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Conserved domains on  [gi|24653745|ref|NP_611003|]
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cytochrome P450 6a21 [Drosophila melanogaster]

Protein Classification

cytochrome P450( domain architecture ID 15296490)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
68-498 0e+00

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: 593.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  68 GSGPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYM 147
Cdd:cd11056   1 GGEPFVGIYLFRRPALLVRDPELIKQILVKDFAHFHDRGLYSDEKDDPLSANLFSLDGEKWKELRQKLTPAFTSGKLKNM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 148 FPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLTEQRLGPVGIGFVN 227
Cdd:cd11056  81 FPLMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGLDANSLNDPENEFREMGRRLFEPSRLRGLKFMLLF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 228 SFPNLARRLHMKMTAEPIERFFMRIVRETVAFREQNNIRRNDFMDQLIDLKNKPLMvSQSGESVNLTIEEIAAQAFVFFA 307
Cdd:cd11056 161 FFPKLARLLRLKFFPKEVEDFFRKLVRDTIEYREKNNIVRNDFIDLLLELKKKGKI-EDDKSEKELTDEELAAQAFVFFL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 308 AGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEV 387
Cdd:cd11056 240 AGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTL 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 388 PGhPKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLI 467
Cdd:cd11056 320 PG-TDVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLL 398
                       410       420       430
                ....*....|....*....|....*....|.
gi 24653745 468 KDFKFSVCEKTTIPMTYNKEMFLIASNSGIY 498
Cdd:cd11056 399 SNFRVEPSSKTKIPLKLSPKSFVLSPKGGIW 429
 
Name Accession Description Interval E-value
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
68-498 0e+00

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: 593.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  68 GSGPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYM 147
Cdd:cd11056   1 GGEPFVGIYLFRRPALLVRDPELIKQILVKDFAHFHDRGLYSDEKDDPLSANLFSLDGEKWKELRQKLTPAFTSGKLKNM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 148 FPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLTEQRLGPVGIGFVN 227
Cdd:cd11056  81 FPLMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGLDANSLNDPENEFREMGRRLFEPSRLRGLKFMLLF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 228 SFPNLARRLHMKMTAEPIERFFMRIVRETVAFREQNNIRRNDFMDQLIDLKNKPLMvSQSGESVNLTIEEIAAQAFVFFA 307
Cdd:cd11056 161 FFPKLARLLRLKFFPKEVEDFFRKLVRDTIEYREKNNIVRNDFIDLLLELKKKGKI-EDDKSEKELTDEELAAQAFVFFL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 308 AGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEV 387
Cdd:cd11056 240 AGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTL 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 388 PGhPKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLI 467
Cdd:cd11056 320 PG-TDVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLL 398
                       410       420       430
                ....*....|....*....|....*....|.
gi 24653745 468 KDFKFSVCEKTTIPMTYNKEMFLIASNSGIY 498
Cdd:cd11056 399 SNFRVEPSSKTKIPLKLSPKSFVLSPKGGIW 429
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
35-499 1.33e-102

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: 315.37  E-value: 1.33e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745    35 PCEEPHILMGSMKGVRTARSFNEIWTSYYNKFrgsGPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRG---FFHNP 111
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKGNLHSVFTKLQKKY---GPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPdepWFATS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   112 EDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAF 191
Cdd:pfam00067  79 RGPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   192 GIECSSLKDPDA-EFREMGRR--SLTEQRLGPVGIGF--VNSFPNLARRLHMKMTAEPIE--RFFMRIVRETVafrEQNN 264
Cdd:pfam00067 159 GERFGSLEDPKFlELVKAVQElsSLLSSPSPQLLDLFpiLKYFPGPHGRKLKRARKKIKDllDKLIEERRETL---DSAK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   265 IRRNDFMDQLIDLKNKplmvsqsGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEK 344
Cdd:pfam00067 236 KSPRDFLDALLLAKEE-------EDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   345 cNGELNYESMKDLVYLDQVVSETLRLYTVLPVLN-RECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNP 423
Cdd:pfam00067 309 -KRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLpREVTKDTVIPG---YLIPKGTLVIVNLYALHRDPEVFPNPEEFDP 384
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653745   424 DNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTTIPMTYNKEMFLIASNSGIYL 499
Cdd:pfam00067 385 ERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLK 460
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
62-470 1.43e-49

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: 175.08  E-value: 1.43e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  62 YYNKFRGSGPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQ-LFLLDGQKWRTMRNKLSSTFT 140
Cdd:COG2124  24 FYARLREYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDsLLTLDGPEHTRLRRLVQPAFT 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 141 SGKMKYMFPTVVKVANEFTDvfgqNVAKSPVVEVRELLARFTTDVIGTCAFGIecsslkdPDAEFREMgrrslteQRLGP 220
Cdd:COG2124 104 PRRVAALRPRIREIADELLD----RLAARGPVDLVEEFARPLPVIVICELLGV-------PEEDRDRL-------RRWSD 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 221 VGIGFVNSFPNLARRLHMKMTAEpIERFFMRIVREtvafREQNniRRNDFMDQLIDlknkplmVSQSGESvnLTIEEIAA 300
Cdd:COG2124 166 ALLDALGPLPPERRRRARRARAE-LDAYLRELIAE----RRAE--PGDDLLSALLA-------ARDDGER--LSDEELRD 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 301 QAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKEcqeviekcngelnyesmkdLVYLDQVVSETLRLYTVLPVLNRE 380
Cdd:COG2124 230 ELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE-------------------PELLPAAVEETLRLYPPVPLLPRT 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 381 CLEDYEVPGHPkyvIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDSVEWLPFGDGPRNCIGMRFGQMQAR 460
Cdd:COG2124 291 ATEDVELGGVT---IPAGDRVLLSLAAANRDPRVFPDPDRFDPD---------RPPNAHLPFGGGPHRCLGAALARLEAR 358
                       410
                ....*....|
gi 24653745 461 IGLALLIKDF 470
Cdd:COG2124 359 IALATLLRRF 368
PLN02290 PLN02290
cytokinin trans-hydroxylase
76-476 5.83e-32

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 128.39  E-value: 5.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   76 YWF-RRPAVFVLETSLAKQILIKeFNKFTDRGFFHNPEDDPLSGQ-LFLLDGQKWRTMRNKLSSTFTSGKMK----YMFP 149
Cdd:PLN02290  99 YWNgTEPRLCLTETELIKELLTK-YNTVTGKSWLQQQGTKHFIGRgLLMANGADWYHQRHIAAPAFMGDRLKgyagHMVE 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  150 TVVKVANEFtdvfgQNVAKSPV--VEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLTEQR-LGPVGIGFv 226
Cdd:PLN02290 178 CTKQMLQSL-----QKAVESGQteVEIGEYMTRLTADIISRTEFDSSYEKGKQIFHLLTVLQRLCAQATRhLCFPGSRF- 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  227 nsFPNLARRlHMKMTAEPIERFFMRIVRETvafREQNNIRRNDF--MDQLIDLKNKplMVSQSGESVNLTIEEIAAQAFV 304
Cdd:PLN02290 252 --FPSKYNR-EIKSLKGEVERLLMEIIQSR---RDCVEIGRSSSygDDLLGMLLNE--MEKKRSNGFNLNLQLIMDECKT 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  305 FFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEViekCNGEL-NYESMKDLVYLDQVVSETLRLYTVLPVLNRECLE 383
Cdd:PLN02290 324 FFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEV---CGGETpSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFE 400
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  384 DYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLY-ANPNTFNPDNFSPERVKErdSVEWLPFGDGPRNCIGMRFGQMQARIG 462
Cdd:PLN02290 401 DIKLGD---LHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAP--GRHFIPFAAGPRNCIGQAFAMMEAKII 475
                        410
                 ....*....|....
gi 24653745  463 LALLIKDFKFSVCE 476
Cdd:PLN02290 476 LAMLISKFSFTISD 489
 
Name Accession Description Interval E-value
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
68-498 0e+00

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: 593.75  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  68 GSGPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYM 147
Cdd:cd11056   1 GGEPFVGIYLFRRPALLVRDPELIKQILVKDFAHFHDRGLYSDEKDDPLSANLFSLDGEKWKELRQKLTPAFTSGKLKNM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 148 FPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLTEQRLGPVGIGFVN 227
Cdd:cd11056  81 FPLMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGLDANSLNDPENEFREMGRRLFEPSRLRGLKFMLLF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 228 SFPNLARRLHMKMTAEPIERFFMRIVRETVAFREQNNIRRNDFMDQLIDLKNKPLMvSQSGESVNLTIEEIAAQAFVFFA 307
Cdd:cd11056 161 FFPKLARLLRLKFFPKEVEDFFRKLVRDTIEYREKNNIVRNDFIDLLLELKKKGKI-EDDKSEKELTDEELAAQAFVFFL 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 308 AGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEV 387
Cdd:cd11056 240 AGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTL 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 388 PGhPKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLI 467
Cdd:cd11056 320 PG-TDVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLL 398
                       410       420       430
                ....*....|....*....|....*....|.
gi 24653745 468 KDFKFSVCEKTTIPMTYNKEMFLIASNSGIY 498
Cdd:cd11056 399 SNFRVEPSSKTKIPLKLSPKSFVLSPKGGIW 429
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
70-498 2.50e-117

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: 351.89  E-value: 2.50e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFhNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFP 149
Cdd:cd11055   3 GKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRPLF-ILLDEPFDSSLLFLKGERWKRLRTTLSPTFSSGKLKLMVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 150 TVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLTEQRLGPVGIGFVNSF 229
Cdd:cd11055  82 IINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKAAKKIFRNSIIRLFLLLLLFPL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 230 PNLARRLHMKMTAEPIERFFMRIVRETVAFREQNN-IRRNDFMDQLIDLKNKPLMVSQSGesvnLTIEEIAAQAFVFFAA 308
Cdd:cd11055 162 RLFLFLLFPFVFGFKSFSFLEDVVKKIIEQRRKNKsSRRKDLLQLMLDAQDSDEDVSKKK----LTDDEIVAQSFIFLLA 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 309 GFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVP 388
Cdd:cd11055 238 GYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPD-DGSPTYDTVSKLKYLDMVINETLRLYPPAFFISRECKEDCTIN 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 389 GhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIK 468
Cdd:cd11055 317 G---VFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKILQ 393
                       410       420       430
                ....*....|....*....|....*....|
gi 24653745 469 DFKFSVCEKTTIPMTYNKEMFLIASNsGIY 498
Cdd:cd11055 394 KFRFVPCKETEIPLKLVGGATLSPKN-GIY 422
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
35-499 1.33e-102

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: 315.37  E-value: 1.33e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745    35 PCEEPHILMGSMKGVRTARSFNEIWTSYYNKFrgsGPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRG---FFHNP 111
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKGNLHSVFTKLQKKY---GPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPdepWFATS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   112 EDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAF 191
Cdd:pfam00067  79 RGPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   192 GIECSSLKDPDA-EFREMGRR--SLTEQRLGPVGIGF--VNSFPNLARRLHMKMTAEPIE--RFFMRIVRETVafrEQNN 264
Cdd:pfam00067 159 GERFGSLEDPKFlELVKAVQElsSLLSSPSPQLLDLFpiLKYFPGPHGRKLKRARKKIKDllDKLIEERRETL---DSAK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   265 IRRNDFMDQLIDLKNKplmvsqsGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEK 344
Cdd:pfam00067 236 KSPRDFLDALLLAKEE-------EDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   345 cNGELNYESMKDLVYLDQVVSETLRLYTVLPVLN-RECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNP 423
Cdd:pfam00067 309 -KRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLpREVTKDTVIPG---YLIPKGTLVIVNLYALHRDPEVFPNPEEFDP 384
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653745   424 DNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTTIPMTYNKEMFLIASNSGIYL 499
Cdd:pfam00067 385 ERFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLK 460
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
70-498 2.46e-73

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: 239.36  E-value: 2.46e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFhNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFP 149
Cdd:cd20649   3 GPICGYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNRMKA-NLITKPMSDSLLCLRDERWKRVRSILTPAFSAAKMKEMVP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 150 TVvkvaNEFTDVFGQNV---AKS-PVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLTEQRLGPVGIgF 225
Cdd:cd20649  82 LI----NQACDVLLRNLksyAESgNAFNIQRCYGCFTMDVVASVAFGTQVDSQKNPDDPFVKNCKRFFEFSFFRPILI-L 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 226 VNSFPN----LARRLHMKMTAEpIERFFMRIVRETVAFREQN--NIRRNDFMDQLIDLKN--KPL------MVSQSGESV 291
Cdd:cd20649 157 FLAFPFimipLARILPNKSRDE-LNSFFTQCIRNMIAFRDQQspEERRRDFLQLMLDARTsaKFLsvehfdIVNDADESA 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 292 N--------------------LTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNY 351
Cdd:cd20649 236 YdghpnspaneqtkpskqkrmLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSK-HEMVDY 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 352 ESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGHpkyVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERV 431
Cdd:cd20649 315 ANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQ---RIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAK 391
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653745 432 KERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTTIPMTYnKEMFLIASNSGIY 498
Cdd:cd20649 392 QRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIPLQL-KSKSTLGPKNGVY 457
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
70-473 2.71e-73

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: 237.41  E-value: 2.71e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFP 149
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 150 TVVKVANEFTDVFGQNVAKSpvVEVRELLARFTTDVIGTCAFGIEcssLKDPDAEFREMGRRSLTEQRLGPVgigfvNSF 229
Cdd:cd00302  81 VIREIARELLDRLAAGGEVG--DDVADLAQPLALDVIARLLGGPD---LGEDLEELAELLEALLKLLGPRLL-----RPL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 230 PNLARRLHMKMTAEpierfFMRIVRETVAFREQNNIRRNDFMDQLIDLKNKPLmvsqsgesvnlTIEEIAAQAFVFFAAG 309
Cdd:cd00302 151 PSPRLRRLRRARAR-----LRDYLEELIARRRAEPADDLDLLLLADADDGGGL-----------SDEEIVAELLTLLLAG 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 310 FETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcnGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPG 389
Cdd:cd00302 215 HETTASLLAWALYLLARHPEVQERLRAEIDAVL----GDGTPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGG 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 390 hpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSveWLPFGDGPRNCIGMRFGQMQARIGLALLIKD 469
Cdd:cd00302 291 ---YTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEPRYA--HLPFGAGPHRCLGARLARLELKLALATLLRR 365

                ....
gi 24653745 470 FKFS 473
Cdd:cd00302 366 FDFE 369
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
74-490 1.07e-71

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: 234.23  E-value: 1.07e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  74 GFYWFRRPAVFVLETSLAKQILIKE-FNKFTDRGFFHnpEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVV 152
Cdd:cd20650   7 GIYDGRQPVLAITDPDMIKTVLVKEcYSVFTNRRPFG--PVGFMKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMFPIIA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 153 KVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLTEQRLGPVGIgFVNSFPNL 232
Cdd:cd20650  85 QYGDVLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLKFDFLDPLFL-SITVFPFL 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 233 A---RRLHMKMTAEPIERFFMRIVRETVAFREQN-NIRRNDFMDQLIDLKNkplmvSQSGESVN-LTIEEIAAQAFVFFA 307
Cdd:cd20650 164 TpilEKLNISVFPKDVTNFFYKSVKKIKESRLDStQKHRVDFLQLMIDSQN-----SKETESHKaLSDLEILAQSIIFIF 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 308 AGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEV 387
Cdd:cd20650 239 AGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPN-KAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEI 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 388 PGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLI 467
Cdd:cd20650 318 NG---VFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVL 394
                       410       420
                ....*....|....*....|...
gi 24653745 468 KDFKFSVCEKTTIPMTYNKEMFL 490
Cdd:cd20650 395 QNFSFKPCKETQIPLKLSLQGLL 417
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
70-473 3.14e-60

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: 203.91  E-value: 3.14e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQIL--IKEFNKFTDRGFFHnpeddPLSGQ-LFLLDGQKWRTMRNKLSSTFTSGKMKY 146
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPEDIEVILssSKLITKSFLYDFLK-----PWLGDgLLTSTGEKWRKRRKLLTPAFHFKILES 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 147 MFPTVVKVANEFTDVFGQNVAKsPVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEfremgrrslteqrlgpvgigFV 226
Cdd:cd20628  76 FVEVFNENSKILVEKLKKKAGG-GEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSE--------------------YV 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 227 NSFPNLARRLHMKMTaepieRFFMR---IVRETVAFREQNNIRR--NDFMDQLIDL---------------------KNK 280
Cdd:cd20628 135 KAVKRILEIILKRIF-----SPWLRfdfIFRLTSLGKEQRKALKvlHDFTNKVIKErreelkaekrnseeddefgkkKRK 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 281 P---LMVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELNYESMKDL 357
Cdd:cd20628 210 AfldLLLEAHEDGGPLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDRRPTLEDLNKM 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 358 VYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSV 437
Cdd:cd20628 290 KYLERVIKETLRLYPSVPFIGRRLTEDIKLDG---YTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPY 366
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 24653745 438 EWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFS 473
Cdd:cd20628 367 AYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVL 402
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
120-481 4.26e-60

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: 204.04  E-value: 4.26e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 120 LFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVAKSP----VVEVRELLARFTTDVIGTCAFGIEC 195
Cdd:cd11069  53 LLAAEGEEHKRQRKILNPAFSYRHVKELYPIFWSKAEELVDKLEEEIEESGdesiSIDVLEWLSRATLDIIGLAGFGYDF 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 196 SSLKDPDAEFREMGRRSLTEQRLGPVGIGFVNSFP-NLARRL------HMKMTAEPIERFFMRIVRE-TVAFREQNNIRR 267
Cdd:cd11069 133 DSLENPDNELAEAYRRLFEPTLLGSLLFILLLFLPrWLVRILpwkanrEIRRAKDVLRRLAREIIREkKAALLEGKDDSG 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 268 NDFMDQLIDLKNkplmvsqSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNG 347
Cdd:cd11069 213 KDILSILLRAND-------FADDERLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPD 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 348 E-LNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGHPkyvIKKGMPVLIPCGAMHRDEKLY-ANPNTFNPDN 425
Cdd:cd11069 286 GdLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKDTVIKGVP---IPKGTVVLIPPAAINRSPEIWgPDAEEFNPER 362
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24653745 426 F---SPERVKERDSV--EWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTTIP 481
Cdd:cd11069 363 WlepDGAASPGGAGSnyALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPDAEVE 423
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
120-482 2.68e-56

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: 193.59  E-value: 2.68e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 120 LFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVvEVRELLARFTTDVIGTCAFGIECSSLK 199
Cdd:cd11057  47 LFSAPYPIWKLQRKALNPSFNPKILLSFLPIFNEEAQKLVQRLDTYVGGGEF-DILPDLSRCTLEMICQTTLGSDVNDES 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 200 DPDAEFREMGRRSLTeqrLGPVGIGFVNSFPNLARRL-----HMKMTAEPIERFFMRIVRETVAFREQNNI--------- 265
Cdd:cd11057 126 DGNEEYLESYERLFE---LIAKRVLNPWLHPEFIYRLtgdykEEQKARKILRAFSEKIIEKKLQEVELESNldseedeen 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 266 --RRNDFMDQLIDLKNKplmvsqsgeSVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIE 343
Cdd:cd11057 203 grKPQIFIDQLLELARN---------GEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFP 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 344 KCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpKYVIKKGMPVLIPCGAMHRDEKLY-ANPNTFN 422
Cdd:cd11057 274 DDGQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSN--GVVIPKGTTIVIDIFNMHRRKDIWgPDADQFD 351
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 423 PDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFsvceKTTIPM 482
Cdd:cd11057 352 PDNFLPERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRL----KTSLRL 407
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
59-474 6.13e-54

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: 187.16  E-value: 6.13e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  59 WTSYYNKfrgsgPFagFYWF-RRPAVFVLETSLAKQILIKEFnKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSS 137
Cdd:cd11052   7 WIKQYGK-----NF--LYWYgTDPRLYVTEPELIKELLSKKE-GYFGKSPLQPGLKKLLGRGLVMSNGEKWAKHRRIANP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 138 TFTSGKMKYMFPTVVKVANEFTDVFGQNVAKS-PVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRrsLTEQ 216
Cdd:cd11052  79 AFHGEKLKGMVPAMVESVSDMLERWKKQMGEEgEEVDVFEEFKALTADIISRTAFGSSYEEGKEVFKLLRELQK--ICAQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 217 RLGPVGIGFVNSFPNlARRLHMKMTAEPIERFFMRIV--RETVAFREQNNIRRNDFMDQLIDLKNKplmvsqSGESVNLT 294
Cdd:cd11052 157 ANRDVGIPGSRFLPT-KGNKKIKKLDKEIEDSLLEIIkkREDSLKMGRGDDYGDDLLGLLLEANQS------DDQNKNMT 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 295 IEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKEcqeVIEKC-NGELNYESMKDLVYLDQVVSETLRLYTV 373
Cdd:cd11052 230 VQEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREE---VLEVCgKDKPPSDSLSKLKTVSMVINESLRLYPP 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 374 LPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLY-ANPNTFNPDNFSPERVKERDS-VEWLPFGDGPRNCIG 451
Cdd:cd11052 307 AVFLTRKAKEDIKLGG---LVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGVAKAAKHpMAFLPFGLGPRNCIG 383
                       410       420
                ....*....|....*....|...
gi 24653745 452 MRFGQMQARIGLALLIKDFKFSV 474
Cdd:cd11052 384 QNFATMEAKIVLAMILQRFSFTL 406
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
57-476 1.44e-52

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: 183.49  E-value: 1.44e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  57 EIWTSYYNKFrgsGPFAGFYWFRRPAVFVLETSLAKQILIKE-FNK--FTDRGFFHnpeddpLSGQLFL-------LDGQ 126
Cdd:cd20613   2 DLLLEWAKEY---GPVFVFWILHRPIVVVSDPEAVKEVLITLnLPKppRVYSRLAF------LFGERFLgnglvteVDHE 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 127 KWRTMRNKLSSTFTSGKMKYMFPTVvkvaNEFTDVFGQNVAK----SPVVEVRELLARFTTDVIGTCAFGIECSSLKDPD 202
Cdd:cd20613  73 KWKKRRAILNPAFHRKYLKNLMDEF----NESADLLVEKLSKkadgKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDPD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 203 AEFREMGRRSLTeqrlgpvgiGFVNSFpnlaRRLHMKMTaePIERFFMRIVRETVAF-----REQNNIRRNDfMDQLIDL 277
Cdd:cd20613 149 SPFPKAISLVLE---------GIQESF----RNPLLKYN--PSKRKYRREVREAIKFlretgRECIEERLEA-LKRGEEV 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 278 KNKPL--MVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIeKCNGELNYESMK 355
Cdd:cd20613 213 PNDILthILKASEEEPDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVL-GSKQYVEYEDLG 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 356 DLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERD 435
Cdd:cd20613 292 KLEYLSQVLKETLRLYPPVPGTSRELTKDIELGG---YKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIP 368
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 24653745 436 SVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCE 476
Cdd:cd20613 369 SYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFELVP 409
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
77-475 2.80e-50

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: 177.40  E-value: 2.80e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  77 WF-RRPAVFVLETSLAKQILIKEFNKFTDRgfFHNPEDDPLSGQ--LFLLDGQKWRTMRNKLSSTFT-SGKMKYMFPTVV 152
Cdd:cd20617   7 WLgDVPTVVLSDPEIIKEAFVKNGDNFSDR--PLLPSFEIISGGkgILFSNGDYWKELRRFALSSLTkTKLKKKMEELIE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 153 KVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPdaEFREMgRRSLTEQ--RLGPVGIGFVNSFP 230
Cdd:cd20617  85 EEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDDG--EFLKL-VKPIEEIfkELGSGNPSDFIPIL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 231 NLARRLHMKMTAEPIER---FFMRIVRETVAFREQNNIRRNDFMDQLIDLKNkplmvsqsGESVNLTIEEIAAQAFVFFA 307
Cdd:cd20617 162 LPFYFLYLKKLKKSYDKikdFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKE--------GDSGLFDDDSIISTCLDLFL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 308 AGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYE 386
Cdd:cd20617 234 AGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGN-DRRVTLSDRSKLPYLNAVIKEVLRLRPILPLgLPRVTTEDTE 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 387 VPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSpERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALL 466
Cdd:cd20617 313 IGG---YFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFL-ENDGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANL 388

                ....*....
gi 24653745 467 IKDFKFSVC 475
Cdd:cd20617 389 LLNFKFKSS 397
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
62-470 1.43e-49

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: 175.08  E-value: 1.43e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  62 YYNKFRGSGPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQ-LFLLDGQKWRTMRNKLSSTFT 140
Cdd:COG2124  24 FYARLREYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDsLLTLDGPEHTRLRRLVQPAFT 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 141 SGKMKYMFPTVVKVANEFTDvfgqNVAKSPVVEVRELLARFTTDVIGTCAFGIecsslkdPDAEFREMgrrslteQRLGP 220
Cdd:COG2124 104 PRRVAALRPRIREIADELLD----RLAARGPVDLVEEFARPLPVIVICELLGV-------PEEDRDRL-------RRWSD 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 221 VGIGFVNSFPNLARRLHMKMTAEpIERFFMRIVREtvafREQNniRRNDFMDQLIDlknkplmVSQSGESvnLTIEEIAA 300
Cdd:COG2124 166 ALLDALGPLPPERRRRARRARAE-LDAYLRELIAE----RRAE--PGDDLLSALLA-------ARDDGER--LSDEELRD 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 301 QAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKEcqeviekcngelnyesmkdLVYLDQVVSETLRLYTVLPVLNRE 380
Cdd:COG2124 230 ELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE-------------------PELLPAAVEETLRLYPPVPLLPRT 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 381 CLEDYEVPGHPkyvIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDSVEWLPFGDGPRNCIGMRFGQMQAR 460
Cdd:COG2124 291 ATEDVELGGVT---IPAGDRVLLSLAAANRDPRVFPDPDRFDPD---------RPPNAHLPFGGGPHRCLGAALARLEAR 358
                       410
                ....*....|
gi 24653745 461 IGLALLIKDF 470
Cdd:COG2124 359 IALATLLRRF 368
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
128-473 2.65e-48

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: 172.37  E-value: 2.65e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 128 WRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVvEVRELLARFTTDVIGTCAFGIECSSLKDPDAE-FR 206
Cdd:cd11068  72 WGKAHRILMPAFGPLAMRGYFPMMLDIAEQLVLKWERLGPDEPI-DVPDDMTRLTLDTIALCGFGYRFNSFYRDEPHpFV 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 207 EMGRRSLTEQRLGPVGIGFVNSFPNLARRLHMKMTAepierfFMR-IVRETVAFREQNNIRR-NDFMDQLIDLKNKplmv 284
Cdd:cd11068 151 EAMVRALTEAGRRANRPPILNKLRRRAKRQFREDIA------LMRdLVDEIIAERRANPDGSpDDLLNLMLNGKDP---- 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 285 sQSGESvnLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEkcNGELNYESMKDLVYLDQVV 364
Cdd:cd11068 221 -ETGEK--LSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLG--DDPPPYEQVAKLRYIRRVL 295
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 365 SETLRLYTVLPVLNRECLEDYEVPGhpKYVIKKGMPVLIPCGAMHRDEKLY-ANPNTFNPDNFSPERVKERDSVEWLPFG 443
Cdd:cd11068 296 DETLRLWPTAPAFARKPKEDTVLGG--KYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFRKLPPNAWKPFG 373
                       330       340       350
                ....*....|....*....|....*....|
gi 24653745 444 DGPRNCIGMRFGQMQARIGLALLIKDFKFS 473
Cdd:cd11068 374 NGQRACIGRQFALQEATLVLAMLLQRFDFE 403
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
71-500 6.67e-46

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: 165.42  E-value: 6.67e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  71 PFAGFYWF--RRPAVFVLETSLAKQILIKEFNKFTDRGFFHnpedDPLSGQ-LFLLDGQKWRTMRNKLSSTFTSGKMKYM 147
Cdd:cd20659   1 PRAYVFWLgpFRPILVLNHPDTIKAVLKTSEPKDRDSYRFL----KPWLGDgLLLSNGKKWKRNRRLLTPAFHFDILKPY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 148 FPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIE--CSSLKDPD---AEFREMGRrsLTEQR-LGP- 220
Cdd:cd20659  77 VPVYNECTDILLEKWSKLAETGESVEVFEDISLLTLDIILRCAFSYKsnCQQTGKNHpyvAAVHELSR--LVMERfLNPl 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 221 VGIGFVNSFPNLARR-------LHmKMTAEPI-ERffmRIVRETVAFREQNNIRRNDFMDQLIDLKNkplmvsQSGesVN 292
Cdd:cd20659 155 LHFDWIYYLTPEGRRfkkacdyVH-KFAEEIIkKR---RKELEDNKDEALSKRKYLDFLDILLTARD------EDG--KG 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 293 LTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNgELNYESMKDLVYLDQVVSETLRLYT 372
Cdd:cd20659 223 LTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRD-DIEWDDLSKLPYLTMCIKESLRLYP 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 373 VLPVLNRECLEDYEVPGHpkyVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGM 452
Cdd:cd20659 302 PVPFIARTLTKPITIDGV---TLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSAGPRNCIGQ 378
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 24653745 453 RFGQMQARIGLALLIKDFKFSVCEKTTIPMtynKEMFLIASNSGIYLK 500
Cdd:cd20659 379 NFAMNEMKVVLARILRRFELSVDPNHPVEP---KPGLVLRSKNGIKLK 423
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
70-473 7.15e-45

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: 162.36  E-value: 7.15e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEddPLSGQ-LFLLDGQKWRTMRNKLSSTFTSGKMKYMF 148
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVKGGVYERLK--LLLGNgLLTSEGDLWRRQRRLAQPAFHRRRIAAYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 149 PTVVKVANEFTDVFGQNvAKSPVVEVRELLARFTTDVIGTCAFGIecsslkDPDAEFREMGR-------RSLTEQRLGPV 221
Cdd:cd20620  79 DAMVEATAALLDRWEAG-ARRGPVDVHAEMMRLTLRIVAKTLFGT------DVEGEADEIGDaldvaleYAARRMLSPFL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 222 GIGFVNSFPNLARRLHMKMtaepIERFFMRIVREtvafREQNNIRRNDFMDQLIDLKNkplmvSQSGESvnLTIEEIAAQ 301
Cdd:cd20620 152 LPLWLPTPANRRFRRARRR----LDEVIYRLIAE----RRAAPADGGDLLSMLLAARD-----EETGEP--MSDQQLRDE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 302 AFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIekCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNREC 381
Cdd:cd20620 217 VMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVL--GGRPPTAEDLPQLPYTEMVLQESLRLYPPAWIIGREA 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 382 LEDYEVPGHPkyvIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARI 461
Cdd:cd20620 295 VEDDEIGGYR---IPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVL 371
                       410
                ....*....|..
gi 24653745 462 GLALLIKDFKFS 473
Cdd:cd20620 372 LLATIAQRFRLR 383
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
80-472 7.53e-42

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: 154.72  E-value: 7.53e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  80 RPAVFVLETSLAKQILIKEFNKFTDRGFFHNpedDPLSGQ-LFLLDGQKWRTMRNKLSSTFTSGKMKYMfptvVKVANEF 158
Cdd:cd20621  13 KPLISLVDPEYIKEFLQNHHYYKKKFGPLGI---DRLFGKgLLFSEGEEWKKQRKLLSNSFHFEKLKSR----LPMINEI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 159 TDVFGQNVAKSPVVEVrELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLTEQRLGpvgigFVNSFPNLARRLHM 238
Cdd:cd20621  86 TKEKIKKLDNQNVNII-QFLQKITGEVVIRSFFGEEAKDLKINGKEIQVELVEILIESFLY-----RFSSPYFQLKRLIF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 239 KMTA-----EPIERFFMRIVREtvaFRE---------QNNIRRNDFMDQLIDLKNKPLMVSQSGESVNLTIEEIAAQAFV 304
Cdd:cd20621 160 GRKSwklfpTKKEKKLQKRVKE---LRQfiekiiqnrIKQIKKNKDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFIT 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 305 FFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIeKCNGELNYESMKDLVYLDQVVSETLRLYTVLP-VLNRECLE 383
Cdd:cd20621 237 FFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVV-GNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPfLFPRVATQ 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 384 DYEVPghpKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGL 463
Cdd:cd20621 316 DHQIG---DLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIIL 392

                ....*....
gi 24653745 464 ALLIKDFKF 472
Cdd:cd20621 393 IYILKNFEI 401
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
123-472 9.17e-41

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: 151.60  E-value: 9.17e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 123 LDGQKWrtMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQnvakSPVVEVRELLARFTTDVIGTCAFGiecsslkdpd 202
Cdd:cd11042  61 FAEQKE--QLKFGLNILRRGKLRGYVPLIVEEVEKYFAKWGE----SGEVDLFEEMSELTILTASRCLLG---------- 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 203 AEFREMGRRSLT------EQRLGPvgIGFVnsFPNL----ARRL---HMKMTaepieRFFMRIVREtvafREQNNIRR-N 268
Cdd:cd11042 125 KEVRELLDDEFAqlyhdlDGGFTP--IAFF--FPPLplpsFRRRdraRAKLK-----EIFSEIIQK----RRKSPDKDeD 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 269 DFMDQLIDLKNKplmvsqsgESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGE 348
Cdd:cd11042 192 DMLQTLMDAKYK--------DGRPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDP 263
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 349 LNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGHPkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSP 428
Cdd:cd11042 264 LTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVEGGG-YVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLK 342
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 24653745 429 ER--VKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKF 472
Cdd:cd11042 343 GRaeDSKGGKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDF 388
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
63-483 9.62e-41

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: 152.13  E-value: 9.62e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  63 YNKFRGSGPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFtsg 142
Cdd:cd11046   4 YKWFLEYGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDKKGLLAEILEPIMGKGLIPADGEIWKKRRRALVPAL--- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 143 KMKY--MFPTVVKVANEFT-DVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEF-------REMGRRS 212
Cdd:cd11046  81 HKDYleMMVRVFGRCSERLmEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVTEESPVIkavylplVEAEHRS 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 213 LTE-QRLGPVGIGFVnsfpnLARRLHMKMTAEPIERFFMRIVRETVAFREQNNIRR-NDFMDQLIDLKNKPLMVSQSGEs 290
Cdd:cd11046 161 VWEpPYWDIPAALFI-----VPRQRKFLRDLKLLNDTLDDLIRKRKEMRQEEDIELqQEDYLNEDDPSLLRFLVDMRDE- 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 291 vNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRL 370
Cdd:cd11046 235 -DVDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGD-RLPPTYEDLKKLKYTRRVLNESLRL 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 371 YTVLPVLNRECLEDYEVPGHpKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNF----SPERVKERDSVEWLPFGDGP 446
Cdd:cd11046 313 YPQPPVLIRRAVEDDKLPGG-GVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFldpfINPPNEVIDDFAFLPFGGGP 391
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 24653745 447 RNCIGMRFGQMQARIGLALLIKDFKFS-VCEKTTIPMT 483
Cdd:cd11046 392 RKCLGDQFALLEATVALAMLLRRFDFElDVGPRHVGMT 429
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
54-474 1.38e-40

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: 151.45  E-value: 1.38e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  54 SFNEIWTSYYNKfrgsgPFagFYWF-RRPAVFVLETSLAKQILIKEFnkftdrGFFHNPEDDPLSGQLF-----LLDGQK 127
Cdd:cd20639   2 PFYHHWRKIYGK-----TF--LYWFgPTPRLTVADPELIREILLTRA------DHFDRYEAHPLVRQLEgdglvSLRGEK 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 128 WRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQ--NVAKSPVVEVRELLARFTTDVIGTCAFGiecSSLKDPDAEF 205
Cdd:cd20639  69 WAHHRRVITPAFHMENLKRLVPHVVKSVADMLDKWEAmaEAGGEGEVDVAEWFQNLTEDVISRTAFG---SSYEDGKAVF 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 206 R----EMGRRSLTEQRLGPVGIGFvnsFPNLARRLHMKMTAEpIERFFMRIV--RETVAFREQNNIRRNDFMDQLIDLKN 279
Cdd:cd20639 146 RlqaqQMLLAAEAFRKVYIPGYRF---LPTKKNRKSWRLDKE-IRKSLLKLIerRQTAADDEKDDEDSKDLLGLMISAKN 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 280 KplmvsqsGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKecqEVIEKC--NGELNYESMKDL 357
Cdd:cd20639 222 A-------RNGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARR---EVLAVCgkGDVPTKDHLPKL 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 358 VYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYAN-PNTFNPDNFS-PERVKERD 435
Cdd:cd20639 292 KTLGMILNETLRLYPPAVATIRRAKKDVKLGG---LDIPAGTELLIPIMAIHHDAELWGNdAAEFNPARFAdGVARAAKH 368
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 24653745 436 SVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSV 474
Cdd:cd20639 369 PLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRL 407
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
124-474 1.18e-39

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: 149.02  E-value: 1.18e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 124 DGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVF--GQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDP 201
Cdd:cd11070  54 EGEDWKRYRKIVAPAFNERNNALVWEESIRQAQRLIRYLleEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEE 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 202 DAEFREMGrrSLTEQRLGPvgiGFVNSFPNLARRLHM-----KMTAEPIERFfMRIVRETVafreQNNIRRNDFMDQLID 276
Cdd:cd11070 134 ESSLHDTL--NAIKLAIFP---PLFLNFPFLDRLPWVlfpsrKRAFKDVDEF-LSELLDEV----EAELSADSKGKQGTE 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 277 LKNKPLMVSQSGESVnLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELNYESM-K 355
Cdd:cd11070 204 SVVASRLKRARRSGG-LTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEEDfP 282
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 356 DLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGH--PKYVIKKGMPVLIPCGAMHRDEKLY-ANPNTFNPDNF------ 426
Cdd:cd11070 283 KLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVITGlgQEIVIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWgstsge 362
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 24653745 427 -SPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSV 474
Cdd:cd11070 363 iGAATRFTPARGAFIPFSAGPRACLGRKFALVEFVAALAELFRQYEWRV 411
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
120-477 2.19e-39

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: 148.06  E-value: 2.19e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 120 LFLLDGQKWRTMRNKLSSTFTSGK-MKYMFPTVVKVANEFTDVFGQ--NVAKSPVVEVRELLARFTTDVIGTCAFGIECS 196
Cdd:cd11054  58 LLNSNGEEWHRLRSAVQKPLLRPKsVASYLPAINEVADDFVERIRRlrDEDGEEVPDLEDELYKWSLESIGTVLFGKRLG 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 197 SL-KDPDAEFREMgrrslteqrlgpvgIGFVNSFPNLARRLhmkMTAEPIERFFmrivrETVAFRE----QNNIRR--ND 269
Cdd:cd11054 138 CLdDNPDSDAQKL--------------IEAVKDIFESSAKL---MFGPPLWKYF-----PTPAWKKfvkaWDTIFDiaSK 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 270 FMDQLIDLKNKPLMVSQSGESV--------NLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEV 341
Cdd:cd11054 196 YVDEALEELKKKDEEDEEEDSLleyllskpGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSV 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 342 IEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTF 421
Cdd:cd11054 276 LPD-GEPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKDIVLSG---YHIPKGTLVVLSNYVMGRDEEYFPDPEEF 351
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653745 422 NpdnfsPER-VKERDSVE------WLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEK 477
Cdd:cd11054 352 I-----PERwLRDDSENKnihpfaSLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHE 409
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
70-470 3.72e-39

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: 147.08  E-value: 3.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQIL---IKEFNKFTD--RGFfhnpEDDPLSGqLFLLDGQKWRTMRNKLSSTFTSGKM 144
Cdd:cd11083   1 GSAYRFRLGRQPVLVISDPELIREVLrrrPDEFRRISSleSVF----REMGING-VFSAEGDAWRRQRRLVMPAFSPKHL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 145 KYMFPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLkdpdaefrEMGRRSLTEqRLGPVgig 224
Cdd:cd11083  76 RYFFPTLRQITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYDLNTL--------ERGGDPLQE-HLERV--- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 225 fvnsFPNLARRLHM-----KMTAEPIERFFMRIVRETVAFREQNNIRRNDFMDQLIDLKNKP-----LMVSQSGESVNLT 294
Cdd:cd11083 144 ----FPMLNRRVNApfpywRYLRLPADRALDRALVEVRALVLDIIAAARARLAANPALAEAPetllaMMLAEDDPDARLT 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 295 IEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTVL 374
Cdd:cd11083 220 DDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPLLEALDRLPYLEAVARETLRLKPVA 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 375 PVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNF---SPERVKERDSVeWLPFGDGPRNCIG 451
Cdd:cd11083 300 PLLFLEPNEDTVVGD---IALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWldgARAAEPHDPSS-LLPFGAGPRLCPG 375
                       410
                ....*....|....*....
gi 24653745 452 MRFGQMQARIGLALLIKDF 470
Cdd:cd11083 376 RSLALMEMKLVFAMLCRNF 394
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
125-477 3.73e-39

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: 147.41  E-value: 3.73e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 125 GQKWRTMRNKLSSTFtsgkmkyMFptvvKVANEFTDVFG----------QNVAKSPVVEVRELLARFTTDVIGTCAFGIE 194
Cdd:cd20660  54 GEKWHSRRKMLTPTF-------HF----KILEDFLDVFNeqseilvkklKKEVGKEEFDIFPYITLCALDIICETAMGKS 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 195 CSSLKDPDAEF-REMGRRS-LTEQR-------------LGPVG------IGFVNSFPNlarrlhmKMTAEPIErfFMRIV 253
Cdd:cd20660 123 VNAQQNSDSEYvKAVYRMSeLVQKRqknpwlwpdfiysLTPDGrehkkcLKILHGFTN-------KVIQERKA--ELQKS 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 254 RETVAFREQNNI----RRNDFMDQLIDlknkplmVSQSGESvnLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQD 329
Cdd:cd20660 194 LEEEEEDDEDADigkrKRLAFLDLLLE-------ASEEGTK--LSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPE 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 330 IQNRVRKECQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMH 409
Cdd:cd20660 265 VQEKVHEELDRIFGDSDRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGG---YTIPKGTTVLVLTYALH 341
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24653745 410 RDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEK 477
Cdd:cd20660 342 RDPRQFPDPEKFDPDRFLPENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESVQK 409
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
80-472 1.07e-35

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: 137.33  E-value: 1.07e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  80 RPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEddPLSGQ--LFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANE 157
Cdd:cd11053  23 GPVVVLSDPEAIKQIFTADPDVLHPGEGNSLLE--PLLGPnsLLLLDGDRHRRRRKLLMPAFHGERLRAYGELIAEITER 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 158 FTD--VFGQnvakspVVEVRELLARFTTDVIGTCAFGIEcsslkDPD--AEFREMGRRSLTeqRLGPVGIGFVNSFPNLA 233
Cdd:cd11053 101 EIDrwPPGQ------PFDLRELMQEITLEVILRVVFGVD-----DGErlQELRRLLPRLLD--LLSSPLASFPALQRDLG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 234 RRL---HMKMTAEPIERFFMRIVRETvafREQNNIRRNDFMDQLIDlknkplmvSQSGESVNLTIEEIAAQAFVFFAAGF 310
Cdd:cd11053 168 PWSpwgRFLRARRRIDALIYAEIAER---RAEPDAERDDILSLLLS--------ARDEDGQPLSDEELRDELMTLLFAGH 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKEcqevIEKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGh 390
Cdd:cd11053 237 ETTATALAWAFYWLHRHPEVLARLLAE----LDALGGDPDPEDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGG- 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 391 pkYVIKKGMpVLIPC-GAMHRDEKLYANPNTFNPDNFSPERVkerDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKD 469
Cdd:cd11053 312 --YTLPAGT-TVAPSiYLTHHRPDLYPDPERFRPERFLGRKP---SPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRR 385

                ...
gi 24653745 470 FKF 472
Cdd:cd11053 386 FRL 388
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
75-472 1.02e-34

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: 135.10  E-value: 1.02e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  75 FYWF-RRPAVFVLETSLAKQIlikeFNKFTDrgfFHNPEDDPLsGQLFL-----LDGQKWRTMRNKLSSTFTSGKMKYMF 148
Cdd:cd20642  16 FTWFgPIPRVIIMDPELIKEV----LNKVYD---FQKPKTNPL-TKLLAtglasYEGDKWAKHRKIINPAFHLEKLKNML 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 149 PTVVKVANEFTDVFGQNVAK--SPVVEVRELLARFTTDVIGTCAFGiecSSLKDPDAEF---REMGRRSLTE-QRLGPVG 222
Cdd:cd20642  88 PAFYLSCSEMISKWEKLVSSkgSCELDVWPELQNLTSDVISRTAFG---SSYEEGKKIFelqKEQGELIIQAlRKVYIPG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 223 IGFVNSFPNlaRRlhMKMTAEPIERFFMRIVRETVAFREQNNIRRNDFMDQLIDLKNKPLMvSQSGESVNLTIEEIAAQA 302
Cdd:cd20642 165 WRFLPTKRN--RR--MKEIEKEIRSSLRGIINKREKAMKAGEATNDDLLGILLESNHKEIK-EQGNKNGGMSTEDVIEEC 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 303 FVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEkcNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNREC- 381
Cdd:cd20642 240 KLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFG--NNKPDFEGLNHLKVVTMILYEVLRLYPPVIQLTRAIh 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 382 ----LEDYEVPGhpkyvikkGMPVLIPCGAMHRDEKLYANpntfNPDNFSPERVKE------RDSVEWLPFGDGPRNCIG 451
Cdd:cd20642 318 kdtkLGDLTLPA--------GVQVSLPILLVHRDPELWGD----DAKEFNPERFAEgiskatKGQVSYFPFGWGPRICIG 385
                       410       420
                ....*....|....*....|.
gi 24653745 452 MRFGQMQARIGLALLIKDFKF 472
Cdd:cd20642 386 QNFALLEAKMALALILQRFSF 406
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
80-473 1.64e-34

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: 134.22  E-value: 1.64e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  80 RPAVFVLETSLAKQILIKEFNKFTDRgffhnPEddPLSGQLFLLDGQ---------KWRTMRnKLSST-FTSGKMKYMFP 149
Cdd:cd20618  11 VPTVVVSSPEMAKEVLKTQDAVFASR-----PR--TAAGKIFSYNGQdivfapygpHWRHLR-KICTLeLFSAKRLESFQ 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 150 TVVK--VANEFTDVFgQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPDA----EFREMGRRSLteqRLGpvgi 223
Cdd:cd20618  83 GVRKeeLSHLVKSLL-EESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKESeearEFKELIDEAF---ELA---- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 224 GFVNS---FPNLaRRL-------HMKMTAEPIERFFMRIVREtvafREQNNIRRNDFMDQLIDLknkpLMVSQSGESVNL 293
Cdd:cd20618 155 GAFNIgdyIPWL-RWLdlqgyekRMKKLHAKLDRFLQKIIEE----HREKRGESKKGGDDDDDL----LLLLDLDGEGKL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 294 TIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTV 373
Cdd:cd20618 226 SDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGR-ERLVEESDLPKLPYLQAVVKETLRLHPP 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 374 LPVL-NRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNF---SPERVKERDsVEWLPFGDGPRNC 449
Cdd:cd20618 305 GPLLlPHESTEDCKVAG---YDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFlesDIDDVKGQD-FELLPFGSGRRMC 380
                       410       420
                ....*....|....*....|....
gi 24653745 450 IGMRFGQMQARIGLALLIKDFKFS 473
Cdd:cd20618 381 PGMPLGLRMVQLTLANLLHGFDWS 404
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
59-477 1.91e-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: 134.11  E-value: 1.91e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  59 WTSYYNKfrgsgPFagFYWF-RRPAVFVLETSLAKQILikeFNKFtdrGFFHNPEDDP----LSGQ-LFLLDGQKWRTMR 132
Cdd:cd20641   7 WKSQYGE-----TF--LYWQgTTPRICISDHELAKQVL---SDKF---GFFGKSKARPeilkLSGKgLVFVNGDDWVRHR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 133 NKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPV----VEVRELLARFTTDVIGTCAFGiecSSLKD------PD 202
Cdd:cd20641  74 RVLNPAFSMDKLKSMTQVMADCTERMFQEWRKQRNNSETerieVEVSREFQDLTADIIATTAFG---SSYAEgievflSQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 203 AEFREMGRRSLTEQRLgPvGIGFVNSFPNLAR-RLHMKMTAEpierfFMRIVRETVAfreqnnIRRNDFMDQLIDLKNKP 281
Cdd:cd20641 151 LELQKCAAASLTNLYI-P-GTQYLPTPRNLRVwKLEKKVRNS-----IKRIIDSRLT------SEGKGYGDDLLGLMLEA 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 282 LMVSQSGESVN--LTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRkecQEVIEKCNGEL--NYESMKDL 357
Cdd:cd20641 218 ASSNEGGRRTErkMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLR---EEVFRECGKDKipDADTLSKL 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 358 VYLDQVVSETLRLYTVLPVLNRECLEDYEVpGHPKyvIKKGMPVLIPCGAMHRDEKLY-ANPNTFNPDNFSPERVKE-RD 435
Cdd:cd20641 295 KLMNMVLMETLRLYGPVINIARRASEDMKL-GGLE--IPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAaTH 371
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 24653745 436 SVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEK 477
Cdd:cd20641 372 PNALLSFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLSPE 413
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
78-491 2.52e-34

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: 133.46  E-value: 2.52e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  78 FRRPAVFVLETSLAKQILIKEFNKF------TDRGFFHNPeddplsgQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFptv 151
Cdd:cd11043  14 FGRPTVVSADPEANRFILQNEGKLFvswypkSVRKLLGKS-------SLLTVSGEEHKRLRGLLLSFLGPEALKDRL--- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 152 VKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIEcsslkdpDAEFREMGRRSLTEQRLGpvgigfVNSFP- 230
Cdd:cd11043  84 LGDIDELVRQHLDSWWRGKSVVVLELAKKMTFELICKLLLGID-------PEEVVEELRKEFQAFLEG------LLSFPl 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 231 NL-ARRLHMKMTAEpieRFFMRIVRETVAFREQN---NIRRNDFMDQLIDLKNKplmvsqsgESVNLTIEEIAAQAFVFF 306
Cdd:cd11043 151 NLpGTTFHRALKAR---KRIRKELKKIIEERRAElekASPKGDLLDVLLEEKDE--------DGDSLTDEEILDNILTLL 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 307 AAGFETSSTTMGFALYELAQNQDIQNRVRKEcQEVIEKCNGE---LNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLE 383
Cdd:cd11043 220 FAGHETTSTTLTLAVKFLAENPKVLQELLEE-HEEIAKRKEEgegLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQ 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 384 DYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFspERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGL 463
Cdd:cd11043 299 DVEYKG---YTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRW--EGKGKGVPYTFLPFGGGPRLCPGAELAKLEILVFL 373
                       410       420       430
                ....*....|....*....|....*....|.
gi 24653745 464 ALLIKDFKFSVCEKTTI---PMTYNKEMFLI 491
Cdd:cd11043 374 HHLVTRFRWEVVPDEKIsrfPLPRPPKGLPI 404
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
70-473 1.10e-33

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: 131.95  E-value: 1.10e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRgffhnPEddPLSGQLFLLDGQ---------KWRTMRnKLSST-- 138
Cdd:cd11027   2 GDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGR-----PK--LFTFDLFSRGGKdiafgdyspTWKLHR-KLAHSal 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 139 --FTSGKMKyMFPTVVKVANEFTDVFgqNVAKSPVVEVRELLARFTTDVIGTCAFGiECSSLKDPdaEFREM------GR 210
Cdd:cd11027  74 rlYASGGPR-LEEKIAEEAEKLLKRL--ASQEGQPFDPKDELFLAVLNVICSITFG-KRYKLDDP--EFLRLldlndkFF 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 211 RSLTeqrlgpvGIGFVNSFPNL------ARRLhMKMTAEPIERFFMRIVRETVA-FREqNNIRrnDFMDQLIDLKNKPLM 283
Cdd:cd11027 148 ELLG-------AGSLLDIFPFLkyfpnkALRE-LKELMKERDEILRKKLEEHKEtFDP-GNIR--DLTDALIKAKKEAED 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 284 VSQSGESVnLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcnGELNYESMKD---LVYL 360
Cdd:cd11027 217 EGDEDSGL-LTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVI----GRDRLPTLSDrkrLPYL 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 361 DQVVSETLRLYTVLPV-LNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVE- 438
Cdd:cd11027 292 EATIAEVLRLSSVVPLaLPHKTTCDTTLRG---YTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVPKPEs 368
                       410       420       430
                ....*....|....*....|....*....|....*
gi 24653745 439 WLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFS 473
Cdd:cd11027 369 FLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFS 403
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
97-492 3.30e-33

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: 130.50  E-value: 3.30e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  97 KEFNKFTDRGFFHNPEDDPLsgqLFLLDGQKWRTMRNKLSSTF--TSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVVEV 174
Cdd:cd11059  27 FGKTKSYWYFTLRGGGGPNL---FSTLDPKEHSARRRLLSGVYskSSLLRAAMEPIIRERVLPLIDRIAKEAGKSGSVDV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 175 RELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLTEQRLGP--VGIGFVNSFPNLARRLHMKMTAEP-IERFFMR 251
Cdd:cd11059 104 YPLFTALAMDVVSHLLFGESFGTLLLGDKDSRERELLRRLLASLAPwlRWLPRYLPLATSRLIIGIYFRAFDeIEEWALD 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 252 IVRETVAFREQNNIRRNDFMDQLIDLKNKPlmvsqsgeSVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQ 331
Cdd:cd11059 184 LCARAESSLAESSDSESLTVLLLEKLKGLK--------KQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQ 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 332 NRVRKECQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVlnrecledyevpGHPKYVIKKGMPV---LIPCG-- 406
Cdd:cd11059 256 EKLREELAGLPGPFRGPPDLEDLDKLPYLNAVIRETLRLYPPIPG------------SLPRVVPEGGATIggyYIPGGti 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 407 ------AMHRDEKLYANPNTFNPDNF---SPERVKERDSVEWlPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSvcek 477
Cdd:cd11059 324 vstqaySLHRDPEVFPDPEEFDPERWldpSGETAREMKRAFW-PFGSGSRMCIGMNLALMEMKLALAAIYRNYRTS---- 398
                       410
                ....*....|....*
gi 24653745 478 TTIPMTYNKEMFLIA 492
Cdd:cd11059 399 TTTDDDMEQEDAFLA 413
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
79-475 2.84e-32

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: 127.76  E-value: 2.84e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  79 RRPAVFVLETSLAKQILIKEfNKFTDRGFFHNPEDdPLSGQ-LFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANE 157
Cdd:cd11049  22 PRPAYVVTSPELVRQVLVND-RVFDKGGPLFDRAR-PLLGNgLATCPGEDHRRQRRLMQPAFHRSRIPAYAEVMREEAEA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 158 FTDVF--GQnvakspVVEVRELLARFTTDVIGTCAFGiecSSLKDPDAE---------FREMGRRSLTEQRLGPVGIGFV 226
Cdd:cd11049 100 LAGSWrpGR------VVDVDAEMHRLTLRVVARTLFS---TDLGPEAAAelrqalpvvLAGMLRRAVPPKFLERLPTPGN 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 227 NSFPNLARRLHmkmtaepierffmRIVRETVAFREQNNIRRNDFMDQLIDlknkplmvSQSGESVNLTIEEIAAQAFVFF 306
Cdd:cd11049 171 RRFDRALARLR-------------ELVDEIIAEYRASGTDRDDLLSLLLA--------ARDEEGRPLSDEELRDQVITLL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 307 AAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEkcNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYE 386
Cdd:cd11049 230 TAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG--GRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVE 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 387 VPGHPkyvIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALL 466
Cdd:cd11049 308 LGGHR---LPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATI 384

                ....*....
gi 24653745 467 IKDFKFSVC 475
Cdd:cd11049 385 ASRWRLRPV 393
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
130-472 5.65e-32

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: 126.95  E-value: 5.65e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 130 TMRNK---------LSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVAK--SPVVEVRELLARFTTDVIGTCAFGIECSSL 198
Cdd:cd11061  47 TTRDKaeharrrrvWSHAFSDKALRGYEPRILSHVEQLCEQLDDRAGKpvSWPVDMSDWFNYLSFDVMGDLAFGKSFGML 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 199 KDPDAEFREMGRRSlTEQRLGPVG--------IGFVNSFPNLARRLhmkmtaepieRFFMRIVRETVAFREQNNI-RRND 269
Cdd:cd11061 127 ESGKDRYILDLLEK-SMVRLGVLGhapwlrplLLDLPLFPGATKAR----------KRFLDFVRAQLKERLKAEEeKRPD 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 270 FMDQLIDLKNKplmvsqsGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGEL 349
Cdd:cd11061 196 IFSYLLEAKDP-------ETGEGLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIR 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 350 NYESMKDLVYLDQVVSETLRLY-TVLPVLNRECL-EDYEVPGHpkyVIKKGMPVLIPCGAMHRDEKLYANPNTFNpdnfs 427
Cdd:cd11061 269 LGPKLKSLPYLRACIDEALRLSpPVPSGLPRETPpGGLTIDGE---YIPGGTTVSVPIYSIHRDERYFPDPFEFI----- 340
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24653745 428 PER--------VKERDSveWLPFGDGPRNCIGMRFGQMQARIGLALLIK--DFKF 472
Cdd:cd11061 341 PERwlsrpeelVRARSA--FIPFSIGPRGCIGKNLAYMELRLVLARLLHryDFRL 393
PLN02290 PLN02290
cytokinin trans-hydroxylase
76-476 5.83e-32

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 128.39  E-value: 5.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   76 YWF-RRPAVFVLETSLAKQILIKeFNKFTDRGFFHNPEDDPLSGQ-LFLLDGQKWRTMRNKLSSTFTSGKMK----YMFP 149
Cdd:PLN02290  99 YWNgTEPRLCLTETELIKELLTK-YNTVTGKSWLQQQGTKHFIGRgLLMANGADWYHQRHIAAPAFMGDRLKgyagHMVE 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  150 TVVKVANEFtdvfgQNVAKSPV--VEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLTEQR-LGPVGIGFv 226
Cdd:PLN02290 178 CTKQMLQSL-----QKAVESGQteVEIGEYMTRLTADIISRTEFDSSYEKGKQIFHLLTVLQRLCAQATRhLCFPGSRF- 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  227 nsFPNLARRlHMKMTAEPIERFFMRIVRETvafREQNNIRRNDF--MDQLIDLKNKplMVSQSGESVNLTIEEIAAQAFV 304
Cdd:PLN02290 252 --FPSKYNR-EIKSLKGEVERLLMEIIQSR---RDCVEIGRSSSygDDLLGMLLNE--MEKKRSNGFNLNLQLIMDECKT 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  305 FFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEViekCNGEL-NYESMKDLVYLDQVVSETLRLYTVLPVLNRECLE 383
Cdd:PLN02290 324 FFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEV---CGGETpSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFE 400
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  384 DYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLY-ANPNTFNPDNFSPERVKErdSVEWLPFGDGPRNCIGMRFGQMQARIG 462
Cdd:PLN02290 401 DIKLGD---LHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAP--GRHFIPFAAGPRNCIGQAFAMMEAKII 475
                        410
                 ....*....|....
gi 24653745  463 LALLIKDFKFSVCE 476
Cdd:PLN02290 476 LAMLISKFSFTISD 489
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
312-474 7.51e-32

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: 126.66  E-value: 7.51e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 312 TSSTTMGFALYELAQNQDIQNRVRKECQEViekCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhp 391
Cdd:cd11045 226 TTTSTLTSMAYFLARHPEWQERLREESLAL---GKGTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEVLG-- 300
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 392 kYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDS-VEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:cd11045 301 -YRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHrYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRF 379

                ....
gi 24653745 471 KFSV 474
Cdd:cd11045 380 RWWS 383
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
94-474 4.02e-31

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: 125.01  E-value: 4.02e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  94 ILIKEFNKFtDRG-FFHNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMK-YMFPTVVKVANEFTDVFGQNVAKSP- 170
Cdd:cd11064  25 ILKTNFDNY-PKGpEFRDLFFDLLGDGIFNVDGELWKFQRKTASHEFSSRALReFMESVVREKVEKLLVPLLDHAAESGk 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 171 VVEVRELLARFTTDVIGTCAFGIE--CSSLKDPDAEFRE-MGRRS-LTEQRLGpvgigFVNSFPNLARRLHM---KMTAE 243
Cdd:cd11064 104 VVDLQDVLQRFTFDVICKIAFGVDpgSLSPSLPEVPFAKaFDDASeAVAKRFI-----VPPWLWKLKRWLNIgseKKLRE 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 244 P---IERFFMRIV---RETVAFREQNNIRRND----FMDqlIDLKNKPLMVSQSGESVNLTIeeiaaqafvfFAAGFETS 313
Cdd:cd11064 179 AirvIDDFVYEVIsrrREELNSREEENNVREDllsrFLA--SEEEEGEPVSDKFLRDIVLNF----------ILAGRDTT 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 314 STTMGFALYELAQNQDIQNRVRKECQEVIEKCNGE----LNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVP- 388
Cdd:cd11064 247 AAALTWFFWLLSKNPRVEEKIREELKSKLPKLTTDesrvPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPd 326
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 389 GHPkyvIKKGMPVLIPCGAMHRdeklyaNPNTFNPD--NFSPER-------VKERDSVEWLPFGDGPRNCIGMRFGQMQA 459
Cdd:cd11064 327 GTF---VKKGTRIVYSIYAMGR------MESIWGEDalEFKPERwldedggLRPESPYKFPAFNAGPRICLGKDLAYLQM 397
                       410
                ....*....|....*
gi 24653745 460 RIGLALLIKDFKFSV 474
Cdd:cd11064 398 KIVAAAILRRFDFKV 412
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
92-459 1.32e-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: 123.05  E-value: 1.32e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  92 KQILIKEFNKFtDRGFFHNPEDDPLSGQ-LFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVaksp 170
Cdd:cd11063  24 KAVLATQFKDF-GLGERRRDAFKPLLGDgIFTSDGEEWKHSRALLRPQFSRDQISDLELFERHVQNLIKLLPRDGS---- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 171 VVEVRELLARFTTDVIGTCAFGIECSSLKD-----PDAEF--------REMGRRSlteqRLGPVGIgFVNS--FPNLARR 235
Cdd:cd11063  99 TVDLQDLFFRLTLDSATEFLFGESVDSLKPggdspPAARFaeafdyaqKYLAKRL----RLGKLLW-LLRDkkFREACKV 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 236 LHmkmtaepieRFFMRIVRETVAFREQ----NNIRRNDFMDQLIDLKNKPLMVSqsGESVNLTIeeiaaqafvffaAGFE 311
Cdd:cd11063 174 VH---------RFVDPYVDKALARKEEskdeESSDRYVFLDELAKETRDPKELR--DQLLNILL------------AGRD 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 312 TSSTTMGFALYELAQNQDIQNRVRkecQEVIEKCNGELN--YESMKDLVYLDQVVSETLRLYTVLPVLNRECLED--YEV 387
Cdd:cd11063 231 TTASLLSFLFYELARHPEVWAKLR---EEVLSLFGPEPTptYEDLKNMKYLRAVINETLRLYPPVPLNSRVAVRDttLPR 307
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24653745 388 PGHP----KYVIKKGMPVLIPCGAMHRDEKLYANpntfNPDNFSPERVKERDSVEW--LPFGDGPRNCIGMRFGQMQA 459
Cdd:cd11063 308 GGGPdgksPIFVPKGTRVLYSVYAMHRRKDIWGP----DAEEFRPERWEDLKRPGWeyLPFNGGPRICLGQQFALTEA 381
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
78-474 2.41e-30

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: 122.39  E-value: 2.41e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  78 FRRPAVFVLETSLAKQILIKEfNKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANE 157
Cdd:cd11044  30 LGRPTVFVIGAEAVRFILSGE-GKLVRYGWPRSVRRLLGENSLSLQDGEEHRRRRKLLAPAFSREALESYVPTIQAIVQS 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 158 FTdvfgQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAE-FREMGRRSLTEqrlgPVGIGFVNSFPNLARRl 236
Cdd:cd11044 109 YL----RKWLKAGEVALYPELRRLTFDVAARLLLGLDPEVEAEALSQdFETWTDGLFSL----PVPLPFTPFGRAIRAR- 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 237 hmkmtaEPIERFFMRIVRETvafREQNNIRRNDFMDQLIDLKNkplmvsQSGESvnLTIEEIAAQAFVFFAAGFETSSTT 316
Cdd:cd11044 180 ------NKLLARLEQAIRER---QEEENAEAKDALGLLLEAKD------EDGEP--LSMDELKDQALLLLFAGHETTASA 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 317 MGFALYELAQNQDIQNRVRKEcQEVIEkCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIK 396
Cdd:cd11044 243 LTSLCFELAQHPDVLEKLRQE-QDALG-LEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGG---YQIP 317
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24653745 397 KGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKE-RDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSV 474
Cdd:cd11044 318 KGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDkKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWEL 396
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
311-477 1.05e-29

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: 121.02  E-value: 1.05e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGh 390
Cdd:cd20680 257 DTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDRPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEIRG- 335
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 391 pkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:cd20680 336 --FKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHF 413

                ....*..
gi 24653745 471 KFSVCEK 477
Cdd:cd20680 414 WVEANQK 420
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
125-452 1.24e-28

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: 117.63  E-value: 1.24e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 125 GQKWRTMRnKLSST--FTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVVEVRELLarFTT--DVIGTCAFGIEcssLKD 200
Cdd:cd11073  62 GPRWRMLR-KICTTelFSPKRLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAA--FLTslNLISNTLFSVD---LVD 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 201 PDA----EFREMGRRSLTEqrlgpVGI-GFVNSFPNLAR------RLHMKMTAEPIERFFMRIVRETVAFREQNNIRRND 269
Cdd:cd11073 136 PDSesgsEFKELVREIMEL-----AGKpNVADFFPFLKFldlqglRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKD 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 270 FMDQLIDLKNKplmvsqsGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGEL 349
Cdd:cd11073 211 DDLLLLLDLEL-------DSESELTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGK-DKIV 282
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 350 NYESMKDLVYLDQVVSETLRLYTVLPVL-NRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNF-- 426
Cdd:cd11073 283 EESDISKLPYLQAVVKETLRLHPPAPLLlPRKAEEDVEVMG---YTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFlg 359
                       330       340
                ....*....|....*....|....*.
gi 24653745 427 SPERVKERDsVEWLPFGDGPRNCIGM 452
Cdd:cd11073 360 SEIDFKGRD-FELIPFGSGRRICPGL 384
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
80-472 4.26e-28

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: 116.19  E-value: 4.26e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  80 RPAVFVLETSLAKQILIKEFNKFTDRgffhnPEDDPLSgQLFLLD---------GQKWRTMR-NKLSSTFTSGKMKYMFP 149
Cdd:cd11075  13 RPLIVVASRELAHEALVQKGSSFASR-----PPANPLR-VLFSSNkhmvnsspyGPLWRTLRrNLVSEVLSPSRLKQFRP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 150 TVVKVANEFTDVFGQNVAKSP-VVEVRELLaRFTtdvigtcAFGI---ECSSLKDPDAEFREMgRRSLTEQRLGPVGIGF 225
Cdd:cd11075  87 ARRRALDNLVERLREEAKENPgPVNVRDHF-RHA-------LFSLllyMCFGERLDEETVREL-ERVQRELLLSFTDFDV 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 226 VNSFPNLARRLHMKMtaepiERFFMRIVRETVAF-----REQNNIRRNDFMDQ---LIDLKNKPLMVSQSGESvNLTIEE 297
Cdd:cd11075 158 RDFFPALTWLLNRRR-----WKKVLELRRRQEEVllpliRARRKRRASGEADKdytDFLLLDLLDLKEEGGER-KLTDEE 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 298 IAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLY-TVLPV 376
Cdd:cd11075 232 LVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGD-EAVVTEEDLPKMPYLKAVVLETLRRHpPGHFL 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 377 LNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKER-----DSVEWLPFGDGPRNCIG 451
Cdd:cd11075 311 LPHAVTEDTVLGG---YDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAADidtgsKEIKMMPFGAGRRICPG 387
                       410       420
                ....*....|....*....|.
gi 24653745 452 MRFGQMQARIGLALLIKDFKF 472
Cdd:cd11075 388 LGLATLHLELFVARLVQEFEW 408
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
125-470 1.64e-27

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: 114.48  E-value: 1.64e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 125 GQKWRTMRnKLSST-FTSGKMKYMFPTVVK-VANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSlKDPD 202
Cdd:cd11072  60 GEYWRQMR-KICVLeLLSAKRVQSFRSIREeEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEG-KDQD 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 203 aEFREMGRRSLTEQRLGPVG-----IGFVNSFPNLARRLHmKMTAEpIERFFMRIVREtvafREQNNIRRNDFMDQLIDL 277
Cdd:cd11072 138 -KFKELVKEALELLGGFSVGdyfpsLGWIDLLTGLDRKLE-KVFKE-LDAFLEKIIDE----HLDKKRSKDEDDDDDDLL 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 278 KNKplMVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQdiqnRVRKECQEVIEKC---NGELNYESM 354
Cdd:cd11072 211 DLR--LQKEGDLEFPLTRDNIKAIILDMFLAGTDTSATTLEWAMTELIRNP----RVMKKAQEEVREVvggKGKVTEEDL 284
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 355 KDLVYLDQVVSETLRLYTVLPVLN-RECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNF--SPERV 431
Cdd:cd11072 285 EKLKYLKAVIKETLRLHPPAPLLLpRECREDCKING---YDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFldSSIDF 361
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 24653745 432 KERDSvEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:cd11072 362 KGQDF-ELIPFGAGRRICPGITFGLANVELALANLLYHF 399
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
116-473 3.33e-27

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: 113.66  E-value: 3.33e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 116 LSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVA----NEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAF 191
Cdd:cd20640  58 FGGGILTSNGPHWAHQRKIIAPEFFLDKVKGMVDLMVDSAqpllSSWEERIDRAGGMAADIVVDEDLRAFSADVISRACF 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 192 GIECSSLKDPDAEFREMgRRSLTEQRLgPVGIGFVNSFPNLARRLHMKMTAEpIERFFMRIVREtvafREQNNIRRNDFM 271
Cdd:cd20640 138 GSSYSKGKEIFSKLREL-QKAVSKQSV-LFSIPGLRHLPTKSNRKIWELEGE-IRSLILEIVKE----REEECDHEKDLL 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 272 DQLIDlknkplmVSQSGESVNLTIEE-IAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIekCNGELN 350
Cdd:cd20640 211 QAILE-------GARSSCDKKAEAEDfIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVC--KGGPPD 281
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 351 YESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLY-ANPNTFNPDNFSPE 429
Cdd:cd20640 282 ADSLSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLGG---LVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNG 358
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 24653745 430 RVKE-RDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFS 473
Cdd:cd20640 359 VAAAcKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLILSKFSFT 403
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
70-476 4.21e-27

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: 113.08  E-value: 4.21e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEfnKFTDR--GFFHNPEDDPLSGQLFLLDGQKW--------RTMRNklsstF 139
Cdd:cd20651   1 GDVVGLKLGKDKVVVVSGYEAVREVLSRE--EFDGRpdGFFFRLRTFGKRLGITFTDGPFWkeqrrfvlRHLRD-----F 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 140 TSGKmKYMFPTVVKVANEFTDVFGQNVAKspVVEVRELLARFTTDVIGTCAFGiECSSLKDPD-AEFREMGRRSlteQRL 218
Cdd:cd20651  74 GFGR-RSMEEVIQEEAEELIDLLKKGEKG--PIQMPDLFNVSVLNVLWAMVAG-ERYSLEDQKlRKLLELVHLL---FRN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 219 GPVGIGFVNSFP------------NLARRLHMKMTAepierFFMRIVRETVAFREQNNIRrnDFMDQ-LIDLKNkplmvs 285
Cdd:cd20651 147 FDMSGGLLNQFPwlrfiapefsgyNLLVELNQKLIE-----FLKEEIKEHKKTYDEDNPR--DLIDAyLREMKK------ 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 286 QSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcnGEL-NYESMKDLVYLDQVV 364
Cdd:cd20651 214 KEPPSSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGR--DRLpTLDDRSKLPYTEAVI 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 365 SETLRLYTVLPV-LNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSvEW-LPF 442
Cdd:cd20651 292 LEVLRIFTLVPIgIPHRALKDTTLGG---YRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKD-EWfLPF 367
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 24653745 443 GDGPRNCIgmrfGQMQARIGLAL----LIKDFKFSVCE 476
Cdd:cd20651 368 GAGKRRCL----GESLARNELFLfftgLLQNFTFSPPN 401
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
120-472 4.32e-27

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: 113.63  E-value: 4.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 120 LFLLDGQKWRTMRNKLSSTFTSGKMKymfpTVVKVANEFTDVFG---QNVAK--SPVVEVRELLARFTTDVIGTCAFGIE 194
Cdd:cd20679  63 LLLSSGDKWSRHRRLLTPAFHFNILK----PYVKIFNQSTNIMHakwRRLASegSARLDMFEHISLMTLDSLQKCVFSFD 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 195 CSSLKDPD---AEFREMGRRSLTEQRLGPVGIGFVNSFPNLARRLHM------KMTAEPI-ERffMRIVRETVAFREQNN 264
Cdd:cd20679 139 SNCQEKPSeyiAAILELSALVVKRQQQLLLHLDFLYYLTADGRRFRRacrlvhDFTDAVIqER--RRTLPSQGVDDFLKA 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 265 IRRNDFMDqLIDLknkpLMVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVI-E 343
Cdd:cd20679 217 KAKSKTLD-FIDV----LLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLkD 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 344 KCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNP 423
Cdd:cd20679 292 REPEEIEWDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLPD--GRVIPKGIICLISIYGTHHNPTVWPDPEVYDP 369
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*....
gi 24653745 424 DNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKF 472
Cdd:cd20679 370 FRFDPENSQGRSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRV 418
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
71-473 3.39e-26

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: 110.42  E-value: 3.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  71 PFAGfywfrrPAVFVLETSLAKQILIKE--FNKFTDRGFFHnpeddPLSGQ--LFLLDGQKWRTMRNKLSSTFTSGKMKY 146
Cdd:cd11051   7 PFAP------PLLVVTDPELAEQITQVTnlPKPPPLRKFLT-----PLTGGssLISMEGEEWKRLRKRFNPGFSPQHLMT 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 147 MFPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIecsslkDPDAEfreMGRRSLTEQRLgpVGIGFV 226
Cdd:cd11051  76 LVPTILDEVEIFAAILRELAESGEVFSLEELTTNLTFDVIGRVTLDI------DLHAQ---TGDNSLLTALR--LLLALY 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 227 NSFPNLARRLhmkmtaepierFFMRIVRetvafREQNNIRRNDFMDQLIDLK-NKPLMVSQ------SGEsvnltieeia 299
Cdd:cd11051 145 RSLLNPFKRL-----------NPLRPLR-----RWRNGRRLDRYLKPEVRKRfELERAIDQiktflfAGH---------- 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 300 aqafvffaagfETSSTTMGFALYELAQNQDIQNRVRKECQEVI--------EKCNGelNYESMKDLVYLDQVVSETLRLY 371
Cdd:cd11051 199 -----------DTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFgpdpsaaaELLRE--GPELLNQLPYTTAVIKETLRLF 265
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 372 TVLPVLNRecledyevpGHP--KYVIKKGMP------VLIPC-GAMHRDEKLYANPntfnpDNFSPERVKERDSVE---- 438
Cdd:cd11051 266 PPAGTARR---------GPPgvGLTDRDGKEyptdgcIVYVChHAIHRDPEYWPRP-----DEFIPERWLVDEGHElypp 331
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 24653745 439 ---WLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFS 473
Cdd:cd11051 332 ksaWRPFERGPRNCIGQELAMLELKIILAMTVRRFDFE 369
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
129-478 1.30e-25

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: 108.88  E-value: 1.30e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 129 RTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPD--AEFR 206
Cdd:cd11062  56 RLRRKALSPFFSKRSILRLEPLIQEKVDKLVSRLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGYLDEPDfgPEFL 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 207 EMGR---RSLTEQRLGPVGIGFVNSFP-NLARRLHMKMTAEpieRFFMRIVRETVAFREQNNirrNDFMDQLIDLKNKPL 282
Cdd:cd11062 136 DALRalaEMIHLLRHFPWLLKLLRSLPeSLLKRLNPGLAVF---LDFQESIAKQVDEVLRQV---SAGDPPSIVTSLFHA 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 283 MVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELNYESMKDLVYLDQ 362
Cdd:cd11062 210 LLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDPDSPPSLAELEKLPYLTA 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 363 VVSETLRLYTVLPV-LNRECLEDYEVPGhpKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDN-FSPERVKERDSveWL 440
Cdd:cd11062 290 VIKEGLRLSYGVPTrLPRVVPDEGLYYK--GWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERwLGAAEKGKLDR--YL 365
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 24653745 441 -PFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKT 478
Cdd:cd11062 366 vPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYETT 404
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
104-477 1.96e-25

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: 108.44  E-value: 1.96e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 104 DRGFFHNPEDDPLSgqLFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTT 183
Cdd:cd11058  36 DPRFYPPAPNGPPS--ISTADDEDHARLRRLLAHAFSEKALREQEPIIQRYVDLLVSRLRERAGSGTPVDMVKWFNFTTF 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 184 DVIGTCAFGIECSSLKDPD---------AEFREMGRRSLTeQRLGPVGIGFVNSFPNLA---RRLHMKMTAEPIERffmR 251
Cdd:cd11058 114 DIIGDLAFGESFGCLENGEyhpwvalifDSIKALTIIQAL-RRYPWLLRLLRLLIPKSLrkkRKEHFQYTREKVDR---R 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 252 IVRETvafreqnniRRNDFMDQLIDlknkplmvsQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQ 331
Cdd:cd11058 190 LAKGT---------DRPDFMSYILR---------NKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVL 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 332 NRVRkecQEVIEKCN--GELNYESMKDLVYLDQVVSETLRLYTVLPV-LNREC------LEDYEVPGhpkyvikkGMPVL 402
Cdd:cd11058 252 RKLV---DEIRSAFSseDDITLDSLAQLPYLNAVIQEALRLYPPVPAgLPRVVpaggatIDGQFVPG--------GTSVS 320
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24653745 403 IPCGAMHRDEKLYANPNTFNPDNF--SPERVKERDSVEWL-PFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEK 477
Cdd:cd11058 321 VSQWAAYRSPRNFHDPDEFIPERWlgDPRFEFDNDKKEAFqPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPE 398
PLN02738 PLN02738
carotene beta-ring hydroxylase
44-474 8.56e-25

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 108.08  E-value: 8.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   44 GSMKGVRTARSF---NEIWTSYYNKFRGS-GPfagfywfrRPAVFVLETSLAKQILiKEFNKFTDRGFFHNPEDDPLSGQ 119
Cdd:PLN02738 143 GSISAVRGEAFFiplYELFLTYGGIFRLTfGP--------KSFLIVSDPSIAKHIL-RDNSKAYSKGILAEILEFVMGKG 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  120 LFLLDGQKWRTMRNKLSSTFtsgKMKYMfPTVVKVANEFTDVFGQNVAKSPV----VEVRELLARFTTDVIGTCAFGIEC 195
Cdd:PLN02738 214 LIPADGEIWRVRRRAIVPAL---HQKYV-AAMISLFGQASDRLCQKLDAAASdgedVEMESLFSRLTLDIIGKAVFNYDF 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  196 SSLKDpDAefremgrrslteqrlgpvgiGFVNSFPNLARRLHMKMTAePIERFFMRIVRETVAFREQNNIRR---NDFMD 272
Cdd:PLN02738 290 DSLSN-DT--------------------GIVEAVYTVLREAEDRSVS-PIPVWEIPIWKDISPRQRKVAEALkliNDTLD 347
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  273 QLIDLKNKplMVSQ-----------------------SGESVnlTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQD 329
Cdd:PLN02738 348 DLIAICKR--MVEEeelqfheeymnerdpsilhfllaSGDDV--SSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPS 423
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  330 IQNRVRKECQEVIEkcNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGHPkyvIKKGMPVLIPCGAMH 409
Cdd:PLN02738 424 VVAKLQEEVDSVLG--DRFPTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGYP---IKRGEDIFISVWNLH 498
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24653745  410 RDEKLYANPNTFNPDNF---SPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSV 474
Cdd:PLN02738 499 RSPKHWDDAEKFNPERWpldGPNPNETNQNFSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQL 566
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
70-482 1.01e-24

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: 106.53  E-value: 1.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLD--GQKWRTMRnKLSST-FTSGKMKY 146
Cdd:cd20655   1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFApyGDYWKFMK-KLCMTeLLGPRALE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 147 MFptvVKVANEFTDVFGQNVAKSP----VVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRSLteqrlGPVG 222
Cdd:cd20655  80 RF---RPIRAQELERFLRRLLDKAekgeSVDIGKELMKLTNNIICRMIMGRSCSEENGEAEEVRKLVKESA-----ELAG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 223 IGFVNSFPNLARRLHM----KMTAEPIERF---FMRIVRETVAFREQN-NIRRNDFMDQLIDlknkplmVSQSGES-VNL 293
Cdd:cd20655 152 KFNASDFIWPLKKLDLqgfgKRIMDVSNRFdelLERIIKEHEEKRKKRkEGGSKDLLDILLD-------AYEDENAeYKI 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 294 TIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNgeLNYES-MKDLVYLDQVVSETLRLYT 372
Cdd:cd20655 225 TRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTR--LVQESdLPNLPYLQAVVKETLRLHP 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 373 VLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNF-------SPERVKERDsVEWLPFGDG 445
Cdd:cd20655 303 PGPLLVRESTEGCKING---YDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFlassrsgQELDVRGQH-FKLLPFGSG 378
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 24653745 446 PRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTTIPM 482
Cdd:cd20655 379 RRGCPGASLAYQVVGTAIAAMVQCFDWKVGDGEKVNM 415
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
63-454 3.72e-23

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: 101.99  E-value: 3.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  63 YNKFRGSG-PFAgFYWFRRPAVfVLETSLAKQI-------LIKEFNKFTDRGFFHNPEDDPLSGQLFlldgqkWRTMRNK 134
Cdd:cd11041   4 YEKYKKNGgPFQ-LPTPDGPLV-VLPPKYLDELrnlpesvLSFLEALEEHLAGFGTGGSVVLDSPLH------VDVVRKD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 135 LSStftsgKMKYMFPTVVK-VANEFTDVFGQNVAKSPVVeVRELLARFTTDVIGTCAFGIECSSlkdpDAEFREMgrrSL 213
Cdd:cd11041  76 LTP-----NLPKLLPDLQEeLRAALDEELGSCTEWTEVN-LYDTVLRIVARVSARVFVGPPLCR----NEEWLDL---TI 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 214 TEQRLGPVGIGFVNSFPNLAR-------------RLHMKMTAEPIERffmRIVRETVAFREQNNIRRNDFMDQLIDlknk 280
Cdd:cd11041 143 NYTIDVFAAAAALRLFPPFLRplvapflpeprrlRRLLRRARPLIIP---EIERRRKLKKGPKEDKPNDLLQWLIE---- 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 281 plmvsQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCnGELNYESMKDLVYL 360
Cdd:cd11041 216 -----AAKGEGERTPYDLADRQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEH-GGWTKAALNKLKKL 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 361 DQVVSETLRLYTVLPV-LNRECLEDYEVP-GhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERD--- 435
Cdd:cd11041 290 DSFMKESQRLNPLSLVsLRRKVLKDVTLSdG---LTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQekk 366
                       410       420
                ....*....|....*....|....*
gi 24653745 436 ------SVEWLPFGDGPRNCIGmRF 454
Cdd:cd11041 367 hqfvstSPDFLGFGHGRHACPG-RF 390
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
80-488 1.78e-22

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: 99.68  E-value: 1.78e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  80 RPAVFVLETSLAKQILIKEFNKFTDRGFFHN----PEDDPLSgqlFLLDGQKWRtMRNKLSS----TFTSGKMK-YMFPT 150
Cdd:cd11028  12 RPVVVLNGLETIKQALVRQGEDFAGRPDFYSfqfiSNGKSMA---FSDYGPRWK-LHRKLAQnalrTFSNARTHnPLEEH 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 151 VVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGieCSSLKDpDAEFREMgrRSLTEQRLGPVGIG----FV 226
Cdd:cd11028  88 VTEEAEELVTELTENNGKPGPFDPRNEIYLSVGNVICAICFG--KRYSRD-DPEFLEL--VKSNDDFGAFVGAGnpvdVM 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 227 NSFPNLARRLHMKMTA--EPIERFFMRIVRETVAFREQNNIRrnDFMDQLIDLKNKplMVSQSGESVNLTIEEIAAQAFV 304
Cdd:cd11028 163 PWLRYLTRRKLQKFKEllNRLNSFILKKVKEHLDTYDKGHIR--DITDALIKASEE--KPEEEKPEVGLTDEHIISTVQD 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 305 FFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVI-EKCNGELnyESMKDLVYLDQVVSETLRLYTVLPV-LNRECL 382
Cdd:cd11028 239 LFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIgRERLPRL--SDRPNLPYTEAFILETMRHSSFVPFtIPHATT 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 383 EDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNF-SPERVKERDSVE-WLPFGDGPRNCIGMRFGQMQAR 460
Cdd:cd11028 317 RDTTLNG---YFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFlDDNGLLDKTKVDkFLPFGAGRRRCLGEELARMELF 393
                       410       420       430
                ....*....|....*....|....*....|
gi 24653745 461 IGLALLIKDFKFSVC--EKTTIPMTYNKEM 488
Cdd:cd11028 394 LFFATLLQQCEFSVKpgEKLDLTPIYGLTM 423
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
125-492 2.05e-22

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: 99.42  E-value: 2.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 125 GQKWRTMRnKLSST-FTSGKMKYMFPTVVK--VANEFTDVFGQNVAKSPVVeVRELLARFTTDVIGTCA-----FGIECS 196
Cdd:cd20657  58 GPRWRLLR-KLCNLhLFGGKALEDWAHVREneVGHMLKSMAEASRKGEPVV-LGEMLNVCMANMLGRVMlskrvFAAKAG 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 197 SLKDpdaEFREMgrrsLTE--QRLGPVGIG-FVnsfPNLA-----------RRLHMKMTAepierFFMRIVRETVAfREQ 262
Cdd:cd20657 136 AKAN---EFKEM----VVElmTVAGVFNIGdFI---PSLAwmdlqgvekkmKRLHKRFDA-----LLTKILEEHKA-TAQ 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 263 NNIRRNDFMDqlIDLKNKPLmvsqSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVI 342
Cdd:cd20657 200 ERKGKPDFLD--FVLLENDD----NGEGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVI 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 343 EKcNGELNYESMKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTF 421
Cdd:cd20657 274 GR-DRRLLESDIPNLPYLQAICKETFRLHPSTPLnLPRIASEACEVDG---YYIPKGTRLLVNIWAIGRDPDVWENPLEF 349
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653745 422 NPDNFSPER-----VKERDsVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTTIPMTYNKEMFLIA 492
Cdd:cd20657 350 KPERFLPGRnakvdVRGND-FELIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKLPAGQTPEELNMEEAFGLA 424
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
70-457 1.20e-21

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: 97.26  E-value: 1.20e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVleTSL--AKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLL--DGQKWRTMRnklsstftsgKMk 145
Cdd:cd11065   2 GPIISLKVGGQTIIVL--NSPkaAKDLLEKRSAIYSSRPRMPMAGELMGWGMRLLLmpYGPRWRLHR----------RL- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 146 ymfptvvkvaneFTDVFGQNVAKS--PVVE------VRELLA----------RFTTDVIGTCAFGIECSSLKDPDAEFRE 207
Cdd:cd11065  69 ------------FHQLLNPSAVRKyrPLQEleskqlLRDLLEspddfldhirRYAASIILRLAYGYRVPSYDDPLLRDAE 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 208 MGRRSLTEqrLGPVGIGFVNSFPNLaRRL----------HMKMTAEPIERFFMRIVRETVAFREQNNIRRNdFMDQLIDL 277
Cdd:cd11065 137 EAMEGFSE--AGSPGAYLVDFFPFL-RYLpswlgapwkrKARELRELTRRLYEGPFEAAKERMASGTATPS-FVKDLLEE 212
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 278 KNKplmvsqsgeSVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDL 357
Cdd:cd11065 213 LDK---------EGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGP-DRLPTFEDRPNL 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 358 VYLDQVVSETLRLYTVLPV-LNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERvKERDS 436
Cdd:cd11065 283 PYVNAIVKEVLRWRPVAPLgIPHALTEDDEYEG---YFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDP-KGTPD 358
                       410       420
                ....*....|....*....|....
gi 24653745 437 VEWLP---FGDGPRNCIGMRFGQM 457
Cdd:cd11065 359 PPDPPhfaFGFGRRICPGRHLAEN 382
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
120-500 1.23e-21

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: 97.35  E-value: 1.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 120 LFLLDGQKWRTMRNKLSSTFTSGKMK-YmfptvVKVANEFT----DVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIE 194
Cdd:cd20678  60 LLVLNGQKWFQHRRLLTPAFHYDILKpY-----VKLMADSVrvmlDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQ 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 195 CSSLKDPDAE-----FREMGR------RSLTEQ-----RLGPVGIGFvnsfpNLARRLHMKMTAEPI-ERffmrivRETV 257
Cdd:cd20678 135 GSCQLDGRSNsyiqaVSDLSNlifqrlRNFFYHndfiyKLSPHGRRF-----RRACQLAHQHTDKVIqQR------KEQL 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 258 -AFREQNNI---RRNDFMDQLIDLKnkplmvSQSGESvnLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNR 333
Cdd:cd20678 204 qDEGELEKIkkkRHLDFLDILLFAK------DENGKS--LSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQR 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 334 VRKECQEVIekcnGE---LNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVP-GHPkyvIKKGMPVLIPCGAMH 409
Cdd:cd20678 276 CREEIREIL----GDgdsITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPdGRS---LPAGITVSLSIYGLH 348
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 410 RDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVcEKTTIPMTYNKemF 489
Cdd:cd20678 349 HNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFELLP-DPTRIPIPIPQ--L 425
                       410
                ....*....|.
gi 24653745 490 LIASNSGIYLK 500
Cdd:cd20678 426 VLKSKNGIHLY 436
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
92-503 2.46e-21

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 97.16  E-value: 2.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   92 KQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYmFPTVV--KVANEFTDVFGQNVAKS 169
Cdd:PLN03195  87 EHVLKTNFANYPKGEVYHSYMEVLLGDGIFNVDGELWRKQRKTASFEFASKNLRD-FSTVVfrEYSLKLSSILSQASFAN 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  170 PVVEVRELLARFTTDVIGTCAFGIECSSL-----KDPDAEFREMGRRSLTEQRLGPvgIGFVNSFPNLARRLHMKMTAEP 244
Cdd:PLN03195 166 QVVDMQDLFMRMTLDSICKVGFGVEIGTLspslpENPFAQAFDTANIIVTLRFIDP--LWKLKKFLNIGSEALLSKSIKV 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  245 IERFFMRIVR----ETVAFREQNNIRRNDFMDQLIDLKNKPlmvsqsgESvNLTIEEIAAQAFVFFAAGFETSSTTMGFA 320
Cdd:PLN03195 244 VDDFTYSVIRrrkaEMDEARKSGKKVKHDILSRFIELGEDP-------DS-NFTDKSLRDIVLNFVIAGRDTTATTLSWF 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  321 LYELAQNQDIQNRVRKECQ----EVIEKCNGE---------------LNYESMKDLVYLDQVVSETLRLYTVLPVLNREC 381
Cdd:PLN03195 316 VYMIMMNPHVAEKLYSELKalekERAKEEDPEdsqsfnqrvtqfaglLTYDSLGKLQYLHAVITETLRLYPAVPQDPKGI 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  382 LEDYEVPGHPKyVIKKGMPVLIPCgAMHRDEKLYAnpntfnPD--NFSPER------VKERDSVEWLPFGDGPRNCIGMR 453
Cdd:PLN03195 396 LEDDVLPDGTK-VKAGGMVTYVPY-SMGRMEYNWG------PDaaSFKPERwikdgvFQNASPFKFTAFQAGPRICLGKD 467
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 24653745  454 FGQMQARIGLALLIKDFKFSVCEKTtiPMTYnKEMFLIASNSGIYLKAER 503
Cdd:PLN03195 468 SAYLQMKMALALLCRFFKFQLVPGH--PVKY-RMMTILSMANGLKVTVSR 514
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
311-477 2.68e-21

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: 96.60  E-value: 2.68e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELNYESMKDLV-----YLDQVVSETLRLYTVLPVLNRECLEDY 385
Cdd:cd20622 276 DTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEAVAEGRLPTAQEIAqaripYLDAVIEEILRCANTAPILSREATVDT 355
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 386 EVPGhpkYVIKKGMPV-LIPCG----------------AMHRDEKLYANPN-TFNPDNFSPER--VKERDSVE------- 438
Cdd:cd20622 356 QVLG---YSIPKGTNVfLLNNGpsylsppieidesrrsSSSAAKGKKAGVWdSKDIADFDPERwlVTDEETGEtvfdpsa 432
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 24653745 439 --WLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEK 477
Cdd:cd20622 433 gpTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPLPE 473
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
311-475 1.14e-20

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: 93.96  E-value: 1.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcnGE--LNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVP 388
Cdd:cd20616 238 DTMSVSLFFMLLLIAQHPEVEEAILKEIQTVL----GErdIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVID 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 389 GhpkYVIKKGMPVLIPCGAMHRDEkLYANPNTFNPDNFSpERVKERdsvEWLPFGDGPRNCIGMRFGQMQARIGLALLIK 468
Cdd:cd20616 314 G---YPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFE-KNVPSR---YFQPFGFGPRSCVGKYIAMVMMKAILVTLLR 385

                ....*..
gi 24653745 469 dfKFSVC 475
Cdd:cd20616 386 --RFQVC 390
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
108-476 1.45e-20

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: 93.80  E-value: 1.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 108 FHNPEDDPLSGQLfllDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIG 187
Cdd:cd11060  40 PKDPRKDNLFSER---DEKRHAALRRKVASGYSMSSLLSLEPFVDECIDLLVDLLDEKAVSGKEVDLGKWLQYFAFDVIG 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 188 TCAFGiecsslkdpdaefREMG--------RRSLTEQRLGPVGIGFVNSFPNLARRLHMK--MTAEPIERFF---MRIVR 254
Cdd:cd11060 117 EITFG-------------KPFGfleagtdvDGYIASIDKLLPYFAVVGQIPWLDRLLLKNplGPKRKDKTGFgplMRFAL 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 255 ETVAFREQNN----IRRNDFMDQLIDLKNKplmvsqsgESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDI 330
Cdd:cd11060 184 EAVAERLAEDaesaKGRKDMLDSFLEAGLK--------DPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRV 255
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 331 QNRVRKECQEVIEKcnGELN----YESMKDLVYLDQVVSETLRLY--TVLPvLNRECLED-YEVPGH--PKYVIkkgmpV 401
Cdd:cd11060 256 YAKLRAEIDAAVAE--GKLSspitFAEAQKLPYLQAVIKEALRLHppVGLP-LERVVPPGgATICGRfiPGGTI-----V 327
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24653745 402 LIPCGAMHRDEKLY-ANPNTFNPDNF---SPERVKERDSVEwLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCE 476
Cdd:cd11060 328 GVNPWVIHRDKEVFgEDADVFRPERWleaDEEQRRMMDRAD-LTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVD 405
PLN02966 PLN02966
cytochrome P450 83A1
70-474 1.59e-20

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 94.43  E-value: 1.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRgffhnpedDPLSGQLFLLDGQK----------WRTMRNK-LSST 138
Cdd:PLN02966  63 GPILSYRIGSRTMVVISSAELAKELLKTQDVNFADR--------PPHRGHEFISYGRRdmalnhytpyYREIRKMgMNHL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  139 FTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGiecsslKDPDAEFREMGRRSL----T 214
Cdd:PLN02966 135 FSPTRVATFKHVREEEARRMMDKINKAADKSEVVDISELMLTFTNSVVCRQAFG------KKYNEDGEEMKRFIKilygT 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  215 EQRLGPVGI-------GFVNSFPNLArrLHMKMTAEPIERFFMRIVRETVAFReqnniRRNDFMDQLIDL-----KNKPL 282
Cdd:PLN02966 209 QSVLGKIFFsdffpycGFLDDLSGLT--AYMKECFERQDTYIQEVVNETLDPK-----RVKPETESMIDLlmeiyKEQPF 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  283 mvsqsgeSVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVI-EKCNGELNYESMKDLVYLD 361
Cdd:PLN02966 282 -------ASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMkEKGSTFVTEDDVKNLPYFR 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  362 QVVSETLRLYTVLPVL-NRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANpntfNPDNFSPERVKERD----- 435
Cdd:PLN02966 355 ALVKETLRIEPVIPLLiPRACIQDTKIAG---YDIPAGTTVNVNAWAVSRDEKEWGP----NPDEFRPERFLEKEvdfkg 427
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 24653745  436 -SVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSV 474
Cdd:PLN02966 428 tDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKL 467
PLN02936 PLN02936
epsilon-ring hydroxylase
311-503 3.91e-20

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 93.32  E-value: 3.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcNGEL-NYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPG 389
Cdd:PLN02936 292 ETTGSVLTWTLYLLSKNPEALRKAQEELDRVL---QGRPpTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPG 368
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  390 HpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDS---VEWLPFGDGPRNCIGMRFGQMQARIGLALL 466
Cdd:PLN02936 369 G--YKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETntdFRYIPFSGGPRKCVGDQFALLEAIVALAVL 446
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24653745  467 IKDFKFSVCEKTTIPMTYNKEmflIASNSGIYLKAER 503
Cdd:PLN02936 447 LQRLDLELVPDQDIVMTTGAT---IHTTNGLYMTVSR 480
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
70-451 4.45e-20

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: 92.24  E-value: 4.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLDGQKWR--------TMRNklsstFTS 141
Cdd:cd11026   2 GPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSNGERWKqlrrfsltTLRN-----FGM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 142 GKmKYMFPTVVKVANEFTDVFGQNvaKSPVVEVRELLARFTTDVIGTCAFGiecSSLKDPDAEFREMGRR-SLTEQRLGP 220
Cdd:cd11026  77 GK-RSIEERIQEEAKFLVEAFRKT--KGKPFDPTFLLSNAVSNVICSIVFG---SRFDYEDKEFLKLLDLiNENLRLLSS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 221 VGIGFVNSFPNLARRL---HMKMT--AEPIERFFMRIVRETVAFREQNNIRrnDFMDQLID--LKNKPLMVSQ-SGESVN 292
Cdd:cd11026 151 PWGQLYNMFPPLLKHLpgpHQKLFrnVEEIKSFIRELVEEHRETLDPSSPR--DFIDCFLLkmEKEKDNPNSEfHEENLV 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 293 LTIEEIAAQAFvffaagfETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYT 372
Cdd:cd11026 229 MTVLDLFFAGT-------ETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGR-NRTPSLEDRAKMPYTDAVIHEVQRFGD 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 373 VLPV-LNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIG 451
Cdd:cd11026 301 IVPLgVPHAVTRDTKFRG---YTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLG 377
PLN02655 PLN02655
ent-kaurene oxidase
266-470 5.07e-20

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 92.50  E-value: 5.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  266 RRNDFMDQLIDLKNKPLMVSQ---------SGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRK 336
Cdd:PLN02655 222 RRTAVMKALIKQQKKRIARGEerdcyldflLSEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYR 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  337 ECQEViekCNGE-LNYESMKDLVYLDQVVSETLRLYTVLPVL-NRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKL 414
Cdd:PLN02655 302 EIREV---CGDErVTEEDLPNLPYLNAVFHETLRKYSPVPLLpPRFVHEDTTLGG---YDIPAGTQIAINIYGCNMDKKR 375
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 24653745  415 YANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:PLN02655 376 WENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEF 431
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
312-471 7.11e-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: 91.54  E-value: 7.11e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 312 TSSTTMGFALyeLAQNQDIQNRVRkecQEVIEKCNGE---LNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVP 388
Cdd:cd11082 237 TSSLVWALQL--LADHPDVLAKVR---EEQARLRPNDeppLTLDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLT 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 389 ghPKYVIKKG---MPVLIPCgamHRDEklYANPNTFNPDNFSPERVKERDS-VEWLPFGDGPRNCIGMRFGQMQ--ARIG 462
Cdd:cd11082 312 --EDYTVPKGtivIPSIYDS---CFQG--FPEPDKFDPDRFSPERQEDRKYkKNFLVFGAGPHQCVGQEYAINHlmLFLA 384

                ....*....
gi 24653745 463 LALLIKDFK 471
Cdd:cd11082 385 LFSTLVDWK 393
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
168-486 2.62e-19

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: 89.97  E-value: 2.62e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 168 KSPVVEVRELLARFTTDVI-----GTCAFGiECSSLKDPDAEFREMGRRSLTEQRLGPVG--IGFVNSFPNLARRLHMKM 240
Cdd:cd20653 103 GFAKVELKPLFSELTFNNImrmvaGKRYYG-EDVSDAEEAKLFRELVSEIFELSGAGNPAdfLPILRWFDFQGLEKRVKK 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 241 TAEPIERFFMRIVRETvafREQNNIRRNDFMDQLIDLknkplmvsQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFA 320
Cdd:cd20653 182 LAKRRDAFLQGLIDEH---RKNKESGKNTMIDHLLSL--------QESQPEYYTDEIIKGLILVMLLAGTDTSAVTLEWA 250
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 321 LYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPVL-NRECLEDYEVPGhpkYVIKKGM 399
Cdd:cd20653 251 MSNLLNHPEVLKKAREEIDTQVGQ-DRLIEESDLPKLPYLQNIISETLRLYPAAPLLvPHESSEDCKIGG---YDIPRGT 326
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 400 PVLIPCGAMHRDEKLYANPNTFNPDNFSPErvkERDSVEWLPFGDGPRNCIGMrfGQMQARIGLAL--LIKDFKFSVCEK 477
Cdd:cd20653 327 MLLVNAWAIHRDPKLWEDPTKFKPERFEGE---EREGYKLIPFGLGRRACPGA--GLAQRVVGLALgsLIQCFEWERVGE 401

                ....*....
gi 24653745 478 TTIPMTYNK 486
Cdd:cd20653 402 EEVDMTEGK 410
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
311-483 6.02e-19

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: 89.21  E-value: 6.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcnGELNYES-MKDLVYLDQVVSETLRLYTVLP-VLNRECLEDYEVP 388
Cdd:cd20654 255 DTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGK--DRWVEESdIKNLVYLQAIVKETLRLYPPGPlLGPREATEDCTVG 332
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 389 GhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERvKERD----SVEWLPFGDGPRNCIGMRFGQMQARIGLA 464
Cdd:cd20654 333 G---YHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTH-KDIDvrgqNFELIPFGSGRRSCPGVSFGLQVMHLTLA 408
                       170
                ....*....|....*....
gi 24653745 465 LLIKDFKFSVCEKTTIPMT 483
Cdd:cd20654 409 RLLHGFDIKTPSNEPVDMT 427
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
70-481 9.47e-19

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: 88.53  E-value: 9.47e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRgffhnpeddPLSGQLFLL-DGQK----------WRTMRNKLSST 138
Cdd:cd20673   2 GPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGR---------PRMVTTDLLsRNGKdiafadysatWQLHRKLVHSA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 139 FT-----SGKMKYMfptVVKVANEFTDVF----GQNVAKSPVvevrelLARFTTDVIGTCAFGiecSSLKDPDAEFREMg 209
Cdd:cd20673  73 FAlfgegSQKLEKI---ICQEASSLCDTLathnGESIDLSPP------LFRAVTNVICLLCFN---SSYKNGDPELETI- 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 210 rRSLTEQRLGPVGIG-FVNSFPNLarrlhmkmtaepieRFF----MRIVRETVAFREQ-------------NNIRRNDFM 271
Cdd:cd20673 140 -LNYNEGIVDTVAKDsLVDIFPWL--------------QIFpnkdLEKLKQCVKIRDKllqkkleehkekfSSDSIRDLL 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 272 DQLIDLKNKP--LMVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVrkecQEVIEKCNGEL 349
Cdd:cd20673 205 DALLQAKMNAenNNAGPDQDSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKI----QEEIDQNIGFS 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 350 NYESMKD---LVYLDQVVSETLRLYTVLPVL-NRECLEDYEVPghpKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDN 425
Cdd:cd20673 281 RTPTLSDrnhLPLLEATIREVLRIRPVAPLLiPHVALQDSSIG---EFTIPKGTRVVINLWALHHDEKEWDQPDQFMPER 357
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653745 426 F---------SPervkerdSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTTIP 481
Cdd:cd20673 358 FldptgsqliSP-------SLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLEVPDGGQLP 415
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
311-470 1.40e-18

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: 87.89  E-value: 1.40e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIeKCNGELNYESMKDLVYLDQVVSETLRLYTVLP----VLNReclEDYE 386
Cdd:cd20648 248 DTISSTLSWSLYELSRHPDVQTALHREITAAL-KDNSVPSAADVARMPLLKAVVKEVLRLYPVIPgnarVIPD---RDIQ 323
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 387 VPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFsperVKERDSVE---WLPFGDGPRNCIGMRFGQMQARIGL 463
Cdd:cd20648 324 VGE---YIIPKKTLITLCHYATSRDENQFPDPNSFRPERW----LGKGDTHHpyaSLPFGFGKRSCIGRRIAELEVYLAL 396

                ....*..
gi 24653745 464 ALLIKDF 470
Cdd:cd20648 397 ARILTHF 403
PLN02302 PLN02302
ent-kaurenoic acid oxidase
249-471 2.18e-18

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 87.85  E-value: 2.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  249 FMRIVRETVAFREQNNI-RRNDFMDQLIDLKNkplmvsQSGESvnLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQN 327
Cdd:PLN02302 246 FQSIVDERRNSRKQNISpRKKDMLDLLLDAED------ENGRK--LDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEH 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  328 QDIQNRVRKEcQEVIEKCNGE----LNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLI 403
Cdd:PLN02302 318 PEVLQKAKAE-QEEIAKKRPPgqkgLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNG---YTIPKGWKVLA 393
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24653745  404 PCGAMHRDEKLYANPNTFNPDNFSPERVKerdSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFK 471
Cdd:PLN02302 394 WFRQVHMDPEVYPNPKEFDPSRWDNYTPK---AGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYR 458
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
293-471 6.90e-18

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: 85.92  E-value: 6.90e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 293 LTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELnYESMKDLVYLDQVVSETLRLYT 372
Cdd:cd20643 230 LPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDM-VKMLKSVPLLKAAIKETLRLHP 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 373 VLPVLNRECLEDYEVpghPKYVIKKGMPVLIPCGAMHRDEKLYanpntFNPDNFSPERVKERDSVEW--LPFGDGPRNCI 450
Cdd:cd20643 309 VAVSLQRYITEDLVL---QNYHIPAGTLVQVGLYAMGRDPTVF-----PKPEKYDPERWLSKDITHFrnLGFGFGPRQCL 380
                       170       180
                ....*....|....*....|.
gi 24653745 451 GMRFGQMQARIGLALLIKDFK 471
Cdd:cd20643 381 GRRIAETEMQLFLIHMLENFK 401
PTZ00404 PTZ00404
cytochrome P450; Provisional
311-473 8.51e-18

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 85.93  E-value: 8.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNgELNYESMKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYEVPG 389
Cdd:PTZ00404 297 DTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRN-KVLLSDRQSTPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIGG 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  390 hpKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFsperVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKD 469
Cdd:PTZ00404 376 --GHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRF----LNPDSNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILN 449

                 ....
gi 24653745  470 FKFS 473
Cdd:PTZ00404 450 FKLK 453
PLN02183 PLN02183
ferulate 5-hydroxylase
245-470 8.60e-18

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 86.06  E-value: 8.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  245 IERFFMRIVRETVAFREQNNIRRN------DFMDQLIDLKNKPLMVSQSGE---SVNLTIEEIAAQAFVFFAAGFETSST 315
Cdd:PLN02183 243 LDGFIDDIIDDHIQKRKNQNADNDseeaetDMVDDLLAFYSEEAKVNESDDlqnSIKLTRDNIKAIIMDVMFGGTETVAS 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  316 TMGFALYELAQNQDIQNRVRKECQEVIeKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVI 395
Cdd:PLN02183 323 AIEWAMAELMKSPEDLKRVQQELADVV-GLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAG---YFI 398
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653745  396 KKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKE--RDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:PLN02183 399 PKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVPDfkGSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCF 475
PLN02687 PLN02687
flavonoid 3'-monooxygenase
125-479 1.07e-17

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 85.63  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  125 GQKWRTMRnKLSSTftsgkmkYMFPTvvKVANEFTDVFGQNVAkspvVEVREL----------------------LARFT 182
Cdd:PLN02687 124 GPRWRALR-KICAV-------HLFSA--KALDDFRHVREEEVA----LLVRELarqhgtapvnlgqlvnvcttnaLGRAM 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  183 tdvIGTCAFGIEcsslKDPDA-EFREMgrrsLTE--QRLGPVGIG-FVnsfPNLA-----------RRLHMKMTAepier 247
Cdd:PLN02687 190 ---VGRRVFAGD----GDEKArEFKEM----VVElmQLAGVFNVGdFV---PALRwldlqgvvgkmKRLHRRFDA----- 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  248 FFMRIVRETVAFREQNNIRRNDFMDQLIDLKNKPLMvsqSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQN 327
Cdd:PLN02687 251 MMNGIIEEHKAAGQTGSEEHKDLLSTLLALKREQQA---DGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRH 327
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  328 QDIQNRVRKECQEVIEKcnGELNYES-MKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYEVPGhpkYVIKKGMPVLIPC 405
Cdd:PLN02687 328 PDILKKAQEELDAVVGR--DRLVSESdLPQLTYLQAVIKETFRLHPSTPLsLPRMAAEECEING---YHIPKGATLLVNV 402
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  406 GAMHRDEKLYANPNTFNPDNFSPER------VKERDsVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTT 479
Cdd:PLN02687 403 WAIARDPEQWPDPLEFRPDRFLPGGehagvdVKGSD-FELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQT 481
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
269-471 1.30e-17

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: 85.10  E-value: 1.30e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 269 DFMDQLIDLKNKPL--MVSQSGE-----------SVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVR 335
Cdd:cd20646 192 SFGKKLIDKKMEEIeeRVDRGEPvegeyltyllsSGKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLY 271
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 336 kecQEVIEKCNGEL--NYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpKYVI-KKGMPVLipCG-AMHRD 411
Cdd:cd20646 272 ---QEVISVCPGDRipTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIVEKEVVVG--DYLFpKNTLFHL--CHyAVSHD 344
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 412 EKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFK 471
Cdd:cd20646 345 ETNFPEPERFKPERWLRDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALSRLIKRFE 404
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
83-481 1.72e-17

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: 84.39  E-value: 1.72e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  83 VFVLETS-LAKQILIKEFNKFTDRgffhnPEddPLSGQLFLLDGQK---------WRTMRNKLSSTFTSGKMKYMFPTVV 152
Cdd:cd20674  14 VVVLNSKrTIREALVRKWADFAGR-----PH--SYTGKLVSQGGQDlslgdysllWKAHRKLTRSALQLGIRNSLEPVVE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 153 KVANEFTDVFgQNVAKSPVVEVRELLARfTTDVIGTCAFGiecsSLKDPDAEFREMgRRSLTE--QRLGPVGIGFVNSFP 230
Cdd:cd20674  87 QLTQELCERM-RAQAGTPVDIQEEFSLL-TCSIICCLTFG----DKEDKDTLVQAF-HDCVQEllKTWGHWSIQALDSIP 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 231 NLaRRL------HMKMTAEPIERFFMRIVRETVAFREQNNIRrnDFMDQLIDLKNKPLMVSQSGEsvnLTIEEIAAQAFV 304
Cdd:cd20674 160 FL-RFFpnpglrRLKQAVENRDHIVESQLRQHKESLVAGQWR--DMTDYMLQGLGQPRGEKGMGQ---LLEGHVHMAVVD 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 305 FFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPV-LNRECLE 383
Cdd:cd20674 234 LFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGP-GASPSYKDRARLPLLNATIAEVLRLRPVVPLaLPHRTTR 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 384 DYEVPGhpkYVIKKGMpVLIP--CGAmHRDEKLYANPNTFNPDNF-SPERVKERdsveWLPFGDGPRNCIGMRFGQMQAR 460
Cdd:cd20674 313 DSSIAG---YDIPKGT-VVIPnlQGA-HLDETVWEQPHEFRPERFlEPGAANRA----LLPFGCGARVCLGEPLARLELF 383
                       410       420
                ....*....|....*....|.
gi 24653745 461 IGLALLIKDFKFSVCEKTTIP 481
Cdd:cd20674 384 VFLARLLQAFTLLPPSDGALP 404
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
125-483 2.34e-17

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: 84.38  E-value: 2.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 125 GQKWRTMRNKLSSTFTSGKMKY-------MFPTVVKVANEFTDVFGQNvAKSPVvEVRELLARFTTDVIGTCAFGIecsS 197
Cdd:cd20652  54 GDLWRDQRRFVHDWLRQFGMTKfgngrakMEKRIATGVHELIKHLKAE-SGQPV-DPSPVLMHSLGNVINDLVFGF---R 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 198 LKDPDAEFREMgrRSLTEQRLGPVGI-GFVNSFPNLARRLHMKMTAEPI-------ERFFMRIVRETVAFREQNNIRRND 269
Cdd:cd20652 129 YKEDDPTWRWL--RFLQEEGTKLIGVaGPVNFLPFLRHLPSYKKAIEFLvqgqaktHAIYQKIIDEHKRRLKPENPRDAE 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 270 FMDQLIDLKNKPLMVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIeKCNGEL 349
Cdd:cd20652 207 DFELCELEKAKKEGEDRDLFDGFYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVV-GRPDLV 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 350 NYESMKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSP 428
Cdd:cd20652 286 TLEDLSSLPYLQACISESQRIRSVVPLgIPHGCTEDAVLAG---YRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLD 362
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24653745 429 ERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTTIPMT 483
Cdd:cd20652 363 TDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKFRIALPDGQPVDSE 417
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
282-479 2.38e-17

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: 84.20  E-value: 2.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 282 LMVSQSgesvnLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKEcqevIEKCNGELNYESMKDLVYLD 361
Cdd:cd20647 227 LLVSKE-----LTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEE----IVRNLGKRVVPTAEDVPKLP 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 362 ---QVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKER-DSV 437
Cdd:cd20647 298 lirALLKETLRLFPVLPGNGRVTQDDLIVGG---YLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRvDNF 374
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 24653745 438 EWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTT 479
Cdd:cd20647 375 GSIPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIKVSPQTT 416
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
70-470 3.93e-17

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: 83.44  E-value: 3.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRnKLSST----FTSGKmK 145
Cdd:cd20670   2 GPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIERNFQGHGVALANGERWRILR-RFSLTilrnFGMGK-R 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 146 YMFPTVVKVANEFTDVFGQnvAKSPVVEVRELLARFTTDVIGTCAFGiecSSLKDPDAEFREMGR---RSLTEQ-----R 217
Cdd:cd20670  80 SIEERIQEEAGYLLEEFRK--TKGAPIDPTFFLSRTVSNVISSVVFG---SRFDYEDKQFLSLLRminESFIEMstpwaQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 218 LGPVGIGFVNSFPNLARRLHMKMtaEPIERFFMRIVRETVAFREQNNIRrnDFMD----QLIDLKNKPlmvsqsgeSVNL 293
Cdd:cd20670 155 LYDMYSGIMQYLPGRHNRIYYLI--EELKDFIASRVKINEASLDPQNPR--DFIDcfliKMHQDKNNP--------HTEF 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 294 TIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcnGELNYESMKDLV---YLDQVVSETLRL 370
Cdd:cd20670 223 NLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVI----GPHRLPSVDDRVkmpYTDAVIHEIQRL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 371 YTVLPV-LNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNC 449
Cdd:cd20670 299 TDIVPLgVPHNVIRDTQFRG---YLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVC 375
                       410       420
                ....*....|....*....|.
gi 24653745 450 IGMRFGQMQARIGLALLIKDF 470
Cdd:cd20670 376 LGEAMARMELFLYFTSILQNF 396
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
120-484 5.32e-17

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: 82.97  E-value: 5.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 120 LFLLDGQKWRTMRNKLSSTFTSGKMKYMF-PTVVKVANEFTDVFGQNVAK----SPVVEVRELLARFTtdvigtcafgIE 194
Cdd:cd20644  58 VFLLNGPEWRFDRLRLNPEVLSPAAVQRFlPMLDAVARDFSQALKKRVLQnargSLTLDVQPDLFRFT----------LE 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 195 CSSLkdpdaefremgrrSLTEQRLGPVG-------IGFVNSF--------------PNLARRLHMKMTAEPIERFfmriv 253
Cdd:cd20644 128 ASNL-------------ALYGERLGLVGhspssasLRFISAVevmlkttvpllfmpRSLSRWISPKLWKEHFEAW----- 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 254 reTVAFREQNNIRRNDFMD-QLIDLKNKPLMVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQN 332
Cdd:cd20644 190 --DCIFQYADNCIQKIYQElAFGRPQHYTGIVAELLLQAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQ 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 333 RVRKECQEVIEKCNGELNyESMKDLVYLDQVVSETLRLYTVLPVLNRE-----CLEDYEVPGhpkyvikkGMPVLIPCGA 407
Cdd:cd20644 268 ILRQESLAAAAQISEHPQ-KALTELPLLKAALKETLRLYPVGITVQRVpssdlVLQNYHIPA--------GTLVQVFLYS 338
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653745 408 MHRDEKLYANPNTFNPDNFSPERVKERdSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTTIPMTY 484
Cdd:cd20644 339 LGRSAALFPRPERYDPQRWLDIRGSGR-NFKHLAFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLVETLSQEDIKTVY 414
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
79-474 7.41e-17

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 83.20  E-value: 7.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745   79 RRPAVfVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLdGQK---WRTMRNK-LSSTFTSGKMKYMFPTVVKV 154
Cdd:PLN03234  72 RRLAV-ISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGF-GQYtayYREMRKMcMVNLFSPNRVASFRPVREEE 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  155 ANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGIECSSLKDPDAEFREMGRRslTEQRLGPV-------GIGFVN 227
Cdd:PLN03234 150 CQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFIDILYE--TQALLGTLffsdlfpYFGFLD 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  228 SFPNLARRLhmKMTAEPIERFFMRIVRETVafrEQNNIRRN--DFMDQLIDL-KNKPLMVSQSGESVNLTIEEIAAQAFv 304
Cdd:PLN03234 228 NLTGLSARL--KKAFKELDTYLQELLDETL---DPNRPKQEteSFIDLLMQIyKDQPFSIKFTHENVKAMILDIVVPGT- 301
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  305 ffaagfETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPVL-NRECLE 383
Cdd:PLN03234 302 ------DTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGD-KGYVSEEDIPNLPYLKAVIKESLRLEPVIPILlHRETIA 374
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  384 DYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYA-NPNTFNPDNFSPER----VKERDsVEWLPFGDGPRNCIGMRFGQMQ 458
Cdd:PLN03234 375 DAKIGG---YDIPAKTIIQVNAWAVSRDTAAWGdNPNEFIPERFMKEHkgvdFKGQD-FELLPFGSGRRMCPAMHLGIAM 450
                        410
                 ....*....|....*.
gi 24653745  459 ARIGLALLIKDFKFSV 474
Cdd:PLN03234 451 VEIPFANLLYKFDWSL 466
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
92-473 1.74e-16

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: 81.39  E-value: 1.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  92 KQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSST---FTSGKmKYMFPTVVKVANEFTDVFgqNVAK 168
Cdd:cd20664  24 KEALVNHAEAFGGRPIIPIFEDFNKGYGILFSNGENWKEMRRFTLTTlrdFGMGK-KTSEDKILEEIPYLIEVF--EKHK 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 169 SPVVEVRELLARFTTDVIGTCAFGiecSSLKDPDAEFREMGRRSLTEQRL-GPVGIGFVNSFPNLArrlhmkmtaePIER 247
Cdd:cd20664 101 GKPFETTLSMNVAVSNIIASIVLG---HRFEYTDPTLLRMVDRINENMKLtGSPSVQLYNMFPWLG----------PFPG 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 248 FFMRIVRETvafREQNNIRRNDFMDQLiDLKNK--------PLMVSQSGESVNLTI----EEIAAQAFVFFAAGFETSST 315
Cdd:cd20664 168 DINKLLRNT---KELNDFLMETFMKHL-DVLEPndqrgfidAFLVKQQEEEESSDSffhdDNLTCSVGNLFGAGTDTTGT 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 316 TMGFALYELAQNQDIQNRVRKECQEVIEkcNGELNYESMKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYEVPGhpkYV 394
Cdd:cd20664 244 TLRWGLLLMMKYPEIQKKVQEEIDRVIG--SRQPQVEHRKNMPYTDAVIHEIQRFANIVPMnLPHATTRDVTFRG---YF 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 395 IKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVK--ERDSveWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKF 472
Cdd:cd20664 319 IPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKfvKRDA--FMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRF 396

                .
gi 24653745 473 S 473
Cdd:cd20664 397 Q 397
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
155-479 2.06e-16

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: 81.42  E-value: 2.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 155 ANEFTDVFGQNVAKSpvVEVRELLARFTTDVIGTCAFGIECSSlkdPDAEFREMGRR-SLTEQRLGPVGIGFVNSFPNLA 233
Cdd:cd20667  89 AAELVKVFAQENGRP--FDPQDPIVHATANVIGAVVFGHRFSS---EDPIFLELIRAiNLGLAFASTIWGRLYDAFPWLM 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 234 RRL---HMKMTA--EPIERFfmrIVRETVAFREQNNIRRNDFMD----QLIDLKNKPLMVSQSGESVNLTIEeiaaqafv 304
Cdd:cd20667 164 RYLpgpHQKIFAyhDAVRSF---IKKEVIRHELRTNEAPQDFIDcylaQITKTKDDPVSTFSEENMIQVVID-------- 232
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 305 FFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNgELNYESMKDLVYLDQVVSETLRLYTVLPV-LNRECLE 383
Cdd:cd20667 233 LFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQ-LICYEDRKRLPYTNAVIHEVQRLSNVVSVgAVRQCVT 311
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 384 DYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGL 463
Cdd:cd20667 312 STTMHG---YYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFF 388
                       330
                ....*....|....*.
gi 24653745 464 ALLIKDFKFSVCEKTT 479
Cdd:cd20667 389 TTLLRTFNFQLPEGVQ 404
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
227-479 2.81e-16

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 81.14  E-value: 2.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  227 NSFP-NLARRL-HMKMTAEpieRFFMRIVRETVAFREQNNIRRNDfmdqlidlknkpLMVSQSGESVNLTIEEIAAQAFV 304
Cdd:PLN02196 207 NSMPiNLPGTLfHKSMKAR---KELAQILAKILSKRRQNGSSHND------------LLGSFMGDKEGLTDEQIADNIIG 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  305 FFAAGFETSSTTMGFALYELAQNQDIQNRVRKEcQEVIEKCNGE---LNYESMKDLVYLDQVVSETLRLYTVLPVLNREC 381
Cdd:PLN02196 272 VIFAARDTTASVLTWILKYLAENPSVLEAVTEE-QMAIRKDKEEgesLTWEDTKKMPLTSRVIQETLRVASILSFTFREA 350
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  382 LEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFspeRVKERDSVeWLPFGDGPRNCIGMRFGQMQARI 461
Cdd:PLN02196 351 VEDVEYEG---YLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRF---EVAPKPNT-FMPFGNGTHSCPGNELAKLEISV 423
                        250
                 ....*....|....*...
gi 24653745  462 GLALLIKDFKFSVCEKTT 479
Cdd:PLN02196 424 LIHHLTTKYRWSIVGTSN 441
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
122-477 3.73e-16

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: 80.41  E-value: 3.73e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 122 LLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQN--VAKSPVVEVRELLARFTTDVIGTCAFGiECSslk 199
Cdd:cd20615  54 LLSGTDWKRVRKVFDPAFSHSAAVYYIPQFSREARKWVQNLPTNsgDGRRFVIDPAQALKFLPFRVIAEILYG-ELS--- 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 200 dpDAEFREMgrRSLTEQRLGPVGIGFVNsfpnlarrlhmKMTAEPIERFF----MRIVRE----TVAF-REQNNIRRNDF 270
Cdd:cd20615 130 --PEEKEEL--WDLAPLREELFKYVIKG-----------GLYRFKISRYLptaaNRRLREfqtrWRAFnLKIYNRARQRG 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 271 MDQLIDLknkplmVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKEcqevIEKCNGELN 350
Cdd:cd20615 195 QSTPIVK------LYEAVEKGDITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREE----ISAAREQSG 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 351 YESMKDL----VYLDQVVSETLRLYTVLPVLNRECL-EDYEVPGhpkYVIKKGMPVLIPCGAM-HRDEKLYANPNTFNPD 424
Cdd:cd20615 265 YPMEDYIlstdTLLAYCVLESLRLRPLLAFSVPESSpTDKIIGG---YRIPANTPVVVDTYALnINNPFWGPDGEAYRPE 341
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 24653745 425 NF-SPERVKERDSveWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEK 477
Cdd:cd20615 342 RFlGISPTDLRYN--FWRFGFGPRKCLGQHVADVILKALLAHLLEQYELKLPDQ 393
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
311-488 4.04e-16

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: 80.23  E-value: 4.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcnGEL-NYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPG 389
Cdd:cd20671 237 ETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGP--GCLpNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQFKG 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 390 hpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKD 469
Cdd:cd20671 315 ---YLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQK 391
                       170
                ....*....|....*....
gi 24653745 470 FKFSvcektTIPMTYNKEM 488
Cdd:cd20671 392 FTFL-----PPPGVSPADL 405
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
102-466 8.38e-16

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: 78.88  E-value: 8.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 102 FTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKM-KYMFPTVVKVANEFTDVFgqnVAKSPVVEVRELLAR 180
Cdd:cd20629  30 FSSETYDATLGGPFLGHSILAMDGEEHRRRRRLLQPAFAPRAVaRWEEPIVRPIAEELVDDL---ADLGRADLVEDFALE 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 181 FTTDVIGTcAFGIecsslkdPDAEFREMGRRSLTEqrlgpvgIGFVNSFPNLARRLHMKMTAEpierfFMRIVRETVAFR 260
Cdd:cd20629 107 LPARVIYA-LLGL-------PEEDLPEFTRLALAM-------LRGLSDPPDPDVPAAEAAAAE-----LYDYVLPLIAER 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 261 EQNNirRNDFMDQLIdlknkplmvSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKecqe 340
Cdd:cd20629 167 RRAP--GDDLISRLL---------RAEVEGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRR---- 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 341 viekcngelnyesmkDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGHpkyVIKKGMPVLIPCGAMHRDEKLYANPNT 420
Cdd:cd20629 232 ---------------DRSLIPAAIEEGLRWEPPVASVPRMALRDVELDGV---TIPAGSLLDLSVGSANRDEDVYPDPDV 293
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 24653745 421 FNPDnfspervkeRDSVEWLPFGDGPRNCIGMRFGQMQARIGLALL 466
Cdd:cd20629 294 FDID---------RKPKPHLVFGGGAHRCLGEHLARVELREALNAL 330
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
311-472 9.08e-16

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: 79.46  E-value: 9.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYEVPG 389
Cdd:cd20668 240 ETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGR-NRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMgLARRVTKDTKFRD 318
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 390 hpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKD 469
Cdd:cd20668 319 ---FFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQN 395

                ...
gi 24653745 470 FKF 472
Cdd:cd20668 396 FRF 398
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
312-456 9.13e-16

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: 79.49  E-value: 9.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 312 TSSTTMgfaLYELAQNQDIQNRVRKE--CQEVIEKCN---GELNYESMKDLVYLDQVVSETLRLytvLPVLN---RECLE 383
Cdd:cd20636 245 SASTSL---VLLLLQHPSAIEKIRQElvSHGLIDQCQccpGALSLEKLSRLRYLDCVVKEVLRL---LPPVSggyRTALQ 318
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24653745 384 DYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDS-VEWLPFGDGPRNCIGMRFGQ 456
Cdd:cd20636 319 TFELDG---YQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGrFNYIPFGGGVRSCIGKELAQ 389
PLN02500 PLN02500
cytochrome P450 90B1
292-477 4.43e-15

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 77.60  E-value: 4.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  292 NLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVI----EKCNGELNYESMKDLVYLDQVVSET 367
Cdd:PLN02500 274 NLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIArakkQSGESELNWEDYKKMEFTQCVINET 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  368 LRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNP-------DNFSPERVKERDSVEWL 440
Cdd:PLN02500 354 LRLGNVVRFLHRKALKDVRYKG---YDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPwrwqqnnNRGGSSGSSSATTNNFM 430
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24653745  441 PFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEK 477
Cdd:PLN02500 431 PFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELAEA 467
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
320-482 7.00e-15

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: 76.64  E-value: 7.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 320 ALYELAQNQDIQNRVRKECQEVIEKCNGELNYESMKDLV----YLDQVVSETLRLYTVlPVLNRECLEDYEVPGhpKYVI 395
Cdd:cd11040 246 LLAHILSDPELLERIREEIEPAVTPDSGTNAILDLTDLLtscpLLDSTYLETLRLHSS-STSVRLVTEDTVLGG--GYLL 322
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 396 KKGMPVLIPCGAMHRDEKLY-ANPNTFNPDNF---SPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFK 471
Cdd:cd11040 323 RKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkkDGDKKGRGLPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFD 402
                       170
                ....*....|.
gi 24653745 472 FSVCEKTTIPM 482
Cdd:cd11040 403 VEPVGGGDWKV 413
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
108-461 2.51e-14

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: 74.49  E-value: 2.51e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 108 FHNPEDDPLSGQLFL-LDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDvfgQNVAKSPVVEVRELLARFTTDVI 186
Cdd:cd11033  52 LPEEDADPAAGRMLInMDPPRHTRLRRLVSRAFTPRAVARLEDRIRERARRLVD---RALARGECDFVEDVAAELPLQVI 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 187 GTcAFGIecsslkdPDAEFREMGRrsLTEQRLGPVGIGFVNSFPNLARRLHMKMTAepierFFMRIVREtvafreqnniR 266
Cdd:cd11033 129 AD-LLGV-------PEEDRPKLLE--WTNELVGADDPDYAGEAEEELAAALAELFA-----YFRELAEE----------R 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 267 RNDFMDQLIDLknkplMVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRkecqeviekcn 346
Cdd:cd11033 184 RANPGDDLISV-----LANAEVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLR----------- 247
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 347 gelnyesmKDLVYLDQVVSETLRLYTvlPVLN--RECLEDYEVPGHPkyvIKKGMPVLIPCGAMHRDEKLYANPNTFNPD 424
Cdd:cd11033 248 --------ADPSLLPTAVEEILRWAS--PVIHfrRTATRDTELGGQR---IRAGDKVVLWYASANRDEEVFDDPDRFDIT 314
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 24653745 425 nfspervkeRDSVEWLPFGDGPRNCIGMRFGQMQARI 461
Cdd:cd11033 315 ---------RSPNPHLAFGGGPHFCLGAHLARLELRV 342
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
311-471 2.86e-14

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: 74.46  E-value: 2.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNREcLEDYEVPGh 390
Cdd:cd20645 240 ETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPA-NQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRT-LDKDTVLG- 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 391 pKYVIKKGMPVLIPCGAMHRDEKLYANPntfnpDNFSPER-VKERDSVE---WLPFGDGPRNCIGMRFGQMQARIGLALL 466
Cdd:cd20645 317 -DYLLPKGTVLMINSQALGSSEEYFEDG-----RQFKPERwLQEKHSINpfaHVPFGIGKRMCIGRRLAELQLQLALCWI 390

                ....*
gi 24653745 467 IKDFK 471
Cdd:cd20645 391 IQKYQ 395
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
345-457 4.28e-14

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: 74.12  E-value: 4.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 345 CNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPD 424
Cdd:cd20637 279 CEGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDG---FQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPD 355
                        90       100       110
                ....*....|....*....|....*....|....
gi 24653745 425 NFSPERVKERDS-VEWLPFGDGPRNCIGMRFGQM 457
Cdd:cd20637 356 RFGQERSEDKDGrFHYLPFGGGVRTCLGKQLAKL 389
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
170-501 5.92e-14

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 74.12  E-value: 5.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  170 PVVeVRELLARFTTDVIGTCAFGIECSSLKDPDA-EFREMGRRSLTEQRLGPVGigfvNSFPNLA-----------RRLH 237
Cdd:PLN00110 168 PVV-VPEMLTFSMANMIGQVILSRRVFETKGSESnEFKDMVVELMTTAGYFNIG----DFIPSIAwmdiqgiergmKHLH 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  238 MKMtaepiERFFMRIVRETVAFREQNNiRRNDFMDQLidlknkplMVSQ-SGESVNLTIEEIAAQAFVFFAAGFETSSTT 316
Cdd:PLN00110 243 KKF-----DKLLTRMIEEHTASAHERK-GNPDFLDVV--------MANQeNSTGEKLTLTNIKALLLNLFTAGTDTSSSV 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  317 MGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYEVPGhpkYVI 395
Cdd:PLN00110 309 IEWSLAEMLKNPSILKRAHEEMDQVIGR-NRRLVESDLPKLPYLQAICKESFRKHPSTPLnLPRVSTQACEVNG---YYI 384
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  396 KKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERD----SVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFK 471
Cdd:PLN00110 385 PKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIDprgnDFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFD 464
                        330       340       350
                 ....*....|....*....|....*....|
gi 24653745  472 FSVCEKTTIPMtynKEMFLIASNSGIYLKA 501
Cdd:PLN00110 465 WKLPDGVELNM---DEAFGLALQKAVPLSA 491
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
311-475 6.56e-14

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: 73.68  E-value: 6.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcnGELNYESMKDLV---YLDQVVSETLRLYTVLPvLN--RECLEDY 385
Cdd:cd20662 239 ETTSTTLRWALLYMALYPEIQEKVQAEIDRVI----GQKRQPSLADREsmpYTNAVIHEVQRMGNIIP-LNvpREVAVDT 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 386 EVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPE-RVKERDSveWLPFGDGPRNCIGMRFGQMQARIGLA 464
Cdd:cd20662 314 KLAG---FHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENgQFKKREA--FLPFSMGKRACLGEQLARSELFIFFT 388
                       170
                ....*....|.
gi 24653745 465 LLIKDFKFSVC 475
Cdd:cd20662 389 SLLQKFTFKPP 399
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
70-472 1.05e-13

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: 72.87  E-value: 1.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNPEDDPLSGQLFLLDGQKWRTMRNKLSST---FTSGKmKY 146
Cdd:cd20669   2 GSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTlrnFGMGK-RS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 147 MFPTVVKVANEFTDVFgQNVAKSPVvEVRELLARFTTDVIGTCAFGiecSSLKDPDAEFREMgRRSLTE--QRLGPVGIG 224
Cdd:cd20669  81 IEERILEEAQFLLEEL-RKTKGAPF-DPTFLLSRAVSNIICSVVFG---SRFDYDDKRLLTI-LNLINDnfQIMSSPWGE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 225 FVNSFPNLARRL---HMKM--TAEPIERFFMRIVRETVAFREQNNIRrnDFMD----QLIDLKNKPLMVSQSgESVNLTI 295
Cdd:cd20669 155 LYNIFPSVMDWLpgpHQRIfqNFEKLRDFIAESVREHQESLDPNSPR--DFIDcfltKMAEEKQDPLSHFNM-ETLVMTT 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 296 EEIAAQAFvffaagfETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLP 375
Cdd:cd20669 232 HNLLFGGT-------ETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGR-NRLPTLEDRARMPYTDAVIHEIQRFADIIP 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 376 V-LNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRF 454
Cdd:cd20669 304 MsLPHAVTRDTNFRG---FLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESL 380
                       410
                ....*....|....*...
gi 24653745 455 GQMQARIGLALLIKDFKF 472
Cdd:cd20669 381 ARMELFLYLTAILQNFSL 398
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
312-461 1.05e-13

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: 72.92  E-value: 1.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 312 TSSTTMGFALYeLAQNQDIQNRVRKECQEVIEKC-----NGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYE 386
Cdd:cd20638 246 TASAATSLIMF-LGLHPEVLQKVRKELQEKGLLStkpneNKELSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFE 324
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653745 387 VPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARI 461
Cdd:cd20638 325 LNG---YQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKI 396
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
252-491 2.30e-13

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 71.93  E-value: 2.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  252 IVRETVAFREQNNIRRNDFMDQLIDlknkplmvsqSGEsvNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQ 331
Cdd:PLN02987 234 VVMKRRKEEEEGAEKKKDMLAALLA----------SDD--GFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLAL 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  332 NRVRKECQEVIEKCN--GELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMH 409
Cdd:PLN02987 302 AQLKEEHEKIRAMKSdsYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKG---YTIPKGWKVFASFRAVH 378
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  410 RDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTTI---PMTYNK 486
Cdd:PLN02987 379 LDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSWVPAEQDKLvffPTTRTQ 458

                 ....*
gi 24653745  487 EMFLI 491
Cdd:PLN02987 459 KRYPI 463
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
78-466 3.23e-13

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: 71.09  E-value: 3.23e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  78 FRRPAVFVLETSLAKQILIKEFNKFTDRGFFHNpEDDPLSGQlflldgqkwrtMRNKLSSTFTSGKMKYMFPTVVKVANE 157
Cdd:cd11078  34 LRDPQTFSSAGGLTPESPLWPEAGFAPTPSLVN-EDPPRHTR-----------LRRLVSRAFTPRRIAALEPRIRELAAE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 158 FTDVFGQnvaKSPVVEVRELLARFTTDVIGTcAFGIecsslkdPDAEFREMgrRSLTEQRLGPVGIgfVNSFPNLARRLH 237
Cdd:cd11078 102 LLDRLAE---DGRADFVADFAAPLPALVIAE-LLGV-------PEEDMERF--RRWADAFALVTWG--RPSEEEQVEAAA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 238 MKMTaepierfFMRIVRETVAFREQNniRRNDFMDQLIdlknkpLMVSQSGESvnLTIEEIAAQAFVFFAAGFETSSTTM 317
Cdd:cd11078 167 AVGE-------LWAYFADLVAERRRE--PRDDLISDLL------AAADGDGER--LTDEELVAFLFLLLVAGHETTTNLL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 318 GFALYELAQNQDIQNRVRkecqeviekcngelnyesmKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKK 397
Cdd:cd11078 230 GNAVKLLLEHPDQWRRLR-------------------ADPSLIPNAVEETLRYDSPVQGLRRTATRDVEIGG---VTIPA 287
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24653745 398 GMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDSV-EWLPFGDGPRNCIGMRFGQMQARIGL-ALL 466
Cdd:cd11078 288 GARVLLLFGSANRDERVFPDPDRFDID---------RPNArKHLTFGHGIHFCLGAALARMEARIALeELL 349
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
311-471 4.85e-13

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: 70.32  E-value: 4.85e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKEcqeviekcngelnyesmKDLVylDQVVSETLRLYTVLPVLNRECLEDYEVPGH 390
Cdd:cd11032 212 ETTTNLLGNAVLCLDEDPEVAARLRAD-----------------PSLI--PGAIEEVLRYRPPVQRTARVTTEDVELGGV 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 391 PkyvIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:cd11032 273 T---IPAGQLVIAWLASANRDERQFEDPDTFDID---------RNPNPHLSFGHGIHFCLGAPLARLEARIALEALLDRF 340

                .
gi 24653745 471 K 471
Cdd:cd11032 341 P 341
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
248-483 5.70e-13

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: 70.81  E-value: 5.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 248 FFMRIVRETVAFREQNNIRrnDFMDQLID-LKNKPLmvsqsGESVNLTI--EEIAAQAFVFFAAGFETSSTTMGFALYEL 324
Cdd:cd20676 192 FLQKIVKEHYQTFDKDNIR--DITDSLIEhCQDKKL-----DENANIQLsdEKIVNIVNDLFGAGFDTVTTALSWSLMYL 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 325 AQNQDIQNRVRKECQEVIEKCNG-ELNYESMkdLVYLDQVVSETLRLYTVLPVLNREC-LEDYEVPGhpkYVIKKGMPVL 402
Cdd:cd20676 265 VTYPEIQKKIQEELDEVIGRERRpRLSDRPQ--LPYLEAFILETFRHSSFVPFTIPHCtTRDTSLNG---YYIPKDTCVF 339
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 403 IPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEW---LPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTT 479
Cdd:cd20676 340 INQWQVNHDEKLWKDPSSFRPERFLTADGTEINKTESekvMLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVPPGVK 419

                ....
gi 24653745 480 IPMT 483
Cdd:cd20676 420 VDMT 423
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
227-471 8.25e-13

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: 69.98  E-value: 8.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 227 NSFPNLARRL---HMKMTA--EPIERFFMRIVRETVAFREQNNIRrnDFMDQ-LIDLKnkplmvsQSGESVNL--TIEEI 298
Cdd:cd20665 157 NNFPALLDYLpgsHNKLLKnvAYIKSYILEKVKEHQESLDVNNPR--DFIDCfLIKME-------QEKHNQQSefTLENL 227
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 299 AAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcnGELNYESMKD---LVYLDQVVSETLRLYTVLP 375
Cdd:cd20665 228 AVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVI----GRHRSPCMQDrshMPYTDAVIHEIQRYIDLVP 303
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 376 V-LNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRF 454
Cdd:cd20665 304 NnLPHAVTCDTKFRN---YLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGL 380
                       250
                ....*....|....*..
gi 24653745 455 GQMQARIGLALLIKDFK 471
Cdd:cd20665 381 ARMELFLFLTTILQNFN 397
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
123-470 1.11e-12

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: 69.29  E-value: 1.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 123 LDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFGQNvAKSPVVEV--RELLARFTTDVIGtcafgiecssLKD 200
Cdd:cd11034  56 TDPPEHKKYRKLLNPFFTPEAVEAFRPRVRQLTNDLIDAFIER-GECDLVTElaNPLPARLTLRLLG----------LPD 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 201 PDAE-FREMGRRSLTEQrlgpvgigfvnsfpnlarrlhmkmTAEPIERFFMRIV---RETVAFREQNNirRNDFMDQLI- 275
Cdd:cd11034 125 EDGErLRDWVHAILHDE------------------------DPEEGAAAFAELFghlRDLIAERRANP--RDDLISRLIe 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 276 -DLKNKPLMVSQSGESVNLTIeeiaaqafvffAAGFETSSTTMGFALYELAQNQDIQNRVRkecqeviekcngelnyesm 354
Cdd:cd11034 179 gEIDGKPLSDGEVIGFLTLLL-----------LGGTDTTSSALSGALLWLAQHPEDRRRLI------------------- 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 355 KDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGHPkyvIKKGMPVLIPCGAMHRDEKLYAnpntfNPDNFSPERVKER 434
Cdd:cd11034 229 ADPSLIPNAVEEFLRFYSPVAGLARTVTQEVEVGGCR---LKPGDRVLLAFASANRDEEKFE-----DPDRIDIDRTPNR 300
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 24653745 435 DsvewLPFGDGPRNCIGMRFGQMQARIGLALLIK---DF 470
Cdd:cd11034 301 H----LAFGSGVHRCLGSHLARVEARVALTEVLKripDF 335
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
234-467 1.44e-12

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: 69.04  E-value: 1.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 234 RRLHMKMTAEPIERFFMRIVREtvafreqnniRRNDFMDQLIDLknkpLMVSQSgESVNLTIEEIAAQAFVFFAAGFETS 313
Cdd:cd11080 145 ARAHGLRCAEQLSQYLLPVIEE----------RRVNPGSDLISI----LCTAEY-EGEALSDEDIKALILNVLLAATEPA 209
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 314 STTMGFALYELAQNQDIQNRVRKecqeviekcngelnyesmkDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGHpky 393
Cdd:cd11080 210 DKTLALMIYHLLNNPEQLAAVRA-------------------DRSLVPRAIAETLRYHPPVQLIPRQASQDVVVSGM--- 267
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653745 394 VIKKGMPVLIPCGAMHRDEKLYANPNTFNPdnFSPERVKERD---SVEWLPFGDGPRNCIGMRFGQMQARIGLALLI 467
Cdd:cd11080 268 EIKKGTTVFCLIGAANRDPAAFEDPDTFNI--HREDLGIRSAfsgAADHLAFGSGRHFCVGAALAKREIEIVANQVL 342
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
123-466 1.62e-12

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: 68.54  E-value: 1.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 123 LDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFtdvfgqnvakspvveVRELLARFTTDVIGtcAFG------IECS 196
Cdd:cd11079  43 MDPPEHTAYRAAIDRYFTPERLARFEPVCRRVAARL---------------VAELPAGGGGDVVG--QFAqpfavrVQTA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 197 SLKDPDAefremgrrslteqrLGPVGIGFVNSFPNLARRLHMKMTAEPIERFFMRIvretvafREQNNIRRNDFMDQLID 276
Cdd:cd11079 106 FLGWPAA--------------LERPLAEWVNKNHAATRSGDRAATAEVAEEFDGII-------RDLLADRRAAPRDADDD 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 277 LKNKPLMVSQSGEsvNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEviekcngelnyesmkd 356
Cdd:cd11079 165 VTARLLRERVDGR--PLTDEEIVSILRNWTVGELGTIAACVGVLVHYLARHPELQARLRANPAL---------------- 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 357 lvyLDQVVSETLRLYTVLPVLNRECLEDYEVPGHPkyvIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDS 436
Cdd:cd11079 227 ---LPAAIDEILRLDDPFVANRRITTRDVELGGRT---IPAGSRVTLNWASANRDERVFGDPDEFDPD---------RHA 291
                       330       340       350
                ....*....|....*....|....*....|.
gi 24653745 437 VEWLPFGDGPRNCIGMRFGQMQARIGL-ALL 466
Cdd:cd11079 292 ADNLVYGRGIHVCPGAPLARLELRILLeELL 322
PLN00168 PLN00168
Cytochrome P450; Provisional
311-472 1.77e-12

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 69.59  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTvlP---VLNRECLEDYEV 387
Cdd:PLN00168 320 DTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQEEVSEEDVHKMPYLKAVVLEGLRKHP--PahfVLPHKAAEDMEV 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  388 PGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSP----ERVKERDS--VEWLPFGDGPRNCIGMRFGQMQARI 461
Cdd:PLN00168 398 GG---YLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLAggdgEGVDVTGSreIRMMPFGVGRRICAGLGIAMLHLEY 474
                        170
                 ....*....|.
gi 24653745  462 GLALLIKDFKF 472
Cdd:PLN00168 475 FVANMVREFEW 485
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
70-484 1.94e-12

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: 68.69  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  70 GPFAGFYWFRRPAVFVLETSLAKQilikEFNKftdrgffhNPEDDPLSGQLFLLDGQKWRT--------MRNKLSSTFTS 141
Cdd:cd20627   2 GPVASFWFGRRLVVSLGSVDLLKQ----HINP--------NKTSDPFETMLKSLLGYQSGSggdaseshVRKKLYENGVT 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 142 GKMKYMFPTVVKVANEFTDVFGQNVAKSPVVEVRELLArFTTDVIGTCAFGiecSSLKDpDAE---FREMGRRSLTEqrl 218
Cdd:cd20627  70 KALQSNFPLLLKLSEELLDKWLSYPESQHVPLCQHMLG-FAMKSVTQMVMG---STFED-DQEvirFRKNHDAIWSE--- 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 219 gpVGIGFVNSF--PNLARRLHMKMTAEPIERFFMRIVREtvafREQNNIRRNDFMDQLIdlknkplmvsqsgeSVNLTIE 296
Cdd:cd20627 142 --IGKGFLDGSleKSTTRKKQYEDALMEMESVLKKVIKE----RKGKNFSQHVFIDSLL--------------QGNLSEQ 201
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 297 EIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcnGELNYESMKDLVYLDQVVSETLRLYTVLPV 376
Cdd:cd20627 202 QVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQVLGK--GPITLEKIEQLRYCQQVLCETVRTAKLTPV 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 377 LNRecLEDYEVPGHPkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVewLPFgDGPRNCIGMRFGQ 456
Cdd:cd20627 280 SAR--LQELEGKVDQ-HIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRFDDESVMKSFSL--LGF-SGSQECPELRFAY 353
                       410       420
                ....*....|....*....|....*...
gi 24653745 457 MQARIGLALLIKDFKFSVCEKTTIPMTY 484
Cdd:cd20627 354 MVATVLLSVLVRKLRLLPVDGQVMETKY 381
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
311-474 2.23e-12

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: 68.95  E-value: 2.23e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcnGELNYESMKDLV---YLDQVVSETLRLYTVLPV-LNRECLEDYE 386
Cdd:cd20663 244 VTTSTTLSWALLLMILHPDVQRRVQQEIDEVI----GQVRRPEMADQArmpYTNAVIHEVQRFGDIVPLgVPHMTSRDIE 319
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 387 VPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPER---VKERdsvEWLPFGDGPRNCIGMRFGQMQARIGL 463
Cdd:cd20663 320 VQG---FLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQghfVKPE---AFMPFSAGRRACLGEPLARMELFLFF 393
                       170
                ....*....|.
gi 24653745 464 ALLIKDFKFSV 474
Cdd:cd20663 394 TCLLQRFSFSV 404
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
246-485 6.58e-12

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


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 67.51  E-value: 6.58e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 246 ERFFMRIVRETvAFREQNNIRRNDFMDQLIDLKNKplmvsqsgesVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELA 325
Cdd:cd20656 190 DRLTKAIMEEH-TLARQKSGGGQQHFVALLTLKEQ----------YDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMI 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 326 QNQDIQNRVRKECQEVIEKcnGELNYES-MKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYEVPGhpkYVIKKGMPVLI 403
Cdd:cd20656 259 RNPRVQEKAQEELDRVVGS--DRVMTEAdFPQLPYLQCVVKEALRLHPPTPLmLPHKASENVKIGG---YDIPKGANVHV 333
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 404 PCGAMHRDEKLYANPNTFNPDNFSPERV--KERDsVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKTT-- 479
Cdd:cd20656 334 NVWAIARDPAVWKNPLEFRPERFLEEDVdiKGHD-FRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHFSWTPPEGTPpe 412

                ....*..
gi 24653745 480 -IPMTYN 485
Cdd:cd20656 413 eIDMTEN 419
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
317-439 6.85e-12

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: 67.29  E-value: 6.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 317 MGFALYELAQ-NQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGHP-KYV 394
Cdd:cd11071 245 LPSLLARLGLaGEELHARLAEEIRSALGS-EGGLTLAALEKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIESHDaSYK 323
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 24653745 395 IKKGMPVlipCGAM---HRDEKLYANPNTFNPDNFSPERVKERDSVEW 439
Cdd:cd11071 324 IKKGELL---VGYQplaTRDPKVFDNPDEFVPDRFMGEEGKLLKHLIW 368
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
238-473 7.55e-12

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 67.54  E-value: 7.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  238 MKMTAEPIERFFMRIVRETVAFREQNNIRR--NDFMDQLIDLKnkplmvSQSGESvNLTIEEIAAQAFVFFAAGFETSST 315
Cdd:PLN03112 242 MREVEKRVDEFHDKIIDEHRRARSGKLPGGkdMDFVDVLLSLP------GENGKE-HMDDVEIKALMQDMIAAATDTSAV 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  316 TMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPVL-NRECLEDYEVPGhpkYV 394
Cdd:PLN03112 315 TNEWAMAEVIKNPRVLRKIQEELDSVVGR-NRMVQESDLVHLNYLRCVVRETFRMHPAGPFLiPHESLRATTING---YY 390
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  395 IKKGMPVLIPCGAMHRDEKLYANPntfnpDNFSPERVKERDS--VEW--------LPFGDGPRNCIGMRFGQMQARIGLA 464
Cdd:PLN03112 391 IPAKTRVFINTHGLGRNTKIWDDV-----EEFRPERHWPAEGsrVEIshgpdfkiLPFSAGKRKCPGAPLGVTMVLMALA 465

                 ....*....
gi 24653745  465 LLIKDFKFS 473
Cdd:PLN03112 466 RLFHCFDWS 474
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
125-472 9.63e-12

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: 66.97  E-value: 9.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 125 GQKWRTMRnKLSST--FTSGKMKYMFPTVVKVANEFTDVFGQNVAKSPVVEVRELLARFTTDVIGTCAFGiECSSLKDPD 202
Cdd:cd11076  57 GEYWRNLR-RIASNhlFSPRRIAASEPQRQAIAAQMVKAIAKEMERSGEVAVRKHLQRASLNNIMGSVFG-RRYDFEAGN 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 203 AEFREMGrrSLTEQrlGPVGIGFVN-----------SFPNLARRLHMkmTAEPIERFFMRIVRETVAFREQNNIRRNDFM 271
Cdd:cd11076 135 EEAEELG--EMVRE--GYELLGAFNwsdhlpwlrwlDLQGIRRRCSA--LVPRVNTFVGKIIEEHRAKRSNRARDDEDDV 208
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 272 DQLIDL-KNKPL-----------MVSQSGESVNLTIEEIaaqafvffaagfetssttmgfaLYELAQNQDIQNRVRKECQ 339
Cdd:cd11076 209 DVLLSLqGEEKLsdsdmiavlweMIFRGTDTVAILTEWI----------------------MARMVLHPDIQSKAQAEID 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 340 EVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPVLN--RECLEDYEVPGHpkyVIKKGMPVLIPCGAMHRDEKLYAN 417
Cdd:cd11076 267 AAVGG-SRRVADSDVAKLPYLQAVVKETLRLHPPGPLLSwaRLAIHDVTVGGH---VVPAGTTAMVNMWAITHDPHVWED 342
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 418 PNTFNPDNFSPERVKERDSV-----EWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKF 472
Cdd:cd11076 343 PLEFKPERFVAAEGGADVSVlgsdlRLAPFGAGRRVCPGKALGLATVHLWVAQLLHEFEW 402
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
311-452 1.51e-11

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 66.29  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcnGELNYES-MKDLVYLDQVVSETLRLYTVLPVL----NrecLEDY 385
Cdd:PLN02394 307 ETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGP--GNQVTEPdTHKLPYLQAVVKETLRLHMAIPLLvphmN---LEDA 381
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  386 EVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSV---EWLPFGDGPRNCIGM 452
Cdd:PLN02394 382 KLGG---YDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAKVEANGndfRFLPFGVGRRSCPGI 448
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
311-465 1.76e-11

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: 65.93  E-value: 1.76e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVrkeCQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGH 390
Cdd:cd20614 222 ETTASIMAWMVIMLAEHPAVWDAL---CDEAAAAGDVPRTPAELRRFPLAEALFRETLRLHPPVPFVFRRVLEEIELGGR 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 391 pkyVIKKGMPVLIPCGAMHRDEKLYAnpntfNPDNFSPERVKERD----SVEWLPFGDGPRNCIG-----MRFGQMQARI 461
Cdd:cd20614 299 ---RIPAGTHLGIPLLLFSRDPELYP-----DPDRFRPERWLGRDrapnPVELLQFGGGPHFCLGyhvacVELVQFIVAL 370

                ....
gi 24653745 462 GLAL 465
Cdd:cd20614 371 AREL 374
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
311-463 2.09e-11

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: 65.31  E-value: 2.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKecqeviekcNGELnyesmkdlvyLDQVVSETLRLYTVlPVLNRECLEDYEVPGH 390
Cdd:cd11035 204 DTVASALGFIFRHLARHPEDRRRLRE---------DPEL----------IPAAVEELLRRYPL-VNVARIVTRDVEFHGV 263
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653745 391 PkyvIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDSVEWLPFGDGPRNCIGMRFGQMQARIGL 463
Cdd:cd11035 264 Q---LKAGDMVLLPLALANRDPREFPDPDTVDFD---------RKPNRHLAFGAGPHRCLGSHLARLELRIAL 324
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
357-480 3.48e-11

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 65.15  E-value: 3.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  357 LVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNpdnfsPERVKERD- 435
Cdd:PLN03141 314 LPFTQNVITETLRMGNIINGVMRKAMKDVEIKG---YLIPKGWCVLAYFRSVHLDEENYDNPYQFN-----PWRWQEKDm 385
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 24653745  436 -SVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFsVCEKTTI 480
Cdd:PLN03141 386 nNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFRW-VAEEDTI 430
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
81-451 6.06e-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: 64.35  E-value: 6.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  81 PAVFVLETSLAKQILIKEFNKFTDR------GFFHNPEDDPLSGQLflldGQKW----RTMRNKL---------SSTFTS 141
Cdd:cd20677  13 PVVVVSGLETIKQVLLKQGESFAGRpdfytfSLIANGKSMTFSEKY----GESWklhkKIAKNALrtfskeeakSSTCSC 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 142 GKMKYMFPTVVKVANEFTDVFGQNVAKSPvvevRELLARFTTDVIGTCAFGiecSSLKDPDAEFREMGRrsLTEQRLGPV 221
Cdd:cd20677  89 LLEEHVCAEASELVKTLVELSKEKGSFDP----VSLITCAVANVVCALCFG---KRYDHSDKEFLTIVE--INNDLLKAS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 222 GIGFVNSFPNLARRL------HMKMTAEPIERFFMRIVRETVAFREQNNIRrnDFMDQLIDL-KNKPLmvsqSGESVNLT 294
Cdd:cd20677 160 GAGNLADFIPILRYLpspslkALRKFISRLNNFIAKSVQDHYATYDKNHIR--DITDALIALcQERKA----EDKSAVLS 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 295 IEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKECQEVIeKCNGELNYESMKDLVYLDQVVSETLRLYTVL 374
Cdd:cd20677 234 DEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKI-GLSRLPRFEDRKSLHYTEAFINEVFRHSSFV 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 375 PVLNREC-LEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVK-ERDSVE-WLPFGDGPRNCIG 451
Cdd:cd20677 313 PFTIPHCtTADTTLNG---YFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQlNKSLVEkVLIFGMGVRKCLG 389
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
311-486 7.68e-11

cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific cytochrome P450 that catalyzes omega- and (omega-1)-hydroxylation of fatty acids such as arachidonic acid, docosahexaenoic acid, and other long chain fatty acids. Mutations in CYP2U1 are associated with hereditary spastic paraplegia (HSP), a neurological disorder, and pigmentary degenerative maculopathy associated with progressive spastic paraplegia. CYP2U1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 64.03  E-value: 7.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcnGELNYESMKD---LVYLDQVVSETLRLYTVLPV-LNRECLEDYE 386
Cdd:cd20666 242 DTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVI----GPDRAPSLTDkaqMPFTEATIMEVQRMTVVVPLsIPHMASENTV 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 387 VPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALL 466
Cdd:cd20666 318 LQG---YTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSL 394
                       170       180
                ....*....|....*....|
gi 24653745 467 IKDFKFSVCEKTTIPMTYNK 486
Cdd:cd20666 395 MQSFTFLLPPNAPKPSMEGR 414
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
311-471 1.42e-10

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


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 63.26  E-value: 1.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKCNgELNYESMKDLVYLDQVVSETLRLYTVLPVL------NRECLED 384
Cdd:cd11074 247 ETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGV-QITEPDLHKLPYLQAVVKETLRLRMAIPLLvphmnlHDAKLGG 325
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 385 YEVPGHPKyvikkgmpVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDS---VEWLPFGDGPRNCIGMRFGQMQARI 461
Cdd:cd11074 326 YDIPAESK--------ILVNAWWLANNPAHWKKPEEFRPERFLEEESKVEANgndFRYLPFGVGRRSCPGIILALPILGI 397
                       170
                ....*....|
gi 24653745 462 GLALLIKDFK 471
Cdd:cd11074 398 TIGRLVQNFE 407
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
114-470 2.65e-10

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: 62.20  E-value: 2.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 114 DPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDVFgqnVAKSPVVEVRELLA-RFTTDVIgtCA-F 191
Cdd:cd11031  60 PLLPGSLMSMDPPEHTRLRRLVAKAFTARRVERLRPRIEEIADELLDAM---EAQGPPADLVEALAlPLPVAVI--CElL 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 192 GIecsSLKDPDaEFREMGRRSLTEQRLGPVGIgfvnsfpnlaRRLHMKMTAepierFFMRIVREtvafreqnniRRNDFM 271
Cdd:cd11031 135 GV---PYEDRE-RFRAWSDALLSTSALTPEEA----------EAARQELRG-----YMAELVAA----------RRAEPG 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 272 DQLIDLknkplMVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKEcqeviekcngelny 351
Cdd:cd11031 186 DDLLSA-----LVAARDDDDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRAD-------------- 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 352 esmKDLVylDQVVSETLRLY--TVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspe 429
Cdd:cd11031 247 ---PELV--PAAVEELLRYIplGAGGGFPRYATEDVELGG---VTIRAGEAVLVSLNAANRDPEVFPDPDRLDLD----- 313
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 24653745 430 rvkeRDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:cd11031 314 ----REPNPHLAFGHGPHHCLGAPLARLELQVALGALLRRL 350
PLN02971 PLN02971
tryptophan N-hydroxylase
238-490 3.18e-10

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 62.36  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  238 MKMTAEPIERFFMRIVRETVA-FREQNNIRRNDFMDQLIDLKNkplmvsQSGESVnLTIEEIAAQAFVFFAAGFETSSTT 316
Cdd:PLN02971 274 MRESSAIMDKYHDPIIDERIKmWREGKRTQIEDFLDIFISIKD------EAGQPL-LTADEIKPTIKELVMAAPDNPSNA 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  317 MGFALYELAQNQDIQNRVRKECQEVIEKcnGELNYES-MKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYEVPGhpkYV 394
Cdd:PLN02971 347 VEWAMAEMINKPEILHKAMEEIDRVVGK--ERFVQESdIPKLNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAG---YH 421
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  395 IKKGMPVLIPCGAMHRDEKLYANPNTFNPD---NFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFK 471
Cdd:PLN02971 422 IPKGSQVLLSRYGLGRNPKVWSDPLSFKPErhlNECSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFK 501
                        250       260
                 ....*....|....*....|.
gi 24653745  472 FSVCEKTTIP--MTYNKEMFL 490
Cdd:PLN02971 502 WKLAGSETRVelMESSHDMFL 522
PLN02774 PLN02774
brassinosteroid-6-oxidase
251-455 3.19e-10

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 62.10  E-value: 3.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  251 RIVRETVAFREQNNIRRNDFMDQLIdlknkplmvSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDI 330
Cdd:PLN02774 227 RMLRQLIQERRASGETHTDMLGYLM---------RKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKA 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  331 QNRVRKECQEVIEKCNGE--LNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAM 408
Cdd:PLN02774 298 LQELRKEHLAIRERKRPEdpIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNG---YVIPKGWRIYVYTREI 374
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24653745  409 HRDEKLYANPNTFNPDNFSPERVKERDSveWLPFGDGPRNCIGMRFG 455
Cdd:PLN02774 375 NYDPFLYPDPMTFNPWRWLDKSLESHNY--FFLFGGGTRLCPGKELG 419
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
363-470 6.82e-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: 60.64  E-value: 6.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 363 VVSETLRLYTVLPVLNRECLEDYEVPGHPkyvIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDSVEWLPF 442
Cdd:cd20625 248 AVEELLRYDSPVQLTARVALEDVEIGGQT---IPAGDRVLLLLGAANRDPAVFPDPDRFDIT---------RAPNRHLAF 315
                        90       100
                ....*....|....*....|....*...
gi 24653745 443 GDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:cd20625 316 GAGIHFCLGAPLARLEAEIALRALLRRF 343
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
360-452 7.80e-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: 60.43  E-value: 7.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 360 LDQVVSETLRLYTVLPVLNRECLEDYEVP--GHPKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDSV 437
Cdd:cd20612 240 LRGYVLEALRLNPIAPGLYRRATTDTTVAdgGGRTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLD---------RPLE 310
                        90
                ....*....|....*
gi 24653745 438 EWLPFGDGPRNCIGM 452
Cdd:cd20612 311 SYIHFGHGPHQCLGE 325
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
105-470 1.02e-09

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: 60.13  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 105 RGFFHNPE-DDPLSGQLFLLDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEftdVFGQNVAKSPVVEVRELLARFTT 183
Cdd:cd20630  42 LPLADEPSlARLIKGGLFLLAPEDHARVRKLVAPAFTPRAIDRLRAEIQAIVDQ---LLDELGEPEEFDVIREIAEHIPF 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 184 DVIgtcafgieCSSLKDPdAEFREMGRR--SLTEQRLGPVGIgfvnsfpnlARRLhmkMTAEPIERFFMRIVRETVAFRE 261
Cdd:cd20630 119 RVI--------SAMLGVP-AEWDEQFRRfgTATIRLLPPGLD---------PEEL---ETAAPDVTEGLALIEEVIAERR 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 262 QNNIRrNDFMDQLIDlknkplmVSQSGESvnLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRKEcqev 341
Cdd:cd20630 178 QAPVE-DDLLTTLLR-------AEEDGER--LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE---- 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 342 iekcngelnyesmKDLvyLDQVVSETLRLYTVLPV-LNRECLEDYEVPGHPkyvIKKGMPVLIPCGAMHRDEKLYANPNT 420
Cdd:cd20630 244 -------------PEL--LRNALEEVLRWDNFGKMgTARYATEDVELCGVT---IRKGQMVLLLLPSALRDEKVFSDPDR 305
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 24653745 421 FNPdnfspervkERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:cd20630 306 FDV---------RRDPNANIAFGYGPHFCIGAALARLELELAVSTLLRRF 346
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
123-451 1.25e-09

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: 60.07  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 123 LDGQKWRTMRNKLSSTFTSGKMKYMFPTVVKVANEFTDvfgqNVAKSPVVEVRELLAR-FTTDVIgtcafgieCSSLKDP 201
Cdd:cd11038  74 LEGADHARLRGLVNPAFTPKAVEALRPRFRATANDLID----GFAEGGECEFVEAFAEpYPARVI--------CTLLGLP 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 202 DAEFREMGRRSLTeqrlgpVGIGFVNSFPNLARRlhmkmtaepIERFFMRI---VRETVAFREQNNirRNDFMDQlidlk 278
Cdd:cd11038 142 EEDWPRVHRWSAD------LGLAFGLEVKDHLPR---------IEAAVEELydyADALIEARRAEP--GDDLIST----- 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 279 nkplMVSQSGESVNLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDiQNRVRKECQEVIEkcngelnyesmkdlv 358
Cdd:cd11038 200 ----LVAAEQDGDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPD-QWRALREDPELAP--------------- 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 359 yldQVVSETLRLYTVLPVLNRECLEDYEVPGHPkyvIKKGMPVLIPCGAMHRDeklyanPNTFNPDNFSPERVKERDsve 438
Cdd:cd11038 260 ---AAVEEVLRWCPTTTWATREAVEDVEYNGVT---IPAGTVVHLCSHAANRD------PRVFDADRFDITAKRAPH--- 324
                       330
                ....*....|...
gi 24653745 439 wLPFGDGPRNCIG 451
Cdd:cd11038 325 -LGFGGGVHHCLG 336
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
311-470 1.62e-09

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: 59.83  E-value: 1.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIEKcNGELNYESMKDLVYLDQVVSETLRLYTVLPV-LNRECLEDYEVPG 389
Cdd:cd20661 252 ETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGP-NGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSKDAVVRG 330
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 390 hpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKD 469
Cdd:cd20661 331 ---YSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQR 407

                .
gi 24653745 470 F 470
Cdd:cd20661 408 F 408
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
360-470 2.14e-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: 2.14e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 360 LDQVVSETLRLYTvlPVLN---RECLEDYEVPGHpkyVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDS 436
Cdd:cd11029 255 WPAAVEELLRYDG--PVALatlRFATEDVEVGGV---TIPAGEPVLVSLAAANRDPARFPDPDRLDIT---------RDA 320
                        90       100       110
                ....*....|....*....|....*....|....
gi 24653745 437 VEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:cd11029 321 NGHLAFGHGIHYCLGAPLARLEAEIALGALLTRF 354
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
260-473 2.19e-09

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: 59.30  E-value: 2.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 260 REQNNIRRNDFMDQLIDLK---NKPLmvsqsgesvnLTIEEIAAQAFVFFAAGFETSSTTMGFALYELAQNQDIQNRVRK 336
Cdd:cd20658 207 REGKKKEEEDWLDVFITLKdenGNPL----------LTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATE 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 337 ECQEVIEKcnGELNYES-MKDLVYLDQVVSETLRLYTVLP-VLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKL 414
Cdd:cd20658 277 ELDRVVGK--ERLVQESdIPNLNYVKACAREAFRLHPVAPfNVPHVAMSDTTVGG---YFIPKGSHVLLSRYGLGRNPKV 351
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24653745 415 YANPNTFNPD---NFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFS 473
Cdd:cd20658 352 WDDPLKFKPErhlNEDSEVTLTEPDLRFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWT 413
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
316-474 1.59e-08

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: 56.55  E-value: 1.59e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 316 TMGFALyelaQNQDIQNRVRKECQEVI---EKCNGELNYESMKDLVYLDQVVSETLRLYTVlPVLNRECLEDYEVPGhpk 392
Cdd:cd20635 233 TLAFIL----SHPSVYKKVMEEISSVLgkaGKDKIKISEDDLKKMPYIKRCVLEAIRLRSP-GAITRKVVKPIKIKN--- 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 393 YVIKKG-MPVLIPCGAmHRDEKLYANPNTFNPDNFSPERVKERDSVE-WLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:cd20635 305 YTIPAGdMLMLSPYWA-HRNPKYFPDPELFKPERWKKADLEKNVFLEgFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKY 383

                ....
gi 24653745 471 KFSV 474
Cdd:cd20635 384 DFTL 387
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
249-451 2.80e-08

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: 55.78  E-value: 2.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 249 FMRIVRETVAFREQNNIRRNDFMDQLIDLKNKPLMVSQSGESVN-------------LTIEEIAAQAFVFFAAGFETSST 315
Cdd:cd11066 167 ILRYFPKMSKFRERADEYRNRRDKYLKKLLAKLKEEIEDGTDKPcivgnilkdkeskLTDAELQSICLTMVSAGLDTVPL 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 316 TMGFALYELAQ--NQDIQNRVRKEcqevIEKCNGELNYESMKDLV-----YLDQVVSETLRLYTVLPV-LNRECLEDYEV 387
Cdd:cd11066 247 NLNHLIGHLSHppGQEIQEKAYEE----ILEAYGNDEDAWEDCAAeekcpYVVALVKETLRYFTVLPLgLPRKTTKDIVY 322
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24653745 388 PGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIG 451
Cdd:cd11066 323 NG---AVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHFSFGAGSRMCAG 383
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
311-476 3.14e-08

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 56.17  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  311 ETSSTTMGFALYELAQNQDIQNRVRKECqeviekcNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGH 390
Cdd:PLN02169 315 DTTSSALTWFFWLLSKHPQVMAKIRHEI-------NTKFDNEDLEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLPSG 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  391 PKyvIKKGMPVLIPCGAMHRDEKLYANpntfNPDNFSPER-------VKERDSVEWLPFGDGPRNCIGMRFGQMQARIGL 463
Cdd:PLN02169 388 HK--VDAESKIVICIYALGRMRSVWGE----DALDFKPERwisdnggLRHEPSYKFMAFNSGPRTCLGKHLALLQMKIVA 461
                        170
                 ....*....|...
gi 24653745  464 ALLIKDFKFSVCE 476
Cdd:PLN02169 462 LEIIKNYDFKVIE 474
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
360-470 2.59e-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: 52.91  E-value: 2.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 360 LDQVVSETLRLYTVLP-VLNRECLEDYEVPGHpkyVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDSVE 438
Cdd:cd11030 252 VPGAVEELLRYLSIVQdGLPRVATEDVEIGGV---TIRAGEGVIVSLPAANRDPAVFPDPDRLDIT---------RPARR 319
                        90       100       110
                ....*....|....*....|....*....|..
gi 24653745 439 WLPFGDGPRNCIGMRFGQMQARIGLALLIKDF 470
Cdd:cd11030 320 HLAFGHGVHQCLGQNLARLELEIALPTLFRRF 351
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
311-473 3.91e-07

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: 52.47  E-value: 3.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 311 ETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcnGELNYESMKD---LVYLDQVVSETLRLYTVLPV-LNRECLEDYE 386
Cdd:cd20672 240 ETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVI----GSHRLPTLDDrakMPYTDAVIHEIQRFSDLIPIgVPHRVTKDTL 315
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 387 VPGhpkYVIKKGMPV-LIPCGAMHrDEKLYANPNTFNPDNFSPERVKERDSVEWLPFGDGPRNCIGMRFGQMQARIGLAL 465
Cdd:cd20672 316 FRG---YLLPKNTEVyPILSSALH-DPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTT 391

                ....*...
gi 24653745 466 LIKDFKFS 473
Cdd:cd20672 392 ILQNFSVA 399
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
320-470 3.07e-06

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: 49.61  E-value: 3.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 320 ALYELAQNQDIQNRVRKECQEVIEKCNGE--------LNYESMKDLVYLDQVVSETLRLYTV-LPVlnRECLEDYEVPGH 390
Cdd:cd20632 238 AMYYLLRHPEALAAVRDEIDHVLQSTGQElgpdfdihLTREQLDSLVYLESAINESLRLSSAsMNI--RVVQEDFTLKLE 315
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 391 PKYVIK--KGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVE--------WLPFGDGPRNCIGMRFGQMQAR 460
Cdd:cd20632 316 SDGSVNlrKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKKTTFYKrgqklkyyLMPFGSGSSKCPGRFFAVNEIK 395
                       170
                ....*....|
gi 24653745 461 IGLALLIKDF 470
Cdd:cd20632 396 QFLSLLLLYF 405
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
320-454 3.13e-06

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: 49.68  E-value: 3.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 320 ALYELAQNQDIQNRVRKECQEVIEKCNGE---------LNYESMKDLVYLDQVVSETLRLYTVLPVLnRECLEDY--EVP 388
Cdd:cd20631 250 SLFYLLRCPEAMKAATKEVKRTLEKTGQKvsdggnpivLTREQLDDMPVLGSIIKEALRLSSASLNI-RVAKEDFtlHLD 328
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653745 389 GHPKYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVE---------WLPFGDGPRNCIGMRF 454
Cdd:cd20631 329 SGESYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTFYkngrklkyyYMPFGSGTSKCPGRFF 403
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
312-468 4.14e-06

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: 48.73  E-value: 4.14e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 312 TSSTTMGFALYELAQNQDIQNRVRKEcqeviekcngelnyesmKDLVylDQVVSETLRLYTVLPVLNRECLEDYEVPGHP 391
Cdd:cd11037 217 TTISAIGNALWLLARHPDQWERLRAD-----------------PSLA--PNAFEEAVRLESPVQTFSRTTTRDTELAGVT 277
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653745 392 kyvIKKGMPVLIPCGAMHRDEKLYANPNTFnpdnfspeRVkERDSVEWLPFGDGPRNCIGMRFGQMQARIGLALLIK 468
Cdd:cd11037 278 ---IPAGSRVLVFLGSANRDPRKWDDPDRF--------DI-TRNPSGHVGFGHGVHACVGQHLARLEGEALLTALAR 342
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
320-485 5.63e-06

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: 48.61  E-value: 5.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 320 ALYELAQNQDIQNRVRKECQEViekcNGELnyesmkDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGM 399
Cdd:cd20624 214 ALALLAAHPEQAARAREEAAVP----PGPL------ARPYLRACVLDAVRLWPTTPAVLRESTEDTVWGG---RTVPAGT 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 400 PVLIPCGAMHRDEKLYANPNTFNPDNFSPERVKERDSVewLPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEKT- 478
Cdd:cd20624 281 GFLIFAPFFHRDDEALPFADRFVPEIWLDGRAQPDEGL--VPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLESPr 358
                       170
                ....*....|..
gi 24653745 479 -----TIPMTYN 485
Cdd:cd20624 359 sgpgePLPGTLD 370
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
362-471 1.22e-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: 47.50  E-value: 1.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 362 QVVSETLRLYTVLPVLNRECLEDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDnfspervkeRDSVEWLP 441
Cdd:cd11039 248 RAFEEGLRWISPIGMSPRRVAEDFEIRG---VTLPAGDRVFLMFGSANRDEARFENPDRFDVF---------RPKSPHVS 315
                        90       100       110
                ....*....|....*....|....*....|.
gi 24653745 442 FGDGPRNCIGMRFG-QMQARIGLALLIKDFK 471
Cdd:cd11039 316 FGAGPHFCAGAWASrQMVGEIALPELFRRLP 346
PLN02648 PLN02648
allene oxide synthase
321-426 2.23e-05

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 46.85  E-value: 2.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  321 LYELAQ-NQDIQNRVRKECQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGH-PKYVIKKG 398
Cdd:PLN02648 296 LKWVGRaGEELQARLAEEVRSAVKAGGGGVTFAALEKMPLVKSVVYEALRIEPPVPFQYGRAREDFVIESHdAAFEIKKG 375
                         90       100       110
                 ....*....|....*....|....*....|..
gi 24653745  399 MpvLIpCG----AMhRDEKLYANPNTFNPDNF 426
Cdd:PLN02648 376 E--ML-FGyqplVT-RDPKVFDRPEEFVPDRF 403
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
161-458 1.01e-04

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: 44.61  E-value: 1.01e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 161 VFGQNVakspVVEVRELLARF-------------------TTDVIGTCAFGieCSSLKDpDAEFREMGRRSltEQRLGPV 221
Cdd:cd20675  85 AFERHV----LGEARELVALFlrksaggayfdpapplvvaVANVMSAVCFG--KRYSHD-DAEFRSLLGRN--DQFGRTV 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 222 GIG-------FVNSFPNLARRLHMKMTAepIERFFMRIVRETVAFREQ---NNIRRnDFMDQLIDL----KNKPLMVSQS 287
Cdd:cd20675 156 GAGslvdvmpWLQYFPNPVRTVFRNFKQ--LNREFYNFVLDKVLQHREtlrGGAPR-DMMDAFILAlekgKSGDSGVGLD 232
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 288 GESVNLTIEEIAAQAFvffaagfETSSTTMGFALYELAQNQDIQNRVRKECQEVIekcnGELNYESMKD---LVYLDQVV 364
Cdd:cd20675 233 KEYVPSTVTDIFGASQ-------DTLSTALQWILLLLVRYPDVQARLQEELDRVV----GRDRLPCIEDqpnLPYVMAFL 301
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 365 SETLRLYTVLPVLNRECL-EDYEVPGhpkYVIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNFSPER-VKERD---SVew 439
Cdd:cd20675 302 YEAMRFSSFVPVTIPHATtADTSILG---YHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENgFLNKDlasSV-- 376
                       330
                ....*....|....*....
gi 24653745 440 LPFGDGPRNCIGMRFGQMQ 458
Cdd:cd20675 377 MIFSVGKRRCIGEELSKMQ 395
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
324-479 1.04e-04

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 44.68  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  324 LAQNQDIQNRVRKECQEVIEKCNGELNYESMKDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPgHPKYViKKGMPVLI 403
Cdd:PLN02426 320 LSKHPEVASAIREEADRVMGPNQEAASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLP-DGTFV-AKGTRVTY 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745  404 PCGAMHRDEKLYAnpntfnPD--NFSPERvkerdsveWLP--------------FGDGPRNCIG--MRFGQMQArIGLAl 465
Cdd:PLN02426 398 HPYAMGRMERIWG------PDclEFKPER--------WLKngvfvpenpfkypvFQAGLRVCLGkeMALMEMKS-VAVA- 461
                        170
                 ....*....|....
gi 24653745  466 LIKDFKFSVCEKTT 479
Cdd:PLN02426 462 VVRRFDIEVVGRSN 475
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
361-460 3.61e-04

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: 42.80  E-value: 3.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 361 DQVVSETLRLYTVLPVLNRECLEDYEVPGHPkyvIKKGMPVLIPCGAMHRDEKLYANPNTFNPDNfSPERVKErdsvewL 440
Cdd:cd20619 235 AAIINEMVRMDPPQLSFLRFPTEDVEIGGVL---IEAGSPIRFMIGAANRDPEVFDDPDVFDHTR-PPAASRN------L 304
                        90       100
                ....*....|....*....|
gi 24653745 441 PFGDGPRNCIGMRFGQMQAR 460
Cdd:cd20619 305 SFGLGPHSCAGQIISRAEAT 324
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
348-481 6.32e-04

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: 42.05  E-value: 6.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 348 ELNYESMKDLVYLDQVVSETLRLyTVLPVLNRECLEDYEVP--GHPKYVIKKGMPV-LIPCGAMHRDEKLYANPNTFNPD 424
Cdd:cd20634 278 TINQELLDNTPVFDSVLSETLRL-TAAPFITREVLQDMKLRlaDGQEYNLRRGDRLcLFPFLSPQMDPEIHQEPEVFKYD 356
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653745 425 NF-SPERVKERD------SVEW--LPFGDGPRNCIGMRFGQMQARIGLALLIKDFKFSVCEK-TTIP 481
Cdd:cd20634 357 RFlNADGTEKKDfykngkRLKYynMPWGAGDNVCIGRHFAVNSIKQFVFLILTHFDVELKDPeAEIP 423
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
319-426 1.51e-03

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: 40.98  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653745 319 FALYELAQNQDIQNRVRKEcqeviekcngelnyesmkDLVYLDQVVSETLRLYTVLPVLNRECLEDYEVPGHPkyvIKKG 398
Cdd:cd11067 242 FAALALHEHPEWRERLRSG------------------DEDYAEAFVQEVRRFYPFFPFVGARARRDFEWQGYR---FPKG 300
                        90       100
                ....*....|....*....|....*...
gi 24653745 399 MPVLIPCGAMHRDEKLYANPNTFNPDNF 426
Cdd:cd11067 301 QRVLLDLYGTNHDPRLWEDPDRFRPERF 328
 
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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