFKSVK---ACIDN------RL---------EKY 293
Cdd:PLN02738 298 IvEAVYTVLREAEDRS------VSPIPV---WEIPIWKDISPRQRKVAEALKlinDTLDDliaickRMveeeelqfhEEY 368

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 294 --SQQPSA-DFLcdIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPEnQVPRAED 370
Cdd:PLN02738 369 mnERDPSIlHFL--LASGDDVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGD-RFPTIED 445

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 193083117 371 LRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:PLN02738 446 MKKLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGYPIKRG 487
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
 93-412 1.70e-11

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: 65.57  E-value: 1.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  93 YGKIFRMKLGSFESVHL-GSPCLLEALYRTESAYPQRLEIkpwkAYRDYRKEGYGLLILEGEDWQRVRSaFQKKLMKpge 171
Cdd:cd20672    1 YGDVFTVHLGPRPVVMLcGTDAIREALVDQAEAFSGRGTI----AVVDPIFQGYGVIFANGERWKTLRR-FSLATMR--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 172 vmkldnkinevlaDF-MGR--IDELCDERGHVedLYSELNKWS---------FES-----ICLVLYEKRFGLlQKNAGDE 234
Cdd:cd20672   73 -------------DFgMGKrsVEERIQEEAQC--LVEELRKSKgalldptflFQSitaniICSIVFGERFDY-KDPQFLR 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 235 AVNFIMAIKTMMSTFGRMMVtpvELHKSLNTKVWQDHTLAWDTIfKSVKACIDNRLEKYSQ--QPSA--DFLcDIY---- 306
Cdd:cd20672  137 LLDLFYQTFSLISSFSSQVF---ELFSGFLKYFPGAHRQIYKNL-QEILDYIGHSVEKHRAtlDPSAprDFI-DTYllrm 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 307 ------HQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKAC 380
Cdd:cd20672  212 ekeksnHHTEFHHQNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAV 291

                        330       340       350
                 ....*....|....*....|....*....|...
gi 193083117 381 LKESMRLTPSVPF-TTRTLDKATVLGEYALPKG 412
Cdd:cd20672  292 IHEIQRFSDLIPIgVPHRVTKDTLFRGYLLPKN 324
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 91-413 3.99e-11

cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Characterized members, among others, include: Catharanthus roseus cytochrome P450 72A1 (CYP72A1), also called secologanin synthase (EC 1.3.3.9), that catalyzes the conversion of loganin into secologanin, the precursor of monoterpenoid indole alkaloids and ipecac alkaloids; Medicago truncatula CYP72A67 that catalyzes a key oxidative step in hemolytic sapogenin biosynthesis; and Arabidopsis thaliana CYP72C1, an atypical CYP that acts on brassinolide precursors and functions as a brassinosteroid-inactivating enzyme. This family also includes Panax ginseng CYP716A47 that catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis. CYP72 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 64.61  E-value: 3.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  91 KKYGKIFRMKLGSFESVHLGSPCLLEALYRTESAYPqrleiKPwKAYRDYRKEGYGLLILEGEDWQRVRsafqkKLMKPG 170
Cdd:cd20642    9 KTYGKNSFTWFGPIPRVIIMDPELIKEVLNKVYDFQ-----KP-KTNPLTKLLATGLASYEGDKWAKHR-----KIINPA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 171 -EVMKLDNKI---NEVLADFMGRIDELCDERGHvedlySELNKW-SFESI-CLVL--------YE--KRFGLLQKNAGD- 233
Cdd:cd20642   78 fHLEKLKNMLpafYLSCSEMISKWEKLVSSKGS-----CELDVWpELQNLtSDVIsrtafgssYEegKKIFELQKEQGEl 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 234 --EAV--NFIMAIKTMMSTFGRMMVtpvELHKSLNTkvwqdhtlawdtifkSVKACIDNRLE--KYSQQPSADFL----- 302
Cdd:cd20642  153 iiQALrkVYIPGWRFLPTKRNRRMK---EIEKEIRS---------------SLRGIINKREKamKAGEATNDDLLgille 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 303 ---CDIYHQNR----LSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLpENQVPRAEDLRNMP 375
Cdd:cd20642  215 snhKEIKEQGNknggMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVF-GNNKPDFEGLNHLK 293

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 193083117 376 YLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGI 413
Cdd:cd20642  294 VVTMILYEVLRLYPPVIQLTRAIHKDTKLGDLTLPAGV 331
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 310-414 5.36e-11

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: 63.97  E-value: 5.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 310 RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTP 389
Cdd:cd20674  221 QLLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRP 300

                         90       100
                 ....*....|....*....|....*..
gi 193083117 390 SVPFTT--RTLDKATVLGeYALPKGIV 414
Cdd:cd20674  301 VVPLALphRTTRDSSIAG-YDIPKGTV 326
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 318-412 6.84e-11

cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically reside in dicots and are usually induced by distinct environmental stresses. Characterized members include: Glycine max CYP82A3 that is induced by infection, salinity and drought stresses, and is involved in the jasmonic acid and ethylene signaling pathway, enhancing plant resistance; Arabidopsis thaliana CYP82G1 that catalyzes the breakdown of the C(20)-precursor (E,E)-geranyllinalool to the insect-induced C(16)-homoterpene (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT); and Papaver somniferum CYP82N4, also called methyltetrahydroprotoberberine 14-monooxygenase, and CYP82Y1, also called N-methylcanadine 1-hydroxylase. CYP82N4 catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively, in the biosynthesis of isoquinoline alkaloid sanguinarine. CYP82Y1 catalyzes the 1-hydroxylation of N-methylcanadine to 1-hydroxy-N-methylcanadine, the first committed step in the formation of noscapine. CYP82 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 63.79  E-value: 6.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 318 AAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQS-VLPENQVpRAEDLRNMPYLKACLKESMRLTPSVPFTT- 395
Cdd:cd20654  244 ATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDThVGKDRWV-EESDIKNLVYLQAIVKETLRLYPPGPLLGp 322

                         90
                 ....*....|....*...
gi 193083117 396 -RTLDKATVlGEYALPKG 412
Cdd:cd20654  323 rEATEDCTV-GGYHVPKG 339
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 86-412 9.09e-11

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: 63.54  E-value: 9.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  86 LVEYHKKY---GKIFRMKLGsFESVHL-GSPCLLEALYR---TESAYP--QRLEIKPWKAYRDYRKegYGLLILEGEDWQ 156
Cdd:cd11040    1 LLRNGKKYfsgGPIFTIRLG-GQKIYViTDPELISAVFRnpkTLSFDPivIVVVGRVFGSPESAKK--KEGEPGGKGLIR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 157 RVRSAFqKKLMKPGEvmkLDNKINEVLADFM-GRIDELCDERG---HVEDLYSelnkWSFESICLVLYEKRFG--LLQKN 230
Cdd:cd11040   78 LLHDLH-KKALSGGE---GLDRLNEAMLENLsKLLDELSLSGGtstVEVDLYE----WLRDVLTRATTEALFGpkLPELD 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 231 AgdeavNFIMAIKTMMSTFGRMMVTPVELhksLNTKVWQdhtlAWDTIFKSVKACIDNRLEKYSQQpsADFLC---DIYH 307
Cdd:cd11040  150 P-----DLVEDFWTFDRGLPKLLLGLPRL---LARKAYA----ARDRLLKALEKYYQAAREERDDG--SELIRaraKVLR 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 308 QNRLSKKELyaAVTELQL--AAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVL-PENQVPRAED----LRNMPYLKAC 380
Cdd:cd11040  216 EAGLSEEDI--ARAELALlwAINANTIPAAFWLLAHILSDPELLERIREEIEPAVtPDSGTNAILDltdlLTSCPLLDST 293

                        330       340       350
                 ....*....|....*....|....*....|...
gi 193083117 381 LKESMRLTpSVPFTTRTLDKATVL-GEYALPKG 412
Cdd:cd11040  294 YLETLRLH-SSSTSVRLVTEDTVLgGGYLLRKG 325
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 310-412 9.70e-11

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: 63.39  E-value: 9.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 310 RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVL-PENQVPRAEDLRNMPYLKACLKESMRLT 388
Cdd:cd11042  207 PLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLgDGDDPLTYDVLKEMPLLHACIKETLRLH 286

                         90       100
                 ....*....|....*....|....*.
gi 193083117 389 PSVPFTTRTLDKA-TVL-GEYALPKG 412
Cdd:cd11042  287 PPIHSLMRKARKPfEVEgGGYVIPKG 312
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 60-416 1.30e-10

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 63.26  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  60 GPTSWPLLGSLLQILwkGGLKKQHDTLVEYHKKyGKIFRMKLGSFESVHLGSPCLLEALYRTESA-YPQRleikpwKAYR 138
Cdd:PLN03195  34 GPKSWPIIGAALEQL--KNYDRMHDWLVEYLSK-DRTVVVKMPFTTYTYIADPVNVEHVLKTNFAnYPKG------EVYH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 139 DYRKE--GYGLLILEGEDW--QRVRSAFQ---KKLMKPGEVMKLDNKINevLADFMGRIDElcdeRGHVEDLYSELNKWS 211
Cdd:PLN03195 105 SYMEVllGDGIFNVDGELWrkQRKTASFEfasKNLRDFSTVVFREYSLK--LSSILSQASF----ANQVVDMQDLFMRMT 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 212 FESICLVLYEKRFGLLQKNAGDE--AVNFIMAIKTMMSTFgrmmVTPV-ELHKSLN----------TKVWQDHTLawdTI 278
Cdd:PLN03195 179 LDSICKVGFGVEIGTLSPSLPENpfAQAFDTANIIVTLRF----IDPLwKLKKFLNigseallsksIKVVDDFTY---SV 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 279 FKSVKACIDNRlEKYSQQPSADFLCDIYH-----QNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKL- 352
Cdd:PLN03195 252 IRRRKAEMDEA-RKSGKKVKHDILSRFIElgedpDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLy 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 353 --LKEIQSVLPENQVPRA-----------------EDLRNMPYLKACLKESMRLTPSVPfttrtLDKATVLGEYALPKGI 413
Cdd:PLN03195 331 seLKALEKERAKEEDPEDsqsfnqrvtqfaglltyDSLGKLQYLHAVITETLRLYPAVP-----QDPKGILEDDVLPDGT 405


                 ...
gi 193083117 414 VRK 416
Cdd:PLN03195 406 KVK 408
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 309-412 1.48e-10

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: 62.72  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 309 NRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENqvPRAEDLRNMPYLKACLKESMRLT 388
Cdd:cd11045  205 DRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLALGKGT--LDYEDLGQLEVTDWVFKEALRLV 282

                         90       100
                 ....*....|....*....|....
gi 193083117 389 PSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd11045  283 PPVPTLPRRAVKDTEVLGYRIPAG 306
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 320-392 1.77e-10

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: 62.49  E-value: 1.77e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193083117 320 VTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVL-PENQVPRAeDLRNMPYLKACLKESMRLTPSVP 392
Cdd:cd11074  238 VENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLgPGVQITEP-DLHKLPYLQAVVKETLRLRMAIP 310
PLN02971 PLN02971
tryptophan N-hydroxylase
 59-412 2.40e-10

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 62.36  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  59 PGPTSWPLLGSLLQIL-------WKGGLKKQHDTlveyhkkygKIFRMKLGSFESVHLGSPCLLEALYRTESAYpqrLEI 131
Cdd:PLN02971  60 PGPTGFPIVGMIPAMLknrpvfrWLHSLMKELNT---------EIACVRLGNTHVIPVTCPKIAREIFKQQDAL---FAS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 132 KPWKAYRDYRKEGYGLLILE--GEDWQRVRSAFQKKLMKPGEVMKLDNKINEVLADFMGRIDELCDERGHVeDLYSELNK 209
Cdd:PLN02971 128 RPLTYAQKILSNGYKTCVITpfGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNSEPV-DLRFVTRH 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 210 WSFESICLVLYEKR-FGLLQKNAGDEAVNFIMAIKTMMSTFGRM----------MVTPVELHKslNTKVWQDHTLAWDTI 278
Cdd:PLN02971 207 YCGNAIKRLMFGTRtFSEKTEPDGGPTLEDIEHMDAMFEGLGFTfafcisdylpMLTGLDLNG--HEKIMRESSAIMDKY 284

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 279 FKSVkacIDNRLEKYSQQPSA---DFLcDIY-------HQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQV 348
Cdd:PLN02971 285 HDPI---IDERIKMWREGKRTqieDFL-DIFisikdeaGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEI 360

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193083117 349 QQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTR--TLDKATVLGeYALPKG 412
Cdd:PLN02971 361 LHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPhvALSDTTVAG-YHIPKG 425
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 94-412 5.67e-10

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


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 60.90  E-value: 5.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  94 GKIFRMKLGSFESVHLGSPCLLEALYRTES---------------AY-PQRLEIKP----WKAYRDYRkegyGLLILEG- 152
Cdd:cd20657    1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDanfsnrppnagathmAYnAQDMVFAPygprWRLLRKLC----NLHLFGGk 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 153 --EDWQRVRSAFQKKLMKP-------GEVMKLDNKINEVLADFMGRIdeLCDERGHVEDLYSELNKwsFESICLVLYEKR 223
Cdd:cd20657   77 alEDWAHVRENEVGHMLKSmaeasrkGEPVVLGEMLNVCMANMLGRV--MLSKRVFAAKAGAKANE--FKEMVVELMTVA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 224 fGLLqkNAGDeavnFIMAIKTM--MSTFGRMMVtpveLHK---SLNTKVWQDHtlawdtifksvKACIDNRLEKysqqps 298
Cdd:cd20657  153 -GVF--NIGD----FIPSLAWMdlQGVEKKMKR----LHKrfdALLTKILEEH-----------KATAQERKGK------ 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 299 ADFLCDIYHQN-------RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDL 371
Cdd:cd20657  205 PDFLDFVLLENddngegeRLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDI 284

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 193083117 372 RNMPYLKACLKESMRLTPSVPFT-TRTLDKATVLGEYALPKG 412
Cdd:cd20657  285 PNLPYLQAICKETFRLHPSTPLNlPRIASEACEVDGYYIPKG 326
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 245-412 5.71e-10

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


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 60.81  E-value: 5.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 245 MMSTFGR---------------MMVTP-VELHKSLNtkvWQDHT--LAWD----------------TIFksVKACIDNRL 290
Cdd:cd11076  120 MGSVFGRrydfeagneeaeelgEMVREgYELLGAFN---WSDHLpwLRWLdlqgirrrcsalvprvNTF--VGKIIEEHR 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 291 EKYSQQPSADF-----LCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQV 365
Cdd:cd11076  195 AKRSNRARDDEddvdvLLSLQGEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRR 274

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 193083117 366 PRAEDLRNMPYLKACLKESMRLTPSVPFTT--RTLDKATVLGEYALPKG 412
Cdd:cd11076  275 VADSDVAKLPYLQAVVKETLRLHPPGPLLSwaRLAIHDVTVGGHVVPAG 323
PLN00168 PLN00168
Cytochrome P450; Provisional
 311-412 5.73e-10

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 61.12  E-value: 5.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 311 LSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRA-EDLRNMPYLKACLKESMRLTP 389
Cdd:PLN00168 302 LTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQEEVSeEDVHKMPYLKAVVLEGLRKHP 381

                         90       100
                 ....*....|....*....|....*..
gi 193083117 390 SVPFttrTLDKATV----LGEYALPKG 412
Cdd:PLN00168 382 PAHF---VLPHKAAedmeVGGYLIPKG 405
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 312-414 7.54e-10

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: 60.62  E-value: 7.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 312 SKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTP-- 389
Cdd:cd20667  222 SEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNvv 301

                         90       100
                 ....*....|....*....|....*
gi 193083117 390 SVPFTTRTLDKATVLGeYALPKGIV 414
Cdd:cd20667  302 SVGAVRQCVTSTTMHG-YYVEKGTI 325
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 310-389 8.70e-10

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: 60.35  E-value: 8.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 310 RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVL-----PENQVPRAED--LRNMPYLKACLK 382
Cdd:cd11051  180 RFELERAIDQIKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFgpdpsAAAELLREGPelLNQLPYTTAVIK 259


                 ....*..
gi 193083117 383 ESMRLTP 389
Cdd:cd11051  260 ETLRLFP 266
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 320-404 3.55e-09

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 58.87  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 320 VTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIqsvlpeNQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLD 399
Cdd:PLN02169 306 IFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI------NTKFDNEDLEKLVYLHAALSESMRLYPPLPFNHKAPA 379


                 ....*
gi 193083117 400 KATVL 404
Cdd:PLN02169 380 KPDVL 384
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 325-448 7.17e-09

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: 57.54  E-value: 7.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 325 LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVL 404
Cdd:cd20649  271 IAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVV 350

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 193083117 405 GEYALPKGIVRKYDIQATDNEPVEMLHSGTLVPSRELPIAFCQR 448
Cdd:cd20649  351 LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRR 394
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 320-413 3.79e-08

cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists of two human members, CYP1A1 and CYP1A2, which overlap in their activities. CYP1A2 is the highly expressed cytochrome enzyme in the human liver, while CYP1A1 is mostly found in extrahepatic tissues. Known common substrates include aromatic compounds such as polycyclic aromatic hydrocarbons, arachidonic acid and eicosapentoic acid, as well as melatonin and 6-hydroxylate melatonin. In addition, CYP1A1 activates procarcinogens into carcinogens via epoxides, and metabolizes heterocyclic aromatic amines of industrial origin. CYP1A2 metabolizes numerous natural products that result in toxic products, such as the transformation of methyleugenol to 1'-hydroxymethyleugenol, estragole to reactive metabolites, and oxidation of nephrotoxins. It also plays an important role in the metabolism of several clinical drugs including analgesics, antipyretics, antipsychotics, antidepressants, anti-inflammatory, and cardiovascular drugs. The CYP1A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 55.41  E-value: 3.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 320 VTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTT-RTL 398
Cdd:cd20676  242 VNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPFTIpHCT 321

                         90
                 ....*....|....*
gi 193083117 399 DKATVLGEYALPKGI 413
Cdd:cd20676  322 TRDTSLNGYYIPKDT 336
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 285-412 4.36e-08

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: 55.15  E-value: 4.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 285 CIDNRLEKYSQQPSADFlcdiyhqnrlSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQ 364
Cdd:cd20669  206 CFLTKMAEEKQDPLSHF----------NMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNR 275

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 193083117 365 VPRAEDLRNMPYLKACLKESMRLTPSVPFT-TRTLDKATVLGEYALPKG 412
Cdd:cd20669  276 LPTLEDRARMPYTDAVIHEIQRFADIIPMSlPHAVTRDTNFRGFLIPKG 324
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 310-425 5.36e-08

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: 54.82  E-value: 5.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 310 RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQS------VLPENQVPRAEDLRNMPYLKACLKE 383
Cdd:cd20638  225 PLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEkgllstKPNENKELSMEVLEQLKYTGCVIKE 304

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 193083117 384 SMRLTPSVPFTTRTLDKATVLGEYALPKGIVRKYDIQATDNE 425
Cdd:cd20638  305 TLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDV 346
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 93-412 5.39e-08

cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes CYP2A1, 2A2, and 2A3 in rats; CYP2A4, 2A5, 2A12, 2A20p, 2A21p, 2A22, and 2A23p in mice; CYP2A6, 2A7, 2A13, 2A18P in humans; CYP2A8, 2A9, 2A14, 2A15, 2A16, and 2A17 in hamsters; CYP2A10 and 2A11 in rabbits; and CYP2A19 in pigs. CYP2A enzymes metabolize numerous xenobiotic compounds, including coumarin, aflatoxin B1, nicotine, cotinine, 1,3-butadiene, and acetaminophen, among others, as well as endogenous compounds, including testosterone, progesterone, and other steroid hormones. Human CYP2A6 is responsible for the systemic clearance of nicotine, while CYP2A13 activates the nicotine-derived procarcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) into DNA-altering compounds that cause lung cancer. The CYP2A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 54.80  E-value: 5.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117  93 YGKIFRMKLGSFESVHL-GSPCLLEALYRTESAYPQRLEikpwKAYRDYRKEGYGLLILEGEDWQRVRSaFQKKLMKPGE 171
Cdd:cd20668    1 YGPVFTIHLGPRRVVVLcGYDAVKEALVDQAEEFSGRGE----QATFDWLFKGYGVAFSNGERAKQLRR-FSIATLRDFG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 172 VMK--LDNKINEVlADFMgrIDELCDERGHVEDLYSELNKWSFESICLVLYEKRFGLLQKNagdeavnFIMAIKTMMSTF 249
Cdd:cd20668   76 VGKrgIEERIQEE-AGFL--IDALRGTGGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKE-------FLSLLRMMLGSF 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 250 gRMMVTPVELHKSLNTKVWQDHTLAWDTIFKSVKACIDNRLEKYSQ-QPSAD----------FLCDIYHQNRLSKKELYA 318
Cdd:cd20668  146 -QFTATSTGQLYEMFSSVMKHLPGPQQQAFKELQGLEDFIAKKVEHnQRTLDpnsprdfidsFLIRMQEEKKNPNTEFYM 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 319 ---AVTELQL--AAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPF 393
Cdd:cd20668  225 knlVMTTLNLffAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPM 304

                        330       340
                 ....*....|....*....|
gi 193083117 394 -TTRTLDKATVLGEYALPKG 412
Cdd:cd20668  305 gLARRVTKDTKFRDFFLPKG 324
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 144-414 8.28e-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: 54.38  E-value: 8.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 144 GYGLLILEGEDWQRVRsafqkKLMKPGEVMKLDNKINEVLADFMGR-IDELCDERGHVEDLYS--ELNKWSFESICLVLY 220
Cdd:cd20641   58 GKGLVFVNGDDWVRHR-----RVLNPAFSMDKLKSMTQVMADCTERmFQEWRKQRNNSETERIevEVSREFQDLTADIIA 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 221 EKRFGL-LQKnaGDEAVNFIMAIKTMMSTFGRMMVTPVE--LHKSLNTKVWQDHTLAWDTIfksvKACIDNRLEKYSQQP 297
Cdd:cd20641  133 TTAFGSsYAE--GIEVFLSQLELQKCAAASLTNLYIPGTqyLPTPRNLRVWKLEKKVRNSI----KRIIDSRLTSEGKGY 206

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 298 SADFL-----------CDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVP 366
Cdd:cd20641  207 GDDLLglmleaassneGGRRTERKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIP 286

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 193083117 367 RAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGIV 414
Cdd:cd20641  287 DADTLSKLKLMNMVLMETLRLYGPVINIARRASEDMKLGGLEIPKGTT 334
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 325-393 9.00e-08

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 54.15  E-value: 9.00e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193083117 325 LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPF 393
Cdd:cd20653  237 LAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPL 305
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 325-412 1.19e-07

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 53.93  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 325 LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQV-PRAEDLRNMPYLKACLKESMRLTPSVPFttrtlDKATV 403
Cdd:PLN02426 303 LAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNQEaASFEEMKEMHYLHAALYESMRLFPPVQF-----DSKFA 377


                 ....*....
gi 193083117 404 LGEYALPKG 412
Cdd:PLN02426 378 AEDDVLPDG 386
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 274-427 2.48e-07

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: 52.54  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 274 AWDTIFKSVKACIDNRLEKYSQQPSADFLcDIY------HQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQ 347
Cdd:cd20637  180 ARDSLQKSLEKAIREKLQGTQGKDYADAL-DILiesakeHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPG 258

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 348 VQQKLLKEIQSV-LPENQVP-----RAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGIVRKYDIQA 421
Cdd:cd20637  259 VLEKLREELRSNgILHNGCLcegtlRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSVLYSIRD 338


                 ....*..
gi 193083117 422 T-DNEPV 427
Cdd:cd20637  339 ThDTAPV 345
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 274-439 4.49e-07

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: 51.76  E-value: 4.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 274 AWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQNR-----LSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQV 348
Cdd:cd20636  181 ARDILHEYMEKAIEEKLQRQQAAEYCDALDYMIHSARengkeLTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 349 QQKLLKEIQS--VLPENQVPRA----EDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKGIVRKYDIQAT 422
Cdd:cd20636  261 IEKIRQELVShgLIDQCQCCPGalslEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQIPKGWSVMYSIRDT 340

                        170
                 ....*....|....*..
gi 193083117 423 DNEPVEMLHSGTLVPSR 439
Cdd:cd20636  341 HETAAVYQNPEGFDPDR 357
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 337-412 7.70e-07

cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also called 24-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.26) or oxysterol 7-alpha-hydroxylase. It is involved in the metabolism of bile acids and has a preference for 24-hydroxycholesterol, converting it into the 7-alpha-hydroxylated product. It may play a role in the alternative bile acid synthesis pathway in the liver. CYP39A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410728  Cd Length: 410  Bit Score: 51.16  E-value: 7.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 337 WILYNLSRNPQVQQKLLKEIQSVLPENQVPRA----EDLRNMPYLKACLKESMRLTpSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd20635  232 WTLAFILSHPSVYKKVMEEISSVLGKAGKDKIkiseDDLKKMPYIKRCVLEAIRLR-SPGAITRKVVKPIKIKNYTIPAG 310
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 316-412 1.11e-06

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


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 50.72  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 316 LYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMR---LTP-SV 391
Cdd:cd20665  227 LAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRyidLVPnNL 306

                         90       100
                 ....*....|....*....|.
gi 193083117 392 PfttRTLDKATVLGEYALPKG 412
Cdd:cd20665  307 P---HAVTCDTKFRNYLIPKG 324
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 193-412 1.32e-06

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: 50.46  E-value: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 193 LCD----ERGHVEDLYSELNKWSFESICLVLYEKRFgllqkNAGDEavNFIMAIKTMMSTFGR--------MMVTPVELH 260
Cdd:cd20663   96 LCAaftdQAGRPFNPNTLLNKAVCNVIASLIFARRF-----EYEDP--RFIRLLKLLEESLKEesgflpevLNAFPVLLR 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 261 -KSLNTKVWQDHtlawdtifKSVKACIDNRLEKYSQ-----QPSAD----FLCDIYH-----QNRLSKKELYAAVTELQL 325
Cdd:cd20663  169 iPGLAGKVFPGQ--------KAFLALLDELLTEHRTtwdpaQPPRDltdaFLAEMEKakgnpESSFNDENLRLVVADLFS 240

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 326 AAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVP-----FTTRTLDk 400
Cdd:cd20663  241 AGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPlgvphMTSRDIE- 319

                        250
                 ....*....|..
gi 193083117 401 atVLGeYALPKG 412
Cdd:cd20663  320 --VQG-FLIPKG 328
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 326-412 3.07e-06

C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 710; C-22 sterol desaturase (EC 1.14.19.41), also called sterol 22-desaturase, is required for the formation of the C-22 double bond in the sterol side chain of delta22-unsaturated sterols, which are present specifically in fungi and plants. This enzyme is also called cytochrome P450 61 (CYP61) in fungi and cytochrome P450 710 (CYP710) in plants. The CYP61/CYP710 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 49.17  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 326 AAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENQVP-RAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVL 404
Cdd:cd11082  231 ASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEPPlTLDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPL 310


                 ....*....
gi 193083117 405 GE-YALPKG 412
Cdd:cd11082  311 TEdYTVPKG 319
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 325-412 3.31e-06

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 49.16  E-value: 3.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 325 LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVL---PENQVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKA 401
Cdd:PLN02196 274 FAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRkdkEEGESLTWEDTKKMPLTSRVIQETLRVASILSFTFREAVED 353

                         90
                 ....*....|.
gi 193083117 402 TVLGEYALPKG 412
Cdd:PLN02196 354 VEYEGYLIPKG 364
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 290-412 7.03e-06

cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes Mycobacterium tuberculosis cytochrome P450 130 (CYP130), Rhodococcus erythropolis CYP116, and similar bacterial proteins. CYP130 catalyzes the N-demethylation of dextromethorphan, and has also shown a natural propensity to bind primary arylamines. CYP116 is involved in the degradation of thiocarbamate herbicides. The CYP130-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 47.98  E-value: 7.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 290 LEKYSQQPSADFLCDIYHQN-----RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEIQsvlpenQ 364
Cdd:cd11078  179 VAERRREPRDDLISDLLAAAdgdgeRLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRADPS------L 252

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 193083117 365 VPRAedlrnmpylkacLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd11078  253 IPNA------------VEETLRYDSPVQGLRRTATRDVEIGGVTIPAG 288
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
 266-411 1.38e-05

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: 47.12  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 266 KVWQDHTLAWDTIFKSVKAcidnrlEKYSQQPSADFLCDIYHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRN 345
Cdd:cd20627  159 KQYEDALMEMESVLKKVIK------ERKGKNFSQHVFIDSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTS 232

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193083117 346 PQVQQKLLKEIQSVLPENQVPrAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPK 411
Cdd:cd20627  233 EEVQKKLYKEVDQVLGKGPIT-LEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPK 297
PLN02290 PLN02290
cytokinin trans-hydroxylase
 326-413 2.35e-05

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 46.73  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 326 AAVETTANSLMWILYNLSRNPQVQQKLLKEIQSVLPENqVPRAEDLRNMPYLKACLKESMRLTPSVPFTTRTLDKATVLG 405
Cdd:PLN02290 327 AGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGE-TPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLG 405


                 ....*...
gi 193083117 406 EYALPKGI 413
Cdd:PLN02290 406 DLHIPKGL 413
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 146-414 3.65e-05

cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus P450 monooxygenase AurH which is uniquely capable of forming a homochiral tetrahydrofuran ring, a vital component of the polyketide antibiotic aureothin. AurH catalyzes an unprecedented tandem oxygenation process: first, it catalyzes an asymmetric hydroxylation of deoxyaureothin to yield (7R)-7-hydroxydeoxyaureothin as an intermediate; and second, it mediates another C-O bond formation that leads to O-heterocyclization. The AurH-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: 410664 [Multi-domain]  Cd Length: 382  Bit Score: 45.82  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 146 GLLILEGEDWQRVRsafqkKLMKPGevmkLDNKINEVLADFMGRI-DELCD---ERGHVEDLYSELNKWSFESICLVLye 221
Cdd:cd11038   70 FLLSLEGADHARLR-----GLVNPA----FTPKAVEALRPRFRATaNDLIDgfaEGGECEFVEAFAEPYPARVICTLL-- 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 222 krfGLLQKNAGDeavnfimaIKTMMSTFGRMMVTPVELHKSlntKVWQdhtlAWDTIFksvkACIDNRLEKYSQQPSADF 301
Cdd:cd11038  139 ---GLPEEDWPR--------VHRWSADLGLAFGLEVKDHLP---RIEA----AVEELY----DYADALIEARRAEPGDDL 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 302 LCDIYHQ----NRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQvQQKLLKEIQSvLPENQVpraedlrnmpyl 377
Cdd:cd11038  197 ISTLVAAeqdgDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPD-QWRALREDPE-LAPAAV------------ 262

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 193083117 378 kaclKESMRLTPSVPFTTRTLDKATVLGEYALPKGIV 414
Cdd:cd11038  263 ----EEVLRWCPTTTWATREAVEDVEYNGVTIPAGTV 295
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 297-412 1.33e-04

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: 43.83  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 297 PSADFLCDI----YHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEiqsvlpENQVPRAedlr 372
Cdd:cd20629  170 PGDDLISRLlraeVEGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRRD------RSLIPAA---- 239

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 193083117 373 nmpylkacLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd20629  240 --------IEEGLRWEPPVASVPRMALRDVELDGVTIPAG 271
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 301-412 1.73e-04

cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1.14.15.13), also called pulcherriminic acid synthase or cyclo-L-leucyl-L-leucyl dipeptide oxidase or cytochrome P450 CYPX, catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms the red pigment pulcherrimin via a non-enzymatic spontaneous reaction with Fe(3+). It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 43.61  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 301 FLCDI-YHQNRLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQvQQKLLKEIQSVLPenqvpraedlrnmpylkA 379
Cdd:cd11080  178 ILCTAeYEGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPE-QLAAVRADRSLVP-----------------R 239

                         90       100       110
                 ....*....|....*....|....*....|...
gi 193083117 380 CLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd11080  240 AIAETLRYHPPVQLIPRQASQDVVVSGMEIKKG 272
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 338-393 1.84e-04

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: 43.79  E-value: 1.84e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 193083117 338 ILYNLSR-NPQVQQKLLKEIQSVLPENQVPRAEDLRNMPYLKACLKESMRLTPSVPF 393
Cdd:cd11071  248 LLARLGLaGEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPL 304
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 332-412 1.87e-04

cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also called cholesterol 7-alpha-monooxygenase (EC 1.14.14.23) or cholesterol 7-alpha-hydroxylase. It catalyzes the hydroxylation at position 7 of cholesterol, a rate-limiting step in the classic (or neutral) pathway of cholesterol catabolism and bile acid biosynthesis. It is important for cholesterol homeostasis. CYP7A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 43.52  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 332 ANSL---MWILYNLSRNPQVQQKLLKEIQSVLPE-NQVPR---------AEDLRNMPYLKACLKESMRLTpSVPFTTRTL 398
Cdd:cd20631  241 ANTLpatFWSLFYLLRCPEAMKAATKEVKRTLEKtGQKVSdggnpivltREQLDDMPVLGSIIKEALRLS-SASLNIRVA 319

                         90
                 ....*....|....*....
gi 193083117 399 DKATVL-----GEYALPKG 412
Cdd:cd20631  320 KEDFTLhldsgESYAIRKD 338
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 326-412 2.96e-04

cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Rhodopseudomonas palustris CYP199A2 and CYP199A4. CYP199A2 catalyzes the oxidation of aromatic carboxylic acids including indole-2-carboxylic acid, 2-naphthoic acid and 4-ethylbenzoic acid. CYP199A4 catalyzes the hydroxylation of para-substituted benzoic acids. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 42.96  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 326 AAVETTANSLMWILYNLSRNPQVQQKLlkeiqsvlpenqvpraedlRNMPYL-KACLKESMRLTPSVPFTTRTLDKATVL 404
Cdd:cd11037  213 AGLDTTISAIGNALWLLARHPDQWERL-------------------RADPSLaPNAFEEAVRLESPVQTFSRTTTRDTEL 273


                 ....*...
gi 193083117 405 GEYALPKG 412
Cdd:cd11037  274 AGVTIPAG 281
PLN02648 PLN02648
allene oxide synthase
 338-393 4.29e-04

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 42.61  E-value: 4.29e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193083117 338 ILYNLSR-NPQVQQKLLKEIQSVLPEN-QVPRAEDLRNMPYLKACLKESMRLTPSVPF 393
Cdd:PLN02648 295 LLKWVGRaGEELQARLAEEVRSAVKAGgGGVTFAALEKMPLVKSVVYEALRIEPPVPF 352
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 289-412 7.66e-04

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


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 41.68  E-value: 7.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 289 RLEKYSQQPSADFLcdIYHQNRLSKKELYAAVTELQ--LAAVETTANSLMWILYNLSRNPQVQQKLLKEIQsvlpenQVP 366
Cdd:cd20624  165 RLREYVERAEPGSL--VGELSRLPEGDEVDPEGQVPqwLFAFDAAGMALLRALALLAAHPEQAARAREEAA------VPP 236

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 193083117 367 RAEDLrnmPYLKACLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd20624  237 GPLAR---PYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRTVPAG 279
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 288-387 1.42e-03

cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also called 25-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.29) or oxysterol 7-alpha-hydroxylase. It catalyzes the 7alpha-hydroxylation of both steroids and oxysterols, and is thus implicated in the metabolism of neurosteroids and bile acid synthesis, respectively. It participates in the alternative (or acidic) pathway of cholesterol catabolism and bile acid biosynthesis. It also mediates the formation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) from 25-hydroxycholesterol; 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor in lymphoid cells. CYP7B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410725  Cd Length: 438  Bit Score: 40.75  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 288 NRLEKYsqQPSADFLcdiyhQNRlskKELYAAVTELQ------------LAAVETTANSLMWILYNLSRNPQVQQKLLKE 355
Cdd:cd20632  186 QKMAKW--SNPSEVI-----QAR---QELLEQYDVLQdydkaahhfaflWASVGNTIPATFWAMYYLLRHPEALAAVRDE 255

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 193083117 356 IQSVLPENQVPRA---------EDLRNMPYLKACLKESMRL 387
Cdd:cd20632  256 IDHVLQSTGQELGpdfdihltrEQLDSLVYLESAINESLRL 296
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 256-412 1.58e-03

P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome P450cin (P450cin, also called CYP176A1) and similar proteins. P450cin is a bacterial P450 enzyme that catalyzes the enantiospecific hydroxylation of 1,8-cineole to (1R)-6beta-hydroxycineole; its natural reduction-oxidation partner is cindoxin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 40.40  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 256 PVELHKSLNTKVWQDHTL----AWDTIFKSVKACIDNRLEKYSQQPSADFLCDIYHQN----RLSKKELYAAVTELQLAA 327
Cdd:cd11034  123 PDEDGERLRDWVHAILHDedpeEGAAAFAELFGHLRDLIAERRANPRDDLISRLIEGEidgkPLSDGEVIGFLTLLLLGG 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 328 VETTANSLMWILYNLSRNPQVQQKLLKEiqsvlpENQVPRAEDlrnmpylkaclkESMRLTPSVPFTTRTLDKATVLGEY 407
Cdd:cd11034  203 TDTTSSALSGALLWLAQHPEDRRRLIAD------PSLIPNAVE------------EFLRFYSPVAGLARTVTQEVEVGGC 264


                 ....*
gi 193083117 408 ALPKG 412
Cdd:cd11034  265 RLKPG 269
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 326-412 1.87e-03

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 40.47  E-value: 1.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 326 AAVETTANSLMWILYNLSRNPQVQQKLLKE---IQSVLPENQVPRA-EDLRNMPYLKACLKESMRLTPSVPFTTRTLDKA 401
Cdd:PLN02302 298 AGHESSGHLTMWATIFLQEHPEVLQKAKAEqeeIAKKRPPGQKGLTlKDVRKMEYLSQVIDETLRLINISLTVFREAKTD 377

                         90
                 ....*....|.
gi 193083117 402 TVLGEYALPKG 412
Cdd:PLN02302 378 VEVNGYTIPKG 388
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 289-412 4.62e-03

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 39.12  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 289 RLEKYSQQPSADFLCDIYHQN----RLSKKELYAAVTELQLAAVETTANSLMWILYNLSRNPQVQQKLLKEiQSVLPenq 364
Cdd:cd11032  168 HLEERRRNPRDDLISRLVEAEvdgeRLTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRAD-PSLIP--- 243

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 193083117 365 vpraedlrnmpylkACLKESMRLTPSVPFTTRTLDKATVLGEYALPKG 412
Cdd:cd11032  244 --------------GAIEEVLRYRPPVQRTARVTTEDVELGGVTIPAG 277
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 323-412 5.70e-03

prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; Prostacyclin synthase, also called prostaglandin I2 synthase (PGIS) or cytochrome P450 8a1 (CYP8A1), catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 38.97  E-value: 5.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083117 323 LQLAAVETTAN-SLMWILYNLSRNPQVQQKLLKEIQSVLPENQVPRA-------EDLRNMPYLKACLKESMRLTpSVPFT 394
Cdd:cd20634  228 LQLWATQGNAGpAAFWLLLFLLKHPEAMAAVRGEIQRIKHQRGQPVSqtltinqELLDNTPVFDSVLSETLRLT-AAPFI 306

                         90       100
                 ....*....|....*....|...
gi 193083117 395 TR--TLDKATVLG---EYALPKG 412
Cdd:cd20634  307 TRevLQDMKLRLAdgqEYNLRRG 329
 
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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