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Conserved domains on  [gi|30683024|ref|NP_565617|]
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cytochrome P450, family 711, subfamily A, polypeptide 1 [Arabidopsis thaliana]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
75-515 7.78e-86

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


The actual alignment was detected with superfamily member cd11055:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 422  Bit Score: 271.38  E-value: 7.78e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  75 QYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRsiPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTS 154
Cdd:cd11055   1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNR--PLFILLDEPFDSSLLFLKGERWKRLRTTLSPTFSSGKLKL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 155 LIPTMHSFITSATHNLDSK--PRDIVF-SNLFLKLTTDIIGQAAFGVDfgLSGKKPIKDvEVTDFINQHVYSTTQLKMDL 231
Cdd:cd11055  79 MVPIINDCCDELVEKLEKAaeTGKPVDmKDLFQGFTLDVILSTAFGID--VDSQNNPDD-PFLKAAKKIFRNSIIRLFLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 232 SGSLSIILGLLIPILQEPFRQVLKRIpgtmdwrvektnarlSGQLNEIVSKRAKEAETDSKDFLSLILKARESDPFAKNI 311
Cdd:cd11055 156 LLLFPLRLFLFLLFPFVFGFKSFSFL---------------EDVVKKIIEQRRKNKSSRRKDLLQLMLDAQDSDEDVSKK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 312 -FTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRDLIPtaHDLQHKFPYLDQVIKEAMRF 389
Cdd:cd11055 221 kLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEvLPDDGSPT--YDTVSKLKYLDMVINETLRL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 390 YMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPngEEEKHRHPYAFIPFGIGPRACVG 469
Cdd:cd11055 299 YPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSP--ENKAKRHPYAYLPFGAGPRNCIG 376
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 30683024 470 QRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDYGIILSFKNGVK 515
Cdd:cd11055 377 MRFALLEVKLALVKILQKFRFVPCKETEIPLKLVGGATLSPKNGIY 422
 
Name Accession Description Interval E-value
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
75-515 7.78e-86

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: 271.38  E-value: 7.78e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  75 QYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRsiPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTS 154
Cdd:cd11055   1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNR--PLFILLDEPFDSSLLFLKGERWKRLRTTLSPTFSSGKLKL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 155 LIPTMHSFITSATHNLDSK--PRDIVF-SNLFLKLTTDIIGQAAFGVDfgLSGKKPIKDvEVTDFINQHVYSTTQLKMDL 231
Cdd:cd11055  79 MVPIINDCCDELVEKLEKAaeTGKPVDmKDLFQGFTLDVILSTAFGID--VDSQNNPDD-PFLKAAKKIFRNSIIRLFLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 232 SGSLSIILGLLIPILQEPFRQVLKRIpgtmdwrvektnarlSGQLNEIVSKRAKEAETDSKDFLSLILKARESDPFAKNI 311
Cdd:cd11055 156 LLLFPLRLFLFLLFPFVFGFKSFSFL---------------EDVVKKIIEQRRKNKSSRRKDLLQLMLDAQDSDEDVSKK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 312 -FTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRDLIPtaHDLQHKFPYLDQVIKEAMRF 389
Cdd:cd11055 221 kLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEvLPDDGSPT--YDTVSKLKYLDMVINETLRL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 390 YMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPngEEEKHRHPYAFIPFGIGPRACVG 469
Cdd:cd11055 299 YPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSP--ENKAKRHPYAYLPFGAGPRNCIG 376
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 30683024 470 QRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDYGIILSFKNGVK 515
Cdd:cd11055 377 MRFALLEVKLALVKILQKFRFVPCKETEIPLKLVGGATLSPKNGIY 422
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
47-494 5.56e-82

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: 262.60  E-value: 5.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024    47 PGPTAMPLVGHLPLMAKYGP--DVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSP--ISASP 122
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKGNlhSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWfaTSRGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   123 LHKKGLFFTRDKRWSKMRNTilslyqpshltsLIPTMHSF--------ITSATHNLDSK-------PRDIVFSNLFLKLT 187
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRF------------LTPTFTSFgklsfeprVEEEARDLVEKlrktagePGVIDITDLLFRAA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   188 TDIIGQAAFGVDFGLsgkkpIKDVEVTDFInqhvysttqlKMDLSGSLSIILGLLIPILQEPFrqvLKRIPGTMDWRVEK 267
Cdd:pfam00067 150 LNVICSILFGERFGS-----LEDPKFLELV----------KAVQELSSLLSSPSPQLLDLFPI---LKYFPGPHGRKLKR 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   268 TNARLSGQLNEIVSKRAKEAETDSK---DFLSLILKARESDPFAKniFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVS 344
Cdd:pfam00067 212 ARKKIKDLLDKLIEERRETLDSAKKsprDFLDALLLAKEEEDGSK--LTDEELRATVLELFFAGTDTTSSTLSWALYELA 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   345 GHLDVEKRLLQEIDGFGNRDLIPTAHDLQHkFPYLDQVIKEAMRFYMVSP-LVARETAKEVEIGGYLLPKGTWVWLALGV 423
Cdd:pfam00067 290 KHPEVQEKLREEIDEVIGDKRSPTYDDLQN-MPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYA 368
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30683024   424 LAKDPKNFPEPEKFKPERFDPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNyiFRHSL 494
Cdd:pfam00067 369 LHRDPEVFPNPEEFDPERFLD--ENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQN--FEVEL 435
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
49-488 1.46e-47

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: 170.07  E-value: 1.46e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  49 PTAMPLVGHLPLMAKYGPDVFSVLAK--QYGPIFRFQMGRQPLIIIAEAELCREVgikkFKD----LPNRSIPSPISASP 122
Cdd:COG2124   2 TATATPAADLPLDPAFLRDPYPFYARlrEYGPVFRVRLPGGGAWLVTRYEDVREV----LRDprtfSSDGGLPEVLRPLP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 123 LHKKGLFFTRDKRWSKMRNTILSLYQPSHLTSLIPTMHSFITSATHNL-DSKPRDIVfsNLFLKLTTDIIGQAAFGVdfg 201
Cdd:COG2124  78 LLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIREIADELLDRLaARGPVDLV--EEFARPLPVIVICELLGV--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 202 lsgkkPIKDVE-VTDFINQHVYSTTqlkmdlsgslsiilgllipilqepfrqvlkRIPGTMDWRVEKTNARLSGQLNEIV 280
Cdd:COG2124 153 -----PEEDRDrLRRWSDALLDALG------------------------------PLPPERRRRARRARAELDAYLRELI 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 281 SKRAKEAETDskdFLSLILKARESDpfakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIdgf 360
Cdd:COG2124 198 AERRAEPGDD---LLSALLAARDDG----ERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP--- 267
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 361 gnrdliptahdlqhkfPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPE 440
Cdd:COG2124 268 ----------------ELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPD 331
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 30683024 441 rfdpngeeekhRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:COG2124 332 -----------RPPNAHLPFGGGPHRCLGAALARLEARIALATLLRRF 368
PLN02687 PLN02687
flavonoid 3'-monooxygenase
47-483 2.32e-31

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 127.23  E-value: 2.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   47 PGPTAMPLVGHLPLMAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCRE---VGIKKFKDLPNRSIPSPISASpl 123
Cdd:PLN02687  37 PGPRGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQflrTHDANFSNRPPNSGAEHMAYN-- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  124 HKKGLFFTRDKRWSKMRN-TILSLYQPSHLTSLIPTMHSFITSATHNLDSKPRD--IVFSNLFLKLTTDIIGQAA----- 195
Cdd:PLN02687 115 YQDLVFAPYGPRWRALRKiCAVHLFSAKALDDFRHVREEEVALLVRELARQHGTapVNLGQLVNVCTTNALGRAMvgrrv 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  196 FGVDFGlSGKKPIKDVEVTDFINQHVYSTTQlkmdlsgslsiilgllipilqepFRQVLKRI-PGTMDWRVEKTNARLSG 274
Cdd:PLN02687 195 FAGDGD-EKAREFKEMVVELMQLAGVFNVGD-----------------------FVPALRWLdLQGVVGKMKRLHRRFDA 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  275 QLNEIVSKRAKEAETDS---KDFLSLILKARESDPFA--KNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDV 349
Cdd:PLN02687 251 MMNGIIEEHKAAGQTGSeehKDLLSTLLALKREQQADgeGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDI 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  350 EKRLLQEIDGFGNRDLIPTAHDLQHkFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDP 428
Cdd:PLN02687 331 LKKAQEELDAVVGRDRLVSESDLPQ-LTYLQAVIKETFRLHPSTPLsLPRMAAEECEINGYHIPKGATLLVNVWAIARDP 409
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024  429 KNFPEPEKFKPERFDPNGEeekhrHP--------YAFIPFGIGPRACVGQRFALQEIKL---TLLH 483
Cdd:PLN02687 410 EQWPDPLEFRPDRFLPGGE-----HAgvdvkgsdFELIPFGAGRRICAGLSWGLRMVTLltaTLVH 470
 
Name Accession Description Interval E-value
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
75-515 7.78e-86

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: 271.38  E-value: 7.78e-86
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  75 QYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRsiPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTS 154
Cdd:cd11055   1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNR--PLFILLDEPFDSSLLFLKGERWKRLRTTLSPTFSSGKLKL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 155 LIPTMHSFITSATHNLDSK--PRDIVF-SNLFLKLTTDIIGQAAFGVDfgLSGKKPIKDvEVTDFINQHVYSTTQLKMDL 231
Cdd:cd11055  79 MVPIINDCCDELVEKLEKAaeTGKPVDmKDLFQGFTLDVILSTAFGID--VDSQNNPDD-PFLKAAKKIFRNSIIRLFLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 232 SGSLSIILGLLIPILQEPFRQVLKRIpgtmdwrvektnarlSGQLNEIVSKRAKEAETDSKDFLSLILKARESDPFAKNI 311
Cdd:cd11055 156 LLLFPLRLFLFLLFPFVFGFKSFSFL---------------EDVVKKIIEQRRKNKSSRRKDLLQLMLDAQDSDEDVSKK 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 312 -FTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRDLIPtaHDLQHKFPYLDQVIKEAMRF 389
Cdd:cd11055 221 kLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEvLPDDGSPT--YDTVSKLKYLDMVINETLRL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 390 YMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPngEEEKHRHPYAFIPFGIGPRACVG 469
Cdd:cd11055 299 YPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSP--ENKAKRHPYAYLPFGAGPRNCIG 376
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 30683024 470 QRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDYGIILSFKNGVK 515
Cdd:cd11055 377 MRFALLEVKLALVKILQKFRFVPCKETEIPLKLVGGATLSPKNGIY 422
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
47-494 5.56e-82

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: 262.60  E-value: 5.56e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024    47 PGPTAMPLVGHLPLMAKYGP--DVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSP--ISASP 122
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKGNlhSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWfaTSRGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   123 LHKKGLFFTRDKRWSKMRNTilslyqpshltsLIPTMHSF--------ITSATHNLDSK-------PRDIVFSNLFLKLT 187
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRF------------LTPTFTSFgklsfeprVEEEARDLVEKlrktagePGVIDITDLLFRAA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   188 TDIIGQAAFGVDFGLsgkkpIKDVEVTDFInqhvysttqlKMDLSGSLSIILGLLIPILQEPFrqvLKRIPGTMDWRVEK 267
Cdd:pfam00067 150 LNVICSILFGERFGS-----LEDPKFLELV----------KAVQELSSLLSSPSPQLLDLFPI---LKYFPGPHGRKLKR 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   268 TNARLSGQLNEIVSKRAKEAETDSK---DFLSLILKARESDPFAKniFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVS 344
Cdd:pfam00067 212 ARKKIKDLLDKLIEERRETLDSAKKsprDFLDALLLAKEEEDGSK--LTDEELRATVLELFFAGTDTTSSTLSWALYELA 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   345 GHLDVEKRLLQEIDGFGNRDLIPTAHDLQHkFPYLDQVIKEAMRFYMVSP-LVARETAKEVEIGGYLLPKGTWVWLALGV 423
Cdd:pfam00067 290 KHPEVQEKLREEIDEVIGDKRSPTYDDLQN-MPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYA 368
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30683024   424 LAKDPKNFPEPEKFKPERFDPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNyiFRHSL 494
Cdd:pfam00067 369 LHRDPEVFPNPEEFDPERFLD--ENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQN--FEVEL 435
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
77-514 2.90e-76

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: 245.50  E-value: 2.90e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  77 GPIFRFQMGRQPLIIIAEAELCREVgIKKFKDLPNRSIPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTSLI 156
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREV-LRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 157 PTMHSFITSATHNLDSKPRDIVF-SNLFLKLTTDIIGQAAFGVDFglsgkkpikDVEVTDFINQHVYSTTQLKmdlsgsl 235
Cdd:cd00302  80 PVIREIARELLDRLAAGGEVGDDvADLAQPLALDVIARLLGGPDL---------GEDLEELAELLEALLKLLG------- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 236 siilgllipilqepfRQVLKRIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETDSKDFLSLilkaresDPFAKNIFTSD 315
Cdd:cd00302 144 ---------------PRLLRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDLLLLA-------DADDGGGLSDE 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 316 YISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLiptaHDLQHKFPYLDQVIKEAMRFYMVSPL 395
Cdd:cd00302 202 EIVAELLTLLLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDGT----PEDLSKLPYLEAVVEETLRLYPPVPL 277
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 396 VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEekhrHPYAFIPFGIGPRACVGQRFALQ 475
Cdd:cd00302 278 LPRVATEDVELGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREE----PRYAHLPFGAGPHRCLGARLARL 353
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 30683024 476 EIKLTLLHLYRNYIFrHSLEMEIPLQLDYGIILSFKNGV 514
Cdd:cd00302 354 ELKLALATLLRRFDF-ELVPDEELEWRPSLGTLGPASLP 391
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
74-488 3.81e-69

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: 227.79  E-value: 3.81e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  74 KQYGPIFRFQMGRQPLIIIAEAELCREVgikkFK---DLPNRSIPSPISASPLHKK---GLFFTRDKRWSKMRnTILS-- 145
Cdd:cd11054   2 KKYGPIVREKLGGRDIVHLFDPDDIEKV----FRnegKYPIRPSLEPLEKYRKKRGkplGLLNSNGEEWHRLR-SAVQkp 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 146 LYQPSHLTSLIPTMHS----FITSATHNLDSKPRDIV-FSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKDVEvtDFINQ- 219
Cdd:cd11054  77 LLRPKSVASYLPAINEvaddFVERIRRLRDEDGEEVPdLEDELYKWSLESIGTVLFGKRLGCLDDNPDSDAQ--KLIEAv 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 220 HVYSTTQLKMDlsgslsiilgllipilqepFRQVLKRIPGTMDWR-----VEKTNARLSGQLNEIVSKRAKEAETDS--K 292
Cdd:cd11054 155 KDIFESSAKLM-------------------FGPPLWKYFPTPAWKkfvkaWDTIFDIASKYVDEALEELKKKDEEDEeeD 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 293 DFLSLILkaresdpfAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDL 372
Cdd:cd11054 216 SLLEYLL--------SKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDL 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 373 QhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEKHR 452
Cdd:cd11054 288 K-KMPYLKACIKESLRLYPVAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENKNI 366
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 30683024 453 HPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd11054 367 HPFASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNF 402
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
76-514 7.17e-68

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: 225.49  E-value: 7.17e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISASPLhkKGLFFTRDKRWSKMRNTILSLYQPSHLTSL 155
Cdd:cd20649   2 YGPICGYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNRMKANLITKPMS--DSLLCLRDERWKRVRSILTPAFSAAKMKEM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 156 IPtmhsFITSAThnldskprDIVFSNL---------------FLKLTTDIIGQAAFG--VDfglSGKKPikdvevTDFIN 218
Cdd:cd20649  80 VP----LINQAC--------DVLLRNLksyaesgnafniqrcYGCFTMDVVASVAFGtqVD---SQKNP------DDPFV 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 219 QHvySTTQLKMDLSGSLSIILGLLipilqePF--RQVLKRIPgtmdwrvEKTNARLSGQLNEIVSKRAK-----EAETDS 291
Cdd:cd20649 139 KN--CKRFFEFSFFRPILILFLAF------PFimIPLARILP-------NKSRDELNSFFTQCIRNMIAfrdqqSPEERR 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 292 KDFLSLILKARESDPF---------------------------------AKNIFTSDYISAVTYEHLLAGSATTAFTLSS 338
Cdd:cd20649 204 RDFLQLMLDARTSAKFlsvehfdivndadesaydghpnspaneqtkpskQKRMLTEDEIVGQAFIFLIAGYETTTNTLSF 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 339 VLYLVSGHLDVEKRLLQEIDGFGNRDLIPTaHDLQHKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVW 418
Cdd:cd20649 284 ATYLLATHPECQKKLLREVDEFFSKHEMVD-YANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLE 362
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 419 LALGVLAKDPKNFPEPEKFKPERFDPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEI 498
Cdd:cd20649 363 IPVGFLHHDPEHWPEPEKFIPERFTA--EAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEI 440
                       490
                ....*....|....*.
gi 30683024 499 PLQLDYGIILSFKNGV 514
Cdd:cd20649 441 PLQLKSKSTLGPKNGV 456
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
77-516 8.91e-66

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: 218.93  E-value: 8.91e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  77 GPIFRFQMGRQPLIIIAEAE-----LCREVGIKKFKDLpnrsipspisaSPLHK---KGLFFTRDKRWSKMRNTILSLYQ 148
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPEdieviLSSSKLITKSFLY-----------DFLKPwlgDGLLTSTGEKWRKRRKLLTPAFH 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 149 PSHLTSLIPTMH----SFITSATHNLDSKPRDIvfSNLFLKLTTDIIGQAAFGVDFGlsgkkpIKDVEVTDFInQHVYST 224
Cdd:cd20628  70 FKILESFVEVFNenskILVEKLKKKAGGGEFDI--FPYISLCTLDIICETAMGVKLN------AQSNEDSEYV-KAVKRI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 225 TQLkmdlsgslsiilgllipiLQEPFRQVLKRIPGT-----MDWRVEKTNARLSGQLNEIVSKRAKEAETDS-------- 291
Cdd:cd20628 141 LEI------------------ILKRIFSPWLRFDFIfrltsLGKEQRKALKVLHDFTNKVIKERREELKAEKrnseedde 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 292 ------KDFLSLILKARESDpfakNIFTSDYIsavtYEH----LLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-F 360
Cdd:cd20628 203 fgkkkrKAFLDLLLEAHEDG----GPLTDEDI----REEvdtfMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEiF 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 361 GNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPE 440
Cdd:cd20628 275 GDDDRRPTLEDLN-KMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPD 353
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024 441 RFDPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFrHSLEMEIPLQLDYGIILSFKNGVKL 516
Cdd:cd20628 354 RFLP--ENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRV-LPVPPGEDLKLIAEIVLRSKNGIRV 426
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
76-515 6.27e-65

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: 217.02  E-value: 6.27e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISASPLHKKgLFFTRDKRWSKMRNTILSLYQPSHLTSL 155
Cdd:cd11056   2 GEPFVGIYLFRRPALLVRDPELIKQILVKDFAHFHDRGLYSDEKDDPLSAN-LFSLDGEKWKELRQKLTPAFTSGKLKNM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 156 IPTMHS----FITSATHNLDSKPrDIVFSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKDVEVTDFINQHVYSTTQLKMdl 231
Cdd:cd11056  81 FPLMVEvgdeLVDYLKKQAEKGK-ELEIKDLMARYTTDVIASCAFGLDANSLNDPENEFREMGRRLFEPSRLRGLKFM-- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 232 sgslsiilgllipilqepFRQVLKRIPGTMDWRV--EKTNARLSGQLNEIVSKRAKEAETDsKDFLSLILKARESDPFAK 309
Cdd:cd11056 158 ------------------LLFFFPKLARLLRLKFfpKEVEDFFRKLVRDTIEYREKNNIVR-NDFIDLLLELKKKGKIED 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 310 NI----FTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQHKFPYLDQVIKE 385
Cdd:cd11056 219 DKsekeLTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGGELTYEALQEMKYLDQVVNE 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 386 AMRFYMVSPLVARETAKEVEIGG--YLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPngEEEKHRHPYAFIPFGIG 463
Cdd:cd11056 299 TLRKYPPLPFLDRVCTKDYTLPGtdVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSP--ENKKKRHPYTYLPFGDG 376
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 30683024 464 PRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLD-YGIILSFKNGVK 515
Cdd:cd11056 377 PRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPLKLSpKSFVLSPKGGIW 429
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
66-491 6.28e-63

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: 211.61  E-value: 6.28e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  66 PDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKfkDLPnrsiPSPISASPLHK--------KGLFFTRD-KRW 136
Cdd:cd20613   1 HDLLLEWAKEYGPVFVFWILHRPIVVVSDPEAVKEVLITL--NLP----KPPRVYSRLAFlfgerflgNGLVTEVDhEKW 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 137 SKMRNTILSLYQPSHLTSLIPTMHSFITSATHNL----DSKpRDIVFSNLFLKLTTDIIGQAAFGVDFglsgkKPIKDvE 212
Cdd:cd20613  75 KKRRAILNPAFHRKYLKNLMDEFNESADLLVEKLskkaDGK-TEVNMLDEFNRVTLDVIAKVAFGMDL-----NSIED-P 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 213 VTDFINqhvYSTTQLKmdlsgslsiilgllipILQEPFRQVLKRI-PGTMDWRVEKTNA----RLSGQlnEIVSKRaKEA 287
Cdd:cd20613 148 DSPFPK---AISLVLE----------------GIQESFRNPLLKYnPSKRKYRREVREAikflRETGR--ECIEER-LEA 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 288 ----ETDSKDFLSLILKARESDP-FAKNIFTSDYisaVTYehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FG 361
Cdd:cd20613 206 lkrgEEVPNDILTHILKASEEEPdFDMEELLDDF---VTF--FIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEvLG 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 362 NRDLIPTAhDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPER 441
Cdd:cd20613 281 SKQYVEYE-DLG-KLEYLSQVLKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPER 358
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 30683024 442 FDPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR 491
Cdd:cd20613 359 FSP--EAPEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFE 406
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
77-516 8.78e-55

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: 189.33  E-value: 8.78e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  77 GPIFRFQMGRQPLIIIAEAELCREVgikkfkdLPNRSipspisasPLHKKGLFFTRDKR-------------WSKMRNTI 143
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHPDHIQHV-------LVTNA--------RNYVKGGVYERLKLllgnglltsegdlWRRQRRLA 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 144 LSLYQPSHLTSLIPTMhsfiTSATHNL--------DSKPRDIVFSnlFLKLTTDIIGQAAFGVDFGLSGKKpIKDVevTD 215
Cdd:cd20620  66 QPAFHRRRIAAYADAM----VEATAALldrweagaRRGPVDVHAE--MMRLTLRIVAKTLFGTDVEGEADE-IGDA--LD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 216 FINQHVYSttqlkmdlsgslsiilgllipiLQEPFRQVLKRIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAEtDSKDFL 295
Cdd:cd20620 137 VALEYAAR----------------------RMLSPFLLPLWLPTPANRRFRRARRRLDEVIYRLIAERRAAPA-DGGDLL 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 296 SLILKARESDpfaknifTSDYIS-------AVTYehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGF-GNRdlIP 367
Cdd:cd20620 194 SMLLAARDEE-------TGEPMSdqqlrdeVMTL--FLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVlGGR--PP 262
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 368 TAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPngE 447
Cdd:cd20620 263 TAEDLP-QLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTP--E 339
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30683024 448 EEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR----HSLEMEIplqldyGIILSFKNGVKL 516
Cdd:cd20620 340 REAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRlvpgQPVEPEP------LITLRPKNGVRM 406
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
72-517 1.80e-54

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: 189.32  E-value: 1.80e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  72 LAKQYGPIFRFQMGRQPLIIIAE----AELCREvgiKKFKdlpnRSIPSPISA-SPLHKKGLF--FTRDKRWSKMRNTIL 144
Cdd:cd11068   8 LADELGPIFKLTLPGRRVVVVSShdliAELCDE---SRFD----KKVSGPLEElRDFAGDGLFtaYTHEPNWGKAHRILM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 145 SLYQPSHLTSLIPTMHSFITSATHNLDSKPRD--IVFSNLFLKLTTDIIGQAAFGVDFGlSGKKPikdvEVTDFINQHVY 222
Cdd:cd11068  81 PAFGPLAMRGYFPMMLDIAEQLVLKWERLGPDepIDVPDDMTRLTLDTIALCGFGYRFN-SFYRD----EPHPFVEAMVR 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 223 STTQLKMdlsgslsiilgllipilqepfRQVLKRIPGTMDWRVEKTNARLSGQLN----EIVSKRAKEAETDSKDFLSLI 298
Cdd:cd11068 156 ALTEAGR---------------------RANRPPILNKLRRRAKRQFREDIALMRdlvdEIIAERRANPDGSPDDLLNLM 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 299 LKAResDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHdLQhKFPY 378
Cdd:cd11068 215 LNGK--DPETGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPPPYEQ-VA-KLRY 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 379 LDQVIKEAMRFYMVSPLVARETAKEVEIGG-YLLPKGTWVWLALGVLAKDPKNF-PEPEKFKPERFDPngEEEKHRHPYA 456
Cdd:cd11068 291 IRRVLDETLRLWPTAPAFARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLP--EEFRKLPPNA 368
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30683024 457 FIPFGIGPRACVGQRFALQEIKLTLLHLYRNYifrhSLEMEIPLQLDYGIILSFK-NGVKLR 517
Cdd:cd11068 369 WKPFGNGQRACIGRQFALQEATLVLAMLLQRF----DFEDDPDYELDIKETLTLKpDGFRLK 426
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
77-488 8.97e-54

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: 187.14  E-value: 8.97e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  77 GPIFRFQMGRQPLIIIAEAELCREVgIKKFKDLPNRSIPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTSLI 156
Cdd:cd11083   1 GSAYRFRLGRQPVLVISDPELIREV-LRRRPDEFRRISSLESVFREMGINGVFSAEGDAWRRQRRLVMPAFSPKHLRYFF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 157 PTMHSfITSATHNLDSK----PRDIVFSNLFLKLTTDIIGQAAFGVDFGL--SGKKPIKDVEVTDF--INQHVYST---- 224
Cdd:cd11083  80 PTLRQ-ITERLRERWERaaaeGEAVDVHKDLMRYTVDVTTSLAFGYDLNTleRGGDPLQEHLERVFpmLNRRVNAPfpyw 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 225 --TQLKMDLSgslsiilgllipilqepFRQVLKRIPGTMDWRVEKTNARLsgQLNeivSKRAKEAETdskdfLSLILKAR 302
Cdd:cd11083 159 ryLRLPADRA-----------------LDRALVEVRALVLDIIAAARARL--AAN---PALAEAPET-----LLAMMLAE 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 303 ESDpfaKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQHKFPYLDQV 382
Cdd:cd11083 212 DDP---DARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPLLEALDRLPYLEAV 288
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 383 IKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHrHPYAFIPFG 461
Cdd:cd11083 289 ARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWlDGARAAEPH-DPSSLLPFG 367
                       410       420
                ....*....|....*....|....*..
gi 30683024 462 IGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd11083 368 AGPRLCPGRSLALMEMKLVFAMLCRNF 394
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
77-512 1.62e-53

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: 186.26  E-value: 1.62e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  77 GPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIpSPISASPLHKKGLFFTRDKRWSKMRNTILSlyqpsHLTS-- 154
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPL-LPSFEIISGGKGILFSNGDYWKELRRFALS-----SLTKtk 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 155 LIPTMHSFITS---------ATHNLDSKPRDIvfSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKDVevTDFINQHVYSTT 225
Cdd:cd20617  75 LKKKMEELIEEevnklieslKKHSKSGEPFDP--RPYFKKFVLNIINQFLFGKRFPDEDDGEFLKL--VKPIEEIFKELG 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 226 QLKMDLSGSLSiilgllipilQEPFRQVLKRIpgtmdwrvEKTNARLSGQLNEIVSKRAKEAETDS-KDFLSLILKARES 304
Cdd:cd20617 151 SGNPSDFIPIL----------LPFYFLYLKKL--------KKSYDKIKDFIEKIIEEHLKTIDPNNpRDLIDDELLLLLK 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 305 DpFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQhKFPYLDQVIK 384
Cdd:cd20617 213 E-GDSGLFDDDSIISTCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRS-KLPYLNAVIK 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 385 EAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDpngEEEKHRHPYAFIPFGIG 463
Cdd:cd20617 291 EVLRLRPILPLgLPRVTTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFL---ENDGNKLSEQFIPFGIG 367
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 30683024 464 PRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDYGIILSFKN 512
Cdd:cd20617 368 KRNCVGENLARDELFLFFANLLLNFKFKSSDGLPIDEKEVFGLTLKPKP 416
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
76-499 2.10e-51

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: 181.31  E-value: 2.10e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQ--MGRQPLIIIaEAELCREVGIKKFKDLPnRSIPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLT 153
Cdd:cd11069   1 YGGLIRYRglFGSERLLVT-DPKALKHILVTNSYDFE-KPPAFRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 154 SLIPTMHS----FITSATHNLDSKP---RDIVFSNLFLKLTTDIIGQAAFGVDFGlSGKKPikDVEVTDFINQHVYSTTQ 226
Cdd:cd11069  79 ELYPIFWSkaeeLVDKLEEEIEESGdesISIDVLEWLSRATLDIIGLAGFGYDFD-SLENP--DNELAEAYRRLFEPTLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 227 LKMDLSGSLSIilgllipilqepFRQVLKRIPGTMDWRVEKTNARLSGQLNEIVSKR----AKEAETDSKDFLSLILKAR 302
Cdd:cd11069 156 GSLLFILLLFL------------PRWLVRILPWKANREIRRAKDVLRRLAREIIREKkaalLEGKDDSGKDILSILLRAN 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 303 ESDPFAKniFTSDYISA--VTYehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGF--GNRDLIPTAHDLQHkFPY 378
Cdd:cd11069 224 DFADDER--LSDEELIDqiLTF--LAAGHETTSTALTWALYLLAKHPDVQERLREEIRAAlpDPPDGDLSYDDLDR-LPY 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 379 LDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNF-PEPEKFKPERFDPNGEEEKHRHP--- 454
Cdd:cd11069 299 LNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASPGGAgsn 378
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 30683024 455 YAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNyiFRHSLEMEIP 499
Cdd:cd11069 379 YALLTFLHGPRSCIGKKFALAEMKVLLAALVSR--FEFELDPDAE 421
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
277-517 9.49e-50

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: 176.21  E-value: 9.49e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 277 NEIVSKRAKEAETDSK---------DFLSLILKARESDpfaKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHL 347
Cdd:cd20659 182 EEIIKKRRKELEDNKDealskrkylDFLDILLTARDED---GKGLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHP 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 348 DVEKRLLQEIDG-FGNRDliPTAHDLQHKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAK 426
Cdd:cd20659 259 EHQQKCREEVDEvLGDRD--DIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHH 336
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 427 DPKNFPEPEKFKPERFDPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNyiFRHSLEMEIPLQLDYGI 506
Cdd:cd20659 337 NPTVWEDPEEFDPERFLP--ENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRR--FELSVDPNHPVEPKPGL 412
                       250
                ....*....|.
gi 30683024 507 ILSFKNGVKLR 517
Cdd:cd20659 413 VLRSKNGIKLK 423
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
75-517 5.68e-49

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: 174.53  E-value: 5.68e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  75 QYGPIFRFQMGRQPLIIIAEAELCREVGIKK-FKDLPNRSIPSPisASPLhKKGLFFTRDKRWSKMRNTILSLYQPSHLT 153
Cdd:cd20650   1 KYGKVWGIYDGRQPVLAITDPDMIKTVLVKEcYSVFTNRRPFGP--VGFM-KSAISIAEDEEWKRIRSLLSPTFTSGKLK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 154 SLIPTMHSFITSATHNL---DSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGlSGKKP-------IKDVEVTDFINQHVYS 223
Cdd:cd20650  78 EMFPIIAQYGDVLVKNLrkeAEKGKPVTLKDVFGAYSMDVITSTSFGVNID-SLNNPqdpfvenTKKLLKFDFLDPLFLS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 224 TTQLkmdlsgslsiilgllipilqePFrqvLKRIPGTMDWRV--EKTNARLSGQLNEIVSKRAKEAETDSKDFLSLILKA 301
Cdd:cd20650 157 ITVF---------------------PF---LTPILEKLNISVfpKDVTNFFYKSVKKIKESRLDSTQKHRVDFLQLMIDS 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 302 RESDPFAKNIFTSDY-ISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTaHDLQHKFPYLD 380
Cdd:cd20650 213 QNSKETESHKALSDLeILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPT-YDTVMQMEYLD 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 381 QVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPngeEEKHRH-PYAFIP 459
Cdd:cd20650 292 MVVNETLRLFPIAGRLERVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSK---KNKDNIdPYIYLP 368
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30683024 460 FGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDYGIILSFKNGVKLR 517
Cdd:cd20650 369 FGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPCKETQIPLKLSLQGLLQPEKPIVLK 426
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
77-517 5.80e-48

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: 171.63  E-value: 5.80e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  77 GPIFRFQMGRQPLIIIAEAELCREVgikkFKDlpnrsiPSPISASPLHK-----KGLFFTRDKRWSKMRNTILSLYQPSH 151
Cdd:cd11057   1 GSPFRAWLGPRPFVITSDPEIVQVV----LNS------PHCLNKSFFYDffrlgRGLFSAPYPIWKLQRKALNPSFNPKI 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 152 LTSLIPTMHSFITSATHNLDS----KPRDIvfSNLFLKLTTDIIGQAAFGVDFGLsgkKPIKDVEVTDFINQHVYSTTql 227
Cdd:cd11057  71 LLSFLPIFNEEAQKLVQRLDTyvggGEFDI--LPDLSRCTLEMICQTTLGSDVND---ESDGNEEYLESYERLFELIA-- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 228 kmdlsgslsiilgllipilqepfRQVLK---------RIPGtmDWRVEKTNARLSGQ-----LNEIVSKRAKEAETDSKD 293
Cdd:cd11057 144 -----------------------KRVLNpwlhpefiyRLTG--DYKEEQKARKILRAfsekiIEKKLQEVELESNLDSEE 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 294 ----------FLSLILKARESDPfaknIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGN 362
Cdd:cd11057 199 deengrkpqiFIDQLLELARNGE----EFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEvFPD 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 363 RDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIG-GYLLPKGTWVWLALGVLAKDPKNF-PEPEKFKPE 440
Cdd:cd11057 275 DGQFITYEDLQ-QLVYLEMVLKETMRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPD 353
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 441 RFDPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEiPLQLDYGIILSFKNGVKLR 517
Cdd:cd11057 354 NFLP--ERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKTSLRLE-DLRFKFNITLKLANGHLVT 427
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
49-488 1.46e-47

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: 170.07  E-value: 1.46e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  49 PTAMPLVGHLPLMAKYGPDVFSVLAK--QYGPIFRFQMGRQPLIIIAEAELCREVgikkFKD----LPNRSIPSPISASP 122
Cdd:COG2124   2 TATATPAADLPLDPAFLRDPYPFYARlrEYGPVFRVRLPGGGAWLVTRYEDVREV----LRDprtfSSDGGLPEVLRPLP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 123 LHKKGLFFTRDKRWSKMRNTILSLYQPSHLTSLIPTMHSFITSATHNL-DSKPRDIVfsNLFLKLTTDIIGQAAFGVdfg 201
Cdd:COG2124  78 LLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIREIADELLDRLaARGPVDLV--EEFARPLPVIVICELLGV--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 202 lsgkkPIKDVE-VTDFINQHVYSTTqlkmdlsgslsiilgllipilqepfrqvlkRIPGTMDWRVEKTNARLSGQLNEIV 280
Cdd:COG2124 153 -----PEEDRDrLRRWSDALLDALG------------------------------PLPPERRRRARRARAELDAYLRELI 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 281 SKRAKEAETDskdFLSLILKARESDpfakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIdgf 360
Cdd:COG2124 198 AERRAEPGDD---LLSALLAARDDG----ERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP--- 267
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 361 gnrdliptahdlqhkfPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPE 440
Cdd:COG2124 268 ----------------ELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPD 331
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 30683024 441 rfdpngeeekhRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:COG2124 332 -----------RPPNAHLPFGGGPHRCLGAALARLEARIALATLLRRF 368
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
294-516 2.59e-47

cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of vertebrate cytochrome P450 family 4, subfamily V (CYP4V) enzymes and similar proteins, including invertebrate subfamily C (CYP4C). Insect CYP4C enzymes may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. CYP4V2, the most characterized member of the CYP4V subfamily, is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410753 [Multi-domain]  Cd Length: 429  Bit Score: 170.14  E-value: 2.59e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 294 FLSLILKARESDpfakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRDLIPTAHDL 372
Cdd:cd20660 214 FLDLLLEASEEG----TKLSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRiFGDSDRPATMDDL 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 373 qHKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPngEEEKHR 452
Cdd:cd20660 290 -KEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLP--ENSAGR 366
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30683024 453 HPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRhSLEMEIPLQLDYGIILSFKNGVKL 516
Cdd:cd20660 367 HPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIE-SVQKREDLKPAGELILRPVDGIRV 429
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
76-511 3.22e-46

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: 167.00  E-value: 3.22e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRsipspisasPLHKKGLFFTRDKRwskmrNTILSLYQPS----- 150
Cdd:cd11027   1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGR---------PKLFTFDLFSRGGK-----DIAFGDYSPTwklhr 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 151 --------HLTSLIPTMHSFITSATHNL-------DSKPRDIvfSNLFLKLTTDIIGQAAFGVDFGLSgkkpikDVEVTD 215
Cdd:cd11027  67 klahsalrLYASGGPRLEEKIAEEAEKLlkrlasqEGQPFDP--KDELFLAVLNVICSITFGKRYKLD------DPEFLR 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 216 FINQHVYSTTQLKMDLSGSLSiilgllipilqePFrqvLKRIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETDS-KDF 294
Cdd:cd11027 139 LLDLNDKFFELLGAGSLLDIF------------PF---LKYFPNKALRELKELMKERDEILRKKLEEHKETFDPGNiRDL 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 295 LSLILKARES----DPFAKNIFTSDYISAVTYEHLLAGSATTAFTLS-SVLYLVSgHLDVEKRLLQEIDGFGNRDLIPTA 369
Cdd:cd11027 204 TDALIKAKKEaedeGDEDSGLLTDDHLVMTISDIFGAGTETTATTLRwAIAYLVN-YPEVQAKLHAELDDVIGRDRLPTL 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 370 HDlQHKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGe 447
Cdd:cd11027 283 SD-RKRLPYLEATIAEVLRLSSVVPLaLPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFlDENG- 360
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30683024 448 eEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIP-LQLDYGIILSFK 511
Cdd:cd11027 361 -KLVPKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEPPPeLEGIPGLVLYPL 424
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
61-488 7.06e-46

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: 165.92  E-value: 7.06e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  61 MAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREV---GIKKFkdlpnrSIPSPISA-SPLHKKGLFFTRDKRW 136
Cdd:cd11044   6 FLRDPEDFIQSRYQKYGPVFKTHLLGRPTVFVIGAEAVRFIlsgEGKLV------RYGWPRSVrRLLGENSLSLQDGEEH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 137 SKMRNTILSLYQPSHLTSLIPTMHSFITSATHNLDSKPRDIVFSNlFLKLTTDIIGQAAFGVDFGlsgkkpikdVEVTDF 216
Cdd:cd11044  80 RRRRKLLAPAFSREALESYVPTIQAIVQSYLRKWLKAGEVALYPE-LRRLTFDVAARLLLGLDPE---------VEAEAL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 217 inQHVYSTTQLKMDLSgslsiilgllipilqePFRqvlkrIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETDSKDFLS 296
Cdd:cd11044 150 --SQDFETWTDGLFSL----------------PVP-----LPFTPFGRAIRARNKLLARLEQAIRERQEEENAEAKDALG 206
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 297 LILKARESDpfaKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFG-NRDLipTAHDLqHK 375
Cdd:cd11044 207 LLLEAKDED---GEPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGlEEPL--TLESL-KK 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 376 FPYLDQVIKEAMRfyMVSPLVA--RETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEkHRH 453
Cdd:cd11044 281 MPYLDQVIKEVLR--LVPPVGGgfRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSED-KKK 357
                       410       420       430
                ....*....|....*....|....*....|....*
gi 30683024 454 PYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd11044 358 PFSLIPFGGGPRECLGKEFAQLEMKILASELLRNY 392
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
252-492 8.18e-46

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: 165.51  E-value: 8.18e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 252 QVLKRIPGTMDWRVEKTNARLSGQLNEIVSKRaKEAETDSKDFLSLILKARESDPFAkniFTSDYI--SAVTYehLLAGS 329
Cdd:cd11049 160 KFLERLPTPGNRRFDRALARLRELVDEIIAEY-RASGTDRDDLLSLLLAARDEEGRP---LSDEELrdQVITL--LTAGT 233
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 330 ATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRdlIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGG 408
Cdd:cd11049 234 ETTASTLAWAFHLLARHPEVERRLHAELDAvLGGR--PATFEDLP-RLTYTRRVVTEALRLYPPVWLLTRRTTADVELGG 310
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 409 YLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd11049 311 HRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLP--GRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRW 388

                ....
gi 30683024 489 IFRH 492
Cdd:cd11049 389 RLRP 392
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
72-517 1.53e-45

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: 164.68  E-value: 1.53e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  72 LAKQYGPIFRFQM-GRQPLIIIAEAELCREVgikkFKDLPNRSIPSPISaSPLhkKGLFFtrdkrwskmRNTILSLYQPS 150
Cdd:cd11053   7 LRARYGDVFTLRVpGLGPVVVLSDPEAIKQI----FTADPDVLHPGEGN-SLL--EPLLG---------PNSLLLLDGDR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 151 HLTS---LIPTMH--------SFITSATHN-LDSKPRDIVFS--NLFLKLTTDIIGQAAFGVDfglsgkkpiKDVEVTDF 216
Cdd:cd11053  71 HRRRrklLMPAFHgerlraygELIAEITEReIDRWPPGQPFDlrELMQEITLEVILRVVFGVD---------DGERLQEL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 217 InQHVYSTTQLkmdlsgslsiilGLLIPILQEPFRQVLKRIPGtmdW-RVEKTNARLSGQLNEIVSKRAKEAETDSKDFL 295
Cdd:cd11053 142 R-RLLPRLLDL------------LSSPLASFPALQRDLGPWSP---WgRFLRARRRIDALIYAEIAERRAEPDAERDDIL 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 296 SLILKARESDpfaKNIFTSDYIS--AVTYehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEID-GFGNRDLIPTAHDl 372
Cdd:cd11053 206 SLLLSARDED---GQPLSDEELRdeLMTL--LFAGHETTATALAWAFYWLHRHPEVLARLLAELDaLGGDPDPEDIAKL- 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 373 qhkfPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGeeekhR 452
Cdd:cd11053 280 ----PYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRK-----P 350
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30683024 453 HPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDyGIILSFKNGVKLR 517
Cdd:cd11053 351 SPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPERPVRR-GVTLAPSRGVRMV 414
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
74-506 6.06e-44

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: 160.97  E-value: 6.06e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  74 KQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISasPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLT 153
Cdd:cd11052   9 KQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEGYFGKSPLQPGLK--KLLGRGLVMSNGEKWAKHRRIANPAFHGEKLK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 154 SLIPTM----HSFITSATHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFgLSGKKPIKDVEVTDFI----NQHVYStt 225
Cdd:cd11052  87 GMVPAMvesvSDMLERWKKQMGEEGEEVDVFEEFKALTADIISRTAFGSSY-EEGKEVFKLLRELQKIcaqaNRDVGI-- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 226 qlkmdlsgslsiilgllipilqePFRQVLkriPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETD-----SKDFLSLILK 300
Cdd:cd11052 164 -----------------------PGSRFL---PTKGNKKIKKLDKEIEDSLLEIIKKREDSLKMGrgddyGDDLLGLLLE 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 301 ARESDPFAKNIFTSDYISAV-TYehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEI-DGFGNRdlIPTAHDLQhKFPY 378
Cdd:cd11052 218 ANQSDDQNKNMTVQEIVDECkTF--FFAGHETTALLLTWTTMLLAIHPEWQEKAREEVlEVCGKD--KPPSDSLS-KLKT 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 379 LDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPE-PEKFKPERFDpNGEEEKHRHPYAF 457
Cdd:cd11052 293 VSMVINESLRLYPPAVFLTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFA-DGVAKAAKHPMAF 371
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 458 IPFGIGPRACVGQRFALQEIKLTL--------LHLYRNYifRHSLEMEIPLQLDYGI 506
Cdd:cd11052 372 LPFGLGPRNCIGQNFATMEAKIVLamilqrfsFTLSPTY--RHAPTVVLTLRPQYGL 426
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
72-488 7.39e-44

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: 160.18  E-value: 7.39e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  72 LAKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPIsASPLHKKGLFFtRDKRWSKMRNTIL-SLYQPS 150
Cdd:cd11045   6 RYRRYGPVSWTGMLGLRVVALLGPDANQLVLRNRDKAFSSKQGWDPV-IGPFFHRGLML-LDFDEHRAHRRIMqQAFTRS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 151 HLTSLIPTMHSFITSAthnLDSKP--RDIVFSNLFLKLTTDIIGQAAFGVDFGLSGKKpikdvevtdfINQHVYSTTQLK 228
Cdd:cd11045  84 ALAGYLDRMTPGIERA---LARWPtgAGFQFYPAIKELTLDLATRVFLGVDLGPEADK----------VNKAFIDTVRAS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 229 MDLsgslsiilgllipilqepfrqVLKRIPGTMDWRVEKTNARL-SGQLNEIVSKRAKEAEtdskDFLSLILKARESDpf 307
Cdd:cd11045 151 TAI---------------------IRTPIPGTRWWRGLRGRRYLeEYFRRRIPERRAGGGD----DLFSALCRAEDED-- 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 308 aKNIFTSDYISavtyEH----LLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLiptAHDLQHKFPYLDQVI 383
Cdd:cd11045 204 -GDRFSDDDIV----NHmiflMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLALGKGTL---DYEDLGQLEVTDWVF 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 384 KEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEKhRHPYAFIPFGIG 463
Cdd:cd11045 276 KEALRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDK-VHRYAWAPFGGG 354
                       410       420
                ....*....|....*....|....*
gi 30683024 464 PRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd11045 355 AHKCIGLHFAGMEVKAILHQMLRRF 379
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
121-488 1.80e-43

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: 159.39  E-value: 1.80e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 121 SPLHKKGLFFTRDK----RWSKMRNTILS---LYQPSHLTSLIPTMHSFITSATHNlDSKPRDI-VFSnLFLKLTTDIIG 192
Cdd:cd11059  39 RGGGGPNLFSTLDPkehsARRRLLSGVYSkssLLRAAMEPIIRERVLPLIDRIAKE-AGKSGSVdVYP-LFTALAMDVVS 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 193 QAAFGVDFG--LSGKKPIKDVEVTDFINQHVYSTTQLKMDLsgslsiilgllipilqEPFRQVLKRIPGTMDwRVEKTnA 270
Cdd:cd11059 117 HLLFGESFGtlLLGDKDSRERELLRRLLASLAPWLRWLPRY----------------LPLATSRLIIGIYFR-AFDEI-E 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 271 RLSGQLNEIVSKRAKEAETDSKDFLSLILKARESDpfaKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVE 350
Cdd:cd11059 179 EWALDLCARAESSLAESSDSESLTVLLLEKLKGLK---KQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQ 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 351 KRLLQEIDG-FGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVA-RET-AKEVEIGGYLLPKGTWV----WLalgv 423
Cdd:cd11059 256 EKLREELAGlPGPFRGPPDLEDLD-KLPYLNAVIRETLRLYPPIPGSLpRVVpEGGATIGGYYIPGGTIVstqaYS---- 330
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30683024 424 LAKDPKNFPEPEKFKPERF-DPNGEE--EKHRhpyAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd11059 331 LHRDPEVFPDPEEFDPERWlDPSGETarEMKR---AFWPFGSGSRMCIGMNLALMEMKLALAAIYRNY 395
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
127-491 4.48e-42

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: 155.46  E-value: 4.48e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 127 GLFFTRDK----RWSKMRNTILSlyqPSHLTSLIPTMHSFITSATHNLDSKPRD-----IVFSNLFLKLTTDIIGQAAFG 197
Cdd:cd11061  44 LTFTTRDKaehaRRRRVWSHAFS---DKALRGYEPRILSHVEQLCEQLDDRAGKpvswpVDMSDWFNYLSFDVMGDLAFG 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 198 VDFGLSGKKpiKDVEVTDFINQHVYSTTqlkmdlsgslsiilgllipilqePFRQV--LKRIPGTMDWRVEKTNA--RLS 273
Cdd:cd11061 121 KSFGMLESG--KDRYILDLLEKSMVRLG-----------------------VLGHApwLRPLLLDLPLFPGATKArkRFL 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 274 GQLNEIVSKRAKEAETDSKDFLSLILKARESD---PFAKNIFTSDYISAVTyehllAGSATTAFTLSSVLYLVSGHLDVE 350
Cdd:cd11061 176 DFVRAQLKERLKAEEEKRPDIFSYLLEAKDPEtgeGLDLEELVGEARLLIV-----AGSDTTATALSAIFYYLARNPEAY 250
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 351 KRLLQEIDG-FGNRDLIPTAHDLQHkFPYLDQVIKEAMRFYmvsPLVA----RETAKE-VEIGGYLLPKGTWVWLALGVL 424
Cdd:cd11061 251 EKLRAELDStFPSDDEIRLGPKLKS-LPYLRACIDEALRLS---PPVPsglpRETPPGgLTIDGEYIPGGTTVSVPIYSI 326
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 425 AKDPKNFPEPEKFKPERFDPNGEEEKhRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR 491
Cdd:cd11061 327 HRDERYFPDPFEFIPERWLSRPEELV-RARSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFR 392
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
75-490 9.81e-42

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: 155.22  E-value: 9.81e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  75 QYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISaSPLHKKGLFFTRDKRWSKMRntiLSLYQPSHLTS 154
Cdd:cd11046   9 EYGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDKKGLLAEIL-EPIMGKGLIPADGEIWKKRR---RALVPALHKDY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 155 LIPTMHSFITSATH---NLDSKPRDIVFSNL---FLKLTTDIIGQAAFGVDFGlsgkkpikDVEVTDFINQHVYST---- 224
Cdd:cd11046  85 LEMMVRVFGRCSERlmeKLDAAAETGESVDMeeeFSSLTLDIIGLAVFNYDFG--------SVTEESPVIKAVYLPlvea 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 225 TQLKMDLSGSLSIILGLLIPILQEPFRQVLKRIPGTMDWRVEKtnARLSGQLNEIVSKRAKEAETDSKDFLSLILKARES 304
Cdd:cd11046 157 EHRSVWEPPYWDIPAALFIVPRQRKFLRDLKLLNDTLDDLIRK--RKEMRQEEDIELQQEDYLNEDDPSLLRFLVDMRDE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 305 DPFAKNiFTSDYISAvtyehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRdlIPTAHDLQHKFPYLDQVI 383
Cdd:cd11046 235 DVDSKQ-LRDDLMTM-----LIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAvLGDR--LPPTYEDLKKLKYTRRVL 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 384 KEAMRFYMVSPLVARETAKEVEI--GGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGE--EEKHRHPYAFIP 459
Cdd:cd11046 307 NESLRLYPQPPVLIRRAVEDDKLpgGGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFInpPNEVIDDFAFLP 386
                       410       420       430
                ....*....|....*....|....*....|.
gi 30683024 460 FGIGPRACVGQRFALQEIKLTLLHLYRNYIF 490
Cdd:cd11046 387 FGGGPRKCLGDQFALLEATVALAMLLRRFDF 417
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
266-488 1.41e-40

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


Pssm-ID: 410773 [Multi-domain]  Cd Length: 440  Bit Score: 151.84  E-value: 1.41e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 266 EKTNARLSGQLNEIVSKRAKEAETDSKDFLSLILKAreSDPFAKNIFTSDYISAV-TYehLLAGSATTAFTLSSVLYLVS 344
Cdd:cd20680 196 ERAEEMKAEEDKTGDSDGESPSKKKRKAFLDMLLSV--TDEEGNKLSHEDIREEVdTF--MFEGHDTTAAAMNWSLYLLG 271
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 345 GHLDVEKRLLQEIDG-FGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGV 423
Cdd:cd20680 272 SHPEVQRKVHKELDEvFGKSDRPVTMEDLK-KLRYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYA 350
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30683024 424 LAKDPKNFPEPEKFKPERFDPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd20680 351 LHRDPRYFPEPEEFRPERFFP--ENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHF 413
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
74-488 8.07e-40

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: 148.87  E-value: 8.07e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  74 KQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNrSIPSPIsASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHL- 152
Cdd:cd11043   3 KRYGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVS-WYPKSV-RKLLGKSSLLTVSGEEHKRLRGLLLSFLGPEALk 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 153 TSLIPTMHSfITSATHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGvdfglsgkkpIKDVEVTDFInqhvysttqlkmdls 232
Cdd:cd11043  81 DRLLGDIDE-LVRQHLDSWWRGKSVVVLELAKKMTFELICKLLLG----------IDPEEVVEEL--------------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 233 gslsiilgllipilQEPFRQVLK-------RIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETDS--KDFLSLILKARE 303
Cdd:cd11043 135 --------------RKEFQAFLEgllsfplNLPGTTFHRALKARKRIRKELKKIIEERRAELEKASpkGDLLDVLLEEKD 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 304 SDpfaKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGF-----GNRDLipTAHDLQhKFPY 378
Cdd:cd11043 201 ED---GDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIakrkeEGEGL--TWEDYK-SMKY 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 379 LDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEkhrhPYAFI 458
Cdd:cd11043 275 TWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGV----PYTFL 350
                       410       420       430
                ....*....|....*....|....*....|
gi 30683024 459 PFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd11043 351 PFGGGPRLCPGAELAKLEILVFLHHLVTRF 380
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
75-484 5.39e-39

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: 147.22  E-value: 5.39e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  75 QYGPIFRFQMGRQPLIIIAEAELCREVgIK----KFKDLPNRSIPSPISaspLHKKGLFFTR-DKRWSKMRN-TILSLYQ 148
Cdd:cd11072   1 KYGPLMLLRLGSVPTVVVSSPEAAKEV-LKthdlVFASRPKLLAARILS---YGGKDIAFAPyGEYWRQMRKiCVLELLS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 149 PSHLTSLIP-------TMHSFITSAThnldSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKDV---------- 211
Cdd:cd11072  77 AKRVQSFRSireeevsLLVKKIRESA----SSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQDKFKELvkealellgg 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 212 -EVTDFInqhvysttqlkmdlsgslsiilgllipilqePFrqvLKRIP--GTMDWRVEKTNARLSGQLNEIV-----SKR 283
Cdd:cd11072 153 fSVGDYF-------------------------------PS---LGWIDllTGLDRKLEKVFKELDAFLEKIIdehldKKR 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 284 AKEAETDSKDFLSLILKARESDPFAkniFTSDYISAVTYEHLLAGSATTAFTLSSVL-YLVSgHLDVEKRLLQEIDG-FG 361
Cdd:cd11072 199 SKDEDDDDDDLLDLRLQKEGDLEFP---LTRDNIKAIILDMFLAGTDTSATTLEWAMtELIR-NPRVMKKAQEEVREvVG 274
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 362 NRDLIpTAHDLQhKFPYLDQVIKEAMRFYMVSP-LVARETAKEVEIGGYLLPKGTWV----WlALGvlaKDPKNFPEPEK 436
Cdd:cd11072 275 GKGKV-TEEDLE-KLKYLKAVIKETLRLHPPAPlLLPRECREDCKINGYDIPAKTRVivnaW-AIG---RDPKYWEDPEE 348
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 30683024 437 FKPERFDPNGEEEKHRHpYAFIPFGIGPRACVGQRFALQEIKLTLLHL 484
Cdd:cd11072 349 FRPERFLDSSIDFKGQD-FELIPFGAGRRICPGITFGLANVELALANL 395
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
323-488 9.51e-38

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: 143.65  E-value: 9.51e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 323 EHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETA- 401
Cdd:cd20646 240 ELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIA-KMPLLKAVIKETLRLYPVVPGNARVIVe 318
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 402 KEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGeEEKHrHPYAFIPFGIGPRACVGQRFALQEIKLTL 481
Cdd:cd20646 319 KEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDG-GLKH-HPFGSIPFGYGVRACVGRRIAELEMYLAL 396

                ....*..
gi 30683024 482 LHLYRNY 488
Cdd:cd20646 397 SRLIKRF 403
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
79-516 9.66e-38

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: 143.55  E-value: 9.66e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  79 IFRFQMGRQPLIIIAEAELCREV-----GIKKFKDLPNRSIpspisaspLHKKGLFFTRDKRWSKMRNtILSlyQPSH-- 151
Cdd:cd20621   5 IIVSNLGSKPLISLVDPEYIKEFlqnhhYYKKKFGPLGIDR--------LFGKGLLFSEGEEWKKQRK-LLS--NSFHfe 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 152 -LTSLIPTMHSFITSATHNLDSKPRDIVfsNLFLKLTTDIIGQAAFGVDFG---LSGKKPIkdVEVTDFINQHVYSTT-- 225
Cdd:cd20621  74 kLKSRLPMINEITKEKIKKLDNQNVNII--QFLQKITGEVVIRSFFGEEAKdlkINGKEIQ--VELVEILIESFLYRFss 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 226 ---QLKMdlSGSLSIILGLLIPILQEPFRQVLKRIPGTMDWRVEKTNARLSGQLNEIvskrakeaETDSKDFLSLILKAR 302
Cdd:cd20621 150 pyfQLKR--LIFGRKSWKLFPTKKEKKLQKRVKELRQFIEKIIQNRIKQIKKNKDEI--------KDIIIDLDLYLLQKK 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 303 ESDPfakNIFTSDYIS-AVTYehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQhKFPYLDQ 381
Cdd:cd20621 220 KLEQ---EITKEEIIQqFITF--FFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQ-KLNYLNA 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 382 VIKEAMRFYMVSP-LVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFdpNGEEEKHRHPYAFIPF 460
Cdd:cd20621 294 FIKEVLRLYNPAPfLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERW--LNQNNIEDNPFVFIPF 371
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 461 GIGPRACVGQRFALQEIKLTLLHLYRNYifrhslEMEIP----LQLDYGIILSFKNGVKL 516
Cdd:cd20621 372 SAGPRNCIGQHLALMEAKIILIYILKNF------EIEIIpnpkLKLIFKLLYEPVNDLLL 425
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
186-488 2.21e-37

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: 142.34  E-value: 2.21e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 186 LTTDIIGQAAFGVDFG-LSGKKPikdVEVTDFINQHVYSTT--QLKMDLSGSLSIILGLLIPILQEPFRQVLKripgtmd 262
Cdd:cd11058 111 TTFDIIGDLAFGESFGcLENGEY---HPWVALIFDSIKALTiiQALRRYPWLLRLLRLLIPKSLRKKRKEHFQ------- 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 263 WRVEKTNARLsgqlneivskrakEAETDSKDFLSLILKAREsdpfAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYL 342
Cdd:cd11058 181 YTREKVDRRL-------------AKGTDRPDFMSYILRNKD----EKKGLTREELEANASLLIIAGSETTATALSGLTYY 243
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 343 VSGHLDVEKRLLQEIdgfgnRDLIPTAHDL----QHKFPYLDQVIKEAMRFYmvsPLVA----RETAKE-VEIGGYLLPK 413
Cdd:cd11058 244 LLKNPEVLRKLVDEI-----RSAFSSEDDItldsLAQLPYLNAVIQEALRLY---PPVPaglpRVVPAGgATIDGQFVPG 315
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 414 GTWVWLALGVLAKDPKNFPEPEKFKPERF--DPNGEEEKHRHPyAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd11058 316 GTSVSVSQWAAYRSPRNFHDPDEFIPERWlgDPRFEFDNDKKE-AFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNF 391
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
168-488 2.01e-36

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: 140.16  E-value: 2.01e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 168 HNLDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKDVEVTDFINQHVYSTTQLKMdlsgslsiilgllipilq 247
Cdd:cd11070  95 EQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHDTLNAIKLAIFPPLFLNF------------------ 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 248 ePFRQVLKRIPGTMDWRVEKTNARLSGQLNEIVSKRaKEAETDSKDFLSLILKARESDPFAKNIFTSDYISAVTYEHLLA 327
Cdd:cd11070 157 -PFLDRLPWVLFPSRKRAFKDVDEFLSELLDEVEAE-LSADSKGKQGTESVVASRLKRARRSGGLTEKELLGNLFIFFIA 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 328 GSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRDLIPTAHDLQHKFPYLDQVIKEAMRFYMVSPLVARETAKEVEI 406
Cdd:cd11070 235 GHETTANTLSFALYLLAKHPEVQDWLREEIDSvLGDEPDDWDYEEDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVV 314
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 407 -----GGYLLPKGTWVWLALGVLAKDPKN-FPEPEKFKPERFDPNGEE---EKHRHPY--AFIPFGIGPRACVGQRFALQ 475
Cdd:cd11070 315 itglgQEIVIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWGSTSGEigaATRFTPArgAFIPFSAGPRACLGRKFALV 394
                       330
                ....*....|...
gi 30683024 476 EIKLTLLHLYRNY 488
Cdd:cd11070 395 EFVAALAELFRQY 407
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
74-508 3.40e-36

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: 139.47  E-value: 3.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  74 KQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNrsiPSPISAS--PLHKKGLFFTRDKRWSKMRNTILSLYQPSH 151
Cdd:cd20640   9 KQYGPIFTYSTGNKQFLYVSRPEMVKEINLCVSLDLGK---PSYLKKTlkPLFGGGILTSNGPHWAHQRKIIAPEFFLDK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 152 LTSLIPTMhsfITSATHNLDS----------KPRDIVFSNLFLKLTTDIIGQAAFGVDFglsgkkpIKDVEVTDFINQhv 221
Cdd:cd20640  86 VKGMVDLM---VDSAQPLLSSweeridraggMAADIVVDEDLRAFSADVISRACFGSSY-------SKGKEIFSKLRE-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 222 ystTQLKMDLsgslsiilgllipilqepfRQVLKRIPGtmdWRVEKTNA-----RLSGQLN----EIVSKRaKEAETDSK 292
Cdd:cd20640 154 ---LQKAVSK-------------------QSVLFSIPG---LRHLPTKSnrkiwELEGEIRslilEIVKER-EEECDHEK 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 293 DFLSLILKARESDPFAK---NIFTSDYISAVtyehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEI-DGFGNRdliPT 368
Cdd:cd20640 208 DLLQAILEGARSSCDKKaeaEDFIVDNCKNI----YFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVlEVCKGG---PP 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 369 AHDLQHKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNF-PEPEKFKPERFDpNGE 447
Cdd:cd20640 281 DADSLSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFS-NGV 359
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 448 EEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIF------RHSLEMEIPLQLDYGIIL 508
Cdd:cd20640 360 AAACKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLILSKFSFtlspeyQHSPAFRLIVEPEFGVRL 426
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
269-509 4.38e-36

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: 138.89  E-value: 4.38e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 269 NARLSGQLNEIVSK-RAKEAETDSKDFLSLILKARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLS-SVLYLVSgH 346
Cdd:cd20651 177 NQKLIEFLKEEIKEhKKTYDEDNPRDLIDAYLREMKKKEPPSSSFTDDQLVMICLDLFIAGSETTSNTLGfAFLYLLL-N 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 347 LDVEKRLLQEIDGFGNRDLIPTAHDlQHKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLA 425
Cdd:cd20651 256 PEVQRKVQEEIDEVVGRDRLPTLDD-RSKLPYTEAVILEVLRIFTLVPIgIPHRALKDTTLGGYRIPKDTTILASLYSVH 334
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 426 KDPKNFPEPEKFKPERF-DPNGEEEKHRHpyaFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIPL-QLD 503
Cdd:cd20651 335 MDPEYWGDPEEFRPERFlDEDGKLLKDEW---FLPFGAGKRRCLGESLARNELFLFFTGLLQNFTFSPPNGSLPDLeGIP 411

                ....*.
gi 30683024 504 YGIILS 509
Cdd:cd20651 412 GGITLS 417
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
270-491 9.79e-36

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: 137.73  E-value: 9.79e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 270 ARLSGQLNEIVSKRAKEAETDSKDFLSLILKARESDPFAkniFTSDYISAVTYEHLLAGSATTAFTLS-SVLYLVSgHLD 348
Cdd:cd11042 169 AKLKEIFSEIIQKRRKSPDKDEDDMLQTLMDAKYKDGRP---LTDDEIAGLLIALLFAGQHTSSATSAwTGLELLR-NPE 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 349 VEKRLLQEIDG-FGNRDLIPTAHDLqHKFPYLDQVIKEAMRFYMVSPLVARETAK--EVEIGGYLLPKGTWVWLALGVLA 425
Cdd:cd11042 245 HLEALREEQKEvLGDGDDPLTYDVL-KEMPLLHACIKETLRLHPPIHSLMRKARKpfEVEGGGYVIPKGHIVLASPAVSH 323
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024 426 KDPKNFPEPEKFKPERFDPNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR 491
Cdd:cd11042 324 RDPEIFKNPDEFDPERFLKGRAEDSKGGKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFE 389
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
128-488 3.74e-35

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: 136.56  E-value: 3.74e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 128 LFFTRDKRW-SKMRNTILSLYQPSHLTSLIPTMHSFITSATHNLDSKPRDIVFSNLFLKL---TTDIIGQAAFGVDFGL- 202
Cdd:cd11060  48 LFSERDEKRhAALRRKVASGYSMSSLLSLEPFVDECIDLLVDLLDEKAVSGKEVDLGKWLqyfAFDVIGEITFGKPFGFl 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 203 -SGKkpikDVEvtDFI----NQHVYSTTQLKMDlsgslsiilgllipilqePFRQVLKRIPGTMDWRVEKTNARLSGQLN 277
Cdd:cd11060 128 eAGT----DVD--GYIasidKLLPYFAVVGQIP------------------WLDRLLLKNPLGPKRKDKTGFGPLMRFAL 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 278 EIVSKR---AKEAETDSKDFLSLILKARESDPfakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLL 354
Cdd:cd11060 184 EAVAERlaeDAESAKGRKDMLDSFLEAGLKDP---EKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLR 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 355 QEIDGFGNRDLIPT--AHDLQHKFPYLDQVIKEAMRFYMVSPLV-ARETAKE-VEIGGYLLPKGTWV----WlalgVLAK 426
Cdd:cd11060 261 AEIDAAVAEGKLSSpiTFAEAQKLPYLQAVIKEALRLHPPVGLPlERVVPPGgATICGRFIPGGTIVgvnpW----VIHR 336
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30683024 427 DPKNF-PEPEKFKPERFDPNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd11060 337 DKEVFgEDADVFRPERWLEADEEQRRMMDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRF 399
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
76-475 9.31e-35

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: 135.40  E-value: 9.31e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRsiPSPISASPLHKKGLFFTR---DKRWSKMRNTILSLYQPSHL 152
Cdd:cd11065   1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSR--PRMPMAGELMGWGMRLLLmpyGPRWRLHRRLFHQLLNPSAV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 153 TSLIPTMHSFITSATHNLDSKPRDivFSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKDVE-VTDFINQHVYSTTQLkMDL 231
Cdd:cd11065  79 RKYRPLQELESKQLLRDLLESPDD--FLDHIRRYAASIILRLAYGYRVPSYDDPLLRDAEeAMEGFSEAGSPGAYL-VDF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 232 SgslsiilgllipilqePFrqvLKRIPGTMD--W-RVEKTNARLSGQLNEIVSKRAKEAETDSKD---FLSLILKARESD 305
Cdd:cd11065 156 F----------------PF---LRYLPSWLGapWkRKARELRELTRRLYEGPFEAAKERMASGTAtpsFVKDLLEELDKE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 306 PfAKNIFTSDYISAVTYEhllAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQHkFPYLDQVIKE 385
Cdd:cd11065 217 G-GLSEEEIKYLAGSLYE---AGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPN-LPYVNAIVKE 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 386 AMRFYMVSPL-VARETAKEVEIGGYLLPKGTWV----WlALGvlaKDPKNFPEPEKFKPERFDPNGEEEKHRHPYAFIPF 460
Cdd:cd11065 292 VLRWRPVAPLgIPHALTEDDEYEGYFIPKGTTVipnaW-AIH---HDPEVYPDPEEFDPERYLDDPKGTPDPPDPPHFAF 367
                       410
                ....*....|....*
gi 30683024 461 GIGPRACVGQRFALQ 475
Cdd:cd11065 368 GFGRRICPGRHLAEN 382
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
75-495 2.23e-34

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: 134.50  E-value: 2.23e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  75 QYGPIFRFQMGRQPLIIIAEAELCREVGIKKFkDLPNRSIPSPISASpLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTS 154
Cdd:cd20641  10 QYGETFLYWQGTTPRICISDHELAKQVLSDKF-GFFGKSKARPEILK-LSGKGLVFVNGDDWVRHRRVLNPAFSMDKLKS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 155 LIPTMHS-----FITSATHNLDSKPRDIV--FSNLFLKLTTDIIGQAAFGVDFglsgkkpIKDVEVtdFINQH----VYS 223
Cdd:cd20641  88 MTQVMADctermFQEWRKQRNNSETERIEveVSREFQDLTADIIATTAFGSSY-------AEGIEV--FLSQLelqkCAA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 224 TTQLKMDLsgslsiilgllipilqePFRQVLKRIPGTMDWRVEKTnarLSGQLNEIVSKRAKEAETD-SKDFLSLILKAR 302
Cdd:cd20641 159 ASLTNLYI-----------------PGTQYLPTPRNLRVWKLEKK---VRNSIKRIIDSRLTSEGKGyGDDLLGLMLEAA 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 303 ESDPFAKNIFTSDYISAVTYE---HLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAhDLQHKFPYL 379
Cdd:cd20641 219 SSNEGGRRTERKMSIDEIIDEcktFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDA-DTLSKLKLM 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 380 DQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNF-PEPEKFKPERFDpNGEEEKHRHPYAFI 458
Cdd:cd20641 298 NMVLMETLRLYGPVINIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFA-NGVSRAATHPNALL 376
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 30683024 459 PFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLE 495
Cdd:cd20641 377 SFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLSPE 413
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
74-493 2.61e-34

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: 134.11  E-value: 2.61e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  74 KQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNrsipspISASPLHKK----GLFFTRDKRWSKMRNTILSLYQP 149
Cdd:cd20639   9 KIYGKTFLYWFGPTPRLTVADPELIREILLTRADHFDR------YEAHPLVRQlegdGLVSLRGEKWAHHRRVITPAFHM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 150 SHLTSLIPTMhsfITSATHNLDsKPRDIVFSN---------LFLKLTTDIIGQAAFGVDFGlSGKkpikdvevtdfinqH 220
Cdd:cd20639  83 ENLKRLVPHV---VKSVADMLD-KWEAMAEAGgegevdvaeWFQNLTEDVISRTAFGSSYE-DGK--------------A 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 221 VYSTTQLKMdlsgslsiilglliPILQEPFRQVLkrIPG---------TMDWRVEKTNARLSGQLNEIVSKRA--KEAET 289
Cdd:cd20639 144 VFRLQAQQM--------------LLAAEAFRKVY--IPGyrflptkknRKSWRLDKEIRKSLLKLIERRQTAAddEKDDE 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 290 DSKDFLSLILKARESDPFAKniFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQE-IDGFGNRDLiPT 368
Cdd:cd20639 208 DSKDLLGLMISAKNARNGEK--MTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREvLAVCGKGDV-PT 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 369 AHDLQhKFPYLDQVIKEAMRFYmvSPLVA--RETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNF-PEPEKFKPERFDpN 445
Cdd:cd20639 285 KDHLP-KLKTLGMILNETLRLY--PPAVAtiRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFA-D 360
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 30683024 446 GEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHS 493
Cdd:cd20639 361 GVARAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRLS 408
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
75-484 2.06e-33

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: 131.60  E-value: 2.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  75 QYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISasplhkkgLFFTRDKR----------WSKMRNTIL 144
Cdd:cd11075   1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLR--------VLFSSNKHmvnsspygplWRTLRRNLV 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 145 S-LYQPSHLTSLIPT----MHSFIT-----SATHNLDSKPRDI----VFSnLFLKLttdiigqaAFGVDfglSGKKPIKD 210
Cdd:cd11075  73 SeVLSPSRLKQFRPArrraLDNLVErlreeAKENPGPVNVRDHfrhaLFS-LLLYM--------CFGER---LDEETVRE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 211 VEVTdfINQHVYSTTQLKMDLSGSLSIILgllipilqePFRQVLKRIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETD 290
Cdd:cd11075 141 LERV--QRELLLSFTDFDVRDFFPALTWL---------LNRRRWKKVLELRRRQEEVLLPLIRARRKRRASGEADKDYTD 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 291 SKDFLSLILKARESdpfaKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAH 370
Cdd:cd11075 210 FLLLDLLDLKEEGG----ERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEE 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 371 DLqHKFPYLDQVIKEAMRFYM-VSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEE 449
Cdd:cd11075 286 DL-PKMPYLKAVVLETLRRHPpGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAA 364
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 30683024 450 KHRHP---YAFIPFGIGPRACVGqrfalqeIKLTLLHL 484
Cdd:cd11075 365 DIDTGskeIKMMPFGAGRRICPG-------LGLATLHL 395
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
73-493 2.68e-33

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: 131.58  E-value: 2.68e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  73 AKQYGPIFRFQMGRQPLIIIAEAELCREV--------------GIKKFKDLPNRSipspisasplhkKGLFFTRDKRWSK 138
Cdd:cd20647   1 TREYGKIFKSHFGPQFVVSIADRDMVAQVlraegaapqranmeSWQEYRDLRGRS------------TGLISAEGEQWLK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 139 MRNTILS-LYQPSHLTSLIPTMHSFIT---SATHNLDSKPRD----IVFSNLFLKLTTDIIGQAAFGVDFG-LSGKKPIK 209
Cdd:cd20647  69 MRSVLRQkILRPRDVAVYSGGVNEVVAdliKRIKTLRSQEDDgetvTNVNDLFFKYSMEGVATILYECRLGcLENEIPKQ 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 210 DVEVTDFInQHVYSTTQLKMdlsgSLSIILGLLIPILQEPFRQVLKRIPGTMDWrvekTNARLSGQLNEIvSKRAKEAET 289
Cdd:cd20647 149 TVEYIEAL-ELMFSMFKTTM----YAGAIPKWLRPFIPKPWEEFCRSWDGLFKF----SQIHVDNRLREI-QKQMDRGEE 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 290 DSKDFLSLILKAREsdpfakniFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTA 369
Cdd:cd20647 219 VKGGLLTYLLVSKE--------LTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTA 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 370 HDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEE 449
Cdd:cd20647 291 EDVP-KLPLIRALLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALD 369
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 30683024 450 KHRHpYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHS 493
Cdd:cd20647 370 RVDN-FGSIPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIKVS 412
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
77-488 5.98e-33

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: 130.37  E-value: 5.98e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  77 GPIFRFQMGRQPLIIIAEAELCREVgikkFK--DLPNRSIPSPISASPL--HKKGLFFTR-DKRWSKMR-NTILSLYQPS 150
Cdd:cd20618   1 GPLMYLRLGSVPTVVVSSPEMAKEV----LKtqDAVFASRPRTAAGKIFsyNGQDIVFAPyGPHWRHLRkICTLELFSAK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 151 HLTSLIPT----MHSFITSaTHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFglSGKKPIKDVEVTDFINqhvysttq 226
Cdd:cd20618  77 RLESFQGVrkeeLSHLVKS-LLEESESGKPVNLREHLSDLTLNNITRMLFGKRY--FGESEKESEEAREFKE-------- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 227 lkmdlsgslsiilgllipILQEPFRQVLKRIPGT-------MDW-----RVEKTNARLSGQLNEIV-----SKRAKEAET 289
Cdd:cd20618 146 ------------------LIDEAFELAGAFNIGDyipwlrwLDLqgyekRMKKLHAKLDRFLQKIIeehreKRGESKKGG 207
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 290 DSKDFLSLILkaresDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTA 369
Cdd:cd20618 208 DDDDDLLLLL-----DLDGEGKLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEE 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 370 HDLQhKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEE 448
Cdd:cd20618 283 SDLP-KLPYLQAVVKETLRLHPPGPLlLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDID 361
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 30683024 449 E-KHRHpYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd20618 362 DvKGQD-FELLPFGSGRRMCPGMPLGLRMVQLTLANLLHGF 401
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
272-499 2.01e-32

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: 129.27  E-value: 2.01e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 272 LSGQLNEIVSKRAKEA--ETDSKDFLSLILKARESDPFAKniFTSDY-ISAVTYEHLLAGSATTAFTLSSVLYLVSGHLD 348
Cdd:cd20654 196 LEEWLEEHRQKRSSSGksKNDEDDDDVMMLSILEDSQISG--YDADTvIKATCLELILGGSDTTAVTLTWALSLLLNNPH 273
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 349 VEKRLLQEIDGFGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVA-RETAKEVEIGGYLLPKGTWVWLALGVLAKD 427
Cdd:cd20654 274 VLKKAQEELDTHVGKDRWVEESDIK-NLVYLQAIVKETLRLYPPGPLLGpREATEDCTVGGYHVPKGTRLLVNVWKIQRD 352
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30683024 428 PKNFPEPEKFKPERF-DPNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYrnyifrHSLEMEIP 499
Cdd:cd20654 353 PNVWSDPLEFKPERFlTTHKDIDVRGQNFELIPFGSGRRSCPGVSFGLQVMHLTLARLL------HGFDIKTP 419
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
76-491 2.04e-32

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: 128.83  E-value: 2.04e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSiPSPISASPLHKKGLFFTRDKRWSKMRNTILSlyqpshltsl 155
Cdd:cd11026   1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRP-PVPLFDRVTKGYGVVFSNGERWKQLRRFSLT---------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 156 ipTMHSF----------ITSATHNL-----DSKPRDIVFSNLFLKLTTDIIGQAAFGVDFglsgkkpikDVEVTDFIN-- 218
Cdd:cd11026  70 --TLRNFgmgkrsieerIQEEAKFLveafrKTKGKPFDPTFLLSNAVSNVICSIVFGSRF---------DYEDKEFLKll 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 219 QHVYSTTQLkmdlsgslsiiLGLLIPILQEPFRQVLKRIPGTmdwrvEKTNARLSGQLNEIVSKRAKEAETD-----SKD 293
Cdd:cd11026 139 DLINENLRL-----------LSSPWGQLYNMFPPLLKHLPGP-----HQKLFRNVEEIKSFIRELVEEHRETldpssPRD 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 294 FL-SLILKARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDl 372
Cdd:cd11026 203 FIdCFLLKMEKEKDNPNSEFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLED- 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 373 QHKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEK 450
Cdd:cd11026 282 RAKMPYTDAVIHEVQRFGDIVPLgVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFlDEQGKFKK 361
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 30683024 451 HRhpyAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR 491
Cdd:cd11026 362 NE---AFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLS 399
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
279-488 4.66e-32

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: 127.62  E-value: 4.66e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 279 IVSKRAKEAETDSKDFLSLIlkaresdpFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEID 358
Cdd:cd20645 197 IDKRLQRYSQGPANDFLCDI--------YHDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQ 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 359 GFGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFK 438
Cdd:cd20645 269 SVLPANQTPRAEDLK-NMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFK 347
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 30683024 439 PERFdpngEEEKHR-HPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd20645 348 PERW----LQEKHSiNPFAHVPFGIGKRMCIGRRLAELQLQLALCWIIQKY 394
PLN02687 PLN02687
flavonoid 3'-monooxygenase
47-483 2.32e-31

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 127.23  E-value: 2.32e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   47 PGPTAMPLVGHLPLMAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCRE---VGIKKFKDLPNRSIPSPISASpl 123
Cdd:PLN02687  37 PGPRGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQflrTHDANFSNRPPNSGAEHMAYN-- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  124 HKKGLFFTRDKRWSKMRN-TILSLYQPSHLTSLIPTMHSFITSATHNLDSKPRD--IVFSNLFLKLTTDIIGQAA----- 195
Cdd:PLN02687 115 YQDLVFAPYGPRWRALRKiCAVHLFSAKALDDFRHVREEEVALLVRELARQHGTapVNLGQLVNVCTTNALGRAMvgrrv 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  196 FGVDFGlSGKKPIKDVEVTDFINQHVYSTTQlkmdlsgslsiilgllipilqepFRQVLKRI-PGTMDWRVEKTNARLSG 274
Cdd:PLN02687 195 FAGDGD-EKAREFKEMVVELMQLAGVFNVGD-----------------------FVPALRWLdLQGVVGKMKRLHRRFDA 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  275 QLNEIVSKRAKEAETDS---KDFLSLILKARESDPFA--KNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDV 349
Cdd:PLN02687 251 MMNGIIEEHKAAGQTGSeehKDLLSTLLALKREQQADgeGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDI 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  350 EKRLLQEIDGFGNRDLIPTAHDLQHkFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDP 428
Cdd:PLN02687 331 LKKAQEELDAVVGRDRLVSESDLPQ-LTYLQAVIKETFRLHPSTPLsLPRMAAEECEINGYHIPKGATLLVNVWAIARDP 409
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024  429 KNFPEPEKFKPERFDPNGEeekhrHP--------YAFIPFGIGPRACVGQRFALQEIKL---TLLH 483
Cdd:PLN02687 410 EQWPDPLEFRPDRFLPGGE-----HAgvdvkgsdFELIPFGAGRRICAGLSWGLRMVTLltaTLVH 470
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
325-515 1.00e-30

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: 123.82  E-value: 1.00e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 325 LLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKE- 403
Cdd:cd11063 225 LLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLK-NMKYLRAVINETLRLYPPVPLNSRVAVRDt 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 404 -VEIGG-------YLLPKGTWVWLALGVLAKDPKNF-PEPEKFKPERFdpngeEEKHRHPYAFIPFGIGPRACVGQRFAL 474
Cdd:cd11063 304 tLPRGGgpdgkspIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERW-----EDLKRPGWEYLPFNGGPRICLGQQFAL 378
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30683024 475 QEIKLTLLHLYRNYifrHSLEM--EIPLQLDYGIILSFKNGVK 515
Cdd:cd11063 379 TEASYVLVRLLQTF---DRIESrdVRPPEERLTLTLSNANGVK 418
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
282-481 2.13e-30

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: 123.09  E-value: 2.13e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 282 KRAKEAETDSKDFLSLILKAREsDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGF- 360
Cdd:cd20655 195 KRKKRKEGGSKDLLDILLDAYE-DENAEYKITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVv 273
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 361 GNRDLIPTAhDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPE 440
Cdd:cd20655 274 GKTRLVQES-DLP-NLPYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPE 351
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 30683024 441 RFDPNG----EEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTL 481
Cdd:cd20655 352 RFLASSrsgqELDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTAI 396
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
76-509 3.70e-30

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: 122.21  E-value: 3.70e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSiPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQ-----PS 150
Cdd:cd20662   1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRP-ETPLRERIFNKNGLIFSSGQTWKEQRRFALMTLRnfglgKK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 151 HLTSLIPTMHSFITSATHNLDSKPRDIVFSnlFLKLTTDIIGQAAFGVDFglsgkkpikDVEVTDF------INQHVY-- 222
Cdd:cd20662  80 SLEERIQEECRHLVEAIREEKGNPFNPHFK--INNAVSNIICSVTFGERF---------EYHDEWFqellrlLDETVYle 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 223 --STTQLkmdlsgslsiilgllipilQEPFRQVLKRIPGTMDwRVEKTNARLSGQLNEIVSKRAKEAETD-SKDFLSLIL 299
Cdd:cd20662 149 gsPMSQL-------------------YNAFPWIMKYLPGSHQ-TVFSNWKKLKLFVSDMIDKHREDWNPDePRDFIDAYL 208
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 300 KARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDlQHKFPYL 379
Cdd:cd20662 209 KEMAKYPDPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLAD-RESMPYT 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 380 DQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEKHRhpyAFI 458
Cdd:cd20662 288 NAVIHEVQRMGNIIPLnVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQFKKRE---AFL 364
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 30683024 459 PFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDYGIILS 509
Cdd:cd20662 365 PFSMGKRACLGEQLARSELFIFFTSLLQKFTFKPPPNEKLSLKFRMGITLS 415
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
266-481 1.78e-29

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: 120.02  E-value: 1.78e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 266 EKTNARLSGQLNEIVSKRAKEAETDSKDFLSLilkaRESDPfakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSG 345
Cdd:cd20653 184 KRRDAFLQGLIDEHRKNKESGKNTMIDHLLSL----QESQP---EYYTDEIIKGLILVMLLAGTDTSAVTLEWAMSNLLN 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 346 HLDVEKRLLQEIDG-FGNRDLIpTAHDLQhKFPYLDQVIKEAMRFYMVSP-LVARETAKEVEIGGYLLPKGTWVWLALGV 423
Cdd:cd20653 257 HPEVLKKAREEIDTqVGQDRLI-EESDLP-KLPYLQNIISETLRLYPAAPlLVPHESSEDCKIGGYDIPRGTMLLVNAWA 334
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30683024 424 LAKDPKNFPEPEKFKPERFdpngeEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTL 481
Cdd:cd20653 335 IHRDPKLWEDPTKFKPERF-----EGEEREGYKLIPFGLGRRACPGAGLAQRVVGLAL 387
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
76-490 2.11e-29

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


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 119.90  E-value: 2.11e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSiPSPISASPLHKKGLFFTRDKRWSKMRN-TILSLY-----QP 149
Cdd:cd20671   1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRP-PIPIFQAIQHGNGVFFSSGERWRTTRRfTVRSMKslgmgKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 150 SHLTSLIPTMhSFITSATHNLDSKPRDIvfsNLFLKLTTDIIGQAAFGVDFGLsgKKPIKdVEVTDFINQHVysttqLKM 229
Cdd:cd20671  80 TIEDKILEEL-QFLNGQIDSFNGKPFPL---RLLGWAPTNITFAMLFGRRFDY--KDPTF-VSLLDLIDEVM-----VLL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 230 DLSGSLSIILGLLIPILQEPFRQVLKRIpgtmdwrvEKTNARLSGQLNEivsKRAKEAETDSKDFLSLILKARESDPFAK 309
Cdd:cd20671 148 GSPGLQLFNLYPVLGAFLKLHKPILDKV--------EEVCMILRTLIEA---RRPTIDGNPLHSYIEALIQKQEEDDPKE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 310 NIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDlQHKFPYLDQVIKEAMRF 389
Cdd:cd20671 217 TLFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYED-RKALPYTSAVIHEVQRF 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 390 YMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHRhpyAFIPFGIGPRACV 468
Cdd:cd20671 296 ITLLPHVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFlDAEGKFVKKE---AFLPFSAGRRVCV 372
                       410       420
                ....*....|....*....|..
gi 30683024 469 GQRFALQEIKLTLLHLYRNYIF 490
Cdd:cd20671 373 GESLARTELFIFFTGLLQKFTF 394
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
282-517 2.23e-29

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: 120.07  E-value: 2.23e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 282 KRAKEAETDSK----DFLSLILKARESDpfaKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEI 357
Cdd:cd20678 204 QDEGELEKIKKkrhlDFLDILLFAKDEN---GKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEI 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 358 DG-FGNRDLIpTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEI-GGYLLPKGTWVWLALGVLAKDPKNFPEPE 435
Cdd:cd20678 281 REiLGDGDSI-TWEHLD-QMPYTTMCIKEALRLYPPVPGISRELSKPVTFpDGRSLPAGITVSLSIYGLHHNPAVWPNPE 358
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 436 KFKPERFDPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIK----LTLLHlyrnyiFRHSLEMEIPLQLDYGIILSFK 511
Cdd:cd20678 359 VFDPLRFSP--ENSSKRHSHAFLPFSAGPRNCIGQQFAMNEMKvavaLTLLR------FELLPDPTRIPIPIPQLVLKSK 430

                ....*.
gi 30683024 512 NGVKLR 517
Cdd:cd20678 431 NGIHLY 436
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
280-481 2.64e-29

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: 119.86  E-value: 2.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 280 VSKRAKEAETDSKDFLSLILkARESDPfAKNIFtsdyiSAVTyEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG 359
Cdd:cd20648 206 VAAKLPRGEAIEGKYLTYFL-AREKLP-MKSIY-----GNVT-ELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITA 277
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 360 FGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAK-EVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFK 438
Cdd:cd20648 278 ALKDNSVPSAADVA-RMPLLKAVVKEVLRLYPVIPGNARVIPDrDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFR 356
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30683024 439 PERFdpNGEEEKHrHPYAFIPFGIGPRACVGQRFALQEIKLTL 481
Cdd:cd20648 357 PERW--LGKGDTH-HPYASLPFGFGKRSCIGRRIAELEVYLAL 396
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
182-513 2.66e-29

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


Pssm-ID: 410687 [Multi-domain]  Cd Length: 432  Bit Score: 120.00  E-value: 2.66e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 182 LFLKLTTDIIGQAAFGVDFG-LSGKKPikDVEVT---DFINQHVYSTTQlkmdlsgslsiilgllipilqePFRQV--LK 255
Cdd:cd11064 110 VLQRFTFDVICKIAFGVDPGsLSPSLP--EVPFAkafDDASEAVAKRFI----------------------VPPWLwkLK 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 256 RIPGTMDWRVEKTNAR-LSGQLNEIVSKR------AKEAETDSKDFLSLILKARESDPF-AKNIFTSDyiSAVTYehLLA 327
Cdd:cd11064 166 RWLNIGSEKKLREAIRvIDDFVYEVISRRreelnsREEENNVREDLLSRFLASEEEEGEpVSDKFLRD--IVLNF--ILA 241
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 328 GSATTAFTLSSVLYLVSGHLDVEKRLLQEID-----GFGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAK 402
Cdd:cd11064 242 GRDTTAAALTWFFWLLSKNPRVEEKIREELKsklpkLTTDESRVPTYEELK-KLVYLHAALSESLRLYPPVPFDSKEAVN 320
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 403 E-VEIGGYLLPKGTWVWL---ALG----VLAKDPknfpepEKFKPERF-DPNGEEeKHRHPYAFIPFGIGPRACVGQRFA 473
Cdd:cd11064 321 DdVLPDGTFVKKGTRIVYsiyAMGrmesIWGEDA------LEFKPERWlDEDGGL-RPESPYKFPAFNAGPRICLGKDLA 393
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 30683024 474 LQEIKLTLLHLYRNYifrhSLEMEIPLQL--DYGIILSFKNG 513
Cdd:cd11064 394 YLQMKIVAAAILRRF----DFKVVPGHKVepKMSLTLHMKGG 431
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
88-490 2.72e-29

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: 119.28  E-value: 2.72e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  88 PLIIIAEAELCREVGIKK--FKDLPNRSIPSPIsaspLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTSLIPTMHSFITS 165
Cdd:cd11051  11 PLLVVTDPELAEQITQVTnlPKPPPLRKFLTPL----TGGSSLISMEGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVEI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 166 ATHNLDSKPR-DIVFS--NLFLKLTTDIIGQAAFGVDFGlsgkkpikdvevtdfiNQHVYSTTQLKMDLSGSlsiilgll 242
Cdd:cd11051  87 FAAILRELAEsGEVFSleELTTNLTFDVIGRVTLDIDLH----------------AQTGDNSLLTALRLLLA-------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 243 ipilqePFRQVLKRIPGTMDWRVEKTnARLSGQLNeivskrakeaetdskDFLSLILKAResdpFAKNiFTSDYISAVty 322
Cdd:cd11051 143 ------LYRSLLNPFKRLNPLRPLRR-WRNGRRLD---------------RYLKPEVRKR----FELE-RAIDQIKTF-- 193
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 323 ehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FG-----NRDLIPTAHDLQHKFPYLDQVIKEAMRFYMVSpLV 396
Cdd:cd11051 194 --LFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEvFGpdpsaAAELLREGPELLNQLPYTTAVIKETLRLFPPA-GT 270
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 397 ARETAKEVEI----GGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEKHRHPYAFIPFGIGPRACVGQRF 472
Cdd:cd11051 271 ARRGPPGVGLtdrdGKEYPTDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHELYPPKSAWRPFERGPRNCIGQEL 350
                       410
                ....*....|....*...
gi 30683024 473 ALQEIKLTLLHLYRNYIF 490
Cdd:cd11051 351 AMLELKIILAMTVRRFDF 368
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
127-491 2.82e-29

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: 119.67  E-value: 2.82e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 127 GLFFTRDKRWSKMRNTILS-LYQPSHLTSLIPTMHSFIT---SATHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGL 202
Cdd:cd11062  45 STFSTVDHDLHRLRRKALSpFFSKRSILRLEPLIQEKVDklvSRLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGY 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 203 SGKKPIKdVEVTDFINQHVYSTTQLKMDlsgslsiilgllipilqePF-RQVLKRIPgtmDWRVEKTNARLSG--QLNEI 279
Cdd:cd11062 125 LDEPDFG-PEFLDALRALAEMIHLLRHF------------------PWlLKLLRSLP---ESLLKRLNPGLAVflDFQES 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 280 VSKRAKEAetdskdflslilkARESDPFAKNIFTSDYISAVTYEHL------------------LAGSATTAFTLSSVLY 341
Cdd:cd11062 183 IAKQVDEV-------------LRQVSAGDPPSIVTSLFHALLNSDLppsektlerladeaqtliGAGTETTARTLSVATF 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 342 LVSGHLDVEKRLLQEIDG-FGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMV----SPLVARETAkeVEIGGYLLPKGTW 416
Cdd:cd11062 250 HLLSNPEILERLREELKTaMPDPDSPPSLAELE-KLPYLTAVIKEGLRLSYGvptrLPRVVPDEG--LYYKGWVIPPGTP 326
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024 417 VWLALGVLAKDPKNFPEPEKFKPER-FDPNGEEEKHRHpyaFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR 491
Cdd:cd11062 327 VSMSSYFVHHDEEIFPDPHEFRPERwLGAAEKGKLDRY---LVPFSKGSRSCLGINLAYAELYLALAALFRRFDLE 399
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
76-491 1.08e-28

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: 118.10  E-value: 1.08e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISASpLHKKGLFFTRDKRWSKMRNTILSLYQ-----PS 150
Cdd:cd20670   1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIERN-FQGHGVALANGERWRILRRFSLTILRnfgmgKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 151 HLTSLIPTMHSFITSATHNLDSKPRDIVFsnlFLKLT-TDIIGQAAFGVDFglsgkkpikDVEVTDFINQhvysttqLKM 229
Cdd:cd20670  80 SIEERIQEEAGYLLEEFRKTKGAPIDPTF---FLSRTvSNVISSVVFGSRF---------DYEDKQFLSL-------LRM 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 230 dlsgslsiiLGLLIPILQEPFRQVLKRIPGTMDWRVEKTNA--RLSGQLNEIVSKRAK--EAETDS---KDFLSLIL--- 299
Cdd:cd20670 141 ---------INESFIEMSTPWAQLYDMYSGIMQYLPGRHNRiyYLIEELKDFIASRVKinEASLDPqnpRDFIDCFLikm 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 300 KARESDPFAKniFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDlQHKFPYL 379
Cdd:cd20670 212 HQDKNNPHTE--FNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDD-RVKMPYT 288
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 380 DQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHRhpyAF 457
Cdd:cd20670 289 DAVIHEIQRLTDIVPLgVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFlDEQGRFKKNE---AF 365
                       410       420       430
                ....*....|....*....|....*....|....
gi 30683024 458 IPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR 491
Cdd:cd20670 366 VPFSSGKRVCLGEAMARMELFLYFTSILQNFSLR 399
PTZ00404 PTZ00404
cytochrome P450; Provisional
47-521 3.25e-28

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 117.52  E-value: 3.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   47 PGPTAMPLVGHLPLMAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNR-SIPSPISASPLHk 125
Cdd:PTZ00404  32 KGPIPIPILGNLHQLGNLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRpKIPSIKHGTFYH- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  126 kGLFFTRDKRWSKMRNTILSLYQPSHLT-----------SLIPTMHSFITSathnldSKPRDIVFsnLFLKLTTDIIGQA 194
Cdd:PTZ00404 111 -GIVTSSGEYWKRNREIVGKAMRKTNLKhiydllddqvdVLIESMKKIESS------GETFEPRY--YLTKFTMSAMFKY 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  195 AFGVDFGLSGK-KPIKDVEVTDFINQHVYSTTQLKMdlsgslsiilGLLIPILQEPFRQVLkripgtmdwrvEKTNARLS 273
Cdd:PTZ00404 182 IFNEDISFDEDiHNGKLAELMGPMEQVFKDLGSGSL----------FDVIEITQPLYYQYL-----------EHTDKNFK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  274 GQLNEIVSKRAKEAET----DSKDFLSLILKARESDPfAKNIFTsdyISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDV 349
Cdd:PTZ00404 241 KIKKFIKEKYHEHLKTidpeVPRDLLDLLIKEYGTNT-DDDILS---ILATILDFFLAGVDTSATSLEWMVLMLCNYPEI 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  350 EKRLLQEI-DGFGNRDLIpTAHDLQhKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIG-GYLLPKGTWVWLALGVLAK 426
Cdd:PTZ00404 317 QEKAYNEIkSTVNGRNKV-LLSDRQ-STPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIGgGHFIPKDAQILINYYSLGR 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  427 DPKNFPEPEKFKPERFdpngeeEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDYGI 506
Cdd:PTZ00404 395 NEKYFENPEQFDPSRF------LNPDSNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGKKIDETEEYGL 468
                        490
                 ....*....|....*
gi 30683024  507 ILSfKNGVKLRTIKR 521
Cdd:PTZ00404 469 TLK-PNKFKVLLEKR 482
PLN02183 PLN02183
ferulate 5-hydroxylase
24-499 3.01e-27

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 114.95  E-value: 3.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   24 FLTFAAVVIVIYLYRPSWSVCNVPGPTAMPLVGHLPLMAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREVGI 103
Cdd:PLN02183  16 LILISLFLFLGLISRLRRRLPYPPGPKGLPIIGNMLMMDQLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQ 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  104 KKFKDLPNRSIPSPISASPLHKKGLFFTR-DKRWSKMRN----TILSLYQPSHLTSLIPTMHSFITSATHNLdSKPRDIv 178
Cdd:PLN02183  96 VQDSVFSNRPANIAISYLTYDRADMAFAHyGPFWRQMRKlcvmKLFSRKRAESWASVRDEVDSMVRSVSSNI-GKPVNI- 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  179 fSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKDVE----------VTDFINQHVYSTTQlkmdlsgslsiilgllipilqe 248
Cdd:PLN02183 174 -GELIFTLTRNITYRAAFGSSSNEGQDEFIKILQefsklfgafnVADFIPWLGWIDPQ---------------------- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  249 PFRQVLKRIPGTMDWRVEKT-NARLSGQLNEIVSKRAKEAETDSKD----FLSLILKARESDPFAKNI-FTSDYISAVTY 322
Cdd:PLN02183 231 GLNKRLVKARKSLDGFIDDIiDDHIQKRKNQNADNDSEEAETDMVDdllaFYSEEAKVNESDDLQNSIkLTRDNIKAIIM 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  323 EHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQE-IDGFG-NRDLipTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARET 400
Cdd:PLN02183 311 DVMFGGTETVASAIEWAMAELMKSPEDLKRVQQElADVVGlNRRV--EESDLE-KLTYLKCTLKETLRLHPPIPLLLHET 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  401 AKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHRHpYAFIPFGIGPRACVGQRFALQEIKL 479
Cdd:PLN02183 388 AEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFlKPGVPDFKGSH-FEFIPFGSGRRSCPGMQLGLYALDL 466
                        490       500
                 ....*....|....*....|
gi 30683024  480 TLLHLYrnyifrHSLEMEIP 499
Cdd:PLN02183 467 AVAHLL------HCFTWELP 480
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
76-484 4.26e-27

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: 113.35  E-value: 4.26e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRsipspisasPLHKKGLFFTR---DKRWS-------KMRNT-IL 144
Cdd:cd20656   1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADR---------HRTRSAARFSRngqDLIWAdygphyvKVRKLcTL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 145 SLYQPSHLTSLIP-------TMHSFITSATHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKD-VEVTDF 216
Cdd:cd20656  72 ELFTPKRLESLRPiredevtAMVESIFNDCMSPENEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEQgVEFKAI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 217 INQHVYSTTQLKMdlsgslsiilgllipILQEPFrqvLKRIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETD--SKDF 294
Cdd:cd20656 152 VSNGLKLGASLTM---------------AEHIPW---LRWMFPLSEKAFAKHGARRDRLTKAIMEEHTLARQKSggGQQH 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 295 LSLILKARESDPFaknifTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQH 374
Cdd:cd20656 214 FVALLTLKEQYDL-----SEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQ 288
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 375 kFPYLDQVIKEAMRFYMVSPLVARETAKE-VEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFdpnGEEEK--H 451
Cdd:cd20656 289 -LPYLQCVVKEALRLHPPTPLMLPHKASEnVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERF---LEEDVdiK 364
                       410       420       430
                ....*....|....*....|....*....|...
gi 30683024 452 RHPYAFIPFGIGPRACVGQRFALQEIKLTLLHL 484
Cdd:cd20656 365 GHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHL 397
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
73-483 4.84e-27

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: 113.40  E-value: 4.84e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  73 AKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISASPLHKKGLFFT-RDKRWSKMRnTILS--LYQP 149
Cdd:cd11073   1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPpYGPRWRMLR-KICTteLFSP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 150 SHLTSLIPT-------MHSFItsATHNLDSKPRDI---VFSNLFlklttDIIGQAAFGVDFGLSGKKPIKDVEvtdfinQ 219
Cdd:cd11073  80 KRLDATQPLrrrkvreLVRYV--REKAGSGEAVDIgraAFLTSL-----NLISNTLFSVDLVDPDSESGSEFK------E 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 220 HVYSTTQLKMdlsgslsiilgllipilqEP----FRQVLKRipgtMDW-----RVEKTNARLSGQLNEIVSKRAKE---A 287
Cdd:cd11073 147 LVREIMELAG------------------KPnvadFFPFLKF----LDLqglrrRMAEHFGKLFDIFDGFIDERLAEreaG 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 288 ETDSKDFLSLILKARESDpfAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVL-YLVSgHLDVEKRLLQEIDGFGNRDLI 366
Cdd:cd11073 205 GDKKKDDDLLLLLDLELD--SESELTRNHIKALLLDLFVAGTDTTSSTIEWAMaELLR-NPEKMAKARAELDEVIGKDKI 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 367 PTAHDLqHKFPYLDQVIKEAMRFYMVSP-LVARETAKEVEIGGYLLPKGTWV----WlALGvlaKDPKNFPEPEKFKPER 441
Cdd:cd11073 282 VEESDI-SKLPYLQAVVKETLRLHPPAPlLLPRKAEEDVEVMGYTIPKGTQVlvnvW-AIG---RDPSVWEDPLEFKPER 356
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 30683024 442 FDPNGEEEKHRHpYAFIPFGIGPRACVGQRFALQEIKL---TLLH 483
Cdd:cd11073 357 FLGSEIDFKGRD-FELIPFGSGRRICPGLPLAERMVHLvlaSLLH 400
PLN02966 PLN02966
cytochrome P450 83A1
19-491 5.05e-27

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 114.07  E-value: 5.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   19 EALIAFLTFAAVVIVIYLYRPSWSVCNVP-GPTAMPLVGHLPLMAKYGPD-VFSVLAKQYGPIFRFQMGRQPLIIIAEAE 96
Cdd:PLN02966   3 DIIIGVVALAAVLLFFLYQKPKTKRYKLPpGPSPLPVIGNLLQLQKLNPQrFFAGWAKKYGPILSYRIGSRTMVVISSAE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   97 LCREVGIKKFKDLPNRsipspisasPLHKKGLFFTRDKrwskmRNTILSLYQP----------SHL---TSLIPTMHSFI 163
Cdd:PLN02966  83 LAKELLKTQDVNFADR---------PPHRGHEFISYGR-----RDMALNHYTPyyreirkmgmNHLfspTRVATFKHVRE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  164 TSATHNLDS------KPRDIVFSNLFLKLTTDIIGQAAFGVDFGLSGKkpikdvEVTDFInQHVYSTTQLKMDLSGSLSI 237
Cdd:PLN02966 149 EEARRMMDKinkaadKSEVVDISELMLTFTNSVVCRQAFGKKYNEDGE------EMKRFI-KILYGTQSVLGKIFFSDFF 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  238 ilgllipilqePFRQVLKRIPGT---MDWRVEKTNARLSGQLNEIVSKRAKEAETDSkdFLSLILKARESDPFAKNiFTS 314
Cdd:PLN02966 222 -----------PYCGFLDDLSGLtayMKECFERQDTYIQEVVNETLDPKRVKPETES--MIDLLMEIYKEQPFASE-FTV 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  315 DYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEI-DGFGNRDLIPTAHDLQHKFPYLDQVIKEAMRFYMVS 393
Cdd:PLN02966 288 DNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVrEYMKEKGSTFVTEDDVKNLPYFRALVKETLRIEPVI 367
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  394 P-LVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNF-PEPEKFKPERFdPNGEEEKHRHPYAFIPFGIGPRACVGQR 471
Cdd:PLN02966 368 PlLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERF-LEKEVDFKGTDYEFIPFGSGRRMCPGMR 446
                        490       500
                 ....*....|....*....|
gi 30683024  472 FALQEIKLTLLHLYRNYIFR 491
Cdd:PLN02966 447 LGAAMLEVPYANLLLNFNFK 466
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
248-497 2.63e-26

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: 111.04  E-value: 2.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 248 EPFRQVLKRIPGTMDWRVEKTNArlsgqLNEIVSKRAKEAET-----DSKDFL-SLILKARESDPFAKNIFTSDYISAVT 321
Cdd:cd20668 157 EMFSSVMKHLPGPQQQAFKELQG-----LEDFIAKKVEHNQRtldpnSPRDFIdSFLIRMQEEKKNPNTEFYMKNLVMTT 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 322 YEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDlQHKFPYLDQVIKEAMRFYMVSPL-VARET 400
Cdd:cd20668 232 LNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFED-RAKMPYTEAVIHEIQRFGDVIPMgLARRV 310
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 401 AKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHRhpyAFIPFGIGPRACVGQRFALQEIKL 479
Cdd:cd20668 311 TKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFlDDKGQFKKSD---AFVPFSIGKRYCFGEGLARMELFL 387
                       250
                ....*....|....*...
gi 30683024 480 TLLHLYRNYIFRHSLEME 497
Cdd:cd20668 388 FFTTIMQNFRFKSPQSPE 405
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
76-483 2.74e-26

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: 111.24  E-value: 2.74e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKK---FKDLPN----RSIPSPISASplhkkglFFTRDKRWSKMRNTILSlyq 148
Cdd:cd11028   1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQgedFAGRPDfysfQFISNGKSMA-------FSDYGPRWKLHRKLAQN--- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 149 pshltslipTMHSFITSATHN-------------------LDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGLSGKKPIK 209
Cdd:cd11028  71 ---------ALRTFSNARTHNpleehvteeaeelvtelteNNGKPGPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFLE 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 210 DVEVTDFINQHVYSTTQLKMDLSGSLSIILGLLIpilqepFRQVLKRIPGTMDWRVEktnarlsgqlnEIVSKRAKEAET 289
Cdd:cd11028 142 LVKSNDDFGAFVGAGNPVDVMPWLRYLTRRKLQK------FKELLNRLNSFILKKVK-----------EHLDTYDKGHIR 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 290 DSKDflSLILKARESDPFAK--NIFTSDYISAVTYEHLLAGSATTAFTLS-SVLYLVSgHLDVEKRLLQEIDGFGNRDLI 366
Cdd:cd11028 205 DITD--ALIKASEEKPEEEKpeVGLTDEHIISTVQDLFGAGFDTISTTLQwSLLYMIR-YPEIQEKVQAELDRVIGRERL 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 367 PTAHDLQHkFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DP 444
Cdd:cd11028 282 PRLSDRPN-LPYTEAFILETMRHSSFVPFtIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFlDD 360
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 30683024 445 NGEEEKHRHPyAFIPFGIGPRACVGQRFALQEIKL---TLLH 483
Cdd:cd11028 361 NGLLDKTKVD-KFLPFGAGRRRCLGEELARMELFLffaTLLQ 401
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
276-508 1.03e-25

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: 109.33  E-value: 1.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 276 LNEIVSKRAKEAETDS-KDFLSLILKARESdPFAKNIFTSDYISAVTYEHLL--------AGSATTAFTLS-SVLYLVSg 345
Cdd:cd20673 184 LQKKLEEHKEKFSSDSiRDLLDALLQAKMN-AENNNAGPDQDSVGLSDDHILmtvgdifgAGVETTTTVLKwIIAFLLH- 261
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 346 HLDVEKRLLQEIDGFGNRDLIPTAHDLQHkFPYLDQVIKEAMRFYMVSPLVARETA-KEVEIGGYLLPKGTWVWLALGVL 424
Cdd:cd20673 262 NPEVQKKIQEEIDQNIGFSRTPTLSDRNH-LPLLEATIREVLRIRPVAPLLIPHVAlQDSSIGEFTIPKGTRVVINLWAL 340
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 425 AKDPKNFPEPEKFKPERF-DPNGeeeKHRH--PYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRnyifRHSLEM----E 497
Cdd:cd20673 341 HHDEKEWDQPDQFMPERFlDPTG---SQLIspSLSYLPFGAGPRVCLGEALARQELFLFMAWLLQ----RFDLEVpdggQ 413
                       250
                ....*....|..
gi 30683024 498 IP-LQLDYGIIL 508
Cdd:cd20673 414 LPsLEGKFGVVL 425
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
279-488 1.60e-25

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: 108.60  E-value: 1.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 279 IVSKRAK----EAETDSKDFLS-LILKARESDPFAKNIftsdyiSAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRL 353
Cdd:cd20616 188 IEQKRRRistaEKLEDHMDFATeLIFAQKRGELTAENV------NQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAI 261
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 354 LQEIDG-FGNRDliPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPkNFP 432
Cdd:cd20616 262 LKEIQTvLGERD--IQNDDLQ-KLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFP 337
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 433 EPEKFKPERFDPNgeeekhrHPYA-FIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd20616 338 KPNEFTLENFEKN-------VPSRyFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRF 387
PLN02738 PLN02738
carotene beta-ring hydroxylase
76-521 2.66e-25

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 110.00  E-value: 2.66e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   76 YGPIFRFQMGRQPLIIIAEAELCREVgikkFKDlPNRSIPSPISASPLH---KKGLFFTRDKRWSKMRNTILSLYQPSHL 152
Cdd:PLN02738 164 YGGIFRLTFGPKSFLIVSDPSIAKHI----LRD-NSKAYSKGILAEILEfvmGKGLIPADGEIWRVRRRAIVPALHQKYV 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  153 TSLIptmhSFITSATHNL-------DSKPRDIVFSNLFLKLTTDIIGQAAFGVDF-GLSGKKPIkdVEVtdfinqhVYST 224
Cdd:PLN02738 239 AAMI----SLFGQASDRLcqkldaaASDGEDVEMESLFSRLTLDIIGKAVFNYDFdSLSNDTGI--VEA-------VYTV 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  225 TQLKMDLSGSLSIILGLLIPILQEPfRQVlkripgtmdwRVEKTNARLSGQLNEIVS--KRAKEAE--------TDSKD- 293
Cdd:PLN02738 306 LREAEDRSVSPIPVWEIPIWKDISP-RQR----------KVAEALKLINDTLDDLIAicKRMVEEEelqfheeyMNERDp 374
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  294 -FLSLILKAreSDPFAKNIFTSDYISAvtyehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRdlIPTAHD 371
Cdd:PLN02738 375 sILHFLLAS--GDDVSSKQLRDDLMTM-----LIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSvLGDR--FPTIED 445
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  372 LQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF---DPNGEE 448
Cdd:PLN02738 446 MK-KLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpldGPNPNE 524
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30683024  449 EKHRhpYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEiPLQLDYGIILSFKNGVKLRTIKR 521
Cdd:PLN02738 525 TNQN--FSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQLAPGAP-PVKMTTGATIHTTEGLKMTVTRR 594
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
279-509 2.68e-25

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: 108.33  E-value: 2.68e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 279 IVSKRAKEAETDSKDFLSLIL--KARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQE 356
Cdd:cd20666 189 IADHRETLDPANPRDFIDMYLlhIEEEQKNNAESSFNEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAE 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 357 IDGFGNRDLIPTAHDlQHKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPE 435
Cdd:cd20666 269 IDTVIGPDRAPSLTD-KAQMPFTEATIMEVQRMTVVVPLsIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPD 347
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024 436 KFKPERF-DPNGEEEKHRhpyAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIP-LQLDYGIILS 509
Cdd:cd20666 348 DFMPSRFlDENGQLIKKE---AFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNAPKPsMEGRFGLTLA 420
PLN02655 PLN02655
ent-kaurene oxidase
43-469 3.75e-25

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 108.29  E-value: 3.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   43 VCNVPGptaMPLVGHLPLMAKYGP-DVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIPSPISAs 121
Cdd:PLN02655   1 VPAVPG---LPVIGNLLQLKEKKPhRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTV- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  122 plhkkglfFTRDKR---------WSKM--RNTILSLYQPS---HLTSLIPTMHSFITSATHN-LDSKP------RDIVFS 180
Cdd:PLN02655  77 --------LTRDKSmvatsdygdFHKMvkRYVMNNLLGANaqkRFRDTRDMLIENMLSGLHAlVKDDPhspvnfRDVFEN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  181 NLF-LKLttdiigQAAFGVD--------FGLS-GKKPIKDVEVTDFINQHVysttqlKMDlsgslsiilgllipilQEPF 250
Cdd:PLN02655 149 ELFgLSL------IQALGEDvesvyveeLGTEiSKEEIFDVLVHDMMMCAI------EVD----------------WRDF 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  251 RQVLKRIPG-TMDWRVEKTNARLSGQLNEIVSKRAK-----EAETDSKDFLSLilkaresdpfAKNIFTSDYISAVTYEH 324
Cdd:PLN02655 201 FPYLSWIPNkSFETRVQTTEFRRTAVMKALIKQQKKriargEERDCYLDFLLS----------EATHLTDEQLMMLVWEP 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  325 LLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIpTAHDLQhKFPYLDQVIKEAMRFYMVSPLV-ARETAKE 403
Cdd:PLN02655 271 IIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDERV-TEEDLP-NLPYLNAVFHETLRKYSPVPLLpPRFVHED 348
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024  404 VEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFdpNGEEEKHRHPYAFIPFGIGPRACVG 469
Cdd:PLN02655 349 TTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERF--LGEKYESADMYKTMAFGAGKRVCAG 412
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
280-488 5.08e-25

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


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 107.35  E-value: 5.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 280 VSKRAKEAE-----TDSKDFLS-LILKARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRL 353
Cdd:cd20665 184 ILEKVKEHQesldvNNPRDFIDcFLIKMEQEKHNQQSEFTLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKV 263
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 354 LQEIDGFGNRDLIPTAHDLQHkFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFP 432
Cdd:cd20665 264 QEEIDRVIGRHRSPCMQDRSH-MPYTDAVIHEIQRYIDLVPNnLPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFP 342
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 433 EPEKFKPERF-DPNGEEEKHRHpyaFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd20665 343 NPEKFDPGHFlDENGNFKKSDY---FMPFSAGKRICAGEGLARMELFLFLTTILQNF 396
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
253-479 5.48e-25

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


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 107.09  E-value: 5.48e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 253 VLKRIPGTMDwRVEKTNARLSGQLNEIVSKRAKEAE--------TDSkdFLSLILKARESdpfAKNIFTSDYISAVTYEH 324
Cdd:cd20663 165 VLLRIPGLAG-KVFPGQKAFLALLDELLTEHRTTWDpaqpprdlTDA--FLAEMEKAKGN---PESSFNDENLRLVVADL 238
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 325 LLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDlQHKFPYLDQVIKEAMRFYMVSPL-VARETAKE 403
Cdd:cd20663 239 FSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMAD-QARMPYTNAVIHEVQRFGDIVPLgVPHMTSRD 317
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 404 VEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHRhpyAFIPFGIGPRACVGQRFALQEIKL 479
Cdd:cd20663 318 IEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFlDAQGHFVKPE---AFMPFSAGRRACLGEPLARMELFL 391
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
77-485 8.53e-25

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: 106.68  E-value: 8.53e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  77 GPIFRFQMGRQPLIIIAEAELCREVgIKKFKDLPNRSI-------PSPISASPLHKKGLFFTRDkRWSKMRNTIL-SLYQ 148
Cdd:cd11040  12 GPIFTIRLGGQKIYVITDPELISAV-FRNPKTLSFDPIvivvvgrVFGSPESAKKKEGEPGGKG-LIRLLHDLHKkALSG 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 149 PSHLTSLIPTMHSFITSATHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGlsgkkpikdvEVTDFINQHVYSTTQlK 228
Cdd:cd11040  90 GEGLDRLNEAMLENLSKLLDELSLSGGTSTVEVDLYEWLRDVLTRATTEALFG----------PKLPELDPDLVEDFW-T 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 229 MDLSgslsiilgllipilqepFRQVLKRIPGTMDWRVEKTNARLSGQLneivsKRAKEAETDSKDFLSLILKAREsDPFA 308
Cdd:cd11040 159 FDRG-----------------LPKLLLGLPRLLARKAYAARDRLLKAL-----EKYYQAAREERDDGSELIRARA-KVLR 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 309 KNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEID-GFGNRDLIPTAHDLQHKF---PYLDQVIK 384
Cdd:cd11040 216 EAGLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEpAVTPDSGTNAILDLTDLLtscPLLDSTYL 295
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 385 EAMRFYMVSPlVARETAKE-VEIGGYLLPKGTWVWLALGVLAKDPKNF-PEPEKFKPERF-DPNGEEEKHRHPYAFIPFG 461
Cdd:cd11040 296 ETLRLHSSST-SVRLVTEDtVLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlKKDGDKKGRGLPGAFRPFG 374
                       410       420
                ....*....|....*....|....*..
gi 30683024 462 IGPRACVGQRFALQEIKL---TLLHLY 485
Cdd:cd11040 375 GGASLCPGRHFAKNEILAfvaLLLSRF 401
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
76-491 1.08e-24

cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members are selectively expressed in lung tissues. They are responsible for the bioactivation of several pneumotoxic and carcinogenic chemicals such as benzene, styrene, naphthalene, and 1,1-dichloroethylene. CYP2F1 and CYP2F3 selectively catalyzes the 3-methyl dehydrogenation of 3-methylindole, forming toxic reactive intermediates that can form adducts with proteins and DNA. The CYP2F subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 106.38  E-value: 1.08e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSiPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQ-----PS 150
Cdd:cd20669   1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRG-DYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRnfgmgKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 151 HLTSLIPTMHSFITSATHNLDSKPRDIVFsnLFLKLTTDIIGQAAFGVDFGLSGKKPIKdveVTDFINQH--VYSTtqlk 228
Cdd:cd20669  80 SIEERILEEAQFLLEELRKTKGAPFDPTF--LLSRAVSNIICSVVFGSRFDYDDKRLLT---ILNLINDNfqIMSS---- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 229 mdlsgslsiilgllipilqePFRQVLKRIPGTMDW------RVEKTNARLSGQLNEIVSKRAKEAETDS-KDFLS--LIL 299
Cdd:cd20669 151 --------------------PWGELYNIFPSVMDWlpgphqRIFQNFEKLRDFIAESVREHQESLDPNSpRDFIDcfLTK 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 300 KARES-DPFakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDlQHKFPY 378
Cdd:cd20669 211 MAEEKqDPL--SHFNMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLED-RARMPY 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 379 LDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHRhpyA 456
Cdd:cd20669 288 TDAVIHEIQRFADIIPMsLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFlDDNGSFKKND---A 364
                       410       420       430
                ....*....|....*....|....*....|....*
gi 30683024 457 FIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR 491
Cdd:cd20669 365 FMPFSAGKRICLGESLARMELFLYLTAILQNFSLQ 399
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
76-490 2.29e-24

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: 105.27  E-value: 2.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIpSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQ-----PS 150
Cdd:cd20664   1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPI-IPIFEDFNKGYGILFSNGENWKEMRRFTLTTLRdfgmgKK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 151 HLTSLIPTMHSFITSATHNLDSKPRDIvfSNLFLKLTTDIIGQAAFGVDFGLSGKKPIKdveVTDFINQHVYSTTQlkmd 230
Cdd:cd20664  80 TSEDKILEEIPYLIEVFEKHKGKPFET--TLSMNVAVSNIIASIVLGHRFEYTDPTLLR---MVDRINENMKLTGS---- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 231 lsgslsiilgllipilqePFRQVLKRIPGTMDWRVE-KTNARLSGQLN----EIVSKRAKEAET-DSKDFL-SLILKARE 303
Cdd:cd20664 151 ------------------PSVQLYNMFPWLGPFPGDiNKLLRNTKELNdflmETFMKHLDVLEPnDQRGFIdAFLVKQQE 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 304 SDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRDliPTAHDlQHKFPYLDQV 382
Cdd:cd20664 213 EEESSDSFFHDDNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRvIGSRQ--PQVEH-RKNMPYTDAV 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 383 IKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHRhpyAFIPF 460
Cdd:cd20664 290 IHEIQRFANIVPMnLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFlDSQGKFVKRD---AFMPF 366
                       410       420       430
                ....*....|....*....|....*....|
gi 30683024 461 GIGPRACVGQRFALQEIKLTLLHLYRNYIF 490
Cdd:cd20664 367 SAGRRVCIGETLAKMELFLFFTSLLQRFRF 396
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
285-517 2.62e-24

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: 105.54  E-value: 2.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 285 KEAETDSKDFLSLILKARESDpfaKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEI-DGFGNR 363
Cdd:cd20679 216 AKAKSKTLDFIDVLLLSKDED---GKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVqELLKDR 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 364 DLIPTAHDLQHKFPYLDQVIKEAMRFYMVSPLVARETAKEVEI-GGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF 442
Cdd:cd20679 293 EPEEIEWDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRF 372
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024 443 DPngEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTL-LHLYRnyiFRhSLEMEIPLQLDYGIILSFKNGVKLR 517
Cdd:cd20679 373 DP--ENSQGRSPLAFIPFSAGPRNCIGQTFAMAEMKVVLaLTLLR---FR-VLPDDKEPRRKPELILRAEGGLWLR 442
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
281-506 2.66e-24

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: 105.18  E-value: 2.66e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 281 SKRAKEAETDSKDFLSLILKARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGF 360
Cdd:cd20652 199 PENPRDAEDFELCELEKAKKEGEDRDLFDGFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEV 278
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 361 GNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKP 439
Cdd:cd20652 279 VGRPDLVTLEDLS-SLPYLQACISESQRIRSVVPLgIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRP 357
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30683024 440 ERF-DPNGeeeKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNyiFRHSLEMEIPLQLDYGI 506
Cdd:cd20652 358 ERFlDTDG---KYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRK--FRIALPDGQPVDSEGGN 420
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
47-494 4.99e-24

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 105.16  E-value: 4.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   47 PGPTAMPLVGHLPLMAKYGPDVFSV-LAKQYGPIFRFQMGRQPLIIIAEAELCREvgIKKFKDLPNRSIPSPISASPLHK 125
Cdd:PLN03234  31 PGPKGLPIIGNLHQMEKFNPQHFLFrLSKLYGPIFTMKIGGRRLAVISSAELAKE--LLKTQDLNFTARPLLKGQQTMSY 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  126 KGL---FFTRDKRWSKMRNT-ILSLYQPSHLTSLIPTMH---SFITSATHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGV 198
Cdd:PLN03234 109 QGRelgFGQYTAYYREMRKMcMVNLFSPNRVASFRPVREeecQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGK 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  199 DFGLSGkkpikdVEVTDFINQhVYSTTQLKMDLSGSLSIilgllipilqePFRQVLKRIPGtMDWRVEKTNARLSGQLNE 278
Cdd:PLN03234 189 RYNEYG------TEMKRFIDI-LYETQALLGTLFFSDLF-----------PYFGFLDNLTG-LSARLKKAFKELDTYLQE 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  279 IVSKR--AKEAETDSKDFLSLILKARESDPFAKNiFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQE 356
Cdd:PLN03234 250 LLDETldPNRPKQETESFIDLLMQIYKDQPFSIK-FTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDE 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  357 I------DGFGNRDLIPTahdlqhkFPYLDQVIKEAMRFYMVSP-LVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPK 429
Cdd:PLN03234 329 VrnvigdKGYVSEEDIPN-------LPYLKAVIKESLRLEPVIPiLLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTA 401
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30683024  430 NFPE-PEKFKPERF--DPNGEEEKHRHpYAFIPFGIGPRACVGQRFALQEIKLTLLHLYrnYIFRHSL 494
Cdd:PLN03234 402 AWGDnPNEFIPERFmkEHKGVDFKGQD-FELLPFGSGRRMCPAMHLGIAMVEIPFANLL--YKFDWSL 466
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
72-505 5.65e-24

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: 104.28  E-value: 5.65e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  72 LAKQYGPIFRFQMGRQPLIIIAEAELCREVgIKKFKDLPNrsiPSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQPSH 151
Cdd:cd20642   7 TVKTYGKNSFTWFGPIPRVIIMDPELIKEV-LNKVYDFQK---PKTNPLTKLLATGLASYEGDKWAKHRKIINPAFHLEK 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 152 LTSLIPT-MHSFI-----------TSATHNLDSKPRdivfsnlFLKLTTDIIGQAAFGVDFGlSGKKpIkdvevtdFINQ 219
Cdd:cd20642  83 LKNMLPAfYLSCSemiskweklvsSKGSCELDVWPE-------LQNLTSDVISRTAFGSSYE-EGKK-I-------FELQ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 220 HvySTTQLKMDLsgslsiilgllipilqepFRQVLkrIPGtmdWRV--EKTNARLS-------GQLNEIVSKRAKE---A 287
Cdd:cd20642 147 K--EQGELIIQA------------------LRKVY--IPG---WRFlpTKRNRRMKeiekeirSSLRGIINKREKAmkaG 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 288 ETDSKDFLSLILKARESD---PFAKNI--FTSDYISAVTYEHLlAGSATTAFTLSSVLYLVSGHLDVEKRLLQEI-DGFG 361
Cdd:cd20642 202 EATNDDLLGILLESNHKEikeQGNKNGgmSTEDVIEECKLFYF-AGQETTSVLLVWTMVLLSQHPDWQERAREEVlQVFG 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 362 NRDliPTAHDLQHkFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEK-FKPE 440
Cdd:cd20642 281 NNK--PDFEGLNH-LKVVTMILYEVLRLYPPVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWGDDAKeFNPE 357
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30683024 441 RFdPNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIF------RHSLEMEIPLQLDYG 505
Cdd:cd20642 358 RF-AEGISKATKGQVSYFPFGWGPRICIGQNFALLEAKMALALILQRFSFelspsyVHAPYTVLTLQPQFG 427
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
264-483 1.27e-23

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: 103.27  E-value: 1.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 264 RVEKTNARLSGQLNEIVS--KRAKEAETDSKDFLSLILKARESDPFAKNIFTSDyISAVTYEHLLAGSATTAFTLSSVLY 341
Cdd:cd20657 175 KMKRLHKRFDALLTKILEehKATAQERKGKPDFLDFVLLENDDNGEGERLTDTN-IKALLLNLFTAGTDTSSSTVEWALA 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 342 LVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQHkFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLA 420
Cdd:cd20657 254 ELIRHPDILKKAQEEMDQVIGRDRRLLESDIPN-LPYLQAICKETFRLHPSTPLnLPRIASEACEVDGYYIPKGTRLLVN 332
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30683024 421 LGVLAKDPKNFPEPEKFKPERF--------DPNGEEekhrhpYAFIPFGIGPRACVGQRFALQEIKL---TLLH 483
Cdd:cd20657 333 IWAIGRDPDVWENPLEFKPERFlpgrnakvDVRGND------FELIPFGAGRRICAGTRMGIRMVEYilaTLVH 400
PLN02302 PLN02302
ent-kaurenoic acid oxidase
47-488 3.16e-23

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 102.87  E-value: 3.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   47 PGPTAMPLVGHlplMAKY-------GPDVF-SVLAKQYGP--IFRFQMGRQPLIIIAEAELCREVgikkFKDLPNRSIPS 116
Cdd:PLN02302  45 PGDLGWPVIGN---MWSFlrafkssNPDSFiASFISRYGRtgIYKAFMFGQPTVLVTTPEACKRV----LTDDDAFEPGW 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  117 PISASPLHKK----GLFFTRDKRWSKMrnTILSLYQPSHLTSLIPTMHSFITSAthnLD--SKPRDIVFSNLFLKLTTDI 190
Cdd:PLN02302 118 PESTVELIGRksfvGITGEEHKRLRRL--TAAPVNGPEALSTYIPYIEENVKSC---LEkwSKMGEIEFLTELRKLTFKI 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  191 IGQAAFGVDFGLsgkkpikDVEVTdfinQHVYSTTQLKMdlsgslsiilgllipilqepfRQVLKRIPGTMDWRVEKTNA 270
Cdd:PLN02302 193 IMYIFLSSESEL-------VMEAL----EREYTTLNYGV---------------------RAMAINLPGFAYHRALKARK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  271 RLSGQLNEIVSKR----AKEAETDSKDFLSLILKARESDpfaKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGH 346
Cdd:PLN02302 241 KLVALFQSIVDERrnsrKQNISPRKKDMLDLLLDAEDEN---GRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEH 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  347 LDVEKRLLQEIDGFGNRDLiPTAHDLQ----HKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALG 422
Cdd:PLN02302 318 PEVLQKAKAEQEEIAKKRP-PGQKGLTlkdvRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFR 396
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024  423 VLAKDPKNFPEPEKFKPERFDPNGEEekhrhPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:PLN02302 397 QVHMDPEVYPNPKEFDPSRWDNYTPK-----AGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGY 457
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
256-486 1.41e-22

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: 99.82  E-value: 1.41e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 256 RIPGTMDWRVEKTNARLSGQLNEIVskRAKEAETDSKDFLSLILKAR--ESDPFAK-NIFtsDYISAVtyehLLAGSATT 332
Cdd:cd20614 153 DLPGMPARRSRRARAWIDARLSQLV--ATARANGARTGLVAALIRARddNGAGLSEqELV--DNLRLL----VLAGHETT 224
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 333 AFTLS-SVLYLVSgHLDVEKRLLQEIDGFGNrdlIPTAHDLQHKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLL 411
Cdd:cd20614 225 ASIMAwMVIMLAE-HPAVWDALCDEAAAAGD---VPRTPAELRRFPLAEALFRETLRLHPPVPFVFRRVLEEIELGGRRI 300
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30683024 412 PKGTWVWLALGVLAKDPKNFPEPEKFKPERFdpNGEEEKHRhPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYR 486
Cdd:cd20614 301 PAGTHLGIPLLLFSRDPELYPDPDRFRPERW--LGRDRAPN-PVELLQFGGGPHFCLGYHVACVELVQFIVALAR 372
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
271-484 1.73e-22

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: 100.08  E-value: 1.73e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 271 RLSGQLNEIVSKRAKEAE--TDSKDFLSLILKARESDpfakniFTSDYISAVTYEHLLAGSATTAFTLSSVLylvsGHL- 347
Cdd:cd11066 187 RRDKYLKKLLAKLKEEIEdgTDKPCIVGNILKDKESK------LTDAELQSICLTMVSAGLDTVPLNLNHLI----GHLs 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 348 -----DVEKRLLQEIDGFGNRDlIPTAHDL--QHKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWL 419
Cdd:cd11066 257 hppgqEIQEKAYEEILEAYGND-EDAWEDCaaEEKCPYVVALVKETLRYFTVLPLgLPRKTTKDIVYNGAVIPAGTILFM 335
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024 420 ALGVLAKDPKNFPEPEKFKPER-FDPNGEEEKHRHPYAFipfGIGPRACVGQRFALQEIKLTLLHL 484
Cdd:cd11066 336 NAWAANHDPEHFGDPDEFIPERwLDASGDLIPGPPHFSF---GAGSRMCAGSHLANRELYTAICRL 398
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
24-488 4.61e-22

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 98.85  E-value: 4.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   24 FLTFAAVVIVIYLYR-----PSWSVCNVP---GPTAMPLVGHLPLMAKYGPDVF-SVLAKQYGPIFRFQMGRQPLIIIAE 94
Cdd:PLN02196   7 FLTLFAGALFLCLLRflagfRRSSSTKLPlppGTMGWPYVGETFQLYSQDPNVFfASKQKRYGSVFKTHVLGCPCVMISS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   95 AELCREVGIKKfKDLPNRSIPSPiSASPLHKKGLFFTRDKRWSKMRNTILSLYQPSHLTSLIPTMHSFITSATHNLDSkp 174
Cdd:PLN02196  87 PEAAKFVLVTK-SHLFKPTFPAS-KERMLGKQAIFFHQGDYHAKLRKLVLRAFMPDAIRNMVPDIESIAQESLNSWEG-- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  175 RDIvfsNLFLKLTTDIIGQAAFGVdFGLSGKKPIKDVEVTDFINQHVYSTTQLKmdlsgslsiilgllipilqepfrqvl 254
Cdd:PLN02196 163 TQI---NTYQEMKTYTFNVALLSI-FGKDEVLYREDLKRCYYILEKGYNSMPIN-------------------------- 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  255 krIPGTMDWRVEKTNARLSGQLNEIVSKRaKEAETDSKDFLSLILKARESdpfakniFTSDYISAVTYEHLLAGSATTAF 334
Cdd:PLN02196 213 --LPGTLFHKSMKARKELAQILAKILSKR-RQNGSSHNDLLGSFMGDKEG-------LTDEQIADNIIGVIFAARDTTAS 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  335 TLSSVLYLVSGHLDVEKRLLQE---IDGFGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLL 411
Cdd:PLN02196 283 VLTWILKYLAENPSVLEAVTEEqmaIRKDKEEGESLTWEDTK-KMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLI 361
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024  412 PKGTWVWLALGVLAKDPKNFPEPEKFKPERFdpngeeEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:PLN02196 362 PKGWKVLPLFRNIHHSADIFSDPGKFDPSRF------EVAPKPNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTKY 432
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
270-500 1.29e-21

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: 97.01  E-value: 1.29e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 270 ARLSGQLNEIVSK-----RAKEAETDSKDF------LSLILKARESDpfakniftSDYIsAVTYEHLLAGSATTAFTLSS 338
Cdd:cd11076 176 SALVPRVNTFVGKiieehRAKRSNRARDDEddvdvlLSLQGEEKLSD--------SDMI-AVLWEMIFRGTDTVAILTEW 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 339 VLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLqHKFPYLDQVIKEAMRFYMVSPLV--ARETAKEVEIGGYLLPKGTW 416
Cdd:cd11076 247 IMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDV-AKLPYLQAVVKETLRLHPPGPLLswARLAIHDVTVGGHVVPAGTT 325
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 417 VWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEKH-------RhpyaFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYI 489
Cdd:cd11076 326 AMVNMWAITHDPHVWEDPLEFKPERFVAAEGGADVsvlgsdlR----LAPFGAGRRVCPGKALGLATVHLWVAQLLHEFE 401
                       250       260
                ....*....|....*....|....*
gi 30683024 490 F--------------RHSLEMEIPL 500
Cdd:cd11076 402 WlpddakpvdlsevlKLSCEMKNPL 426
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
76-488 3.51e-21

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: 96.00  E-value: 3.51e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNR---SIPSPIsaspLHKKGLFFTRDKRWSKMRNTILSlyqpshl 152
Cdd:cd20672   1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRgtiAVVDPI----FQGYGVIFANGERWKTLRRFSLA------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 153 tslipTMHSF-----------------ITSATHNLDSKPRDIVFsnLFLKLTTDIIGQAAFGVDFGLsgkkpiKDVEVTD 215
Cdd:cd20672  70 -----TMRDFgmgkrsveeriqeeaqcLVEELRKSKGALLDPTF--LFQSITANIICSIVFGERFDY------KDPQFLR 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 216 FINQhVYSTTQLkmdlsgslsiiLGLLIPILQEPFRQVLKRIPGTMDwRVEKTNARLSGQLNEIVSK-RAKEAETDSKDF 294
Cdd:cd20672 137 LLDL-FYQTFSL-----------ISSFSSQVFELFSGFLKYFPGAHR-QIYKNLQEILDYIGHSVEKhRATLDPSAPRDF 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 295 LS---LILKARESDPFAKNIFTSDYISAVTYehLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHD 371
Cdd:cd20672 204 IDtylLRMEKEKSNHHTEFHHQNLMISVLSL--FFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDD 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 372 lQHKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEE 449
Cdd:cd20672 282 -RAKMPYTDAVIHEIQRFSDLIPIgVPHRVTKDTLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFlDANGALK 360
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 30683024 450 KHRhpyAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd20672 361 KSE---AFMPFSTGKRICLGEGIARNELFLFFTTILQNF 396
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
282-477 5.43e-21

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: 94.29  E-value: 5.43e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 282 KRAKEAETDSKDFLSLILKARESDPfaKNIFTSDYISAVTYEH--------------LLAGSATTAFTLSSVLYLVSGHL 347
Cdd:cd20629 146 PAAEAAAAELYDYVLPLIAERRRAP--GDDLISRLLRAEVEGEklddeeiisflrllLPAGSDTTYRALANLLTLLLQHP 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 348 DVEKRLLQeidgfgNRDLIPtahdlqhkfpyldQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKD 427
Cdd:cd20629 224 EQLERVRR------DRSLIP-------------AAIEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRD 284
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 30683024 428 PKNFPepekfKPERFDpngeeeKHRHPYAFIPFGIGPRACVGQRFALQEI 477
Cdd:cd20629 285 EDVYP-----DPDVFD------IDRKPKPHLVFGGGAHRCLGEHLARVEL 323
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
278-481 6.19e-21

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: 94.59  E-value: 6.19e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 278 EIVSKRAKEAETDskdFLSLILKARESDPfakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQei 357
Cdd:cd11078 177 DLVAERRREPRDD---LISDLLAAADGDG---ERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRA-- 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 358 dgfgNRDLIPTAhdlqhkfpyldqvIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKF 437
Cdd:cd11078 249 ----DPSLIPNA-------------VEETLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRF 311
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 30683024 438 KPERfdPNGeeEKHrhpyafIPFGIGPRACVGQRFALQEIKLTL 481
Cdd:cd11078 312 DIDR--PNA--RKH------LTFGHGIHFCLGAALARMEARIAL 345
PLN02290 PLN02290
cytokinin trans-hydroxylase
20-511 1.07e-20

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 95.27  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   20 ALIAFLTFAAVVIVIYLYRPSW-SVC----------------NVPGPTAMPLVGHLPLMAKY-----GPDVFSV------ 71
Cdd:PLN02290   1 MLGVVLKVLLVIFLTLLLRVAYdTIScyfltprrikkimerqGVRGPKPRPLTGNILDVSALvsqstSKDMDSIhhdivg 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   72 --------LAKQYGPIFRFQMGRQPLIIIAEAELCREVgIKKFKDLPNRSIPSPISASPLHKKGLFFTRDKRWSKMRNTI 143
Cdd:PLN02290  81 rllphyvaWSKQYGKRFIYWNGTEPRLCLTETELIKEL-LTKYNTVTGKSWLQQQGTKHFIGRGLLMANGADWYHQRHIA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  144 LSLYQPSHLTSLIPTM----HSFITSATHNLDSKPRDIVFSNLFLKLTTDIIGQAAFGVDFGlSGKKpIKDVeVTDFINQ 219
Cdd:PLN02290 160 APAFMGDRLKGYAGHMvectKQMLQSLQKAVESGQTEVEIGEYMTRLTADIISRTEFDSSYE-KGKQ-IFHL-LTVLQRL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  220 HVYSTTQLKMdlsgslsiilgllipilqePFRQVLkriPGTMDWRVEKTNARLSGQLNEIVSKRAKEAE-----TDSKDF 294
Cdd:PLN02290 237 CAQATRHLCF-------------------PGSRFF---PSKYNREIKSLKGEVERLLMEIIQSRRDCVEigrssSYGDDL 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  295 LSLILKARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLiPTAHDLQh 374
Cdd:PLN02290 295 LGMLLNEMEKKRSNGFNLNLQLIMDECKTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGET-PSVDHLS- 372
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  375 KFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLAlgVLA---------KDPKNFpEPEKFKPERFDPN 445
Cdd:PLN02290 373 KLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLHIPKGLSIWIP--VLAihhseelwgKDANEF-NPDRFAGRPFAPG 449
                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30683024  446 geeekhRHpyaFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIF------RHSLEMEIPLQLDYGIILSFK 511
Cdd:PLN02290 450 ------RH---FIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFtisdnyRHAPVVVLTIKPKYGVQVCLK 512
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
257-481 1.51e-20

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: 93.85  E-value: 1.51e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 257 IPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETDSK-----DFLSLIL----KARESDPFAKNIFTSDY-ISAVTYEHLL 326
Cdd:cd11082 151 FPGTALWKAIQARKRIVKTLEKCAAKSKKRMAAGEEptcllDFWTHEIleeiKEAEEEGEPPPPHSSDEeIAGTLLDFLF 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 327 AGS-ATTaftlSSVLY---LVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQHKFPYLDQVIKEAMRFYMVSPLVARETAK 402
Cdd:cd11082 231 ASQdAST----SSLVWalqLLADHPDVLAKVREEQARLRPNDEPPLTLDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKK 306
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 403 EVEIG-GYLLPKGTWVWLALGVLAKDPknFPEPEKFKPERFDPNGEEEKhRHPYAFIPFGIGPRACVGQRFALQEIKLTL 481
Cdd:cd11082 307 DFPLTeDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQEDR-KYKKNFLVFGAGPHQCVGQEYAINHLMLFL 383
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
76-491 2.06e-20

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: 93.75  E-value: 2.06e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRSIpSPISASPLHKKGLFFTRDKRWSKMRNTILSLYQ-----PS 150
Cdd:cd20667   1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPL-TPFFRDLFGEKGIICTNGLTWKQQRRFCMTTLRelglgKQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 151 HLTSLIPTMHSFITSATHNLDSKPRDIvfSNLFLKLTTDIIGQAAFGVDFglSGKKPIKdVEVTDFINQHVY--STTQLK 228
Cdd:cd20667  80 ALESQIQHEAAELVKVFAQENGRPFDP--QDPIVHATANVIGAVVFGHRF--SSEDPIF-LELIRAINLGLAfaSTIWGR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 229 MdlsgslsiilgllipilQEPFRQVLKRIPGTMDwRVEKTNARLSGQLNEIVSKRAKEAETDSKDF----LSLILKAREs 304
Cdd:cd20667 155 L-----------------YDAFPWLMRYLPGPHQ-KIFAYHDAVRSFIKKEVIRHELRTNEAPQDFidcyLAQITKTKD- 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 305 DPFAKniFTSDYISAVTYEHLLAGSATTAFTLS-SVLYLVSgHLDVEKRLLQEIDgfgnrDLIPTAHDL----QHKFPYL 379
Cdd:cd20667 216 DPVST--FSEENMIQVVIDLFLGGTETTATTLHwALLYMVH-HPEIQEKVQQELD-----EVLGASQLIcyedRKRLPYT 287
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 380 DQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEeekHRHPYAF 457
Cdd:cd20667 288 NAVIHEVQRLSNVVSVgAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFlDKDGN---FVMNEAF 364
                       410       420       430
                ....*....|....*....|....*....|....
gi 30683024 458 IPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR 491
Cdd:cd20667 365 LPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQ 398
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
346-488 4.81e-20

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 93.26  E-value: 4.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  346 HLDVEKRLLQEIDGFGNRDLIPTAHDLqHKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVL 424
Cdd:PLN02394 323 HPEIQKKLRDELDTVLGPGNQVTEPDT-HKLPYLQAVVKETLRLHMAIPLlVPHMNLEDAKLGGYDIPAESKILVNAWWL 401
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30683024  425 AKDPKNFPEPEKFKPERF-DPNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:PLN02394 402 ANNPELWKNPEEFRPERFlEEEAKVEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNF 466
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
47-516 1.11e-19

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 91.84  E-value: 1.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   47 PGPTAMPLVGHLPLMAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCRevGIKKFKDL--PNRsipsPISASPLH 124
Cdd:PLN00110  34 PGPRGWPLLGALPLLGNMPHVALAKMAKRYGPVMFLKMGTNSMVVASTPEAAR--AFLKTLDInfSNR----PPNAGATH 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  125 -----KKGLFFTRDKRWSKMRN-TILSLYQPSHLTSLIPTMHS---FITSATHNLDSKPRDIVFSNLFLKLTTDIIGQAA 195
Cdd:PLN00110 108 laygaQDMVFADYGPRWKLLRKlSNLHMLGGKALEDWSQVRTVelgHMLRAMLELSQRGEPVVVPEMLTFSMANMIGQVI 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  196 FGVDFGLSgkkpiKDVEVTDFINQHVYSTTQlkmdlsgslsiilgllipilqEPFRQVLKRIPGT--MDWR-VEKTNARL 272
Cdd:PLN00110 188 LSRRVFET-----KGSESNEFKDMVVELMTT---------------------AGYFNIGDFIPSIawMDIQgIERGMKHL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  273 SGQLNEIVSKRAKE--AETDSK----DFLSLILKARESDPFAKNIFTSdyISAVTYEHLLAGSATTAFTLSSVLYLVSGH 346
Cdd:PLN00110 242 HKKFDKLLTRMIEEhtASAHERkgnpDFLDVVMANQENSTGEKLTLTN--IKALLLNLFTAGTDTSSSVIEWSLAEMLKN 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  347 LDVEKRLLQEIDGFGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLA 425
Cdd:PLN00110 320 PSILKRAHEEMDQVIGRNRRLVESDLP-KLPYLQAICKESFRKHPSTPLnLPRVSTQACEVNGYYIPKNTRLSVNIWAIG 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  426 KDPKNFPEPEKFKPERF--------DPNGEEekhrhpYAFIPFGIGPRACVGQRFALQEIKLTLLHLYrnyifrHSLEME 497
Cdd:PLN00110 399 RDPDVWENPEEFRPERFlseknakiDPRGND------FELIPFGAGRRICAGTRMGIVLVEYILGTLV------HSFDWK 466
                        490       500
                 ....*....|....*....|...
gi 30683024  498 IP----LQLDYGIILSFKNGVKL 516
Cdd:PLN00110 467 LPdgveLNMDEAFGLALQKAVPL 489
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
76-508 1.34e-19

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: 90.94  E-value: 1.34e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  76 YGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRsiPSPISASPLHKKGlfftRD----------KRWSKMRNTILS 145
Cdd:cd20674   1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGR--PHSYTGKLVSQGG----QDlslgdysllwKAHRKLTRSALQ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 146 LYQPSHLTSLIPTMHSFITSATHNLDSKPRDIvfSNLFLKLTTDIIGQAAFGVDFGLSGKKPikdvEVTDFINQHV---- 221
Cdd:cd20674  75 LGIRNSLEPVVEQLTQELCERMRAQAGTPVDI--QEEFSLLTCSIICCLTFGDKEDKDTLVQ----AFHDCVQELLktwg 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 222 -YSTTQLKMdlsgslsiilgllipilqEPFrqvLKRIPGTMDWR----VEKTNARLSGQLneivsKRAKEA--ETDSKDF 294
Cdd:cd20674 149 hWSIQALDS------------------IPF---LRFFPNPGLRRlkqaVENRDHIVESQL-----RQHKESlvAGQWRDM 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 295 LSLILK--ARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLS-SVLYLVSgHLDVEKRLLQEIDGFGNRDLIPTAHD 371
Cdd:cd20674 203 TDYMLQglGQPRGEKGMGQLLEGHVHMAVVDLFIGGTETTASTLSwAVAFLLH-HPEIQDRLQEELDRVLGPGASPSYKD 281
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 372 lQHKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEK 450
Cdd:cd20674 282 -RARLPLLNATIAEVLRLRPVVPLaLPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAANR 360
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30683024 451 hrhpyAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIP-LQLDYGIIL 508
Cdd:cd20674 361 -----ALLPFGCGARVCLGEPLARLELFVFLARLLQAFTLLPPSDGALPsLQPVAGINL 414
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
315-488 2.27e-19

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: 90.55  E-value: 2.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 315 DYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEI-----DGFGNRdliptAHDLQhKFPYLDQVIKEAMRF 389
Cdd:cd20643 233 EDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVlaarqEAQGDM-----VKMLK-SVPLLKAAIKETLRL 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 390 YMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFdPNGEEEKHRHpyafIPFGIGPRACVG 469
Cdd:cd20643 307 HPVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERW-LSKDITHFRN----LGFGFGPRQCLG 381
                       170
                ....*....|....*....
gi 30683024 470 QRFALQEIKLTLLHLYRNY 488
Cdd:cd20643 382 RRIAETEMQLFLIHMLENF 400
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
346-488 2.51e-19

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: 90.22  E-value: 2.51e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 346 HLDVEKRLLQEIDGFGNRDLIPTAHDLqHKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVL 424
Cdd:cd11074 263 HPEIQKKLRDELDTVLGPGVQITEPDL-HKLPYLQAVVKETLRLRMAIPLlVPHMNLHDAKLGGYDIPAESKILVNAWWL 341
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30683024 425 AKDPKNFPEPEKFKPERF-DPNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd11074 342 ANNPAHWKKPEEFRPERFlEEESKVEANGNDFRYLPFGVGRRSCPGIILALPILGITIGRLVQNF 406
PLN00168 PLN00168
Cytochrome P450; Provisional
47-484 4.32e-19

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 90.39  E-value: 4.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   47 PGPTAMPLVGHLPLMAKYGPDVFSVLAK---QYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDLPNRsiPSPISASPL 123
Cdd:PLN00168  38 PGPPAVPLLGSLVWLTNSSADVEPLLRRliaRYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADR--PAVASSRLL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  124 HKKGLFFTRDKR---WSKMR-NTILSLYQPSHLTSLIPTMHSFITSATHNL-----DSKPRDIVfsNLFLKLTTDIIGQA 194
Cdd:PLN00168 116 GESDNTITRSSYgpvWRLLRrNLVAETLHPSRVRLFAPARAWVRRVLVDKLrreaeDAAAPRVV--ETFQYAMFCLLVLM 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  195 AFGVDFGLSGKKPIKDVEVTDFInqhvYSTTQLKM-DLSGSLSIILGLLIPILQEPFRQVLKR--IPGTMDWRVEKTNAR 271
Cdd:PLN00168 194 CFGERLDEPAVRAIAAAQRDWLL----YVSKKMSVfAFFPAVTKHLFRGRLQKALALRRRQKElfVPLIDARREYKNHLG 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  272 LSGQlneivskRAKEAETDSKDFLSLILKARESDPFAKNIfTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEK 351
Cdd:PLN00168 270 QGGE-------PPKKETTFEHSYVDTLLDIRLPEDGDRAL-TDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQS 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  352 RLLQEIDGFGNRDLIPTAHDLQHKFPYLDQVIKEAMR----FYMVSPLVAretAKEVEIGGYLLPKGTWVWLALGVLAKD 427
Cdd:PLN00168 342 KLHDEIKAKTGDDQEEVSEEDVHKMPYLKAVVLEGLRkhppAHFVLPHKA---AEDMEVGGYLIPKGATVNFMVAEMGRD 418
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30683024  428 PKNFPEPEKFKPERFDPNGEEE----KHRHPYAFIPFGIGPRACVGQRFAlqeikltLLHL 484
Cdd:PLN00168 419 EREWERPMEFVPERFLAGGDGEgvdvTGSREIRMMPFGVGRRICAGLGIA-------MLHL 472
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
315-508 7.13e-19

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: 89.13  E-value: 7.13e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 315 DYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEI---DGFGNRDLIPTAHDLqhkfPYLDQVIKEAMRFYM 391
Cdd:cd20644 231 EAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESlaaAAQISEHPQKALTEL----PLLKAALKETLRLYP 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 392 VSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHRHpyafIPFGIGPRACVGQ 470
Cdd:cd20644 307 VGITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWlDIRGSGRNFKH----LAFGFGMRQCLGR 382
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 30683024 471 RFALQEIKLTLLHLYRNYIFRHSLEMEIplQLDYGIIL 508
Cdd:cd20644 383 RLAEAEMLLLLMHVLKNFLVETLSQEDI--KTVYSFIL 418
PLN02936 PLN02936
epsilon-ring hydroxylase
325-490 9.40e-19

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 89.08  E-value: 9.40e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  325 LLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRDliPTAHDLQhKFPYLDQVIKEAMRFYMVSP-LVARETAK 402
Cdd:PLN02936 287 LVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRvLQGRP--PTYEDIK-ELKYLTRCINESMRLYPHPPvLIRRAQVE 363
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  403 EVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEKHRHP-YAFIPFGIGPRACVGQRFALQEIKLTL 481
Cdd:PLN02936 364 DVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETNTdFRYIPFSGGPRKCVGDQFALLEAIVAL 443

                 ....*....
gi 30683024  482 LHLYRNYIF 490
Cdd:PLN02936 444 AVLLQRLDL 452
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
325-482 1.44e-18

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: 88.51  E-value: 1.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 325 LLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEID------GFGNRdlIPTAHDL-QHKFPYLDQVIKEAMRFYMVSPLVA 397
Cdd:cd20622 271 LIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYsahpeaVAEGR--LPTAQEIaQARIPYLDAVIEEILRCANTAPILS 348
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 398 RETAKEVEIGGYLLPKGTWVWLAL---GVL---------------AKDPKNFPE-----PEKFKPER------------F 442
Cdd:cd20622 349 REATVDTQVLGYSIPKGTNVFLLNngpSYLsppieidesrrssssAAKGKKAGVwdskdIADFDPERwlvtdeetgetvF 428
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 30683024 443 DPNGeeekhrhpYAFIPFGIGPRACVGQRFALQEIKL--TLL 482
Cdd:cd20622 429 DPSA--------GPTLAFGLGPRGCFGRRLAYLEMRLiiTLL 462
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
323-511 3.92e-18

cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a microsomal enzyme that is required for the activation of vitamin D; it catalyzes the initial step converting vitamin D into 25-hydroxyvitamin D (25(OH)D), the major circulating metabolite of vitamin D. The 1alpha-hydroxylation of 25(OH)D by CYP27B1 generates the fully active vitamin D metabolite, 1,25-dihydroxyvitamin D (1,25(OH)2D). Mutations in the CYP2R1 gene are associated with an atypical form of vitamin D-deficiency rickets, which has been classified as vitamin D dependent rickets type 1B. CYP2R1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 86.79  E-value: 3.92e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 323 EHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPL-VARETA 401
Cdd:cd20661 245 ELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKC-KMPYTEAVLHEVLRFCNIVPLgIFHATS 323
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 402 KEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHRhpyAFIPFGIGPRACVGQRFALQEIklt 480
Cdd:cd20661 324 KDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFlDSNGQFAKKE---AFVPFSLGRRHCLGEQLARMEM--- 397
                       170       180       190
                ....*....|....*....|....*....|.
gi 30683024 481 llhlyrnYIFRHSLEMEIPLQLDYGIILSFK 511
Cdd:cd20661 398 -------FLFFTALLQRFHLHFPHGLIPDLK 421
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
21-485 6.36e-18

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 86.42  E-value: 6.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   21 LIAFLTFAAVVIVIYLYRPSWSVCNV----PGPTAMPLVGHLPLMAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAE 96
Cdd:PLN03112   5 LLSLLFSVLIFNVLIWRWLNASMRKSlrlpPGPPRWPIVGNLLQLGPLPHRDLASLCKKYGPLVYLRLGSVDAITTDDPE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   97 LCREVGIKK---FKDLPnRSIPSPISASPLHKKGLFfTRDKRWSKMRNTILS-LYQPSHLTSLI-------PTMHSFITS 165
Cdd:PLN03112  85 LIREILLRQddvFASRP-RTLAAVHLAYGCGDVALA-PLGPHWKRMRRICMEhLLTTKRLESFAkhraeeaRHLIQDVWE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  166 ATHNldSKP---RDIVFSNLFLKLTTDIIGQAAFGVDfGLSGKKPIKDVEVTD-------FINQHVYSTTQLKMDLSGSl 235
Cdd:PLN03112 163 AAQT--GKPvnlREVLGAFSMNNVTRMLLGKQYFGAE-SAGPKEAMEFMHITHelfrllgVIYLGDYLPAWRWLDPYGC- 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  236 siilgllipilQEPFRQVLKRIPGTMDWRVEKTNArlsgqlneivSKRAKEAETDSKDFLSLILKARESDpfAKNIFTSD 315
Cdd:PLN03112 239 -----------EKKMREVEKRVDEFHDKIIDEHRR----------ARSGKLPGGKDMDFVDVLLSLPGEN--GKEHMDDV 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  316 YISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQHkFPYLDQVIKEAMRFYMVSP- 394
Cdd:PLN03112 296 EIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVH-LNYLRCVVRETFRMHPAGPf 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  395 LVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGE---EEKHRHPYAFIPFGIGPRACVGQR 471
Cdd:PLN03112 375 LIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAEGsrvEISHGPDFKILPFSAGKRKCPGAP 454
                        490
                 ....*....|....
gi 30683024  472 FALQEIKLTLLHLY 485
Cdd:PLN03112 455 LGVTMVLMALARLF 468
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
282-503 1.40e-17

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: 84.65  E-value: 1.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 282 KRAKEAETDSKDFLSLILK-ARESD--PFAKNIFTSDYISAVT--------YEHLLAGSATTAFTLSSVLYLVSGHLDVE 350
Cdd:cd20615 170 RRLREFQTRWRAFNLKIYNrARQRGqsTPIVKLYEAVEKGDITfeellqtlDEMLFANLDVTTGVLSWNLVFLAANPAVQ 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 351 KRLLQEIDGFGNRDLIPTAHDLQHKFPYLDQVIKEAMRfymVSPL----VARETAKEVEIGGYLLPKGTWV---WLALGV 423
Cdd:cd20615 250 EKLREEISAAREQSGYPMEDYILSTDTLLAYCVLESLR---LRPLlafsVPESSPTDKIIGGYRIPANTPVvvdTYALNI 326
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 424 laKDPKNFPEPEKFKPERF-DPNGEEEKhrhpYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYifrhslEMEIPLQL 502
Cdd:cd20615 327 --NNPFWGPDGEAYRPERFlGISPTDLR----YNFWRFGFGPRKCLGQHVADVILKALLAHLLEQY------ELKLPDQG 394

                .
gi 30683024 503 D 503
Cdd:cd20615 395 E 395
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
281-485 4.80e-17

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: 83.13  E-value: 4.80e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 281 SKRAKEAETDSKDFLSLILKaresdpfaknifTSDYISAVTYEHL-----LAGSATTAF-TLSSVLYlvsgHLDVEKRLL 354
Cdd:cd20635 185 AEKTKPLENNSKTLLQHLLD------------TVDKENAPNYSLLllwasLANAIPITFwTLAFILS----HPSVYKKVM 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 355 QEID---GFGNRDLIPTAHDLQHKFPYLDQVIKEAMRfyMVSP-LVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKN 430
Cdd:cd20635 249 EEISsvlGKAGKDKIKISEDDLKKMPYIKRCVLEAIR--LRSPgAITRKVVKPIKIKNYTIPAGDMLMLSPYWAHRNPKY 326
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30683024 431 FPEPEKFKPERFDpNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKL---TLLHLY 485
Cdd:cd20635 327 FPDPELFKPERWK-KADLEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMfvaMFLYKY 383
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
263-491 7.96e-17

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: 82.73  E-value: 7.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 263 WRVEKTNARLSGQLNEIVSKRAKEAETDSK----DFLS-LILKARESDPfaknifTSDYISAVTYEHLLAGSA-TTAFTL 336
Cdd:cd11041 174 RRLRRLLRRARPLIIPEIERRRKLKKGPKEdkpnDLLQwLIEAAKGEGE------RTPYDLADRQLALSFAAIhTTSMTL 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 337 SSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLqHKFPYLDQVIKEAMRFYMVSPLVARETAKEVE--IGGYLLPKG 414
Cdd:cd11041 248 THVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAAL-NKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVtlSDGLTLPKG 326
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 415 TWVWLALGVLAKDPKNFPEPEKFKPERF--DPNGEEEKHRHPYA-----FIPFGIGPRACVGQRFALQEIKLTLLHLYRN 487
Cdd:cd11041 327 TRIAVPAHAIHRDPDIYPDPETFDGFRFyrLREQPGQEKKHQFVstspdFLGFGHGRHACPGRFFASNEIKLILAHLLLN 406

                ....
gi 30683024 488 YIFR 491
Cdd:cd11041 407 YDFK 410
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
294-508 1.28e-15

cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome P450 1B1 (CYP1B1) is expressed in liver and extrahepatic tissues where it carries out the metabolism of numerous xenobiotics, including metabolic activation of polycyclic aromatic hydrocarbons. It is also important in regulating endogenous metabolic pathways, including the metabolism of steroid hormones, fatty acids, melatonin, and vitamins. CYP1B1 is overexpressed in a wide variety of tumors and is associated with angiogenesis. It is also associated with adipogenesis, obesity, hypertension, and atherosclerosis. It is therefore a target for the treatment of metabolic diseases and cancer. Also included in this subfamily are CYP1C proteins from fish, birds and amphibians. The CYP1B1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 78.89  E-value: 1.28e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 294 FLSLILKARESDPFAknIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQ 373
Cdd:cd20675 215 FILALEKGKSGDSGV--GLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQP 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 374 HkFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKH 451
Cdd:cd20675 293 N-LPYVMAFLYEAMRFSSFVPVtIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFlDENGFLNKD 371
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 452 RHPYAFIpFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLEMEIPLQLDYGIIL 508
Cdd:cd20675 372 LASSVMI-FSVGKRRCIGEELSKMQLFLFTSILAHQCNFTANPNEPLTMDFSYGLTL 427
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
270-521 2.68e-15

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 78.51  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  270 ARLSGQLNEIVSKRAKE------AETDSKDFLSLILKARESDPFAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLV 343
Cdd:PLN02169 249 ATVNRMFAKIISSRRKEeisraeTEPYSKDALTYYMNVDTSKYKLLKPKKDKFIRDVIFSLVLAGRDTTSSALTWFFWLL 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  344 SGHLDVEKRLLQEID-GFGNRDLiptahdlqHKFPYLDQVIKEAMRFYMVSPLVARETAK-EVEIGGYLLPKGTWVWLAL 421
Cdd:PLN02169 329 SKHPQVMAKIRHEINtKFDNEDL--------EKLVYLHAALSESMRLYPPLPFNHKAPAKpDVLPSGHKVDAESKIVICI 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  422 GVLAKDPKNFPE-PEKFKPERFDPNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR----HSLEm 496
Cdd:PLN02169 401 YALGRMRSVWGEdALDFKPERWISDNGGLRHEPSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDFKviegHKIE- 479
                        250       260
                 ....*....|....*....|....*
gi 30683024  497 EIPlqldyGIILSFKNGVKLRTIKR 521
Cdd:PLN02169 480 AIP-----SILLRMKHGLKVTVTKK 499
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
264-469 8.03e-15

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 76.10  E-value: 8.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 264 RVEKTNARLSGQLNEIVSKRAkeaETDSKDFLSLILKArESDPFAkniFTSDYIsaVTYEHLL--AGSATTAFTLSSVLY 341
Cdd:cd11032 153 EMAEALRELNAYLLEHLEERR---RNPRDDLISRLVEA-EVDGER---LTDEEI--VGFAILLliAGHETTTNLLGNAVL 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 342 LVSGHLDVEKRLLQeidgfgNRDLIPtahdlqhkfpyldQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLAL 421
Cdd:cd11032 224 CLDEDPEVAARLRA------DPSLIP-------------GAIEEVLRYRPPVQRTARVTTEDVELGGVTIPAGQLVIAWL 284
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 30683024 422 GVLAKDPKNFPEPEKFKPerfdpngeeekHRHPYAFIPFGIGPRACVG 469
Cdd:cd11032 285 ASANRDERQFEDPDTFDI-----------DRNPNPHLSFGHGIHFCLG 321
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
276-481 1.62e-14

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: 74.94  E-value: 1.62e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 276 LNEIVSKRAKEAETDskdFLSLILKAR-ESDPFaknifTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLL 354
Cdd:cd11035 157 LTPLIAERRANPGDD---LISAILNAEiDGRPL-----TDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLR 228
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 355 QeidgfgNRDLIPTAhdlqhkfpyldqvIKEAMRFYMVsPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEP 434
Cdd:cd11035 229 E------DPELIPAA-------------VEELLRRYPL-VNVARIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDP 288
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 30683024 435 EKFKPERfdpngeeEKHRHpyafIPFGIGPRACVGQRFALQEIKLTL 481
Cdd:cd11035 289 DTVDFDR-------KPNRH----LAFGAGPHRCLGSHLARLELRIAL 324
PLN02774 PLN02774
brassinosteroid-6-oxidase
47-485 1.66e-14

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 75.58  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   47 PGPTAMPLVGHLPLMAKYGPDVFSVLAKQYGPIFRFQMGRQPLIIIAEAELCREVGIKKFKDL----PNRSI----PSPI 118
Cdd:PLN02774  34 PGTMGWPLFGETTEFLKQGPDFMKNQRLRYGSFFKSHILGCPTIVSMDPELNRYILMNEGKGLvpgyPQSMLdilgTCNI 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  119 SA--SPLHKKglfftrdkrwskMRNTILSLYQPSHL-TSLIPTMHSFITSATHNLDSKP----RDIVFSNLFLKLTTDII 191
Cdd:PLN02774 114 AAvhGSTHRY------------MRGSLLSLISPTMIrDHLLPKIDEFMRSHLSGWDGLKtidiQEKTKEMALLSALKQIA 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  192 GqaafgvdfglSGKKPIKDVEVTDFInQHVYSTTQLKMDlsgslsiilgllipilqepfrqvlkrIPGTMDWRVEKTNAR 271
Cdd:PLN02774 182 G----------TLSKPISEEFKTEFF-KLVLGTLSLPID--------------------------LPGTNYRSGVQARKN 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  272 LSGQLNEIVSKRAKEAETDSkDFLSLILKARESdpfaKNIFTSDYISAVTYEHLLAGSATTAFT-LSSVLYLVSG----- 345
Cdd:PLN02774 225 IVRMLRQLIQERRASGETHT-DMLGYLMRKEGN----RYKLTDEEIIDQIITILYSGYETVSTTsMMAVKYLHDHpkalq 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  346 -----HLDVEKRLLQEiDGFGNRDLIPTAhdlqhkfpYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLA 420
Cdd:PLN02774 300 elrkeHLAIRERKRPE-DPIDWNDYKSMR--------FTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVY 370
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30683024  421 LGVLAKDPKNFPEPEKFKPERFDPNGEEEkhrHPYAFIpFGIGPRACVGQRFALQEIKlTLLHLY 485
Cdd:PLN02774 371 TREINYDPFLYPDPMTFNPWRWLDKSLES---HNYFFL-FGGGTRLCPGKELGIVEIS-TFLHYF 430
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
259-473 1.91e-14

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


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 75.24  E-value: 1.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 259 GTMDWRVEKTNARlsgqlneivSKRAKEAETDSKDFLSLILKARESDPFAKNIFTSDYISAVTYEH---------LLAGS 329
Cdd:cd20627 145 GFLDGSLEKSTTR---------KKQYEDALMEMESVLKKVIKERKGKNFSQHVFIDSLLQGNLSEQqvledsmifSLAGC 215
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 330 ATTAFTLSSVLYLVSGHLDVEKRLLQEIDG-FGNRdliPTAHDLQHKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGG 408
Cdd:cd20627 216 VITANLCTWAIYFLTTSEEVQKKLYKEVDQvLGKG---PITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQ 292
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30683024 409 YLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDpngeEEKHRHPYAFIPFGiGPRACVGQRFA 473
Cdd:cd20627 293 HIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRFD----DESVMKSFSLLGFS-GSQECPELRFA 352
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
272-486 2.00e-14

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: 75.26  E-value: 2.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 272 LSGQLNEIVSKRAKEAETDSKDFLslILKARESDpfakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEK 351
Cdd:cd20636 189 MEKAIEEKLQRQQAAEYCDALDYM--IHSARENG----KELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIE 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 352 RLLQEIDGFGNRD---LIPTAHDLQH--KFPYLDQVIKEAMRFYmvsPLVA---RETAKEVEIGGYLLPKGTWVWLALGV 423
Cdd:cd20636 263 KIRQELVSHGLIDqcqCCPGALSLEKlsRLRYLDCVVKEVLRLL---PPVSggyRTALQTFELDGYQIPKGWSVMYSIRD 339
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30683024 424 LAKDPKNFPEPEKFKPERFDPNGEEEKHRHpYAFIPFGIGPRACVGQRFALQEIKLTLLHLYR 486
Cdd:cd20636 340 THETAAVYQNPEGFDPDRFGVEREESKSGR-FNYIPFGGGVRSCIGKELAQVILKTLAVELVT 401
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
285-487 2.35e-14

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: 75.24  E-value: 2.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 285 KEAETDSKDFLSLILKARESDPFAKNIftsDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEID--GFGN 362
Cdd:cd20638 202 EDTEQQCKDALQLLIEHSRRNGEPLNL---QALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQekGLLS 278
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 363 RDLIPTAH---DLQHKFPYLDQVIKEAMRfymVSPLVA---RETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEK 436
Cdd:cd20638 279 TKPNENKElsmEVLEQLKYTGCVIKETLR---LSPPVPggfRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDE 355
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 30683024 437 FKPERFDPNGEEEKHRhpYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRN 487
Cdd:cd20638 356 FNPDRFMSPLPEDSSR--FSFIPFGGGSRSCVGKEFAKVLLKIFTVELARH 404
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
325-481 2.79e-14

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: 74.29  E-value: 2.79e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 325 LLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEidgfgnRDLIPTAhdlqhkfpyldqvIKEAMRFYMVSPLVARETAKEV 404
Cdd:cd11034 199 LLGGTDTTSSALSGALLWLAQHPEDRRRLIAD------PSLIPNA-------------VEEFLRFYSPVAGLARTVTQEV 259
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 405 EIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFdPNgeeekhRHpyafIPFGIGPRACVGQRFALQEIKLTL 481
Cdd:cd11034 260 EVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRT-PN------RH----LAFGSGVHRCLGSHLARVEARVAL 325
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
248-487 7.05e-14

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: 73.00  E-value: 7.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 248 EPFRQVLKRIPGTMDWRVE--KTNARLSGQLNEIVSKRAKEAETDSKDFLSLIlkaresdpfakniftSDYISAvtyehl 325
Cdd:cd11037 155 ERTRAALPRLKELRDWVAEqcARERLRPGGWGAAIFEAADRGEITEDEAPLLM---------------RDYLSA------ 213
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 326 laGSATTAFTLSSVLYLVSGHLDvEKRLLQEidgfgNRDLIPTAhdlqhkfpyldqvIKEAMRFYMVSPLVARETAKEVE 405
Cdd:cd11037 214 --GLDTTISAIGNALWLLARHPD-QWERLRA-----DPSLAPNA-------------FEEAVRLESPVQTFSRTTTRDTE 272
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 406 IGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERfDPNGeeekHrhpyafIPFGIGPRACVGQRFALQEIKLTLLHLY 485
Cdd:cd11037 273 LAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR-NPSG----H------VGFGHGVHACVGQHLARLEGEALLTALA 341

                ..
gi 30683024 486 RN 487
Cdd:cd11037 342 RR 343
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
277-469 6.65e-13

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: 70.47  E-value: 6.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 277 NEIVSKRAK----EAETDSKDFLSLILKARESDpfAKNIFTSDYISAVTYEHLLAG----SATTAFTLSSVLylvsGHLD 348
Cdd:cd20658 196 DPIIDERIKqwreGKKKEEEDWLDVFITLKDEN--GNPLLTPDEIKAQIKELMIAAidnpSNAVEWALAEML----NQPE 269
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 349 VEKRLLQEIDGFGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETAKE-VEIGGYLLPKGTWVWLALGVLAKD 427
Cdd:cd20658 270 ILRKATEELDRVVGKERLVQESDIP-NLNYVKACAREAFRLHPVAPFNVPHVAMSdTTVGGYFIPKGSHVLLSRYGLGRN 348
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30683024 428 PKNFPEPEKFKPER-FDPNGEEEKHRHPYAFIPFGIGPRACVG 469
Cdd:cd20658 349 PKVWDDPLKFKPERhLNEDSEVTLTEPDLRFISFSTGRRGCPG 391
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
279-521 7.35e-13

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 70.58  E-value: 7.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  279 IVSKRAK--EAETDSK----DFLSLILKAREsDPfaKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKR 352
Cdd:PLN03195 252 IRRRKAEmdEARKSGKkvkhDILSRFIELGE-DP--DSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEK 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  353 LLQEIDGFG---------------NRDLIPTA----HDLQHKFPYLDQVIKEAMRFYMVSPLVARET-AKEVEIGGYLLP 412
Cdd:PLN03195 329 LYSELKALEkerakeedpedsqsfNQRVTQFAglltYDSLGKLQYLHAVITETLRLYPAVPQDPKGIlEDDVLPDGTKVK 408
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  413 KG---TWVWLALGvlaKDPKNF-PEPEKFKPERFDPNGEEEkHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:PLN03195 409 AGgmvTYVPYSMG---RMEYNWgPDAASFKPERWIKDGVFQ-NASPFKFTAFQAGPRICLGKDSAYLQMKMALALLCRFF 484
                        250       260       270
                 ....*....|....*....|....*....|...
gi 30683024  489 IFRhsLEMEIPLQLDYGIILSFKNGVKLRTIKR 521
Cdd:PLN03195 485 KFQ--LVPGHPVKYRMMTILSMANGLKVTVSRR 515
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
250-511 2.53e-12

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: 68.89  E-value: 2.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 250 FRQVLKRIPGTMDWRVEKTNARLSGQLNEIVSKRAKEAETDS-KDFL-SLILKARES--DPFAKNIFTSDYISAVTYEHL 325
Cdd:cd20676 167 FIPILRYLPNPAMKRFKDINKRFNSFLQKIVKEHYQTFDKDNiRDITdSLIEHCQDKklDENANIQLSDEKIVNIVNDLF 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 326 LAGSATTAFTLS-SVLYLVSgHLDVEKRLLQEIDGFGNRDLIPTAHDlQHKFPYLDQVIKEAMRFYMVSPL-VARETAKE 403
Cdd:cd20676 247 GAGFDTVTTALSwSLMYLVT-YPEIQKKIQEELDEVIGRERRPRLSD-RPQLPYLEAFILETFRHSSFVPFtIPHCTTRD 324
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 404 VEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERF-DPNG------EEEKhrhpyaFIPFGIGPRACVGQRFALQE 476
Cdd:cd20676 325 TSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFlTADGteinktESEK------VMLFGLGKRRCIGESIARWE 398
                       250       260       270
                ....*....|....*....|....*....|....*
gi 30683024 477 IKLTLLHLYRNYIFRHSLEMEIPLQLDYGIILSFK 511
Cdd:cd20676 399 VFLFLAILLQQLEFSVPPGVKVDMTPEYGLTMKHK 433
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
378-484 3.31e-12

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: 68.32  E-value: 3.31e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 378 YLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLAL-GVLaKDPKNFPEPEKFKPERFdpngeEEKHRHPYA 456
Cdd:cd11067 264 YAEAFVQEVRRFYPFFPFVGARARRDFEWQGYRFPKGQRVLLDLyGTN-HDPRLWEDPDRFRPERF-----LGWEGDPFD 337
                        90       100       110
                ....*....|....*....|....*....|..
gi 30683024 457 FIPFGIGPRA----CVGQRFALQEIKLTLLHL 484
Cdd:cd11067 338 FIPQGGGDHAtghrCPGEWITIALMKEALRLL 369
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
325-486 4.25e-12

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: 67.55  E-value: 4.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 325 LLAGSATTAFTLSSVLYLVSGHLDvEKRLLQEidgfgNRDLIPTAhdlqhkfpyldqvIKEAMRFymVSPLVA-RETAKE 403
Cdd:cd11033 218 AVAGNETTRNSISGGVLALAEHPD-QWERLRA-----DPSLLPTA-------------VEEILRW--ASPVIHfRRTATR 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 404 -VEIGGYLLPKGTWV--WLALGvlAKDPKNFPEPEKFKPERfDPNgeeekhRHpyafIPFGIGPRACVGQRFALQEIKLT 480
Cdd:cd11033 277 dTELGGQRIRAGDKVvlWYASA--NRDEEVFDDPDRFDITR-SPN------PH----LAFGGGPHFCLGAHLARLELRVL 343

                ....*.
gi 30683024 481 LLHLYR 486
Cdd:cd11033 344 FEELLD 349
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
264-482 5.83e-12

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: 67.39  E-value: 5.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 264 RVEKTNARLSGQLNEIVSKRAKEaetDSKDFLSLILKARESDpfakniftsDYISAVTYEHLL-----AGSATTAFTLSS 338
Cdd:cd11038 169 RIEAAVEELYDYADALIEARRAE---PGDDLISTLVAAEQDG---------DRLSDEELRNLIvallfAGVDTTRNQLGL 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 339 VLYLVSGHLDvEKRLLQEidgfgNRDLIPTAhdlqhkfpyldqvIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVW 418
Cdd:cd11038 237 AMLTFAEHPD-QWRALRE-----DPELAPAA-------------VEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVH 297
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30683024 419 LALGVLAKDPKNFPEPekfkpeRFDPNGEEEKHrhpyafIPFGIGPRACVGQ---RFALQEiKLTLL 482
Cdd:cd11038 298 LCSHAANRDPRVFDAD------RFDITAKRAPH------LGFGGGVHHCLGAflaRAELAE-ALTVL 351
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
276-488 9.98e-12

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: 66.68  E-value: 9.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 276 LNEIVSKRAKEAETDskDFLSLILKARESDpfakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQ 355
Cdd:cd20630 169 IEEVIAERRQAPVED--DLLTTLLRAEEDG----ERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKA 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 356 EidgfgnRDLIPTAhdlqhkfpyldqvIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEP 434
Cdd:cd20630 243 E------PELLRNA-------------LEEVLRWDNFGKMgTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDP 303
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 30683024 435 EKFKPErfdpngeeekhRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:cd20630 304 DRFDVR-----------RDPNANIAFGYGPHFCIGAALARLELELAVSTLLRRF 346
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
47-488 4.28e-11

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 65.00  E-value: 4.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   47 PGPTAMPLVGH-LPLMAKY---GPDVF-SVLAKQYGPIFRFQMGRQPLIIIAEAELCREVgIKKFKDLPNRSIPSPISaS 121
Cdd:PLN02987  33 PGSLGLPLVGEtLQLISAYkteNPEPFiDERVARYGSLFMTHLFGEPTVFSADPETNRFI-LQNEGKLFECSYPGSIS-N 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  122 PLHKKGLFFTRDKRWSKMRNTILSLYQPS----HLTSLIPTMHSFitsathNLDSKPRDIVFSNLFLKLTTDIIGQAAFG 197
Cdd:PLN02987 111 LLGKHSLLLMKGNLHKKMHSLTMSFANSSiikdHLLLDIDRLIRF------NLDSWSSRVLLMEEAKKITFELTVKQLMS 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  198 VDFGlsgkkpikdvEVTDFINQHVYSTTqlkmdlsgslsiilgllipilqEPFRQVLKRIPGTMDWRVEKTNARLSGQLN 277
Cdd:PLN02987 185 FDPG----------EWTESLRKEYVLVI----------------------EGFFSVPLPLFSTTYRRAIQARTKVAEALT 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  278 EIVSKRAKEAETDS---KDFLSLILKAreSDPFAKNIFTsDYISAVtyehLLAGSATTAFTLS-SVLYLVSGHLDVEKrL 353
Cdd:PLN02987 233 LVVMKRRKEEEEGAekkKDMLAALLAS--DDGFSDEEIV-DFLVAL----LVAGYETTSTIMTlAVKFLTETPLALAQ-L 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  354 LQEIDGFgnRDLIPTAHDLQ----HKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPK 429
Cdd:PLN02987 305 KEEHEKI--RAMKSDSYSLEwsdyKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHE 382
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 30683024  430 NFPEPEKFKPERFDPNGEEEKHRHpyAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:PLN02987 383 YFKDARTFNPWRWQSNSGTTVPSN--VFTPFGGGPRLCPGYELARVALSVFLHRLVTRF 439
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
338-508 4.62e-11

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


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 64.73  E-value: 4.62e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 338 SVLYLVSgHLDVEKRLLQEIDGFGNRDLIPTAHDlQHKFPYLDQVIKEAMRFYMVSPL-VARETAKEVEIGGYLLPKGTW 416
Cdd:cd20677 259 SLLYLIK-YPEIQDKIQEEIDEKIGLSRLPRFED-RKSLHYTEAFINEVFRHSSFVPFtIPHCTTADTTLNGYFIPKDTC 336
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 417 VWLALGVLAKDPKNFPEPEKFKPERF-DPNGEEEKHRHPYAFIpFGIGPRACVGQRFALQEIKLTLLHLYRNYIFRHSLE 495
Cdd:cd20677 337 VFINMYQVNHDETLWKDPDLFMPERFlDENGQLNKSLVEKVLI-FGMGVRKCLGEDVARNEIFVFLTTILQQLKLEKPPG 415
                       170
                ....*....|...
gi 30683024 496 MEIPLQLDYGIIL 508
Cdd:cd20677 416 QKLDLTPVYGLTM 428
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
293-486 1.19e-10

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: 63.34  E-value: 1.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 293 DFLSLILKARESDpfakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQeidgfgNRDLIPTAhdl 372
Cdd:cd20625 182 DLISALVAAEEDG----DRLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQLALLRA------DPELIPAA--- 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 373 qhkfpyldqvIKEAMRFYmvSP--LVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERfDPNgeeek 450
Cdd:cd20625 249 ----------VEELLRYD--SPvqLTARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITR-APN----- 310
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 30683024 451 hRHpyafIPFGIGPRACVGQRFALQEIKLTLLHLYR 486
Cdd:cd20625 311 -RH----LAFGAGIHFCLGAPLARLEAEIALRALLR 341
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
278-488 1.41e-10

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 63.56  E-value: 1.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  278 EIVSKRAKEAETDSKDFLSLILKARESDPFAKNIFTSdyisavtyeHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEI 357
Cdd:PLN02426 264 EVIRQRRKLGFSASKDLLSRFMASINDDKYLRDIVVS---------FLLAGRDTVASALTSFFWLLSKHPEVASAIREEA 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  358 DGFGNRDLIPTAHDLQHKFPYLDQVIKEAMRFYmvsPLVARET----AKEVEIGGYLLPKGTWVWLALGVLAKDPKNF-P 432
Cdd:PLN02426 335 DRVMGPNQEAASFEEMKEMHYLHAALYESMRLF---PPVQFDSkfaaEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgP 411
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 30683024  433 EPEKFKPERFDPNGEEEKhRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNY 488
Cdd:PLN02426 412 DCLEFKPERWLKNGVFVP-ENPFKYPVFQAGLRVCLGKEMALMEMKSVAVAVVRRF 466
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
351-485 1.90e-10

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: 62.78  E-value: 1.90e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 351 KRLLQEID---GFGNRDLIPTAHDLQHkFPYLDQVIKEAMRFYMVSpLVAReTAKE-----VEIGG-YLLPKGTWVWLAL 421
Cdd:cd20631 269 KRTLEKTGqkvSDGGNPIVLTREQLDD-MPVLGSIIKEALRLSSAS-LNIR-VAKEdftlhLDSGEsYAIRKDDIIALYP 345
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30683024 422 GVLAKDPKNFPEPEKFKPERF-DPNGEEE------KHRHPYAFIPFGIGPRACVGQRFALQEIK--LTLLHLY 485
Cdd:cd20631 346 QLLHLDPEIYEDPLTFKYDRYlDENGKEKttfyknGRKLKYYYMPFGSGTSKCPGRFFAINEIKqfLSLMLCY 418
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
378-485 3.29e-10

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: 62.32  E-value: 3.29e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 378 YLDQVIKEAMRFYMVS--PLVARE--TAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEK--- 450
Cdd:cd20632 285 YLESAINESLRLSSASmnIRVVQEdfTLKLESDGSVNLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKKTtfy 364
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30683024 451 ---HRHPYAFIPFGIGPRACVGQRFALQEIK--LTLLHLY 485
Cdd:cd20632 365 krgQKLKYYLMPFGSGSSKCPGRFFAVNEIKqfLSLLLLY 404
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
325-486 7.05e-10

C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; This family contains Gaeumannomyces graminis linoleate diol synthase (LDS) and similar proteins including Ssp1 from the phytopathogenic basidiomycete Ustilago maydis. LDS, also called linoleate (8R)-dioxygenase, catalyzes the dioxygenation of linoleic acid to (8R)-hydroperoxylinoleate and the isomerization of the resulting hydroperoxide to (7S,8S)-dihydroxylinoleate. Ssp1 is expressed in mature teliospores, which are produced by U. maydis only after infection of its host plant, maize. Ssp1 is localized on lipid bodies in germinating teliospores, suggesting a role in the mobilization of storage lipids. LDS and Ssp1 contain an N-terminal dioxygenase domain related to animal heme peroxidases, and a C-terminal cytochrome P450 domain. The LDS-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 60.82  E-value: 7.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 325 LLAGSATTAFTLSSVL-YLVS----GHLDVEKRLLQEIDGFGNRdliptahdlqhkfpyLDQVIKEAMRFYMVSPLVARE 399
Cdd:cd20612 196 AVGGVPTQSQAFAQILdFYLRrpgaAHLAEIQALARENDEADAT---------------LRGYVLEALRLNPIAPGLYRR 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 400 TAKEVEI-----GGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERfdPNgeeekhrHPYafIPFGIGPRACVGQRFAL 474
Cdd:cd20612 261 ATTDTTVadgggRTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR--PL-------ESY--IHFGHGPHQCLGEEIAR 329
                       170
                ....*....|..
gi 30683024 475 QEIKLTLLHLYR 486
Cdd:cd20612 330 AALTEMLRVVLR 341
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
256-488 9.93e-10

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 60.52  E-value: 9.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  256 RIPGTMDWRVEKTNARLSGQLNEIV-SKRAK------EAETDSKDFLSLILKAresdpfAKNIFTSDYISAVTYEHLLAG 328
Cdd:PLN03141 190 KLPGTRLYRSLQAKKRMVKLVKKIIeEKRRAmknkeeDETGIPKDVVDVLLRD------GSDELTDDLISDNMIDMMIPG 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  329 --SATTAFTLSsVLYLVSGHLDVEkrLLQEIDGFGNRDLIPTAHDLQ----HKFPYLDQVIKEAMRFYMVSPLVARETAK 402
Cdd:PLN03141 264 edSVPVLMTLA-VKFLSDCPVALQ--QLTEENMKLKRLKADTGEPLYwtdyMSLPFTQNVITETLRMGNIINGVMRKAMK 340
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  403 EVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFdpngeEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLL 482
Cdd:PLN03141 341 DVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRW-----QEKDMNNSSFTPFGGGQRLCPGLDLARLEASIFLH 415

                 ....*.
gi 30683024  483 HLYRNY 488
Cdd:PLN03141 416 HLVTRF 421
PLN02500 PLN02500
cytochrome P450 90B1
257-488 1.03e-09

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 60.65  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  257 IPGTMDWRVEKTNARLSG----QLNEIVSKRAKEAET-DSKDFLSLILKAREsdpfakniFTSDYISAVTYEHLLAGSAT 331
Cdd:PLN02500 223 FPGTAYRKALKSRATILKfierKMEERIEKLKEEDESvEEDDLLGWVLKHSN--------LSTEQILDLILSLLFAGHET 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  332 TAFTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQ----HKFPYLDQVIKEAMRFYMVSPLVARETAKEVEIG 407
Cdd:PLN02500 295 SSVAIALAIFFLQGCPKAVQELREEHLEIARAKKQSGESELNwedyKKMEFTQCVINETLRLGNVVRFLHRKALKDVRYK 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  408 GYLLPKGtwvWLALGVLAK---DPKNFPEPEKFKPERFDPNGEEEKHRHPYA-----FIPFGIGPRACVGQRFALQEIKL 479
Cdd:PLN02500 375 GYDIPSG---WKVLPVIAAvhlDSSLYDQPQLFNPWRWQQNNNRGGSSGSSSattnnFMPFGGGPRLCAGSELAKLEMAV 451

                 ....*....
gi 30683024  480 TLLHLYRNY 488
Cdd:PLN02500 452 FIHHLVLNF 460
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
264-476 1.13e-09

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: 60.27  E-value: 1.13e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 264 RVEKTNARLSGQLNEIV-SKRAKEAEtdskDFLSLILKARESDpfakNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYL 342
Cdd:cd11031 161 EAEAARQELRGYMAELVaARRAEPGD----DLLSALVAARDDD----DRLSEEELVTLAVGLLVAGHETTASQIGNGVLL 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 343 VSGHLDVEKRLLqeidgfGNRDLIPTAhdlqhkfpyldqvIKEAMRFY-----MVSPLVAREtakEVEIGGYLLPKGTWV 417
Cdd:cd11031 233 LLRHPEQLARLR------ADPELVPAA-------------VEELLRYIplgagGGFPRYATE---DVELGGVTIRAGEAV 290
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30683024 418 WLALGVLAKDPKNFPEpekfkPERFDPNGEEEKHrhpyafIPFGIGPRACVGQRFA---LQE 476
Cdd:cd11031 291 LVSLNAANRDPEVFPD-----PDRLDLDREPNPH------LAFGHGPHHCLGAPLArleLQV 341
PLN02971 PLN02971
tryptophan N-hydroxylase
47-491 2.18e-09

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 59.67  E-value: 2.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024   47 PGPTAMPLVGHLPLMAKYGPdVF----SVLAKQYGPIFRFQMGRQPLIIIAEAELCREvgIKKFKDLPNRSIPSPISASP 122
Cdd:PLN02971  60 PGPTGFPIVGMIPAMLKNRP-VFrwlhSLMKELNTEIACVRLGNTHVIPVTCPKIARE--IFKQQDALFASRPLTYAQKI 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  123 L---HKKGLFFTRDKRWSKMRNTILS-LYQPS-----HLTSLIPTMHsfITSATHNL--DSKPRDIVF------SNLFLK 185
Cdd:PLN02971 137 LsngYKTCVITPFGEQFKKMRKVIMTeIVCPArhrwlHDNRAEETDH--LTAWLYNMvkNSEPVDLRFvtrhycGNAIKR 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  186 LttdIIGQAAFGVDFGLSGKKPIKDVEVTDF------------INQHVYSTTQLKMDLSGSLSIILGLLIPILQEPFrqV 253
Cdd:PLN02971 215 L---MFGTRTFSEKTEPDGGPTLEDIEHMDAmfeglgftfafcISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPI--I 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  254 LKRIPGtmdWRVEKtnarlsgqlneivskrakeaETDSKDFLSLILKAResDPFAKNIFTSDYISAVTYEHLLAGSATTA 333
Cdd:PLN02971 290 DERIKM---WREGK--------------------RTQIEDFLDIFISIK--DEAGQPLLTADEIKPTIKELVMAAPDNPS 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  334 FTLSSVLYLVSGHLDVEKRLLQEIDGFGNRDLIPTAHDLQhKFPYLDQVIKEAMRFYMVSPLVARETA-KEVEIGGYLLP 412
Cdd:PLN02971 345 NAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIP-KLNYVKAIIREAFRLHPVAAFNLPHVAlSDTTVAGYHIP 423
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  413 KGTWVWLALGVLAKDPKNFPEPEKFKPER-FDPNGEEEKHRHPYAFIPFGIGPRACVGQRFALQEIKLTLLHLYRNYIFR 491
Cdd:PLN02971 424 KGSQVLLSRYGLGRNPKVWSDPLSFKPERhLNECSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWK 503
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
325-482 2.59e-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: 59.08  E-value: 2.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 325 LLAGSATTAFTLSSVLYLVSGHLDvEKRLLQEidgfgNRDLIPTAhdlqhkfpyldqvIKEAMRFY-MVSPLVARETAKE 403
Cdd:cd11029 220 LVAGHETTVNLIGNGVLALLTHPD-QLALLRA-----DPELWPAA-------------VEELLRYDgPVALATLRFATED 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 404 VEIGGYLLPKGTWVWLALGVLAKDPKNFPEpekfkPERFDPNGEEEKHrhpyafIPFGIGPRACVGQRFALQE--IKLTL 481
Cdd:cd11029 281 VEVGGVTIPAGEPVLVSLAAANRDPARFPD-----PDRLDITRDANGH------LAFGHGIHYCLGAPLARLEaeIALGA 349

                .
gi 30683024 482 L 482
Cdd:cd11029 350 L 350
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
365-479 5.52e-09

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: 58.15  E-value: 5.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 365 LIPTAHDLQHKFPYLDQVIKEAMRFyMVSPLVARETAKEVEI---GG--YLLPKGTWVWLA--LGVlAKDPKNFPEPEKF 437
Cdd:cd20633 282 LINLTRDMLLKTPVLDSAVEETLRL-TAAPVLIRAVVQDMTLkmaNGreYALRKGDRLALFpyLAV-QMDPEIHPEPHTF 359
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 30683024 438 KPERF-DPNGEEEK------HRHPYAFIPFGIGPRACVGQRFALQEIKL 479
Cdd:cd20633 360 KYDRFlNPDGGKKKdfykngKKLKYYNMPWGAGVSICPGRFFAVNEMKQ 408
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
270-477 5.80e-09

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: 57.87  E-value: 5.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 270 ARLSGQLNEIVSKRAKEAETDSKDFLSLILKARESDPFAkniFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDV 349
Cdd:cd11080 150 LRCAEQLSQYLLPVIEERRVNPGSDLISILCTAEYEGEA---LSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQ 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 350 EKRLLQEidgfgnRDLIPTAhdlqhkfpyldqvIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPK 429
Cdd:cd11080 227 LAAVRAD------RSLVPRA-------------IAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPA 287
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 30683024 430 NFPEPEKFKPERFDPNGEEekhrhpyAFIP------FGIGPRACVGQRFALQEI 477
Cdd:cd11080 288 AFEDPDTFNIHREDLGIRS-------AFSGaadhlaFGSGRHFCVGAALAKREI 334
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
379-481 1.58e-08

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: 56.59  E-value: 1.58e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 379 LDQVIKEAMRFYmvSPLVA--RETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPerfdpngeeekHRHPYA 456
Cdd:cd11079 227 LPAAIDEILRLD--DPFVAnrRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDP-----------DRHAAD 293
                        90       100
                ....*....|....*....|....*
gi 30683024 457 FIPFGIGPRACVGQRFALQEIKLTL 481
Cdd:cd11079 294 NLVYGRGIHVCPGAPLARLELRILL 318
PLN03018 PLN03018
homomethionine N-hydroxylase
283-469 2.17e-08

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 56.56  E-value: 2.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  283 RAKEAETDSKDFLSLILKARESDpfAKNIFTSDYISAVTYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFGN 362
Cdd:PLN03018 283 REKGGKAAVEDWLDTFITLKDQN--GKYLVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVG 360
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024  363 RDLIPTAHDLQHkFPYLDQVIKEAMRFY----MVSPLVAREtakEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFK 438
Cdd:PLN03018 361 KDRLVQESDIPN-LNYLKACCRETFRIHpsahYVPPHVARQ---DTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYE 436
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 30683024  439 PERfDPNGE---------EEKHRhpyaFIPFGIGPRACVG 469
Cdd:PLN03018 437 PER-HLQGDgitkevtlvETEMR----FVSFSTGRRGCVG 471
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
321-484 5.20e-08

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: 55.24  E-value: 5.20e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 321 TYEHLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGFG------------NRDLIPTAHdlqhkfpYLDQVIKEAMR 388
Cdd:cd20637 231 TIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELRSNGilhngclcegtlRLDTISSLK-------YLDCVIKEVLR 303
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 389 FYmvSPLVA--RETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERFDPNGEEEKHRHpYAFIPFGIGPRA 466
Cdd:cd20637 304 LF--TPVSGgyRTALQTFELDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGR-FHYLPFGGGVRT 380
                       170
                ....*....|....*...
gi 30683024 467 CVGQRFALQEIKLTLLHL 484
Cdd:cd20637 381 CLGKQLAKLFLKVLAVEL 398
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
374-498 7.71e-08

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: 54.57  E-value: 7.71e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 374 HKFPYLDQVIKEAMRFYMVSPLV-ARetAKE---VEIGG--YLLPKGTwvwLALGVLA---KDPKNFPEPEKFKPERFDp 444
Cdd:cd11071 283 EKMPLLKSVVYETLRLHPPVPLQyGR--ARKdfvIESHDasYKIKKGE---LLVGYQPlatRDPKVFDNPDEFVPDRFM- 356
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30683024 445 nGEEEK-------HRHPYAFIPfGIGPRACVGQRFALQEIKLTLLHLYRNYifrHSLEMEI 498
Cdd:cd11071 357 -GEEGKllkhliwSNGPETEEP-TPDNKQCPGKDLVVLLARLFVAELFLRY---DTFTIEP 412
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
324-491 2.27e-07

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: 52.85  E-value: 2.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 324 HLLAGSATTAFTLSSVLYLVSGHLDVEKRLLQEIDGfgnrdlIPTAHDLqhkfPYLDQVIKEAMRFYMVSPLVARETAKE 403
Cdd:cd20624 199 QWLFAFDAAGMALLRALALLAAHPEQAARAREEAAV------PPGPLAR----PYLRACVLDAVRLWPTTPAVLRESTED 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 404 VEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPER-FDpnGEEEKHrhpYAFIPFGIGPRACVGQRFALQEIKLTLL 482
Cdd:cd20624 269 TVWGGRTVPAGTGFLIFAPFFHRDDEALPFADRFVPEIwLD--GRAQPD---EGLVPFSAGPARCPGENLVLLVASTALA 343

                ....*....
gi 30683024 483 HLYRNYIFR 491
Cdd:cd20624 344 ALLRRAEID 352
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
325-486 5.55e-07

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: 51.75  E-value: 5.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 325 LLAGSATTAFTLS-SVLYLVsGHLDVEKRLLqeidgfGNRDLIPTAhdlqhkfpyldqvIKEAMRFYMVSPLVARETAKE 403
Cdd:cd11030 217 LVAGHETTANMIAlGTLALL-EHPEQLAALR------ADPSLVPGA-------------VEELLRYLSIVQDGLPRVATE 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 404 -VEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERfdpngeeeKHRHPYAFipfGIGPRACVGQRFALQEIKLTLL 482
Cdd:cd11030 277 dVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR--------PARRHLAF---GHGVHQCLGQNLARLELEIALP 345

                ....
gi 30683024 483 HLYR 486
Cdd:cd11030 346 TLFR 349
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
327-479 1.90e-06

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: 50.14  E-value: 1.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 327 AGSATtaFTLssVLYLVSgHLDVEKRLLQEIDGFGNRDLIPTAH------DLQHKFPYLDQVIKEAMRFyMVSPLVARET 400
Cdd:cd20634 237 AGPAA--FWL--LLFLLK-HPEAMAAVRGEIQRIKHQRGQPVSQtltinqELLDNTPVFDSVLSETLRL-TAAPFITREV 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 401 AKEVEI-----GGYLLPKGTWVWLALGVLAK-DPKNFPEPEKFKPERF-DPNGEEEKH------RHPYAFIPFGIGPRAC 467
Cdd:cd20634 311 LQDMKLrladgQEYNLRRGDRLCLFPFLSPQmDPEIHQEPEVFKYDRFlNADGTEKKDfykngkRLKYYNMPWGAGDNVC 390
                       170
                ....*....|..
gi 30683024 468 VGQRFALQEIKL 479
Cdd:cd20634 391 IGRHFAVNSIKQ 402
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
379-473 5.27e-05

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: 45.56  E-value: 5.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 379 LDQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEpekfkPERFDPngeeekHRHPYAFI 458
Cdd:cd11036 221 AAAAVAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPD-----PDRFDL------GRPTARSA 289
                        90
                ....*....|....*
gi 30683024 459 PFGIGPRACVGQRFA 473
Cdd:cd11036 290 HFGLGRHACLGAALA 304
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
381-482 6.68e-05

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: 45.19  E-value: 6.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 381 QVIKEAMRFymVSPLVA--RETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPepekfKPERFDPNGEEEKHrhpyafI 458
Cdd:cd11039 248 RAFEEGLRW--ISPIGMspRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFE-----NPDRFDVFRPKSPH------V 314
                        90       100
                ....*....|....*....|....*..
gi 30683024 459 PFGIGPRACVGQRFALQ---EIKLTLL 482
Cdd:cd11039 315 SFGAGPHFCAGAWASRQmvgEIALPEL 341
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
380-478 1.02e-03

cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial metabolism of the military explosive, hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX). XplA has an unusual structural organization comprising a heme domain that is fused to its flavodoxin redox partner. XplA, along with its partner reductase XplB, are plasmid encoded and the xplA gene has now been found in divergent genera across the globe with near sequence identity. It has only been detected at explosive-contaminated sites, suggesting rapid dissemination of this novel catabolic activity, possibly within a 50-year period since the introduction of RDX into the environment. XplA belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 41.26  E-value: 1.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30683024 380 DQVIKEAMRFYMVSPLVARETAKEVEIGGYLLPKGTWVWLALGVLAKDPKNFPEPEKFKPERfDPNGEEEkhrhpyafIP 459
Cdd:cd20619 235 AAIINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTR-PPAASRN--------LS 305
                        90
                ....*....|....*....
gi 30683024 460 FGIGPRACVGQRFALQEIK 478
Cdd:cd20619 306 FGLGPHSCAGQIISRAEAT 324
 
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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