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Conserved domains on  [gi|1148921820|ref|XP_020124983|]
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cytochrome p450 [Diplodia corticola]

Protein Classification

cytochrome P450( domain architecture ID 15296315)

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

CATH:  1.10.630.10
Gene Ontology:  GO:0004497|GO:0005506|GO:0016705|GO:0020037
PubMed:  27267697|8405421|7678494|28124606
SCOP:  4001206

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 55-496 3.51e-157

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: 454.06  E-value: 3.51e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820  55 EGYEKAKLNPQwIFQIPTVSSPMTILAPALLDEIRAVSEKKLNFRREMYDRFVGRYTAFA--SNDSAMVVAIKNKLTPGI 132
Cdd:cd11041     2 EGYEKYKKNGG-PFQLPTPDGPLVVLPPKYLDELRNLPESVLSFLEALEEHLAGFGTGGSvvLDSPLHVDVVRKDLTPNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 133 DRLLPTMDDEAQFAVRTTLASCgaDGWTTVPLHSTATRLIALLSGRVFVGLPLSRNEEWIDAAVNVTQHSIAGAFKLLAY 212
Cdd:cd11041    81 PKLLPDLQEELRAALDEELGSC--TEWTEVNLYDTVLRIVARVSARVFVGPPLCRNEEWLDLTINYTIDVFAAAAALRLF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 213 PAWLRPLVRLFVREVGGVEECRQATERMLRPLVEQRLRDMRSGGADfqGQDDMIQWLITHAPPGSVSDVAWHVSQHLVLN 292
Cdd:cd11041   159 PPFLRPLVAPFLPEPRRLRRLLRRARPLIIPEIERRRKLKKGPKED--KPNDLLQWLIEAAKGEGERTPYDLADRQLALS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 293 IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPIT 372
Cdd:cd11041   237 FAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVT 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 373 LSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENSFQFVSSNASGISFGHGKAACPGRWFAATEL 452
Cdd:cd11041   317 LSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQEKKHQFVSTSPDFLGFGHGRHACPGRFFASNEI 396

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1148921820 453 KVMLARLLPDFDFALAEGGDGPLHAFVDVLGAPDPTRQIRVRRR 496
Cdd:cd11041   397 KLILAHLLLNYDFKLPEGGERPKNIWFGEFIMPDPNAKVLVRRR 440
 
Name Accession Description Interval E-value
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 55-496 3.51e-157

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: 454.06  E-value: 3.51e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820  55 EGYEKAKLNPQwIFQIPTVSSPMTILAPALLDEIRAVSEKKLNFRREMYDRFVGRYTAFA--SNDSAMVVAIKNKLTPGI 132
Cdd:cd11041     2 EGYEKYKKNGG-PFQLPTPDGPLVVLPPKYLDELRNLPESVLSFLEALEEHLAGFGTGGSvvLDSPLHVDVVRKDLTPNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 133 DRLLPTMDDEAQFAVRTTLASCgaDGWTTVPLHSTATRLIALLSGRVFVGLPLSRNEEWIDAAVNVTQHSIAGAFKLLAY 212
Cdd:cd11041    81 PKLLPDLQEELRAALDEELGSC--TEWTEVNLYDTVLRIVARVSARVFVGPPLCRNEEWLDLTINYTIDVFAAAAALRLF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 213 PAWLRPLVRLFVREVGGVEECRQATERMLRPLVEQRLRDMRSGGADfqGQDDMIQWLITHAPPGSVSDVAWHVSQHLVLN 292
Cdd:cd11041   159 PPFLRPLVAPFLPEPRRLRRLLRRARPLIIPEIERRRKLKKGPKED--KPNDLLQWLIEAAKGEGERTPYDLADRQLALS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 293 IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPIT 372
Cdd:cd11041   237 FAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVT 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 373 LSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENSFQFVSSNASGISFGHGKAACPGRWFAATEL 452
Cdd:cd11041   317 LSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQEKKHQFVSTSPDFLGFGHGRHACPGRFFASNEI 396

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1148921820 453 KVMLARLLPDFDFALAEGGDGPLHAFVDVLGAPDPTRQIRVRRR 496
Cdd:cd11041   397 KLILAHLLLNYDFKLPEGGERPKNIWFGEFIMPDPNAKVLVRRR 440
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 128-475 1.85e-32

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: 128.94  E-value: 1.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 128 LTPGIDRLLPTMDDEAQFAVRTTLASCGADGWTTVplhstaTRLIAL----LSGRVFVGLPLSRNEE--------WIDAA 195
Cdd:pfam00067 107 TSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDI------TDLLFRaalnVICSILFGERFGSLEDpkflelvkAVQEL 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 196 VNVTQHSiagAFKLLAYPAWLRPLVRLFVREVggvEECRQATERMLRPLVEQRLRDMRSggaDFQGQDDMIQWLI---TH 272
Cdd:pfam00067 181 SSLLSSP---SPQLLDLFPILKYFPGPHGRKL---KRARKKIKDLLDKLIEERRETLDS---AKKSPRDFLDALLlakEE 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 273 APPGSVSD---VAwhvsQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFL 349
Cdd:pfam00067 252 EDGSKLTDeelRA----TVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVI 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 350 REVQRLSPPGLVSVNRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSENSFQFvssn 429
Cdd:pfam00067 328 KETLRLHPVVPLLLPREVTKDTVI-PGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERF--LDENGKFRKSFAF---- 400

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1148921820 430 asgISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGGDGPL 475
Cdd:pfam00067 401 ---LPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPD 443
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 128-472 4.44e-24

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: 103.82  E-value: 4.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 128 LTPG-IDRLLPTMDDEAqfavRTTLASCGADGwtTVPLHSTATRLIALLSGRVFVGLPLSRNEEWIDAAvnvtqHSIAGA 206
Cdd:COG2124   102 FTPRrVAALRPRIREIA----DELLDRLAARG--PVDLVEEFARPLPVIVICELLGVPEEDRDRLRRWS-----DALLDA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 207 FKLLAYPAWLRplvrlfvrevggVEECRQATERMLRPLVEQRLRDmrsggadfqGQDDMIQWLITHAPPG---SVSDVAW 283
Cdd:COG2124   171 LGPLPPERRRR------------ARRARAELDAYLRELIAERRAE---------PGDDLLSALLAARDDGerlSDEELRD 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 284 HVSQHLVlniAAIHTTSGQLSGTLFALAARPHYMQPLREEIEAcilkhgaltkqclhdmvkLDSFLREVQRLSPPGLVsV 363
Cdd:COG2124   230 ELLLLLL---AGHETTANALAWALYALLRHPEQLARLRAEPEL------------------LPAAVEETLRLYPPVPL-L 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 364 NRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPadfDGFRFARlrtepgsensfqfvsSNASGISFGHGKAACP 443
Cdd:COG2124   288 PRTATEDVEL-GGVTIPAGDRVLLSLAAANRDPRVFPDP---DRFDPDR---------------PPNAHLPFGGGPHRCL 348

                         330       340       350
                  ....*....|....*....|....*....|
gi 1148921820 444 GRWFAATELKVMLARLLPDF-DFALAEGGD 472
Cdd:COG2124   349 GAALARLEARIALATLLRRFpDLRLAPPEE 378
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 218-464 1.89e-14

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 75.54  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 218 PLVRLFVRevGGVEECRQATERMLR----PLVEQRLRDMRSGGADFQGQDDMIQWLITHAPPGSVS--DVAWHVSQhlvL 291
Cdd:PLN02394  227 PILRPFLR--GYLKICQDVKERRLAlfkdYFVDERKKLMSAKGMDKEGLKCAIDHILEAQKKGEINedNVLYIVEN---I 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 292 NIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPI 371
Cdd:PLN02394  302 NVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDA 381

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 372 TLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSE---NSFQFVSsnasgisFGHGKAACPGRWFA 448
Cdd:PLN02394  382 KLG-GYDIPAESKILVNAWWLANNPELWKNPEEFRPERF--LEEEAKVEangNDFRFLP-------FGVGRRSCPGIILA 451

                         250
                  ....*....|....*.
gi 1148921820 449 ATELKVMLARLLPDFD 464
Cdd:PLN02394  452 LPILGIVLGRLVQNFE 467
 
Name Accession Description Interval E-value
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 55-496 3.51e-157

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: 454.06  E-value: 3.51e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820  55 EGYEKAKLNPQwIFQIPTVSSPMTILAPALLDEIRAVSEKKLNFRREMYDRFVGRYTAFA--SNDSAMVVAIKNKLTPGI 132
Cdd:cd11041     2 EGYEKYKKNGG-PFQLPTPDGPLVVLPPKYLDELRNLPESVLSFLEALEEHLAGFGTGGSvvLDSPLHVDVVRKDLTPNL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 133 DRLLPTMDDEAQFAVRTTLASCgaDGWTTVPLHSTATRLIALLSGRVFVGLPLSRNEEWIDAAVNVTQHSIAGAFKLLAY 212
Cdd:cd11041    81 PKLLPDLQEELRAALDEELGSC--TEWTEVNLYDTVLRIVARVSARVFVGPPLCRNEEWLDLTINYTIDVFAAAAALRLF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 213 PAWLRPLVRLFVREVGGVEECRQATERMLRPLVEQRLRDMRSGGADfqGQDDMIQWLITHAPPGSVSDVAWHVSQHLVLN 292
Cdd:cd11041   159 PPFLRPLVAPFLPEPRRLRRLLRRARPLIIPEIERRRKLKKGPKED--KPNDLLQWLIEAAKGEGERTPYDLADRQLALS 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 293 IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPIT 372
Cdd:cd11041   237 FAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVT 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 373 LSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENSFQFVSSNASGISFGHGKAACPGRWFAATEL 452
Cdd:cd11041   317 LSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQEKKHQFVSTSPDFLGFGHGRHACPGRFFASNEI 396

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1148921820 453 KVMLARLLPDFDFALAEGGDGPLHAFVDVLGAPDPTRQIRVRRR 496
Cdd:cd11041   397 KLILAHLLLNYDFKLPEGGERPKNIWFGEFIMPDPNAKVLVRRR 440
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 128-475 1.85e-32

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: 128.94  E-value: 1.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 128 LTPGIDRLLPTMDDEAQFAVRTTLASCGADGWTTVplhstaTRLIAL----LSGRVFVGLPLSRNEE--------WIDAA 195
Cdd:pfam00067 107 TSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDI------TDLLFRaalnVICSILFGERFGSLEDpkflelvkAVQEL 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 196 VNVTQHSiagAFKLLAYPAWLRPLVRLFVREVggvEECRQATERMLRPLVEQRLRDMRSggaDFQGQDDMIQWLI---TH 272
Cdd:pfam00067 181 SSLLSSP---SPQLLDLFPILKYFPGPHGRKL---KRARKKIKDLLDKLIEERRETLDS---AKKSPRDFLDALLlakEE 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 273 APPGSVSD---VAwhvsQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFL 349
Cdd:pfam00067 252 EDGSKLTDeelRA----TVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVI 327

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 350 REVQRLSPPGLVSVNRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSENSFQFvssn 429
Cdd:pfam00067 328 KETLRLHPVVPLLLPREVTKDTVI-PGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERF--LDENGKFRKSFAF---- 400

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1148921820 430 asgISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGGDGPL 475
Cdd:pfam00067 401 ---LPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPD 443
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 132-483 5.96e-32

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: 126.48  E-value: 5.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 132 IDRLLPTMDDEAQFAVrTTLASCGADGwttVPLHSTATRLIALLSGRVFVGLPLsrneewidaavNVTQHSIAGAFKLLA 211
Cdd:cd00302    75 LAALRPVIREIARELL-DRLAAGGEVG---DDVADLAQPLALDVIARLLGGPDL-----------GEDLEELAELLEALL 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 212 YPAWLRPLVRLFVREVGGVEECRQATERMLRPLVEQRLRDmrsggadfqGQDDMIQWLITHAPPGSVSDVAWHVSQHLVL 291
Cdd:cd00302   140 KLLGPRLLRPLPSPRLRRLRRARARLRDYLEELIARRRAE---------PADDLDLLLLADADDGGGLSDEEIVAELLTL 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 292 NIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHgalTKQCLHDMVKLDSFLREVQRLSPPgLVSVNRKVLEPI 371
Cdd:cd00302   211 LLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG---TPEDLSKLPYLEAVVEETLRLYPP-VPLLPRVATEDV 286

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 372 TLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtEPGSENSFQFvssnasgISFGHGKAACPGRWFAATE 451
Cdd:cd00302   287 EL-GGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFL----PEREEPRYAH-------LPFGAGPHRCLGARLARLE 354

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1148921820 452 LKVMLARLLPDFDFALAEGGDGPLHAFVDVLG 483
Cdd:cd00302   355 LKLALATLLRRFDFELVPDEELEWRPSLGTLG 386
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 186-470 5.51e-30

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: 121.61  E-value: 5.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 186 SRNEEWIDAAVNVTQHSIAGAFKLLAYPAWLRPLVRLFVREVGG-VEECRQATERMLRPLVEQRLRDMRSGGADfQGQDd 264
Cdd:cd11069   137 NPDNELAEAYRRLFEPTLLGSLLFILLLFLPRWLVRILPWKANReIRRAKDVLRRLAREIIREKKAALLEGKDD-SGKD- 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 265 miqwLITHAPPGSVSDVAWHVSQHLVLN-----IAAIH-TTSGQLSGTLFALAARPHYMQPLREEIEACILKHGA--LTK 336
Cdd:cd11069   215 ----ILSILLRANDFADDERLSDEELIDqiltfLAAGHeTTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDgdLSY 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 337 QCLHDMVKLDSFLREVQRLSPPGLVSVnRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWerPADFDGFRFAR-Lrt 415
Cdd:cd11069   291 DDLDRLPYLNAVCRETLRLYPPVPLTS-REATKDTVI-KGVPIPKGTVVLIPPAAINRSPEIW--GPDAEEFNPERwL-- 364

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1148921820 416 EPGSENSFQFVSSNASGISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd11069   365 EPDGAASPGGAGSNYALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPD 419
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 201-471 9.94e-30

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: 120.40  E-value: 9.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 201 HSIAGAFKLLAYPAWLRPLVRlFVRevggveecRQATERMLRPLVEQRLRDMRSGGADfqGQDDMIQWLI----THAPPG 276
Cdd:cd11042   140 HDLDGGFTPIAFFFPPLPLPS-FRR--------RDRARAKLKEIFSEIIQKRRKSPDK--DEDDMLQTLMdakyKDGRPL 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 277 SVSDVAWHvsqHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGA-LTKQCLHDMVKLDSFLREVQRL 355
Cdd:cd11042   209 TDDEIAGL---LIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDpLTYDVLKEMPLLHACIKETLRL 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 356 SPPgLVSVNRKVLEPITLSNGQ-RLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENSFQFvssnasgIS 434
Cdd:cd11042   286 HPP-IHSLMRKARKPFEVEGGGyVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKGGKFAY-------LP 357

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1148921820 435 FGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGG 471
Cdd:cd11042   358 FGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSP 394
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 187-476 6.81e-29

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: 118.07  E-value: 6.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 187 RNEEWIDAAVNVTQHSIAGAFKLLAYPAWLRPLVRLFVREVGG--VEECRQATERMlrplVEQRLRDMRSGgadfqgQDD 264
Cdd:cd11055   133 PDDPFLKAAKKIFRNSIIRLFLLLLLFPLRLFLFLLFPFVFGFksFSFLEDVVKKI----IEQRRKNKSSR------RKD 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 265 MIQWLI------THAPPGSVSD--VawhVSQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTK 336
Cdd:cd11055   203 LLQLMLdaqdsdEDVSKKKLTDdeI---VAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTY 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 337 QCLHDMVKLDSFLREVQRLSPPGLVsVNRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarlrtE 416
Cdd:cd11055   280 DTVSKLKYLDMVINETLRLYPPAFF-ISRECKEDCTI-NGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERF-----S 352

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 417 PGSENSFQfvssNASGISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGGDGPLH 476
Cdd:cd11055   353 PENKAKRH----PYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETEIPLK 408
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 129-494 1.36e-26

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


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 111.61  E-value: 1.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 129 TPGIDRLLPTMDDEAQFAVRTtLASCGadgwtTVPLHSTATRLIALLSGRVFVGLplsRNEEWIDAAVNVTQHSIAGAFK 208
Cdd:cd11044    92 REALESYVPTIQAIVQSYLRK-WLKAG-----EVALYPELRRLTFDVAARLLLGL---DPEVEAEALSQDFETWTDGLFS 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 209 L-LAYPAwlrplvrlfvrevGGVEECRQATERMLRpLVEQRLRDMRSGGAdfQGQDDMIQWLITHAP----PGSVSDVaw 283
Cdd:cd11044   163 LpVPLPF-------------TPFGRAIRARNKLLA-RLEQAIRERQEEEN--AEAKDALGLLLEAKDedgePLSMDEL-- 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 284 hVSQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKhGALTKQCLHDMVKLDSFLREVQRLSPPgLVSV 363
Cdd:cd11044   225 -KDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLE-EPLTLESLKKMPYLDQVIKEVLRLVPP-VGGG 301

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 364 NRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARlrtePGSENSfqfvSSNASGISFGHGKAACP 443
Cdd:cd11044   302 FRKVLEDFEL-GGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSP----ARSEDK----KKPFSLIPFGGGPRECL 372

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1148921820 444 GRWFAATELKVMLARLLPDFDFALAEGGDGPLHafvdVLGAPDPTRQIRVR 494
Cdd:cd11044   373 GKEFAQLEMKILASELLRNYDWELLPNQDLEPV----VVPTPRPKDGLRVR 419
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 209-476 2.33e-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: 110.78  E-value: 2.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 209 LLAYPAWLRPLVRLFVREVGGVEEcRQATERMLRPLVEQRLRdmrsggADFQGQDDMIQWLI--THAPPGSVSDVAWHVS 286
Cdd:cd11061   147 VLGHAPWLRPLLLDLPLFPGATKA-RKRFLDFVRAQLKERLK------AEEEKRPDIFSYLLeaKDPETGEGLDLEELVG 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 287 QHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACI-----LKHGALTKQCLHdmvkLDSFLREVQRLSPPGLV 361
Cdd:cd11061   220 EARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFpsddeIRLGPKLKSLPY----LRACIDEALRLSPPVPS 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 362 SVNRKVL-EPITLsNGQRLPVGTSIAFPADAINRDPELWERPADF-------DGFRFARLRtepgseNSFqfvssnasgI 433
Cdd:cd11061   296 GLPRETPpGGLTI-DGEYIPGGTTVSVPIYSIHRDERYFPDPFEFiperwlsRPEELVRAR------SAF---------I 359

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1148921820 434 SFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGGDGPLH 476
Cdd:cd11061   360 PFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPGEDGEAG 402
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 297-469 8.50e-25

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: 106.49  E-value: 8.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 297 HTTSGQLSGTLFALAARPHYMQPLREEIEAcILKHGA-LTKQCLHDMVKLDSFLREVQRLSPPgLVSVNRKVLEPITLSn 375
Cdd:cd20659   241 DTTASGISWTLYSLAKHPEHQQKCREEVDE-VLGDRDdIEWDDLSKLPYLTMCIKESLRLYPP-VPFIARTLTKPITID- 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 376 GQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtepgSENS-----FQFvssnasgISFGHGKAACPGRWFAAT 450
Cdd:cd20659   318 GVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFL-------PENIkkrdpFAF-------IPFSAGPRNCIGQNFAMN 383

                         170
                  ....*....|....*....
gi 1148921820 451 ELKVMLARLLPDFDFALAE 469
Cdd:cd20659   384 EMKVVLARILRRFELSVDP 402
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 128-472 4.44e-24

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: 103.82  E-value: 4.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 128 LTPG-IDRLLPTMDDEAqfavRTTLASCGADGwtTVPLHSTATRLIALLSGRVFVGLPLSRNEEWIDAAvnvtqHSIAGA 206
Cdd:COG2124   102 FTPRrVAALRPRIREIA----DELLDRLAARG--PVDLVEEFARPLPVIVICELLGVPEEDRDRLRRWS-----DALLDA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 207 FKLLAYPAWLRplvrlfvrevggVEECRQATERMLRPLVEQRLRDmrsggadfqGQDDMIQWLITHAPPG---SVSDVAW 283
Cdd:COG2124   171 LGPLPPERRRR------------ARRARAELDAYLRELIAERRAE---------PGDDLLSALLAARDDGerlSDEELRD 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 284 HVSQHLVlniAAIHTTSGQLSGTLFALAARPHYMQPLREEIEAcilkhgaltkqclhdmvkLDSFLREVQRLSPPGLVsV 363
Cdd:COG2124   230 ELLLLLL---AGHETTANALAWALYALLRHPEQLARLRAEPEL------------------LPAAVEETLRLYPPVPL-L 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 364 NRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPadfDGFRFARlrtepgsensfqfvsSNASGISFGHGKAACP 443
Cdd:COG2124   288 PRTATEDVEL-GGVTIPAGDRVLLSLAAANRDPRVFPDP---DRFDPDR---------------PPNAHLPFGGGPHRCL 348

                         330       340       350
                  ....*....|....*....|....*....|
gi 1148921820 444 GRWFAATELKVMLARLLPDF-DFALAEGGD 472
Cdd:COG2124   349 GAALARLEARIALATLLRRFpDLRLAPPEE 378
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 184-486 5.94e-24

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: 103.76  E-value: 5.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 184 PLSRNEEWIDAAVNVTQHSiagaFKLLAYPAWLR----PLVRLFVRevgGVEECRQATERmlrpLVEQRLRDMRSGGADF 259
Cdd:cd11054   143 PDSDAQKLIEAVKDIFESS----AKLMFGPPLWKyfptPAWKKFVK---AWDTIFDIASK----YVDEALEELKKKDEED 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 260 QGQDDMIQWLITHaPPGSVSDVAWHVSQHLvlnIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCL 339
Cdd:cd11054   212 EEEDSLLEYLLSK-PGLSKKEIVTMALDLL---LAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDL 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 340 HDMVKLDSFLREVQRLSPPGLVsVNRKVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGS 419
Cdd:cd11054   288 KKMPYLKACIKESLRLYPVAPG-NGRILPKDIVLS-GYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERW--LRDDSEN 363

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148921820 420 ENSFQFVSsnasgISFGHGKAACPGRWFAATELKVMLARLLPDFDFalaEGGDGPLHAFVDVLGAPD 486
Cdd:cd11054   364 KNIHPFAS-----LPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKV---EYHHEELKVKTRLILVPD 422
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 132-472 5.13e-22

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: 98.03  E-value: 5.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 132 IDRLLPTMDDEAQFAVRTTLAscGADGwTTVPLHSTATRLIALLSGRVFVGLPLSRNEEWIDAAVNVTQHSIAGAFKLLA 211
Cdd:cd20620    74 IAAYADAMVEATAALLDRWEA--GARR-GPVDVHAEMMRLTLRIVAKTLFGTDVEGEADEIGDALDVALEYAARRMLSPF 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 212 YP--AWLRPLVRLFVREVGGVEecrqateRMLRPLVEQRLRDMRSGGadfqgqdDMIQWLITHAPPGSvsDVAWHVSQ-- 287
Cdd:cd20620   151 LLplWLPTPANRRFRRARRRLD-------EVIYRLIAERRAAPADGG-------DLLSMLLAARDEET--GEPMSDQQlr 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 288 -HLVLNIAAIH-TTSGQLSGTLFALAARPHYMQPLREEIEAcILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVsVNR 365
Cdd:cd20620   215 dEVMTLFLAGHeTTANALSWTWYLLAQHPEVAARLRAEVDR-VLGGRPPTAEDLPQLPYTEMVLQESLRLYPPAWI-IGR 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 366 KVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENSFqfvssnasgISFGHGKAACPGR 445
Cdd:cd20620   293 EAVEDDEIG-GYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPRYAY---------FPFGGGPRICIGN 362

                         330       340
                  ....*....|....*....|....*..
gi 1148921820 446 WFAATELKVMLARLLPDFDFALAEGGD 472
Cdd:cd20620   363 HFAMMEAVLLLATIAQRFRLRLVPGQP 389
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 306-492 1.31e-21

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: 97.05  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 306 TLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVK-----LDSFLREVQRLSPPGLVsvNRKVLEPITLSNGQRLP 380
Cdd:cd11040   246 LLAHILSDPELLERIREEIEPAVTPDSGTNAILDLTDLLtscplLDSTYLETLRLHSSSTS--VRLVTEDTVLGGGYLLR 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 381 VGTSIAFPADAINRDPELWERPAD-FDGFRFARlrtEPGSENSFQFVSSNasgISFGHGKAACPGRWFAATELKVMLARL 459
Cdd:cd11040   324 KGSLVMIPPRLLHMDPEIWGPDPEeFDPERFLK---KDGDKKGRGLPGAF---RPFGGGASLCPGRHFAKNEILAFVALL 397

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1148921820 460 LPDFDFALAEGGD--GPLHAFVDVLGAPDPTRQIR 492
Cdd:cd11040   398 LSRFDVEPVGGGDwkVPGMDESPGLGILPPKRDVR 432
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 132-470 2.22e-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: 96.17  E-value: 2.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 132 IDRLLPTMDDEAQFAVrttlascgaDGWT---TVPLHSTATRLIALLSGRVFVGLPL-SRNEEWIDAAVNVTqhsIAGAF 207
Cdd:cd11049    86 IPAYAEVMREEAEALA---------GSWRpgrVVDVDAEMHRLTLRVVARTLFSTDLgPEAAAELRQALPVV---LAGML 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 208 KLLAYPAWLRPLVRLFVREvggveeCRQATERmLRPLVEQRLRDMRSGGADfqgQDDMIQWLITHAPPGSV--SDVAWHv 285
Cdd:cd11049   154 RRAVPPKFLERLPTPGNRR------FDRALAR-LRELVDEIIAEYRASGTD---RDDLLSLLLAARDEEGRplSDEELR- 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 286 SQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEAcILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVsVNR 365
Cdd:cd11049   223 DQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDA-VLGGRPATFEDLPRLTYTRRVVTEALRLYPPVWL-LTR 300

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 366 KVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENSFqfvssnasgISFGHGKAACPGR 445
Cdd:cd11049   301 RTTADVELG-GHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAF---------IPFGAGARKCIGD 370

                         330       340
                  ....*....|....*....|....*
gi 1148921820 446 WFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd11049   371 TFALTELTLALATIASRWRLRPVPG 395
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 245-476 6.47e-21

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: 94.96  E-value: 6.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 245 VEQRLRDMRSGGadfQGQDDMIQWLITH--APPGSVSDvaWHVSQHLVLNI-AAIHTTSGQLSGTLFALAARPHYMQPLR 321
Cdd:cd11060   186 VAERLAEDAESA---KGRKDMLDSFLEAglKDPEKVTD--REVVAEALSNIlAGSDTTAIALRAILYYLLKNPRVYAKLR 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 322 EEIEACILKHGA---LTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEP-ITLSnGQRLPVGTSIAFPADAINRDPE 397
Cdd:cd11060   261 AEIDAAVAEGKLsspITFAEAQKLPYLQAVIKEALRLHPPVGLPLERVVPPGgATIC-GRFIPGGTIVGVNPWVIHRDKE 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 398 LWerPADFDGFRFAR-LRTEPGSENSfqfvsSNASGISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEgGDGPLH 476
Cdd:cd11060   340 VF--GEDADVFRPERwLEADEEQRRM-----MDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVD-PEKEWK 411
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 207-465 1.00e-20

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


Pssm-ID: 410680 [Multi-domain]  Cd Length: 427  Bit Score: 94.21  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 207 FKLLAYPAWLRPLVRLFVREvggvEECRQATERMLRPLVEQRLRDMRSGGADFQGQDDM--------IQWLITHAPPGSV 278
Cdd:cd11057   147 LNPWLHPEFIYRLTGDYKEE----QKARKILRAFSEKIIEKKLQEVELESNLDSEEDEEngrkpqifIDQLLELARNGEE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 279 -SDVAwhVSQHLVLNIAAIH-TTSGQLSGTLFALAARPHYMQPLREEI-EACILKHGALTKQCLHDMVKLDSFLREVQRL 355
Cdd:cd11057   223 fTDEE--IMDEIDTMIFAGNdTSATTVAYTLLLLAMHPEVQEKVYEEImEVFPDDGQFITYEDLQQLVYLEMVLKETMRL 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 356 SPPGLVsVNRKVLEPITLSNGQRLPVGTSIAFPADAINRDPELW-ERPADFDGFRFARLRTEPGSENSFqfvssnasgIS 434
Cdd:cd11057   301 FPVGPL-VGRETTADIQLSNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQRHPYAF---------IP 370

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1148921820 435 FGHGKAACPGRWFAATELKVMLARLLPDFDF 465
Cdd:cd11057   371 FSAGPRNCIGWRYAMISMKIMLAKILRNYRL 401
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 217-470 1.98e-20

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: 93.35  E-value: 1.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 217 RPLVRLFVREVGGVEECRQATeRMLRPL----VEQRLRDMRSGgaDFQGQDDMIQWLITHAPPGSVSDvawhvsQHLVLN 292
Cdd:cd20613   168 NPLLKYNPSKRKYRREVREAI-KFLRETgrecIEERLEALKRG--EEVPNDILTHILKASEEEPDFDM------EELLDD 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 293 -----IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLHDMVKL---DSFLREVQRLSPPGlVSVN 364
Cdd:cd20613   239 fvtffIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVL---GSKQYVEYEDLGKLeylSQVLKETLRLYPPV-PGTS 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 365 RKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSENSFQFvssnasgISFGHGKAACPG 444
Cdd:cd20613   315 RELTKDIEL-GGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERF--SPEAPEKIPSYAY-------FPFSLGPRSCIG 384

                         250       260
                  ....*....|....*....|....*.
gi 1148921820 445 RWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd20613   385 QQFAQIEAKVILAKLLQNFKFELVPG 410
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 263-469 3.27e-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: 92.99  E-value: 3.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 263 DDMIQWLI----THAPPGSVSDVAWH----VSQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKH-GA 333
Cdd:cd11056   201 NDFIDLLLelkkKGKIEDDKSEKELTdeelAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHgGE 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 334 LTKQCLHDMVKLDSFLREVQRLSPPgLVSVNRKVLEPITLsNGQR--LPVGTSIAFPADAINRDPELWERPADFDGFRFa 411
Cdd:cd11056   281 LTYEALQEMKYLDQVVNETLRKYPP-LPFLDRVCTKDYTL-PGTDvvIEKGTPVIIPVYALHHDPKYYPEPEKFDPERF- 357

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1148921820 412 rlrTEPGSENSFQFVSsnasgISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAE 469
Cdd:cd11056   358 ---SPENKKKRHPYTY-----LPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSS 407
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 231-483 6.95e-20

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: 91.63  E-value: 6.95e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 231 EECRQATERMLRPLVEQRLRDMRSGGADFQGQDDMiQWLITHAppgSVSDVAWHVSQHLVLN------IAAIHTTSGQLS 304
Cdd:cd11052   178 KKLDKEIEDSLLEIIKKREDSLKMGRGDDYGDDLL-GLLLEAN---QSDDQNKNMTVQEIVDecktffFAGHETTALLLT 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 305 GTLFALAARPHYMQPLREEI-EACilKHGALTKQCLHDMVKLDSFLREVQRLSPPgLVSVNRKVLEPITLsNGQRLPVGT 383
Cdd:cd11052   254 WTTMLLAIHPEWQEKAREEVlEVC--GKDKPPSDSLSKLKTVSMVINESLRLYPP-AVFLTRKAKEDIKL-GGLVIPKGT 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 384 SIAFPADAINRDPELWERPAD-FDGFRFArlrtepgsENSFQFVSSNASGISFGHGKAACPGRWFAATELKVMLARLLPD 462
Cdd:cd11052   330 SIWIPVLALHHDEEIWGEDANeFNPERFA--------DGVAKAAKHPMAFLPFGLGPRNCIGQNFATMEAKIVLAMILQR 401

                         250       260
                  ....*....|....*....|.
gi 1148921820 463 FDFALAEggdGPLHAFVDVLG 483
Cdd:cd11052   402 FSFTLSP---TYRHAPTVVLT 419
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 230-472 2.27e-19

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: 90.38  E-value: 2.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 230 VEECRQATERMLRPLVEQRLRDMRSGGADFQGQDDmiqwLITHAPPGSVSDVAWHVSQHLVLN------IAAIHTTSGQL 303
Cdd:cd11075   176 VLELRRRQEEVLLPLIRARRKRRASGEADKDYTDF----LLLDLLDLKEEGGERKLTDEELVSlcseflNAGTDTTATAL 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 304 SGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPITLsNGQRLPVGT 383
Cdd:cd11075   252 EWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHFLLPHAVTEDTVL-GGYDIPAGA 330

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 384 SIAFPADAINRDPELWERPADFDGFRFArlrtePGSENSfqFVSSNASGIS---FGHGKAACPGRWFAATELKVMLARLL 460
Cdd:cd11075   331 EVNFNVAAIGRDPKVWEDPEEFKPERFL-----AGGEAA--DIDTGSKEIKmmpFGAGRRICPGLGLATLHLELFVARLV 403

                         250
                  ....*....|..
gi 1148921820 461 PDFDFALAEGGD 472
Cdd:cd11075   404 QEFEWKLVEGEE 415
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 239-470 2.96e-19

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: 89.94  E-value: 2.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 239 RMLRPLVEQRLRDMRSGGADfqGQDDMIQWLITHAPPGS---VSDVAWhVSQHLVLNIAAIHTTSGQLSGTLFALAARPH 315
Cdd:cd11068   186 ALMRDLVDEIIAERRANPDG--SPDDLLNLMLNGKDPETgekLSDENI-RYQMITFLIAGHETTSGLLSFALYYLLKNPE 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 316 YMQPLREEIEAcILKHGALTKQCLHDMVKLDSFLREVQRLSP--PGLVsvnRKVLEPITLSNGQRLPVGTSIAFPADAIN 393
Cdd:cd11068   263 VLAKARAEVDE-VLGDDPPPYEQVAKLRYIRRVLDETLRLWPtaPAFA---RKPKEDTVLGGKYPLKKGDPVLVLLPALH 338

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1148921820 394 RDPELW-ERPADFDGFRFARLRTEPGSENSFQfvssnasgiSFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd11068   339 RDPSVWgEDAEEFRPERFLPEEFRKLPPNAWK---------PFGNGQRACIGRQFALQEATLVLAMLLQRFDFEDDPD 407
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 239-491 3.74e-19

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


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 89.78  E-value: 3.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 239 RMLRPLVEQRLRDMRSGGADFqgqddmIQWLI-THAPPGSVSDVAWH----VSQHLVLNIAAIHTTSGQLSGTLFALAAR 313
Cdd:cd20650   185 KSVKKIKESRLDSTQKHRVDF------LQLMIdSQNSKETESHKALSdleiLAQSIIFIFAGYETTSSTLSFLLYELATH 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 314 PHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPG--LVSVNRKVLEpitlSNGQRLPVGTSIAFPADA 391
Cdd:cd20650   259 PDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAgrLERVCKKDVE----INGVFIPKGTVVMIPTYA 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 392 INRDPELWERPADFDGFRFArlRTEPGSENSFQFvssnasgISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGG 471
Cdd:cd20650   335 LHRDPQYWPEPEEFRPERFS--KKNKDNIDPYIY-------LPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPCKET 405

                         250       260
                  ....*....|....*....|
gi 1148921820 472 DGPLHafVDVLGAPDPTRQI 491
Cdd:cd20650   406 QIPLK--LSLQGLLQPEKPI 423
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 202-467 6.70e-19

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: 88.77  E-value: 6.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 202 SIAGAFKLLAYPAWLRPLvrlfvrEVGGVE----ECRQATERMLRPLVEQRlRDMRSGGADFQGQDDMIQWLITHAPPGS 277
Cdd:cd20618   152 ELAGAFNIGDYIPWLRWL------DLQGYEkrmkKLHAKLDRFLQKIIEEH-REKRGESKKGGDDDDDLLLLLDLDGEGK 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 278 VSDvawHVSQHLVLNI--AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRL 355
Cdd:cd20618   225 LSD---DNIKALLLDMlaAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRL 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 356 SPPGLVSVNRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENSFQFvssnasgISF 435
Cdd:cd20618   302 HPPGPLLLPHESTEDCKV-AGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVKGQDFEL-------LPF 373

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1148921820 436 GHGKAACPGRWFAATELKVMLARLLPDFDFAL 467
Cdd:cd20618   374 GSGRRMCPGMPLGLRMVQLTLANLLHGFDWSL 405
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 298-489 3.26e-18

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: 86.95  E-value: 3.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 298 TTSGQLSGTLFALAARPHYMQPLREEIEAcILKHGA-LTKQCLHDMVKLDSFLREVQRLSPPGlVSVNRKVLEPITLSNG 376
Cdd:cd20678   254 TTASGISWILYCLALHPEHQQRCREEIRE-ILGDGDsITWEHLDQMPYTTMCIKEALRLYPPV-PGISRELSKPVTFPDG 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 377 QRLPVGTSIAFPADAINRDPELWERPADFDGFRFARlrtepgsENSFQfVSSNASgISFGHGKAACPGRWFAATELKVML 456
Cdd:cd20678   332 RSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSP-------ENSSK-RHSHAF-LPFSAGPRNCIGQQFAMNEMKVAV 402

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1148921820 457 ARLLPDFDFalaeggdgplhafvdvlgAPDPTR 489
Cdd:cd20678   403 ALTLLRFEL------------------LPDPTR 417
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 210-476 3.88e-18

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: 86.48  E-value: 3.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 210 LAYPAWLRPlVRLFVREVGGVEECRQATERMLRPLVEQRLRDMRSGGadfqgqDDMIQWLI--THAPPGSVSDVawHVSQ 287
Cdd:cd11053   156 LASFPALQR-DLGPWSPWGRFLRARRRIDALIYAEIAERRAEPDAER------DDILSLLLsaRDEDGQPLSDE--ELRD 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 288 HLVLNIAAIH-TTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLHDMVKLDSFLREVQRLSPPGLVsVNRK 366
Cdd:cd11053   227 ELMTLLFAGHeTTATALAWAFYWLHRHPEVLARLLAELDALG---GDPDPEDIAKLPYLDAVIKETLRLYPVAPL-VPRR 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 367 VLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPgsensFQFvssnasgISFGHGKAACPGRW 446
Cdd:cd11053   303 VKEPVEL-GGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRKPSP-----YEY-------LPFGGGVRRCIGAA 369

                         250       260       270
                  ....*....|....*....|....*....|
gi 1148921820 447 FAATELKVMLARLLPDFDFALAEGGDGPLH 476
Cdd:cd11053   370 FALLEMKVVLATLLRRFRLELTDPRPERPV 399
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 213-470 4.07e-18

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: 86.65  E-value: 4.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 213 PAWLRPLVRLFVrevGGVEECRQATERM---LRPLVEQRLR-----DMRSGGADFQGQDDMIQWLITHAPPGSVSDVAWH 284
Cdd:cd11046   165 PYWDIPAALFIV---PRQRKFLRDLKLLndtLDDLIRKRKEmrqeeDIELQQEDYLNEDDPSLLRFLVDMRDEDVDSKQL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 285 VSQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSP-PGLVSv 363
Cdd:cd11046   242 RDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPqPPVLI- 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 364 nRKVLEPITLSNGQ-RLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSEnsfqfVSSNASGISFGHGKAAC 442
Cdd:cd11046   321 -RRAVEDDKLPGGGvKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNE-----VIDDFAFLPFGGGPRKC 394

                         250       260
                  ....*....|....*....|....*...
gi 1148921820 443 PGRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd11046   395 LGDQFALLEATVALAMLLRRFDFELDVG 422
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 290-460 5.19e-18

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


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 86.23  E-value: 5.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 290 VLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQC--LHDMVKLDSFLREVQRLSPPgLVSVNRKV 367
Cdd:cd11070   230 IFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEedFPKLPYLLAVIYETLRLYPP-VQLLNRKT 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 368 LEPITLSNGQ----RLPVGTSIAFPADAINRDPELW-ERPADFDGFRFarLRTEPGSENSFQFVSSNASGISFGHGKAAC 442
Cdd:cd11070   309 TEPVVVITGLgqeiVIPKGTYVGYNAYATHRDPTIWgPDADEFDPERW--GSTSGEIGAATRFTPARGAFIPFSAGPRAC 386

                         170
                  ....*....|....*...
gi 1148921820 443 PGRWFAATELKVMLARLL 460
Cdd:cd11070   387 LGRKFALVEFVAALAELF 404
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 285-465 8.43e-18

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: 85.38  E-value: 8.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 285 VSQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVN 364
Cdd:cd20621   231 IQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLFP 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 365 RKVLEPITLSNGQrLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSENSFQFvssnasgISFGHGKAACPG 444
Cdd:cd20621   311 RVATQDHQIGDLK-IKKGWIVNVGYIYNHFNPKYFENPDEFNPERW--LNQNNIEDNPFVF-------IPFSAGPRNCIG 380

                         170       180
                  ....*....|....*....|.
gi 1148921820 445 RWFAATELKVMLARLLPDFDF 465
Cdd:cd20621   381 QHLALMEAKIILIYILKNFEI 401
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 298-460 3.15e-17

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: 83.73  E-value: 3.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 298 TTSGQLSGTLFALAARPHYMQPLREEIEAcILKH--GALTKQCLHDMVKLDSFLREVQRLSPPG-LVSvnRKVLEPITLs 374
Cdd:cd20628   244 TTASAISFTLYLLGLHPEVQEKVYEELDE-IFGDddRRPTLEDLNKMKYLERVIKETLRLYPSVpFIG--RRLTEDIKL- 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 375 NGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSENSFQFvssnasgISFGHGKAACPGRWFAATELKV 454
Cdd:cd20628   320 DGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRF--LPENSAKRHPYAY-------IPFSAGPRNCIGQKFAMLEMKT 390


                  ....*.
gi 1148921820 455 MLARLL 460
Cdd:cd20628   391 LLAKIL 396
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 285-475 5.27e-17

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: 83.35  E-value: 5.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 285 VSQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLvSVN 364
Cdd:cd20649   263 VGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAF-RFA 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 365 RKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRF---ARLRTEPgsensFQFvssnasgISFGHGKAA 441
Cdd:cd20649   342 REAAEDCVV-LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFtaeAKQRRHP-----FVY-------LPFGAGPRS 408

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1148921820 442 CPGRWFAATELKVMLARLLPDFDFALAEGGDGPL 475
Cdd:cd20649   409 CIGMRLALLEIKVTLLHILRRFRFQACPETEIPL 442
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 190-475 1.00e-16

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: 82.24  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 190 EWIDAavnVTQHSIAGAF-KLLAYPAWLRPLVRLFVREvgGVEECRQATERMLRPLVEQRLrDMRSGGADFqgqddmIQW 268
Cdd:cd11058   135 PWVAL---IFDSIKALTIiQALRRYPWLLRLLRLLIPK--SLRKKRKEHFQYTREKVDRRL-AKGTDRPDF------MSY 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 269 LITHAPPG---SVSDVAWHVSqhlVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKL 345
Cdd:cd11058   203 ILRNKDEKkglTREELEANAS---LLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQLPYL 279

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 346 DSFLREVQRLSPPGLVSVNRKVLEPITLSNGQRLPVGTSIAFPADAINRDPELWERPADF--------DGFRFARLRTEp 417
Cdd:cd11058   280 NAVIQEALRLYPPVPAGLPRVVPAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFiperwlgdPRFEFDNDKKE- 358

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1148921820 418 gsenSFQFvssnasgisFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGGDGPL 475
Cdd:cd11058   359 ----AFQP---------FSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPESEDWL 403
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 293-465 1.47e-16

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


Pssm-ID: 410710 [Multi-domain]  Cd Length: 419  Bit Score: 81.49  E-value: 1.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 293 IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLHDMVK---LDSFLREVQRLSPPGLVSVNRKVLE 369
Cdd:cd20617   233 LAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVV---GNDRRVTLSDRSKlpyLNAVIKEVLRLRPILPLGLPRVTTE 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 370 PITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLrTEPGSENSFQFvssnasgISFGHGKAACPGRWFAA 449
Cdd:cd20617   310 DTEI-GGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERF--L-ENDGNKLSEQF-------IPFGIGKRNCVGENLAR 378

                         170
                  ....*....|....*.
gi 1148921820 450 TELKVMLARLLPDFDF 465
Cdd:cd20617   379 DELFLFFANLLLNFKF 394
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 284-474 2.03e-16

cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily contains cytochrome P450 17A1 (CYP17A1 or Cyp17a1), cytochrome P450 21 (CYP21 or Cyp21) and similar proteins. CYP17A1, also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione; it catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. This subfamily also contains CYP21, also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2, catalyzes the 21-hydroxylation of steroids and is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. The CYP17A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410653 [Multi-domain]  Cd Length: 428  Bit Score: 81.10  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 284 HVSQHLV-LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTkqcLHDMVKL---DSFLREVQRLSPPG 359
Cdd:cd11027   229 HLVMTISdIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPT---LSDRKRLpylEATIAEVLRLSSVV 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 360 LVSVNRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrTEPGsensfQFVSSNASGISFGHGK 439
Cdd:cd11027   306 PLALPHKTTCDTTL-RGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFL---DENG-----KLVPKPESFLPFSAGR 376

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1148921820 440 AACPGRWFAATELKVMLARLLPDFDFALAEGGDGP 474
Cdd:cd11027   377 RVCLGESLAKAELFLFLARLLQKFRFSPPEGEPPP 411
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 289-470 2.84e-16

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: 80.97  E-value: 2.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNI--AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRK 366
Cdd:cd11072   232 IILDMflAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLPRE 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 367 VLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtepGSE-----NSFQFvssnasgISFGHGKAA 441
Cdd:cd11072   312 CREDCKI-NGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFL------DSSidfkgQDFEL-------IPFGAGRRI 377

                         170       180
                  ....*....|....*....|....*....
gi 1148921820 442 CPGRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd11072   378 CPGITFGLANVELALANLLYHFDWKLPDG 406
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 234-476 7.08e-16

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


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 79.28  E-value: 7.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 234 RQATERMLRPLVEQRLRDmrsGGADF------QGQDDMIQWlithappgSVSDVAWHVsqhLVLNIAAIHTTSGQLSGTL 307
Cdd:cd11045   170 RRYLEEYFRRRIPERRAG---GGDDLfsalcrAEDEDGDRF--------SDDDIVNHM---IFLMMAAHDTTTSTLTSMA 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 308 FALAARPHYMQPLREEIEAciLKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEpiTLSNGQRLPVGTSIAF 387
Cdd:cd11045   236 YFLARHPEWQERLREESLA--LGKGTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKD--TEVLGYRIPAGTLVAV 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 388 PADAINRDPELWERPADFDGFRFARLRTEPGsENSFQFVssnasgiSFGHGKAACPGRWFAATELKVMLARLLPDFDFAL 467
Cdd:cd11045   312 SPGVTHYMPEYWPNPERFDPERFSPERAEDK-VHRYAWA-------PFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWS 383


                  ....*....
gi 1148921820 468 AEGGDGPLH 476
Cdd:cd11045   384 VPGYYPPWW 392
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 293-489 2.56e-15

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: 77.64  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 293 IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlKHGALTKqcLHDMVKL---DSFLREVQRLSPPGLVSVNRKVLE 369
Cdd:cd20651   235 IAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVV-GRDRLPT--LDDRSKLpytEAVILEVLRIFTLVPIGIPHRALK 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 370 PITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrTEPGsensfQFVSSNASgISFGHGKAACPGRWFAA 449
Cdd:cd20651   312 DTTL-GGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFL---DEDG-----KLLKDEWF-LPFGAGKRRCLGESLAR 381

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1148921820 450 TELKVMLARLLPDFDFALAEGGDGPLHAFVDVLGA-PDPTR 489
Cdd:cd20651   382 NELFLFFTGLLQNFTFSPPNGSLPDLEGIPGGITLsPKPFR 422
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 290-464 3.52e-15

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: 77.21  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 290 VLNI--AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPglVSVNRKV 367
Cdd:cd11063   221 LLNIllAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPP--VPLNSRV 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 368 -LEPITLSNG----QRLPV----GTSIAFPADAINRDPELW-ERPADFDGFRFarlrtEPGSENSFQFvssnasgISFGH 437
Cdd:cd11063   299 aVRDTTLPRGggpdGKSPIfvpkGTRVLYSVYAMHRRKDIWgPDAEEFRPERW-----EDLKRPGWEY-------LPFNG 366

                         170       180
                  ....*....|....*....|....*..
gi 1148921820 438 GKAACPGRWFAATELKVMLARLLPDFD 464
Cdd:cd11063   367 GPRICLGQQFALTEASYVLVRLLQTFD 393
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 294-468 3.91e-15

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: 77.49  E-value: 3.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 294 AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGlVSVNRKVLEPITL 373
Cdd:cd20639   243 AGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLYPPA-VATIRRAKKDVKL 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 374 SnGQRLPVGTSIAFPADAINRDPELW-ERPADFDGFRFArlrtepgsENSFQFVSSNASGISFGHGKAACPGRWFAATEL 452
Cdd:cd20639   322 G-GLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFA--------DGVARAAKHPLAFIPFGLGPRTCVGQNLAILEA 392

                         170
                  ....*....|....*.
gi 1148921820 453 KVMLARLLPDFDFALA 468
Cdd:cd20639   393 KLTLAVILQRFEFRLS 408
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 207-473 8.03e-15

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: 76.46  E-value: 8.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 207 FKLLAY-PAWLRplvRLFVREVggvEECRQATERMLRPLVEQRLRDMRSGGA------DFQGQDDmiqwlitHAPPGSVS 279
Cdd:cd11065   156 FPFLRYlPSWLG---APWKRKA---RELRELTRRLYEGPFEAAKERMASGTAtpsfvkDLLEELD-------KEGGLSEE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 280 DVAWHVSqhlVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEAcILKHGALTkqCLHDMVKL---DSFLREVQRLS 356
Cdd:cd11065   223 EIKYLAG---SLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDR-VVGPDRLP--TFEDRPNLpyvNAIVKEVLRWR 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 357 PPGLVSVNRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENSFQFVSsnasgisFG 436
Cdd:cd11065   297 PVAPLGIPHALTEDDEY-EGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPDPPHFA-------FG 368

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1148921820 437 HGKAACPGRWFAATELKVMLARLLPDFDFALAEGGDG 473
Cdd:cd11065   369 FGRRICPGRHLAENSLFIAIARLLWAFDIKKPKDEGG 405
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 298-468 1.58e-14

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: 75.53  E-value: 1.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 298 TTSGQLSGTLFALAARPHYMQPLREEI-EACilKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVsVNRKVLEPITLSnG 376
Cdd:cd20640   245 TTAVTAAWCLMLLALHPEWQDRVRAEVlEVC--KGGPPDADSLSRMKTVTMVIQETLRLYPPAAF-VSREALRDMKLG-G 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 377 QRLPVGTSIAFPADAINRDPELWERPAD-FDGFRFARLRtePGSENSFQfvssnaSGISFGHGKAACPGRWFAATELKVM 455
Cdd:cd20640   321 LVVPKGVNIWVPVSTLHLDPEIWGPDANeFNPERFSNGV--AAACKPPH------SYMPFGAGARTCLGQNFAMAELKVL 392

                         170
                  ....*....|...
gi 1148921820 456 LARLLPDFDFALA 468
Cdd:cd20640   393 VSLILSKFSFTLS 405
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 218-464 1.89e-14

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 75.54  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 218 PLVRLFVRevGGVEECRQATERMLR----PLVEQRLRDMRSGGADFQGQDDMIQWLITHAPPGSVS--DVAWHVSQhlvL 291
Cdd:PLN02394  227 PILRPFLR--GYLKICQDVKERRLAlfkdYFVDERKKLMSAKGMDKEGLKCAIDHILEAQKKGEINedNVLYIVEN---I 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 292 NIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPI 371
Cdd:PLN02394  302 NVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDA 381

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 372 TLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSE---NSFQFVSsnasgisFGHGKAACPGRWFA 448
Cdd:PLN02394  382 KLG-GYDIPAESKILVNAWWLANNPELWKNPEEFRPERF--LEEEAKVEangNDFRFLP-------FGVGRRSCPGIILA 451

                         250
                  ....*....|....*.
gi 1148921820 449 ATELKVMLARLLPDFD 464
Cdd:PLN02394  452 LPILGIVLGRLVQNFE 467
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 291-475 1.01e-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: 72.89  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLHD---MVKLDSFLREVQRLSPPGLVSVNRKV 367
Cdd:cd20666   236 LFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVI---GPDRAPSLTDkaqMPFTEATIMEVQRMTVVVPLSIPHMA 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 368 LEPiTLSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtepgSENSfQFVsSNASGISFGHGKAACPGRWF 447
Cdd:cd20666   313 SEN-TVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFL-------DENG-QLI-KKEAFIPFGIGRRVCMGEQL 382

                         170       180
                  ....*....|....*....|....*...
gi 1148921820 448 AATELKVMLARLLPDFDFALAEGGDGPL 475
Cdd:cd20666   383 AKMELFLMFVSLMQSFTFLLPPNAPKPS 410
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 306-492 2.12e-13

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: 72.03  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 306 TLFALAARPHYMQPLREEIEACILKHG----------ALTKQCLHDMVKLDSFLREVQRLSPpglVSVN-RKVLE--PIT 372
Cdd:cd20631   250 SLFYLLRCPEAMKAATKEVKRTLEKTGqkvsdggnpiVLTREQLDDMPVLGSIIKEALRLSS---ASLNiRVAKEdfTLH 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 373 LSNGQRLPV--GTSIAFPADAINRDPELWERPADFdgfRFARLRTEPGSENSFQFvsSNASGIS-----FGHGKAACPGR 445
Cdd:cd20631   327 LDSGESYAIrkDDIIALYPQLLHLDPEIYEDPLTF---KYDRYLDENGKEKTTFY--KNGRKLKyyympFGSGTSKCPGR 401

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1148921820 446 WFAATELKVMLARLLPDFDFALaeggdgplhafVDVLGAPDPTRQIR 492
Cdd:cd20631   402 FFAINEIKQFLSLMLCYFDMEL-----------LDGNAKCPPLDQSR 437
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 293-471 3.74e-13

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


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 71.09  E-value: 3.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 293 IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVnRKVLEPIT 372
Cdd:cd20655   238 IAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLV-RESTEGCK 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 373 LsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGS------ENSFQFvssnasgISFGHGKAACPGRW 446
Cdd:cd20655   317 I-NGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERF--LASSRSGqeldvrGQHFKL-------LPFGSGRRGCPGAS 386

                         170       180
                  ....*....|....*....|....*
gi 1148921820 447 FAATELKVMLARLLPDFDFALAEGG 471
Cdd:cd20655   387 LAYQVVGTAIAAMVQCFDWKVGDGE 411
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 289-471 4.40e-13

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


Pssm-ID: 410704 [Multi-domain]  Cd Length: 421  Bit Score: 70.81  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALT-KQCLHDMVKLDSFLREVQRLSPpgLVSVNrkV 367
Cdd:cd11083   228 LTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPlLEALDRLPYLEAVARETLRLKP--VAPLL--F 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 368 LEPI--TLSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSENSFQfvssnASGISFGHGKAACPGR 445
Cdd:cd11083   304 LEPNedTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERW--LDGARAAEPHDP-----SSLLPFGAGPRLCPGR 376

                         170       180
                  ....*....|....*....|....*.
gi 1148921820 446 WFAATELKVMLARLLPDFDFALAEGG 471
Cdd:cd11083   377 SLALMEMKLVFAMLCRNFDIELPEPA 402
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 207-470 5.39e-13

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: 70.70  E-value: 5.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 207 FKLLAYPAWLRPLVRLFvrEVGgveecrqaTERMLR-----------PLVEQRLRDMRSGGADFQGQDDMIQWLI--THA 273
Cdd:cd11064   152 AKRFIVPPWLWKLKRWL--NIG--------SEKKLReairviddfvyEVISRRREELNSREEENNVREDLLSRFLasEEE 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 274 PPGSVSDVawhVSQHLVLN--IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEAcILKHGA------LTKQCLHDMVKL 345
Cdd:cd11064   222 EGEPVSDK---FLRDIVLNfiLAGRDTTAAALTWFFWLLSKNPRVEEKIREELKS-KLPKLTtdesrvPTYEELKKLVYL 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 346 DSFLREVQRLSPPglVSVNRK-VLEPITLSNGQRLPVGTSIAFPADAINRDPELW-ERPADFDGFRFarLRTEPG--SEN 421
Cdd:cd11064   298 HAALSESLRLYPP--VPFDSKeAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERW--LDEDGGlrPES 373

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1148921820 422 SFQFVSSNAsgisfghGKAACPGRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd11064   374 PYKFPAFNA-------GPRICLGKDLAYLQMKIVAAAILRRFDFKVVPG 415
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 291-463 1.04e-12

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: 69.87  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLvSVNRKVLEP 370
Cdd:cd20644   240 LTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGI-TVQRVPSSD 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 371 ITLSNgQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRtepGSENSFQFVssnasgiSFGHGKAACPGRWFAAT 450
Cdd:cd20644   319 LVLQN-YHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIR---GSGRNFKHL-------AFGFGMRQCLGRRLAEA 387

                         170
                  ....*....|...
gi 1148921820 451 ELKVMLARLLPDF 463
Cdd:cd20644   388 EMLLLLMHVLKNF 400
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 245-466 2.03e-12

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: 68.80  E-value: 2.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 245 VEQRLRDMRSGGADFQGQDDMIQWLIT----HAPPGSVSDVawhVSQHLVLNI--AAIHTTSGQLSGTLFALAARPHYMQ 318
Cdd:cd20654   200 LEEHRQKRSSSGKSKNDEDDDDVMMLSiledSQISGYDADT---VIKATCLELilGGSDTTAVTLTWALSLLLNNPHVLK 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 319 PLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPITLsNGQRLPVGTSIAFPADAINRDPEL 398
Cdd:cd20654   277 KAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYPPGPLLGPREATEDCTV-GGYHVPKGTRLLVNVWKIQRDPNV 355

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148921820 399 WERPADFDGFRFarLRTEPGSE---NSFQFvssnasgISFGHGKAACPGRWFAateLKVM---LARLLPDFDFA 466
Cdd:cd20654   356 WSDPLEFKPERF--LTTHKDIDvrgQNFEL-------IPFGSGRRSCPGVSFG---LQVMhltLARLLHGFDIK 417
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 298-482 3.02e-12

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: 68.24  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 298 TTSGQLSGTLFALAARPHYMQPLREEI-----EACILKHGALTKQCLHDMVKLDSFlrevqRLSPPgLVSVNRKVLEPIT 372
Cdd:cd20641   250 TTSNLLTWTMFLLSLHPDWQEKLREEVfrecgKDKIPDADTLSKLKLMNMVLMETL-----RLYGP-VINIARRASEDMK 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 373 LSNGQrLPVGTSIAFPADAINRDPELWERPAD-FDGFRFA----RLRTEPgsensfqfvssNASgISFGHGKAACPGRWF 447
Cdd:cd20641   324 LGGLE-IPKGTTIIIPIAKLHRDKEVWGSDADeFNPLRFAngvsRAATHP-----------NAL-LSFSLGPRACIGQNF 390

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1148921820 448 AATELKVMLARLLPDFDFALAeggDGPLHAFVDVL 482
Cdd:cd20641   391 AMIEAKTVLAMILQRFSFSLS---PEYVHAPADHL 422
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 298-493 3.10e-12

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: 68.05  E-value: 3.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 298 TTSGQLSGTLFALAARPHYMQPLREEIE----------ACILKHGAltkQCLHDMVKLDSFLREVQRLSPPGlvSVNRKV 367
Cdd:cd11051   200 TTSSTLCWAFYLLSKHPEVLAKVRAEHDevfgpdpsaaAELLREGP---ELLNQLPYTTAVIKETLRLFPPA--GTARRG 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 368 LE--PITLSNGQRLPV-GTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSE----NSFQFvssnasgisFGHGKA 440
Cdd:cd11051   275 PPgvGLTDRDGKEYPTdGCIVYVCHHAIHRDPEYWPRPDEFIPERW--LVDEGHELyppkSAWRP---------FERGPR 343

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 441 ACPGRWFAATELKVMLARLLPDFDFALA-------EGGDGPLHAFVDVLGAPDPTRQIRV 493
Cdd:cd11051   344 NCIGQELAMLELKIILAMTVRRFDFEKAydewdakGGYKGLKELFVTGQGTAHPVDGMPC 403
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 218-464 6.92e-12

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


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 67.11  E-value: 6.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 218 PLVRLFVRevGGVEECRQATERMLRPL----VEQRLRDMRSGGADFQGQDDMIQWLITHAPPGSVSD--VAWHVSQhlvL 291
Cdd:cd11074   167 PILRPFLR--GYLKICKEVKERRLQLFkdyfVDERKKLGSTKSTKNEGLKCAIDHILDAQKKGEINEdnVLYIVEN---I 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 292 NIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPI 371
Cdd:cd11074   242 NVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLRMAIPLLVPHMNLHDA 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 372 TLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSE---NSFQFvssnasgISFGHGKAACPGRWFA 448
Cdd:cd11074   322 KL-GGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERF--LEEESKVEangNDFRY-------LPFGVGRRSCPGIILA 391

                         250
                  ....*....|....*.
gi 1148921820 449 ATELKVMLARLLPDFD 464
Cdd:cd11074   392 LPILGITIGRLVQNFE 407
PLN02290 PLN02290
cytokinin trans-hydroxylase
 298-482 7.09e-12

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 67.53  E-value: 7.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 298 TTSGQLSGTLFALAARPHYMQPLREEI-EAC-----ILKHgaLTKQCLHDMVkldsfLREVQRLSPPGLVsVNRKVLEPI 371
Cdd:PLN02290  331 TTALLLTWTLMLLASNPTWQDKVRAEVaEVCggetpSVDH--LSKLTLLNMV-----INESLRLYPPATL-LPRMAFEDI 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 372 TLSnGQRLPVGTSIAFPADAINRDPELWERPA-DFDGFRFARLRTEPGSensfQFvssnasgISFGHGKAACPGRWFAAT 450
Cdd:PLN02290  403 KLG-DLHIPKGLSIWIPVLAIHHSEELWGKDAnEFNPDRFAGRPFAPGR----HF-------IPFAAGPRNCIGQAFAMM 470

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1148921820 451 ELKVMLARLLPDFDFALAeggDGPLHAFVDVL 482
Cdd:PLN02290  471 EAKIILAMLISKFSFTIS---DNYRHAPVVVL 499
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 291-479 7.62e-12

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: 67.20  E-value: 7.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLHDMVKL---DSFLREVQRLS---PPGLVsvn 364
Cdd:cd11026   234 LFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVI---GRNRTPSLEDRAKMpytDAVIHEVQRFGdivPLGVP--- 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 365 RKVLEPITLsNGQRLPVGTSIaFPA-DAINRDPELWERPADFDGFRFArlrTEPGsensfQFVSSNASgISFGHGKAACP 443
Cdd:cd11026   308 HAVTRDTKF-RGYTIPKGTTV-IPNlTSVLRDPKQWETPEEFNPGHFL---DEQG-----KFKKNEAF-MPFSAGKRVCL 376

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1148921820 444 GRWFAATELKVMLARLLPDFDFALAEGGDGPLHAFV 479
Cdd:cd11026   377 GEGLARMELFLFFTSLLQRFSLSSPVGPKDPDLTPR 412
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 241-460 1.38e-11

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: 65.78  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 241 LRPLVEQRLRDMRsggadfqgqDDMIQWLITHAPPGSVSDVAWHVSQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPL 320
Cdd:cd20629   159 VLPLIAERRRAPG---------DDLISRLLRAEVEGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERV 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 321 R---EEIEACIlkhgaltkqclhdmvkldsflREVQRLSPPgLVSVNRKVLEPITLSnGQRLPVGTSIAFPADAINRDPE 397
Cdd:cd20629   230 RrdrSLIPAAI---------------------EEGLRWEPP-VASVPRMALRDVELD-GVTIPAGSLLDLSVGSANRDED 286

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148921820 398 LWERPADFDGFRfarlrtepgsensfqfvsSNASGISFGHGKAACPGRWFAATELKVMLARLL 460
Cdd:cd20629   287 VYPDPDVFDIDR------------------KPKPHLVFGGGAHRCLGEHLARVELREALNALL 331
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 289-470 1.48e-11

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 66.37  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLN--IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRK 366
Cdd:PLN02687  301 LLLNlfTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRM 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 367 VLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtePGSENSFQFVSSNASG-ISFGHGKAACPGR 445
Cdd:PLN02687  381 AAEECEI-NGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFL-----PGGEHAGVDVKGSDFElIPFGAGRRICAGL 454

                         170       180
                  ....*....|....*....|....*
gi 1148921820 446 WFAATELKVMLARLLPDFDFALAEG 470
Cdd:PLN02687  455 SWGLRMVTLLTATLVHAFDWELADG 479
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 314-472 2.45e-11

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


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 65.43  E-value: 2.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 314 PHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPG-LVSVNRKVLEPITLSnGQRLPVGTSIAFPADAI 392
Cdd:cd11076   255 PDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGpLLSWARLAIHDVTVG-GHVVPAGTTAMVNMWAI 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 393 NRDPELWERPADFDGFRFarlrTEPGSENSFQFVSSNASGISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGGD 472
Cdd:cd11076   334 THDPHVWEDPLEFKPERF----VAAEGGADVSVLGSDLRLAPFGAGRRVCPGKALGLATVHLWVAQLLHEFEWLPDDAKP 409
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 234-472 4.70e-11

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: 64.51  E-value: 4.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 234 RQATERMLRPLVEQRlRDMRSGGADFQgqdDMIQWLIT-HAPPGSVSDVAWHVSQHLVLNIAAIHTTSGQLSGTLFALAA 312
Cdd:cd11043   164 RKRIRKELKKIIEER-RAELEKASPKG---DLLDVLLEeKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAE 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 313 RPHYMQPLREEIEAcILKH----GALTKQCLHDMVKLDSFLREVQRLSPPgLVSVNRKVLEPITLsNGQRLPVGTSIAFP 388
Cdd:cd11043   240 NPKVLQELLEEHEE-IAKRkeegEGLTWEDYKSMKYTWQVINETLRLAPI-VPGVFRKALQDVEY-KGYTIPKGWKVLWS 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 389 ADAINRDPELWERPADFDGFRFarLRTEPGSENSFqfvssnasgISFGHGKAACPGRWFAATELKVMLARLLPDFDFALA 468
Cdd:cd11043   317 ARATHLDPEYFPDPLKFNPWRW--EGKGKGVPYTF---------LPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVV 385


                  ....
gi 1148921820 469 EGGD 472
Cdd:cd11043   386 PDEK 389
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 298-462 5.30e-11

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: 64.71  E-value: 5.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 298 TTSGQLSGTLFALAARPHYMQPLREEIEAciLKHGALTKQCLHDMVKLDSFL----REVQRLSPPGLVsVNRKVLEPITL 373
Cdd:cd20679   259 TTASGLSWILYNLARHPEYQERCRQEVQE--LLKDREPEEIEWDDLAQLPFLtmciKESLRLHPPVTA-ISRCCTQDIVL 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 374 SNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarlrtEPgsENSFQfvSSNASGISFGHGKAACPGRWFAATELK 453
Cdd:cd20679   336 PDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRF-----DP--ENSQG--RSPLAFIPFSAGPRNCIGQTFAMAEMK 406

                         170
                  ....*....|....*
gi 1148921820 454 VMLA------RLLPD 462
Cdd:cd20679   407 VVLAltllrfRVLPD 421
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 211-464 5.65e-11

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: 64.56  E-value: 5.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 211 AYPAWLRPLV----RLFVREVGGVEECRQATermlrplVEQRLRDMRSG---GADFQGQddmiqwLITH---APPGSVSD 280
Cdd:cd20647   171 AIPKWLRPFIpkpwEEFCRSWDGLFKFSQIH-------VDNRLREIQKQmdrGEEVKGG------LLTYllvSKELTLEE 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 281 VAWHVSQHLvlnIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSP--P 358
Cdd:cd20647   238 IYANMTEML---LAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPvlP 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 359 GlvsvNRKVLEPITLSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARlrtepgsENSFQFVSsNASGISFGHG 438
Cdd:cd20647   315 G----NGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLR-------KDALDRVD-NFGSIPFGYG 382

                         250       260
                  ....*....|....*....|....*.
gi 1148921820 439 KAACPGRWFAATELKVMLARLLPDFD 464
Cdd:cd20647   383 IRSCIGRRIAELEIHLALIQLLQNFE 408
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 295-463 6.12e-11

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: 64.35  E-value: 6.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 295 AIHTTSGQLSGTLFALAARPHYMQPLREEI-EACILKHGALTKqclhdMVK----LDSFLREVQRLSPPGlVSVNRKVLE 369
Cdd:cd20643   246 GVDTTSMTLQWTLYELARNPNVQEMLRAEVlAARQEAQGDMVK-----MLKsvplLKAAIKETLRLHPVA-VSLQRYITE 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 370 PITLSNgQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEpgsENSFQfvssnasGISFGHGKAACPGRWFAA 449
Cdd:cd20643   320 DLVLQN-YHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERW--LSKD---ITHFR-------NLGFGFGPRQCLGRRIAE 386

                         170
                  ....*....|....
gi 1148921820 450 TELKVMLARLLPDF 463
Cdd:cd20643   387 TEMQLFLIHMLENF 400
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 231-463 7.16e-11

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


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 63.74  E-value: 7.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 231 EECRQATERM---LRPLVEQRLRDMRsggadfqgqDDMIQWLIT-HAPPGSVSD---VAWHVSqhlvLNIAAIHTTSGQL 303
Cdd:cd11031   160 EEAEAARQELrgyMAELVAARRAEPG---------DDLLSALVAaRDDDDRLSEeelVTLAVG----LLVAGHETTASQI 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 304 SGTLFALAARPHYMQPLREEIEAcilkhgaltkqclhdmvkLDSFLREVQRLSPPG-LVSVNRKVLEPITLSnGQRLPVG 382
Cdd:cd11031   227 GNGVLLLLRHPEQLARLRADPEL------------------VPAAVEELLRYIPLGaGGGFPRYATEDVELG-GVTIRAG 287

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 383 TSIAFPADAINRDPELWERPADFDgfrFARlrtepgsensfqfvsSNASGISFGHGKAACPGRWFAATELKVMLARLLPD 462
Cdd:cd11031   288 EAVLVSLNAANRDPEVFPDPDRLD---LDR---------------EPNPHLAFGHGPHHCLGAPLARLELQVALGALLRR 349


                  .
gi 1148921820 463 F 463
Cdd:cd11031   350 L 350
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 288-464 7.86e-11

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: 63.82  E-value: 7.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 288 HLVLNIAAIHTTSGqLSGTLFALAAR-----PHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPglVS 362
Cdd:cd11071   227 HNLLFMLGFNAFGG-FSALLPSLLARlglagEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPP--VP 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 363 -VNRKVLEPITLSN---------GQRLpVGtSIAFPadaiNRDPELWERPADFDGFRF-----ARLR---------TEPG 418
Cdd:cd11071   304 lQYGRARKDFVIEShdasykikkGELL-VG-YQPLA----TRDPKVFDNPDEFVPDRFmgeegKLLKhliwsngpeTEEP 377

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1148921820 419 SENSFQfvssnasgisfghgkaaCPGRWFAATELKVMLARLLPDFD 464
Cdd:cd11071   378 TPDNKQ-----------------CPGKDLVVLLARLFVAELFLRYD 406
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 209-460 1.33e-10

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: 63.09  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 209 LLAYPAWLRPLVRLFVR-----EVGGVEECRQATERMLRPLVEQRLRDMRSGGADFQGQDDMIQWLITHAPPG-SVSDVA 282
Cdd:cd11059   144 LASLAPWLRWLPRYLPLatsrlIIGIYFRAFDEIEEWALDLCARAESSLAESSDSESLTVLLLEKLKGLKKQGlDDLEIA 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 283 WHVSQHLVlniAAIHTTSGQLSGTLFALAARPHYMQPLREEIEAciLKHGALTKQCLHDMVK---LDSFLREVQRLSPPG 359
Cdd:cd11059   224 SEALDHIV---AGHDTTAVTLTYLIWELSRPPNLQEKLREELAG--LPGPFRGPPDLEDLDKlpyLNAVIRETLRLYPPI 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 360 LVSVNRKVLEPITLSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtEPGSENSFQfvsSNASGISFGHGK 439
Cdd:cd11059   299 PGSLPRVVPEGGATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWL----DPSGETARE---MKRAFWPFGSGS 371

                         250       260
                  ....*....|....*....|.
gi 1148921820 440 AACPGRWFAATELKVMLARLL 460
Cdd:cd11059   372 RMCIGMNLALMEMKLALAAIY 392
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 320-487 1.65e-10

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: 62.71  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 320 LREEIEACILKHGA----LTKQCLHDMVKLDSFLREVQRLSPPGLVSvnRKVLEPITLSNgQRLPVGTSIAFPADAINRD 395
Cdd:cd20635   247 VMEEISSVLGKAGKdkikISEDDLKKMPYIKRCVLEAIRLRSPGAIT--RKVVKPIKIKN-YTIPAGDMLMLSPYWAHRN 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 396 PELWERPADFDGFRFARLRTEpgsENSF--QFVSsnasgisFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEG--G 471
Cdd:cd20635   324 PKYFPDPELFKPERWKKADLE---KNVFleGFVA-------FGGGRYQCPGRWFALMEIQMFVAMFLYKYDFTLLDPvpK 393

                         170
                  ....*....|....*.
gi 1148921820 472 DGPLHafvdVLGAPDP 487
Cdd:cd20635   394 PSPLH----LVGTQQP 405
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 294-475 2.81e-10

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: 62.04  E-value: 2.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 294 AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPITL 373
Cdd:cd20652   245 AGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPLGIPHGCTEDAVL 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 374 sNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSENSFQFvssnasgISFGHGKAACPGRWFAATELK 453
Cdd:cd20652   325 -AGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERF--LDTDGKYLKPEAF-------IPFQTGKRMCLGDELARMILF 394

                         170       180
                  ....*....|....*....|..
gi 1148921820 454 VMLARLLPDFDFALAEGGDGPL 475
Cdd:cd20652   395 LFTARILRKFRIALPDGQPVDS 416
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 291-470 2.90e-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: 62.16  E-value: 2.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLHDMVKL---DSFLREVQRLSPPGLVSVNRKV 367
Cdd:cd20667   233 LFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVL---GASQLICYEDRKRLpytNAVIHEVQRLSNVVSVGAVRQC 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 368 LEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEpgsensfqFVSsNASGISFGHGKAACPGRWF 447
Cdd:cd20667   310 VTSTTM-HGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGN--------FVM-NEAFLPFSAGHRVCLGEQL 379

                         170       180
                  ....*....|....*....|...
gi 1148921820 448 AATELKVMLARLLPDFDFALAEG 470
Cdd:cd20667   380 ARMELFIFFTTLLRTFNFQLPEG 402
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 289-470 3.33e-10

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


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 62.05  E-value: 3.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNI--AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRK 366
Cdd:cd20657   232 LLLNLftAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRI 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 367 VLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtePGSENSFQFVSSNASGISFGHGKAACPGRW 446
Cdd:cd20657   312 ASEACEV-DGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFL-----PGRNAKVDVRGNDFELIPFGAGRRICAGTR 385

                         170       180
                  ....*....|....*....|....
gi 1148921820 447 FAATELKVMLARLLPDFDFALAEG 470
Cdd:cd20657   386 MGIRMVEYILATLVHSFDWKLPAG 409
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 291-464 3.63e-10

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


Pssm-ID: 410739 [Multi-domain]  Cd Length: 430  Bit Score: 61.98  E-value: 3.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPpgLVSVN-RKVLE 369
Cdd:cd20646   241 LLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYP--VVPGNaRVIVE 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 370 PITLSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPGSENSFqfvssnaSGISFGHGKAACPGRWFAA 449
Cdd:cd20646   319 KEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERW--LRDGGLKHHPF-------GSIPFGYGVRACVGRRIAE 389

                         170
                  ....*....|....*
gi 1148921820 450 TELKVMLARLLPDFD 464
Cdd:cd20646   390 LEMYLALSRLIKRFE 404
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 232-473 4.93e-10

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: 61.39  E-value: 4.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 232 ECRQATERMLRPLVEQRLRDMRSGGADFQGQDDMIQWLITHAPPGSVSDVawHVsQHLVLN--IAAIHTTSgqlSGTLFA 309
Cdd:cd11073   181 EHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLLLLDLELDSESELTRN--HI-KALLLDlfVAGTDTTS---STIEWA 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 310 LAA---RPHYMQPLREEIEACIlkhGalTKQCLH--DMVKLdSFLR----EVQRLSPPGLVSVNRKVLEPITLsNGQRLP 380
Cdd:cd11073   255 MAEllrNPEKMAKARAELDEVI---G--KDKIVEesDISKL-PYLQavvkETLRLHPPAPLLLPRKAEEDVEV-MGYTIP 327

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 381 VGTSIAFPADAINRDPELWERPADFDGFRFArlrtepGSE-----NSFQFvssnasgISFGHGKAACPGRWFAATELKVM 455
Cdd:cd11073   328 KGTQVLVNVWAIGRDPSVWEDPLEFKPERFL------GSEidfkgRDFEL-------IPFGSGRRICPGLPLAERMVHLV 394

                         250
                  ....*....|....*...
gi 1148921820 456 LARLLPDFDFALAEGGDG 473
Cdd:cd11073   395 LASLLHSFDWKLPDGMKP 412
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 232-461 5.46e-10

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: 60.95  E-value: 5.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 232 ECRQATERMLRPLVEQRLRDMRsggadfqgqDDMIQWLITHAPPG-SVSD---VAwhvsqhLVLNI--AAIHTTSGQLSG 305
Cdd:cd11080   151 RCAEQLSQYLLPVIEERRVNPG---------SDLISILCTAEYEGeALSDediKA------LILNVllAATEPADKTLAL 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 306 TLFALAARPHYMQPLREeieacilkhgaltkqclhDMVKLDSFLREVQRLSPPglVSVNRKVLEPITLSNGQRLPVGTSI 385
Cdd:cd11080   216 MIYHLLNNPEQLAAVRA------------------DRSLVPRAIAETLRYHPP--VQLIPRQASQDVVVSGMEIKKGTTV 275

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1148921820 386 AFPADAINRDPELWERPADFDGFrfarlRTEPGSENSFqfvSSNASGISFGHGKAACPGRWFAATELKVMLARLLP 461
Cdd:cd11080   276 FCLIGAANRDPAAFEDPDTFNIH-----REDLGIRSAF---SGAADHLAFGSGRHFCVGAALAKREIEIVANQVLD 343
PLN02936 PLN02936
epsilon-ring hydroxylase
 289-472 5.49e-10

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 61.35  E-value: 5.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEAcILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVL 368
Cdd:PLN02936  284 LSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDR-VLQGRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQV 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 369 EPItLSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENS-FQFvssnasgISFGHGKAACPGRWF 447
Cdd:PLN02936  363 EDV-LPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETNTdFRY-------IPFSGGPRKCVGDQF 434

                         170       180
                  ....*....|....*....|....*
gi 1148921820 448 AATELKVMLARLLPDFDFALAEGGD 472
Cdd:PLN02936  435 ALLEAIVALAVLLQRLDLELVPDQD 459
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 284-465 5.51e-10

cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2 (in humans), catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. It is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. Deficiency of this CYP is involved in ~95% of cases of human congenital adrenal hyperplasia, a disorder of adrenal steroidogenesis. There are two CYP21 genes in the human genome, CYP21A1 (a pseudogene) and CYP21A2 (the functional gene). Deficiencies in steroid 21-hydroxylase activity lead to a type of congenital adrenal hyperplasia, which has three clinical forms: a severe form with concurrent defects in both cortisol and aldosterone biosynthesis; a form with adequate aldosterone biosynthesis; and a mild, non-classic form that can be asymptomatic or associated with signs of postpubertal androgen excess without cortisol deficiency. CYP21A2 is also the major autoantigen in autoimmune Addison disease. Cyp21 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410767 [Multi-domain]  Cd Length: 424  Bit Score: 61.28  E-value: 5.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 284 HVSQHLV-LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEaCILKHGALTKqcLHDMVKLdSFLR----EVQRLSPP 358
Cdd:cd20674   226 HVHMAVVdLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELD-RVLGPGASPS--YKDRARL-PLLNatiaEVLRLRPV 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 359 GLVSVNRKVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtEPGSensfqfvsSNASGISFGHG 438
Cdd:cd20674   302 VPLALPHRTTRDSSIA-GYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFL----EPGA--------ANRALLPFGCG 368

                         170       180
                  ....*....|....*....|....*..
gi 1148921820 439 KAACPGRWFAATELKVMLARLLPDFDF 465
Cdd:cd20674   369 ARVCLGEPLARLELFVFLARLLQAFTL 395
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 307-492 6.13e-10

cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also called 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase (EC 1.14.18.8) or sterol 12-alpha-hydroxylase. It is involved in the classic (or neutral) pathway of cholesterol catabolism and bile acid synthesis, and is responsible for sterol 12alpha-hydroxylation, which directs the synthesis to cholic acid (CA). It converts 7-alpha-hydroxy-4-cholesten-3-one into 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one, but also displays broad substrate specificity including other 7-alpha-hydroxylated C27 steroids. CYP8B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 61.23  E-value: 6.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 307 LFALAARPHYMQPLREEIEACILKHG----------ALTKQCLHDMVKLDSFLREVQRL-SPPGLVsvnRKVLEPITL-- 373
Cdd:cd20633   248 LLYLLKHPEAMKAVREEVEQVLKETGqevkpggpliNLTRDMLLKTPVLDSAVEETLRLtAAPVLI---RAVVQDMTLkm 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 374 SNGQR--LPVGTSIA-FPADAINRDPELWERPADFDGFRFarLRTEPGSENSF--QFVSSNASGISFGHGKAACPGRWFA 448
Cdd:cd20633   325 ANGREyaLRKGDRLAlFPYLAVQMDPEIHPEPHTFKYDRF--LNPDGGKKKDFykNGKKLKYYNMPWGAGVSICPGRFFA 402

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1148921820 449 ATELKVMLARLLPDFDFALAEGGDGPLHAFVD--VLGAPDPTRQIR 492
Cdd:cd20633   403 VNEMKQFVFLMLTYFDLELVNPDEEIPSIDPSrwGFGTMQPTHDIQ 448
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 291-464 9.94e-10

cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; Cytochrome P450 24A1 (CYP24A1, EC 1.14.15.16) is also called 1,25-dihydroxyvitamin D(3) 24-hydroxylase (24-OHase), vitamin D(3) 24-hydroxylase, or cytochrome P450-CC24. It catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3) or 1,25(OH)2D3). CYP24A1 regulates vitamin D activity through its hydroxylation of calcitriol, the physiologically active vitamin D hormone, which controls gene-expression and signal-transduction processes associated with calcium homeostasis, cellular growth, and the maintenance of heart, muscle, immune, and skin function. CYP24A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 60.59  E-value: 9.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPglVSVNRKVLEP 370
Cdd:cd20645   234 LQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPS--VPFTSRTLDK 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 371 ITLSNGQRLPVGTSIAFPADAINRDPELWErpaDFDGFRFARLRTEPGSENSFQFVssnasgiSFGHGKAACPGRWFAAT 450
Cdd:cd20645   312 DTVLGDYLLPKGTVLMINSQALGSSEEYFE---DGRQFKPERWLQEKHSINPFAHV-------PFGIGKRMCIGRRLAEL 381

                         170
                  ....*....|....
gi 1148921820 451 ELKVMLARLLPDFD 464
Cdd:cd20645   382 QLQLALCWIIQKYQ 395
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 239-494 1.48e-09

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: 59.76  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 239 RMLRPLVEQRLR----DMRSGGADfqgqDDMIQWLIT-HAPPGSVSDVAWHVSQHLVLNIAAIHTTSGQLSGTLFALAAR 313
Cdd:cd20614   163 RRARAWIDARLSqlvaTARANGAR----TGLVAALIRaRDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEH 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 314 PHYMQPLREEIEAciLKHGALTKQCLHDMVKLDSFLREVQRLSPPgLVSVNRKVLEPITLSnGQRLPVGTSIAFPADAIN 393
Cdd:cd20614   239 PAVWDALCDEAAA--AGDVPRTPAELRRFPLAEALFRETLRLHPP-VPFVFRRVLEEIELG-GRRIPAGTHLGIPLLLFS 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 394 RDPELWERPADFDGFRFARLRTEPGSENSFQfvssnasgisFGHGKAACPGR---WFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd20614   315 RDPELYPDPDRFRPERWLGRDRAPNPVELLQ----------FGGGPHFCLGYhvaCVELVQFIVALARELGAAGIRPLLV 384

                         250       260
                  ....*....|....*....|....
gi 1148921820 471 GDGPLHAFVDVLgapDPTRQIRVR 494
Cdd:cd20614   385 GVLPGRRYFPTL---HPSNKTRVA 405
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 285-465 1.76e-09

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: 59.81  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 285 VSQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLHD---MVKLDSFLREVQRLSPPGLV 361
Cdd:cd20662   227 ICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVI---GQKRQPSLADresMPYTNAVIHEVQRMGNIIPL 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 362 SVNRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtepgsENSfQFVSSNASgISFGHGKAA 441
Cdd:cd20662   304 NVPREVAVDTKL-AGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFL--------ENG-QFKKREAF-LPFSMGKRA 372

                         170       180
                  ....*....|....*....|....
gi 1148921820 442 CPGRWFAATELKVMLARLLPDFDF 465
Cdd:cd20662   373 CLGEQLARSELFIFFTSLLQKFTF 396
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 291-485 3.26e-09

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: 59.00  E-value: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPpgLVSVNRKVLEP 370
Cdd:cd20648   242 LLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYP--VIPGNARVIPD 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 371 ITLSNGQRL-PVGTSIAFPADAINRDPELWERPadfDGFRFARLRTEPGSENSFqfvssnASgISFGHGKAACPGRWFAA 449
Cdd:cd20648   320 RDIQVGEYIiPKKTLITLCHYATSRDENQFPDP---NSFRPERWLGKGDTHHPY------AS-LPFGFGKRSCIGRRIAE 389

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1148921820 450 TELKVMLARLLPDFDfALAEGGDGPLHAFVDVLGAP 485
Cdd:cd20648   390 LEVYLALARILTHFE-VRPEPGGSPVKPMTRTLLVP 424
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 240-468 3.54e-09

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


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 58.83  E-value: 3.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 240 MLRPLVEQRLRDMRSGGADfqgQDDMIQWLI--------THAPPG---SVSDVawhVSQHLVLNIAAIHTTSGQLSGTLF 308
Cdd:cd20642   186 SLRGIINKREKAMKAGEAT---NDDLLGILLesnhkeikEQGNKNggmSTEDV---IEECKLFYFAGQETTSVLLVWTMV 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 309 ALAARPHYMQPLREEIEACILKHG----ALTKQCLHDMVkldsfLREVQRLSPPGlVSVNRKVLEPITLSNgQRLPVGTS 384
Cdd:cd20642   260 LLSQHPDWQERAREEVLQVFGNNKpdfeGLNHLKVVTMI-----LYEVLRLYPPV-IQLTRAIHKDTKLGD-LTLPAGVQ 332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 385 IAFPADAINRDPELW-ERPADFDGFRFArlrtepgsENSFQFVSSNASGISFGHGKAACPGRWFAATELKVMLARLLPDF 463
Cdd:cd20642   333 VSLPILLVHRDPELWgDDAKEFNPERFA--------EGISKATKGQVSYFPFGWGPRICIGQNFALLEAKMALALILQRF 404


                  ....*
gi 1148921820 464 DFALA 468
Cdd:cd20642   405 SFELS 409
PLN02966 PLN02966
cytochrome P450 83A1
 230-470 3.80e-09

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 58.99  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 230 VEECRQATERMLRPLVEQRLrDMRSGGADFQGQDDMIQWLITHAPPGSVSDVAWHVSQHLVLNIAAIHTTSGQLSGTLFA 309
Cdd:PLN02966  237 MKECFERQDTYIQEVVNETL-DPKRVKPETESMIDLLMEIYKEQPFASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTY 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 310 LAARPHYMQPLREEIEACILKHGA--LTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPITLSnGQRLPVGTSIAF 387
Cdd:PLN02966  316 LMKYPQVLKKAQAEVREYMKEKGStfVTEDDVKNLPYFRALVKETLRIEPVIPLLIPRACIQDTKIA-GYDIPAGTTVNV 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 388 PADAINRDPELW-ERPADFDGFRFArlrtepgsENSFQFVSSNASGISFGHGKAACPGRWFAATELKVMLARLLPDFDFA 466
Cdd:PLN02966  395 NAWAVSRDEKEWgPNPDEFRPERFL--------EKEVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFK 466


                  ....
gi 1148921820 467 LAEG 470
Cdd:PLN02966  467 LPNG 470
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 214-470 6.41e-09

cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of bacterial cytochrome P450s from multiple families, including Mycobacterium smegmatis CYP164A2, Streptomyces sp. CYP245A1, Bacillus subtilis CYP107H1, Micromonospora echinospora P450 oxidase Calo2, and putative P450s such as Xylella fastidiosa CYP133 and Mycobacterium tuberculosis CYP140. CYP107H1, also called cytochrome P450(BioI), catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. CYP245A1, also called cytochrome P450 StaP, catalyzes the intramolecular C-C bond formation and oxidative decarboxylation of chromopyrrolic acid (CPA) to form the indolocarbazole core, a key step in staurosporine biosynthesis. CalO2 is involved in calicheamicin biosynthesis. The CYP164-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 57.56  E-value: 6.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 214 AWLRPLVRLF--VREVGGVEECRQATERM---LRPLVEQRLRdmrsggadfQGQDDMIQWLITHAPPGSVSDVAWHVSQH 288
Cdd:cd20625   136 GWSAALARALdpGPLLEELARANAAAAELaayFRDLIARRRA---------DPGDDLISALVAAEEDGDRLSEDELVANC 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREeieacilkHGALTkqclhdmvklDSFLREVQRLSPPgLVSVNRKVL 368
Cdd:cd20625   207 ILLLVAGHETTVNLIGNGLLALLRHPEQLALLRA--------DPELI----------PAAVEELLRYDSP-VQLTARVAL 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 369 EPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDgfrFARlrtepgsensfqfvsSNASGISFGHGKAACPGRWFA 448
Cdd:cd20625   268 EDVEIG-GQTIPAGDRVLLLLGAANRDPAVFPDPDRFD---ITR---------------APNRHLAFGAGIHFCLGAPLA 328

                         250       260
                  ....*....|....*....|...
gi 1148921820 449 ATELKVMLARLLPDF-DFALAEG 470
Cdd:cd20625   329 RLEAEIALRALLRRFpDLRLLAG 351
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 230-483 6.84e-09

P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Pseudomonas putida P450cam and Cyp101 proteins from Novosphingobium aromaticivorans such as CYP101C1 and CYP101D2. P450cam catalyzes the hydroxylation of camphor in a process that involves two electron transfers from the iron-sulfur protein, putidaredoxin. CYP101D2 is capable of oxidizing camphor while CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives such as alpha- and beta-ionone and beta-damascone. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 57.60  E-value: 6.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 230 VEECRQATERMLRPLVEQRlrdMRSGGADF-----QGQDDMIQWlithaPPGSVSDVAwhvsqHLVLnIAAIHTTSGQLS 304
Cdd:cd11035   146 RAAAAQAVLDYLTPLIAER---RANPGDDLisailNAEIDGRPL-----TDDELLGLC-----FLLF-LAGLDTVASALG 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 305 GTLFALAARPHYMQPLREEIEacilkhgaltkqclhdmvKLDSFLREVQRLSPPglVSVNRKVLEPITLsNGQRLPVGTS 384
Cdd:cd11035   212 FIFRHLARHPEDRRRLREDPE------------------LIPAAVEELLRRYPL--VNVARIVTRDVEF-HGVQLKAGDM 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 385 IAFPADAINRDPELWERPADFDgfrfarlrtepgsensfqFVSSNASGISFGHGKAACPGRWFAATELKVMLA---RLLP 461
Cdd:cd11035   271 VLLPLALANRDPREFPDPDTVD------------------FDRKPNRHLAFGAGPHRCLGSHLARLELRIALEewlKRIP 332

                         250       260
                  ....*....|....*....|..
gi 1148921820 462 dfDFALAEGGDgPLHAFVDVLG 483
Cdd:cd11035   333 --DFRLAPGAQ-PTYHGGSVMG 351
PLN02738 PLN02738
carotene beta-ring hydroxylase
 289-470 7.55e-09

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 58.00  E-value: 7.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEAcILKHGALTkqcLHDMVKLDSFLR---EVQRL--SPPGLVsv 363
Cdd:PLN02738  397 MTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDS-VLGDRFPT---IEDMKKLKYTTRvinESLRLypQPPVLI-- 470

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 364 nRKVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENSfqfvssNASGISFGHGKAACP 443
Cdd:PLN02738  471 -RRSLENDMLG-GYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWPLDGPNPNETNQ------NFSYLPFGGGPRKCV 542

                         170       180
                  ....*....|....*....|....*..
gi 1148921820 444 GRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:PLN02738  543 GDMFASFENVVATAMLVRRFDFQLAPG 569
PLN02500 PLN02500
cytochrome P450 90B1
 245-495 8.21e-09

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 57.95  E-value: 8.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 245 VEQRLRDMRSGGADFQgQDDMIQWLITHappgsvSDVAWHVSQHLVLNI--AAIHTTSGQLSGTLFALAARPHYMQPLRE 322
Cdd:PLN02500  246 MEERIEKLKEEDESVE-EDDLLGWVLKH------SNLSTEQILDLILSLlfAGHETSSVAIALAIFFLQGCPKAVQELRE 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 323 E---IEACILKHGA--LTKQCLHDMVKLDSFLREVQRLsppGLVS--VNRKVLEPITLsNGQRLPVGTSIAFPADAINRD 395
Cdd:PLN02500  319 EhleIARAKKQSGEseLNWEDYKKMEFTQCVINETLRL---GNVVrfLHRKALKDVRY-KGYDIPSGWKVLPVIAAVHLD 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 396 PELWERPADFDGFRFARLRTEPGSENSFQFVSSNAsgISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGGDGPL 475
Cdd:PLN02500  395 SSLYDQPQLFNPWRWQQNNNRGGSSGSSSATTNNF--MPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELAEADQAFA 472

                         250       260
                  ....*....|....*....|.
gi 1148921820 476 HAFVDV-LGAPdptrqIRVRR 495
Cdd:PLN02500  473 FPFVDFpKGLP-----IRVRR 488
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 306-470 8.72e-09

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: 57.69  E-value: 8.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 306 TLFALAARPHYMQPLREEIEACILKHG---------ALTKQCLHDMVKLDSFLREVQRLSPpglVSVN-RKVLEPITLSN 375
Cdd:cd20632   238 AMYYLLRHPEALAAVRDEIDHVLQSTGqelgpdfdiHLTREQLDSLVYLESAINESLRLSS---ASMNiRVVQEDFTLKL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 376 GQ----RLPVGTSIAFPADAINRDPELWERPadfDGFRFARLrTEPGSENSFQFvssnASG-------ISFGHGKAACPG 444
Cdd:cd20632   315 ESdgsvNLRKGDIVALYPQSLHMDPEIYEDP---EVFKFDRF-VEDGKKKTTFY----KRGqklkyylMPFGSGSSKCPG 386

                         170       180
                  ....*....|....*....|....*.
gi 1148921820 445 RWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd20632   387 RFFAVNEIKQFLSLLLLYFDLELLEE 412
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 214-472 9.79e-09

cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-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: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 57.16  E-value: 9.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 214 AWLRPLVRLFVREVGGVEECRQATERM---LRPLVEQRLRdmrsggadfQGQDDMIQWLIthappgSVSDVAWHVSQH-- 288
Cdd:cd11029   148 DRFRRWSDALVDTDPPPEEAAAALRELvdyLAELVARKRA---------EPGDDLLSALV------AARDEGDRLSEEel 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 ---LVLNIAAIH-TTSGQLSGTLFALAARPHYMQPLREeieacilkhgaltkqclhDMVKLDSFLREVQRLSPPGLVSVN 364
Cdd:cd11029   213 vstVFLLLVAGHeTTVNLIGNGVLALLTHPDQLALLRA------------------DPELWPAAVEELLRYDGPVALATL 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 365 RKVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRfarlrtepgsensfqfvsSNASGISFGHGKAACPG 444
Cdd:cd11029   275 RFATEDVEVG-GVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR------------------DANGHLAFGHGIHYCLG 335

                         250       260
                  ....*....|....*....|....*....
gi 1148921820 445 RWFAATELKVMLARLLPDF-DFALAEGGD 472
Cdd:cd11029   336 APLARLEAEIALGALLTRFpDLRLAVPPD 364
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 314-470 9.91e-09

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 57.53  E-value: 9.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 314 PHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPITLsNGQRLPVGTSIAFPADAIN 393
Cdd:PLN03112  327 PRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTI-NGYYIPAKTRVFINTHGLG 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 394 RDPELWERPADFDGFRF---ARLRTEPGSENSFQFvssnasgISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:PLN03112  406 RNTKIWDDVEEFRPERHwpaEGSRVEISHGPDFKI-------LPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDG 478
PLN02183 PLN02183
ferulate 5-hydroxylase
 349-493 2.22e-08

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 56.40  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 349 LREVQRLSPPGLVSVNRKVLEpiTLSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarlrTEPGSENsfqFVSS 428
Cdd:PLN02183  370 LKETLRLHPPIPLLLHETAED--AEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRF----LKPGVPD---FKGS 440

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148921820 429 NASGISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGGDGPLHAFVDVLG--APDPTRQIRV 493
Cdd:PLN02183  441 HFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWELPDGMKPSELDMNDVFGltAPRATRLVAV 507
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 230-460 2.24e-08

cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains bacterial cytochrome P450s, including those belonging to families 105 (CYP105) and 165 (CYP165). Also included in this group are fungal family 55 proteins (CYP55). CYP105s are predominantly found in bacteria belonging to the phylum Actinobacteria and the order Actinomycetales, and are associated with a wide variety of pathways and processes, from steroid biotransformation to production of macrolide metabolites. CYP105A1 catalyzes two sequential hydroxylations of vitamin D3 with differing specificity and cytochrome P450-SOY (also known as CYP105D1) has been shown to be capable of both oxidation and dealkylation reactions. CYP105D6 and CYP105P1, from the filipin biosynthetic pathway, perform highly regio- and stereospecific hydroxylations. Other members of this group include, but are not limited to: CYP165D3 (also called OxyE) from the teicoplanin biosynthetic gene cluster of Actinoplanes teichomyceticus, which is responsible for the phenolic coupling of the aromatic side chains of the first and third peptide residues in the teicoplanin peptide; Micromonospora griseorubida cytochrome P450 MycCI that catalyzes hydroxylation at the C21 methyl group of mycinamicin VIII, the earliest macrolide form in the postpolyketide synthase tailoring pathway; and Fusarium oxysporum CYP55A1 (also called nitric oxide reductase cytochrome P450nor) that catalyzes an unusual reaction, the direct electron transfer from NAD(P)H to bound heme. The CYP105-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: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 55.99  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 230 VEECRQATERMLRPLVEQRLRDmrsggadfqGQDDMIQWLIT-HAPPGSVSDvaWHVSQHLVLNIAAIH-TTSGQLSGTL 307
Cdd:cd11030   164 AAAAGAELRAYLDELVARKRRE---------PGDDLLSRLVAeHGAPGELTD--EELVGIAVLLLVAGHeTTANMIALGT 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 308 FALAARPHYMQPLREEIEacilkhgaltkqclhdmvKLDSFLREVQRLSPPGLVSVNRKVLEPITLSnGQRLPVGTSIAF 387
Cdd:cd11030   233 LALLEHPEQLAALRADPS------------------LVPGAVEELLRYLSIVQDGLPRVATEDVEIG-GVTIRAGEGVIV 293

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1148921820 388 PADAINRDPELWERPADFDgfrFARlrtepgsensfqfvsSNASGISFGHGKAACPGRWFAATELKVMLARLL 460
Cdd:cd11030   294 SLPAANRDPAVFPDPDRLD---ITR---------------PARRHLAFGHGVHQCLGQNLARLELEIALPTLF 348
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 289-444 2.47e-08

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


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 56.07  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlKHGALTKQclHDMVKLdSFLR----EVQRLSPPGLVSVN 364
Cdd:cd20653   233 LVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQV-GQDRLIEE--SDLPKL-PYLQniisETLRLYPAAPLLVP 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 365 RKVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarlrtEPGSENSFQFvssnasgISFGHGKAACPG 444
Cdd:cd20653   309 HESSEDCKIG-GYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF-----EGEEREGYKL-------IPFGLGRRACPG 375
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 180-477 3.02e-08

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: 55.42  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 180 FVGLPLSRNEEWIDAAVNVTqhsiagafKLLAYPAWLRPLVRLFVREVGGVEECRQatermlrplveqrlrdmrsggadf 259
Cdd:cd11034   119 LLGLPDEDGERLRDWVHAIL--------HDEDPEEGAAAFAELFGHLRDLIAERRA------------------------ 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 260 QGQDDMIQWLITHAPPG-SVSDVawHVSQHLVLNI-AAIHTTSGQLSGTLFALAarphymqplreeieacilKHGALTKQ 337
Cdd:cd11034   167 NPRDDLISRLIEGEIDGkPLSDG--EVIGFLTLLLlGGTDTTSSALSGALLWLA------------------QHPEDRRR 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 338 CLHDMVKLDSFLREVQRLSPPGLvSVNRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRtep 417
Cdd:cd11034   227 LIADPSLIPNAVEEFLRFYSPVA-GLARTVTQEVEV-GGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRTPNRH--- 301

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1148921820 418 gsensfqfvssnasgISFGHGKAACPGRWFAATELKVMLARLLPDF-DFALAEGGDGPLHA 477
Cdd:cd11034   302 ---------------LAFGSGVHRCLGSHLARVEARVALTEVLKRIpDFELDPGATCEFLD 347
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 234-469 4.20e-08

cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The cytochrome P450 152 (CYP152) family enzymes act as peroxygenases, converting fatty acids through oxidative decarboxylation, yielding terminal alkenes, and via alpha- and beta-hydroxylation to yield hydroxy-fatty acids. Included in this family are Bacillus subtilis CYP152A1, also called cytochrome P450BsBeta, that catalyzes the alpha- and beta-hydroxylation of long-chain fatty acids such as myristic acid in the presence of hydrogen peroxide, and Sphingomonas paucimobilis CYP152B1, also called cytochrome P450(SPalpha), that hydroxylates fatty acids with high alpha-regioselectivity. The CYP152 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 55.23  E-value: 4.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 234 RQATERMLRPLVeqrlRDMRSGGAdfqgqddmiqwlitHAPPGS-VSDVAWHVS---QHLVLNIAAI-------HTT--S 300
Cdd:cd11067   176 RRRAERWAAELI----EDVRAGRL--------------APPEGTpLAAIAHHRDpdgELLPERVAAVellnllrPTVavA 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 301 GQLSGTLFALAARPHYMQPLREEieacilkhgaltkqclhDMVKLDSFLREVQRLSP--PGLVSVNRKVLEpitlSNGQR 378
Cdd:cd11067   238 RFVTFAALALHEHPEWRERLRSG-----------------DEDYAEAFVQEVRRFYPffPFVGARARRDFE----WQGYR 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 379 LPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPgsensFQFVSSNASGISFGHgkaACPGRWFAATELKVMLAR 458
Cdd:cd11067   297 FPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGDP-----FDFIPQGGGDHATGH---RCPGEWITIALMKEALRL 368

                         250
                  ....*....|.
gi 1148921820 459 LLPDFDFALAE 469
Cdd:cd11067   369 LARRDYYDVPP 379
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 289-470 5.08e-08

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 55.24  E-value: 5.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLN--IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRK 366
Cdd:PLN00110  293 LLLNlfTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNLPRV 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 367 VLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSE--NSFQFvssnasgISFGHGKAACPG 444
Cdd:PLN00110  373 STQACEV-NGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIDPrgNDFEL-------IPFGAGRRICAG 444

                         170       180
                  ....*....|....*....|....*.
gi 1148921820 445 RWFAATELKVMLARLLPDFDFALAEG 470
Cdd:PLN00110  445 TRMGIVLVEYILGTLVHSFDWKLPDG 470
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 310-469 5.92e-08

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: 54.76  E-value: 5.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 310 LAARPHYMQPLREEIEACILKHGALTKQC-------LHDMVKLDSFLREVQRLSPPGLVSvnRKVLEPIT--LSNGQR-- 378
Cdd:cd20634   248 LLKHPEAMAAVRGEIQRIKHQRGQPVSQTltinqelLDNTPVFDSVLSETLRLTAAPFIT--REVLQDMKlrLADGQEyn 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 379 LPVGTS-IAFPADAINRDPELWERPadfDGFRFARLRTEPGSENSfQFVSSNAS----GISFGHGKAACPGRWFAATELK 453
Cdd:cd20634   326 LRRGDRlCLFPFLSPQMDPEIHQEP---EVFKYDRFLNADGTEKK-DFYKNGKRlkyyNMPWGAGDNVCIGRHFAVNSIK 401

                         170
                  ....*....|....*.
gi 1148921820 454 VMLARLLPDFDFALAE 469
Cdd:cd20634   402 QFVFLILTHFDVELKD 417
PLN02971 PLN02971
tryptophan N-hydroxylase
 291-469 9.02e-08

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 54.66  E-value: 9.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEP 370
Cdd:PLN02971  335 LVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSD 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 371 ITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPG-SENSFQFvssnasgISFGHGKAACPGRWFAA 449
Cdd:PLN02971  415 TTVA-GYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTlTENDLRF-------ISFSTGKRGCAAPALGT 486

                         170       180
                  ....*....|....*....|
gi 1148921820 450 TELKVMLARLLPDFDFALAE 469
Cdd:PLN02971  487 AITTMMLARLLQGFKWKLAG 506
PLN02655 PLN02655
ent-kaurene oxidase
 293-470 9.37e-08

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 54.36  E-value: 9.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 293 IAAIHTTSGQLSGTLFALAARPHYMQPLREEI-EACILKhgALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPI 371
Cdd:PLN02655  272 IEAADTTLVTTEWAMYELAKNPDKQERLYREIrEVCGDE--RVTEEDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDT 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 372 TLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEpgsensfqfVSSNASGISFGHGKAACPGRWFAATE 451
Cdd:PLN02655  350 TLG-GYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYE---------SADMYKTMAFGAGKRVCAGSLQAMLI 419

                         170
                  ....*....|....*....
gi 1148921820 452 LKVMLARLLPDFDFALAEG 470
Cdd:PLN02655  420 ACMAIARLVQEFEWRLREG 438
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 294-474 1.08e-07

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


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 54.25  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 294 AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLHD---MVKLDSFLREVQRLSPPGLVSVNRKVLep 370
Cdd:cd20673   243 AGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNI---GFSRTPTLSDrnhLPLLEATIREVLRIRPVAPLLIPHVAL-- 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 371 ITLSNGQ-RLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtepgSENSFQFVSSNASGISFGHGKAACPGRWFAA 449
Cdd:cd20673   318 QDSSIGEfTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFL-------DPTGSQLISPSLSYLPFGAGPRVCLGEALAR 390

                         170       180
                  ....*....|....*....|....*
gi 1148921820 450 TELKVMLARLLPDFDFALAEGGDGP 474
Cdd:cd20673   391 QELFLFMAWLLQRFDLEVPDGGQLP 415
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 294-472 2.29e-07

cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is composed of cytochrome P450 monooxygenases that are part of gene clusters involved in the biosynthesis of various compounds such as mycotoxins and alkaloids, including Aspergillus fumigatus gliotoxin biosynthesis protein (GliC), Penicillium rubens roquefortine/meleagrin synthesis protein R (RoqR), Aspergillus oryzae aspirochlorine biosynthesis protein C (AclC), Aspergillus terreus bimodular acetylaranotin synthesis protein ataTC, Kluyveromyces lactis pulcherrimin biosynthesis cluster protein 2 (PUL2), and Aspergillus nidulans aspyridones biosynthesis protein B (ApdB). The GliC-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 53.06  E-value: 2.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 294 AAIHTTSGQLSGTLFALAARPHYMQPLREEIEacilkhgALTKQCLHDMVK--------LDSFLREVQRLSPPGLVSVNR 365
Cdd:cd20615   226 ANLDVTTGVLSWNLVFLAANPAVQEKLREEIS-------AAREQSGYPMEDyilstdtlLAYCVLESLRLRPLLAFSVPE 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 366 KVLEPITLSnGQRLPVGTSIAFPADAINRDPELWErpADFDGFRFARLRTEPGSENSFQFVssnasgiSFGHGKAACPGR 445
Cdd:cd20615   299 SSPTDKIIG-GYRIPANTPVVVDTYALNINNPFWG--PDGEAYRPERFLGISPTDLRYNFW-------RFGFGPRKCLGQ 368

                         170       180
                  ....*....|....*....|....*..
gi 1148921820 446 WFAATELKVMLARLLPDFDFALAEGGD 472
Cdd:cd20615   369 HVADVILKALLAHLLEQYELKLPDQGE 395
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
 211-461 2.53e-07

AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis proteins including anthracycline biosynthesis proteins DnrQ and AknT, and macrolide antibiotic biosynthesis proteins TylM3 and DesVIII. Streptomyces peucetius DnrQ is involved in the biosynthesis of carminomycin and daunorubicin (daunomycin) while Streptomyces galilaeus AknT functions in the biosynthesis of aclacinomycin A. Streptomyces fradiae TylM3 is involved in the biosynthesis of tylosin derived from the polyketide lactone tylactone, and Streptomyces venezuelae functions in the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin. These proteins are required for the glycosylation of specific substrates during the biosynthesis of specific anthracyclines and macrolide antibiotics. Although members of this family belong to the large cytochrome P450 (P450, CYP) superfamily and show significant similarity to cytochrome P450s, they lack heme-binding sites and are not functional cytochromes.


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 52.49  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 211 AYPAWLRPLVRLFVREVGGVEECRQAT-----ERMLRPLVEQRLRDMRSGG-ADFQGQDD--MIQWLITHAPPGSVSDVA 282
Cdd:cd11036    97 LVADFLRPLPVRVAAALLGLPADDRARfarlfAALAPALDSLLCARALLAArALLRAALAelLALTRSAAADALALSAPG 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 283 WHVSQHLVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACilkhgaltkqclhdmvklDSFLREVQRLSPPglVS 362
Cdd:cd11036   177 DLVANAILLAVQGAEAAAGLVGNAVLALLRRPAQWARLRPDPELA------------------AAAVAETLRYDPP--VR 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 363 VNRKVLEPITLSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLrtepgsensfqfvssnasGISFGHGKAAC 442
Cdd:cd11036   237 LERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGRPTAR------------------SAHFGLGRHAC 298

                         250       260
                  ....*....|....*....|...
gi 1148921820 443 PG----RWFAATELKVMLARLLP 461
Cdd:cd11036   299 LGaalaRAAAAAALRALAARFPG 321
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 82-469 3.00e-07

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: 52.64  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820  82 PALLDEIRAVSEKKLNFRREMYDRFVGRYTAFASNDSAMVVAIKNKLTP-----GIDRLLPTMDDEAQFAVR--TTLASC 154
Cdd:cd11062    16 PDFYDEIYAGGSRRRKDPPYFYGAFGAPGSTFSTVDHDLHRLRRKALSPffskrSILRLEPLIQEKVDKLVSrlREAKGT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 155 GadgwTTVPLHSTATRLIA-----LLSGRVFVGLPLSR-NEEWIDAAVNVTQHS-IAGAFKLLAYPAWLRP--LVRLFVR 225
Cdd:cd11062    96 G----EPVNLDDAFRALTAdviteYAFGRSYGYLDEPDfGPEFLDALRALAEMIhLLRHFPWLLKLLRSLPesLLKRLNP 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 226 EVGGVEECRQATERMLRplveqRLRDMRSGGADFQGQDDMIQWLITHAPPGSVSDVAWHVSQHLVLNIAAIHTTSGQLSG 305
Cdd:cd11062   172 GLAVFLDFQESIAKQVD-----EVLRQVSAGDPPSIVTSLFHALLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSV 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 306 TLFALAARPHYMQPLREEIEACIlkhgaLTKQCLHDMVKLDS--FLR----EVQRLSpPGLVS-VNRKVLEPITLSNGQR 378
Cdd:cd11062   247 ATFHLLSNPEILERLREELKTAM-----PDPDSPPSLAELEKlpYLTavikEGLRLS-YGVPTrLPRVVPDEGLYYKGWV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 379 LPVGTSIAFPADAINRDPELWERPADFDGFRFarlrTEPGSENSFQ--FVssnasgiSFGHGKAACPGRWFAATELKVML 456
Cdd:cd11062   321 IPPGTPVSMSSYFVHHDEEIFPDPHEFRPERW----LGAAEKGKLDryLV-------PFSKGSRSCLGINLAYAELYLAL 389

                         410
                  ....*....|...
gi 1148921820 457 ARLLPDFDFALAE 469
Cdd:cd11062   390 AALFRRFDLELYE 402
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 310-470 3.54e-07

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 52.77  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 310 LAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPITLSnGQRLPVGTSIAFPA 389
Cdd:PLN03234  315 LIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIG-GYDIPAKTIIQVNA 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 390 DAINRDPELW-ERPADFDGFRFARlrtepgSENSFQFVSSNASGISFGHGKAACPGRWFAATELKVMLARLLPDFDFALA 468
Cdd:PLN03234  394 WAVSRDTAAWgDNPNEFIPERFMK------EHKGVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLP 467


                  ..
gi 1148921820 469 EG 470
Cdd:PLN03234  468 KG 469
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 352-478 4.01e-07

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


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 52.32  E-value: 4.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 352 VQRLSPPglvsvnRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSEnSFQFvssnas 431
Cdd:cd11066   307 VLPLGLP------RKTTKDIVY-NGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPG-PPHF------ 372

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1148921820 432 giSFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEGGDGP-LHAF 478
Cdd:cd11066   373 --SFGAGSRMCAGSHLANRELYTAICRLILLFRIGPKDEEEPMeLDPF 418
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 291-470 4.74e-07

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 52.32  E-value: 4.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEAcilkhgALTKQCLHDMVKLDSFLREVQRLSPPglVSVNRKV-LE 369
Cdd:PLN02169  309 LVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINT------KFDNEDLEKLVYLHAALSESMRLYPP--LPFNHKApAK 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 370 PITLSNGQRLPVGTSIAFPADAINRDPELW-ERPADFDGFRFAR----LRTEPgsenSFQFVSsnasgisFGHGKAACPG 444
Cdd:PLN02169  381 PDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISdnggLRHEP----SYKFMA-------FNSGPRTCLG 449

                         170       180
                  ....*....|....*....|....*.
gi 1148921820 445 RWFAATELKVMLARLLPDFDFALAEG 470
Cdd:PLN02169  450 KHLALLQMKIVALEIIKNYDFKVIEG 475
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 314-470 6.44e-07

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: 51.72  E-value: 6.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 314 PHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPITLSnGQRLPVGTSIAFPADAIN 393
Cdd:cd20656   261 PRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHKASENVKIG-GYDIPKGANVHVNVWAIA 339

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1148921820 394 RDPELWERPADFDGFRFArlrtepgsENSFQFVSSNASGISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd20656   340 RDPAVWKNPLEFRPERFL--------EEDVDIKGHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHFSWTPPEG 408
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 244-469 6.48e-07

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: 51.45  E-value: 6.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 244 LVEQRLRDMRsggadfqgqDDMIQWLITHA----PPGSVSDVAWHVSQHLVlniAAIHTTSGQLSGTLFALAARPHYMQP 319
Cdd:cd11078   178 LVAERRREPR---------DDLISDLLAAAdgdgERLTDEELVAFLFLLLV---AGHETTTNLLGNAVKLLLEHPDQWRR 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 320 LREeieacilkhgaltkqclhDMVKLDSFLREVQRLSPPgLVSVNRKVLEPITLSnGQRLPVGTSIA-FPADAiNRDPEL 398
Cdd:cd11078   246 LRA------------------DPSLIPNAVEETLRYDSP-VQGLRRTATRDVEIG-GVTIPAGARVLlLFGSA-NRDERV 304

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1148921820 399 WERPADFDgfrfarLRTEPGSENsfqfvssnasgISFGHGKAACPGRWFAATELKVMLARLL---PDFDFALAE 469
Cdd:cd11078   305 FPDPDRFD------IDRPNARKH-----------LTFGHGIHFCLGAALARMEARIALEELLrrlPGMRVPGQE 361
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 294-471 7.04e-07

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: 51.35  E-value: 7.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 294 AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLH--DMVKLDSFLREVQRLSPPGLVSVNRKVLEPI 371
Cdd:cd20664   236 AGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVI---GSRQPQVEHrkNMPYTDAVIHEIQRFANIVPMNLPHATTRDV 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 372 TLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFarLRTEPgsensfQFVSSNASgISFGHGKAACPGRWFAATE 451
Cdd:cd20664   313 TF-RGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHF--LDSQG------KFVKRDAF-MPFSAGRRVCIGETLAKME 382

                         170       180
                  ....*....|....*....|
gi 1148921820 452 LKVMLARLLPDFDFALAEGG 471
Cdd:cd20664   383 LFLFFTSLLQRFRFQPPPGV 402
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 209-470 7.24e-07

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: 51.35  E-value: 7.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 209 LLAYPAWLRPLVRLFVREVGGVEECRQ----------ATERMLRPL-------------------------VEQRLRDMR 253
Cdd:cd20638   120 VLVYPEVKRLMFRIAMRILLGFEPQQTdreqeqqlveAFEEMIRNLfslpidvpfsglyrglrarnlihakIEENIRAKI 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 254 SGGADFQGQDDMIQWLITHA----PPGSVSDVAWHVSQHLVlniaAIHTTSGQLSGTLFA-LAARPHYMQPLREEIEACI 328
Cdd:cd20638   200 QREDTEQQCKDALQLLIEHSrrngEPLNLQALKESATELLF----GGHETTASAATSLIMfLGLHPEVLQKVRKELQEKG 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 329 LKHGALTKQCLHDMVKLD------SFLREVQRLSPP--GLVSVNRKVLEpitlSNGQRLPVGTSIAFPADAINRDPELWE 400
Cdd:cd20638   276 LLSTKPNENKELSMEVLEqlkytgCVIKETLRLSPPvpGGFRVALKTFE----LNGYQIPKGWNVIYSICDTHDVADIFP 351

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 401 RPADFDGFRFarlrTEPGSENSFQFvssnaSGISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd20638   352 NKDEFNPDRF----MSPLPEDSSRF-----SFIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQLLNG 412
PLN00168 PLN00168
Cytochrome P450; Provisional
 294-470 7.74e-07

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 51.49  E-value: 7.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 294 AAIHTTSGQLSGTLFALAARPHYMQPLREEIEA-CILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPIT 372
Cdd:PLN00168  317 AGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAkTGDDQEEVSEEDVHKMPYLKAVVLEGLRKHPPAHFVLPHKAAEDME 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 373 LSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrtePGSENSFQFVSSnASGIS---FGHGKAACPGRWFAA 449
Cdd:PLN00168  397 VG-GYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFL-----AGGDGEGVDVTG-SREIRmmpFGVGRRICAGLGIAM 469

                         170       180
                  ....*....|....*....|.
gi 1148921820 450 TELKVMLARLLPDFDFALAEG 470
Cdd:PLN00168  470 LHLEYFVANMVREFEWKEVPG 490
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 291-468 8.99e-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: 51.00  E-value: 8.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKH------GALTKQCLHDMVKLDSFLREVQRLSPPglVSVN 364
Cdd:cd20637   234 LIFAAFATTASASTSLIMQLLKHPGVLEKLREELRSNGILHngclceGTLRLDTISSLKYLDCVIKEVLRLFTP--VSGG 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 365 -RKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEpGSENSFQFvssnasgISFGHGKAACP 443
Cdd:cd20637   312 yRTALQTFEL-DGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSE-DKDGRFHY-------LPFGGGVRTCL 382

                         170       180
                  ....*....|....*....|....*
gi 1148921820 444 GRWFAATELKVMLARLLPDFDFALA 468
Cdd:cd20637   383 GKQLAKLFLKVLAVELASTSRFELA 407
PLN03018 PLN03018
homomethionine N-hydroxylase
 293-475 1.35e-06

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 50.78  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 293 IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVLEPIT 372
Cdd:PLN03018  324 IAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTT 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 373 LSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRfaRLRTEpGSENSFQFVSSNASGISFGHGKAACPGRWFAATEL 452
Cdd:PLN03018  404 LG-GYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPER--HLQGD-GITKEVTLVETEMRFVSFSTGRRGCVGVKVGTIMM 479

                         170       180
                  ....*....|....*....|...
gi 1148921820 453 KVMLARLLPDFDFALAEGGdGPL 475
Cdd:PLN03018  480 VMMLARFLQGFNWKLHQDF-GPL 501
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 291-468 1.38e-06

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


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 50.60  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 291 LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEAcilkHGALTK-QCLHDMVKL---------DSFLREVQRLSPPgl 360
Cdd:cd20636   235 LIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVS----HGLIDQcQCCPGALSLeklsrlrylDCVVKEVLRLLPP-- 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 361 VSVN-RKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSENsFQFvssnasgISFGHGK 439
Cdd:cd20636   309 VSGGyRTALQTFEL-DGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGR-FNY-------IPFGGGV 379

                         170       180
                  ....*....|....*....|....*....
gi 1148921820 440 AACPGRWFAATELKVMLARLLPDFDFALA 468
Cdd:cd20636   380 RSCIGKELAQVILKTLAVELVTTARWELA 408
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 206-470 7.07e-06

cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first committed step in the biosynthesis of the core structure of glucosinolates, the conversion of amino acids to the corresponding aldoximes. Glucosinolates are amino acid-derived natural plant products that function in the defense against herbivores and microorganisms. Arabidopsis thaliana contains seven family members: CYP79B2 and CYP79B3, which metabolize trytophan; CYP79F1 and CYP79F2, which metabolize chain-elongated methionine derivatives with respectively 1-6 or 5-6 additional methylene groups in the side chain; CYP79A2 that metabolizes phenylalanine; and CYP79C1 and CYP79C2, with unknown function. CYP79 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 48.52  E-value: 7.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 206 AFKLLAYPAWLRPLvrlfvrEVGGVE-ECRQATERMLR---PLVEQRLRDMRSGGAdfQGQDDMIQWLIThappgsVSDV 281
Cdd:cd20658   162 AFSISDYLPFLRGL------DLDGHEkIVREAMRIIRKyhdPIIDERIKQWREGKK--KEEEDWLDVFIT------LKDE 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 282 AwhvSQHLV-----------LNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQclhDMVKLD---S 347
Cdd:cd20658   228 N---GNPLLtpdeikaqikeLMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQES---DIPNLNyvkA 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 348 FLREVQRLSPPGLVSVNRKVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRfaRLRTEPG---SENSFQ 424
Cdd:cd20658   302 CAREAFRLHPVAPFNVPHVAMSDTTVG-GYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPER--HLNEDSEvtlTEPDLR 378

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1148921820 425 FvssnasgISFGHGKAACPGRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd20658   379 F-------ISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTLPPN 417
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 167-463 1.01e-05

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 47.74  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 167 TATRLIAL-LSGRVFVGLPLsrNEEwidAAVNVTQHSIAGAFKLLAYPAWLRPLVRLFVREVGGVEECRQATERmlrpLV 245
Cdd:cd20616   118 TLMRRIMLdTSNRLFLGVPL--NEK---AIVLKIQGYFDAWQALLIKPDIFFKISWLYKKYEKAVKDLKDAIEI----LI 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 246 EQRLRDMrSGGADFQGQDDMIQWLITHAPPGSVSdvAWHVSQH-LVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEI 324
Cdd:cd20616   189 EQKRRRI-STAEKLEDHMDFATELIFAQKRGELT--AENVNQCvLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEI 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 325 EAcILKHGALTKQCLHDMVKLDSFLREVQRLSPpgLVS-VNRKVLEPITLsNGQRLPVGTSIAFPADAINRDpELWERPA 403
Cdd:cd20616   266 QT-VLGERDIQNDDLQKLKVLENFINESMRYQP--VVDfVMRKALEDDVI-DGYPVKKGTNIILNIGRMHRL-EFFPKPN 340

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 404 DFDGFRFARlrTEPgsENSFQfvssnasgiSFGHGKAACPGRWFAATELKVMLARLLPDF 463
Cdd:cd20616   341 EFTLENFEK--NVP--SRYFQ---------PFGFGPRSCVGKYIAMVMMKAILVTLLRRF 387
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
 298-464 1.39e-05

cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces sp. P450sky (also called CYP163B3), Sphingopyxis macrogoltabida P450pyr hydroxylase, Novosphingobium aromaticivorans CYP108D1, Pseudomonas sp. cytochrome P450-Terp (P450terp), and Amycolatopsis balhimycina P450 OxyD, as well as several Mycobacterium proteins CYP124, CYP125, CYP126, and CYP142. P450sky is involved in the hydroxylation of three beta-hydroxylated amino acid precursors required for the biosynthesis of the cyclic depsipeptide skyllamycin. P450pyr hydroxylase is an active and selective catalyst for the regio- and stereo-selective hydroxylation at non-activated carbon atoms with a broad substrate range. P450terp catalyzes the hydroxylation of alpha-terpineol as part of its catabolic assimilation. OxyD is involved in beta-hydroxytyrosine formation during vancomycin biosynthesis. CYP124 is a methyl-branched lipid omega-hydroxylase while CYP142 is a cholesterol 27-oxidase with likely roles in host response modulation and cholesterol metabolism. 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: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 47.14  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 298 TTSGQLSGTLFALAARPHYMQPLREeieacilkhgaltkqclhDMVKLDSFLREVQRLSPPgLVSVNRKVLEPITLsNGQ 377
Cdd:cd11033   224 TTRNSISGGVLALAEHPDQWERLRA------------------DPSLLPTAVEEILRWASP-VIHFRRTATRDTEL-GGQ 283

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 378 RLPVGTSIAFPADAINRDPELWERPADFDGFRFARlrtepgsensfqfvssnaSGISFGHGKAACPGRWFAATELKVMLA 457
Cdd:cd11033   284 RIRAGDKVVLWYASANRDEEVFDDPDRFDITRSPN------------------PHLAFGGGPHFCLGAHLARLELRVLFE 345


                  ....*..
gi 1148921820 458 RLLPDFD 464
Cdd:cd11033   346 ELLDRVP 352
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 294-460 2.22e-05

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: 46.42  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 294 AAIHTTSGQLSGTLFALAARPHYMQPLREEIEacilkhgaLTKQCLHDMVKLDSFLREVQRLsppglvsVNRKV-LEPIT 372
Cdd:cd11037   213 AGLDTTISAIGNALWLLARHPDQWERLRADPS--------LAPNAFEEAVRLESPVQTFSRT-------TTRDTeLAGVT 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 373 LSNGQRLpvgtsIAFPADAiNRDPELWERPADFDgfrfarlrtepgsensfqfVSSNASG-ISFGHGKAACPGRWFAATE 451
Cdd:cd11037   278 IPAGSRV-----LVFLGSA-NRDPRKWDDPDRFD-------------------ITRNPSGhVGFGHGVHACVGQHLARLE 332


                  ....*....
gi 1148921820 452 LKVMLARLL 460
Cdd:cd11037   333 GEALLTALA 341
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
 287-466 3.39e-05

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


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 46.31  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 287 QHLVLNI-----AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTkqcLHDMVKL---DSFLREVQRLSPP 358
Cdd:cd20672   225 QNLMISVlslffAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPT---LDDRAKMpytDAVIHEIQRFSDL 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 359 GLVSVNRKVLEPiTLSNGQRLPVGTSIAFPADAINRDPELWERPADFdgfrfarlrtepgseNSFQFVSSNAS------G 432
Cdd:cd20672   302 IPIGVPHRVTKD-TLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTF---------------NPDHFLDANGAlkkseaF 365

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1148921820 433 ISFGHGKAACPGRWFAATELKVMLARLLPDFDFA 466
Cdd:cd20672   366 MPFSTGKRICLGEGIARNELFLFFTTILQNFSVA 399
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 289-463 5.13e-05

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: 45.69  E-value: 5.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVL 368
Cdd:cd20670   232 LNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGVPHNVI 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 369 EPiTLSNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFArlrTEPGSensfqfVSSNASGISFGHGKAACPGRWFA 448
Cdd:cd20670   312 RD-TQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFL---DEQGR------FKKNEAFVPFSSGKRVCLGEAMA 381

                         170
                  ....*....|....*
gi 1148921820 449 ATELKVMLARLLPDF 463
Cdd:cd20670   382 RMELFLYFTSILQNF 396
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 289-465 8.37e-05

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: 44.79  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNIAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVSVNRKVL 368
Cdd:cd20668   232 LNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRVT 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 369 EPITLsNGQRLPVGTSIaFPA-DAINRDPELWERPADFDGFRFarlrtepgSENSFQFVSSNASgISFGHGKAACPGRWF 447
Cdd:cd20668   312 KDTKF-RDFFLPKGTEV-FPMlGSVLKDPKFFSNPKDFNPQHF--------LDDKGQFKKSDAF-VPFSIGKRYCFGEGL 380

                         170
                  ....*....|....*...
gi 1148921820 448 AATELKVMLARLLPDFDF 465
Cdd:cd20668   381 ARMELFLFFTTIMQNFRF 398
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 310-465 1.81e-04

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: 43.77  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 310 LAARPHYMQPLREEIEA-CILKHGALTKQCLHDMVKLDSFLREVQRLSPPGLVsVNRKVLEPITLSNGQRLPVGTSIAfp 388
Cdd:cd11082   247 LADHPDVLAKVREEQARlRPNDEPPLTLDLLEEMKYTRQVVKEVLRYRPPAPM-VPHIAKKDFPLTEDYTVPKGTIVI-- 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 389 adainrdPELWerPADFDGF----RFARLR-TEPGSENSFQFVSSnasgISFGHGKAACPGRWFAATELKVMLARLLPDF 463
Cdd:cd11082   324 -------PSIY--DSCFQGFpepdKFDPDRfSPERQEDRKYKKNF----LVFGAGPHQCVGQEYAINHLMLFLALFSTLV 390


                  ..
gi 1148921820 464 DF 465
Cdd:cd11082   391 DW 392
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 232-469 2.34e-04

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 43.43  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 232 ECRQATERMLRPLVEQRLRDMRSGGadfQGQDDMIQWLITHAPPGSVSDVawhVSQHLVLNIAAIHTTSGQLSGTLFALA 311
Cdd:PLN02987  222 QARTKVAEALTLVVMKRRKEEEEGA---EKKKDMLAALLASDDGFSDEEI---VDFLVALLVAGYETTSTIMTLAVKFLT 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 312 ARPHYMQPLREE---IEACILKHGALTKQCLHDMVKLDSFLREVQRLSPPgLVSVNRKVLEPITLsNGQRLPVGTSIAFP 388
Cdd:PLN02987  296 ETPLALAQLKEEhekIRAMKSDSYSLEWSDYKSMPFTQCVVNETLRVANI-IGGIFRRAMTDIEV-KGYTIPKGWKVFAS 373

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 389 ADAINRDPELWERPADFDGFRFARLRTEPGSENSFQfvssnasgiSFGHGKAACPGRWFAATELKVMLARLLPDFDFALA 468
Cdd:PLN02987  374 FRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFT---------PFGGGPRLCPGYELARVALSVFLHRLVTRFSWVPA 444


                  .
gi 1148921820 469 E 469
Cdd:PLN02987  445 E 445
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 215-460 2.72e-04

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: 43.44  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 215 WLRPLVRlfvrevGGVEECRQATERM---LRPLVEQRLRDMRSGGadfqgQDDMIQWLITHA---PPGSVSDVAwhVSQH 288
Cdd:cd11028   164 WLRYLTR------RKLQKFKELLNRLnsfILKKVKEHLDTYDKGH-----IRDITDALIKASeekPEEEKPEVG--LTDE 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNI------AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLHDMVKL---DSFLREVQRLSPPG 359
Cdd:cd11028   231 HIISTvqdlfgAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVI---GRERLPRLSDRPNLpytEAFILETMRHSSFV 307

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 360 LVSVNRKVLEPITLsNGQRLPVGTsIAFPAD-AINRDPELWERPADFDGFRFArlrTEPGSENSfqfvSSNASGISFGHG 438
Cdd:cd11028   308 PFTIPHATTRDTTL-NGYFIPKGT-VVFVNLwSVNHDEKLWPDPSVFRPERFL---DDNGLLDK----TKVDKFLPFGAG 378

                         250       260
                  ....*....|....*....|..
gi 1148921820 439 KAACPGRWFAATELKVMLARLL 460
Cdd:cd11028   379 RRRCLGEELARMELFLFFATLL 400
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 294-473 2.73e-04

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 43.39  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 294 AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQCLHDMVKLDSFLREVQR-LSPPGLVSVN-RKVLEPI 371
Cdd:PLN02196  275 AARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGESLTWEDTKKMPLTSRVIQEtLRVASILSFTfREAVEDV 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 372 TLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFaRLRTEPgseNSFqfvssnasgISFGHGKAACPGRWFAATE 451
Cdd:PLN02196  355 EYE-GYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRF-EVAPKP---NTF---------MPFGNGTHSCPGNELAKLE 420

                         170       180
                  ....*....|....*....|..
gi 1148921820 452 LKVMLARLLPDFDFALAEGGDG 473
Cdd:PLN02196  421 ISVLIHHLTTKYRWSIVGTSNG 442
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 351-460 2.87e-04

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 43.11  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 351 EVQRLSPPgLVSVNRKVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRfarlrtepgsensfqfvsSNA 430
Cdd:cd11079   233 EILRLDDP-FVANRRITTRDVELG-GRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR------------------HAA 292

                          90       100       110
                  ....*....|....*....|....*....|
gi 1148921820 431 SGISFGHGKAACPGRWFAATELKVMLARLL 460
Cdd:cd11079   293 DNLVYGRGIHVCPGAPLARLELRILLEELL 322
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 284-470 4.55e-04

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


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 42.69  E-value: 4.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 284 HVSQHLVLNI------AAIHTTSGQLSGTLFALAARPHYMQPLREEIEACIlkhGALTKQCLHDMVKL---DSFLREVQR 354
Cdd:cd20676   232 QLSDEKIVNIvndlfgAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVI---GRERRPRLSDRPQLpylEAFILETFR 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 355 LSPpglvsvnrkvLEPITLS---------NGQRLPVGTSIAFPADAINRDPELWERPADFDGFRfarlrtepgsensfqF 425
Cdd:cd20676   309 HSS----------FVPFTIPhcttrdtslNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPER---------------F 363

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1148921820 426 VSSNASGIS---------FGHGKAACPGRWFAATELKVMLARLLPDFDFALAEG 470
Cdd:cd20676   364 LTADGTEINktesekvmlFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVPPG 417
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
 355-448 1.40e-03

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 40.95  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 355 LSPPGLVSvnRKVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDGFRfarlrtepgsensfqfvsSNASGIS 434
Cdd:cd11039   257 ISPIGMSP--RRVAEDFEIR-GVTLPAGDRVFLMFGSANRDEARFENPDRFDVFR------------------PKSPHVS 315

                          90
                  ....*....|....
gi 1148921820 435 FGHGKAACPGRWFA 448
Cdd:cd11039   316 FGAGPHFCAGAWAS 329
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 293-465 4.56e-03

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: 39.59  E-value: 4.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 293 IAAIHTTSGQLSGTLFALAARPHYMQPLREEIEACILKHGALTKQ-CLHDMVK-----LDSFLREVQRLSPPgLVSVNRK 366
Cdd:cd20622   272 IAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEAVAEGRLpTAQEIAQaripyLDAVIEEILRCANT-APILSRE 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 367 VLEPITLSnGQRLPVGTSI-------AFPADAINRDPEL--------------WERP--ADFDGFRFARlRTEPGSENSF 423
Cdd:cd20622   351 ATVDTQVL-GYSIPKGTNVfllnngpSYLSPPIEIDESRrssssaakgkkagvWDSKdiADFDPERWLV-TDEETGETVF 428

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1148921820 424 QfvSSNASGISFGHGKAACPGRWFAATELKVMLARLLPDFDF 465
Cdd:cd20622   429 D--PSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFEL 468
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 289-464 5.16e-03

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 39.31  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 289 LVLNIAAIHTTSGQLS--GTLFaLAARPHYMQPLREEIEAcILKHGALTKQCL-----HDMVKLDSFLREVQRLSPPGLV 361
Cdd:PLN02302  292 LLMYLNAGHESSGHLTmwATIF-LQEHPEVLQKAKAEQEE-IAKKRPPGQKGLtlkdvRKMEYLSQVIDETLRLINISLT 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 362 sVNRKVLEPITLsNGQRLPVGTSIAFPADAINRDPELWERPADFDGFRFARLRTEPGSensfqFVSsnasgisFGHGKAA 441
Cdd:PLN02302  370 -VFREAKTDVEV-NGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTPKAGT-----FLP-------FGLGSRL 435

                         170       180
                  ....*....|....*....|...
gi 1148921820 442 CPGRWFAATELKVMLARLLPDFD 464
Cdd:PLN02302  436 CPGNDLAKLEISIFLHHFLLGYR 458
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 306-488 7.51e-03

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: 38.60  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 306 TLFALAARPHYMQPLREEIEacilkhGALTKQCLHdmvKLDSFLREVQRLSPPGLVsVNRKVLEPiTLSNGQRLPVGTSI 385
Cdd:cd20624   214 ALALLAAHPEQAARAREEAA------VPPGPLARP---YLRACVLDAVRLWPTTPA-VLRESTED-TVWGGRTVPAGTGF 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 386 AFPADAINRDPELWERPADFDGFRFARLRTEPgsensfqfvssNASGISFGHGKAACPGRWFAATELKVMLARLLPDFDF 465
Cdd:cd20624   283 LIFAPFFHRDDEALPFADRFVPEIWLDGRAQP-----------DEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEI 351

                         170       180
                  ....*....|....*....|...
gi 1148921820 466 AlaeggdgPLHAFVDVLGAPDPT 488
Cdd:cd20624   352 D-------PLESPRSGPGEPLPG 367
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 298-470 8.30e-03

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 38.52  E-value: 8.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 298 TTSGQLSGTLFALAARPHYMQPLREEIEACI-LKHGALTKQCLHDMVKLDSFLREVQRLSPPglVSVNRK-VLEPITLSN 375
Cdd:PLN02426  308 TVASALTSFFWLLSKHPEVASAIREEADRVMgPNQEAASFEEMKEMHYLHAALYESMRLFPP--VQFDSKfAAEDDVLPD 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 376 GQRLPVGTSIAFPADAINRDPELWErpADFDGFRFARLRTEpGS---ENSFQFVSsnasgisFGHGKAACPGRWFAATEL 452
Cdd:PLN02426  386 GTFVAKGTRVTYHPYAMGRMERIWG--PDCLEFKPERWLKN-GVfvpENPFKYPV-------FQAGLRVCLGKEMALMEM 455

                         170
                  ....*....|....*...
gi 1148921820 453 KVMLARLLPDFDFALAEG 470
Cdd:PLN02426  456 KSVAVAVVRRFDIEVVGR 473
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 349-469 9.96e-03

cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is a heme-containing monooxygenase which participates in epothilone biosynthesis where it catalyzes the epoxidation of epothilones C and D into epothilones A and B, respectively. This subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 38.18  E-value: 9.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 349 LREVQRLSPPGLVSVNRKVLEPITLSnGQRLPVGTSIAFPADAINRDPELWERPADFDgfrfarLRTEPgsensfqfvss 428
Cdd:cd20630   251 LEEVLRWDNFGKMGTARYATEDVELC-GVTIRKGQMVLLLLPSALRDEKVFSDPDRFD------VRRDP----------- 312

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1148921820 429 NASgISFGHGKAACPGRWFAATELKVMLARLLPDF-DFALAE 469
Cdd:cd20630   313 NAN-IAFGYGPHFCIGAALARLELELAVSTLLRRFpEMELAE 353
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 230-462 9.99e-03

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: 38.11  E-value: 9.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 230 VEECRQATERM---LRPLVEQRLRDMRsggadfqgqDDMIQWLITHAPPGSVSDVAWHVSQHLVLNIAAIHTTSGQLSGT 306
Cdd:cd11038   167 LPRIEAAVEELydyADALIEARRAEPG---------DDLISTLVAAEQDGDRLSDEELRNLIVALLFAGVDTTRNQLGLA 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148921820 307 LFALAARPHYMQPLREEIEaciLKHGALTkqclhdmvkldsflrEVQRLSPpGLVSVNRKVLEPITLsNGQRLPVGTSIA 386
Cdd:cd11038   238 MLTFAEHPDQWRALREDPE---LAPAAVE---------------EVLRWCP-TTTWATREAVEDVEY-NGVTIPAGTVVH 297

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1148921820 387 FPADAINRDPelweRPADFDGFRFARLRTEPgsensfqfvssnasgISFGHGKAACPGRWFAATELKV---MLARLLPD 462
Cdd:cd11038   298 LCSHAANRDP----RVFDADRFDITAKRAPH---------------LGFGGGVHHCLGAFLARAELAEaltVLARRLPT 357
 
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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