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Conserved domains on  [gi|1032284286|gb|OAO98613|]
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hypothetical protein AXX17_AT4G13830 [Arabidopsis thaliana]

Protein Classification

cytochrome P450( domain architecture ID 15297177)

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
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
70-505 0e+00

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: 658.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  70 AQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRK 149
Cdd:cd11073     1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 150 TLDSFYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVkAEEMESVGTEFKGVISEITRLLSEPN 229
Cdd:cd11073    81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDL-VDPDSESGSEFKELVREIMELAGKPN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 230 VSDFFPWLARFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLmkLKDQEGDSEVPITINHVKALLT 309
Cdd:cd11073   160 VADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLL--LLDLELDSESELTRNHIKALLL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 310 DMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAE 389
Cdd:cd11073   238 DLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAEE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 390 NTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTGANYSYFPFGSGRRICAGVALAERMVLYTLA 469
Cdd:cd11073   318 DVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEI-DFKGRDFELIPFGSGRRICPGLPLAERMVHLVLA 396
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1032284286 470 TLLHSFDWKIPEG---HVLDLKEKFGIVLKLKIPLVALP 505
Cdd:cd11073   397 SLLHSFDWKLPDGmkpEDLDMEEKFGLTLQKAVPLKAIP 435
 
Name Accession Description Interval E-value
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
70-505 0e+00

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: 658.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  70 AQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRK 149
Cdd:cd11073     1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 150 TLDSFYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVkAEEMESVGTEFKGVISEITRLLSEPN 229
Cdd:cd11073    81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDL-VDPDSESGSEFKELVREIMELAGKPN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 230 VSDFFPWLARFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLmkLKDQEGDSEVPITINHVKALLT 309
Cdd:cd11073   160 VADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLL--LLDLELDSESELTRNHIKALLL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 310 DMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAE 389
Cdd:cd11073   238 DLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAEE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 390 NTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTGANYSYFPFGSGRRICAGVALAERMVLYTLA 469
Cdd:cd11073   318 DVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEI-DFKGRDFELIPFGSGRRICPGLPLAERMVHLVLA 396
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1032284286 470 TLLHSFDWKIPEG---HVLDLKEKFGIVLKLKIPLVALP 505
Cdd:cd11073   397 SLLHSFDWKLPDGmkpEDLDMEEKFGLTLQKAVPLKAIP 435
PLN02687 PLN02687
flavonoid 3'-monooxygenase
17-512 3.49e-146

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 429.62  E-value: 3.49e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  17 PYAIVILTTVFS-ILWYIFKRSPQPS-----LPPGPRGLPIVGNLPFLDPDLHTYFANLAQSHGPIFKLNLGSKLTIVVN 90
Cdd:PLN02687    4 PLPLLLGTVAVSvLVWCLLLRRGGSGkhkrpLPPGPRGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  91 SPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYELRRKEVRERTRYLY 170
Cdd:PLN02687   84 SASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVALLVRELA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 171 EQGRkQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTEFKGVISEITRLLSEPNVSDFFPWLARFDLQGLVKRMG 250
Cdd:PLN02687  164 RQHG-TAPVNLGQLVNVCTTNALGRAMVGRRVFAGDGDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLDLQGVVGKMK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 251 VCARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLK-DQEGDSE-VPITINHVKALLTDMVVGGTDTSTNTIEFAMA 328
Cdd:PLN02687  243 RLHRRFDAMMNGIIEEHKAAGQTGSEEHKDLLSTLLALKrEQQADGEgGRITDTEIKALLLNLFTAGTDTTSSTVEWAIA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 329 ELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNV 408
Cdd:PLN02687  323 ELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNV 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 409 WSIQRDPNVWENPTEFRPERFL---DNNSCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEGHV- 484
Cdd:PLN02687  403 WAIARDPEQWPDPLEFRPDRFLpggEHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQTp 482
                         490       500       510
                  ....*....|....*....|....*....|
gi 1032284286 485 --LDLKEKFGIVLKLKIPLVALPIPRFSDS 512
Cdd:PLN02687  483 dkLNMEEAYGLTLQRAVPLMVHPRPRLLPS 512
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
43-496 8.82e-114

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: 344.65  E-value: 8.82e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  43 PPGPRGLPIVGNLPFLDPD--LHTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVP--LTGRAA 118
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEpwFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 119 TYGGIDIVwTPYGAEWRQLRKICVLKLLSRKTLdSFYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLW 198
Cdd:pfam00067  81 PFLGKGIV-FANGPRWRQLRRFLTPTFTSFGKL-SFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 199 GGSVKAEEMESVgTEFKGVISEITRLLS--EPNVSDFFPWLaRFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDDD 276
Cdd:pfam00067 159 GERFGSLEDPKF-LELVKAVQELSSLLSspSPQLLDLFPIL-KYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 277 EVKDFLQYLMKLKDQEGDSEvpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEE 356
Cdd:pfam00067 237 SPRDFLDALLLAKEEEDGSK--LTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 357 SHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCd 436
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGK- 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032284286 437 fTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKI-PEGHVLDLKEKFGIVLK 496
Cdd:pfam00067 394 -FRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELpPGTDPPDIDETPGLLLP 453
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
56-493 8.83e-47

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 167.76  E-value: 8.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  56 PFLDPDLHTYFANLAQsHGPIFKLNLGSKLTIVVNSPSLAREILKDQDiNFSNRDVPLTGRAATYGGIDIVWTPYGAEWR 135
Cdd:COG2124    15 PAFLRDPYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREVLRDPR-TFSSDGGLPEVLRPLPLLGDSLLTLDGPEHT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 136 QLRKIcVLKLLSRKTLDSFyelrRKEVRERTRYLYEQGRKQSPVKVGDQL-FLTMMNLTMNMLwggSVKAEEMEsvgtEF 214
Cdd:COG2124    93 RLRRL-VQPAFTPRRVAAL----RPRIREIADELLDRLAARGPVDLVEEFaRPLPVIVICELL---GVPEEDRD----RL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 215 KGVISEITRLLsepnvsDFFPWLARfdlqglvKRMGVCARELDAVLDRAIEQmkpLRGRDDDevkDFLQYLMKLKDQEG- 293
Cdd:COG2124   161 RRWSDALLDAL------GPLPPERR-------RRARRARAELDAYLRELIAE---RRAEPGD---DLLSALLAARDDGEr 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 294 --DSEVpitINHVKALLtdmvVGGTDTSTNTIEFAMAELMSNPELIKRAQEELdevvgkdniveeshitrlPYILAIMKE 371
Cdd:COG2124   222 lsDEEL---RDELLLLL----LAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEE 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 372 TLRLHPTLPLLvPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERfldnnscdftgANYSYFPFGSGR 451
Cdd:COG2124   277 TLRLYPPVPLL-PRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-----------PPNAHLPFGGGP 344
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1032284286 452 RICAGVALAeRMVLYT-LATLLHSF-DWKIPEGHVLDLKEKFGI 493
Cdd:COG2124   345 HRCLGAALA-RLEARIaLATLLRRFpDLRLAPPEELRWRPSLTL 387
 
Name Accession Description Interval E-value
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
70-505 0e+00

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: 658.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  70 AQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRK 149
Cdd:cd11073     1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 150 TLDSFYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVkAEEMESVGTEFKGVISEITRLLSEPN 229
Cdd:cd11073    81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDL-VDPDSESGSEFKELVREIMELAGKPN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 230 VSDFFPWLARFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLmkLKDQEGDSEVPITINHVKALLT 309
Cdd:cd11073   160 VADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLL--LLDLELDSESELTRNHIKALLL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 310 DMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAE 389
Cdd:cd11073   238 DLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAEE 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 390 NTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTGANYSYFPFGSGRRICAGVALAERMVLYTLA 469
Cdd:cd11073   318 DVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEI-DFKGRDFELIPFGSGRRICPGLPLAERMVHLVLA 396
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1032284286 470 TLLHSFDWKIPEG---HVLDLKEKFGIVLKLKIPLVALP 505
Cdd:cd11073   397 SLLHSFDWKLPDGmkpEDLDMEEKFGLTLQKAVPLKAIP 435
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
74-501 0e+00

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: 523.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDS 153
Cdd:cd20618     1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGQDIVFAPYGPHWRHLRKICTLELFSAKRLES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 154 FYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGS--VKAEEMESVGTEFKGVISEITRLLSEPNVS 231
Cdd:cd20618    81 FQGVRKEELSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRyfGESEKESEEAREFKELIDEAFELAGAFNIG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 232 DFFPWLARFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDQEGDsevPITINHVKALLTDM 311
Cdd:cd20618   161 DYIPWLRWLDLQGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLLDLDGEG---KLSDDNIKALLLDM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 312 VVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENT 391
Cdd:cd20618   238 LAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLPHESTEDC 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 392 VVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATL 471
Cdd:cd20618   318 KVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVKGQDFELLPFGSGRRMCPGMPLGLRMVQLTLANL 397
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1032284286 472 LHSFDWKIP--EGHVLDLKEKFGIVLKLKIPL 501
Cdd:cd20618   398 LHGFDWSLPgpKPEDIDMEEKFGLTVPRAVPL 429
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
73-501 3.30e-168

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: 481.96  E-value: 3.30e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLD 152
Cdd:cd11072     2 YGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGKDIAFAPYGEYWRQMRKICVLELLSAKRVQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 153 SFYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMEsvgtEFKGVISEITRLLSEPNVSD 232
Cdd:cd11072    82 SFRSIREEEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQD----KFKELVKEALELLGGFSVGD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 233 FFPWLARFDLQ-GLVKRMGVCARELDAVLDRAI-EQMKPLRGRDDDEVKDFLqyLMKLKDQEGDSEVPITINHVKALLTD 310
Cdd:cd11072   158 YFPSLGWIDLLtGLDRKLEKVFKELDAFLEKIIdEHLDKKRSKDEDDDDDDL--LDLRLQKEGDLEFPLTRDNIKAIILD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 311 MVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAEN 390
Cdd:cd11072   236 MFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLPRECRED 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 391 TVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTGANYSYFPFGSGRRICAGVALAERMVLYTLAT 470
Cdd:cd11072   316 CKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSI-DFKGQDFELIPFGAGRRICPGITFGLANVELALAN 394
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1032284286 471 LLHSFDWKIPEGHV---LDLKEKFGIVLKLKIPL 501
Cdd:cd11072   395 LLYHFDWKLPDGMKpedLDMEEAFGLTVHRKNPL 428
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
74-508 1.22e-149

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: 435.31  E-value: 1.22e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDS 153
Cdd:cd20657     1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMAYNAQDMVFAPYGPRWRLLRKLCNLHLFGGKALED 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 154 FYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTEFKGVISEITRLLSEPNVSDF 233
Cdd:cd20657    81 WAHVRENEVGHMLKSMAEASRKGEPVVLGEMLNVCMANMLGRVMLSKRVFAAKAGAKANEFKEMVVELMTVAGVFNIGDF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 234 FPWLARFDLQGLVKRMGVCARELDAVLDRAIEQMKpLRGRDDDEVKDFLQYLMKLKDQEGDSEvPITINHVKALLTDMVV 313
Cdd:cd20657   161 IPSLAWMDLQGVEKKMKRLHKRFDALLTKILEEHK-ATAQERKGKPDFLDFVLLENDDNGEGE-RLTDTNIKALLLNLFT 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 314 GGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVV 393
Cdd:cd20657   239 AGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEACEV 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 394 GGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLD--NNSCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATL 471
Cdd:cd20657   319 DGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPgrNAKVDVRGNDFELIPFGAGRRICAGTRMGIRMVEYILATL 398
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1032284286 472 LHSFDWKIPEGHV---LDLKEKFGIVLKLKIPLVALPIPR 508
Cdd:cd20657   399 VHSFDWKLPAGQTpeeLNMEEAFGLALQKAVPLVAHPTPR 438
PLN02687 PLN02687
flavonoid 3'-monooxygenase
17-512 3.49e-146

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 429.62  E-value: 3.49e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  17 PYAIVILTTVFS-ILWYIFKRSPQPS-----LPPGPRGLPIVGNLPFLDPDLHTYFANLAQSHGPIFKLNLGSKLTIVVN 90
Cdd:PLN02687    4 PLPLLLGTVAVSvLVWCLLLRRGGSGkhkrpLPPGPRGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  91 SPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYELRRKEVRERTRYLY 170
Cdd:PLN02687   84 SASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVALLVRELA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 171 EQGRkQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTEFKGVISEITRLLSEPNVSDFFPWLARFDLQGLVKRMG 250
Cdd:PLN02687  164 RQHG-TAPVNLGQLVNVCTTNALGRAMVGRRVFAGDGDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLDLQGVVGKMK 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 251 VCARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLK-DQEGDSE-VPITINHVKALLTDMVVGGTDTSTNTIEFAMA 328
Cdd:PLN02687  243 RLHRRFDAMMNGIIEEHKAAGQTGSEEHKDLLSTLLALKrEQQADGEgGRITDTEIKALLLNLFTAGTDTTSSTVEWAIA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 329 ELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNV 408
Cdd:PLN02687  323 ELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNV 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 409 WSIQRDPNVWENPTEFRPERFL---DNNSCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEGHV- 484
Cdd:PLN02687  403 WAIARDPEQWPDPLEFRPDRFLpggEHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQTp 482
                         490       500       510
                  ....*....|....*....|....*....|
gi 1032284286 485 --LDLKEKFGIVLKLKIPLVALPIPRFSDS 512
Cdd:PLN02687  483 dkLNMEEAYGLTLQRAVPLMVHPRPRLLPS 512
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
74-505 1.36e-143

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: 419.69  E-value: 1.36e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDS 153
Cdd:cd20655     1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 154 FYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMEsvGTEFKGVISEITRLLSEPNVSDF 233
Cdd:cd20655    81 FRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGE--AEEVRKLVKESAELAGKFNASDF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 234 FPWLARFDLQGLVKR-MGVCAReLDAVLDRAI-EQMKPLRGRDDDEVKDFLQYLMKLKDQEGdSEVPITINHVKALLTDM 311
Cdd:cd20655   159 IWPLKKLDLQGFGKRiMDVSNR-FDELLERIIkEHEEKRKKRKEGGSKDLLDILLDAYEDEN-AEYKITRNHIKAFILDL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 312 VVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVpHRPAENT 391
Cdd:cd20655   237 FIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLV-RESTEGC 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 392 VVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNN----SCDFTGANYSYFPFGSGRRICAGVALAERMVLYT 467
Cdd:cd20655   316 KINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSrsgqELDVRGQHFKLLPFGSGRRGCPGASLAYQVVGTA 395
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1032284286 468 LATLLHSFDWKIPEGHVLDLKEKFGIVLKLKIPLVALP 505
Cdd:cd20655   396 IAAMVQCFDWKVGDGEKVNMEEASGLTLPRAHPLKCVP 433
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
74-508 2.37e-138

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: 407.00  E-value: 2.37e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDS 153
Cdd:cd20654     1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMGYNYAMFGFAPYGPYWRELRKIATLELLSNRRLEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 154 FYELRRKEVRERTRYLYEQGRKQSPVKVG-----DQLF-LTMMNLTMNMLWG---GSVKAEEMESVGTEFKGVISEITRL 224
Cdd:cd20654    81 LKHVRVSEVDTSIKELYSLWSNNKKGGGGvlvemKQWFaDLTFNVILRMVVGkryFGGTAVEDDEEAERYKKAIREFMRL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 225 LSEPNVSDFFPWLARFDLQGLVKRMGVCARELDAVLDRAIE---QMKPLRGRDDDEVKDFLQ-YLMKLKDQEGDSEVPIT 300
Cdd:cd20654   161 AGTFVVSDAIPFLGWLDFGGHEKAMKRTAKELDSILEEWLEehrQKRSSSGKSKNDEDDDDVmMLSILEDSQISGYDADT 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 301 InhVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLP 380
Cdd:cd20654   241 V--IKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYPPGP 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 381 LLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNS-CDFTGANYSYFPFGSGRRICAGVAL 459
Cdd:cd20654   319 LLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHKdIDVRGQNFELIPFGSGRRSCPGVSF 398
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1032284286 460 AERMVLYTLATLLHSFDWKIPEGHVLDLKEKFGIVLKLKIPLVALPIPR 508
Cdd:cd20654   399 GLQVMHLTLARLLHGFDIKTPSNEPVDMTEGPGLTNPKATPLEVLLTPR 447
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
13-512 5.86e-133

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 394.99  E-value: 5.86e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  13 INLTPYAIVILTTVFSILWYIFKRSPQpsLPPGPRGLPIVGNLPFLDPDLHTYFANLAQSHGPIFKLNLGSKLTIVVNSP 92
Cdd:PLN00110    5 LELAAATLLFFITRFFIRSLLPKPSRK--LPPGPRGWPLLGALPLLGNMPHVALAKMAKRYGPVMFLKMGTNSMVVASTP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  93 SLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYELRRKEVRERTRYLYEQ 172
Cdd:PLN00110   83 EAARAFLKTLDINFSNRPPNAGATHLAYGAQDMVFADYGPRWKLLRKLSNLHMLGGKALEDWSQVRTVELGHMLRAMLEL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 173 GRKQSPVKVGDQLFLTMMNLTMNMLWGGSVkAEEMESVGTEFKGVISEITRLLSEPNVSDFFPWLARFDLQGLVKRMGVC 252
Cdd:PLN00110  163 SQRGEPVVVPEMLTFSMANMIGQVILSRRV-FETKGSESNEFKDMVVELMTTAGYFNIGDFIPSIAWMDIQGIERGMKHL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 253 ARELDAVLDRAIEQMKPlrgrDDDEVK---DFLQYLMKlkDQEGDSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAE 329
Cdd:PLN00110  242 HKKFDKLLTRMIEEHTA----SAHERKgnpDFLDVVMA--NQENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 330 LMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVW 409
Cdd:PLN00110  316 MLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIW 395
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 410 SIQRDPNVWENPTEFRPERFLD--NNSCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEGHVLDL 487
Cdd:PLN00110  396 AIGRDPDVWENPEEFRPERFLSekNAKIDPRGNDFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVELNM 475
                         490       500
                  ....*....|....*....|....*
gi 1032284286 488 KEKFGIVLKLKIPLVALPIPRFSDS 512
Cdd:PLN00110  476 DEAFGLALQKAVPLSAMVTPRLHQS 500
PLN02183 PLN02183
ferulate 5-hydroxylase
2-508 4.90e-125

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 375.34  E-value: 4.90e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286   2 SPISNLFPdntinlTPYAIVILTTVFSILWYIFKRSPQPSLPPGPRGLPIVGNLPFLDPDLHTYFANLAQSHGPIFKLNL 81
Cdd:PLN02183    3 SPLQSLLT------SPSFFLILISLFLFLGLISRLRRRLPYPPGPKGLPIIGNMLMMDQLTHRGLANLAKQYGGLFHMRM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  82 GSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSfYELRRKE 161
Cdd:PLN02183   77 GYLHMVAVSSPEVARQVLQVQDSVFSNRPANIAISYLTYDRADMAFAHYGPFWRQMRKLCVMKLFSRKRAES-WASVRDE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 162 VRERTRYLYEQGRKqsPVKVGDQLFLTMMNLTMNMLWGGSVKAEEmesvgTEFKGVISEITRLLSEPNVSDFFPWLARFD 241
Cdd:PLN02183  156 VDSMVRSVSSNIGK--PVNIGELIFTLTRNITYRAAFGSSSNEGQ-----DEFIKILQEFSKLFGAFNVADFIPWLGWID 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 242 LQGLVKRMgVCARE-----LDAVLDRAIEQMKPLRGRDDDE------VKDFLQ-YLMKLKDQEGD---SEVPITINHVKA 306
Cdd:PLN02183  229 PQGLNKRL-VKARKsldgfIDDIIDDHIQKRKNQNADNDSEeaetdmVDDLLAfYSEEAKVNESDdlqNSIKLTRDNIKA 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 307 LLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVpHR 386
Cdd:PLN02183  308 IIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLL-HE 386
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 387 PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANYSYFPFGSGRRICAGVALAermvLY 466
Cdd:PLN02183  387 TAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVPDFKGSHFEFIPFGSGRRSCPGMQLG----LY 462
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 1032284286 467 TL----ATLLHSFDWKIPEG---HVLDLKEKFGIVLKLKIPLVALPIPR 508
Cdd:PLN02183  463 ALdlavAHLLHCFTWELPDGmkpSELDMNDVFGLTAPRATRLVAVPTYR 511
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
74-501 8.04e-122

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: 363.46  E-value: 8.04e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDS 153
Cdd:cd20653     1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAPYGDHWRNLRRITTLEIFSSHRLNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 154 FYELRRKEVRERTRYLY-EQGRKQSPVKVGDQLFLTMMNLTMNMLWG------GSVKAEEmesvGTEFKGVISEITRLLS 226
Cdd:cd20653    81 FSSIRRDEIRRLLKRLArDSKGGFAKVELKPLFSELTFNNIMRMVAGkryygeDVSDAEE----AKLFRELVSEIFELSG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 227 EPNVSDFFPWLARFDLQGLVKRMGVCARELDAVLDRAIEQMkplRGRDDDEVKDFLQYLMKLKDQEGDSEVPITInhvKA 306
Cdd:cd20653   157 AGNPADFLPILRWFDFQGLEKRVKKLAKRRDAFLQGLIDEH---RKNKESGKNTMIDHLLSLQESQPEYYTDEII---KG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 307 LLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHR 386
Cdd:cd20653   231 LILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVPHE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 387 PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFldNNSCDftgANYSYFPFGSGRRICAGVALAERMVLY 466
Cdd:cd20653   311 SSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF--EGEER---EGYKLIPFGLGRRACPGAGLAQRVVGL 385
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1032284286 467 TLATLLHSFDWKIPEGHVLDLKEKFGIVLKLKIPL 501
Cdd:cd20653   386 ALGSLIQCFEWERVGEEEVDMTEGKGLTMPKAIPL 420
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
21-508 2.54e-115

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 350.28  E-value: 2.54e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  21 VILTTVFSILWYIFKRSPQPSLPPGPRGLPIVGNLPFLDPDLHTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLAREILK 100
Cdd:PLN03112   12 VLIFNVLIWRWLNASMRKSLRLPPGPPRWPIVGNLLQLGPLPHRDLASLCKKYGPLVYLRLGSVDAITTDDPELIREILL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 101 DQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYELRRKEVRERTRYLYEQGRKQSPVK 180
Cdd:PLN03112   92 RQDDVFASRPRTLAAVHLAYGCGDVALAPLGPHWKRMRRICMEHLLTTKRLESFAKHRAEEARHLIQDVWEAAQTGKPVN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 181 VGDQLFLTMMNLTMNMLWG----GSVKAEEMESVgtEFKGVISEITRLLSEPNVSDFFPWLARFDLQGLVKRMGVCAREL 256
Cdd:PLN03112  172 LREVLGAFSMNNVTRMLLGkqyfGAESAGPKEAM--EFMHITHELFRLLGVIYLGDYLPAWRWLDPYGCEKKMREVEKRV 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 257 DAVLDRAIEQMKPLRGRDDDEVK--DFLQYLMKLKDQEGDSEVP-ITInhvKALLTDMVVGGTDTSTNTIEFAMAELMSN 333
Cdd:PLN03112  250 DEFHDKIIDEHRRARSGKLPGGKdmDFVDVLLSLPGENGKEHMDdVEI---KALMQDMIAAATDTSAVTNEWAMAEVIKN 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 334 PELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQR 413
Cdd:PLN03112  327 PRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGR 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 414 DPNVWENPTEFRPERFLDNNSCDFT---GANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEGHV---LDL 487
Cdd:PLN03112  407 NTKIWDDVEEFRPERHWPAEGSRVEishGPDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDGLRpedIDT 486
                         490       500
                  ....*....|....*....|.
gi 1032284286 488 KEKFGIVLKLKIPLVALPIPR 508
Cdd:PLN03112  487 QEVYGMTMPKAKPLRAVATPR 507
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
43-496 8.82e-114

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: 344.65  E-value: 8.82e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  43 PPGPRGLPIVGNLPFLDPD--LHTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVP--LTGRAA 118
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEpwFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 119 TYGGIDIVwTPYGAEWRQLRKICVLKLLSRKTLdSFYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLW 198
Cdd:pfam00067  81 PFLGKGIV-FANGPRWRQLRRFLTPTFTSFGKL-SFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 199 GGSVKAEEMESVgTEFKGVISEITRLLS--EPNVSDFFPWLaRFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDDD 276
Cdd:pfam00067 159 GERFGSLEDPKF-LELVKAVQELSSLLSspSPQLLDLFPIL-KYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 277 EVKDFLQYLMKLKDQEGDSEvpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEE 356
Cdd:pfam00067 237 SPRDFLDALLLAKEEEDGSK--LTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 357 SHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCd 436
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGK- 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032284286 437 fTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKI-PEGHVLDLKEKFGIVLK 496
Cdd:pfam00067 394 -FRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELpPGTDPPDIDETPGLLLP 453
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
73-503 1.59e-106

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: 324.82  E-value: 1.59e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRdvPLTGRAA--TYGGIDIVWTPYGAEWRQLRKICVLKLLSRKT 150
Cdd:cd20656     1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADR--HRTRSAArfSRNGQDLIWADYGPHYVKVRKLCTLELFTPKR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 151 LDSFYELRRKEVRERTRYLYE----QGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEE--MESVGTEFKGVISEITRL 224
Cdd:cd20656    79 LESLRPIREDEVTAMVESIFNdcmsPENEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEgvMDEQGVEFKAIVSNGLKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 225 LSEPNVSDFFPWLAR-FDLQ-GLVKRMGvcARELDavLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDQEGDSEvpitiN 302
Cdd:cd20656   159 GASLTMAEHIPWLRWmFPLSeKAFAKHG--ARRDR--LTKAIMEEHTLARQKSGGGQQHFVALLTLKEQYDLSE-----D 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 303 HVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLL 382
Cdd:cd20656   230 TVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLM 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 383 VPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTGANYSYFPFGSGRRICAGVALAER 462
Cdd:cd20656   310 LPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDV-DIKGHDFRLLPFGAGRRVCPGAQLGIN 388
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1032284286 463 MVLYTLATLLHSFDWKIPEG---HVLDLKEKFGIVLKLKIPLVA 503
Cdd:cd20656   389 LVTLMLGHLLHHFSWTPPEGtppEEIDMTENPGLVTFMRTPLQA 432
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
74-498 1.11e-102

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: 314.54  E-value: 1.11e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRdvPLTGRAATY-GGIDIVwTPYGAEWRQLRKICVLKLLSRKTLD 152
Cdd:cd20617     1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDR--PLLPSFEIIsGGKGIL-FSNGDYWKELRRFALSSLTKTKLKK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 153 SFYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKaEEMESVGTEFKGVISEITRLLSEPNVSD 232
Cdd:cd20617    78 KMEELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFP-DEDDGEFLKLVKPIEEIFKELGSGNPSD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 233 FFPWLARFDLQGLVKRMGVCARELDAVLDRAIEQmkpLRGRDDDEVKDFLQYLMKLKDQEGDSEvPITINHVKALLTDMV 312
Cdd:cd20617   157 FIPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEH---LKTIDPNNPRDLIDDELLLLLKEGDSG-LFDDDSIISTCLDLF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 313 VGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTV 392
Cdd:cd20617   233 LAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 393 VGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScdfTGANYSYFPFGSGRRICAGVALAeRMVLYT-LATL 471
Cdd:cd20617   313 IGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDG---NKLSEQFIPFGIGKRNCVGENLA-RDELFLfFANL 388
                         410       420
                  ....*....|....*....|....*..
gi 1032284286 472 LHSFDWKIPEGHVLDLKEKFGIVLKLK 498
Cdd:cd20617   389 LLNFKFKSSDGLPIDEKEVFGLTLKPK 415
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
73-498 1.06e-93

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: 291.81  E-value: 1.06e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKL-LSRKTL 151
Cdd:cd11027     1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGKDIAFGDYSPTWKLHRKLAHSALrLYASGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 152 DSFYELRRKEVRERTRYLYEQGRKqsPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESvgTEFKGVISEITRLLSEPNVS 231
Cdd:cd11027    81 PRLEEKIAEEAEKLLKRLASQEGQ--PFDPKDELFLAVLNVICSITFGKRYKLDDPEF--LRLLDLNDKFFELLGAGSLL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 232 DFFPWLARFDLQGLvKRMGVCARELDAVLDRAIEQMKplRGRDDDEVKDFLQYLMKLK----DQEGDSEVPITINHVKAL 307
Cdd:cd11027   157 DIFPFLKYFPNKAL-RELKELMKERDEILRKKLEEHK--ETFDPGNIRDLTDALIKAKkeaeDEGDEDSGLLTDDHLVMT 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 308 LTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRP 387
Cdd:cd11027   234 ISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALPHKT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 388 AENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTGANYSYFPFGSGRRICAGVALAERMVLYT 467
Cdd:cd11027   314 TCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENG-KLVPKPESFLPFSAGRRVCLGESLAKAELFLF 392
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1032284286 468 LATLLHSFDWKIPEGHVL-DLKEKFGIVLKLK 498
Cdd:cd11027   393 LARLLQKFRFSPPEGEPPpELEGIPGLVLYPL 424
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
80-508 1.32e-92

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: 289.27  E-value: 1.32e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  80 NLGSKLTIVVNSPSLAREILKDQDINFSNRdvPLTGRAATYGG--IDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYEL 157
Cdd:cd20658     7 RLGNTHVIPVTCPKIAREILRKQDAVFASR--PLTYATEIISGgyKTTVISPYGEQWKKMRKVLTTELMSPKRHQWLHGK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 158 RRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMM---NLTMNMLWGGSVKAEEMESVGTEFKGV-----ISEITRLLSEPN 229
Cdd:cd20658    85 RTEEADNLVAYVYNMCKKSNGGGLVNVRDAARHycgNVIRKLMFGTRYFGKGMEDGGPGLEEVehmdaIFTALKCLYAFS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 230 VSDFFPWLARFDLQGLVKRMGVCARELDAVLDRAI-EQMKPLRGRDDDEVKDFLQYLMKLKDQEGDSEVpiTINHVKALL 308
Cdd:cd20658   165 ISDYLPFLRGLDLDGHEKIVREAMRIIRKYHDPIIdERIKQWREGKKKEEEDWLDVFITLKDENGNPLL--TPDEIKAQI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 309 TDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPA 388
Cdd:cd20658   243 KELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNVPHVAM 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 389 ENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSC-DFTGANYSYFPFGSGRRICAGVALAERMVLYT 467
Cdd:cd20658   323 SDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEvTLTEPDLRFISFSTGRRGCPGVKLGTAMTVML 402
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1032284286 468 LATLLHSFDWKIPEG-HVLDLKEKFGIVLKLKiPLVALPIPR 508
Cdd:cd20658   403 LARLLQGFTWTLPPNvSSVDLSESKDDLFMAK-PLVLVAKPR 443
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
73-501 2.37e-92

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: 288.37  E-value: 2.37e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNR--DVPLTGRAATyGGIDIVWTPYGAEWRQLRKICVLKLLSRKT 150
Cdd:cd11075     2 YGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRppANPLRVLFSS-NKHMVNSSPYGPLWRTLRRNLVSEVLSPSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 151 LDSFYELRRKEVRERTRYLY-EQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTefkgVISEITRLLSEPN 229
Cdd:cd11075    81 LKQFRPARRRALDNLVERLReEAKENPGPVNVRDHFRHALFSLLLYMCFGERLDEETVRELER----VQRELLLSFTDFD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 230 VSDFFPWLARFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDD---DEVKDFLQYLMKLKDQEGDSEVpiTINHVKA 306
Cdd:cd11075   157 VRDFFPALTWLLNRRRWKKVLELRRRQEEVLLPLIRARRKRRASGEadkDYTDFLLLDLLDLKEEGGERKL--TDEELVS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 307 LLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHR 386
Cdd:cd11075   235 LCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHFLLPHA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 387 PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNN--SCDFTGAN-YSYFPFGSGRRICAGVALAERM 463
Cdd:cd11075   315 VTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGeaADIDTGSKeIKMMPFGAGRRICPGLGLATLH 394
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1032284286 464 VLYTLATLLHSFDWKIPEGHVLDLKEKFGIVLKLKIPL 501
Cdd:cd11075   395 LELFVARLVQEFEWKLVEGEEVDFSEKQEFTVVMKNPL 432
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
20-482 2.40e-86

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 275.03  E-value: 2.40e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  20 IVILTTVFSILWYIFKRSPQPS---LPPGPRGLPIVGNLPFLDP-DLHTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLA 95
Cdd:PLN03234    4 FLIIAALVAAAAFFFLRSTTKKslrLPPGPKGLPIIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  96 REILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYELRRKEVRERTRYLYEQGRK 175
Cdd:PLN03234   84 KELLKTQDLNFTARPLLKGQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 176 QSPVKVgDQLFLTMMNLTMNMLWGGsvkaEEMESVGTEFK---GVISEITRLLSEPNVSDFFPWLARFD-LQGLVKRMGV 251
Cdd:PLN03234  164 SGTVDL-SELLLSFTNCVVCRQAFG----KRYNEYGTEMKrfiDILYETQALLGTLFFSDLFPYFGFLDnLTGLSARLKK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 252 CARELDAVLDRAI-EQMKPlrGRDDDEVKDFLQYLMKL-KDQEgdSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAE 329
Cdd:PLN03234  239 AFKELDTYLQELLdETLDP--NRPKQETESFIDLLMQIyKDQP--FSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 330 LMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVW 409
Cdd:PLN03234  315 LIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAW 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032284286 410 SIQRDPNVW-ENPTEFRPERFL-DNNSCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEG 482
Cdd:PLN03234  395 AVSRDTAAWgDNPNEFIPERFMkEHKGVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKG 469
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
18-492 3.04e-85

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 271.99  E-value: 3.04e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  18 YAIVILTTVFSILwyifkRSPQPSLPPGPRGLPIVGNLPFLDPDL-HTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLAR 96
Cdd:PLN02394   12 FVAIVLALLVSKL-----RGKKLKLPPGPAAVPIFGNWLQVGDDLnHRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  97 EILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYELRRKEVRERTRYLYEQGR-K 175
Cdd:PLN02394   87 EVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGDHWRKMRRIMTVPFFTNKVVQQYRYGWEEEADLVVEDVRANPEaA 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 176 QSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEmESVGTEFKGVISEITRLL--SEPNVSDFFPWLARFdLQGLVKR-MGVC 252
Cdd:PLN02394  167 TEGVVIRRRLQLMMYNIMYRMMFDRRFESED-DPLFLKLKALNGERSRLAqsFEYNYGDFIPILRPF-LRGYLKIcQDVK 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 253 ARELDAVLDRAIEQMKPL---RGRDDDEVKDFLQYLMKlKDQEGDsevpITINHVKALLTDMVVGGTDTSTNTIEFAMAE 329
Cdd:PLN02394  245 ERRLALFKDYFVDERKKLmsaKGMDKEGLKCAIDHILE-AQKKGE----INEDNVLYIVENINVAAIETTLWSIEWGIAE 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 330 LMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVW 409
Cdd:PLN02394  320 LVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGYDIPAESKILVNAW 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 410 SIQRDPNVWENPTEFRPERFLDNNS-CDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEG-HVLDL 487
Cdd:PLN02394  400 WLANNPELWKNPEEFRPERFLEEEAkVEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPPPGqSKIDV 479

                  ....*
gi 1032284286 488 KEKFG 492
Cdd:PLN02394  480 SEKGG 484
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
79-501 1.69e-82

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: 262.65  E-value: 1.69e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  79 LNLGSKLTIVVNSPSLAREILKDQdiNFSNRDVP------LTGRAatyggidIVWTPYGAEWRQLRKICVLKLLSRKTLD 152
Cdd:cd11076     8 FSLGETRVVITSHPETAREILNSP--AFADRPVKesayelMFNRA-------IGFAPYGEYWRNLRRIASNHLFSPRRIA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 153 SFYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTEFKGVISEITRLLSEPNVSD 232
Cdd:cd11076    79 ASEPQRQAIAAQMVKAIAKEMERSGEVAVRKHLQRASLNNIMGSVFGRRYDFEAGNEEAEELGEMVREGYELLGAFNWSD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 233 FFPWLARFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDQEGDSEvpitiNHVKALLTDMV 312
Cdd:cd11076   159 HLPWLRWLDLQGIRRRCSALVPRVNTFVGKIIEEHRAKRSNRARDDEDDVDVLLSLQGEEKLSD-----SDMIAVLWEMI 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 313 VGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPA-ENT 391
Cdd:cd11076   234 FRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGPLLSWARLAiHDV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 392 VVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDN---NSCDFTGANYSYFPFGSGRRICAGVALAERMVLYTL 468
Cdd:cd11076   314 TVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAeggADVSVLGSDLRLAPFGAGRRVCPGKALGLATVHLWV 393
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1032284286 469 ATLLHSFDWKIPEGHVLDLKEKFGIVLKLKIPL 501
Cdd:cd11076   394 AQLLHEFEWLPDDAKPVDLSEVLKLSCEMKNPL 426
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
74-478 2.06e-79

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: 254.42  E-value: 2.06e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNR-DVPLTGRAATYGGIdIVWTPYGAEWRQLRKICVlKLLSRKTLD 152
Cdd:cd11065     2 GPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRpRMPMAGELMGWGMR-LLLMPYGPRWRLHRRLFH-QLLNPSAVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 153 SFYELRRKEVRertRYLYEQGRkqSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVgTEFKGVISEITRLLSePNVS- 231
Cdd:cd11065    80 KYRPLQELESK---QLLRDLLE--SPDDFLDHIRRYAASIILRLAYGYRVPSYDDPLL-RDAEEAMEGFSEAGS-PGAYl 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 232 -DFFPWLA---RFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDDDE---VKDFLQylmklkdqEGDSEVPITINHV 304
Cdd:cd11065   153 vDFFPFLRylpSWLGAPWKRKARELRELTRRLYEGPFEAAKERMASGTATpsfVKDLLE--------ELDKEGGLSEEEI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 305 KALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVP 384
Cdd:cd11065   225 KYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIP 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 385 HRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANYSYFPFGSGRRICAGVALAERMV 464
Cdd:cd11065   305 HALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPDPPHFAFGFGRRICPGRHLAENSL 384
                         410
                  ....*....|....
gi 1032284286 465 LYTLATLLHSFDWK 478
Cdd:cd11065   385 FIAIARLLWAFDIK 398
PLN02966 PLN02966
cytochrome P450 83A1
19-482 3.90e-78

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 253.52  E-value: 3.90e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  19 AIVILTTVFSILWYIFKRSPQPSLPPGPRGLPIVGNLPFLDP-DLHTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLARE 97
Cdd:PLN02966    7 GVVALAAVLLFFLYQKPKTKRYKLPPGPSPLPVIGNLLQLQKlNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  98 ILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYELRRKEVRERTRYLYEQGRKQS 177
Cdd:PLN02966   87 LLKTQDVNFADRPPHRGHEFISYGRRDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAADKSE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 178 PVKVgDQLFLTMMNLTMNMLWGGSVKAEEMESVgTEFKGVISEITRLLSEPNVSDFFPWLARFD-LQGLVKRMGVCAREL 256
Cdd:PLN02966  167 VVDI-SELMLTFTNSVVCRQAFGKKYNEDGEEM-KRFIKILYGTQSVLGKIFFSDFFPYCGFLDdLSGLTAYMKECFERQ 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 257 DAVLDRAI-EQMKPLRGRDddEVKDFLQYLMKL-KDQEGDSEvpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNP 334
Cdd:PLN02966  245 DTYIQEVVnETLDPKRVKP--ETESMIDLLMEIyKEQPFASE--FTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 335 ELIKRAQEELDEVVGKD--NIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQ 412
Cdd:PLN02966  321 QVLKKAQAEVREYMKEKgsTFVTEDDVKNLPYFRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVS 400
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032284286 413 RDPNVW-ENPTEFRPERFLDnNSCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEG 482
Cdd:PLN02966  401 RDEKEWgPNPDEFRPERFLE-KEVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNG 470
PLN02971 PLN02971
tryptophan N-hydroxylase
1-481 6.27e-71

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 235.70  E-value: 6.27e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286   1 MSPISNLFPDNTINLTpYAIVILTTVFSILWYIFKRSPQPsLPPGPRGLPIVGNLPFL---DPDLHTYFANLAQSHGPIF 77
Cdd:PLN02971   19 TSSFTNMYLLTTLQAL-VAITLLMILKKLKSSSRNKKLHP-LPPGPTGFPIVGMIPAMlknRPVFRWLHSLMKELNTEIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  78 KLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYEL 157
Cdd:PLN02971   97 CVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDN 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 158 RRKEVRERTRYLYEQGRKQSPVkvgDQLFLTMM---NLTMNMLWGGSVKAEEMESVG------TEFKGVISEITRLLSEP 228
Cdd:PLN02971  177 RAEETDHLTAWLYNMVKNSEPV---DLRFVTRHycgNAIKRLMFGTRTFSEKTEPDGgptledIEHMDAMFEGLGFTFAF 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 229 NVSDFFPWLARFDLQGLVKRMgvcaRELDAVLDR-----AIEQMKPLRGRDDDEVKDFLQYLMKLKDQEGDSEvpITINH 303
Cdd:PLN02971  254 CISDYLPMLTGLDLNGHEKIM----RESSAIMDKyhdpiIDERIKMWREGKRTQIEDFLDIFISIKDEAGQPL--LTADE 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 304 VKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLV 383
Cdd:PLN02971  328 IKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNL 407
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 384 PHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNS-CDFTGANYSYFPFGSGRRICAGVALAER 462
Cdd:PLN02971  408 PHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSeVTLTENDLRFISFSTGKRGCAAPALGTA 487
                         490
                  ....*....|....*....
gi 1032284286 463 MVLYTLATLLHSFDWKIPE 481
Cdd:PLN02971  488 ITTMMLARLLQGFKWKLAG 506
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
73-498 1.05e-70

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: 232.21  E-value: 1.05e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKicvlklLSRKTLD 152
Cdd:cd20673     1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRNGKDIAFADYSATWQLHRK------LVHSAFA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 153 SFYE----LRRKEVRERTRYLYEQGRKQ-SPVKVGDQLFLTMMNLTMNMLWGGSVKAE--EMESVGTEFKGviseITRLL 225
Cdd:cd20673    75 LFGEgsqkLEKIICQEASSLCDTLATHNgESIDLSPPLFRAVTNVICLLCFNSSYKNGdpELETILNYNEG----IVDTV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 226 SEPNVSDFFPWLARFDLQGLvKRMGVCARELDAVLDRAIEQMKplRGRDDDEVKDFLQYLMKLK-------DQEGDSEVP 298
Cdd:cd20673   151 AKDSLVDIFPWLQIFPNKDL-EKLKQCVKIRDKLLQKKLEEHK--EKFSSDSIRDLLDALLQAKmnaennnAGPDQDSVG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 299 ITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPT 378
Cdd:cd20673   228 LSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPV 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 379 LPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANYSYFPFGSGRRICAGVA 458
Cdd:cd20673   308 APLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQLISPSLSYLPFGAGPRVCLGEA 387
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1032284286 459 LAeRMVLYT-LATLLHSFDWKIPEGHVL-DLKEKFGIVLKLK 498
Cdd:cd20673   388 LA-RQELFLfMAWLLQRFDLEVPDGGQLpSLEGKFGVVLQID 428
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
74-495 1.09e-68

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: 225.47  E-value: 1.09e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGgiDIVWTPYGAEWRQLRKIcVLKLLSRKTLDS 153
Cdd:cd00302     1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLG--DGLLTLDGPEHRRLRRL-LAPAFTPRALAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 154 FYELRRKEVRERTRYLyeQGRKQSPVKVGDQLFLTMMNLTMNMLWGgsvkaEEMESVGTEFKGVISEITRLLSEPNVSDF 233
Cdd:cd00302    78 LRPVIREIARELLDRL--AAGGEVGDDVADLAQPLALDVIARLLGG-----PDLGEDLEELAELLEALLKLLGPRLLRPL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 234 FPWLARfdlqglvkRMGVCARELDAVLDRAIEQMKPLRGRDDDevkdflqYLMKLKDQEGDsevPITINHVKALLTDMVV 313
Cdd:cd00302   151 PSPRLR--------RLRRARARLRDYLEELIARRRAEPADDLD-------LLLLADADDGG---GLSDEEIVAELLTLLL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 314 GGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDnivEESHITRLPYILAIMKETLRLHPTLPLLvPHRPAENTVV 393
Cdd:cd00302   213 AGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG---TPEDLSKLPYLEAVVEETLRLYPPVPLL-PRVATEDVEL 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 394 GGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDftgaNYSYFPFGSGRRICAGVALAERMVLYTLATLLH 473
Cdd:cd00302   289 GGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEP----RYAHLPFGAGPHRCLGARLARLELKLALATLLR 364
                         410       420
                  ....*....|....*....|..
gi 1032284286 474 SFDWKIPEGHVLDLKEKFGIVL 495
Cdd:cd00302   365 RFDFELVPDEELEWRPSLGTLG 386
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
74-498 1.20e-66

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: 221.13  E-value: 1.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKIC--VLKLLSRKTL 151
Cdd:cd20674     2 GPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTGKLVSQGGQDLSLGDYSLLWKAHRKLTrsALQLGIRNSL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 152 DSFYELRRKEVRERTRYLYEqgrkqSPVKVGDQLFLTMMNLTMNMLWGgsvKAEEMESVGTEFKGVISEITRLLSEPNVS 231
Cdd:cd20674    82 EPVVEQLTQELCERMRAQAG-----TPVDIQEEFSLLTCSIICCLTFG---DKEDKDTLVQAFHDCVQELLKTWGHWSIQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 232 --DFFPWLARFDLQGLvKRMGVCARELDAVLDRAIEQMKplRGRDDDEVKDFLQYLMK-LKDQEGDSE-VPITINHVKAL 307
Cdd:cd20674   154 alDSIPFLRFFPNPGL-RRLKQAVENRDHIVESQLRQHK--ESLVAGQWRDMTDYMLQgLGQPRGEKGmGQLLEGHVHMA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 308 LTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRP 387
Cdd:cd20674   231 VVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRT 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 388 AENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNnscdfTGANYSYFPFGSGRRICAGVALAERMVLYT 467
Cdd:cd20674   311 TRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEP-----GAANRALLPFGCGARVCLGEPLARLELFVF 385
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1032284286 468 LATLLHSFDWKIPEGHVL-DLKEKFGIVLKLK 498
Cdd:cd20674   386 LARLLQAFTLLPPSDGALpSLQPVAGINLKVQ 417
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
73-498 4.04e-65

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: 217.17  E-value: 4.04e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATyGGIDIVWTPYGAEWRQLRKIC---VLKLLSRK 149
Cdd:cd11028     1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFIS-NGKSMAFSDYGPRWKLHRKLAqnaLRTFSNAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 150 TLDSFYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVgtEFKGVISEITRLLSEPN 229
Cdd:cd11028    80 THNPLEEHVTEEAEELVTELTENNGKPGPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFL--ELVKSNDDFGAFVGAGN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 230 VSDFFPWLaRFDLQGLVKRMGVCARELDAVLDRAI-EQMKPLrgrDDDEVKDFLQYLMKL---KDQEGDSEVPITINHVK 305
Cdd:cd11028   158 PVDVMPWL-RYLTRRKLQKFKELLNRLNSFILKKVkEHLDTY---DKGHIRDITDALIKAseeKPEEEKPEVGLTDEHII 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 306 ALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPH 385
Cdd:cd11028   234 STVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPFTIPH 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 386 RPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLD-NNSCDFTGANySYFPFGSGRRICAGVALAERMV 464
Cdd:cd11028   314 ATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDdNGLLDKTKVD-KFLPFGAGRRRCLGEELARMEL 392
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1032284286 465 LYTLATLLHSFDWKIPEGHVLDLKEKFGIVLKLK 498
Cdd:cd11028   393 FLFFATLLQQCEFSVKPGEKLDLTPIYGLTMKPK 426
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
71-492 3.49e-64

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: 215.03  E-value: 3.49e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  71 QSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKT 150
Cdd:cd11074     1 KKFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGEHWRKMRRIMTVPFFTNKV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 151 LDSFyelrRKEVRERTRYLYEQGRKQSPVKVG-----DQLFLTMMNLTMNMLWGGSVKAEEmESVGTEFKGVISEITRLL 225
Cdd:cd11074    81 VQQY----RYGWEEEAARVVEDVKKNPEAATEgivirRRLQLMMYNNMYRIMFDRRFESED-DPLFVKLKALNGERSRLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 226 S--EPNVSDFFPWLARFdLQGLVKrmgVCA----RELDAVLDRAIEQMKPL---RGRDDDEVKDFLQYLMKLKdQEGDse 296
Cdd:cd11074   156 QsfEYNYGDFIPILRPF-LRGYLK---ICKevkeRRLQLFKDYFVDERKKLgstKSTKNEGLKCAIDHILDAQ-KKGE-- 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 297 vpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLH 376
Cdd:cd11074   229 --INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLR 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 377 PTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNS-CDFTGANYSYFPFGSGRRICA 455
Cdd:cd11074   307 MAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESkVEANGNDFRYLPFGVGRRSCP 386
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1032284286 456 GVALAERMVLYTLATLLHSFDWKIPEGHV-LDLKEKFG 492
Cdd:cd11074   387 GIILALPILGITIGRLVQNFELLPPPGQSkIDTSEKGG 424
PLN02655 PLN02655
ent-kaurene oxidase
40-482 1.96e-63

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 213.84  E-value: 1.96e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  40 PSLPpgprGLPIVGNLPFL-DPDLHTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAA 118
Cdd:PLN02655    2 PAVP----GLPVIGNLLQLkEKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 119 TYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYELRRKEVRERTRYLYEQGRK--QSPVKVGDQLFLTMMNLTMNM 196
Cdd:PLN02655   78 TRDKSMVATSDYGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSGLHALVKDdpHSPVNFRDVFENELFGLSLIQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 197 LWGGSVKAEEMESVGTE------FKGVISEITRLLSEPNVSDFFP---WLARFDLQGLVKRMgvcARELDAVLDRAIEQM 267
Cdd:PLN02655  158 ALGEDVESVYVEELGTEiskeeiFDVLVHDMMMCAIEVDWRDFFPylsWIPNKSFETRVQTT---EFRRTAVMKALIKQQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 268 KP--LRGRDDDEVKDFLQylmklkdqegDSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELD 345
Cdd:PLN02655  235 KKriARGEERDCYLDFLL----------SEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIR 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 346 EVVGkDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFR 425
Cdd:PLN02655  305 EVCG-DERVTEEDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWD 383
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1032284286 426 PERFLDNNscdFTGAN-YSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEG 482
Cdd:PLN02655  384 PERFLGEK---YESADmYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLREG 438
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
74-495 9.43e-63

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: 210.92  E-value: 9.43e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDinFSNRDVPLTGRAATYGG-IDIVWTPyGAEWRQLRKICVLKL----LSR 148
Cdd:cd20651     1 GDVVGLKLGKDKVVVVSGYEAVREVLSREE--FDGRPDGFFFRLRTFGKrLGITFTD-GPFWKEQRRFVLRHLrdfgFGR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 149 KTLDsfyelrrKEVRERTRYLYEQGRKQS--PVKVGDQLFLTMMNLTMNMLwGGSVKAEEMESVGtefkgVISEITRLLS 226
Cdd:cd20651    78 RSME-------EVIQEEAEELIDLLKKGEkgPIQMPDLFNVSVLNVLWAMV-AGERYSLEDQKLR-----KLLELVHLLF 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 227 E-----PNVSDFFPWLaRF---DLQGlVKRMGVCARELDAVLDRAIEqmKPLRGRDDDEVKDFL-QYLMKLKDQEGDSEV 297
Cdd:cd20651   145 RnfdmsGGLLNQFPWL-RFiapEFSG-YNLLVELNQKLIEFLKEEIK--EHKKTYDEDNPRDLIdAYLREMKKKEPPSSS 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 298 pITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHP 377
Cdd:cd20651   221 -FTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFT 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 378 TLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTGANYSYfPFGSGRRICAGV 457
Cdd:cd20651   300 LVPIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDG-KLLKDEWFL-PFGAGKRRCLGE 377
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1032284286 458 ALAeRMVLYT-LATLLHSFDWKIPEGHVLDL-KEKFGIVL 495
Cdd:cd20651   378 SLA-RNELFLfFTGLLQNFTFSPPNGSLPDLeGIPGGITL 416
PLN00168 PLN00168
Cytochrome P450; Provisional
10-511 4.48e-61

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 209.04  E-value: 4.48e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  10 DNTINLTPYAIVILTTVFSILWYIFKRSPQPS--LPPGPRGLPIVGNLPFLD---PDLHTYFANLAQSHGPIFKLNLGSK 84
Cdd:PLN00168    2 DATQLLLLAALLLLPLLLLLLGKHGGRGGKKGrrLPPGPPAVPLLGSLVWLTnssADVEPLLRRLIARYGPVVSLRVGSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  85 LTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKLLSRKTLDSFYELRRKEVRE 164
Cdd:PLN00168   82 LSVFVADRRLAHAALVERGAALADRPAVASSRLLGESDNTITRSSYGPVWRLLRRNLVAETLHPSRVRLFAPARAWVRRV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 165 RTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTEFKGVISEITRLLSepnVSDFFPWLARFDLQG 244
Cdd:PLN00168  162 LVDKLRREAEDAAAPRVVETFQYAMFCLLVLMCFGERLDEPAVRAIAAAQRDWLLYVSKKMS---VFAFFPAVTKHLFRG 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 245 LVKRMGVCAR---ELDAVLDRAIEQMKPLRGRDDDEVKD-------FLQYLMKLKDQEgDSEVPITINHVKALLTDMVVG 314
Cdd:PLN00168  239 RLQKALALRRrqkELFVPLIDARREYKNHLGQGGEPPKKettfehsYVDTLLDIRLPE-DGDRALTDDEIVNLCSEFLNA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 315 GTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVG-KDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVV 393
Cdd:PLN00168  318 GTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGdDQEEVSEEDVHKMPYLKAVVLEGLRKHPPAHFVLPHKAAEDMEV 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 394 GGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFL---DNNSCDFTGAN-YSYFPFGSGRRICAGVALAERMVLYTLA 469
Cdd:PLN00168  398 GGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLaggDGEGVDVTGSReIRMMPFGVGRRICAGLGIAMLHLEYFVA 477
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1032284286 470 TLLHSFDWKIPEGHVLDLKEKFGIVLKLKIPLVALPIPRFSD 511
Cdd:PLN00168  478 NMVREFEWKEVPGDEVDFAEKREFTTVMAKPLRARLVPRRTT 519
PLN03018 PLN03018
homomethionine N-hydroxylase
19-515 1.88e-59

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 205.25  E-value: 1.88e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  19 AIVILTTVFSILWYIFKRSPQpsLPPGPRGLPIVGNLPFL---DPDLHTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLA 95
Cdd:PLN03018   20 SITLLGRILSRPSKTKDRSRQ--LPPGPPGWPILGNLPELimtRPRSKYFHLAMKELKTDIACFNFAGTHTITINSDEIA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  96 REILKDQDINFSNRD----VPLTGRAATYGGIdivwTPYGAEWRQLRKICVLKLLSRKTLDSFYELRRKEVRERTRYLYE 171
Cdd:PLN03018   98 REAFRERDADLADRPqlsiMETIGDNYKSMGT----SPYGEQFMKMKKVITTEIMSVKTLNMLEAARTIEADNLIAYIHS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 172 QGRKQSPVKVGDQLFLTMMNLTMNMLWGGS-VKAEEMES----VGTEFKGVISEITRLLS-EPNVS--DFFP-WLARFDL 242
Cdd:PLN03018  174 MYQRSETVDVRELSRVYGYAVTMRMLFGRRhVTKENVFSddgrLGKAEKHHLEVIFNTLNcLPGFSpvDYVErWLRGWNI 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 243 QGLVKRMGVCAREL----DAVLDRAIEQMKPLRGRDddEVKDFLQYLMKLKDQEGDSEVpiTINHVKALLTDMVVGGTDT 318
Cdd:PLN03018  254 DGQEERAKVNVNLVrsynNPIIDERVELWREKGGKA--AVEDWLDTFITLKDQNGKYLV--TPDEIKAQCVEFCIAAIDN 329
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 319 STNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTI 398
Cdd:PLN03018  330 PANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFI 409
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 399 PKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNN----SCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHS 474
Cdd:PLN03018  410 PKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDgitkEVTLVETEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQG 489
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1032284286 475 FDWKIPEGH-VLDLKEKFGIVLKLKiPLVALPIPRFSdSNLY 515
Cdd:PLN03018  490 FNWKLHQDFgPLSLEEDDASLLMAK-PLLLSVEPRLA-PNLY 529
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
73-495 2.21e-58

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: 199.62  E-value: 2.21e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNR-DVPLTGRAATYGGIdiVWTPYGAEWRQLRKicvlklLSRKTL 151
Cdd:cd20666     1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRpSVPLVTILTKGKGI--VFAPYGPVWRQQRK------FSHSTL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 152 DSF---YELRRKEVRERTRYLYEQGRK--QSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEmesvgTEFKGVISEITRLL- 225
Cdd:cd20666    73 RHFglgKLSLEPKIIEEFRYVKAEMLKhgGDPFNPFPIVNNAVSNVICSMSFGRRFDYQD-----VEFKTMLGLMSRGLe 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 226 ----SEPNVSDFFPWLARFDLqGLVKRMGVCARELDAVLDRAIEQMKplRGRDDDEVKDFLQ-YLMKLKD-QEGDSEVPI 299
Cdd:cd20666   148 isvnSAAILVNICPWLYYLPF-GPFRELRQIEKDITAFLKKIIADHR--ETLDPANPRDFIDmYLLHIEEeQKNNAESSF 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 300 TINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTL 379
Cdd:cd20666   225 NEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVV 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 380 PLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTgaNYSYFPFGSGRRICAGVAL 459
Cdd:cd20666   305 PLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIK--KEAFIPFGIGRRVCMGEQL 382
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1032284286 460 AeRMVLYTL-ATLLHSFDWKIPEGHVL-DLKEKFGIVL 495
Cdd:cd20666   383 A-KMELFLMfVSLMQSFTFLLPPNAPKpSMEGRFGLTL 419
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
73-491 9.58e-58

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: 197.78  E-value: 9.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRD-VPLTGRAATYGGIDIvwtPYGAEWRQLRKICVLkllsrkTL 151
Cdd:cd11026     1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPpVPLFDRVTKGYGVVF---SNGERWKQLRRFSLT------TL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 152 DSFyELRRKEVRER----TRYLYE--QGRKQSPVkvgDQLFLTM---MNLTMNMLWGgsvkaEEMESVGTEFKGV---IS 219
Cdd:cd11026    72 RNF-GMGKRSIEERiqeeAKFLVEafRKTKGKPF---DPTFLLSnavSNVICSIVFG-----SRFDYEDKEFLKLldlIN 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 220 EITRLLSEP--NVSDFFPWLARFdLQGLVKRMGVCARELDAVLDRAIEQMKPLRgrDDDEVKDFLQ-YLMKLKDQEGDSE 296
Cdd:cd11026   143 ENLRLLSSPwgQLYNMFPPLLKH-LPGPHQKLFRNVEEIKSFIRELVEEHRETL--DPSSPRDFIDcFLLKMEKEKDNPN 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 297 VPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLH 376
Cdd:cd11026   220 SEFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFG 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 377 PTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCdFTgANYSYFPFGSGRRICAG 456
Cdd:cd11026   300 DIVPLGVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGK-FK-KNEAFMPFSAGKRVCLG 377
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1032284286 457 VALAeRMVLYT-LATLLHSFDWKIPEGHV-LDLKEKF 491
Cdd:cd11026   378 EGLA-RMELFLfFTSLLQRFSLSSPVGPKdPDLTPRF 413
PTZ00404 PTZ00404
cytochrome P450; Provisional
26-496 1.42e-53

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 188.01  E-value: 1.42e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  26 VFSILWYI-------FKRSPQPSLPpGPRGLPIVGNLPFLDPDLHTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLAREI 98
Cdd:PTZ00404    8 LFLFIFYIihnaykkYKKIHKNELK-GPIPIPILGNLHQLGNLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  99 LKDQDINFSNR-DVPLTGRAATYGGIDivwTPYGAEWRQLRKIcVLKLLSRKTLDSFYELRRKEVRErtryLYEQGRK-Q 176
Cdd:PTZ00404   87 FVDNFDNFSDRpKIPSIKHGTFYHGIV---TSSGEYWKRNREI-VGKAMRKTNLKHIYDLLDDQVDV----LIESMKKiE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 177 SPVKVGD-QLFLT--MMNLTMNMLWGGSVKAEEMESVG--TEFKGVISEITRLLSEPNVSDFFPWLARFDLQGLVKRMGV 251
Cdd:PTZ00404  159 SSGETFEpRYYLTkfTMSAMFKYIFNEDISFDEDIHNGklAELMGPMEQVFKDLGSGSLFDVIEITQPLYYQYLEHTDKN 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 252 CARELDAVLDRAIEQMKPLrgrDDDEVKDFLQYLMKLKDQEGDSEVPitinHVKALLTDMVVGGTDTSTNTIEFAMAELM 331
Cdd:PTZ00404  239 FKKIKKFIKEKYHEHLKTI---DPEVPRDLLDLLIKEYGTNTDDDIL----SILATILDFFLAGVDTSATSLEWMVLMLC 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 332 SNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVG-GYTIPKDTKIFVNVWS 410
Cdd:PTZ00404  312 NYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFGLPRSTSNDIIIGgGHFIPKDAQILINYYS 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 411 IQRDPNVWENPTEFRPERFLDNNScdftgaNYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEGHVLDLKEK 490
Cdd:PTZ00404  392 LGRNEKYFENPEQFDPSRFLNPDS------NDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGKKIDETEE 465

                  ....*.
gi 1032284286 491 FGIVLK 496
Cdd:PTZ00404  466 YGLTLK 471
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
74-484 4.85e-53

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: 184.70  E-value: 4.85e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSnRDVPLTGRAATYGGiDIVwTPYGAEWRQLRKIcVLKLLSRKTLDS 153
Cdd:cd20620     1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYV-KGGVYERLKLLLGN-GLL-TSEGDLWRRQRRL-AQPAFHRRRIAA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 154 FYELRRKEVRERTRYLyEQGRKQSPVKVGDQlfltMMNLTMNM----LWGGSVKaEEMESVGTEFKGVISEIT-RLLSEP 228
Cdd:cd20620    77 YADAMVEATAALLDRW-EAGARRGPVDVHAE----MMRLTLRIvaktLFGTDVE-GEADEIGDALDVALEYAArRMLSPF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 229 NVSDFFPWLARFDLQGLVKRmgvcareLDAVLDRAIEQmkplRGRDDDEVKDFLQYLMKLKDqEGDSEvPITINHVK-AL 307
Cdd:cd20620   151 LLPLWLPTPANRRFRRARRR-------LDEVIYRLIAE----RRAAPADGGDLLSMLLAARD-EETGE-PMSDQQLRdEV 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 308 LTdMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGkDNIVEESHITRLPYILAIMKETLRLHPTLPLlVPHRP 387
Cdd:cd20620   218 MT-LFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLRLYPPAWI-IGREA 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 388 AENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDftGANYSYFPFGSGRRICAG--VALAErMVL 465
Cdd:cd20620   295 VEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAA--RPRYAYFPFGGGPRICIGnhFAMME-AVL 371
                         410
                  ....*....|....*....
gi 1032284286 466 yTLATLLHSFDWKIPEGHV 484
Cdd:cd20620   372 -LLATIAQRFRLRLVPGQP 389
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
74-495 2.55e-52

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: 183.38  E-value: 2.55e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILkdqdinfsNRDVpLTGRAATY-------GGIDIVWTpyGAEWRQLRKICVLKLL 146
Cdd:cd20652     1 GSIFSLKMGSVYTVVLSDPKLIRDTF--------RRDE-FTGRAPLYlthgimgGNGIICAE--GDLWRDQRRFVHDWLR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 147 S-----RKTLDSFYELR-RKEVRERTRYLyeQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEmesvGT--EFKGVI 218
Cdd:cd20652    70 QfgmtkFGNGRAKMEKRiATGVHELIKHL--KAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDD----PTwrWLRFLQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 219 SEITRLLSEPNVSDFFPWLARF-----DLQGLVKRMGVCARELDAVLDRAIEQMKPlrGRDDDEVKDFLQYLMKLKDQEG 293
Cdd:cd20652   144 EEGTKLIGVAGPVNFLPFLRHLpsykkAIEFLVQGQAKTHAIYQKIIDEHKRRLKP--ENPRDAEDFELCELEKAKKEGE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 294 DSEVPITINHVKAL---LTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMK 370
Cdd:cd20652   222 DRDLFDGFYTDEQLhhlLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACIS 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 371 ETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDnnscdfTGANY----SYFP 446
Cdd:cd20652   302 ESQRIRSVVPLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLD------TDGKYlkpeAFIP 375
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1032284286 447 FGSGRRICAGVALAeRMVLYTLAT-LLHSFDWKIPEGHVLD-LKEKFGIVL 495
Cdd:cd20652   376 FQTGKRMCLGDELA-RMILFLFTArILRKFRIALPDGQPVDsEGGNVGITL 425
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
71-501 7.27e-51

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: 179.26  E-value: 7.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  71 QSHGPIFKLNLGSKLTIVVNSPSLAREILKDQdinfsnrdvpltGRAATYGGIDIvWTPY--------------GAEWRQ 136
Cdd:cd11054     2 KKYGPIVREKLGGRDIVHLFDPDDIEKVFRNE------------GKYPIRPSLEP-LEKYrkkrgkplgllnsnGEEWHR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 137 LRKICVLKLLSRKTLDSFYELRRKEVRERTRYLYEQgRKQSPVKVGDqlfltMMNLTMNmlWGgsvkaeeMESVGT---- 212
Cdd:cd11054    69 LRSAVQKPLLRPKSVASYLPAINEVADDFVERIRRL-RDEDGEEVPD-----LEDELYK--WS-------LESIGTvlfg 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 213 ----EFKGVISEITRLLSEpNVSDFF----------PWLARFDL---QGLVKRMGVCARELDAVLDRAIEQMKPlRGRDD 275
Cdd:cd11054   134 krlgCLDDNPDSDAQKLIE-AVKDIFessaklmfgpPLWKYFPTpawKKFVKAWDTIFDIASKYVDEALEELKK-KDEED 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 276 DEVKDFLQYLMKLKDqegdsevpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVE 355
Cdd:cd11054   212 EEEDSLLEYLLSKPG--------LSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPIT 283
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 356 ESHITRLPYILAIMKETLRLHPTLPLLVphR-PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNS 434
Cdd:cd11054   284 AEDLKKMPYLKACIKESLRLYPVAPGNG--RiLPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDS 361
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032284286 435 CDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEGhvlDLKEKFGIVLKLKIPL 501
Cdd:cd11054   362 ENKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHE---ELKVKTRLILVPDKPL 425
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
61-482 2.10e-49

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: 175.63  E-value: 2.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  61 DLHTYFANlaqsHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDV------PLTGRaatyGGIdivwTPYGAEW 134
Cdd:cd11046     2 DLYKWFLE----YGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDKKGLlaeilePIMGK----GLI----PADGEIW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 135 RQlRKICVLKLLSRKTLDSFYELRRKEVRERTRYLYEQGRKQSPVKVGDQLfltmMNLTMNMLwGGSVKAEEMESVgTEF 214
Cdd:cd11046    70 KK-RRRALVPALHKDYLEMMVRVFGRCSERLMEKLDAAAETGESVDMEEEF----SSLTLDII-GLAVFNYDFGSV-TEE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 215 KGVISEI-TRLLSEPNVSDFFPWL-----ARFDLQGLVKRMGvCARELDAVLDRAIEQMKPLRGRDDDE----------V 278
Cdd:cd11046   143 SPVIKAVyLPLVEAEHRSVWEPPYwdipaALFIVPRQRKFLR-DLKLLNDTLDDLIRKRKEMRQEEDIElqqedylnedD 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 279 KDFLQYLMKLKDQEGDSevpitinhvKALLTD---MVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVE 355
Cdd:cd11046   222 PSLLRFLVDMRDEDVDS---------KQLRDDlmtMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPT 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 356 ESHITRLPYILAIMKETLRLHPTLPLLVpHRPAENTVV--GGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLD-- 431
Cdd:cd11046   293 YEDLKKLKYTRRVLNESLRLYPQPPVLI-RRAVEDDKLpgGGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDpf 371
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032284286 432 NNSCDFTGANYSYFPFGSGRRICAG--VALAERMVlyTLATLLHSFDWKIPEG 482
Cdd:cd11046   372 INPPNEVIDDFAFLPFGGGPRKCLGdqFALLEATV--ALAMLLRRFDFELDVG 422
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
73-486 5.08e-48

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: 171.24  E-value: 5.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNL-GSKLTIVVNsPSLAREIL--KDQDINFSN---RDVPltgraaTYGGIDIVWTPYgAEWRQLRKICvLKLL 146
Cdd:cd11042     5 YGDVFTFNLlGKKVTVLLG-PEANEFFFngKDEDLSAEEvygFLTP------PFGGGVVYYAPF-AEQKEQLKFG-LNIL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 147 SRKTLDSFYELRRKEVRERTRYLYEQGrkqspvkvGDQLFLTMMNLTMNM----LWGGSVKaeemESVGTEFKGVISEIT 222
Cdd:cd11042    76 RRGKLRGYVPLIVEEVEKYFAKWGESG--------EVDLFEEMSELTILTasrcLLGKEVR----ELLDDEFAQLYHDLD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 223 RLLSEPNVsdFFPWLA--RFdlqglvKRMGVCARELDAVLDRAIEQMkplRGRDDDEVKDFLQYLM--KLKDqegdsEVP 298
Cdd:cd11042   144 GGFTPIAF--FFPPLPlpSF------RRRDRARAKLKEIFSEIIQKR---RKSPDKDEDDMLQTLMdaKYKD-----GRP 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 299 ITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDN-IVEESHITRLPYILAIMKETLRLHP 377
Cdd:cd11042   208 LTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDdPLTYDVLKEMPLLHACIKETLRLHP 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 378 TLPLLVphRPAENTV---VGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANYSYFPFGSGRRIC 454
Cdd:cd11042   288 PIHSLM--RKARKPFeveGGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKGGKFAYLPFGAGRHRC 365
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1032284286 455 AGVALAERMVLYTLATLLHSFDWKIPEGHVLD 486
Cdd:cd11042   366 IGENFAYLQIKTILSTLLRNFDFELVDSPFPE 397
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
69-489 2.16e-47

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: 170.06  E-value: 2.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  69 LAQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQdiNFSnRDVPLTGRAATYGGIDIVWTPYGAE--WRQLRKICV---- 142
Cdd:cd11068     8 LADELGPIFKLTLPGRRVVVVSSHDLIAELCDES--RFD-KKVSGPLEELRDFAGDGLFTAYTHEpnWGKAHRILMpafg 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 143 ---LKLLSRKTLDSFYELRRKEVRertrylyeQGRKQsPVKVGDQlfltMMNLTMNM--LWG-----GSVKAEEMESVGT 212
Cdd:cd11068    85 plaMRGYFPMMLDIAEQLVLKWER--------LGPDE-PIDVPDD----MTRLTLDTiaLCGfgyrfNSFYRDEPHPFVE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 213 EFKGVISEITRLLSEPNVSDFFPWLARFDLQGLVKRMGVCARELdaVLDRaieqmkplRGRDDDEVKDFLQYLMKLKDQE 292
Cdd:cd11068   152 AMVRALTEAGRRANRPPILNKLRRRAKRQFREDIALMRDLVDEI--IAER--------RANPDGSPDDLLNLMLNGKDPE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 293 GDSEVPiTINHVKALLTdMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEEsHITRLPYILAIMKET 372
Cdd:cd11068   222 TGEKLS-DENIRYQMIT-FLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPPPYE-QVAKLRYIRRVLDET 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 373 LRLHPTLPLLvPHRPAENTVVGG-YTIPKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFLDNNSCDFtGANySYFPFGSG 450
Cdd:cd11068   299 LRLWPTAPAF-ARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFRKL-PPN-AWKPFGNG 375
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1032284286 451 RRICAGVALAERMVLYTLATLLHSFDWKIPEGHVLDLKE 489
Cdd:cd11068   376 QRACIGRQFALQEATLVLAMLLQRFDFEDDPDYELDIKE 414
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
86-476 6.28e-47

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: 168.87  E-value: 6.28e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  86 TIVVNSPSLAREIL-KDQDiNFSNRDV-------PLTGRAATyggIDivwtpyGAEWRQLRKICVLKLLSRKtLDSFYEL 157
Cdd:cd11056    15 ALLVRDPELIKQILvKDFA-HFHDRGLysdekddPLSANLFS---LD------GEKWKELRQKLTPAFTSGK-LKNMFPL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 158 RRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWG---GSVKAEEmesvgTEFKgvisEITRLLSEPNVSDFF 234
Cdd:cd11056    84 MVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGldaNSLNDPE-----NEFR----EMGRRLFEPSRLRGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 235 PWLARFDLQGLVKRMGVC--ARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDQE----GDSEVPITINHVKALL 308
Cdd:cd11056   155 KFMLLFFFPKLARLLRLKffPKEVEDFFRKLVRDTIEYREKNNIVRNDFIDLLLELKKKGkiedDKSEKELTDEELAAQA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 309 TDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDN--IVEEShITRLPYILAIMKETLRLHPTLPLLvpHR 386
Cdd:cd11056   235 FVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGgeLTYEA-LQEMKYLDQVVNETLRKYPPLPFL--DR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 387 PA-ENTVVGG--YTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTgaNYSYFPFGSGRRICAGVALAERM 463
Cdd:cd11056   312 VCtKDYTLPGtdVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRH--PYTYLPFGDGPRNCIGMRFGLLQ 389
                         410
                  ....*....|...
gi 1032284286 464 VLYTLATLLHSFD 476
Cdd:cd11056   390 VKLGLVHLLSNFR 402
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
56-493 8.83e-47

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 167.76  E-value: 8.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  56 PFLDPDLHTYFANLAQsHGPIFKLNLGSKLTIVVNSPSLAREILKDQDiNFSNRDVPLTGRAATYGGIDIVWTPYGAEWR 135
Cdd:COG2124    15 PAFLRDPYPFYARLRE-YGPVFRVRLPGGGAWLVTRYEDVREVLRDPR-TFSSDGGLPEVLRPLPLLGDSLLTLDGPEHT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 136 QLRKIcVLKLLSRKTLDSFyelrRKEVRERTRYLYEQGRKQSPVKVGDQL-FLTMMNLTMNMLwggSVKAEEMEsvgtEF 214
Cdd:COG2124    93 RLRRL-VQPAFTPRRVAAL----RPRIREIADELLDRLAARGPVDLVEEFaRPLPVIVICELL---GVPEEDRD----RL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 215 KGVISEITRLLsepnvsDFFPWLARfdlqglvKRMGVCARELDAVLDRAIEQmkpLRGRDDDevkDFLQYLMKLKDQEG- 293
Cdd:COG2124   161 RRWSDALLDAL------GPLPPERR-------RRARRARAELDAYLRELIAE---RRAEPGD---DLLSALLAARDDGEr 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 294 --DSEVpitINHVKALLtdmvVGGTDTSTNTIEFAMAELMSNPELIKRAQEELdevvgkdniveeshitrlPYILAIMKE 371
Cdd:COG2124   222 lsDEEL---RDELLLLL----LAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEE 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 372 TLRLHPTLPLLvPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERfldnnscdftgANYSYFPFGSGR 451
Cdd:COG2124   277 TLRLYPPVPLL-PRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-----------PPNAHLPFGGGP 344
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1032284286 452 RICAGVALAeRMVLYT-LATLLHSF-DWKIPEGHVLDLKEKFGI 493
Cdd:COG2124   345 HRCLGAALA-RLEARIaLATLLRRFpDLRLAPPEELRWRPSLTL 387
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
63-490 1.52e-46

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: 167.70  E-value: 1.52e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  63 HTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDinfsnrdvpLTGRAATYGGIdivWTPYG----------- 131
Cdd:cd20613     1 HDLLLEWAKEYGPVFVFWILHRPIVVVSDPEAVKEVLITLN---------LPKPPRVYSRL---AFLFGerflgnglvte 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 132 ---AEWRQLRKIcvlkL---LSRKTLDSF-YELRRK--EVRERTRYLYEqgrKQSPVKVGDQLFLTMMNLTMNMLWG--- 199
Cdd:cd20613    69 vdhEKWKKRRAI----LnpaFHRKYLKNLmDEFNESadLLVEKLSKKAD---GKTEVNMLDEFNRVTLDVIAKVAFGmdl 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 200 GSVKAEE---MESVGTEFKGVISEITRLLSEPNVSDFfpwlarfDLQGLVKRmgvCAREL-----DAVLDRaIEQMKplr 271
Cdd:cd20613   142 NSIEDPDspfPKAISLVLEGIQESFRNPLLKYNPSKR-------KYRREVRE---AIKFLretgrECIEER-LEALK--- 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 272 grDDDEV-KDFLQYLMKLKDQEGDsevpITINHvkaLLTDMV---VGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEV 347
Cdd:cd20613   208 --RGEEVpNDILTHILKASEEEPD----FDMEE---LLDDFVtffIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEV 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 348 VGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVphR-PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRP 426
Cdd:cd20613   279 LGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTS--ReLTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDP 356
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032284286 427 ERFLDNNSCDFTgaNYSYFPFGSGRRICAG--VALAERMVLytLATLLHSFDWKIPEGHVLDLKEK 490
Cdd:cd20613   357 ERFSPEAPEKIP--SYAYFPFSLGPRSCIGqqFAQIEAKVI--LAKLLQNFKFELVPGQSFGILEE 418
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
64-482 2.56e-46

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: 166.99  E-value: 2.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  64 TYFANLAQSHGPIFKLNL-GSKLTIVVNSPSLAREIL----KDQDINFSNRDV-PLTGRAAtyggidiVWTPYGAEWRQL 137
Cdd:cd11053     2 GFLERLRARYGDVFTLRVpGLGPVVVLSDPEAIKQIFtadpDVLHPGEGNSLLePLLGPNS-------LLLLDGDRHRRR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 138 RKIcVLKLLSRKTLDSFYELrrkeVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEmesvgTEFKGV 217
Cdd:cd11053    75 RKL-LMPAFHGERLRAYGEL----IAEITEREIDRWPPGQPFDLRELMQEITLEVILRVVFGVDDGERL-----QELRRL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 218 ISEITRLLSEPNVSdfFPWLARFDLQGL-VKRMGVCARELDAVLDRAIEQ--MKPLRGRDDdevkdFLQYLMKLKDQEGD 294
Cdd:cd11053   145 LPRLLDLLSSPLAS--FPALQRDLGPWSpWGRFLRARRRIDALIYAEIAErrAEPDAERDD-----ILSLLLSARDEDGQ 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 295 sevPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKdniVEESHITRLPYILAIMKETLR 374
Cdd:cd11053   218 ---PLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGD---PDPEDIAKLPYLDAVIKETLR 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 375 LHPTLPLlVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScdftgANYSYFPFGSGRRIC 454
Cdd:cd11053   292 LYPVAPL-VPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRKP-----SPYEYLPFGGGVRRC 365
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1032284286 455 AGVALA--E-RMVlytLATLLHSFDWKIPEG 482
Cdd:cd11053   366 IGAAFAllEmKVV---LATLLRRFRLELTDP 393
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
74-496 1.65e-45

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: 164.80  E-value: 1.65e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFsNRDVPLTgRAATYGGIDIVWTPYGAEWRQLRKIcVLKLLSRKTLDS 153
Cdd:cd11083     1 GSAYRFRLGRQPVLVISDPELIREVLRRRPDEF-RRISSLE-SVFREMGINGVFSAEGDAWRRQRRL-VMPAFSPKHLRY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 154 FY-ELRRKEVRERTRYLyEQGRKQSPVKVGDQL--------FLTMMNLTMNMLWGGSVKAEEmesvgtEFKGVISEITRL 224
Cdd:cd11083    78 FFpTLRQITERLRERWE-RAAAEGEAVDVHKDLmrytvdvtTSLAFGYDLNTLERGGDPLQE------HLERVFPMLNRR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 225 LSEPnvsdfFPWLARFDLQGlvkrmgvcARELDAVLDRAIEQMKPL------RGRDDDEVKDFLQYLMKLKDQEGDSEVP 298
Cdd:cd11083   151 VNAP-----FPYWRYLRLPA--------DRALDRALVEVRALVLDIiaaaraRLAANPALAEAPETLLAMMLAEDDPDAR 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 299 ITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGK-DNIVEESHITRLPYILAIMKETLRLHP 377
Cdd:cd11083   218 LTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGaRVPPLLEALDRLPYLEAVARETLRLKP 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 378 TLPLLvPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANYSYFPFGSGRRICAGV 457
Cdd:cd11083   298 VAPLL-FLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEPHDPSSLLPFGAGPRLCPGR 376
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1032284286 458 ALAERMVLYTLATLLHSFDWKIPEgHVLDLKEKFGIVLK 496
Cdd:cd11083   377 SLALMEMKLVFAMLCRNFDIELPE-PAPAVGEEFAFTMS 414
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
74-498 2.14e-45

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: 164.62  E-value: 2.14e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDinfsnrdvpLTGRAATYGgidiVWTPY---------GAEWRQLRKIcVLK 144
Cdd:cd20628     1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSK---------LITKSFLYD----FLKPWlgdglltstGEKWRKRRKL-LTP 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 145 LLSRKTLDSFYELrrkeVRERTRYLYEQGRKQSPVKVGDqLFLTMMNLTMNML----WGgsVKAEEMESVGTEFKGVISE 220
Cdd:cd20628    67 AFHFKILESFVEV----FNENSKILVEKLKKKAGGGEFD-IFPYISLCTLDIIcetaMG--VKLNAQSNEDSEYVKAVKR 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 221 ITRLLSEPNVSdffPWLaRFD----LQGLVKRMGVCARELDAVLDRAIEQMK------PLRGRDDDEV-----KDFLQYL 285
Cdd:cd20628   140 ILEIILKRIFS---PWL-RFDfifrLTSLGKEQRKALKVLHDFTNKVIKERReelkaeKRNSEEDDEFgkkkrKAFLDLL 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 286 MKLKDQEGdsevPIT----INHVKALLtdmvVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKD-NIVEESHIT 360
Cdd:cd20628   216 LEAHEDGG----PLTdediREEVDTFM----FAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDdRRPTLEDLN 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 361 RLPYILAIMKETLRLHPTLPLlVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScdftgA 440
Cdd:cd20628   288 KMKYLERVIKETLRLYPSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENS-----A 361
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032284286 441 N---YSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWK-IPEGHvlDLKEKFGIVLKLK 498
Cdd:cd20628   362 KrhpYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLpVPPGE--DLKLIAEIVLRSK 421
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
87-472 4.32e-44

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: 160.93  E-value: 4.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  87 IVVNSPSLAREILKdqdINFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQLRKIcVLKLLSRKTLdsFYELRRKEVRERT 166
Cdd:cd11059    11 VSVNDLDAVREIYG---GGFGKTKSYWYFTLRGGGGPNLFSTLDPKEHSARRRL-LSGVYSKSSL--LRAAMEPIIRERV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 167 RYLYEQ----GRKQSPVKVGDQLFLTMMNLTMNMLWGgsvkaeemESVGTEFKGVISEITRLLSEPNVSDFFPWLA---- 238
Cdd:cd11059    85 LPLIDRiakeAGKSGSVDVYPLFTALAMDVVSHLLFG--------ESFGTLLLGDKDSRERELLRRLLASLAPWLRwlpr 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 239 RFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDQEGDSEVPITINHVKALLTDMVVGGTDT 318
Cdd:cd11059   157 YLPLATSRLIIGIYFRAFDEIEEWALDLCARAESSLAESSDSESLTVLLLEKLKGLKKQGLDDLEIASEALDHIVAGHDT 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 319 STNTIEFAMAELMSNPELIKRAQEELDEVVGK-DNIVEESHITRLPYILAIMKETLRLHPTLPLLVPhR--PAENTVVGG 395
Cdd:cd11059   237 TAVTLTYLIWELSRPPNLQEKLREELAGLPGPfRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLP-RvvPEGGATIGG 315
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032284286 396 YTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANYSYFPFGSGRRICAGVALAeRMVLYTLATLL 472
Cdd:cd11059   316 YYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETAREMKRAFWPFGSGSRMCIGMNLA-LMEMKLALAAI 391
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
73-496 7.65e-43

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: 157.36  E-value: 7.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREIL-KDQDiNFSNRdvPLTGRAATYGGIDIVWTPyGAEWRQLRKICV-------LK 144
Cdd:cd11055     2 YGKVFGLYFGTIPVIVVSDPEMIKEILvKEFS-NFTNR--PLFILLDEPFDSSLLFLK-GERWKRLRTTLSptfssgkLK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 145 LLSRKTLDSFYELRRKevrertryLYEQGRKQSPVkvgdQLFLTMMNLTMNMLwgGS----VKAEEMESVGTEFKGVISE 220
Cdd:cd11055    78 LMVPIINDCCDELVEK--------LEKAAETGKPV----DMKDLFQGFTLDVI--LStafgIDVDSQNNPDDPFLKAAKK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 221 I-----TRLLSEPNVSDFFPWLARFDLQGLVKRMgvcARELDAVLDRAIEQmkplrgRDDDEV---KDFLQyLMkLKDQE 292
Cdd:cd11055   144 IfrnsiIRLFLLLLLFPLRLFLFLLFPFVFGFKS---FSFLEDVVKKIIEQ------RRKNKSsrrKDLLQ-LM-LDAQD 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 293 GDSEV---PITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIM 369
Cdd:cd11055   213 SDEDVskkKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVI 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 370 KETLRLHPtlPLLVPHRPA-ENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFtgANYSYFPFG 448
Cdd:cd11055   293 NETLRLYP--PAFFISRECkEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKR--HPYAYLPFG 368
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1032284286 449 SGRRICAGVALAERMVLYTLATLLHSFDWK-IPEGHVlDLKEKFGIVLK 496
Cdd:cd11055   369 AGPRNCIGMRFALLEVKLALVKILQKFRFVpCKETEI-PLKLVGGATLS 416
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
233-482 1.13e-42

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


Pssm-ID: 410684 [Multi-domain]  Cd Length: 418  Bit Score: 157.00  E-value: 1.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 233 FFPWLARFdlqGLVKRMGVCA-RELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDQEGDSEVPITINHVKALLtdM 311
Cdd:cd11061   150 HAPWLRPL---LLDLPLFPGAtKARKRFLDFVRAQLKERLKAEEEKRPDIFSYLLEAKDPETGEGLDLEELVGEARL--L 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 312 VVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVV-GKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHR-PAE 389
Cdd:cd11061   225 IVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFpSDDEIRLGPKLKSLPYLRACIDEALRLSPPVPSGLPREtPPG 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 390 NTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNnsCDFTGANYSYF-PFGSGRRICAGVALAERMVLYTL 468
Cdd:cd11061   305 GLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSR--PEELVRARSAFiPFSIGPRGCIGKNLAYMELRLVL 382
                         250
                  ....*....|....
gi 1032284286 469 ATLLHSFDWKIPEG 482
Cdd:cd11061   383 ARLLHRYDFRLAPG 396
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
73-499 1.21e-42

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: 157.49  E-value: 1.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKlTIVVNSPSLAREILKDQDInFSnRDVPLTGRAATYGgiDIVWTPYGAEWRQLRKICVLKLLSRKTLD 152
Cdd:cd11070     2 LGAVKILFVSRW-NILVTKPEYLTQIFRRRDD-FP-KPGNQYKIPAFYG--PNVISSEGEDWKRYRKIVAPAFNERNNAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 153 SFYELRRKeVRERTRYLYEQGrkQSPVKVGDQLFLTMMNLTMNMLwgGSV--------KAEEMESVGTEFKGVISEI--T 222
Cdd:cd11070    77 VWEESIRQ-AQRLIRYLLEEQ--PSAKGGGVDVRDLLQRLALNVI--GEVgfgfdlpaLDEEESSLHDTLNAIKLAIfpP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 223 RLLSEPnvsdFFPWLARFDLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDQEGDSEVPITIN 302
Cdd:cd11070   152 LFLNFP----FLDRLPWVLFPSRKRAFKDVDEFLSELLDEVEAELSADSKGKQGTESVVASRLKRARRSGGLTEKELLGN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 303 hvkalLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHIT--RLPYILAIMKETLRLHPTLP 380
Cdd:cd11070   228 -----LFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEEDfpKLPYLLAVIYETLRLYPPVQ 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 381 LLvPHRPAENTVV-----GGYTIPKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFLDNN-----SCDFTGANYSYFPFGS 449
Cdd:cd11070   303 LL-NRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSgeigaATRFTPARGAFIPFSA 381
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032284286 450 GRRICAGVALAERMVLYTLATLLHSFDWKIPEGHVLDL---KEKFGIVLKLKI 499
Cdd:cd11070   382 GPRACLGRKFALVEFVAALAELFRQYEWRVDPEWEEGEtpaGATRDSPAKLRL 434
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
211-482 2.31e-42

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: 156.20  E-value: 2.31e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 211 GTEFKGVISEITRLLSEPNVSDFFPWLARFDLQGLVKRMGVCARELDAVLDRAIEQM---KPLRGRDDDEVKDFLQYLMK 287
Cdd:cd11060   130 GTDVDGYIASIDKLLPYFAVVGQIPWLDRLLLKNPLGPKRKDKTGFGPLMRFALEAVaerLAEDAESAKGRKDMLDSFLE 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 288 LKDQEGDsevPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKD---NIVEESHITRLPY 364
Cdd:cd11060   210 AGLKDPE---KVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGklsSPITFAEAQKLPY 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 365 ILAIMKETLRLHPTLPLLVP-HRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFLDNNSCDFTGANY 442
Cdd:cd11060   287 LQAVIKEALRLHPPVGLPLErVVPPGGATICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWLEADEEQRRMMDR 366
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1032284286 443 SYFPFGSGRRICAGVALAeRMVLY-TLATLLHSFDWKIPEG 482
Cdd:cd11060   367 ADLTFGAGSRTCLGKNIA-LLELYkVIPELLRRFDFELVDP 406
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
63-496 4.48e-42

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: 155.74  E-value: 4.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  63 HTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNR-DVPLTGRAATYGGIdiVWTPYGAEWRQLRKIC 141
Cdd:cd20661     2 HVYMKKQSQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRpSLPLFMKLTNMGGL--LNSKYGRGWTEHRKLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 142 VLKLLSRKTLDSFYELRrkeVRERTRYLYE--QGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEmesvgTEFKGVI- 218
Cdd:cd20661    80 VNCFRYFGYGQKSFESK---ISEECKFFLDaiDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYED-----TDFQHMIe 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 219 --SEITRLLSEPNV--SDFFPWLARF---DLQGLVKRMGVCARELDAVLDRAIEQMKPLRGRDddevkdFLQ-YLMKLKD 290
Cdd:cd20661   152 ifSENVELAASAWVflYNAFPWIGILpfgKHQQLFRNAAEVYDFLLRLIERFSENRKPQSPRH------FIDaYLDEMDQ 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 291 QEGDSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMK 370
Cdd:cd20661   226 NKNDPESTFSMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLH 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 371 ETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTGANySYFPFGSG 450
Cdd:cd20661   306 EVLRFCNIVPLGIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNG-QFAKKE-AFVPFSLG 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1032284286 451 RRICAGVALAeRMVLYTLAT-LLHSFDWKIPEGHVLDLKEKFGIVLK 496
Cdd:cd20661   384 RRHCLGEQLA-RMEMFLFFTaLLQRFHLHFPHGLIPDLKPKLGMTLQ 429
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
73-468 4.78e-42

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: 155.55  E-value: 4.78e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLT-------GRAATYGGidivwTPYGAEWRQLRKIcVLKL 145
Cdd:cd11066     1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRPTFYTfhkvvssTQGFTIGT-----SPWDESCKRRRKA-AASA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 146 LSRKTLDSFYELRRKEVRERTRYLY---EQGRKQSPVKVGDQLFltMMNLTMNMLWGGSVKAEEMESVGTEFKGVISEIT 222
Cdd:cd11066    75 LNRPAVQSYAPIIDLESKSFIRELLrdsAEGKGDIDPLIYFQRF--SLNLSLTLNYGIRLDCVDDDSLLLEIIEVESAIS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 223 RLLSE-PNVSDFFPWLARFDLQ-GLVKRMGVCARELDAVLDRAIEQMKPLRGRDDDevKDFLQYLMkLKDQEgdseVPIT 300
Cdd:cd11066   153 KFRSTsSNLQDYIPILRYFPKMsKFRERADEYRNRRDKYLKKLLAKLKEEIEDGTD--KPCIVGNI-LKDKE----SKLT 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 301 INHVKALLTDMVVGGTDTSTNTIEFAMAELMSNP--ELIKRAQEELDEVVGKDNIVEESHIT--RLPYILAIMKETLRLH 376
Cdd:cd11066   226 DAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWEDCAAeeKCPYVVALVKETLRYF 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 377 PTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANysYFPFGSGRRICAG 456
Cdd:cd11066   306 TVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPP--HFSFGAGSRMCAG 383
                         410
                  ....*....|..
gi 1032284286 457 VALAERmVLYTL 468
Cdd:cd11066   384 SHLANR-ELYTA 394
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
73-495 1.94e-41

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: 153.81  E-value: 1.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRD-VPLTGRAATygGIDIVWTpYGAEWRQLRKICVLKL----LS 147
Cdd:cd20664     1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPiIPIFEDFNK--GYGILFS-NGENWKEMRRFTLTTLrdfgMG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 148 RKTLDSFyelrrkeVRERTRYLYEQGRKQ--SPVKVGDQLFLTMMNLTMNMLWGgsVKAEEMESVGTEFKGVISEITRLL 225
Cdd:cd20664    78 KKTSEDK-------ILEEIPYLIEVFEKHkgKPFETTLSMNVAVSNIIASIVLG--HRFEYTDPTLLRMVDRINENMKLT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 226 SEPNVS--DFFPWLARFdlQGLVKRMgvcARELDAVLDRAIEQ-MKPLRGRDDDEVKDFLQ-YLMKLKDQEGDSEVPITI 301
Cdd:cd20664   149 GSPSVQlyNMFPWLGPF--PGDINKL---LRNTKELNDFLMETfMKHLDVLEPNDQRGFIDaFLVKQQEEEESSDSFFHD 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 302 NHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEEsHITRLPYILAIMKETLRLHPTLPL 381
Cdd:cd20664   224 DNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVE-HRKNMPYTDAVIHEIQRFANIVPM 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 382 LVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTgANYSYFPFGSGRRICAGVALAe 461
Cdd:cd20664   303 NLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQG-KFV-KRDAFMPFSAGRRVCIGETLA- 379
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1032284286 462 RMVLYTLAT-LLHSFDWKIPEGHV---LDLKEKFGIVL 495
Cdd:cd20664   380 KMELFLFFTsLLQRFRFQPPPGVSeddLDLTPGLGFTL 417
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
73-495 1.86e-40

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: 151.10  E-value: 1.86e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNR-DVPLtgRAATYGGIDIVWTPyGAEWRQLRKICVLKL----LS 147
Cdd:cd20662     1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRpETPL--RERIFNKNGLIFSS-GQTWKEQRRFALMTLrnfgLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 148 RKTLdsfyELRrkeVRERTRYLYEQGRKQspvkvGDQLF---LTMMNLTMNMLwgGSVK-AEEMESVGTEFKGVI---SE 220
Cdd:cd20662    78 KKSL----EER---IQEECRHLVEAIREE-----KGNPFnphFKINNAVSNII--CSVTfGERFEYHDEWFQELLrllDE 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 221 ITRLLSEPNVS--DFFPWLARF---DLQGLVKRMGVCARELDAVLDRAIEQMKPlrgrddDEVKDFLQYLMKLKDQEGDS 295
Cdd:cd20662   144 TVYLEGSPMSQlyNAFPWIMKYlpgSHQTVFSNWKKLKLFVSDMIDKHREDWNP------DEPRDFIDAYLKEMAKYPDP 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 296 EVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRL 375
Cdd:cd20662   218 TTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRM 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 376 HPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScdFTGANySYFPFGSGRRICA 455
Cdd:cd20662   298 GNIIPLNVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQ--FKKRE-AFLPFSMGKRACL 374
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1032284286 456 GVALAERMVLYTLATLLHSFDWKIPEGHVLDLKEKFGIVL 495
Cdd:cd20662   375 GEQLARSELFIFFTSLLQKFTFKPPPNEKLSLKFRMGITL 414
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
73-478 8.58e-40

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: 149.33  E-value: 8.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNR-DVPLTGRAATygGIDIVWTpYGAEWRQLRKICVLKL----LS 147
Cdd:cd20665     1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRgRFPIFEKVNK--GLGIVFS-NGERWKETRRFSLMTLrnfgMG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 148 RKTLdsfyELRrkeVRERTRYLYEQGRKQ-------------SPVKV------------GDQLFLTMMNLtmnmlwggsv 202
Cdd:cd20665    78 KRSI----EDR---VQEEARCLVEELRKTngspcdptfilgcAPCNVicsiifqnrfdyKDQDFLNLMEK---------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 203 kaeemesvgtefkgvISEITRLLSEP--NVSDFFPWLARFdLQG----LVKRMgvcARELDAVLDRAIEQMKPLrgrDDD 276
Cdd:cd20665   141 ---------------LNENFKILSSPwlQVCNNFPALLDY-LPGshnkLLKNV---AYIKSYILEKVKEHQESL---DVN 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 277 EVKDFLQY-LMKLKDQEGDSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVE 355
Cdd:cd20665   199 NPRDFIDCfLIKMEQEKHNQQSEFTLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPC 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 356 ESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSC 435
Cdd:cd20665   279 MQDRSHMPYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGN 358
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1032284286 436 dFTGANYsYFPFGSGRRICAGVALAeRMVLYT-LATLLHSFDWK 478
Cdd:cd20665   359 -FKKSDY-FMPFSAGKRICAGEGLA-RMELFLfLTTILQNFNLK 399
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
71-477 1.09e-39

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: 148.56  E-value: 1.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  71 QSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRdvPLTGRAATYGGiDIVWTPYGAEWRQLRKIcVLKLLSRKT 150
Cdd:cd11049    10 RAHGDLVRIRLGPRPAYVVTSPELVRQVLVNDRVFDKGG--PLFDRARPLLG-NGLATCPGEDHRRQRRL-MQPAFHRSR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 151 LDSFYELRRKEVRERTRYlYEQGRkqsPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTEFKGVISEITRLLSEPnv 230
Cdd:cd11049    86 IPAYAEVMREEAEALAGS-WRPGR---VVDVDAEMHRLTLRVVARTLFSTDLGPEAAAELRQALPVVLAGMLRRAVPP-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 231 sdffPWLARFDLQGlVKRMGVCARELDAVLDRAIEQmkplRGRDDDEVKDFLQYLMKLKDQEG----DSEVpitINHVKA 306
Cdd:cd11049   160 ----KFLERLPTPG-NRRFDRALARLRELVDEIIAE----YRASGTDRDDLLSLLLAARDEEGrplsDEEL---RDQVIT 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 307 LLTdmvvGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGkDNIVEESHITRLPYILAIMKETLRLHPTLPLLvPHR 386
Cdd:cd11049   228 LLT----AGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWLL-TRR 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 387 PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGanYSYFPFGSGRRICAGVALAERMVLY 466
Cdd:cd11049   302 TTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPR--GAFIPFGAGARKCIGDTFALTELTL 379
                         410
                  ....*....|.
gi 1032284286 467 TLATLLHSFDW 477
Cdd:cd11049   380 ALATIASRWRL 390
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
76-493 2.70e-39

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: 147.79  E-value: 2.70e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  76 IFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGgidIVWTpYGAEWRQLRKicvlkLLSrktlDSF- 154
Cdd:cd20621     5 IIVSNLGSKPLISLVDPEYIKEFLQNHHYYKKKFGPLGIDRLFGKG---LLFS-EGEEWKKQRK-----LLS----NSFh 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 155 YEL---RRKEVRERTRYLYEqgrKQSPVKVGDQLFLTMM---------------NLTMNmlwGGSVKAEE----MESVGT 212
Cdd:cd20621    72 FEKlksRLPMINEITKEKIK---KLDNQNVNIIQFLQKItgevvirsffgeeakDLKIN---GKEIQVELveilIESFLY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 213 EFKGVISEITRLLSEPNVSDFFPWLARFDLQGLVKRMgvcaRE-LDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDQ 291
Cdd:cd20621   146 RFSSPYFQLKRLIFGRKSWKLFPTKKEKKLQKRVKEL----RQfIEKIIQNRIKQIKKNKDEIKDIIIDLDLYLLQKKKL 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 292 EGDsevpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKE 371
Cdd:cd20621   222 EQE----ITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKE 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 372 TLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGanYSYFPFGSGR 451
Cdd:cd20621   298 VLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNP--FVFIPFSAGP 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 1032284286 452 RICAG--VALAERMVLytLATLLHSFDWKIPEGHVLDLKEKFGI 493
Cdd:cd20621   376 RNCIGqhLALMEAKII--LIYILKNFEIEIIPNPKLKLIFKLLY 417
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
73-498 3.25e-39

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: 147.84  E-value: 3.25e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDvPLTGRAATYGGIDIVWTPYGAEWRQLRKIC--VLKLLSRKT 150
Cdd:cd20675     1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRP-DFASFRVVSGGRSLAFGGYSERWKAHRRVAhsTVRAFSTRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 151 LDSFYELRRK---EVRERTRYLYEQGRKQSPVKVGDQLFLTMMNlTMNMLWGGSVKAEEMEsvgtEFKGVIS---EITRL 224
Cdd:cd20675    80 PRTRKAFERHvlgEARELVALFLRKSAGGAYFDPAPPLVVAVAN-VMSAVCFGKRYSHDDA----EFRSLLGrndQFGRT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 225 LSEPNVSDFFPWLARF---------DLQGLvkrmgvcAREL-DAVLDRAIEQMKPLRGRdddEVKDFLQYLMKLKDQ--E 292
Cdd:cd20675   155 VGAGSLVDVMPWLQYFpnpvrtvfrNFKQL-------NREFyNFVLDKVLQHRETLRGG---APRDMMDAFILALEKgkS 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 293 GDSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKET 372
Cdd:cd20675   225 GDSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEA 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 373 LRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSC---DFTGanySYFPFGS 449
Cdd:cd20675   305 MRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFlnkDLAS---SVMIFSV 381
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032284286 450 GRRICAGVALAE-RMVLYTlATLLHSFDWKIPEGHVLDLKEKFGIVLKLK 498
Cdd:cd20675   382 GKRRCIGEELSKmQLFLFT-SILAHQCNFTANPNEPLTMDFSYGLTLKPK 430
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
307-498 3.69e-39

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: 147.85  E-value: 3.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 307 LLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHR 386
Cdd:cd20676   241 IVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPFTIPHC 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 387 PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFL--DNNSCDFTGANySYFPFGSGRRICAGVALAERMV 464
Cdd:cd20676   321 TTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLtaDGTEINKTESE-KVMLFGLGKRRCIGESIARWEV 399
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1032284286 465 LYTLATLLHSFDWKIPEGHVLDLKEKFGIVLKLK 498
Cdd:cd20676   400 FLFLAILLQQLEFSVPPGVKVDMTPEYGLTMKHK 433
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
73-496 5.21e-39

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: 146.91  E-value: 5.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRdvPLTGRAATYGGIDIVWTPYGAEWRQLRKICVLKL----LSR 148
Cdd:cd20667     1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGR--PLTPFFRDLFGEKGIICTNGLTWKQQRRFCMTTLrelgLGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 149 KTLDSFYELRRKEVRERtrYLYEQGRkqsPVKVGDQLFLTMMNLTMNMLWGGSVKAEEmesvgTEFKGVISEITRLLSEP 228
Cdd:cd20667    79 QALESQIQHEAAELVKV--FAQENGR---PFDPQDPIVHATANVIGAVVFGHRFSSED-----PIFLELIRAINLGLAFA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 229 NVS-----DFFPWLARFdLQGLVKRmgvCARELDAVLDRAIEQMKPLRGRDDDEVKDFLQ-YLMKLKDQEGDSEVPITIN 302
Cdd:cd20667   149 STIwgrlyDAFPWLMRY-LPGPHQK---IFAYHDAVRSFIKKEVIRHELRTNEAPQDFIDcYLAQITKTKDDPVSTFSEE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 303 HVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLL 382
Cdd:cd20667   225 NMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVG 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 383 VPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTgANYSYFPFGSGRRICAGVALAeR 462
Cdd:cd20667   305 AVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDG-NFV-MNEAFLPFSAGHRVCLGEQLA-R 381
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1032284286 463 MVLYTL-ATLLHSFDWKIPEG-HVLDLKEKFGIVLK 496
Cdd:cd20667   382 MELFIFfTTLLRTFNFQLPEGvQELNLEYVFGGTLQ 417
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
73-485 1.86e-37

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: 142.32  E-value: 1.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNL-GSKlTIVVNSPSLAREILKDQDINFSNRdVPLTGRAAtyGGIDIVWTPYGAEWRQLRKIcVLKLLS---- 147
Cdd:cd11043     5 YGPVFKTSLfGRP-TVVSADPEANRFILQNEGKLFVSW-YPKSVRKL--LGKSSLLTVSGEEHKRLRGL-LLSFLGpeal 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 148 ------------RKTLDSFYELRRKEVRERTRYLyeqgrkqspvkvgdqlfltMMNLTMNMLWGGSvKAEEMESVGTEFK 215
Cdd:cd11043    80 kdrllgdidelvRQHLDSWWRGKSVVVLELAKKM-------------------TFELICKLLLGID-PEEVVEELRKEFQ 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 216 GVISEitrLLSEPnvsdffpwlarFDLQGLVKRMGVCAR-ELDAVLDRAIEQMKpLRGRDDDEVKDFLQYLMKLKDQEGD 294
Cdd:cd11043   140 AFLEG---LLSFP-----------LNLPGTTFHRALKARkRIRKELKKIIEERR-AELEKASPKGDLLDVLLEEKDEDGD 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 295 SevpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEE---SHITRLPYILAIMKE 371
Cdd:cd11043   205 S---LTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAKRKEEGEGltwEDYKSMKYTWQVINE 281
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 372 TLRLHPTLPLLvpHRPAENTV-VGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScdftGANYSYFPFGSG 450
Cdd:cd11043   282 TLRLAPIVPGV--FRKALQDVeYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGK----GVPYTFLPFGGG 355
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1032284286 451 RRICAGVALAERMVLYTLATLLHSFDWK-IPEGHVL 485
Cdd:cd11043   356 PRLCPGAELAKLEILVFLHHLVTRFRWEvVPDEKIS 391
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
74-482 2.04e-37

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: 142.91  E-value: 2.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  74 GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLTGRAATYGGID--IVWTPYGAEWRQLRKICVLKL----LS 147
Cdd:cd20663     2 GDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGPKSqgVVLARYGPAWREQRRFSVSTLrnfgLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 148 RKTLDSFyelrrkeVRERTRYL-----YEQGRKQSP--------------------VKVGDQLFLTMMNLTMNMLwggsv 202
Cdd:cd20663    82 KKSLEQW-------VTEEAGHLcaaftDQAGRPFNPntllnkavcnviaslifarrFEYEDPRFIRLLKLLEESL----- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 203 kaeemesvgTEFKGVIseitrllsePNVSDFFPWLARfdLQGLVKRMGVCARELDAVLDRAIEQMKplRGRDDDE-VKDF 281
Cdd:cd20663   150 ---------KEESGFL---------PEVLNAFPVLLR--IPGLAGKVFPGQKAFLALLDELLTEHR--TTWDPAQpPRDL 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 282 LQ-YLMKLKDQEGDSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHIT 360
Cdd:cd20663   208 TDaFLAEMEKAKGNPESSFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQA 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 361 RLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCdFTGA 440
Cdd:cd20663   288 RMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGH-FVKP 366
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1032284286 441 NySYFPFGSGRRICAGVALAeRMVLYTLAT-LLHSFDWKIPEG 482
Cdd:cd20663   367 E-AFMPFSAGRRACLGEPLA-RMELFLFFTcLLQRFSFSVPAG 407
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
315-498 2.11e-37

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: 142.70  E-value: 2.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 315 GTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLvpHRPAEN-TVV 393
Cdd:cd20659   239 GHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFI--ARTLTKpITI 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 394 GGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTgaNYSYFPFGSGRRICAG--VALAERMVlyTLATL 471
Cdd:cd20659   317 DGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRD--PFAFIPFSAGPRNCIGqnFAMNEMKV--VLARI 392
                         170       180
                  ....*....|....*....|....*..
gi 1032284286 472 LHSFDWKIPEGHVLDLKEkfGIVLKLK 498
Cdd:cd20659   393 LRRFELSVDPNHPVEPKP--GLVLRSK 417
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
73-498 4.98e-37

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: 141.77  E-value: 4.98e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVPLT------GRAATYGgidivwTPYGAEWRQLRKIC--VLK 144
Cdd:cd20677     1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPDFYTfslianGKSMTFS------EKYGESWKLHKKIAknALR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 145 LLSRKTLDS------FYELRRKEVRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGgsvkaEEMESVGTEFKGVI 218
Cdd:cd20677    75 TFSKEEAKSstcsclLEEHVCAEASELVKTLVELSKEKGSFDPVSLITCAVANVVCALCFG-----KRYDHSDKEFLTIV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 219 ---SEITRLLSEPNVSDFFPWLARFDLQGLvKRMGVCARELDAVLDRAIEqmKPLRGRDDDEVKDF---LQYLMKLKDQE 292
Cdd:cd20677   150 einNDLLKASGAGNLADFIPILRYLPSPSL-KALRKFISRLNNFIAKSVQ--DHYATYDKNHIRDItdaLIALCQERKAE 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 293 GDSEVpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKET 372
Cdd:cd20677   227 DKSAV-LSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEV 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 373 LRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANYSYFPFGSGRR 452
Cdd:cd20677   306 FRHSSFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLVEKVLIFGMGVR 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1032284286 453 ICAGVALAERMVLYTLATLLHSFDWKIPEGHVLDLKEKFGIVLKLK 498
Cdd:cd20677   386 KCLGEDVARNEIFVFLTTILQQLKLEKPPGQKLDLTPVYGLTMKPK 431
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
73-475 5.70e-37

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: 141.44  E-value: 5.70e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNR-DVPLTGRAATYGGIDIvwtPYGAEWRQLRKICVLkllsrkTL 151
Cdd:cd20669     1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRgDYPVFFNFTKGNGIAF---SNGERWKILRRFALQ------TL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 152 DSFYELRR---KEVRERTRYLYEQGRKQSPVKVGDQLFL--TMMNLTMNMLWGGSVKAEEmesvgTEFKGVISEIT---R 223
Cdd:cd20669    72 RNFGMGKRsieERILEEAQFLLEELRKTKGAPFDPTFLLsrAVSNIICSVVFGSRFDYDD-----KRLLTILNLINdnfQ 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 224 LLSEP--NVSDFFPWLARFdLQGLVKRMGVCARELDAVLDRAIEQMKplRGRDDDEVKDFLQ-YLMKLKDQEGDsevPIT 300
Cdd:cd20669   147 IMSSPwgELYNIFPSVMDW-LPGPHQRIFQNFEKLRDFIAESVREHQ--ESLDPNSPRDFIDcFLTKMAEEKQD---PLS 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 301 INHVKALLT---DMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHP 377
Cdd:cd20669   221 HFNMETLVMtthNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFAD 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 378 TLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTgANYSYFPFGSGRRICAGV 457
Cdd:cd20669   301 IIPMSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNG-SFK-KNDAFMPFSAGKRICLGE 378
                         410
                  ....*....|....*....
gi 1032284286 458 ALAeRMVLYT-LATLLHSF 475
Cdd:cd20669   379 SLA-RMELFLyLTAILQNF 396
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
73-482 2.02e-36

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: 139.93  E-value: 2.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNR-DVPLTGRAATYGGIdivWTPYGAEWRQLRKICVLKLlsrKTL 151
Cdd:cd20671     1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRpPIPIFQAIQHGNGV---FFSSGERWRTTRRFTVRSM---KSL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 152 DSFYELRRKEVRERTRYLYEQ--GRKQSPVKVGdQLFLTMMNLTMNMLWGGsvKAEEMESVGTEFKGVISEITRLLSEPN 229
Cdd:cd20671    75 GMGKRTIEDKILEELQFLNGQidSFNGKPFPLR-LLGWAPTNITFAMLFGR--RFDYKDPTFVSLLDLIDEVMVLLGSPG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 230 VS--DFFPWLARF-DLQGLVKRMgvcARELDAVLDRAIEQMKPlrGRDDDEVKDFLQYLMKLKDQEGDSEVPITINHVKA 306
Cdd:cd20671   152 LQlfNLYPVLGAFlKLHKPILDK---VEEVCMILRTLIEARRP--TIDGNPLHSYIEALIQKQEEDDPKETLFHDANVLA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 307 LLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPlLVPHR 386
Cdd:cd20671   227 CTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLP-HVPRC 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 387 PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTGANySYFPFGSGRRICAGVALAeRMVLY 466
Cdd:cd20671   306 TAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEG-KFVKKE-AFLPFSAGRRVCVGESLA-RTELF 382
                         410
                  ....*....|....*..
gi 1032284286 467 TLAT-LLHSFDWKIPEG 482
Cdd:cd20671   383 IFFTgLLQKFTFLPPPG 399
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
73-480 8.37e-36

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: 138.13  E-value: 8.37e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNR-DVPLTGRAATYGGIDIVwtpYGAEWRQLRKicvlklLSRKTL 151
Cdd:cd20670     1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRgELATIERNFQGHGVALA---NGERWRILRR------FSLTIL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 152 DSFYELRR---KEVRERTRYLYEQGRKQSPVKVGDQLFL--TMMNLTMNMLWGGSVKAEEmesvgTEFKGVIseitRLLS 226
Cdd:cd20670    72 RNFGMGKRsieERIQEEAGYLLEEFRKTKGAPIDPTFFLsrTVSNVISSVVFGSRFDYED-----KQFLSLL----RMIN 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 227 EPNVSDFFPWLARFD--------LQGLVKRMGVCAREL-DAVLDRAIEQMKPLrgrDDDEVKDFLQ-YLMKLKDQEGDSE 296
Cdd:cd20670   143 ESFIEMSTPWAQLYDmysgimqyLPGRHNRIYYLIEELkDFIASRVKINEASL---DPQNPRDFIDcFLIKMHQDKNNPH 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 297 VPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLH 376
Cdd:cd20670   220 TEFNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLT 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 377 PTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTgANYSYFPFGSGRRICAG 456
Cdd:cd20670   300 DIVPLGVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQG-RFK-KNEAFVPFSSGKRVCLG 377
                         410       420
                  ....*....|....*....|....
gi 1032284286 457 VALAERMVLYTLATLLHSFDWKIP 480
Cdd:cd20670   378 EAMARMELFLYFTSILQNFSLRSL 401
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
57-479 6.24e-35

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: 135.49  E-value: 6.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  57 FLDPdlhtyfANLAQSH----GPIFKLNLGSKLTIVVNSPSLAREILKDQDINFsnrdvpltgRAATYGGIDIVWTPY-- 130
Cdd:cd11044     7 LRDP------EDFIQSRyqkyGPVFKTHLLGRPTVFVIGAEAVRFILSGEGKLV---------RYGWPRSVRRLLGENsl 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 131 ----GAEWRQLRKIcVLKLLSRKTLDSFYELRRKEVRErtrYLyEQGRKQSPVKVGDQLfltmMNLTMNMlwggsvkaee 206
Cdd:cd11044    72 slqdGEEHRRRRKL-LAPAFSREALESYVPTIQAIVQS---YL-RKWLKAGEVALYPEL----RRLTFDV---------- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 207 mesvgtefkgviseITRLL----SEPNVSDFFPWLARFdLQGLVK----------RMGVCARE-LDAVLDRAIEQMkplR 271
Cdd:cd11044   133 --------------AARLLlgldPEVEAEALSQDFETW-TDGLFSlpvplpftpfGRAIRARNkLLARLEQAIRER---Q 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 272 GRDDDEVKDFLQYLMKLKDQEGdseVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVvGKD 351
Cdd:cd11044   195 EEENAEAKDALGLLLEAKDEDG---EPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDAL-GLE 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 352 NIVEESHITRLPYILAIMKETLRLHPtlpllvPHRPAENTVV-----GGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRP 426
Cdd:cd11044   271 EPLTLESLKKMPYLDQVIKEVLRLVP------PVGGGFRKVLedfelGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDP 344
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1032284286 427 ERFLDNNSCDFTGAnYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKI 479
Cdd:cd11044   345 ERFSPARSEDKKKP-FSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWEL 396
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
221-483 7.12e-34

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: 132.78  E-value: 7.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 221 ITRLLSEPNVSDFFPWLArfdlqglVKRMGVCARELDAVLDRAIEQMKP-LRGRDDDEVKDFLQYLMKLKDQEGDSevPI 299
Cdd:cd11069   161 ILLLFLPRWLVRILPWKA-------NREIRRAKDVLRRLAREIIREKKAaLLEGKDDSGKDILSILLRANDFADDE--RL 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 300 TINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVV--GKDNIVEESHITRLPYILAIMKETLRLHP 377
Cdd:cd11069   232 SDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALpdPPDGDLSYDDLDRLPYLNAVCRETLRLYP 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 378 TLPLLVphRPA-ENTVVGGYTIPKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFLD---NNSCDFTGANYSYFPFGSGRR 452
Cdd:cd11069   312 PVPLTS--REAtKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEpdgAASPGGAGSNYALLTFLHGPR 389
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1032284286 453 ICAG--VALAERMVLytLATLLHSFDWKIPEGH 483
Cdd:cd11069   390 SCIGkkFALAEMKVL--LAALVSRFEFELDPDA 420
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
135-488 1.85e-33

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: 131.61  E-value: 1.85e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 135 RQLRKIcVLKLLSRKTLDSFYELRRKEVRERTRYLYEQGRKQSPVKVGDqLFLTM-MNLTMNMLWGGSVKAEEMESVGTE 213
Cdd:cd11062    56 RLRRKA-LSPFFSKRSILRLEPLIQEKVDKLVSRLREAKGTGEPVNLDD-AFRALtADVITEYAFGRSYGYLDEPDFGPE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 214 FKGVISEITRLLsepNVSDFFPWLARF---DLQGLVKRMGVCARELDAVLDRAIEQMKplRGRDDDEVKDFLQYLMKLKD 290
Cdd:cd11062   134 FLDALRALAEMI---HLLRHFPWLLKLlrsLPESLLKRLNPGLAVFLDFQESIAKQVD--EVLRQVSAGDPPSIVTSLFH 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 291 QEGDSEVP---ITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVV-GKDNIVEESHITRLPYIL 366
Cdd:cd11062   209 ALLNSDLPpseKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMpDPDSPPSLAELEKLPYLT 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 367 AIMKETLRLHPtlplLVPHR-----PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGAN 441
Cdd:cd11062   289 AVIKEGLRLSY----GVPTRlprvvPDEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEKGKLDRY 364
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1032284286 442 ysYFPFGSGRRICAGVALAeRMVLY-TLATLLHSFDWKIPEGHVLDLK 488
Cdd:cd11062   365 --LVPFSKGSRSCLGINLA-YAELYlALAALFRRFDLELYETTEEDVE 409
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
72-481 5.61e-33

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: 130.18  E-value: 5.61e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  72 SHGPIFKLNLGSKLTIVVNSPSLAREILKDQD-INFSNRDVPLTGRAATYGGIDIVWTPYGAEWR-----------QLRK 139
Cdd:cd11040    10 SGGPIFTIRLGGQKIYVITDPELISAVFRNPKtLSFDPIVIVVVGRVFGSPESAKKKEGEPGGKGlirllhdlhkkALSG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 140 ICVLKLLSRKTLDSFYELRRKEVRERTrylyeqgrkQSPVKVGDQLFL--TMMNLTMNMLWGgsvkaeemesvgTEFKGV 217
Cdd:cd11040    90 GEGLDRLNEAMLENLSKLLDELSLSGG---------TSTVEVDLYEWLrdVLTRATTEALFG------------PKLPEL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 218 ISEItrllsepnVSDF------FPWLARFDLQGLVKRMgVCARelDAVLDrAIEQMKPLRGRDDDEVKDFLQYLMKLKDQ 291
Cdd:cd11040   149 DPDL--------VEDFwtfdrgLPKLLLGLPRLLARKA-YAAR--DRLLK-ALEKYYQAAREERDDGSELIRARAKVLRE 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 292 EGDSEVPITINHVkALLtdmvVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHI-----TRLPYIL 366
Cdd:cd11040   217 AGLSEEDIARAEL-ALL----WAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILDltdllTSCPLLD 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 367 AIMKETLRLH--PTLPLLVPhrpaENTVV-GGYTIPKDTKIFVNVWSIQRDPNVWE-NPTEFRPERFLDNN-SCDFTGAN 441
Cdd:cd11040   292 STYLETLRLHssSTSVRLVT----EDTVLgGGYLLRKGSLVMIPPRLLHMDPEIWGpDPEEFDPERFLKKDgDKKGRGLP 367
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1032284286 442 YSYFPFGSGRRICAGVALAERMVLYTLATLLHSFD--------WKIPE 481
Cdd:cd11040   368 GAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDvepvgggdWKVPG 415
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
233-484 2.69e-32

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: 128.56  E-value: 2.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 233 FFPWLARfdLQGLVKRMgvcARELDAVLDRaieQMKPLRGRDDDEVKDFLQYLMKLKDQEGDsevpITINHVKALLTDMV 312
Cdd:cd11041   169 FLPEPRR--LRRLLRRA---RPLIIPEIER---RRKLKKGPKEDKPNDLLQWLIEAAKGEGE----RTPYDLADRQLALS 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 313 VGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPtLPLLVPHRPA--EN 390
Cdd:cd11041   237 FAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNP-LSLVSLRRKVlkDV 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 391 TVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLD-------NNSCDFTGANYSYFPFGSGRRICAGVALAERM 463
Cdd:cd11041   316 TLSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRlreqpgqEKKHQFVSTSPDFLGFGHGRHACPGRFFASNE 395
                         250       260
                  ....*....|....*....|.
gi 1032284286 464 VLYTLATLLHSFDWKIPEGHV 484
Cdd:cd11041   396 IKLILAHLLLNYDFKLPEGGE 416
PLN02738 PLN02738
carotene beta-ring hydroxylase
40-482 1.27e-31

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 128.88  E-value: 1.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  40 PSLPPGPRGLPIVGNLPFLDPdlhtyFANLAQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNrdvpltGRAAT 119
Cdd:PLN02738  136 PKIPEAKGSISAVRGEAFFIP-----LYELFLTYGGIFRLTFGPKSFLIVSDPSIAKHILRDNSKAYSK------GILAE 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 120 YggIDIVW----TPYGAE-WRqLRKICVLKLLSRKTLDSFYELRRKEVRERTRYLYEQGRKQSPVKVgDQLFltmMNLTM 194
Cdd:PLN02738  205 I--LEFVMgkglIPADGEiWR-VRRRAIVPALHQKYVAAMISLFGQASDRLCQKLDAAASDGEDVEM-ESLF---SRLTL 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 195 NMLwGGSVKAEEMESVGTEfKGVISEITRLLSEP---NVSDFFPWLARF--DLQGLVKRMGVCARELDAVLDRAIEQMKp 269
Cdd:PLN02738  278 DII-GKAVFNYDFDSLSND-TGIVEAVYTVLREAedrSVSPIPVWEIPIwkDISPRQRKVAEALKLINDTLDDLIAICK- 354
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 270 lRGRDDDEVKdFLQYLMKLKD--------QEGDSevpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQ 341
Cdd:PLN02738  355 -RMVEEEELQ-FHEEYMNERDpsilhfllASGDD---VSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQ 429
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 342 EELDEVVGkDNIVEESHITRLPYILAIMKETLRLHPTLPLLVpHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENP 421
Cdd:PLN02738  430 EEVDSVLG-DRFPTIEDMKKLKYTTRVINESLRLYPQPPVLI-RRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDA 507
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032284286 422 TEFRPERF-LDNNSCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEG 482
Cdd:PLN02738  508 EKFNPERWpLDGPNPNETNQNFSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQLAPG 569
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
73-481 3.26e-31

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: 125.29  E-value: 3.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRdvpltGRAATYggiDIVWTPYGAEWRQLRKICVLKLLSRKTLD 152
Cdd:cd20668     1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGR-----GEQATF---DWLFKGYGVAFSNGERAKQLRRFSIATLR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 153 SFYELRR---KEVRERTRYLYE--QGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVgtEFKGVISEITRLLSE 227
Cdd:cd20668    73 DFGVGKRgieERIQEEAGFLIDalRGTGGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFL--SLLRMMLGSFQFTAT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 228 P--NVSDFFPWLARFdLQGLVKRMGVCARELDAVLDRAIEQMKplRGRDDDEVKDFLQ-YLMKLKDQEGDsevPITINHV 304
Cdd:cd20668   151 StgQLYEMFSSVMKH-LPGPQQQAFKELQGLEDFIAKKVEHNQ--RTLDPNSPRDFIDsFLIRMQEEKKN---PNTEFYM 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 305 KALLT---DMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPL 381
Cdd:cd20668   225 KNLVMttlNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPM 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 382 LVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScDFTgANYSYFPFGSGRRICAGVALAe 461
Cdd:cd20668   305 GLARRVTKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKG-QFK-KSDAFVPFSIGKRYCFGEGLA- 381
                         410       420
                  ....*....|....*....|.
gi 1032284286 462 RMVLYT-LATLLHSFDWKIPE 481
Cdd:cd20668   382 RMELFLfFTTIMQNFRFKSPQ 402
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
256-498 4.55e-31

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: 124.64  E-value: 4.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 256 LDAVLDRAIEQMKPLRGRDDDEVKD---FLQYLMKLKDQEGdsevPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMS 332
Cdd:cd11057   181 IEKKLQEVELESNLDSEEDEENGRKpqiFIDQLLELARNGE----EFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAM 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 333 NPELIKRAQEELDEVVGKDNIvEESH--ITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWS 410
Cdd:cd11057   257 HPEVQEKVYEEIMEVFPDDGQ-FITYedLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSNGVVIPKGTTIVIDIFN 335
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 411 IQRDPNVW-ENPTEFRPERFLDNNScdfTGAN-YSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIP---Eghvl 485
Cdd:cd11057   336 MHRRKDIWgPDADQFDPDNFLPERS---AQRHpYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKTSlrlE---- 408
                         250
                  ....*....|...
gi 1032284286 486 DLKEKFGIVLKLK 498
Cdd:cd11057   409 DLRFKFNITLKLA 421
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
279-501 3.55e-30

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: 122.30  E-value: 3.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 279 KDFLQYLMKLKDQE-GDSEVPITINHvkallTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELdevvgKDNIVEES 357
Cdd:cd11058   197 PDFMSYILRNKDEKkGLTREELEANA-----SLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEI-----RSAFSSED 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 358 HIT-----RLPYILAIMKETLRLHPTLPLLVPHR-PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLD 431
Cdd:cd11058   267 DITldslaQLPYLNAVIQEALRLYPPVPAGLPRVvPAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLG 346
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032284286 432 NNSCDFTGANYSYF-PFGSGRRICAG--VALAE-RMVlytLATLLHSFDWKIPEGHV--LDLKEKFGIVlkLKIPL 501
Cdd:cd11058   347 DPRFEFDNDKKEAFqPFSVGPRNCIGknLAYAEmRLI---LAKLLWNFDLELDPESEdwLDQQKVYILW--EKPPL 417
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
233-502 6.25e-30

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: 121.75  E-value: 6.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 233 FFPWLARfdlqgLVKRMGVC--ARELDAVLDRAIEQMKPLRGRDDDEVK-DFLQYLMklkdqegDSEVPITINHVKALlT 309
Cdd:cd20650   159 VFPFLTP-----ILEKLNISvfPKDVTNFFYKSVKKIKESRLDSTQKHRvDFLQLMI-------DSQNSKETESHKAL-S 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 310 DM---------VVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLP 380
Cdd:cd20650   226 DLeilaqsiifIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAG 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 381 LLvpHRPAENTV-VGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTgaNYSYFPFGSGRRICAGVAL 459
Cdd:cd20650   306 RL--ERVCKKDVeINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNID--PYIYLPFGSGPRNCIGMRF 381
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1032284286 460 AERMVLYTLATLLHSFDWKIPEGHVLDLKEKFGIVLKLKIPLV 502
Cdd:cd20650   382 ALMNMKLALVRVLQNFSFKPCKETQIPLKLSLQGLLQPEKPIV 424
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
55-494 7.34e-30

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: 121.29  E-value: 7.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  55 LPFLDPDLHTYFANLAQSHGPIFKLnlgskltiVVNSPSLAREILKDQDINFSNrdVPLTGRAATYGGIDIVwTPYGAEW 134
Cdd:cd11052     1 LPHYYHWIKQYGKNFLYWYGTDPRL--------YVTEPELIKELLSKKEGYFGK--SPLQPGLKKLLGRGLV-MSNGEKW 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 135 RQLRKICV-------LKLLSRKTLDSFYELRrkevrerTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGS-VKAEE 206
Cdd:cd11052    70 AKHRRIANpafhgekLKGMVPAMVESVSDML-------ERWKKQMGEEGEEVDVFEEFKALTADIISRTAFGSSyEEGKE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 207 MESVGTEFKGVISEITRLLSEPnVSDFFPwlARFDLQglVKRMGvcaRELDAVLDRAIEQ-MKPLR-GRDDDEVKDFLQY 284
Cdd:cd11052   143 VFKLLRELQKICAQANRDVGIP-GSRFLP--TKGNKK--IKKLD---KEIEDSLLEIIKKrEDSLKmGRGDDYGDDLLGL 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 285 LMKLKDQEgDSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIvEESHITRLPY 364
Cdd:cd11052   215 LLEANQSD-DQNKNMTVQEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKP-PSDSLSKLKT 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 365 ILAIMKETLRLHPTLPLLvpHRPA-ENTVVGGYTIPKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFLDN--NSCDFTGA 440
Cdd:cd11052   293 VSMVINESLRLYPPAVFL--TRKAkEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGvaKAAKHPMA 370
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 441 nysYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEGH------VLDLKEKFGIV 494
Cdd:cd11052   371 ---FLPFGLGPRNCIGQNFATMEAKIVLAMILQRFSFTLSPTYrhaptvVLTLRPQYGLQ 427
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
315-476 2.63e-29

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: 119.67  E-value: 2.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 315 GTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDN-IVEESHITRLPYILAIMKETLRLHPTLPLLVphRPA-ENTV 392
Cdd:cd20660   244 GHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSDrPATMDDLKEMKYLECVIKEALRLFPSVPMFG--RTLsEDIE 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 393 VGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScdftgAN---YSYFPFGSGRRICAG--VALAERMVLyt 467
Cdd:cd20660   322 IGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENS-----AGrhpYAYIPFSAGPRNCIGqkFALMEEKVV-- 394

                  ....*....
gi 1032284286 468 LATLLHSFD 476
Cdd:cd20660   395 LSSILRNFR 403
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
73-495 6.12e-29

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: 118.61  E-value: 6.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILK---------DQDINFSNRDVpltgRAATYGgidiVWTPYGAEWRQLRKICVL 143
Cdd:cd20646     4 YGPIWKSKFGPYDIVNVASAELIEQVLRqegkypmrsDMPHWKEHRDL----RGHAYG----PFTEEGEKWYRLRSVLNQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 144 KLLSRKTLDSFYELRRKEVR---ERTRYLYEqgRKQSPVKVGDQ---------------LFLTMMNLTMNmlwggSVKAE 205
Cdd:cd20646    76 RMLKPKEVSLYADAINEVVSdlmKRIEYLRE--RSGSGVMVSDLanelykfafegissiLFETRIGCLEK-----EIPEE 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 206 EME---SVGTEFKgvISEITRLLsePNVS-DFFPWLARF-----DLQGLVKRMgvcareldavLDRAIEQMKPLRGRDDD 276
Cdd:cd20646   149 TQKfidSIGEMFK--LSEIVTLL--PKWTrPYLPFWKRYvdawdTIFSFGKKL----------IDKKMEEIEERVDRGEP 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 277 EVKDFLQYLMklkdqegdSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEE 356
Cdd:cd20646   215 VEGEYLTYLL--------SSGKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTA 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 357 SHITRLPYILAIMKETLRLHPTLP----LLVphrpAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDN 432
Cdd:cd20646   287 EDIAKMPLLKAVIKETLRLYPVVPgnarVIV----EKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRD 362
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032284286 433 NScdFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKiPEGHVLDLKEKFGIVL 495
Cdd:cd20646   363 GG--LKHHPFGSIPFGYGVRACVGRRIAELEMYLALSRLIKRFEVR-PDPSGGEVKAITRTLL 422
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
87-502 4.64e-28

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: 115.81  E-value: 4.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  87 IVVNSPSLAREILKDQDINFSN--RDV--PLTGraatygGIDIVwTPYGAEWRQLRKIC--------VLKLLSrKTLDS- 153
Cdd:cd11051    13 LVVTDPELAEQITQVTNLPKPPplRKFltPLTG------GSSLI-SMEGEEWKRLRKRFnpgfspqhLMTLVP-TILDEv 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 154 --FYE-LRRKevrertrylyeqgrkqspVKVGDQLFLT--MMNLTMNMLW----GGSVKAEEMESVGTEFkgvisEITRL 224
Cdd:cd11051    85 eiFAAiLREL------------------AESGEVFSLEelTTNLTFDVIGrvtlDIDLHAQTGDNSLLTA-----LRLLL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 225 LSEPNVSDFFPWLarFDLQGLVKRmgVCARELDAVLDRAIEQmkplrgrdddevkdflQYLMKLkdqegdsevpiTINHV 304
Cdd:cd11051   142 ALYRSLLNPFKRL--NPLRPLRRW--RNGRRLDRYLKPEVRK----------------RFELER-----------AIDQI 190
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 305 KALLtdmvVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDN------IVEESH-ITRLPYILAIMKETLRLHP 377
Cdd:cd11051   191 KTFL----FAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPsaaaelLREGPElLNQLPYTTAVIKETLRLFP 266
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 378 tlPLLVPHRPAEN---TVVGGYTIP-KDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANYSYFPFGSGRRI 453
Cdd:cd11051   267 --PAGTARRGPPGvglTDRDGKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHELYPPKSAWRPFERGPRN 344
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1032284286 454 CAGVALA--E-RMVlytLATLLHSFDWKIPEGhVLDLKEKFGIVLKLKIPLV 502
Cdd:cd11051   345 CIGQELAmlElKII---LAMTVRRFDFEKAYD-EWDAKGGYKGLKELFVTGQ 392
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
299-479 4.67e-27

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: 113.48  E-value: 4.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 299 ITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPT 378
Cdd:cd20647   233 LTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPV 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 379 LP--LLVPHrpaENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGaNYSYFPFGSGRRICAG 456
Cdd:cd20647   313 LPgnGRVTQ---DDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRVD-NFGSIPFGYGIRSCIG 388
                         170       180
                  ....*....|....*....|...
gi 1032284286 457 VALAERMVLYTLATLLHSFDWKI 479
Cdd:cd20647   389 RRIAELEIHLALIQLLQNFEIKV 411
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
70-481 5.31e-27

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: 113.31  E-value: 5.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  70 AQSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRDVP-------LTGRAatYGgidiVWTPYGAEWRQLRKICV 142
Cdd:cd20648     2 KAKYGPVWKASFGPILTVHVADPALIEQVLRQEGKHPVRSDLSswkdyrqLRGHA--YG----LLTAEGEEWQRLRSLLA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 143 LKLLSRKTLDSFYELRRKEVRERTRYLYEQGRKQSP--VK-VGDQLFLTMMNLTMNMLWGGSVKAEEMEsVGTEFKGVIS 219
Cdd:cd20648    76 KHMLKPKAVEAYAGVLNAVVTDLIRRLRRQRSRSSPgvVKdIAGEFYKFGLEGISSVLFESRIGCLEAN-VPEETETFIQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 220 EITRLLSEPNVSDFFP-WLARFdLQGLVKRMGVCARELDAVLDRAIEQ-MKPLRGRDDDEVKDFLQYLMKLKDQEGDSEV 297
Cdd:cd20648   155 SINTMFVMTLLTMAMPkWLHRL-FPKPWQRFCRSWDQMFAFAKGHIDRrMAEVAAKLPRGEAIEGKYLTYFLAREKLPMK 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 298 PITINhvkalLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHP 377
Cdd:cd20648   234 SIYGN-----VTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYP 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 378 TLP---LLVPHRPAEntvVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScdfTGANYSYFPFGSGRRIC 454
Cdd:cd20648   309 VIPgnaRVIPDRDIQ---VGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGD---THHPYASLPFGFGKRSC 382
                         410       420
                  ....*....|....*....|....*..
gi 1032284286 455 AGVALAERMVLYTLATLLHSFDWKiPE 481
Cdd:cd20648   383 IGRRIAELEVYLALARILTHFEVR-PE 408
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
73-475 7.12e-27

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: 112.56  E-value: 7.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRdvpltgraATYGGIDIVWTPYGA------EWRQLRKicvlklL 146
Cdd:cd20672     1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGR--------GTIAVVDPIFQGYGVifangeRWKTLRR------F 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 147 SRKTLDSFYELRR---KEVRERTRYLYEQGRKQSPVKVgDQLFLtMMNLTMNMLWGgSVKAEEMESVGTEFKGVISEITR 223
Cdd:cd20672    67 SLATMRDFGMGKRsveERIQEEAQCLVEELRKSKGALL-DPTFL-FQSITANIICS-IVFGERFDYKDPQFLRLLDLFYQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 224 LLS-----EPNVSDFFPWLARFdLQGLVKRMGVCARELDAVLDRAIEQMKPLRgrDDDEVKDFLQ-YLMKLKDQEgdSEV 297
Cdd:cd20672   144 TFSlissfSSQVFELFSGFLKY-FPGAHRQIYKNLQEILDYIGHSVEKHRATL--DPSAPRDFIDtYLLRMEKEK--SNH 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 298 PITINHVKALLT--DMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRL 375
Cdd:cd20672   219 HTEFHHQNLMISvlSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRF 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 376 HPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNscdftGA---NYSYFPFGSGRR 452
Cdd:cd20672   299 SDLIPIGVPHRVTKDTLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDAN-----GAlkkSEAFMPFSTGKR 373
                         410       420
                  ....*....|....*....|...
gi 1032284286 453 ICAGVALAERMVLYTLATLLHSF 475
Cdd:cd20672   374 ICLGEGIARNELFLFFTTILQNF 396
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
257-498 1.80e-26

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: 111.50  E-value: 1.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 257 DAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKlkdqEGDSevPITI-NHVKALLtdmvVGGTDTSTNTIEFAMAELMSNPE 335
Cdd:cd11063   179 DPYVDKALARKEESKDEESSDRYVFLDELAK----ETRD--PKELrDQLLNIL----LAGRDTTASLLSFLFYELARHPE 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 336 LIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVpHRPAENTV--VGG-------YTIPKDTKIFV 406
Cdd:cd11063   249 VWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNS-RVAVRDTTlpRGGgpdgkspIFVPKGTRVLY 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 407 NVWSIQRDPNVW-ENPTEFRPERFLDNnscdfTGANYSYFPFGSGRRICAG--VALAErmVLYTLATLLHSFDwKIPEGH 483
Cdd:cd11063   328 SVYAMHRRKDIWgPDAEEFRPERWEDL-----KRPGWEYLPFNGGPRICLGqqFALTE--ASYVLVRLLQTFD-RIESRD 399
                         250
                  ....*....|....*
gi 1032284286 484 VLDLKEKFGIVLKLK 498
Cdd:cd11063   400 VRPPEERLTLTLSNA 414
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
258-476 3.09e-26

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: 111.01  E-value: 3.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 258 AVLDRA--IEQMKPLRGRDDDEV------KDFLQYLMKLKDQEGDSevpITINHVKALLTDMVVGGTDTSTNTIEFAMAE 329
Cdd:cd20680   193 VIAERAeeMKAEEDKTGDSDGESpskkkrKAFLDMLLSVTDEEGNK---LSHEDIREEVDTFMFEGHDTTAAAMNWSLYL 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 330 LMSNPELIKRAQEELDEVVGK-DNIVEESHITRLPYILAIMKETLRLHPTLPLLVpHRPAENTVVGGYTIPKDTKIFVNV 408
Cdd:cd20680   270 LGSHPEVQRKVHKELDEVFGKsDRPVTMEDLKKLRYLECVIKESLRLFPSVPLFA-RSLCEDCEIRGFKVPKGVNAVIIP 348
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032284286 409 WSIQRDPNVWENPTEFRPERFLDNNScdfTGAN-YSYFPFGSGRRICAG--VALAERMVLytLATLLHSFD 476
Cdd:cd20680   349 YALHRDPRYFPEPEEFRPERFFPENS---SGRHpYAYIPFSAGPRNCIGqrFALMEEKVV--LSCILRHFW 414
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
239-482 1.34e-25

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: 108.56  E-value: 1.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 239 RFDLQGLVKRMGVCAREldaVLDRAIEQMKPLRGRDDDEvkDFLQYLMKLKDQEG----DSEVpitINHVKALLtdmvVG 314
Cdd:cd11045   155 RTPIPGTRWWRGLRGRR---YLEEYFRRRIPERRAGGGD--DLFSALCRAEDEDGdrfsDDDI---VNHMIFLM----MA 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 315 GTDTSTNTIEFAMAELMSNPELIKRAQEELDeVVGKDNIVEEShITRLPYILAIMKETLRLHPTLPLLvPHRPAENTVVG 394
Cdd:cd11045   223 AHDTTTSTLTSMAYFLARHPEWQERLREESL-ALGKGTLDYED-LGQLEVTDWVFKEALRLVPPVPTL-PRRAVKDTEVL 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 395 GYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGAnYSYFPFGSGRRICAGVALAERMVLYTLATLLHS 474
Cdd:cd11045   300 GYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHR-YAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRR 378

                  ....*....
gi 1032284286 475 FD-WKIPEG 482
Cdd:cd11045   379 FRwWSVPGY 387
PLN02936 PLN02936
epsilon-ring hydroxylase
308-483 3.30e-25

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 108.73  E-value: 3.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 308 LTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEEShITRLPYILAIMKETLRLHPTLPLLVPHRP 387
Cdd:PLN02936  283 LLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYED-IKELKYLTRCINESMRLYPHPPVLIRRAQ 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 388 AENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERF-LDNNSCDFTGANYSYFPFGSGRRICAG--VALAERMV 464
Cdd:PLN02936  362 VEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdLDGPVPNETNTDFRYIPFSGGPRKCVGdqFALLEAIV 441
                         170
                  ....*....|....*....
gi 1032284286 465 lyTLATLLHSFDWKIPEGH 483
Cdd:PLN02936  442 --ALAVLLQRLDLELVPDQ 458
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
244-501 4.02e-25

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: 107.68  E-value: 4.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 244 GLVKRMGVCARELDAVLD----RAIEQMKPLRGRDDDEvKDFLQYLMKLKDQEGDSEVPItinhvkaLLTDMVVG----G 315
Cdd:cd11064   171 GSEKKLREAIRVIDDFVYevisRRREELNSREEENNVR-EDLLSRFLASEEEEGEPVSDK-------FLRDIVLNfilaG 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 316 TDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHIT-----RLPYILAIMKETLRLHPTLPLlvPHRPAEN 390
Cdd:cd11064   243 RDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTTDESRVPTyeelkKLVYLHAALSESLRLYPPVPF--DSKEAVN 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 391 TVV--GGYTIPKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFLDNNScDFTGAN-YSYFPFGSGRRICAGVALAERMVLY 466
Cdd:cd11064   321 DDVlpDGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDG-GLRPESpYKFPAFNAGPRICLGKDLAYLQMKI 399
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1032284286 467 TLATLLHSFDWKIPEGHvlDLKEKFGIVLKLKIPL 501
Cdd:cd11064   400 VAAAILRRFDFKVVPGH--KVEPKMSLTLHMKGGL 432
PLN02302 PLN02302
ent-kaurenoic acid oxidase
17-478 4.35e-24

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 105.18  E-value: 4.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  17 PYAIVILTTVFSIL------WYIFKRSP-QPSLPPGPRGLPIVGNL-PFL------DPDlhTYFANLAQSHGP--IFKLN 80
Cdd:PLN02302   11 AAIVAGVFVLKWVLrrvnswLYEPKLGEgQPPLPPGDLGWPVIGNMwSFLrafkssNPD--SFIASFISRYGRtgIYKAF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  81 LGSKLTIVVNSPSLAREILKDQD---INFSNRDVPLTGRAaTYGGIDivwtpyGAEWRQLRKICVLKLLSRKTLDSFY-- 155
Cdd:PLN02302   89 MFGQPTVLVTTPEACKRVLTDDDafePGWPESTVELIGRK-SFVGIT------GEEHKRLRRLTAAPVNGPEALSTYIpy 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 156 -------ELRRKEVRERTRYLYEQgRKQSpvkvgdqlFLTMMNLTMnmlwgGSVKAEEMESVGTEF----KGViseitRL 224
Cdd:PLN02302  162 ieenvksCLEKWSKMGEIEFLTEL-RKLT--------FKIIMYIFL-----SSESELVMEALEREYttlnYGV-----RA 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 225 LSepnvsdffpwlarFDLQGLVKRMGVCARE-LDAVLDRAIEQMKPLR-GRDDDEVKDFLQYLMKLKDQEGDsevPITIN 302
Cdd:PLN02302  223 MA-------------INLPGFAYHRALKARKkLVALFQSIVDERRNSRkQNISPRKKDMLDLLLDAEDENGR---KLDDE 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 303 HVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGK----DNIVEESHITRLPYILAIMKETLRLhPT 378
Cdd:PLN02302  287 EIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKKrppgQKGLTLKDVRKMEYLSQVIDETLRL-IN 365
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 379 LPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTganysYFPFGSGRRICAGVA 458
Cdd:PLN02302  366 ISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTPKAGT-----FLPFGLGSRLCPGND 440
                         490       500
                  ....*....|....*....|
gi 1032284286 459 LAERMVLYTLATLLHSFDWK 478
Cdd:PLN02302  441 LAKLEISIFLHHFLLGYRLE 460
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
73-490 1.21e-23

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: 103.77  E-value: 1.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  73 HGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSNRdvpLTGRAATYGGIDIVWTPYGAEWRQLRKICVlkllsrktlD 152
Cdd:cd20649     2 YGPICGYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNR---MKANLITKPMSDSLLCLRDERWKRVRSILT---------P 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 153 SFYELRRKE----VRERTRYLYEQGRKQSPVKVGDQLFLTMMNLTMNMLwgGSVK-AEEMESVGTEFKGVISEITRLLSe 227
Cdd:cd20649    70 AFSAAKMKEmvplINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVV--ASVAfGTQVDSQKNPDDPFVKNCKRFFE- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 228 pnVSDFFPWLA-----RFDLQGLVKRMGVCAR-ELDAVLDRAIEQMKPLRGRDDDEV--KDFLQYLMKLKDQEG------ 293
Cdd:cd20649   147 --FSFFRPILIlflafPFIMIPLARILPNKSRdELNSFFTQCIRNMIAFRDQQSPEErrRDFLQLMLDARTSAKflsveh 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 294 -------DSEVPITINHV------------KALLTDMVVG--------GTDTSTNTIEFAMAELMSNPELIKRAQEELDE 346
Cdd:cd20649   225 fdivndaDESAYDGHPNSpaneqtkpskqkRMLTEDEIVGqafifliaGYETTTNTLSFATYLLATHPECQKKLLREVDE 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 347 VVGKDNIVEESHITRLPYILAIMKETLRLHPTlPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRP 426
Cdd:cd20649   305 FFSKHEMVDYANVQELPYLDMVIAETLRMYPP-AFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIP 383
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032284286 427 ERFLDNNSCDftGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKI-PEGHV-LDLKEK 490
Cdd:cd20649   384 ERFTAEAKQR--RHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQAcPETEIpLQLKSK 447
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
254-479 6.08e-23

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: 100.99  E-value: 6.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 254 RELDAVLDRAIE--QMKPLRGRDDDEVKDFLQYLMKLKDQEgdSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELM 331
Cdd:cd20639   183 KEIRKSLLKLIErrQTAADDEKDDEDSKDLLGLMISAKNAR--NGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLA 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 332 SNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPtlPLLVPHRPAENTV-VGGYTIPKDTKIFVNVWS 410
Cdd:cd20639   261 MHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLYP--PAVATIRRAKKDVkLGGLDIPAGTELLIPIMA 338
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1032284286 411 IQRDPNVWEN-PTEFRPERFLDNNScdftGANY---SYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKI 479
Cdd:cd20639   339 IHHDAELWGNdAAEFNPARFADGVA----RAAKhplAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRL 407
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
317-481 1.85e-22

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: 99.28  E-value: 1.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 317 DTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILA-IMKETLRLHPTLPLLVPHRPAENTVVGG 395
Cdd:cd20615   229 DVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPMEDYILSTDTLLAyCVLESLRLRPLLAFSVPESSPTDKIIGG 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 396 YTIPKDTKIFVNVWSIQ-RDPNVWENPTEFRPERFLDNNSCDFtgaNYSYFPFGSGRRICAGVALAERMVLYTLATLLHS 474
Cdd:cd20615   309 YRIPANTPVVVDTYALNiNNPFWGPDGEAYRPERFLGISPTDL---RYNFWRFGFGPRKCLGQHVADVILKALLAHLLEQ 385

                  ....*..
gi 1032284286 475 FDWKIPE 481
Cdd:cd20615   386 YELKLPD 392
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
261-496 2.01e-22

cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, X, and Z; This group is composed of family 4 cytochrome P450s from subfamilies A (CYP4A), B (CYP4B), T (CYP4T), X (CYP4X), and Z (CYP4Z). The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B is conserved among vertebrates. CYP4As are known for catalyzing arachidonic acid to 20-HETE (20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoic acid), and some can also metabolize lauric and palmitic acid. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4X1 is expressed at high levels in the mammalian brain and may play a role in regulating fat metabolism. CYP4Z1 is a fatty acid hydroxylase that is unique among human CYPs in that it is predominantly expressed in the mammary gland. Monophyly was not found with the CYP4T and CYP4B subfamilies, and further consideration should be given to their nomenclature. The CYP4B-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 99.66  E-value: 2.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 261 DRAIEQMKPL--RGRDDDEVK-----DFLQYLMKLKDQEGDSevpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSN 333
Cdd:cd20678   193 DKVIQQRKEQlqDEGELEKIKkkrhlDFLDILLFAKDENGKS---LSDEDLRAEVDTFMFEGHDTTASGISWILYCLALH 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 334 PELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQR 413
Cdd:cd20678   270 PEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAGITVSLSIYGLHH 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 414 DPNVWENPTEFRPERFLDNNSCDFtgANYSYFPFGSGRRICAG--VALAERMVLYTLaTLLH---SFDWK---IPEGHVL 485
Cdd:cd20678   350 NPAVWPNPEVFDPLRFSPENSSKR--HSHAFLPFSAGPRNCIGqqFAMNEMKVAVAL-TLLRfelLPDPTripIPIPQLV 426
                         250
                  ....*....|.
gi 1032284286 486 dLKEKFGIVLK 496
Cdd:cd20678   427 -LKSKNGIHLY 436
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
65-495 3.71e-22

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: 98.64  E-value: 3.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  65 YFANLAQSHGPIFKLNLGSKLTIVVNSPSLAREIlkdqdinfsNRDVPLTGRAATY----------GGIdivWTPYGAEW 134
Cdd:cd20640     3 YFDKWRKQYGPIFTYSTGNKQFLYVSRPEMVKEI---------NLCVSLDLGKPSYlkktlkplfgGGI---LTSNGPHW 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 135 RQLRKICVlkllsrktldsfYELRRKEVRertrylyeqgrkqspvkvgdQLFLTMMNLTMNML--WGGSVKA-------- 204
Cdd:cd20640    71 AHQRKIIA------------PEFFLDKVK--------------------GMVDLMVDSAQPLLssWEERIDRaggmaadi 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 205 ---EEMESV----------GTEF-KG-----VISEITRLLSEPNVsdffpwLARFD-LQGLVKRMGVCARELDAVLDRAI 264
Cdd:cd20640   119 vvdEDLRAFsadvisracfGSSYsKGkeifsKLRELQKAVSKQSV------LFSIPgLRHLPTKSNRKIWELEGEIRSLI 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 265 EQMKPLRGRDDDEVKDFLQYLMklkDQEGDSEVpitinhVKALLTDMVV--------GGTDTSTNTIEFAMAELMSNPEL 336
Cdd:cd20640   193 LEIVKEREEECDHEKDLLQAIL---EGARSSCD------KKAEAEDFIVdnckniyfAGHETTAVTAAWCLMLLALHPEW 263
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 337 IKRAQEELDEVVGKDnIVEESHITRLPYILAIMKETLRLHPTLPLlVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPN 416
Cdd:cd20640   264 QDRVRAEVLEVCKGG-PPDADSLSRMKTVTMVIQETLRLYPPAAF-VSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPE 341
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 417 VWeNPT--EFRPERFLDNNSCDFTGAnYSYFPFGSGRRICAG--VALAERMVLytLATLLHSFDWKI-PE-----GHVLD 486
Cdd:cd20640   342 IW-GPDanEFNPERFSNGVAAACKPP-HSYMPFGAGARTCLGqnFAMAELKVL--VSLILSKFSFTLsPEyqhspAFRLI 417

                  ....*....
gi 1032284286 487 LKEKFGIVL 495
Cdd:cd20640   418 VEPEFGVRL 426
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
306-476 1.87e-21

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: 96.80  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 306 ALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPlLVPH 385
Cdd:cd20645   229 AAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVP-FTSR 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 386 RPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFL-DNNSCDftgaNYSYFPFGSGRRICAGVALAERMV 464
Cdd:cd20645   308 TLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLqEKHSIN----PFAHVPFGIGKRMCIGRRLAELQL 383
                         170
                  ....*....|..
gi 1032284286 465 LYTLATLLHSFD 476
Cdd:cd20645   384 QLALCWIIQKYQ 395
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
224-486 4.82e-21

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: 95.12  E-value: 4.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 224 LLSEPNVSDFFPWLARfdlqglvkRMGVCARELDAVLDRAIEQmKPLRGRDDDEVKDFLQYLMKLKDQEGDSEVpiTINH 303
Cdd:cd20616   156 LLIKPDIFFKISWLYK--------KYEKAVKDLKDAIEILIEQ-KRRRISTAEKLEDHMDFATELIFAQKRGEL--TAEN 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 304 VKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGkDNIVEESHITRLPYILAIMKETLRLHPTLPLlV 383
Cdd:cd20616   225 VNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQKLKVLENFINESMRYQPVVDF-V 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 384 PHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPnVWENPTEFRPERFLDNnscdftgANYSYF-PFGSGRRICAGVALAER 462
Cdd:cd20616   303 MRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFEKN-------VPSRYFqPFGFGPRSCVGKYIAMV 374
                         250       260
                  ....*....|....*....|....
gi 1032284286 463 MVLYTLATLLHSFDWKIPEGHVLD 486
Cdd:cd20616   375 MMKAILVTLLRRFQVCTLQGRCVE 398
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
301-501 6.04e-21

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: 95.17  E-value: 6.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 301 INHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELikraQEEL-DEVVGKDNIVEESHITRL---PYILAIMKETLRLH 376
Cdd:cd20643   232 IEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNV----QEMLrAEVLAARQEAQGDMVKMLksvPLLKAAIKETLRLH 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 377 PtLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGanysyFPFGSGRRICAG 456
Cdd:cd20643   308 P-VAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRN-----LGFGFGPRQCLG 381
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1032284286 457 VALAE-RMVLYtLATLLHSFdwKIPEGHVLDLKEKFGIVLKLKIPL 501
Cdd:cd20643   382 RRIAEtEMQLF-LIHMLENF--KIETQRLVEVKTTFDLILVPEKPI 424
PLN02500 PLN02500
cytochrome P450 90B1
21-481 1.24e-20

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 94.93  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  21 VILTTVFSILWYIFKRSPQPSLPPGPRGLPIVG-NLPFLDPDLHTYFANLAQSH----GPIFKLNLGSKLTIVVNSPSLA 95
Cdd:PLN02500   18 ILSLLLVFILTKRRPKQKRFNLPPGNMGWPFLGeTIGYLKPYSATSIGEFMEQHisryGKIYRSNLFGEPTIVSADAGLN 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  96 REILKDQDINFSnrdvplTGRAATYGGIDIVWTPY---GAEWRQLRKICvLKLLSRKTLDSFYelrRKEVRERTRYLYEQ 172
Cdd:PLN02500   98 RFILQNEGRLFE------CSYPRSIGGILGKWSMLvlvGDMHRDMRSIS-LNFLSHARLRTHL---LKEVERHTLLVLDS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 173 GRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTEF----KGVISEITRLLSEPnvsdffpwlARFDLQGLVKR 248
Cdd:PLN02500  168 WKENSTFSAQDEAKKFTFNLMAKHIMSMDPGEEETEQLKKEYvtfmKGVVSAPLNFPGTA---------YRKALKSRATI 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 249 MGVCARELDavlDRaIEQMKplRGRDDDEVKDFLQYLMKLKDqegdsevpITINHVKALLTDMVVGGTDTSTNTIEFAMA 328
Cdd:PLN02500  239 LKFIERKME---ER-IEKLK--EEDESVEEDDLLGWVLKHSN--------LSTEQILDLILSLLFAGHETSSVAIALAIF 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 329 ELMSNPELIKRAQEELDEVVGKDNIVEESHIT-----RLPYILAIMKETLRLHPTLPLLvpHRPA-ENTVVGGYTIPKDT 402
Cdd:PLN02500  305 FLQGCPKAVQELREEHLEIARAKKQSGESELNwedykKMEFTQCVINETLRLGNVVRFL--HRKAlKDVRYKGYDIPSGW 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 403 KIFVNVWSIQRDPNVWENPTEFRPERFLDNN-----SCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDW 477
Cdd:PLN02500  383 KVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNnrggsSGSSSATTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNW 462

                  ....
gi 1032284286 478 KIPE 481
Cdd:PLN02500  463 ELAE 466
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
304-500 9.92e-20

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: 91.44  E-value: 9.92e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 304 VKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPtLPLLV 383
Cdd:cd20644   233 IKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYP-VGITV 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 384 PHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNScdfTGANYSYFPFGSGRRICAGVALAERM 463
Cdd:cd20644   312 QRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRG---SGRNFKHLAFGFGMRQCLGRRLAEAE 388
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1032284286 464 VLYTLATLLHSFdwKIPEGHVLDLKEKFGIVLKLKIP 500
Cdd:cd20644   389 MLLLLMHVLKNF--LVETLSQEDIKTVYSFILRPEKP 423
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
71-482 1.67e-19

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: 91.03  E-value: 1.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  71 QSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDINFSnrdVPLTGRAATYGGIDIVWTPYGAEWRQlRKICVLKLLSRKT 150
Cdd:cd20638    19 QKYGYIYKTHLFGRPTVRVMGAENVRQILLGEHKLVS---VQWPASVRTILGSGCLSNLHDSQHKH-RKKVIMRAFSREA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 151 LDSFYELRRKEVRERTRYLYEQGrkqSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTEFKGVISEITRLLSEPNV 230
Cdd:cd20638    95 LENYVPVIQEEVRSSVNQWLQSG---PCVLVYPEVKRLMFRIAMRILLGFEPQQTDREQEQQLVEAFEEMIRNLFSLPID 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 231 SDFfpwlarfdlQGLVKrmGVCAREldaVLDRAIEQ---MKPLRGRDDDEVKDFLQYLMKLKDQEGDsevPITINHVKAL 307
Cdd:cd20638   172 VPF---------SGLYR--GLRARN---LIHAKIEEnirAKIQREDTEQQCKDALQLLIEHSRRNGE---PLNLQALKES 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 308 LTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDE--VVGKDNiVEESHIT-----RLPYILAIMKETLRLHPTLP 380
Cdd:cd20638   235 ATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEkgLLSTKP-NENKELSmevleQLKYTGCVIKETLRLSPPVP 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 381 llVPHRPAENT-VVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLdnNSCDFTGANYSYFPFGSGRRICAGVAL 459
Cdd:cd20638   314 --GGFRVALKTfELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFM--SPLPEDSSRFSFIPFGGGSRSCVGKEF 389
                         410       420
                  ....*....|....*....|...
gi 1032284286 460 AERMVLYTLATLLHSFDWKIPEG 482
Cdd:cd20638   390 AKVLLKIFTVELARHCDWQLLNG 412
PLN02290 PLN02290
cytokinin trans-hydroxylase
173-502 2.67e-19

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 90.64  E-value: 2.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 173 GRKQSPVKVGDQlfltMMNLTMNML----WGGSV-KAEEMESVGTEFKGVISEITRLLSEPNvSDFFPWLARFDLQGLVK 247
Cdd:PLN02290  191 ESGQTEVEIGEY----MTRLTADIIsrteFDSSYeKGKQIFHLLTVLQRLCAQATRHLCFPG-SRFFPSKYNREIKSLKG 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 248 rmgvcarELDAVLDRAIEQMKPL--RGRDDDEVKDFLQYLMKLKDQEGDSEVPITINHVKALLTDMVVGGTDTSTNTIEF 325
Cdd:PLN02290  266 -------EVERLLMEIIQSRRDCveIGRSSSYGDDLLGMLLNEMEKKRSNGFNLNLQLIMDECKTFFFAGHETTALLLTW 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 326 AMAELMSNPELIKRAQEELDEVVGkDNIVEESHITRLPYILAIMKETLRLHPTLPLLvPHRPAENTVVGGYTIPKDTKIF 405
Cdd:PLN02290  339 TLMLLASNPTWQDKVRAEVAEVCG-GETPSVDHLSKLTLLNMVINESLRLYPPATLL-PRMAFEDIKLGDLHIPKGLSIW 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 406 VNVWSIQRDPNVW-ENPTEFRPERFldnNSCDFTGANYsYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEGH- 483
Cdd:PLN02290  417 IPVLAIHHSEELWgKDANEFNPDRF---AGRPFAPGRH-FIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDNYr 492
                         330       340
                  ....*....|....*....|....
gi 1032284286 484 -----VLDLKEKFGIVLKLKiPLV 502
Cdd:PLN02290  493 hapvvVLTIKPKYGVQVCLK-PLN 515
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
19-477 3.40e-19

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 90.42  E-value: 3.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  19 AIVILTTVFSILWYIFKRSPQP---SLPPGPRGLPIVGNL-------------PFLDPDLHTYfanlaqshGPIFKLNLG 82
Cdd:PLN02987    5 AFLLLLSSLAAIFFLLLRRTRYrrmRLPPGSLGLPLVGETlqlisayktenpePFIDERVARY--------GSLFMTHLF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  83 SKLTIVVNSPSLAREILKDQDINFSnrdvpltgraATYGGidivwtpygaewrqlrKICvlKLLSRKTLdsfyELRRKEV 162
Cdd:PLN02987   77 GEPTVFSADPETNRFILQNEGKLFE----------CSYPG----------------SIS--NLLGKHSL----LLMKGNL 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 163 RERTRYLYEQGRKQSPVKvgDQLFLTMMNLTMNMLWGGSVKAEEMEsvgtEFKGVISEIT--RLLS-EPN---------- 229
Cdd:PLN02987  125 HKKMHSLTMSFANSSIIK--DHLLLDIDRLIRFNLDSWSSRVLLME----EAKKITFELTvkQLMSfDPGewteslrkey 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 230 ---VSDFFPwlARFDLQGLVKRMGVCAR-ELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDQEGDSEVpitINHVK 305
Cdd:PLN02987  199 vlvIEGFFS--VPLPLFSTTYRRAIQARtKVAEALTLVVMKRRKEEEEGAEKKKDMLAALLASDDGFSDEEI---VDFLV 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 306 ALLtdmvVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGK---DNIVEESHITRLPYILAIMKETLRLHPTLPLL 382
Cdd:PLN02987  274 ALL----VAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMksdSYSLEWSDYKSMPFTQCVVNETLRVANIIGGI 349
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 383 VpHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCdfTGANYSYFPFGSGRRICAGVALAER 462
Cdd:PLN02987  350 F-RRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGT--TVPSNVFTPFGGGPRLCPGYELARV 426
                         490
                  ....*....|....*
gi 1032284286 463 MVLYTLATLLHSFDW 477
Cdd:PLN02987  427 ALSVFLHRLVTRFSW 441
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
220-475 3.74e-18

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: 86.56  E-value: 3.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 220 EITRLLSEPNVSDFFPWLaRFDLQGLVKRMGVCARELDAVLDRAIEQ-MKPLR-GRDDDEvkDFLQYLmkLKDQEGDSEV 297
Cdd:cd20642   148 EQGELIIQALRKVYIPGW-RFLPTKRNRRMKEIEKEIRSSLRGIINKrEKAMKaGEATND--DLLGIL--LESNHKEIKE 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 298 PITINhvKALLTDMVVG--------GTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEEShITRLPYILAIM 369
Cdd:cd20642   223 QGNKN--GGMSTEDVIEecklfyfaGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKPDFEG-LNHLKVVTMIL 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 370 KETLRLHPTLPLLVPHrPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFLDNNScDFTGANYSYFPFG 448
Cdd:cd20642   300 YEVLRLYPPVIQLTRA-IHKDTKLGDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFAEGIS-KATKGQVSYFPFG 377
                         250       260       270
                  ....*....|....*....|....*....|
gi 1032284286 449 SGRRICAG--VALAE-RMVlytLATLLHSF 475
Cdd:cd20642   378 WGPRICIGqnFALLEaKMA---LALILQRF 404
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
304-482 3.94e-18

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: 85.99  E-value: 3.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 304 VKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEEldevvgkdniveESHITRlpyilaIMKETLRLHPtlPL-L 382
Cdd:cd11080   194 IKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRAD------------RSLVPR------AIAETLRYHP--PVqL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 383 VPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGANySYFPFGSGRRICAGVALAER 462
Cdd:cd11080   254 IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREDLGIRSAFSGAA-DHLAFGSGRHFCVGAALAKR 332
                         170       180
                  ....*....|....*....|.
gi 1032284286 463 MVLYTLATLLHSF-DWKIPEG 482
Cdd:cd11080   333 EIEIVANQVLDALpNIRLEPG 353
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
257-473 4.54e-18

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: 86.67  E-value: 4.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 257 DAVLDraiEQMKPLRGRDDDE---------VKDFLQYLMKLKDQEGDSevpITINHVKALLTDMVVGGTDTSTNTIEFAM 327
Cdd:cd20679   195 DAVIQ---ERRRTLPSQGVDDflkakakskTLDFIDVLLLSKDEDGKE---LSDEDIRAEADTFMFEGHDTTASGLSWIL 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 328 AELMSNPELIKRAQEELDEVVgKDNIVEE---SHITRLPYILAIMKETLRLHPTLPLlVPHRPAENTVV-GGYTIPKDTK 403
Cdd:cd20679   269 YNLARHPEYQERCRQEVQELL-KDREPEEiewDDLAQLPFLTMCIKESLRLHPPVTA-ISRCCTQDIVLpDGRVIPKGII 346
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1032284286 404 IFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDftGANYSYFPFGSGRRICAG--VALAERMVLYTLaTLLH 473
Cdd:cd20679   347 CLISIYGTHHNPTVWPDPEVYDPFRFDPENSQG--RSPLAFIPFSAGPRNCIGqtFAMAEMKVVLAL-TLLR 415
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
135-479 4.63e-17

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: 83.34  E-value: 4.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 135 RQLRKIcVLKLLSRKTLDSFYELRRKEVRERTRYLYEQGrkqSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTEF 214
Cdd:cd20636    81 RQRRKV-LARVFSRAALESYLPRIQDVVRSEVRGWCRGP---GPVAVYTAAKSLTFRIAVRILLGLRLEEQQFTYLAKTF 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 215 KGVISEITRLLSEPNVSdffpwlarfdlqGLvkRMGVCARE-LDAVLDRAIEQmkPLRGRDDDEVKDFLQYLMKlKDQEG 293
Cdd:cd20636   157 EQLVENLFSLPLDVPFS------------GL--RKGIKARDiLHEYMEKAIEE--KLQRQQAAEYCDALDYMIH-SAREN 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 294 DSEvpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELD-EVVGKD-----NIVEESHITRLPYILA 367
Cdd:cd20636   220 GKE--LTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVsHGLIDQcqccpGALSLEKLSRLRYLDC 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 368 IMKETLRLHPtlPLLVPHRPAENTV-VGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGaNYSYFP 446
Cdd:cd20636   298 VVKEVLRLLP--PVSGGYRTALQTFeLDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSG-RFNYIP 374
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1032284286 447 FGSGRRICAGVALAErMVLYTLAT-LLHSFDWKI 479
Cdd:cd20636   375 FGGGVRSCIGKELAQ-VILKTLAVeLVTTARWEL 407
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
271-486 5.45e-17

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 83.52  E-value: 5.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 271 RGRDDDEVKDFLQYLMKLKDQEGDSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGK 350
Cdd:PLN02169  269 RAETEPYSKDALTYYMNVDTSKYKLLKPKKDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKFDN 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 351 DNIveeshiTRLPYILAIMKETLRLHPTLPL--LVPHRPaeNTVVGGYTIPKDTKIFVNVWSIQRDPNVW-ENPTEFRPE 427
Cdd:PLN02169  349 EDL------EKLVYLHAALSESMRLYPPLPFnhKAPAKP--DVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPE 420
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1032284286 428 RFLDNNSCDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPEGHVLD 486
Cdd:PLN02169  421 RWISDNGGLRHEPSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNYDFKVIEGHKIE 479
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
326-476 1.23e-16

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: 81.97  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 326 AMAELMSNPELIKRAQEELDEVVG---KDNI-VEESHITRLPYILAIMKETLRLHPtlPLLVPHRPAENTVVGGYTIPKD 401
Cdd:cd20635   233 TLAFILSHPSVYKKVMEEISSVLGkagKDKIkISEDDLKKMPYIKRCVLEAIRLRS--PGAITRKVVKPIKIKNYTIPAG 310
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032284286 402 TKIFVNVWSIQRDPNVWENPTEFRPERFLDnnsCDFTGANY--SYFPFGSGRRICAG--VALAErMVLYtLATLLHSFD 476
Cdd:cd20635   311 DMLMLSPYWAHRNPKYFPDPELFKPERWKK---ADLEKNVFleGFVAFGGGRYQCPGrwFALME-IQMF-VAMFLYKYD 384
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
317-478 2.15e-16

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: 81.14  E-value: 2.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 317 DTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDniveESHIT-----RLPYILAIMKETLRLHPTLPLlVPHRPAENT 391
Cdd:cd11082   234 DASTSSLVWALQLLADHPDVLAKVREEQARLRPND----EPPLTldlleEMKYTRQVVKEVLRYRPPAPM-VPHIAKKDF 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 392 VVG-GYTIPKDTKIFVNVWSIQRDPnvWENPTEFRPERFLDNNSCDFTGANySYFPFGSGRRICAGVALAERMVLYTLAT 470
Cdd:cd11082   309 PLTeDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQEDRKYKK-NFLVFGAGPHQCVGQEYAINHLMLFLAL 385

                  ....*...
gi 1032284286 471 LLHSFDWK 478
Cdd:cd11082   386 FSTLVDWK 393
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
253-481 2.17e-16

fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 monooxygenase TRI13, also called core trichothecene cluster (CTC) protein 13, and similar proteins. The tri13 gene is located in the trichothecene biosynthesis gene cluster in Fusarium species, which produce a great diversity of agriculturally important trichothecene toxins that differ from each other in their pattern of oxygenation and esterification. Trichothecenes comprise a large family of chemically related bicyclic sesquiterpene compounds acting as mycotoxins, including the T2-toxin; TRI13 is required for the addition of the C-4 oxygen of T-2 toxin. The TRI13-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 81.58  E-value: 2.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 253 ARELDAVLDRAIEQMKPLRGRDDDE------VKDFLQYLMKLKDQEGDSevpitINHVKALLTD----MVVGGTDTSTNT 322
Cdd:cd20622   207 AKIKDDFLQREIQAIARSLERKGDEgevrsaVDHMVRRELAAAEKEGRK-----PDYYSQVIHDelfgYLIAGHDTTSTA 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 323 IEFAMAELMSNPELIKRAQEELDEVV------GKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVphRPA-ENTVVGG 395
Cdd:cd20622   282 LSWGLKYLTANQDVQSKLRKALYSAHpeavaeGRLPTAQEIAQARIPYLDAVIEEILRCANTAPILS--REAtVDTQVLG 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 396 YTIPKDTKIFVNVW-------SIQRD--------------PNVWENPT--EFRPERFL----DNNSCDFTGANYSYFPFG 448
Cdd:cd20622   360 YSIPKGTNVFLLNNgpsylspPIEIDesrrssssaakgkkAGVWDSKDiaDFDPERWLvtdeETGETVFDPSAGPTLAFG 439
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1032284286 449 SGRRICAGVALAERMVLYTLATLLHSFDW-KIPE 481
Cdd:cd20622   440 LGPRGCFGRRLAYLEMRLIITLLVWNFELlPLPE 473
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
240-460 2.26e-16

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: 80.95  E-value: 2.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 240 FDLQGLVKRMGVCARE-LDAVLDRAIEQmkpLRGRDDDevKDFLQYLMKLKDQEGD--SEVPITINhvkalLTDMVVGGT 316
Cdd:cd20614   152 VDLPGMPARRSRRARAwIDARLSQLVAT---ARANGAR--TGLVAALIRARDDNGAglSEQELVDN-----LRLLVLAGH 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 317 DTSTNTIEFAMAELMSNPELIKRAqeeLDEVVGKDNI-VEESHITRLPYILAIMKETLRLHPTLPLlVPHRPAENTVVGG 395
Cdd:cd20614   222 ETTASIMAWMVIMLAEHPAVWDAL---CDEAAAAGDVpRTPAELRRFPLAEALFRETLRLHPPVPF-VFRRVLEEIELGG 297
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1032284286 396 YTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNnscdfTGA--NYSYFPFGSGRRICAGVALA 460
Cdd:cd20614   298 RRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGR-----DRApnPVELLQFGGGPHFCLGYHVA 359
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
255-463 1.07e-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: 72.64  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 255 ELDAVLDRAIEQMKplrgrdDDEVKDFLQYLMKLKDQEGDsevPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNP 334
Cdd:cd11078   170 ELWAYFADLVAERR------REPRDDLISDLLAAADGDGE---RLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHP 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 335 ELIKRAQEELdevvgkdniveeshiTRLPyilAIMKETLRLHPtlPLLVPHRPA-ENTVVGGYTIPKDTKIFVNVWSIQR 413
Cdd:cd11078   241 DQWRRLRADP---------------SLIP---NAVEETLRYDS--PVQGLRRTAtRDVEIGGVTIPAGARVLLLFGSANR 300
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032284286 414 DPNVWENPTEFRPERfldnnscDFTGANYSyfpFGSGRRICAGVALAeRM 463
Cdd:cd11078   301 DERVFPDPDRFDIDR-------PNARKHLT---FGHGIHFCLGAALA-RM 339
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
314-493 5.17e-13

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: 70.94  E-value: 5.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 314 GGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLVpHRPAENTVV 393
Cdd:cd20641   246 AGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVINIA-RRASEDMKL 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 394 GGYTIPKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFLDNNSCDFTGANySYFPFGSGRRICAGVALAERMVLYTLATLL 472
Cdd:cd20641   325 GGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHPN-ALLSFSLGPRACIGQNFAMIEAKTVLAMIL 403
                         170       180
                  ....*....|....*....|....*..
gi 1032284286 473 HSF------DWKIPEGHVLDLKEKFGI 493
Cdd:cd20641   404 QRFsfslspEYVHAPADHLTLQPQYGL 430
PLN02774 PLN02774
brassinosteroid-6-oxidase
241-475 9.60e-13

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 70.19  E-value: 9.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 241 DLQGLVKRMGVCAREldaVLDRAIEQMKPLRgRDDDEV-KDFLQYLMKLKDQEgdseVPITINHVKALLTDMVVGGTDTS 319
Cdd:PLN02774  209 DLPGTNYRSGVQARK---NIVRMLRQLIQER-RASGEThTDMLGYLMRKEGNR----YKLTDEEIIDQIITILYSGYETV 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 320 TNTIEFAMAELMSNPELIKRAQEE---LDEVVGKDNIVEESHITRLPYILAIMKETLRLhPTLPLLVPHRPAENTVVGGY 396
Cdd:PLN02774  281 STTSMMAVKYLHDHPKALQELRKEhlaIRERKRPEDPIDWNDYKSMRFTRAVIFETSRL-ATIVNGVLRKTTQDMELNGY 359
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032284286 397 TIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNscdFTGANYsYFPFGSGRRICAGVALAermvLYTLATLLHSF 475
Cdd:PLN02774  360 VIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKS---LESHNY-FFLFGGGTRLCPGKELG----IVEISTFLHYF 430
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
259-483 2.76e-12

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 69.04  E-value: 2.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 259 VLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDqegDSEVPITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIK 338
Cdd:PLN03195  251 VIRRRKAEMDEARKSGKKVKHDILSRFIELGE---DPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAE 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 339 RAQEEL---DEVVGKDNIVEESH-----------------ITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVVGGYTI 398
Cdd:PLN03195  328 KLYSELkalEKERAKEEDPEDSQsfnqrvtqfaglltydsLGKLQYLHAVITETLRLYPAVPQDPKGILEDDVLPDGTKV 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 399 PKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFLDNNScdFTGAN-YSYFPFGSGRRICAGVALAERMVLYTLATLLHSFD 476
Cdd:PLN03195  408 KAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDGV--FQNASpFKFTAFQAGPRICLGKDSAYLQMKMALALLCRFFK 485

                  ....*..
gi 1032284286 477 WKIPEGH 483
Cdd:PLN03195  486 FQLVPGH 492
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
202-475 4.06e-12

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 67.84  E-value: 4.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 202 VKAEEMESVGTEFKGVIS--EITRLLSEPNVSD--FFPW---LARFDLQGLVKRMGVCARE-LDAVLDRaIEQMKPLRGR 273
Cdd:cd20630   100 LGEPEEFDVIREIAEHIPfrVISAMLGVPAEWDeqFRRFgtaTIRLLPPGLDPEELETAAPdVTEGLAL-IEEVIAERRQ 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 274 DDDEvKDFLQYLMKLKDQ-EGDSEvpitiNHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEE-------LD 345
Cdd:cd20630   179 APVE-DDLLTTLLRAEEDgERLSE-----DELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEpellrnaLE 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 346 EVVGKDNIVEEShitrlpyilaimkeTLRLHPtlpllvphrpaENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFR 425
Cdd:cd20630   253 EVLRWDNFGKMG--------------TARYAT-----------EDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFD 307
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1032284286 426 PERflDNNScDFTganysyfpFGSGRRICAGVALAERMVLYTLATLLHSF 475
Cdd:cd20630   308 VRR--DPNA-NIA--------FGYGPHFCIGAALARLELELAVSTLLRRF 346
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
35-507 4.77e-12

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 67.84  E-value: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  35 KRSPQPSLPPGPRGLPIVG-NLPFL----DPDLHTYFANLAQSHGPIFKLNLGSKLTIVVNSPSLAREILKdqdiNFSNR 109
Cdd:PLN03141    1 SSKKKSRLPKGSLGWPVIGeTLDFIscaySSRPESFMDKRRSLYGKVFKSHIFGTPTIVSTDAEVNKVVLQ----SDGNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 110 DVPltgraatyggidivWTPygaewRQLRKI----CVLKL---LSRKT---LDSFY---ELRRKEVRERTRYLYE---QG 173
Cdd:PLN03141   77 FVP--------------AYP-----KSLTELmgksSILLIngsLQRRVhglIGAFLkspHLKAQITRDMERYVSEsldSW 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 174 RKQSPVKVGDQlfltMMNLTMNMLwggsVKA-------EEMESVGTEFKGVISEITRL-LSEPNVSDFFPWLARFDLQGL 245
Cdd:PLN03141  138 RDDPPVLVQDE----TKKIAFEVL----VKAlislepgEEMEFLKKEFQEFIKGLMSLpIKLPGTRLYRSLQAKKRMVKL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 246 VKRmgvcareldaVLDRAIEQMKPLRGRDDDEVKDFLQYLMKlkdqegDSEVPITINHVKALLTDMVVGGTDTSTNTIEF 325
Cdd:PLN03141  210 VKK----------IIEEKRRAMKNKEEDETGIPKDVVDVLLR------DGSDELTDDLISDNMIDMMIPGEDSVPVLMTL 273
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 326 AMAELMSNPELIKRAQEELDEV-VGKDNIVEESHIT---RLPYILAIMKETLRLHPTLpLLVPHRPAENTVVGGYTIPKD 401
Cdd:PLN03141  274 AVKFLSDCPVALQQLTEENMKLkRLKADTGEPLYWTdymSLPFTQNVITETLRMGNII-NGVMRKAMKDVEIKGYLIPKG 352
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 402 TKIFVNVWSIQRDPNVWENPTEFRPERFLDNNscdftGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKIPE 481
Cdd:PLN03141  353 WCVLAYFRSVHLDEENYDNPYQFNPWRWQEKD-----MNNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFRWVAEE 427
                         490       500
                  ....*....|....*....|....*..
gi 1032284286 482 GHVLDlkekFGIV-LKLKIPLVALPIP 507
Cdd:PLN03141  428 DTIVN----FPTVrMKRKLPIWVTRID 450
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
71-474 4.78e-12

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: 67.95  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  71 QSHGPIFKLNLGSKLTIVVNSPSLAREILKDQDiNFSNRDVPLTGRaaTYGGIDIVWTPYGAEWRQLRKIcVLKLLSRKT 150
Cdd:cd20637    19 EKYGNVFKTHLLGRPLIRVTGAENVRKILMGEH-SLVSTEWPRSTR--MLLGPNSLVNSIGDIHRHKRKV-FSKLFSHEA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 151 LDSFYELRRKEVRERTRylyEQGRKQSPVKVGDQLFLTMMNLTMNMLWGGSVKAEEMESVGTEFKGVISEITRLLSEPNV 230
Cdd:cd20637    95 LESYLPKIQQVIQDTLR---VWSSNPEPINVYQEAQKLTFRMAIRVLLGFRVSEEELSHLFSVFQQFVENVFSLPLDLPF 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 231 SDFfpwlarfdlqglvkRMGVCARE-LDAVLDRAIEQmKPLRGRDddevKDFLQYLMKLKDQEGDSEVPITINHVKALLT 309
Cdd:cd20637   172 SGY--------------RRGIRARDsLQKSLEKAIRE-KLQGTQG----KDYADALDILIESAKEHGKELTMQELKDSTI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 310 DMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEEL--DEVVGKDNIVEES----HITRLPYILAIMKETLRLHPtlPLLV 383
Cdd:cd20637   233 ELIFAAFATTASASTSLIMQLLKHPGVLEKLREELrsNGILHNGCLCEGTlrldTISSLKYLDCVIKEVLRLFT--PVSG 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 384 PHRPAENTV-VGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGaNYSYFPFGSGRRICAGVALAeR 462
Cdd:cd20637   311 GYRTALQTFeLDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDG-RFHYLPFGGGVRTCLGKQLA-K 388
                         410
                  ....*....|..
gi 1032284286 463 MVLYTLATLLHS 474
Cdd:cd20637   389 LFLKVLAVELAS 400
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
374-481 1.80e-11

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: 66.01  E-value: 1.80e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 374 RLHPTLPLlVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFT-----GANYSyfpfg 448
Cdd:cd11067   274 RFYPFFPF-VGARARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGDPFDfipqgGGDHA----- 347
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1032284286 449 SGRRiCAGVALAERMVLYTLATLLHSFDWKIPE 481
Cdd:cd11067   348 TGHR-CPGEWITIALMKEALRLLARRDYYDVPP 379
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
203-483 2.36e-11

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


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 65.01  E-value: 2.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 203 KAEEMESVGTEFKGVIseITRLLSEPnvSDFFPWLAR----------FDLQGLVKRMGVCARELDAVLDRAIEQmkplRG 272
Cdd:cd20629    96 RADLVEDFALELPARV--IYALLGLP--EEDLPEFTRlalamlrglsDPPDPDVPAAEAAAAELYDYVLPLIAE----RR 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 273 RDDDEvkDFLQYLMKLKDQEGDsevpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPELIK--RAQEELdevvgk 350
Cdd:cd20629   168 RAPGD--DLISRLLRAEVEGEK----LDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLErvRRDRSL------ 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 351 dniveeshitrlpyILAIMKETLRLHPTLpLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWEnptefRPERFl 430
Cdd:cd20629   236 --------------IPAAIEEGLRWEPPV-ASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYP-----DPDVF- 294
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032284286 431 dnnscDFTGANYSYFPFGSGRRICAGVALAeRMVLYT-LATLLHSF-------DWKIPEGH 483
Cdd:cd20629   295 -----DIDRKPKPHLVFGGGAHRCLGEHLA-RVELREaLNALLDRLpnlrldpDAPAPEIS 349
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
239-481 7.46e-11

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: 63.53  E-value: 7.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 239 RFDLQGLVKRMGVCARELDavlDRAIEQMKPLRGRDDDEVKDFLQYLMKlkdqEGDSEVPITINHVKALLTDMVVGGTDT 318
Cdd:cd11079   126 AATRSGDRAATAEVAEEFD---GIIRDLLADRRAAPRDADDDVTARLLR----ERVDGRPLTDEEIVSILRNWTVGELGT 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 319 STNTIEFAMAELMSNPELIKRAQEELDEvvgkdniveeshitrlpyILAIMKETLRLHPtlPLLVPHR-PAENTVVGGYT 397
Cdd:cd11079   199 IAACVGVLVHYLARHPELQARLRANPAL------------------LPAAIDEILRLDD--PFVANRRiTTRDVELGGRT 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 398 IPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNscdftganysyFPFGSGRRICAGVALAeRMVL-YTLATLLHSFD 476
Cdd:cd11079   259 IPAGSRVTLNWASANRDERVFGDPDEFDPDRHAADN-----------LVYGRGIHVCPGAPLA-RLELrILLEELLAQTE 326

                  ....*
gi 1032284286 477 WKIPE 481
Cdd:cd11079   327 AITLA 331
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
254-479 7.89e-11

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 64.19  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 254 RELDAVLDRAIEQMKPLRGRDDDEVKDFLQylmklkDQEGDSEVPITINhvkalLTDMVVGGTDTSTNTIEFAMAELMSN 333
Cdd:PLN02196  226 KELAQILAKILSKRRQNGSSHNDLLGSFMG------DKEGLTDEQIADN-----IIGVIFAARDTTASVLTWILKYLAEN 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 334 PELIKRAQEELDEVVgKDNIVEES----HITRLPYILAIMKETLRLHPTLPLLVpHRPAENTVVGGYTIPKDTKIFVNVW 409
Cdd:PLN02196  295 PSVLEAVTEEQMAIR-KDKEEGESltweDTKKMPLTSRVIQETLRVASILSFTF-REAVEDVEYEGYLIPKGWKVLPLFR 372
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 410 SIQRDPNVWENPTEFRPERFldnnscDFTGANYSYFPFGSGRRICAGVALAERMVLYTLATLLHSFDWKI 479
Cdd:PLN02196  373 NIHHSADIFSDPGKFDPSRF------EVAPKPNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSI 436
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
88-502 1.03e-10

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: 63.38  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  88 VVNSPSLAREILKDQDInFSNRDVPLTGRAatygGIDIVWTPY---GAEWRQLRKIcVLKLLSRKTLdsfyELRRKEVRE 164
Cdd:cd11035    17 IVTRGEDIREVLRDPET-FSSRVITVPPPA----GEPYPLIPLeldPPEHTRYRRL-LNPLFSPKAV----AALEPRIRE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 165 RTRYLYEQ--GRKQSPVkVGD-------QLFLTMMNLTMNMLwggsvkaeemesvgTEFKGVISEITRLlsepnvsdffp 235
Cdd:cd11035    87 RAVELIESfaPRGECDF-VADfaepfptRVFLELMGLPLEDL--------------DRFLEWEDAMLRP----------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 236 wlarfdlQGLVKRMGvCARELDAVLDRAIEQmkplrgRDDDEVKDFLQYLMKlkdqegdSEV---PITINHVKALLTDMV 312
Cdd:cd11035   141 -------DDAEERAA-AAQAVLDYLTPLIAE------RRANPGDDLISAILN-------AEIdgrPLTDDELLGLCFLLF 199
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 313 VGGTDTSTNTIEFAMAELMSNPELikRAQeeldevvgkdnIVEESHItrlpyILAIMKETLRLHPtlPLLVPHRPAENTV 392
Cdd:cd11035   200 LAGLDTVASALGFIFRHLARHPED--RRR-----------LREDPEL-----IPAAVEELLRRYP--LVNVARIVTRDVE 259
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 393 VGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERfldnnscdftgANYSYFPFGSGRRICAGVALAeRMvlyTLATLL 472
Cdd:cd11035   260 FHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR-----------KPNRHLAFGAGPHRCLGSHLA-RL---ELRIAL 324
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1032284286 473 HSFDWKIPEGHV---LDLKEKFGIVLKLK-IPLV 502
Cdd:cd11035   325 EEWLKRIPDFRLapgAQPTYHGGSVMGLEsLPLV 358
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
326-476 1.45e-10

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: 62.86  E-value: 1.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 326 AMAELMSNPELIKRAQEELDEVVGKdniveeshiTRLPYILAIMKETLRLHPTLPLLVpHRPAENTVVGGYTIPKDTKIF 405
Cdd:cd20624   214 ALALLAAHPEQAARAREEAAVPPGP---------LARPYLRACVLDAVRLWPTTPAVL-RESTEDTVWGGRTVPAGTGFL 283
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1032284286 406 VNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTGanysYFPFGSGRRICAGvalaERMVLYT----LATLLHSFD 476
Cdd:cd20624   284 IFAPFFHRDDEALPFADRFVPEIWLDGRAQPDEG----LVPFSAGPARCPG----ENLVLLVastaLAALLRRAE 350
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
233-476 9.49e-10

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: 60.29  E-value: 9.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 233 FFPW-LARFDLQG-LVKRMGVCARELDAVLDRAIEQMKPLRGRDDDevkdFLQYLMKLKDqEGDsevpITINHVKALLTD 310
Cdd:cd11037   139 LLPWaAATFNAFGpLNERTRAALPRLKELRDWVAEQCARERLRPGG----WGAAIFEAAD-RGE----ITEDEAPLLMRD 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 311 MVVGGTDTSTNTIEFAM----------AELMSNPELIKRAqeeLDEVVgkdniveeshitRLpyilaimkETlrlhptlP 380
Cdd:cd11037   210 YLSAGLDTTISAIGNALwllarhpdqwERLRADPSLAPNA---FEEAV------------RL--------ES-------P 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 381 LLVPHR-PAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERfldnNSCDFTGanysyfpFGSGRRICAGVAL 459
Cdd:cd11037   260 VQTFSRtTTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR----NPSGHVG-------FGHGVHACVGQHL 328
                         250       260
                  ....*....|....*....|.
gi 1032284286 460 AeRM----VLYTLATLLHSFD 476
Cdd:cd11037   329 A-RLegeaLLTALARRVDRIE 348
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
190-460 1.49e-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: 59.69  E-value: 1.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 190 MNLTMNMLWGGSVKAEEMESVG---TEFKGVIseITRLLSEP--NVSDFFPWLARFDLQglvkrMGVCARELDAVLDRAI 264
Cdd:cd11038   102 FRATANDLIDGFAEGGECEFVEafaEPYPARV--ICTLLGLPeeDWPRVHRWSADLGLA-----FGLEVKDHLPRIEAAV 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 265 EQM-----KPLRGRDDDEVKDFLQYLMKlKDQEGDSevpITINHVKALLTDMVVGGTDTSTNTIEFAMAELMSNPE---L 336
Cdd:cd11038   175 EELydyadALIEARRAEPGDDLISTLVA-AEQDGDR---LSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDqwrA 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 337 IkRAQEELDEvvgkdNIVEEshitrlpyilaimkeTLRLHPTLPLLVphRPA-ENTVVGGYTIPKDTKIFVNVWSIQRDP 415
Cdd:cd11038   251 L-REDPELAP-----AAVEE---------------VLRWCPTTTWAT--REAvEDVEYNGVTIPAGTVVHLCSHAANRDP 307
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1032284286 416 NVwenpteFRPERFldnnscDFTGANYSYFPFGSGRRICAGVALA 460
Cdd:cd11038   308 RV------FDADRF------DITAKRAPHLGFGGGVHHCLGAFLA 340
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
330-456 1.71e-09

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: 60.08  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 330 LMSNPELIKRAQEELDEVVGK-----DNIVEESHITR-----LPYILAIMKETLRLhPTLPLLVphRPA-ENTVV----- 393
Cdd:cd20631   254 LLRCPEAMKAATKEVKRTLEKtgqkvSDGGNPIVLTReqlddMPVLGSIIKEALRL-SSASLNI--RVAkEDFTLhldsg 330
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 394 GGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNSCDFTG-------ANYSYFPFGSGRRICAG 456
Cdd:cd20631   331 ESYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTfykngrkLKYYYMPFGSGTSKCPG 400
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
255-488 1.86e-09

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: 59.45  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 255 ELDAVLDRAIEQMKplrGRDDDEvKDFLQYLM--KLKDQEgdsevpitinhvkaLLTDMVV---GGTDTSTNTIEFAMAE 329
Cdd:cd20627   167 EMESVLKKVIKERK---GKNFSQ-HVFIDSLLqgNLSEQQ--------------VLEDSMIfslAGCVITANLCTWAIYF 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 330 LMSNPELIKRAQEELDEVVGKDNIVEEShITRLPYILAIMKETLRLHPTLPLLVPHRPAENTVvGGYTIPKDTKIFVNVW 409
Cdd:cd20627   229 LTTSEEVQKKLYKEVDQVLGKGPITLEK-IEQLRYCQQVLCETVRTAKLTPVSARLQELEGKV-DQHIIPKETLVLYALG 306
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1032284286 410 SIQRDPNVWENPTEFRPERFLDNNSCDftgaNYSYFPFgSGRRICAGVALAERMVLYTLATLLHSFDWKIPEGHVLDLK 488
Cdd:cd20627   307 VVLQDNTTWPLPYRFDPDRFDDESVMK----SFSLLGF-SGSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQVMETK 380
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
306-475 2.49e-09

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


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 59.12  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 306 ALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVvgkDNIVEEShitrlpyilaimketLRLHPTLPL-LVP 384
Cdd:cd11031   209 TLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRADPELV---PAAVEEL---------------LRYIPLGAGgGFP 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 385 HRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERflDNNscdftganySYFPFGSGRRICAGVALAeRMV 464
Cdd:cd11031   271 RYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDR--EPN---------PHLAFGHGPHHCLGAPLA-RLE 338
                         170
                  ....*....|..
gi 1032284286 465 LYT-LATLLHSF 475
Cdd:cd11031   339 LQVaLGALLRRL 350
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
227-482 2.88e-09

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: 58.89  E-value: 2.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 227 EPNVSDFFPWLARFDLQGLVKR-MGV----CARELDAVLDRAIEQMKPLRGRDDDEVKDFLQYLMKLKDQEG-------- 293
Cdd:cd11034    97 ERGECDLVTELANPLPARLTLRlLGLpdedGERLRDWVHAILHDEDPEEGAAAFAELFGHLRDLIAERRANPrddlisrl 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 294 -DSEV---PITINHVKALLTDMVVGGTDTSTNTIEFAM----------AELMSNPELIKRAQEELdevvgkdniveeshi 359
Cdd:cd11034   177 iEGEIdgkPLSDGEVIGFLTLLLLGGTDTTSSALSGALlwlaqhpedrRRLIADPSLIPNAVEEF--------------- 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 360 trlpyilaimketLRLH-PTLPLlvPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFldnnscdft 438
Cdd:cd11034   242 -------------LRFYsPVAGL--ARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRT--------- 297
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1032284286 439 gaNYSYFPFGSGRRICAGVALAERMVLYTLATLLHSF-DWKIPEG 482
Cdd:cd11034   298 --PNRHLAFGSGVHRCLGSHLARVEARVALTEVLKRIpDFELDPG 340
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
312-485 3.66e-09

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 58.27  E-value: 3.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 312 VVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVvgkDNIVEEshitrlpyilaimkeTLRLHPtlPLLVPHR-PAEN 390
Cdd:cd11036   186 AVQGAEAAAGLVGNAVLALLRRPAQWARLRPDPELA---AAAVAE---------------TLRYDP--PVRLERRfAAED 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 391 TVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERfldnnscdftgANYSYFPFGSGRRICAGVALAERMVLYTLAT 470
Cdd:cd11036   246 LELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR-----------PTARSAHFGLGRHACLGAALARAAAAAALRA 314
                         170
                  ....*....|....*
gi 1032284286 471 LLHSFDWKIPEGHVL 485
Cdd:cd11036   315 LAARFPGLRAAGPVV 329
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
333-432 4.77e-09

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: 58.43  E-value: 4.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 333 NPELIKRAQEELDEVVGKDNIVEESHITRLPYILAIMKETLRLHPTLPLLvpHRPA-ENTVV----GGYTIPKDTKIFVN 407
Cdd:cd11071   256 GEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPLQ--YGRArKDFVIeshdASYKIKKGELLVGY 333
                          90       100
                  ....*....|....*....|....*
gi 1032284286 408 VWSIQRDPNVWENPTEFRPERFLDN 432
Cdd:cd11071   334 QPLATRDPKVFDNPDEFVPDRFMGE 358
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
243-463 1.17e-08

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: 56.84  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 243 QGLVKRMGVCARELDAVLDRAIEQmKPLRGRDD-------DEVKDflqylMKLKDQEgdsevpiTINHVKALLtdmvVGG 315
Cdd:cd11032   148 EEEVEEMAEALRELNAYLLEHLEE-RRRNPRDDlisrlveAEVDG-----ERLTDEE-------IVGFAILLL----IAG 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 316 TDTSTNTIEFAMAELMSNPELIKRAQEELDEVVGkdnIVEEshitrlpyilaimkeTLRLHPtlPLLVPHR-PAENTVVG 394
Cdd:cd11032   211 HETTTNLLGNAVLCLDEDPEVAARLRADPSLIPG---AIEE---------------VLRYRP--PVQRTARvTTEDVELG 270
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032284286 395 GYTIPKDTkiFVNVW--SIQRDPNVWENPTEFRPERflDNNscdftganySYFPFGSGRRICAGVALAeRM 463
Cdd:cd11032   271 GVTIPAGQ--LVIAWlaSANRDERQFEDPDTFDIDR--NPN---------PHLSFGHGIHFCLGAPLA-RL 327
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
308-460 1.81e-08

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 56.62  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 308 LTDMVV----GGTDT--STNTIEFAMaeLMSNPELIKRAQEELDEVVGKDNIVEES-HITRLPYILAIMKETLRLHPTLP 380
Cdd:PLN02426  294 LRDIVVsfllAGRDTvaSALTSFFWL--LSKHPEVASAIREEADRVMGPNQEAASFeEMKEMHYLHAALYESMRLFPPVQ 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 381 LLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFLDNNScdFTGAN-YSYFPFGSGRRICAGVA 458
Cdd:PLN02426  372 FDSKFAAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGV--FVPENpFKYPVFQAGLRVCLGKE 449

                  ..
gi 1032284286 459 LA 460
Cdd:PLN02426  450 MA 451
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
217-472 3.44e-08

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: 55.62  E-value: 3.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 217 VISEitrLL--SEPNVSDFFPWLAR-FDLQGLVKRMGVCARELDAVLDRAIEQmkplRGRDDDEvkDFLQYLMKLKDQEG 293
Cdd:cd11029   135 VICE---LLgvPEEDRDRFRRWSDAlVDTDPPPEEAAAALRELVDYLAELVAR----KRAEPGD--DLLSALVAARDEGD 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 294 D-SEVPITinhvkALLTDMVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVvgkDNIVEEshitrlpyilaimkeT 372
Cdd:cd11029   206 RlSEEELV-----STVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRADPELW---PAAVEE---------------L 262
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 373 LRLHPTLPLLVPHRPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENptefrPERFldnnscDFTGANYSYFPFGSGRR 452
Cdd:cd11029   263 LRYDGPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPD-----PDRL------DITRDANGHLAFGHGIH 331
                         250       260
                  ....*....|....*....|.
gi 1032284286 453 ICAGVALAeRMVL-YTLATLL 472
Cdd:cd11029   332 YCLGAPLA-RLEAeIALGALL 351
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
311-475 9.60e-08

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: 54.09  E-value: 9.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 311 MVVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVVgkdNIVEEshitrlpyilaimkeTLRLHPtlPLLVPHRPA-E 389
Cdd:cd20625   209 LLVAGHETTVNLIGNGLLALLRHPEQLALLRADPELIP---AAVEE---------------LLRYDS--PVQLTARVAlE 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 390 NTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFlDNNScdftganysyFPFGSGRRICAGVALAeRMVL-YTL 468
Cdd:cd20625   269 DVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITRA-PNRH----------LAFGAGIHFCLGAPLA-RLEAeIAL 336

                  ....*..
gi 1032284286 469 ATLLHSF 475
Cdd:cd20625   337 RALLRRF 343
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
312-468 1.69e-07

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: 53.30  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 312 VVGGTDTSTNTIEFAMAELMSNPELIKRAQEELDEVvgkDNIVEEshitrlpyilaimkeTLRLHPtlPllVPH--RPA- 388
Cdd:cd11033   218 AVAGNETTRNSISGGVLALAEHPDQWERLRADPSLL---PTAVEE---------------ILRWAS--P--VIHfrRTAt 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 389 ENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERflDNNscdftganySYFPFGSGRRICAGVALAeRMVLYTL 468
Cdd:cd11033   276 RDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR--SPN---------PHLAFGGGPHFCLGAHLA-RLELRVL 343
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
248-464 1.07e-06

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: 50.96  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 248 RMGVCARELDAVLDRAIEQMkplRGRDDDEVkdfLQYLMKlkdqegdSEVPITINHVKALLTDMVVGGTDTSTNTIEFAM 327
Cdd:cd11039   160 RCDEATAGIDAAIDALIPVH---RSNPNPSL---LSVMLN-------AGMPMSLEQIRANIKVAIGGGLNEPRDAIAGTC 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 328 AELMSNPElikraqeELDEVVGKDNiveeshitrlPYILAiMKETLRLhpTLPL-LVPHRPAENTVVGGYTIPKDTKIFV 406
Cdd:cd11039   227 WGLLSNPE-------QLAEVMAGDV----------HWLRA-FEEGLRW--ISPIgMSPRRVAEDFEIRGVTLPAGDRVFL 286
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1032284286 407 NVWSIQRDPNVWENPTEF---RPERfldnnscdftganySYFPFGSGRRICAGVALAERMV 464
Cdd:cd11039   287 MFGSANRDEARFENPDRFdvfRPKS--------------PHVSFGAGPHFCAGAWASRQMV 333
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
238-475 2.33e-06

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: 49.83  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 238 ARFDLQGLVKRMGVCARELDAVLDRAIEQmkplRGRDDDEvkDFLQYLMklkdQEGDSEVPITINHVKALLTDMVVGGTD 317
Cdd:cd11030   153 RLLDLSSTAEEAAAAGAELRAYLDELVAR----KRREPGD--DLLSRLV----AEHGAPGELTDEELVGIAVLLLVAGHE 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 318 TSTNTIE---FAM-------AELMSNPELIKRAQEELdevvgkdniveeshitrlpyilaimketLRLHPTLPLLVPHRP 387
Cdd:cd11030   223 TTANMIAlgtLALlehpeqlAALRADPSLVPGAVEEL----------------------------LRYLSIVQDGLPRVA 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 388 AENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFrperfldnnscDFTGANYSYFPFGSGRRICAGVALAeRMVLYT 467
Cdd:cd11030   275 TEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRL-----------DITRPARRHLAFGHGVHQCLGQNLA-RLELEI 342

                  ....*....
gi 1032284286 468 -LATLLHSF 475
Cdd:cd11030   343 aLPTLFRRF 351
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
87-460 2.88e-06

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: 49.65  E-value: 2.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286  87 IVVNSPSLAREILKDQDiNFSNRDVPLTGRAATYGGIDIVWTPYGAEWRQlRKIcVLKLLSR----KTLDSFYELRRKEV 162
Cdd:cd20612    14 VIVTRYADVKKVLEDPE-SFSVPWGPAMEDLTKGGPFFLLGGDTPANDRQ-REL-MRKALYSpdlaKDVVFFYELQTRAL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 163 RERTRYLyEQGRKQSPVkVGDqLFLTMMNLTMNMLWGGSVKAEEMESVGTEfkgvISEITRLLSEPNVSDFFpwlARFDL 242
Cdd:cd20612    91 LVESSRL-GGSGGQVDI-VRD-VANLVPARFCADLFGLPLKTKENPRGGYT----EAELYRALAAIFAYIFF---DLDPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 243 QGLVKRMG--VCARELDAVLDRAIeqmkplrgrdDDEVKDflqylmklkdqegdsevpitinhvkaLLTDMVVGGTDTST 320
Cdd:cd20612   161 KSFQLRRAaqAAAARLGALLDAAV----------ADEVRD--------------------------NVLGTAVGGVPTQS 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 321 NTIEFAMAELMSNPElikraQEELDEV--VGKDNIVEESHITRlpYILaimkETLRLHPTLPLLVPHRPAENTVV----G 394
Cdd:cd20612   205 QAFAQILDFYLRRPG-----AAHLAEIqaLARENDEADATLRG--YVL----EALRLNPIAPGLYRRATTDTTVAdgggR 273
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1032284286 395 GYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDnnscdftganySYFPFGSGRRICAGVALA 460
Cdd:cd20612   274 TVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDRPLE-----------SYIHFGHGPHQCLGEEIA 328
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
321-483 6.19e-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: 48.45  E-value: 6.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 321 NTIE---FAMAELMSNPELIKRAQEELDEVVG----KDNIVEESHITR-----LPYILAIMKETLRLHP----------- 377
Cdd:cd20632   230 NTIPatfWAMYYLLRHPEALAAVRDEIDHVLQstgqELGPDFDIHLTReqldsLVYLESAINESLRLSSasmnirvvqed 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 378 -TLPLlvphrpaENTvvGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDNNS--CDF--TGANYSYF--PFGSG 450
Cdd:cd20632   310 fTLKL-------ESD--GSVNLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKkkTTFykRGQKLKYYlmPFGSG 380
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1032284286 451 RRICAGVALAERMVLYTLATLLHSFDWKIPEGH 483
Cdd:cd20632   381 SSKCPGRFFAVNEIKQFLSLLLLYFDLELLEEQ 413
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
326-476 9.05e-06

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 48.13  E-value: 9.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 326 AMAELMSNPELIKRAQEELDEVVGKDN----------IVEESHITRLPYILAIMKETLRLHpTLPLLVphrpaeNTVVGG 395
Cdd:cd20633   247 LLLYLLKHPEAMKAVREEVEQVLKETGqevkpggpliNLTRDMLLKTPVLDSAVEETLRLT-AAPVLI------RAVVQD 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 396 YTIPKDT------------KIFVNVwSIQRDPNVWENPTEFRPERFLDNNSC---DF--TGA--NYSYFPFGSGRRICAG 456
Cdd:cd20633   320 MTLKMANgreyalrkgdrlALFPYL-AVQMDPEIHPEPHTFKYDRFLNPDGGkkkDFykNGKklKYYNMPWGAGVSICPG 398
                         170       180
                  ....*....|....*....|..
gi 1032284286 457 --VALAErMVLYTLATLLHsFD 476
Cdd:cd20633   399 rfFAVNE-MKQFVFLMLTY-FD 418
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
368-476 3.25e-05

cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a putative cytochrome P450 of unknown function. 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: 410719  Cd Length: 381  Bit Score: 46.24  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 368 IMKETLRLHPTLPLLVPHRPAENTvvggytiPKDTKIFVNVWSIQRDPNVW-ENPTEFRPERFldNNSCDFTGAnySYFP 446
Cdd:cd20626   261 LVKEALRLYPPTRRIYRAFQRPGS-------SKPEIIAADIEACHRSESIWgPDALEFNPSRW--SKLTPTQKE--AFLP 329
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1032284286 447 FGSGRRIC-AGVALAERMVLYTLATLLHSFD 476
Cdd:cd20626   330 FGSGPFRCpAKPVFGPRMIALLVGALLDALG 360
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
367-464 4.45e-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: 42.42  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1032284286 367 AIMKETLRLHPTLPLLVPHrPAENTVVGGYTIPKDTKIFVNVWSIQRDPNVWENPTEFRPERFLDnnscdfTGANYSyfp 446
Cdd:cd20619   236 AIINEMVRMDPPQLSFLRF-PTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTRPPA------ASRNLS--- 305
                          90
                  ....*....|....*...
gi 1032284286 447 FGSGRRICAGVALAERMV 464
Cdd:cd20619   306 FGLGPHSCAGQIISRAEA 323
 
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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