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Conserved domains on  [gi|586644824|ref|XP_006878550|]
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cytochrome P450 76C1 [Amborella trichopoda]

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 ...
57-496 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 586644824  57 SLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTK 136
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 137 RLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVFKKGDELATELKGMVRDVLKLSGEPNA 216
Cdd:cd11073   81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSESGSEFKELVREIMELAGKPNV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 SDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKDMREKGMVNERDeesgrgikesDFLGVLLELMDHNEGLQME 296
Cdd:cd11073  161 ADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDD----------DLLLLLDLELDSESELTRN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 297 HVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLL 376
Cdd:cd11073  231 HIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 377 IPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGMPLASSM 456
Cdd:cd11073  311 LPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKGRDFELIPFGSGRRICPGLPLAERM 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 586644824 457 VHLVLGSLLHYFNWKVEG-----EVDMTEEFGITLQKALPLVVVA 496
Cdd:cd11073  391 VHLVLASLLHSFDWKLPDgmkpeDLDMEEKFGLTLQKAVPLKAIP 435
 
Name Accession Description Interval E-value
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
57-496 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 586644824  57 SLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTK 136
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 137 RLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVFKKGDELATELKGMVRDVLKLSGEPNA 216
Cdd:cd11073   81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSESGSEFKELVREIMELAGKPNV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 SDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKDMREKGMVNERDeesgrgikesDFLGVLLELMDHNEGLQME 296
Cdd:cd11073  161 ADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDD----------DLLLLLDLELDSESELTRN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 297 HVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLL 376
Cdd:cd11073  231 HIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 377 IPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGMPLASSM 456
Cdd:cd11073  311 LPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKGRDFELIPFGSGRRICPGLPLAERM 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 586644824 457 VHLVLGSLLHYFNWKVEG-----EVDMTEEFGITLQKALPLVVVA 496
Cdd:cd11073  391 VHLVLASLLHSFDWKLPDgmkpeDLDMEEKFGLTLQKAVPLKAIP 435
PLN02687 PLN02687
flavonoid 3'-monooxygenase
25-505 5.23e-146

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 428.46  E-value: 5.23e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  25 SAKAQAPSPP---KWPIIGHLHLLGKLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLA 101
Cdd:PLN02687  28 SGKHKRPLPPgprGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 102 AKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSkTMASIYEESIKGNSVNIGSTVFSTMLGIVE 181
Cdd:PLN02687 108 AEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVA-LLVRELARQHGTAPVNLGQLVNVCTTNALG 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 182 NMVCGNYVFK-KGDELATELKGMVRDVLKLSGEPNASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRlkdmrek 260
Cdd:PLN02687 187 RAMVGRRVFAgDGDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLDLQGVVGKMKRLHRRFDAMMNGIIEEH------- 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 261 gmvneRDEESGRGIKESDFLGVLLELMDHNEG------LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEA 334
Cdd:PLN02687 260 -----KAAGQTGSEEHKDLLSTLLALKREQQAdgeggrITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKA 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 335 RDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSD 414
Cdd:PLN02687 335 QEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPD 414
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 415 PLKFDPSRFV----GTNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEG-----EVDMTEEFGIT 485
Cdd:PLN02687 415 PLEFRPDRFLpggeHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADgqtpdKLNMEEAYGLT 494
                        490       500
                 ....*....|....*....|
gi 586644824 486 LQKALPLVVVATPSLPLNPY 505
Cdd:PLN02687 495 LQRAVPLMVHPRPRLLPSAY 514
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
31-494 7.78e-105

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: 321.15  E-value: 7.78e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824   31 PSPPKWPIIGHLHLLG--KLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPV-PLAAKTLSY 107
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGrkGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDePWFATSRGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  108 GGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNsMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGN 187
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLS-FEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  188 YVFKKGDELATELKGMVRDVLKL--SGEPNASDFFPFLRGLdLQGVERRAQKLRERFDGIFSEMIERRlkdmrekgmvne 265
Cdd:pfam00067 161 RFGSLEDPKFLELVKAVQELSSLlsSPSPQLLDLFPILKYF-PGPHGRKLKRARKKIKDLLDKLIEER------------ 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  266 RDEESGRGIKESDFLGVLLELMD--HNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIG 343
Cdd:pfam00067 228 RETLDSAKKSPRDFLDALLLAKEeeDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  344 KDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRF 423
Cdd:pfam00067 308 DKRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERF 387
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586644824  424 VGTNLEFKgNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV--EGEVDMTEEFGITLQKALPLVV 494
Cdd:pfam00067 388 LDENGKFR-KSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELppGTDPPDIDETPGLLLPPKPYKL 459
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
49-496 3.33e-53

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: 184.71  E-value: 3.33e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  49 PHQSLAALsLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVwAAYGHHWRLLRRLs 128
Cdd:COG2124   21 PYPFYARL-REYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLL-TLDGPEHTRLRRL- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 129 FTELFSTKRLNSMEkfrkAEVSKTMASIYEESIKGNSVNIGS--------TVFSTMLGIvenmvcgnyvfkkGDELATEL 200
Cdd:COG2124   98 VQPAFTPRRVAALR----PRIREIADELLDRLAARGPVDLVEefarplpvIVICELLGV-------------PEEDRDRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 201 KGMVRDVLklsgepNASDFFPFLRgldlqgvERRAQKLRERFDGIFSEMIERRLKDMREkgmvnerdeesgrgikesDFL 280
Cdd:COG2124  161 RRWSDALL------DALGPLPPER-------RRRARRARAELDAYLRELIAERRAEPGD------------------DLL 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 281 GVLLELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPyvmeEARDELRRvigkdkmmeeshipDVPFLQ 360
Cdd:COG2124  210 SALLAARDDGERLSDEELRDELLLLLLAGHETTANALAWALYALLRHP----EQLARLRA--------------EPELLP 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 361 AIVKEVLRLHPAAPLLiPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefkgNDYELLPF 440
Cdd:COG2124  272 AAVEETLRLYPPVPLL-PRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPF 340
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 441 GAGRRICIGMPLASSMVHLVLGSLLHYF-NWKVEGEVDMTEEFGITLQ--KALPLVVVA 496
Cdd:COG2124  341 GGGPHRCLGAALARLEARIALATLLRRFpDLRLAPPEELRWRPSLTLRgpKSLPVRLRP 399
P450_cycloAA_1 TIGR04538
cytochrome P450, cyclodipeptide synthase-associated; Members of this subfamily are cytochrome ...
218-473 1.80e-23

cytochrome P450, cyclodipeptide synthase-associated; Members of this subfamily are cytochrome P450 enzymes that occur next to tRNA-dependent cyclodipeptide synthases. This group does NOT include CYP121 (Rv2275) from Mycobacterium tuberculosis, adjacent to the cyclodityrosine synthetase Rv2276.


Pssm-ID: 275331  Cd Length: 395  Bit Score: 102.11  E-value: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  218 DF---FPFLRGLDLQGV-ERRAQKLRERFDGI--F-------SEMIERRLKDMRE-----KGMVNERdeesgRGIKESDF 279
Cdd:TIGR04538 122 DFgktFAVCVTMDLLGLdKRDHEKIREWHSGIakFitslnqsPEERMHSLECSEKlreylMPIIEER-----RKNPGSDL 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  280 LGVLLELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPyvmeearDELRRVIgKDKmmeeshipdvPFL 359
Cdd:TIGR04538 197 ISILCTSEDEGNAMSDTEILALILNILLAATEPADKTLAYMIYHLLNNP-------EQLNDVL-DDR----------KLL 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  360 QAIVKEVLRLHPaaPL-LIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELL 438
Cdd:TIGR04538 259 RRAIAETLRLHS--PVqLIPRQLSQDVTISGKEIKKGDTVFCMIGAANRDPEAFEDPDEFNIHRKDLVNKSAFTGAARHL 336
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 586644824  439 PFGAGRRICIGMPLASSMVHLVLGSLLHYF-NWKVE 473
Cdd:TIGR04538 337 AFGSGVHNCVGAAFAKRQLEIVANILLDLLkNIRLE 372
 
Name Accession Description Interval E-value
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
57-496 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 586644824  57 SLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTK 136
Cdd:cd11073    1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 137 RLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVFKKGDELATELKGMVRDVLKLSGEPNA 216
Cdd:cd11073   81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSESGSEFKELVREIMELAGKPNV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 SDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKDMREKGMVNERDeesgrgikesDFLGVLLELMDHNEGLQME 296
Cdd:cd11073  161 ADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDD----------DLLLLLDLELDSESELTRN 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 297 HVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLL 376
Cdd:cd11073  231 HIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 377 IPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGMPLASSM 456
Cdd:cd11073  311 LPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKGRDFELIPFGSGRRICPGLPLAERM 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 586644824 457 VHLVLGSLLHYFNWKVEG-----EVDMTEEFGITLQKALPLVVVA 496
Cdd:cd11073  391 VHLVLASLLHSFDWKLPDgmkpeDLDMEEKFGLTLQKAVPLKAIP 435
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
61-492 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: 535.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNS 140
Cdd:cd20618    1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGQDIVFAPYGPHWRHLRKICTLELFSAKRLES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 141 MEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVF---KKGDELATELKGMVRDVLKLSGEPNAS 217
Cdd:cd20618   81 FQGVRKEELSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRYFgesEKESEEAREFKELIDEAFELAGAFNIG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 218 DFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRlkdmrekgmvNERDEESGRGIKESDFLgVLLELMDHNEGLQMEH 297
Cdd:cd20618  161 DYIPWLRWLDLQGYEKRMKKLHAKLDRFLQKIIEEH----------REKRGESKKGGDDDDDL-LLLLDLDGEGKLSDDN 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 298 VKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLI 377
Cdd:cd20618  230 IKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLL 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 378 PRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNL-EFKGNDYELLPFGAGRRICIGMPLASSM 456
Cdd:cd20618  310 PHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIdDVKGQDFELLPFGSGRRMCPGMPLGLRM 389
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 586644824 457 VHLVLGSLLHYFNWKVEG----EVDMTEEFGITLQKALPL 492
Cdd:cd20618  390 VQLTLANLLHGFDWSLPGpkpeDIDMEEKFGLTVPRAVPL 429
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
59-492 2.16e-172

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: 492.36  E-value: 2.16e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  59 TYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRL 138
Cdd:cd11072    1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGKDIAFAPYGEYWRQMRKICVLELLSAKRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 139 NSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTmlgiVENMVC-----GNYVFKKGDELatelKGMVRDVLKLSGE 213
Cdd:cd11072   81 QSFRSIREEEVSLLVKKIRESASSSSPVNLSELLFSL----TNDIVCraafgRKYEGKDQDKF----KELVKEALELLGG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 214 PNASDFFPFLRGLDLQ-GVERRAQKLRERFDGIFSEMIERRLKDMREKgmvnerdeesgrgiKESDFLGVLLELMDHNEG 292
Cdd:cd11072  153 FSVGDYFPSLGWIDLLtGLDRKLEKVFKELDAFLEKIIDEHLDKKRSK--------------DEDDDDDDLLDLRLQKEG 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 293 -----LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVL 367
Cdd:cd11072  219 dlefpLTRDNIKAIILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETL 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 368 RLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRIC 447
Cdd:cd11072  299 RLHPPAPLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIDFKGQDFELIPFGAGRRIC 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 586644824 448 IGMPLASSMVHLVLGSLLHYFNWKVEG-----EVDMTEEFGITLQKALPL 492
Cdd:cd11072  379 PGITFGLANVELALANLLYHFDWKLPDgmkpeDLDMEEAFGLTVHRKNPL 428
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
61-498 2.10e-157

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: 454.57  E-value: 2.10e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNS 140
Cdd:cd20657    1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMAYNAQDMVFAPYGPRWRLLRKLCNLHLFGGKALED 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 141 MEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVF-KKGDELATELKGMVRDVLKLSGEPNASDF 219
Cdd:cd20657   81 WAHVRENEVGHMLKSMAEASRKGEPVVLGEMLNVCMANMLGRVMLSKRVFaAKAGAKANEFKEMVVELMTVAGVFNIGDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 220 FPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKDMREKGmvnerdeesgrgiKESDFLG-VLLELMDHNEG--LQME 296
Cdd:cd20657  161 IPSLAWMDLQGVEKKMKRLHKRFDALLTKILEEHKATAQERK-------------GKPDFLDfVLLENDDNGEGerLTDT 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 297 HVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLL 376
Cdd:cd20657  228 NIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLN 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 377 IPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVG---TNLEFKGNDYELLPFGAGRRICIGMPLA 453
Cdd:cd20657  308 LPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPgrnAKVDVRGNDFELIPFGAGRRICAGTRMG 387
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 586644824 454 SSMVHLVLGSLLHYFNWKVEG-----EVDMTEEFGITLQKALPLVVVATP 498
Cdd:cd20657  388 IRMVEYILATLVHSFDWKLPAgqtpeELNMEEAFGLALQKAVPLVAHPTP 437
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
61-495 3.00e-147

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: 428.55  E-value: 3.00e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNS 140
Cdd:cd20655    1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 141 MEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVFKKGDElATELKGMVRDVLKLSGEPNASDFF 220
Cdd:cd20655   81 FRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGE-AEEVRKLVKESAELAGKFNASDFI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 221 PFLRGLDLQGVERRAQKLRERFDgifsEMIERRLKDMREKgmvneRDEESGRGIKesDFLGVLLELM--DHNE-GLQMEH 297
Cdd:cd20655  160 WPLKKLDLQGFGKRIMDVSNRFD----ELLERIIKEHEEK-----RKKRKEGGSK--DLLDILLDAYedENAEyKITRNH 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 298 VKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPlLI 377
Cdd:cd20655  229 IKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGP-LL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 378 PRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFV-----GTNLEFKGNDYELLPFGAGRRICIGMPL 452
Cdd:cd20655  308 VRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLassrsGQELDVRGQHFKLLPFGSGRRGCPGASL 387
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 586644824 453 ASSMVHLVLGSLLHYFNWKVEGE--VDMTEEFGITLQKALPLVVV 495
Cdd:cd20655  388 AYQVVGTAIAAMVQCFDWKVGDGekVNMEEASGLTLPRAHPLKCV 432
PLN02687 PLN02687
flavonoid 3'-monooxygenase
25-505 5.23e-146

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 428.46  E-value: 5.23e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  25 SAKAQAPSPP---KWPIIGHLHLLGKLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLA 101
Cdd:PLN02687  28 SGKHKRPLPPgprGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 102 AKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSkTMASIYEESIKGNSVNIGSTVFSTMLGIVE 181
Cdd:PLN02687 108 AEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVA-LLVRELARQHGTAPVNLGQLVNVCTTNALG 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 182 NMVCGNYVFK-KGDELATELKGMVRDVLKLSGEPNASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRlkdmrek 260
Cdd:PLN02687 187 RAMVGRRVFAgDGDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLDLQGVVGKMKRLHRRFDAMMNGIIEEH------- 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 261 gmvneRDEESGRGIKESDFLGVLLELMDHNEG------LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEA 334
Cdd:PLN02687 260 -----KAAGQTGSEEHKDLLSTLLALKREQQAdgeggrITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKA 334
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 335 RDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSD 414
Cdd:PLN02687 335 QEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPD 414
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 415 PLKFDPSRFV----GTNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEG-----EVDMTEEFGIT 485
Cdd:PLN02687 415 PLEFRPDRFLpggeHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADgqtpdKLNMEEAYGLT 494
                        490       500
                 ....*....|....*....|
gi 586644824 486 LQKALPLVVVATPSLPLNPY 505
Cdd:PLN02687 495 LQRAVPLMVHPRPRLLPSAY 514
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
31-506 2.88e-136

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 403.08  E-value: 2.88e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  31 PSPPKWPIIGHLHLLGKLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGN 110
Cdd:PLN00110  34 PGPRGWPLLGALPLLGNMPHVALAKMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRPPNAGATHLAYGAQ 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 111 SLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVF 190
Cdd:PLN00110 114 DMVFADYGPRWKLLRKLSNLHMLGGKALEDWSQVRTVELGHMLRAMLELSQRGEPVVVPEMLTFSMANMIGQVILSRRVF 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 191 KKGDELATELKGMVRDVLKLSGEPNASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKDMRE-KGmvnerdee 269
Cdd:PLN00110 194 ETKGSESNEFKDMVVELMTTAGYFNIGDFIPSIAWMDIQGIERGMKHLHKKFDKLLTRMIEEHTASAHErKG-------- 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 270 sgrgikESDFLGVLLELMDHNEG--LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKM 347
Cdd:PLN00110 266 ------NPDFLDVVMANQENSTGekLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRR 339
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 348 MEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVG-- 425
Cdd:PLN00110 340 LVESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSek 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 426 -TNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV-EG-EVDMTEEFGITLQKALPLVVVATPSLPL 502
Cdd:PLN00110 420 nAKIDPRGNDFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLpDGvELNMDEAFGLALQKAVPLSAMVTPRLHQ 499

                 ....
gi 586644824 503 NPYL 506
Cdd:PLN00110 500 SAYA 503
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
61-498 8.10e-134

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: 395.06  E-value: 8.10e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNS 140
Cdd:cd20654    1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMGYNYAMFGFAPYGPYWRELRKIATLELLSNRRLEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 141 MEKFRKAEVSKTMASIYEESIKGNSVNIGSTV-----FS-TMLGIVENMVCGNYVFKKGDELATE----LKGMVRDVLKL 210
Cdd:cd20654   81 LKHVRVSEVDTSIKELYSLWSNNKKGGGGVLVemkqwFAdLTFNVILRMVVGKRYFGGTAVEDDEeaerYKKAIREFMRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 211 SGEPNASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIErrlkDMREKGMVNERDEEsgrgiKESDFLGVLLELMDHN 290
Cdd:cd20654  161 AGTFVVSDAIPFLGWLDFGGHEKAMKRTAKELDSILEEWLE----EHRQKRSSSGKSKN-----DEDDDDVMMLSILEDS 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 291 EGLQMEH---VKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVL 367
Cdd:cd20654  232 QISGYDAdtvIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 368 RLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTN--LEFKGNDYELLPFGAGRR 445
Cdd:cd20654  312 RLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHkdIDVRGQNFELIPFGSGRR 391
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 586644824 446 ICIGMPLASSMVHLVLGSLLHYFNWKV--EGEVDMTEEFGITLQKALPLVVVATP 498
Cdd:cd20654  392 SCPGVSFGLQVMHLTLARLLHGFDIKTpsNEPVDMTEGPGLTNPKATPLEVLLTP 446
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
61-492 1.46e-133

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: 393.12  E-value: 1.46e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNS 140
Cdd:cd20653    1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAPYGDHWRNLRRITTLEIFSSHRLNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 141 MEKFRKAEVSKTMASIYEESIKGNS-VNIGSTVFSTMLGIVENMVCGNYVFKKGD---ELATELKGMVRDVLKLSGEPNA 216
Cdd:cd20653   81 FSSIRRDEIRRLLKRLARDSKGGFAkVELKPLFSELTFNNIMRMVAGKRYYGEDVsdaEEAKLFRELVSEIFELSGAGNP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 SDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIE--RRLKDMREKGMVNerdeesgrgikesdflgVLLELMDHneglQ 294
Cdd:cd20653  161 ADFLPILRWFDFQGLEKRVKKLAKRRDAFLQGLIDehRKNKESGKNTMID-----------------HLLSLQES----Q 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 295 MEH-----VKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRL 369
Cdd:cd20653  220 PEYytdeiIKGLILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 370 HPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGtnleFKGNDYELLPFGAGRRICIG 449
Cdd:cd20653  300 YPAAPLLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEG----EEREGYKLIPFGLGRRACPG 375
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 586644824 450 MPLASSMVHLVLGSLLHYFNWK--VEGEVDMTEEFGITLQKALPL 492
Cdd:cd20653  376 AGLAQRVVGLALGSLIQCFEWErvGEEEVDMTEGKGLTMPKAIPL 420
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
31-506 2.45e-119

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 360.29  E-value: 2.45e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  31 PSPPKWPIIGHLHLLGKLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGN 110
Cdd:PLN03112  35 PGPPRWPIVGNLLQLGPLPHRDLASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRPRTLAAVHLAYGCG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 111 SLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVF 190
Cdd:PLN03112 115 DVALAPLGPHWKRMRRICMEHLLTTKRLESFAKHRAEEARHLIQDVWEAAQTGKPVNLREVLGAFSMNNVTRMLLGKQYF 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 191 ---KKGDELATELKGMVRDVLKLSGEPNASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIE--RRLKDMREKGMvne 265
Cdd:PLN03112 195 gaeSAGPKEAMEFMHITHELFRLLGVIYLGDYLPAWRWLDPYGCEKKMREVEKRVDEFHDKIIDehRRARSGKLPGG--- 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 266 rdeesgrgiKESDFLGVLLELMDHNEGLQMEHV--KGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIG 343
Cdd:PLN03112 272 ---------KDMDFVDVLLSLPGENGKEHMDDVeiKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVG 342
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 344 KDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRF 423
Cdd:PLN03112 343 RNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERH 422
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 424 V---GTNLEF-KGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWK-----VEGEVDMTEEFGITLQKALPLVV 494
Cdd:PLN03112 423 WpaeGSRVEIsHGPDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSppdglRPEDIDTQEVYGMTMPKAKPLRA 502
                        490
                 ....*....|..
gi 586644824 495 VATPSLPlnPYL 506
Cdd:PLN03112 503 VATPRLA--PHL 512
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
60-492 5.75e-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: 322.90  E-value: 5.75e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLN 139
Cdd:cd20656    1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGQDLIWADYGPHYVKVRKLCTLELFTPKRLE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 140 SMEKFRKAEVSKTMASIYEE----SIKGNSVNIGSTVFSTMLGIVENMVCGN-YVFKKG--DELATELKGMVRDVLKLSG 212
Cdd:cd20656   81 SLRPIREDEVTAMVESIFNDcmspENEGKPVVLRKYLSAVAFNNITRLAFGKrFVNAEGvmDEQGVEFKAIVSNGLKLGA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 213 EPNASDFFPFLRGL-DLQgverraqklrerfDGIFSEMIERRLKDMREKGMVNERDE-ESGRGIKesdFLGVLLELMDHN 290
Cdd:cd20656  161 SLTMAEHIPWLRWMfPLS-------------EKAFAKHGARRDRLTKAIMEEHTLARqKSGGGQQ---HFVALLTLKEQY 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 291 EgLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLH 370
Cdd:cd20656  225 D-LSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLH 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 371 PAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGM 450
Cdd:cd20656  304 PPTPLMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKGHDFRLLPFGAGRRVCPGA 383
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 586644824 451 PLASSMVHLVLGSLLHYFNWK----VEGE-VDMTEEFGITLQKALPL 492
Cdd:cd20656  384 QLGINLVTLMLGHLLHHFSWTppegTPPEeIDMTENPGLVTFMRTPL 430
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
31-494 7.78e-105

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: 321.15  E-value: 7.78e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824   31 PSPPKWPIIGHLHLLG--KLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPV-PLAAKTLSY 107
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGrkGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDePWFATSRGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  108 GGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNsMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGN 187
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLS-FEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  188 YVFKKGDELATELKGMVRDVLKL--SGEPNASDFFPFLRGLdLQGVERRAQKLRERFDGIFSEMIERRlkdmrekgmvne 265
Cdd:pfam00067 161 RFGSLEDPKFLELVKAVQELSSLlsSPSPQLLDLFPILKYF-PGPHGRKLKRARKKIKDLLDKLIEER------------ 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  266 RDEESGRGIKESDFLGVLLELMD--HNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIG 343
Cdd:pfam00067 228 RETLDSAKKSPRDFLDALLLAKEeeDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  344 KDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRF 423
Cdd:pfam00067 308 DKRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERF 387
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586644824  424 VGTNLEFKgNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV--EGEVDMTEEFGITLQKALPLVV 494
Cdd:pfam00067 388 LDENGKFR-KSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELppGTDPPDIDETPGLLLPPKPYKL 459
PLN02183 PLN02183
ferulate 5-hydroxylase
31-500 1.11e-100

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 312.17  E-value: 1.11e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  31 PSPPKWPIIGHLHLLGKLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGN 110
Cdd:PLN02183  39 PGPKGLPIIGNMLMMDQLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPANIAISYLTYDRA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 111 SLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKaEVSKTMASIyeESIKGNSVNIGSTVFSTMLGIVENMVCGNYVF 190
Cdd:PLN02183 119 DMAFAHYGPFWRQMRKLCVMKLFSRKRAESWASVRD-EVDSMVRSV--SSNIGKPVNIGELIFTLTRNITYRAAFGSSSN 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 191 KKGDELATELKgmvrDVLKLSGEPNASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKDMREKGMVNERDEes 270
Cdd:PLN02183 196 EGQDEFIKILQ----EFSKLFGAFNVADFIPWLGWIDPQGLNKRLVKARKSLDGFIDDIIDDHIQKRKNQNADNDSEE-- 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 271 grgiKESDFLGVLLE------LMDHNEGLQ------MEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDEL 338
Cdd:PLN02183 270 ----AETDMVDDLLAfyseeaKVNESDDLQnsikltRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQEL 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 339 RRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDsDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKF 418
Cdd:PLN02183 346 ADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAE-DAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTF 424
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 419 DPSRFVGTNL-EFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV-----EGEVDMTEEFGITLQKALPL 492
Cdd:PLN02183 425 KPSRFLKPGVpDFKGSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWELpdgmkPSELDMNDVFGLTAPRATRL 504

                 ....*...
gi 586644824 493 VVVATPSL 500
Cdd:PLN02183 505 VAVPTYRL 512
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
62-492 2.12e-99

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: 305.79  E-value: 2.12e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  62 PIMPFKLGMRKAVVISSPHPAKQIFktHDRKFSSRPVPLAAKTLSYGgNSLVWAAYGHHWRLLRRLSFTELFSTKRLNSM 141
Cdd:cd11076    4 RLMAFSLGETRVVITSHPETAREIL--NSPAFADRPVKESAYELMFN-RAIGFAPYGEYWRNLRRIASNHLFSPRRIAAS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 142 EKFRKAEVSKTMASIYEESIKGNSV------------NIGSTVFSTmlgivenmvcgNYVFKKGDELATELKGMVRDVLK 209
Cdd:cd11076   81 EPQRQAIAAQMVKAIAKEMERSGEVavrkhlqraslnNIMGSVFGR-----------RYDFEAGNEEAEELGEMVREGYE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 210 LSGEPNASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRlkdmREKGMVNERDEEsgrgikesDFLGVLLELmDH 289
Cdd:cd11076  150 LLGAFNWSDHLPWLRWLDLQGIRRRCSALVPRVNTFVGKIIEEH----RAKRSNRARDDE--------DDVDVLLSL-QG 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 290 NEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRL 369
Cdd:cd11076  217 EEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRL 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 370 HPAAPLL-IPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFV----GTNLEFKGNDYELLPFGAGR 444
Cdd:cd11076  297 HPPGPLLsWARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVaaegGADVSVLGSDLRLAPFGAGR 376
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 586644824 445 RICIGMPLASSMVHLVLGSLLHYFNWKVEGE--VDMTEEFGITLQKALPL 492
Cdd:cd11076  377 RVCPGKALGLATVHLWVAQLLHEFEWLPDDAkpVDLSEVLKLSCEMKNPL 426
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
61-487 3.57e-99

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: 305.29  E-value: 3.57e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLvwAAYGHHWRLLRRLSFTELFSTKRLNS 140
Cdd:cd20617    1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKGIL--FSNGDYWKELRRFALSSLTKTKLKKK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 141 MEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVFKKGDELATELKGMVRDVLKLSGEPNASDFF 220
Cdd:cd20617   79 MEELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDDGEFLKLVKPIEEIFKELGSGNPSDFI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 221 PFLRGLDLQGvERRAQKLRERFDGIFSEMIERRLKDMREkgmVNERDEESGRGIKEsdflgvllELMDHNEGLQMEHVKG 300
Cdd:cd20617  159 PILLPFYFLY-LKKLKKSYDKIKDFIEKIIEEHLKTIDP---NNPRDLIDDELLLL--------LKEGDSGLFDDDSIIS 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 301 MLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRL 380
Cdd:cd20617  227 TCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRV 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 381 CDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLefKGNDYELLPFGAGRRICIGMPLASSMVHLV 460
Cdd:cd20617  307 TTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDG--NKLSEQFIPFGIGKRNCVGENLARDELFLF 384
                        410       420
                 ....*....|....*....|....*....
gi 586644824 461 LGSLLHYFNWKVEGE--VDMTEEFGITLQ 487
Cdd:cd20617  385 FANLLLNFKFKSSDGlpIDEKEVFGLTLK 413
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
59-492 4.97e-99

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: 305.32  E-value: 4.97e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  59 TYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAA-YGHHWRLLRRLSFTELFSTKR 137
Cdd:cd11075    1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVLFSSNKHMVNSSpYGPLWRTLRRNLVSEVLSPSR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 138 LNSMEKFRKAEVSKTMASIYEES-IKGNSVNIGSTVFSTMLGIVENMVCGNyvfKKGDELATELKGMVRDVLKLSGEPNA 216
Cdd:cd11075   81 LKQFRPARRRALDNLVERLREEAkENPGPVNVRDHFRHALFSLLLYMCFGE---RLDEETVRELERVQRELLLSFTDFDV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 SDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKDMrekgmvnERDEESGRGIKESDFLGVLLELMDHNEGLQME 296
Cdd:cd11075  158 RDFFPALTWLLNRRRWKKVLELRRRQEEVLLPLIRARRKRR-------ASGEADKDYTDFLLLDLLDLKEEGGERKLTDE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 297 HVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLL 376
Cdd:cd11075  231 ELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHFL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 377 IPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFV---GTNLEFKGND-YELLPFGAGRRICIGMPL 452
Cdd:cd11075  311 LPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLaggEAADIDTGSKeIKMMPFGAGRRICPGLGL 390
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 586644824 453 ASSMVHLVLGSLLHYFNWK-VEGE-VDMTEEFGITLQKALPL 492
Cdd:cd11075  391 ATLHLELFVARLVQEFEWKlVEGEeVDFSEKQEFTVVMKNPL 432
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
63-500 1.13e-90

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: 283.87  E-value: 1.13e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  63 IMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNSME 142
Cdd:cd20658    3 IACIRLGNTHVIPVTCPKIAREILRKQDAVFASRPLTYATEIISGGYKTTVISPYGEQWKKMRKVLTTELMSPKRHQWLH 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 143 KFRKAEVSKTMASIYEESIKGN---SVNIGSTVFSTMLGIVENMVCGNYVFKKGDE---LATELKGMVR---DVLKLSGE 213
Cdd:cd20658   83 GKRTEEADNLVAYVYNMCKKSNgggLVNVRDAARHYCGNVIRKLMFGTRYFGKGMEdggPGLEEVEHMDaifTALKCLYA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 214 PNASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKDMREKGMVnerdeesgrgiKESDFLGVLLELMDHNEG- 292
Cdd:cd20658  163 FSISDYLPFLRGLDLDGHEKIVREAMRIIRKYHDPIIDERIKQWREGKKK-----------EEEDWLDVFITLKDENGNp 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 293 -LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHP 371
Cdd:cd20658  232 lLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHP 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 372 AAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLE--FKGNDYELLPFGAGRRICIG 449
Cdd:cd20658  312 VAPFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEvtLTEPDLRFISFSTGRRGCPG 391
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 586644824 450 MPLASSMVHLVLGSLLHYFNWKV---EGEVDMTE-EFGITLQKalPLVVVATPSL 500
Cdd:cd20658  392 VKLGTAMTVMLLARLLQGFTWTLppnVSSVDLSEsKDDLFMAK--PLVLVAKPRL 444
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
31-497 1.76e-87

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 277.73  E-value: 1.76e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  31 PSPPKWPIIGHLHLLGKL-PHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGG 109
Cdd:PLN03234  31 PGPKGLPIIGNLHQMEKFnPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 110 NSLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTvfstMLGIVENMVCGNYV 189
Cdd:PLN03234 111 RELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSEL----LLSFTNCVVCRQAF 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 190 FKKGDELATELKGMVrDVL----KLSGEPNASDFFPFLRGLD-LQGVERRAQKLRERFDGIFSEMIERRLKDMREKgmvn 264
Cdd:PLN03234 187 GKRYNEYGTEMKRFI-DILyetqALLGTLFFSDLFPYFGFLDnLTGLSARLKKAFKELDTYLQELLDETLDPNRPK---- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 265 eRDEESgrgikesdFLGVLLELM-DHNEGLQMEH--VKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRV 341
Cdd:PLN03234 262 -QETES--------FIDLLMQIYkDQPFSIKFTHenVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNV 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 342 IGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSD-PLKFDP 420
Cdd:PLN03234 333 IGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIP 412
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 421 SRFVGTN--LEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEG-----EVDMTEEFGITLQKALPLV 493
Cdd:PLN03234 413 ERFMKEHkgVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKgikpeDIKMDVMTGLAMHKKEHLV 492

                 ....
gi 586644824 494 VVAT 497
Cdd:PLN03234 493 LAPT 496
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
60-482 1.85e-83

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: 264.82  E-value: 1.85e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLsFTELFSTKRLN 139
Cdd:cd11065    1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELMGWGMRLLLMPYGPRWRLHRRL-FHQLLNPSAVR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 140 SMEKFRKAEvSKTMASIYEESIKGNSVNIGSTVFSTMLGIVenmvcgnY---VFKKGDELATELKGMVRDVLKLsGEPNA 216
Cdd:cd11065   80 KYRPLQELE-SKQLLRDLLESPDDFLDHIRRYAASIILRLA-------YgyrVPSYDDPLLRDAEEAMEGFSEA-GSPGA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 S--DFFPFLR---GLDLQGVERRAQKLRERFDgifsEMIERRLKDMREKgMVNERDEESgrgikesdFLGVLLELMDHNE 291
Cdd:cd11065  151 YlvDFFPFLRylpSWLGAPWKRKARELRELTR----RLYEGPFEAAKER-MASGTATPS--------FVKDLLEELDKEG 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 292 GLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHP 371
Cdd:cd11065  218 GLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRP 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 372 AAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFV-GTNLEFKGNDYELLPFGAGRRICIGM 450
Cdd:cd11065  298 VAPLGIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLdDPKGTPDPPDPPHFAFGFGRRICPGR 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 586644824 451 PLASSMVHLVLGSLLHYFNWK---------VEGEVDMTEEF 482
Cdd:cd11065  378 HLAENSLFIAIARLLWAFDIKkpkdeggkeIPDEPEFTDGL 418
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
60-486 2.58e-82

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: 261.76  E-value: 2.58e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTEL----FST 135
Cdd:cd11027    1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGKDIAFGDYSPTWKLHRKLAHSALrlyaSGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 136 KRLNsmEKFRKaEVSKTMASIyeESIKGNSVNIGSTVFSTMLGIVENMVCGNYvFKKGDELATELKGMVRDVLKLSGEPN 215
Cdd:cd11027   81 PRLE--EKIAE-EAEKLLKRL--ASQEGQPFDPKDELFLAVLNVICSITFGKR-YKLDDPEFLRLLDLNDKFFELLGAGS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 216 ASDFFPFLRGLDLQGVeRRAQKLRERFDGIFSEMIERRLKDMREK-------GMVNERDEESGRGIKESdflGVLLElmd 288
Cdd:cd11027  155 LLDIFPFLKYFPNKAL-RELKELMKERDEILRKKLEEHKETFDPGnirdltdALIKAKKEAEDEGDEDS---GLLTD--- 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 289 hneglqmEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLR 368
Cdd:cd11027  228 -------DHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLR 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 369 LHPAAPLLIPR--LCDSdcQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRI 446
Cdd:cd11027  301 LSSVVPLALPHktTCDT--TLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVPKPESFLPFSAGRRV 378
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 586644824 447 CIGMPLASSMVHLVLGSLLHYFNWKVEGEV---DMTEEFGITL 486
Cdd:cd11027  379 CLGESLAKAELFLFLARLLQKFRFSPPEGEpppELEGIPGLVL 421
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
31-498 5.04e-76

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 247.72  E-value: 5.04e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  31 PSPPKWPIIGH-LHLLGKLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGG 109
Cdd:PLN02394  33 PGPAAVPIFGNwLQVGDDLNHRNLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKG 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 110 NSLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSKTMASIY-EESIKGNSVNIGSTVFSTMLGIVENMVCGNY 188
Cdd:PLN02394 113 QDMVFTVYGDHWRKMRRIMTVPFFTNKVVQQYRYGWEEEADLVVEDVRaNPEAATEGVVIRRRLQLMMYNIMYRMMFDRR 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 189 VFKKGDELATELKGM--VRDVLKLSGEPNASDFFPFLRGLdLQGVERRAQKLRERFDGIFSE-MIERRLKDMREKGMVNE 265
Cdd:PLN02394 193 FESEDDPLFLKLKALngERSRLAQSFEYNYGDFIPILRPF-LRGYLKICQDVKERRLALFKDyFVDERKKLMSAKGMDKE 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 266 RDEESGRGIKESDFLGVLLElmdhneglqmEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKD 345
Cdd:PLN02394 272 GLKCAIDHILEAQKKGEINE----------DNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPG 341
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 346 KMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVG 425
Cdd:PLN02394 342 NQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLE 421
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 426 --TNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV---EGEVDMTEEFG-ITLQKALPLVVVATP 498
Cdd:PLN02394 422 eeAKVEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPppgQSKIDVSEKGGqFSLHIAKHSTVVFKP 500
PLN02966 PLN02966
cytochrome P450 83A1
31-495 6.42e-75

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 245.04  E-value: 6.42e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  31 PSPPKWPIIGHLHLLGKL-PHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGG 109
Cdd:PLN02966  32 PGPSPLPVIGNLLQLQKLnPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRPPHRGHEFISYGR 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 110 NSLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGstvfSTMLGIVENMVCGNYV 189
Cdd:PLN02966 112 RDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAADKSEVVDIS----ELMLTFTNSVVCRQAF 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 190 FKKGDELATELKGMVRDVL---KLSGEPNASDFFPFLRGL-DLQGVERRAQKLRERFDGIFSEMIERRLKDMREKgmvne 265
Cdd:PLN02966 188 GKKYNEDGEEMKRFIKILYgtqSVLGKIFFSDFFPYCGFLdDLSGLTAYMKECFERQDTYIQEVVNETLDPKRVK----- 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 266 rdEESGRGIkesDFLGVLLELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKD 345
Cdd:PLN02966 263 --PETESMI---DLLMEIYKEQPFASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEK 337
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 346 --KMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWS-DPLKFDPSR 422
Cdd:PLN02966 338 gsTFVTEDDVKNLPYFRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWGpNPDEFRPER 417
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586644824 423 FVGTNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEG-----EVDMTEEFGITLQKALPLVVV 495
Cdd:PLN02966 418 FLEKEVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNgmkpdDINMDVMTGLAMHKSQHLKLV 495
PLN02655 PLN02655
ent-kaurene oxidase
31-498 1.02e-71

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 235.41  E-value: 1.02e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  31 PSPPKWPIIGHLHLLG-KLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKThdrKFSS---RPVPLAAKTLS 106
Cdd:PLN02655   2 PAVPGLPVIGNLLQLKeKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVT---KFSSistRKLSKALTVLT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 107 YGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSKTMASIYEE--SIKGNSVN----IGSTVFStmLGIV 180
Cdd:PLN02655  79 RDKSMVATSDYGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSGLHALvkDDPHSPVNfrdvFENELFG--LSLI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 181 ENM---VCGNYVFKKGDELATE--LKGMVRDVLKLSGEPNASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLK 255
Cdd:PLN02655 157 QALgedVESVYVEELGTEISKEeiFDVLVHDMMMCAIEVDWRDFFPYLSWIPNKSFETRVQTTEFRRTAVMKALIKQQKK 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 256 DMrekgmvnerdeesGRGIKESDFLGVLLElmdHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEAR 335
Cdd:PLN02655 237 RI-------------ARGEERDCYLDFLLS---EATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLY 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 336 DELRRVIGKDKMMEEsHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDP 415
Cdd:PLN02655 301 REIREVCGDERVTEE-DLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENP 379
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 416 LKFDPSRFVGTNLEfKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV-EGEVDMTEEFGITLQKALPLVV 494
Cdd:PLN02655 380 EEWDPERFLGEKYE-SADMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLrEGDEEKEDTVQLTTQKLHPLHA 458

                 ....
gi 586644824 495 VATP 498
Cdd:PLN02655 459 HLKP 462
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
61-486 1.73e-67

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: 222.00  E-value: 1.73e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKTHdRKFSSRPVPLAAKTLSYGGNSLVwAAYGHHWRLLRRLsFTELFSTKRLNS 140
Cdd:cd00302    1 GPVFRVRLGGGPVVVVSDPELVREVLRDP-RDFSSDAGPGLPALGDFLGDGLL-TLDGPEHRRLRRL-LAPAFTPRALAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 141 MEKFRKAEVSKTMASIyeESIKGNSVNIGSTVFSTMLGIVENMVCGnyvfKKGDELATELKGMVRDVLKLSGEPNASDFF 220
Cdd:cd00302   78 LRPVIREIARELLDRL--AAGGEVGDDVADLAQPLALDVIARLLGG----PDLGEDLEELAELLEALLKLLGPRLLRPLP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 221 PflrgldlqGVERRAQKLRERFDGIFSEMIERRLKDMrekgmvnerdeesgrgikESDFLGVLLELMDHNEGLQMEHVKG 300
Cdd:cd00302  152 S--------PRLRRLRRARARLRDYLEELIARRRAEP------------------ADDLDLLLLADADDGGGLSDEEIVA 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 301 MLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDkmmEESHIPDVPFLQAIVKEVLRLHPAAPLLiPRL 380
Cdd:cd00302  206 ELLTLLLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG---TPEDLSKLPYLEAVVEETLRLYPPVPLL-PRV 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 381 CDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGtnlEFKGNDYELLPFGAGRRICIGMPLASSMVHLV 460
Cdd:cd00302  282 ATEDVELGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLP---EREEPRYAHLPFGAGPHRCLGARLARLELKLA 358
                        410       420
                 ....*....|....*....|....*.
gi 586644824 461 LGSLLHYFNWKVEGEVDMTEEFGITL 486
Cdd:cd00302  359 LATLLRRFDFELVPDEELEWRPSLGT 384
PLN02971 PLN02971
tryptophan N-hydroxylase
31-505 2.42e-64

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 217.98  E-value: 2.42e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  31 PSPPKWPIIGHL-HLLGKLP-----HQSLAALSLTygpIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKT 104
Cdd:PLN02971  60 PGPTGFPIVGMIpAMLKNRPvfrwlHSLMKELNTE---IACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKI 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 105 LSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMV 184
Cdd:PLN02971 137 LSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLM 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 185 CGNYVFKKGdelaTELKG--MVRDVLKLSGEPNA---------SDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERR 253
Cdd:PLN02971 217 FGTRTFSEK----TEPDGgpTLEDIEHMDAMFEGlgftfafciSDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDER 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 254 LKDMREkgmvnerdeesGRGIKESDFLGVLLELMDH--NEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVM 331
Cdd:PLN02971 293 IKMWRE-----------GKRTQIEDFLDIFISIKDEagQPLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEIL 361
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 332 EEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKV 411
Cdd:PLN02971 362 HKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKV 441
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 412 WSDPLKFDPSRFVG--TNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEGEVDMTE--EFGITLQ 487
Cdd:PLN02971 442 WSDPLSFKPERHLNecSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSETRVElmESSHDMF 521
                        490
                 ....*....|....*...
gi 586644824 488 KALPLVVVATPSLPLNPY 505
Cdd:PLN02971 522 LSKPLVMVGELRLSEDLY 539
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
59-483 5.55e-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: 214.26  E-value: 5.55e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  59 TYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRL 138
Cdd:cd11074    2 KFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGEHWRKMRRIMTVPFFTNKVV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 139 NSMEKFRKAEvsktMASIYEESIKGNSVNIGSTVFS-----TMLGIVENMVCGNYVFKKGDELATELKGM--VRDVLKLS 211
Cdd:cd11074   82 QQYRYGWEEE----AARVVEDVKKNPEAATEGIVIRrrlqlMMYNNMYRIMFDRRFESEDDPLFVKLKALngERSRLAQS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 212 GEPNASDFFPFLRGLdLQGVERRAQKLRERFDGIFSE-MIERRLKDMREKGMVNERDEESGRGIKESDFLGvllELMDHN 290
Cdd:cd11074  158 FEYNYGDFIPILRPF-LRGYLKICKEVKERRLQLFKDyFVDERKKLGSTKSTKNEGLKCAIDHILDAQKKG---EINEDN 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 291 EGLQMEHVKgmlmdmfIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLH 370
Cdd:cd11074  234 VLYIVENIN-------VAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLR 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 371 PAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVG--TNLEFKGNDYELLPFGAGRRICI 448
Cdd:cd11074  307 MAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEeeSKVEANGNDFRYLPFGVGRRSCP 386
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 586644824 449 GMPLASSMVHLVLGSLLHYFNWKV---EGEVDMTEEFG 483
Cdd:cd11074  387 GIILALPILGITIGRLVQNFELLPppgQSKIDTSEKGG 424
PTZ00404 PTZ00404
cytochrome P450; Provisional
27-489 2.96e-63

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 213.43  E-value: 2.96e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  27 KAQAPSPPKWPIIGHLHLLGKLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRP-VPLAAKTL 105
Cdd:PTZ00404  28 KNELKGPIPIPILGNLHQLGNLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPkIPSIKHGT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 106 SYGGNSlvwAAYGHHWRLLRRLSftelfstkrLNSMEKFR--------KAEVSKTMASIYEESIKGNSVN----IGSTVF 173
Cdd:PTZ00404 108 FYHGIV---TSSGEYWKRNREIV---------GKAMRKTNlkhiydllDDQVDVLIESMKKIESSGETFEpryyLTKFTM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 174 STMLGIVENM-VCGNYVFKKGDElaTELKGMVRDVLKLSGEPNASDFFPFLRGLDLQGVERraqklrerFDGIFSEMieR 252
Cdd:PTZ00404 176 SAMFKYIFNEdISFDEDIHNGKL--AELMGPMEQVFKDLGSGSLFDVIEITQPLYYQYLEH--------TDKNFKKI--K 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 253 RLKDMREKGMVNERDEESGRgikesDFLGVLL-ELMDHNEGlQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVM 331
Cdd:PTZ00404 244 KFIKEKYHEHLKTIDPEVPR-----DLLDLLIkEYGTNTDD-DILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQ 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 332 EEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQI-DGHIIEKNTEVLVNVWAIGRDPK 410
Cdd:PTZ00404 318 EKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFGLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNEK 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 411 VWSDPLKFDPSRFVGTNlefkgNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEGE--VDMTEEFGITLQK 488
Cdd:PTZ00404 398 YFENPEQFDPSRFLNPD-----SNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGkkIDETEEYGLTLKP 472

                 .
gi 586644824 489 A 489
Cdd:PTZ00404 473 N 473
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
60-487 7.21e-58

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: 197.93  E-value: 7.21e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTKRLN 139
Cdd:cd20673    1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRNGKDIAFADYSATWQLHRKLVHSAFALFGEGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 140 -SMEKFRKAEVSkTMASIYEESiKGNSVNIGSTVFSTMLGIVeNMVCGNYVFKKGD-ELATELK---GMVRDVlklsGEP 214
Cdd:cd20673   81 qKLEKIICQEAS-SLCDTLATH-NGESIDLSPPLFRAVTNVI-CLLCFNSSYKNGDpELETILNyneGIVDTV----AKD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 215 NASDFFPFL-----RGLDL--QGVERRAQKLRERFD---GIFSEMIERRLKDMREKGMVNERDEESGRGikesdflgvll 284
Cdd:cd20673  154 SLVDIFPWLqifpnKDLEKlkQCVKIRDKLLQKKLEehkEKFSSDSIRDLLDALLQAKMNAENNNAGPD----------- 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 285 elmDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVK 364
Cdd:cd20673  223 ---QDSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIR 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 365 EVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFV---GTNLEFKGNDYelLPFG 441
Cdd:cd20673  300 EVLRIRPVAPLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLdptGSQLISPSLSY--LPFG 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 586644824 442 AGRRICIGMPLASSMVHLVLGSLLHYFNWKVEGEV---DMTEEFGITLQ 487
Cdd:cd20673  378 AGPRVCLGEALARQELFLFMAWLLQRFDLEVPDGGqlpSLEGKFGVVLQ 426
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
60-486 3.18e-57

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: 196.36  E-value: 3.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSyGGNSLVWAAYGHHWRLLRRLSFTEL--FSTKR 137
Cdd:cd11028    1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFIS-NGKSMAFSDYGPRWKLHRKLAQNALrtFSNAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 138 L-NSMEKFRKAEVSKTMASIYEESIKGNSVN----IGSTVFSTMLGIvenmvCGNYVFKKGDELATELKGMVRDVLKLSG 212
Cdd:cd11028   80 ThNPLEEHVTEEAEELVTELTENNGKPGPFDprneIYLSVGNVICAI-----CFGKRYSRDDPEFLELVKSNDDFGAFVG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 213 EPNASDFFPFLRGLDLQGVeRRAQKLRERFDGIFSEMIERRLKDMREKgmvNERD---------EESGRGIKESDflgvl 283
Cdd:cd11028  155 AGNPVDVMPWLRYLTRRKL-QKFKELLNRLNSFILKKVKEHLDTYDKG---HIRDitdalikasEEKPEEEKPEV----- 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 284 lelmdhneGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIV 363
Cdd:cd11028  226 --------GLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFI 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 364 KEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYEL-LPFGA 442
Cdd:cd11028  298 LETMRHSSFVPFTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDKTKVDKfLPFGA 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 586644824 443 GRRICIGMPLASSMVHLVLGSLLH--YFNWKVEGEVDMTEEFGITL 486
Cdd:cd11028  378 GRRRCLGEELARMELFLFFATLLQqcEFSVKPGEKLDLTPIYGLTM 423
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
61-486 1.86e-54

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: 188.58  E-value: 1.86e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFktHDRKFSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRlsftelFSTKRL-- 138
Cdd:cd20651    1 GDVVGLKLGKDKVVVVSGYEAVREVL--SREEFDGRPDGFFFRLRTFGKRLGITFTDGPFWKEQRR------FVLRHLrd 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 139 -----NSMEKFRKAEVSKTMASIYEEsiKGNSVNIGSTVFSTMLGIVENMVCGNYvFKKGDELATELKGMVRDVLKL--- 210
Cdd:cd20651   73 fgfgrRSMEEVIQEEAEELIDLLKKG--EKGPIQMPDLFNVSVLNVLWAMVAGER-YSLEDQKLRKLLELVHLLFRNfdm 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 211 SGepNASDFFPFLRGL--DLQGVeRRAQKLRERFDGIFSEMIERRLKDMREKgmvNERDeesgrgikesdFLGVLLELMD 288
Cdd:cd20651  150 SG--GLLNQFPWLRFIapEFSGY-NLLVELNQKLIEFLKEEIKEHKKTYDED---NPRD-----------LIDAYLREMK 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 289 HNE----GLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVK 364
Cdd:cd20651  213 KKEppssSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVIL 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 365 EVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYeLLPFGAGR 444
Cdd:cd20651  293 EVLRIFTLVPIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEW-FLPFGAGK 371
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 586644824 445 RICIGMPLASSMVHLVLGSLLHYFNWKVEGEVDMTEE---FGITL 486
Cdd:cd20651  372 RRCLGESLARNELFLFFTGLLQNFTFSPPNGSLPDLEgipGGITL 416
PLN03018 PLN03018
homomethionine N-hydroxylase
31-505 1.28e-53

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 189.07  E-value: 1.28e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  31 PSPPKWPIIGHL-HLLGKLPHQSLAALSLT--YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSY 107
Cdd:PLN03018  43 PGPPGWPILGNLpELIMTRPRSKYFHLAMKelKTDIACFNFAGTHTITINSDEIAREAFRERDADLADRPQLSIMETIGD 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 108 GGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNI-------GSTVFSTMLgIV 180
Cdd:PLN03018 123 NYKSMGTSPYGEQFMKMKKVITTEIMSVKTLNMLEAARTIEADNLIAYIHSMYQRSETVDVrelsrvyGYAVTMRML-FG 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 181 ENMVCGNYVFKKGDELATELKGMVRDVLK-LSGEPNAS--DFFP-FLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKD 256
Cdd:PLN03018 202 RRHVTKENVFSDDGRLGKAEKHHLEVIFNtLNCLPGFSpvDYVErWLRGWNIDGQEERAKVNVNLVRSYNNPIIDERVEL 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 257 MREKGmvnerdeesGRGIKEsDFLGVLLELMDHNEG--LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEA 334
Cdd:PLN03018 282 WREKG---------GKAAVE-DWLDTFITLKDQNGKylVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKA 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 335 RDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSD 414
Cdd:PLN03018 352 LKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKD 431
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 415 PLKFDPSRFV---GTNLEFKGNDYEL--LPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVE---GEVDMtEEFGITL 486
Cdd:PLN03018 432 PLVYEPERHLqgdGITKEVTLVETEMrfVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHqdfGPLSL-EEDDASL 510
                        490
                 ....*....|....*....
gi 586644824 487 QKALPLVVVATPSLPLNPY 505
Cdd:PLN03018 511 LMAKPLLLSVEPRLAPNLY 529
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
60-468 2.31e-53

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: 185.69  E-value: 2.31e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSphpAKQIFKTHDRK---FSSRPVPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTELFSTK 136
Cdd:cd20674    1 YGPIYRLRLGLQDVVVLNS---KRTIREALVRKwadFAGRPHSYTGKLVSQGGQDLSLGDYSLLWKAHRKLTRSALQLGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 137 RlNSMEkfrkAEVSKTMASIYEE--SIKGNSVNIgSTVFSTMlgiVENMVCgNYVFKKGDELATELK---GMVRDVLKLS 211
Cdd:cd20674   78 R-NSLE----PVVEQLTQELCERmrAQAGTPVDI-QEEFSLL---TCSIIC-CLTFGDKEDKDTLVQafhDCVQELLKTW 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 212 GEPN--ASDFFPFLRGLDLQGVeRRAQKLRERFDGIfsemIERRLKDMREkGMVnerdEESGRGIKESDFLGVLLELMDH 289
Cdd:cd20674  148 GHWSiqALDSIPFLRFFPNPGL-RRLKQAVENRDHI----VESQLRQHKE-SLV----AGQWRDMTDYMLQGLGQPRGEK 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 290 NEG-LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLR 368
Cdd:cd20674  218 GMGqLLEGHVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLR 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 369 LHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFvgtnLEFKGNDYELLPFGAGRRICI 448
Cdd:cd20674  298 LRPVVPLALPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERF----LEPGAANRALLPFGCGARVCL 373
                        410       420
                 ....*....|....*....|
gi 586644824 449 GMPLASSMVHLVLGSLLHYF 468
Cdd:cd20674  374 GEPLARLELFVFLARLLQAF 393
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
53-465 2.60e-53

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: 185.48  E-value: 2.60e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  53 LAALSLTYGPIMPFKL-GMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLsYGGNSLVWAAYGHHwRLLRRLSfTE 131
Cdd:cd11053    4 LERLRARYGDVFTLRVpGLGPVVVLSDPEAIKQIFTADPDVLHPGEGNSLLEPL-LGPNSLLLLDGDRH-RRRRKLL-MP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 132 LFSTKRLnsmekfrkAEVSKTMASIYEESIKGNSVNigsTVFST-------MLGIVENMVCGNYVfkkGDELAtELKGMV 204
Cdd:cd11053   81 AFHGERL--------RAYGELIAEITEREIDRWPPG---QPFDLrelmqeiTLEVILRVVFGVDD---GERLQ-ELRRLL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 205 RDVLKLSGEPNASdfFPFLRgLDLQGVE--RRAQKLRERFDGIFSEMIERRlkdmRekgmvneRDEESGRgikeSDFLGV 282
Cdd:cd11053  146 PRLLDLLSSPLAS--FPALQ-RDLGPWSpwGRFLRARRRIDALIYAEIAER----R-------AEPDAER----DDILSL 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 283 LLELMDHN-EGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDkmmEESHIPDVPFLQA 361
Cdd:cd11053  208 LLSARDEDgQPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDP---DPEDIAKLPYLDA 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 362 IVKEVLRLHPAAPLlIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFkgndYELLPFG 441
Cdd:cd11053  285 VIKETLRLYPVAPL-VPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRKPSP----YEYLPFG 359
                        410       420
                 ....*....|....*....|....
gi 586644824 442 AGRRICIGMPLASSMVHLVLGSLL 465
Cdd:cd11053  360 GGVRRCIGAAFALLEMKVVLATLL 383
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
49-496 3.33e-53

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: 184.71  E-value: 3.33e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  49 PHQSLAALsLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLVwAAYGHHWRLLRRLs 128
Cdd:COG2124   21 PYPFYARL-REYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDSLL-TLDGPEHTRLRRL- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 129 FTELFSTKRLNSMEkfrkAEVSKTMASIYEESIKGNSVNIGS--------TVFSTMLGIvenmvcgnyvfkkGDELATEL 200
Cdd:COG2124   98 VQPAFTPRRVAALR----PRIREIADELLDRLAARGPVDLVEefarplpvIVICELLGV-------------PEEDRDRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 201 KGMVRDVLklsgepNASDFFPFLRgldlqgvERRAQKLRERFDGIFSEMIERRLKDMREkgmvnerdeesgrgikesDFL 280
Cdd:COG2124  161 RRWSDALL------DALGPLPPER-------RRRARRARAELDAYLRELIAERRAEPGD------------------DLL 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 281 GVLLELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPyvmeEARDELRRvigkdkmmeeshipDVPFLQ 360
Cdd:COG2124  210 SALLAARDDGERLSDEELRDELLLLLLAGHETTANALAWALYALLRHP----EQLARLRA--------------EPELLP 271
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 361 AIVKEVLRLHPAAPLLiPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefkgNDYELLPF 440
Cdd:COG2124  272 AAVEETLRLYPPVPLL-PRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPF 340
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 441 GAGRRICIGMPLASSMVHLVLGSLLHYF-NWKVEGEVDMTEEFGITLQ--KALPLVVVA 496
Cdd:COG2124  341 GGGPHRCLGAALARLEARIALATLLRRFpDLRLAPPEELRWRPSLTLRgpKSLPVRLRP 399
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
60-487 3.72e-53

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: 185.10  E-value: 3.72e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVP-LAAKTLsyggNSLVWAAYGHHWRLLRRLsFTELFSTKRL 138
Cdd:cd11055    2 YGKVFGLYFGTIPVIVVSDPEMIKEILVKEFSNFTNRPLFiLLDEPF----DSSLLFLKGERWKRLRTT-LSPTFSSGKL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 139 NSMEKFRKAEVSKTMASIYEESIKGNSVNIGS--------TVFSTMLGIVENmvcgnyVFKKGDELATElkgMVRDVLKL 210
Cdd:cd11055   77 KLMVPIINDCCDELVEKLEKAAETGKPVDMKDlfqgftldVILSTAFGIDVD------SQNNPDDPFLK---AAKKIFRN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 211 SGEPNASDFFPFLRGLDLqgveRRAQKLRERFDGI--FSEMIERRLKDmREKGMVNERdeesgrgikeSDFLGVLLELMD 288
Cdd:cd11055  148 SIIRLFLLLLLFPLRLFL----FLLFPFVFGFKSFsfLEDVVKKIIEQ-RRKNKSSRR----------KDLLQLMLDAQD 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 289 HNE-----GLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIV 363
Cdd:cd11055  213 SDEdvskkKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVI 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 364 KEVLRLHPAAPLLIpRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNlEFKGNDYELLPFGAG 443
Cdd:cd11055  293 NETLRLYPPAFFIS-RECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPEN-KAKRHPYAYLPFGAG 370
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 586644824 444 RRICIGMPLASSMVHLVLGSLLHYFNWKV--EGEVDMTEEFGITLQ 487
Cdd:cd11055  371 PRNCIGMRFALLEVKLALVKILQKFRFVPckETEIPLKLVGGATLS 416
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
60-482 6.00e-50

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: 176.56  E-value: 6.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKtHDRKFSSRPVPLAAKT--LSYGGNSLVWAAYGHHWRLLRRLSFTELFstkR 137
Cdd:cd11054    4 YGPIVREKLGGRDIVHLFDPDDIEKVFR-NEGKYPIRPSLEPLEKyrKKRGKPLGLLNSNGEEWHRLRSAVQKPLL---R 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 138 LNSMEKFRKA--EVSKTMASIYEESIKGNSVN---------------IGSTVFSTMLGIVENmvcgnyvfkKGDELATEL 200
Cdd:cd11054   80 PKSVASYLPAinEVADDFVERIRRLRDEDGEEvpdledelykwslesIGTVLFGKRLGCLDD---------NPDSDAQKL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 201 KGMVRDVLKLSGEpnaSDF-FPFLRGLDLqgveRRAQKLRERFDGIFS---EMIERRLKDMREKGMVNErdeesgrgiKE 276
Cdd:cd11054  151 IEAVKDIFESSAK---LMFgPPLWKYFPT----PAWKKFVKAWDTIFDiasKYVDEALEELKKKDEEDE---------EE 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 277 SDFLGVLLelmdHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDV 356
Cdd:cd11054  215 DSLLEYLL----SKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKM 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 357 PFLQAIVKEVLRLHPAAPlLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRF-VGTNLEFKGNDY 435
Cdd:cd11054  291 PYLKACIKESLRLYPVAP-GNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlRDDSENKNIHPF 369
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 586644824 436 ELLPFGAGRRICIGMPLASSMVHLVLGSLLHyfNWKVE---GEVDMTEEF 482
Cdd:cd11054  370 ASLPFGFGPRMCIGRRFAELEMYLLLAKLLQ--NFKVEyhhEELKVKTRL 417
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
61-487 1.92e-49

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: 174.69  E-value: 1.92e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLsyGGNSLVwAAYGHHWRLLRRLSfTELFSTKRLNS 140
Cdd:cd20620    1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVKGGVYERLKLL--LGNGLL-TSEGDLWRRQRRLA-QPAFHRRRIAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 141 MEKFRKAEVSKTMASIyEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVFKKGDELATELKGMVRDVLKLsgepnASDFF 220
Cdd:cd20620   77 YADAMVEATAALLDRW-EAGARRGPVDVHAEMMRLTLRIVAKTLFGTDVEGEADEIGDALDVALEYAARR-----MLSPF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 221 PFLRGLdLQGVERRAQKLRERFDGIFSEMIERRLKDMREKG-----MVNERDEESGRGikesdflgvllelMDhNEGLQM 295
Cdd:cd20620  151 LLPLWL-PTPANRRFRRARRRLDEVIYRLIAERRAAPADGGdllsmLLAARDEETGEP-------------MS-DQQLRD 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 296 EhvkgmLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGkDKMMEESHIPDVPFLQAIVKEVLRLHPAAPL 375
Cdd:cd20620  216 E-----VMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLRLYPPAWI 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 376 lIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFvGTNLEFKGNDYELLPFGAGRRICIGMPLAss 455
Cdd:cd20620  290 -IGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERF-TPEREAARPRYAYFPFGGGPRICIGNHFA-- 365
                        410       420       430
                 ....*....|....*....|....*....|....
gi 586644824 456 MV--HLVLGSLLHYFNWKVEGEVDMTEEFGITLQ 487
Cdd:cd20620  366 MMeaVLLLATIAQRFRLRLVPGQPVEPEPLITLR 399
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
61-468 6.51e-49

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: 173.86  E-value: 6.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKTHDrkfssrpvpLAAKTLSYG------GNSLVWAAyGHHWRLLRRLsFTELFS 134
Cdd:cd20628    1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSK---------LITKSFLYDflkpwlGDGLLTST-GEKWRKRRKL-LTPAFH 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 135 TKRLNS-MEKFRKAevSKTMASIYEESIKGNSVNIGS--------TVFSTMLGIveNMVCGN-----YV--FKKGDELAt 198
Cdd:cd20628   70 FKILESfVEVFNEN--SKILVEKLKKKAGGGEFDIFPyislctldIICETAMGV--KLNAQSnedseYVkaVKRILEII- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 199 eLKGMVRDVLKlsgepnaSDFFPFLRGLdlqgvERRAQKLRERFDGIFSEMIERRLKDMREKGMVNERDEESGRGiKESD 278
Cdd:cd20628  145 -LKRIFSPWLR-------FDFIFRLTSL-----GKEQRKALKVLHDFTNKVIKERREELKAEKRNSEEDDEFGKK-KRKA 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 279 FLGVLLELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEE-SHIPDVP 357
Cdd:cd20628  211 FLDLLLEAHEDGGPLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDRRPTlEDLNKMK 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 358 FLQAIVKEVLRLHPAAPLlIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEfKGNDYEL 437
Cdd:cd20628  291 YLERVIKETLRLYPSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSA-KRHPYAY 368
                        410       420       430
                 ....*....|....*....|....*....|.
gi 586644824 438 LPFGAGRRICIGMPLASSMVHLVLGSLLHYF 468
Cdd:cd20628  369 IPFSAGPRNCIGQKFAMLEMKTLLAKILRNF 399
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
61-486 8.53e-48

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: 171.05  E-value: 8.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKThdRKFSSR-PVPLAAKTLSYGGnslVWAAYGHHWRLLRRLSFTEL------- 132
Cdd:cd20652    1 GSIFSLKMGSVYTVVLSDPKLIRDTFRR--DEFTGRaPLYLTHGIMGGNG---IICAEGDLWRDQRRFVHDWLrqfgmtk 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 133 FSTKRlNSMEKFRKAEVSKTMASIYEESikGNSVNIGSTVFSTMLGIVENMVCGnYVFKKGDELATELKGMVRDVLKLSG 212
Cdd:cd20652   76 FGNGR-AKMEKRIATGVHELIKHLKAES--GQPVDPSPVLMHSLGNVINDLVFG-FRYKEDDPTWRWLRFLQEEGTKLIG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 213 EPNASDFFPFLRGL-DLQGVERRAQKLRERFDGIFSEMIE---RRLKDMREKGMVNERDEESGRGIKESDFLGVLLELMd 288
Cdd:cd20652  152 VAGPVNFLPFLRHLpSYKKAIEFLVQGQAKTHAIYQKIIDehkRRLKPENPRDAEDFELCELEKAKKEGEDRDLFDGFY- 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 289 HNEglQMEHVkgmLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLR 368
Cdd:cd20652  231 TDE--QLHHL---LADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQR 305
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 369 LHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYeLLPFGAGRRICI 448
Cdd:cd20652  306 IRSVVPLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEA-FIPFQTGKRMCL 384
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 586644824 449 GMPLASSMVHLVLGSLLHYFNWKVEGEVDMTEEF---GITL 486
Cdd:cd20652  385 GDELARMILFLFTARILRKFRIALPDGQPVDSEGgnvGITL 425
PLN00168 PLN00168
Cytochrome P450; Provisional
31-490 9.48e-48

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 172.83  E-value: 9.48e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  31 PSPPKWPIIGHLHLLGKLPHQSLAALS---LTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSY 107
Cdd:PLN00168  38 PGPPAVPLLGSLVWLTNSSADVEPLLRrliARYGPVVSLRVGSRLSVFVADRRLAHAALVERGAALADRPAVASSRLLGE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 108 GGNSLVWAAYGHHWRLLRRLSFTELFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGn 187
Cdd:PLN00168 118 SDNTITRSSYGPVWRLLRRNLVAETLHPSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVETFQYAMFCLLVLMCFG- 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 188 yvfKKGDELATELKGMV-RD-VLKLSGEPNASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKdmREKGMVNE 265
Cdd:PLN00168 197 ---ERLDEPAVRAIAAAqRDwLLYVSKKMSVFAFFPAVTKHLFRGRLQKALALRRRQKELFVPLIDARRE--YKNHLGQG 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 266 RDEESGRGIKESDFLGVLLELMDHNEG---LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVI 342
Cdd:PLN00168 272 GEPPKKETTFEHSYVDTLLDIRLPEDGdraLTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKT 351
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 343 GKDK-MMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPS 421
Cdd:PLN00168 352 GDDQeEVSEEDVHKMPYLKAVVLEGLRKHPPAHFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPE 431
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 422 RFV----GTNLEFKGN-DYELLPFGAGRRICIGMPLAssMVHL--VLGSLLHYFNWK-VEG-EVDMTE--EFGITLQKAL 490
Cdd:PLN00168 432 RFLaggdGEGVDVTGSrEIRMMPFGVGRRICAGLGIA--MLHLeyFVANMVREFEWKeVPGdEVDFAEkrEFTTVMAKPL 509
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
60-487 1.21e-46

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: 167.74  E-value: 1.21e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRP-VPLAAKTL-SYGgnslVWAAYGHHWRLLRRLSFTEL--F-S 134
Cdd:cd11026    1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPpVPLFDRVTkGYG----VVFSNGERWKQLRRFSLTTLrnFgM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 135 TKRlnSMEkFRKAEVSKTMASIYEESiKGNSVNigstvFSTMLG-IVENMVCgNYVFKK----GDELATELKGMVRDVLK 209
Cdd:cd11026   77 GKR--SIE-ERIQEEAKFLVEAFRKT-KGKPFD-----PTFLLSnAVSNVIC-SIVFGSrfdyEDKEFLKLLDLINENLR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 210 LSGEP-----NAsdFFPFLRGLDLqgverRAQKLRERFDGIFSeMIERRLKDMREKgmvneRDEESGRgikesDFLGVLL 284
Cdd:cd11026  147 LLSSPwgqlyNM--FPPLLKHLPG-----PHQKLFRNVEEIKS-FIRELVEEHRET-----LDPSSPR-----DFIDCFL 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 285 ELMD-HNEGLQME-HVKGMLM---DMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFL 359
Cdd:cd11026  209 LKMEkEKDNPNSEfHEENLVMtvlDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYT 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 360 QAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYeLLP 439
Cdd:cd11026  289 DAVIHEVQRFGDIVPLGVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEA-FMP 367
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 586644824 440 FGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV---EGEVDMTEEF-GITLQ 487
Cdd:cd11026  368 FSAGKRVCLGEGLARMELFLFFTSLLQRFSLSSpvgPKDPDLTPRFsGFTNS 419
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
50-474 2.21e-45

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: 164.23  E-value: 2.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  50 HQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPvplaAKTLS--YG----GNSLVWAAYGHHWRL 123
Cdd:cd20613    1 HDLLLEWAKEYGPVFVFWILHRPIVVVSDPEAVKEVLITLNLPKPPRV----YSRLAflFGerflGNGLVTEVDHEKWKK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 124 LRRLsFTELFSTKRL-NSMEKF-RKAEV----------SKTMASIYEESikgNSV---NIGSTVFSTMLGIVENmvcGNY 188
Cdd:cd20613   77 RRAI-LNPAFHRKYLkNLMDEFnESADLlveklskkadGKTEVNMLDEF---NRVtldVIAKVAFGMDLNSIED---PDS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 189 VFKKgdELATELKGMVRDVLKLSGEPNASDFfPFLRGldlqgVERRAQKLRErfdgIFSEMIERRLKDMRekgmvneRDE 268
Cdd:cd20613  150 PFPK--AISLVLEGIQESFRNPLLKYNPSKR-KYRRE-----VREAIKFLRE----TGRECIEERLEALK-------RGE 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 269 ESgrgikESDFLGVLLELMDHNEGLQMEHvkgmLMD----MFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGK 344
Cdd:cd20613  211 EV-----PNDILTHILKASEEEPDFDMEE----LLDdfvtFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGS 281
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 345 DKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIpRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFV 424
Cdd:cd20613  282 KQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTS-RELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFS 360
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 586644824 425 GTNLEFKGNdYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWK-VEG 474
Cdd:cd20613  361 PEAPEKIPS-YAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFElVPG 410
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
60-486 3.17e-45

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: 163.79  E-value: 3.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRP-VPLAakTLSYGGNSLVWAAYGHHWRLLRRLSFTEL--FSTK 136
Cdd:cd20666    1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPsVPLV--TILTKGKGIVFAPYGPVWRQQRKFSHSTLrhFGLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 137 RLnSMEkfrkAEVSKTMASIYEESIK--GNSVNIGSTVFSTMLGIVENMVCGNYVFKKGDELATELKGMVRdVLKLSGEP 214
Cdd:cd20666   79 KL-SLE----PKIIEEFRYVKAEMLKhgGDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLMSR-GLEISVNS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 215 NASDFF--PFLRGLDLQGVerraQKLRErFDGIFSEMIERRLKDMREKgmvneRDEESGRgikesDFLGV-LLELMDHNE 291
Cdd:cd20666  153 AAILVNicPWLYYLPFGPF----RELRQ-IEKDITAFLKKIIADHRET-----LDPANPR-----DFIDMyLLHIEEEQK 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 292 G-----LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEV 366
Cdd:cd20666  218 NnaessFNEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEV 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 367 LRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYeLLPFGAGRRI 446
Cdd:cd20666  298 QRMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEA-FIPFGIGRRV 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 586644824 447 CIGMPLASSMVHLVLGSLLHYFNWKVEGEV---DMTEEFGITL 486
Cdd:cd20666  377 CMGEQLAKMELFLMFVSLMQSFTFLLPPNApkpSMEGRFGLTL 419
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
52-485 6.04e-44

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: 160.61  E-value: 6.04e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  52 SLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSrpVPLAAKTLSY-GGNSLVwAAYGHHWRLlRRLSFT 130
Cdd:cd11046    2 DLYKWFLEYGPIYKLAFGPKSFLVISDPAIAKHVLRSNAFSYDK--KGLLAEILEPiMGKGLI-PADGEIWKK-RRRALV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 131 ELFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVenmvcGNYVFKKGDELATELKGMVRDV-LK 209
Cdd:cd11046   78 PALHKDYLEMMVRVFGRCSERLMEKLDAAAETGESVDMEEEFSSLTLDII-----GLAVFNYDFGSVTEESPVIKAVyLP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 210 LSGEPNASDFFP----FLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKDMREKGMvnERDEESGRGIKESDFLGVLLE 285
Cdd:cd11046  153 LVEAEHRSVWEPpywdIPAALFIVPRQRKFLRDLKLLNDTLDDLIRKRKEMRQEEDI--ELQQEDYLNEDDPSLLRFLVD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 286 LMDhnEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKE 365
Cdd:cd11046  231 MRD--EDVDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNE 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 366 VLRLHPAAPLLIPRLCDSDCQIDGHI-IEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFV---GTNLEFKGNDYELLPFG 441
Cdd:cd11046  309 SLRLYPQPPVLIRRAVEDDKLPGGGVkVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLdpfINPPNEVIDDFAFLPFG 388
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 586644824 442 AGRRICIGMPLASSMVHLVLGSLLHyfNWKVEGEVDMTEEFGIT 485
Cdd:cd11046  389 GGPRKCLGDQFALLEATVALAMLLR--RFDFELDVGPRHVGMTT 430
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
60-487 4.05e-43

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: 158.25  E-value: 4.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPvPLAAKTLSYGGNSLVWAA-YGHHWRLLRRLSftelfstkrL 138
Cdd:cd20676    1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRP-DLYSFRFISDGQSLTFSTdSGPVWRARRKLA---------Q 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 139 NSMEKFRKAEvSKTMAS--IYEESIKGNSVNIGSTVFSTMLGI------------VENMVCGNYVFKKGDELATELKGMV 204
Cdd:cd20676   71 NALKTFSIAS-SPTSSSscLLEEHVSKEAEYLVSKLQELMAEKgsfdpyryivvsVANVICAMCFGKRYSHDDQELLSLV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 205 R---DVLKLSGEPNASDFFPFLRGLDLQGVeRRAQKLRERFDGIFSEMIERRLKDMrekgmvnerDEESGRGIKESDFLG 281
Cdd:cd20676  150 NlsdEFGEVAGSGNPADFIPILRYLPNPAM-KRFKDINKRFNSFLQKIVKEHYQTF---------DKDNIRDITDSLIEH 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 282 VLLELMDHNEGLQM--EHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFL 359
Cdd:cd20676  220 CQDKKLDENANIQLsdEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYL 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 360 QAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFV---GTNLEfKGNDYE 436
Cdd:cd20676  300 EAFILETFRHSSFVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLtadGTEIN-KTESEK 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 586644824 437 LLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV-EGE-VDMTEEFGITLQ 487
Cdd:cd20676  379 VMLFGLGKRRCIGESIARWEVFLFLAILLQQLEFSVpPGVkVDMTPEYGLTMK 431
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
68-482 5.85e-42

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: 155.00  E-value: 5.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  68 LGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNsLVWAAyGHHWRLLRRLsFTELFSTKRLNSMekF-RK 146
Cdd:cd11056   10 LFRRPALLVRDPELIKQILVKDFAHFHDRGLYSDEKDDPLSAN-LFSLD-GEKWKELRQK-LTPAFTSGKLKNM--FpLM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 147 AEVSKTM-ASIYEESIKGNSVN------------IGSTVFstmlGIVENmvcgnyVFKKGDelaTELKGMVRDVLKLSGE 213
Cdd:cd11056   85 VEVGDELvDYLKKQAEKGKELEikdlmaryttdvIASCAF----GLDAN------SLNDPE---NEFREMGRRLFEPSRL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 214 PNASDFFPFLrgldlqgVERRAQKLRERFdgiFSEMIERRLKD-MREkgMVNERDEEsgrGIKESDFLGVLLELMDHNEG 292
Cdd:cd11056  152 RGLKFMLLFF-------FPKLARLLRLKF---FPKEVEDFFRKlVRD--TIEYREKN---NIVRNDFIDLLLELKKKGKI 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 293 LQMEHVKGMLMDM--------FIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGK--DKMMEEShIPDVPFLQAI 362
Cdd:cd11056  217 EDDKSEKELTDEElaaqafvfFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKhgGELTYEA-LQEMKYLDQV 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 363 VKEVLRLHPAAPLLIpRLCDSDCQIDGH--IIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEfKGNDYELLPF 440
Cdd:cd11056  296 VNETLRKYPPLPFLD-RVCTKDYTLPGTdvVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKK-KRHPYTYLPF 373
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 586644824 441 GAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEGEVDMTEEF 482
Cdd:cd11056  374 GDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPLKL 415
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
109-453 5.06e-41

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: 152.41  E-value: 5.06e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 109 GNSLVWAaYGHHWRLLRRLsFTELFSTKRLNSMEKFRKaEVSKTMaSIYEESIKGNSVNI-----GSTVFSTMLGivENM 183
Cdd:cd20621   48 GKGLLFS-EGEEWKKQRKL-LSNSFHFEKLKSRLPMIN-EITKEK-IKKLDNQNVNIIQFlqkitGEVVIRSFFG--EEA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 184 vcGNYVFKKGDELATELKGMVRDVLKLSGEP-----------NASDFFPFLrgldlqgVERRAQKLRERFDGIFSEMIER 252
Cdd:cd20621  122 --KDLKINGKEIQVELVEILIESFLYRFSSPyfqlkrlifgrKSWKLFPTK-------KEKKLQKRVKELRQFIEKIIQN 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 253 RLKDMREKGMVNERDEesgrgikeSDFLGVLLELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVME 332
Cdd:cd20621  193 RIKQIKKNKDEIKDII--------IDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQE 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 333 EARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVW 412
Cdd:cd20621  265 KLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYF 344
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 586644824 413 SDPLKFDPSRFVGTNlEFKGNDYELLPFGAGRRICIGMPLA 453
Cdd:cd20621  345 ENPDEFNPERWLNQN-NIEDNPFVFIPFSAGPRNCIGQHLA 384
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
60-486 5.63e-40

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: 149.57  E-value: 5.63e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRP-VPLAAKTlsYGGNSLVWAAyGHHWRLLRRLSFTEL--FSTK 136
Cdd:cd20664    1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPiIPIFEDF--NKGYGILFSN-GENWKEMRRFTLTTLrdFGMG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 137 RLNSMEKFrkAEVSKTMASIYEeSIKGNSVNIGSTVFSTMLGIVENMVCGNYvFKKGDELATELKGMVRDVLKLSGEPNA 216
Cdd:cd20664   78 KKTSEDKI--LEEIPYLIEVFE-KHKGKPFETTLSMNVAVSNIIASIVLGHR-FEYTDPTLLRMVDRINENMKLTGSPSV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 S--DFFPFLRGL--DLQGVERRAQKLRErfdgIFSEMIERRLKdmrekgmVNERDEEsgRGIKESdFLGVLLELMD---- 288
Cdd:cd20664  154 QlyNMFPWLGPFpgDINKLLRNTKELND----FLMETFMKHLD-------VLEPNDQ--RGFIDA-FLVKQQEEEEssds 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 289 --HNEGLQMehvkgMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEEsHIPDVPFLQAIVKEV 366
Cdd:cd20664  220 ffHDDNLTC-----SVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVE-HRKNMPYTDAVIHEI 293
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 367 LRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDyELLPFGAGRRI 446
Cdd:cd20664  294 QRFANIVPMNLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRD-AFMPFSAGRRV 372
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 586644824 447 CIGMPLASSMVHLVLGSLLHYFNWK-----VEGEVDMTEEFGITL 486
Cdd:cd20664  373 CIGETLAKMELFLFFTSLLQRFRFQpppgvSEDDLDLTPGLGFTL 417
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
60-469 6.40e-40

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: 149.77  E-value: 6.40e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVplaaktlSYGGNSLVWAA---------YGHHWRLLRRLSFT 130
Cdd:cd11066    1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRPT-------FYTFHKVVSSTqgftigtspWDESCKRRRKAAAS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 131 ELfSTKRLNSMEKFRKAEVSKTMASIYEESiKGNSVNIGSTVFSTMLGIVENMVCgNYVFK----KGDELATELKGMVRD 206
Cdd:cd11066   74 AL-NRPAVQSYAPIIDLESKSFIRELLRDS-AEGKGDIDPLIYFQRFSLNLSLTL-NYGIRldcvDDDSLLLEIIEVESA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 207 VLKL-SGEPNASDFFPFLRGLDLQGVER-RAQKLRERfdgifsemierRLKDMreKGMVNERDEESGRGIKESDFLGVLL 284
Cdd:cd11066  151 ISKFrSTSSNLQDYIPILRYFPKMSKFReRADEYRNR-----------RDKYL--KKLLAKLKEEIEDGTDKPCIVGNIL 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 285 ElmDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPY--VMEEARDELRRVIGKD-----KMMEEShipDVP 357
Cdd:cd11066  218 K--DKESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPGqeIQEKAYEEILEAYGNDedaweDCAAEE---KCP 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 358 FLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFvgtnLEFKGNDYEL 437
Cdd:cd11066  293 YVVALVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERW----LDASGDLIPG 368
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 586644824 438 LP---FGAGRRICIGMPLASSMVHLVLGSLLHYFN 469
Cdd:cd11066  369 PPhfsFGAGSRMCAGSHLANRELYTAICRLILLFR 403
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
59-481 8.11e-39

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


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 146.71  E-value: 8.11e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  59 TYGPIMPFKLGmRKAVVISSPHPAKQIFKthDRKFSSRPVPLAaKTLSYGGNSLVwAAYGHHWRLLRRL---SFTELFSt 135
Cdd:cd11070    1 KLGAVKILFVS-RWNILVTKPEYLTQIFR--RRDDFPKPGNQY-KIPAFYGPNVI-SSEGEDWKRYRKIvapAFNERNN- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 136 kRLNSMEKFRKAevsKTMASIYEESIKGNSvNIGSTVFSTMLGIVENMVCG-----NYVFKKGDELAT-----ELKGMVR 205
Cdd:cd11070   75 -ALVWEESIRQA---QRLIRYLLEEQPSAK-GGGVDVRDLLQRLALNVIGEvgfgfDLPALDEEESSLhdtlnAIKLAIF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 206 DVLKLSgepnasdfFPFLRGLDLQGVERRAQKlrerfdgifSEMIERRLKDMREKGMVNERDEESGRGIKESDFLGVLLE 285
Cdd:cd11070  150 PPLFLN--------FPFLDRLPWVLFPSRKRA---------FKDVDEFLSELLDEVEAELSADSKGKQGTESVVASRLKR 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 286 LMDhNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHI--PDVPFLQAIV 363
Cdd:cd11070  213 ARR-SGGLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEEdfPKLPYLLAVI 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 364 KEVLRLHPAApLLIPRLCDSDCQI-----DGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLE------FK 431
Cdd:cd11070  292 YETLRLYPPV-QLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSGEigaatrFT 370
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 586644824 432 GNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV--EGEVDMTEE 481
Cdd:cd11070  371 PARGAFIPFSAGPRACLGRKFALVEFVAALAELFRQYEWRVdpEWEEGETPA 422
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
233-476 1.55e-38

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: 145.44  E-value: 1.55e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 233 RRAQKLRERFDGIFSEMIERRlkdmrekgmvneRDEESGrgiKESDFLGVLLE--------LMDHneglqmeHVKGMLMD 304
Cdd:cd11042  162 RRRDRARAKLKEIFSEIIQKR------------RKSPDK---DEDDMLQTLMDakykdgrpLTDD-------EIAGLLIA 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 305 MFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDK-MMEESHIPDVPFLQAIVKEVLRLHPAAPLLIpRLCDS 383
Cdd:cd11042  220 LLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDdPLTYDVLKEMPLLHACIKETLRLHPPIHSLM-RKARK 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 384 DCQID--GHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRF-VGTNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLV 460
Cdd:cd11042  299 PFEVEggGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFlKGRAEDSKGGKFAYLPFGAGRHRCIGENFAYLQIKTI 378
                        250
                 ....*....|....*..
gi 586644824 461 LGSLLHYFNWK-VEGEV 476
Cdd:cd11042  379 LSTLLRNFDFElVDSPF 395
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
60-487 4.85e-38

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: 144.47  E-value: 4.85e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPvPLAAKTLSYGGNSLVWAA-YGHHWRL--------LRRLSFT 130
Cdd:cd20677    1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRP-DFYTFSLIANGKSMTFSEkYGESWKLhkkiaknaLRTFSKE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 131 ELFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTmlgiVENMVCGNYVFKKGDELATELKGMVR---DV 207
Cdd:cd20677   80 EAKSSTCSCLLEEHVCAEASELVKTLVELSKEKGSFDPVSLITCA----VANVVCALCFGKRYDHSDKEFLTIVEinnDL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 208 LKLSGEPNASDFFPFLRGLDLQGVerraQKLRErFDGIFSEMIERRLKDMrekgmVNERDEESGRGIkeSDFLGVLLE-- 285
Cdd:cd20677  156 LKASGAGNLADFIPILRYLPSPSL----KALRK-FISRLNNFIAKSVQDH-----YATYDKNHIRDI--TDALIALCQer 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 286 -LMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVK 364
Cdd:cd20677  224 kAEDKSAVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFIN 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 365 EVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYE-LLPFGAG 443
Cdd:cd20677  304 EVFRHSSFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLVEkVLIFGMG 383
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 586644824 444 RRICIGMPLASSMVHLVLGSLLHYFNWK--VEGEVDMTEEFGITLQ 487
Cdd:cd20677  384 VRKCLGEDVARNEIFVFLTTILQQLKLEkpPGQKLDLTPVYGLTMK 429
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
60-491 5.07e-38

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: 143.86  E-value: 5.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPImpFK---LGmRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLsygGNSLVWAAYGHHWRLLRRLSFTELFStk 136
Cdd:cd11043    5 YGPV--FKtslFG-RPTVVSADPEANRFILQNEGKLFVSWYPKSVRKLL---GKSSLLTVSGEEHKRLRGLLLSFLGP-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 137 rlnsmekfrkaevsktmasiyeESIKgnsvnigstvfSTMLGIVENMVC---GNYVFKKGDELATELKGM-----VRDVL 208
Cdd:cd11043   77 ----------------------EALK-----------DRLLGDIDELVRqhlDSWWRGKSVVVLELAKKMtfeliCKLLL 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 209 KLSGEPN----ASDFFPFLRG-----LDLQGVE-RRAQKLRERFDGIFSEMIERRLkdmrekgmvNERDEESGRGikesD 278
Cdd:cd11043  124 GIDPEEVveelRKEFQAFLEGllsfpLNLPGTTfHRALKARKRIRKELKKIIEERR---------AELEKASPKG----D 190
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 279 FLGVLLELMDHN-EGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEAR---DELRRVIGKDKMMEESHIP 354
Cdd:cd11043  191 LLDVLLEEKDEDgDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLeehEEIAKRKEEGEGLTWEDYK 270
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 355 DVPFLQAIVKEVLRLHPAAPLlIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNlefKGND 434
Cdd:cd11043  271 SMKYTWQVINETLRLAPIVPG-VFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKG---KGVP 346
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 586644824 435 YELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEGEVDMTEEFGITLQKALP 491
Cdd:cd11043  347 YTFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVVPDEKISRFPLPRPPKGLP 403
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
53-494 8.49e-38

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: 143.17  E-value: 8.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  53 LAALSlTYGPIMPFKLGMRKAVVISSPHPAKQIFkTHDRKFSSRPvPLAAKTLSYGGNSLVWAAYGHHwRLLRRLsFTEL 132
Cdd:cd11049    6 LSSLR-AHGDLVRIRLGPRPAYVVTSPELVRQVL-VNDRVFDKGG-PLFDRARPLLGNGLATCPGEDH-RRQRRL-MQPA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 133 FSTKRLnsmekfrkAEVSKTMASIYEESIK----GNSVNigstVFSTMLGIVENMVCGN-YVFKKGDELATELKGMVRDV 207
Cdd:cd11049   81 FHRSRI--------PAYAEVMREEAEALAGswrpGRVVD----VDAEMHRLTLRVVARTlFSTDLGPEAAAELRQALPVV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 208 LKlsGEPNASDFFPFLRGLDLQGvERRAQKLRERFDGIFSEMIERRlkdmrekgmvneRDEESGRGikesDFLGVLLEL- 286
Cdd:cd11049  149 LA--GMLRRAVPPKFLERLPTPG-NRRFDRALARLRELVDEIIAEY------------RASGTDRD----DLLSLLLAAr 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 287 MDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGkDKMMEESHIPDVPFLQAIVKEV 366
Cdd:cd11049  210 DEEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEA 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 367 LRLHPAAPLLiPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGtnlEFKGND--YELLPFGAGR 444
Cdd:cd11049  289 LRLYPPVWLL-TRRTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLP---GRAAAVprGAFIPFGAGA 364
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 586644824 445 RICIGMPLASSMVHLVLGSLLHYFNWKVEGEVDMTEEFGITLQ-KALPLVV 494
Cdd:cd11049  365 RKCIGDTFALTELTLALATIASRWRLRPVPGRPVRPRPLATLRpRRLRMRV 415
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
60-473 1.60e-37

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: 142.81  E-value: 1.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPImpFK---LGmRKAVVISSPHPAKQIFkTHDRKFSSRPVPLAAKTLsYGGNSLVWAAyGHHWRLLRRLsFTELFSTK 136
Cdd:cd11044   21 YGPV--FKthlLG-RPTVFVIGAEAVRFIL-SGEGKLVRYGWPRSVRRL-LGENSLSLQD-GEEHRRRRKL-LAPAFSRE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 137 RLNS----MEKFRKAEVSKTmasiyeesIKGNSVNIGSTVFSTMLGIVENMVCGNYVFKKGDELATELKGMVRDVLKLsg 212
Cdd:cd11044   94 ALESyvptIQAIVQSYLRKW--------LKAGEVALYPELRRLTFDVAARLLLGLDPEVEAEALSQDFETWTDGLFSL-- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 213 ePNASDFFPFlrgldlqgveRRAQKLRERFDGIFSEMIERRLKdmrekgmvNERDEESgrgikesDFLGVLLELMD-HNE 291
Cdd:cd11044  164 -PVPLPFTPF----------GRAIRARNKLLARLEQAIRERQE--------EENAEAK-------DALGLLLEAKDeDGE 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 292 GLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRvIGKDKMMEESHIPDVPFLQAIVKEVLRLHP 371
Cdd:cd11044  218 PLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDA-LGLEEPLTLESLKKMPYLDQVIKEVLRLVP 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 372 AAPLLIPRLCDsDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGMP 451
Cdd:cd11044  297 PVGGGFRKVLE-DFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPFSLIPFGGGPRECLGKE 375
                        410       420
                 ....*....|....*....|..
gi 586644824 452 LASSMVHLVLGSLLHYFNWKVE 473
Cdd:cd11044  376 FAQLEMKILASELLRNYDWELL 397
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
60-491 2.27e-37

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: 142.45  E-value: 2.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPvPLAAKTLSYGGNSLVWAAYGHHWRLLRRLSFTEL--FSTKR 137
Cdd:cd20675    1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRP-DFASFRVVSGGRSLAFGGYSERWKAHRRVAHSTVraFSTRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 138 LNSMEKFRK---AEVSKTMASIYEESIKGNSVN----IGSTVFSTMlgiveNMVCGNYVFKKGDELATELKGMVRDVLKL 210
Cdd:cd20675   80 PRTRKAFERhvlGEARELVALFLRKSAGGAYFDpappLVVAVANVM-----SAVCFGKRYSHDDAEFRSLLGRNDQFGRT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 211 SGEPNASDFFPFLRGLD--LQGVERRAQKL-RERFDGIFSEMIERRlkdmrekgmvnerdeESGRGIKESDFLGVLLELM 287
Cdd:cd20675  155 VGAGSLVDVMPWLQYFPnpVRTVFRNFKQLnREFYNFVLDKVLQHR---------------ETLRGGAPRDMMDAFILAL 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 288 DHNE------GLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKM--MEEShiPDVPFL 359
Cdd:cd20675  220 EKGKsgdsgvGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLpcIEDQ--PNLPYV 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 360 QAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFkgnDYEL-- 437
Cdd:cd20675  298 MAFLYEAMRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFL---NKDLas 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 586644824 438 --LPFGAGRRICIGMPLASSMVHLVLGSLLH--YFNWKVEGEVDMTEEFGITLqKALP 491
Cdd:cd20675  375 svMIFSVGKRRCIGEELSKMQLFLFTSILAHqcNFTANPNEPLTMDFSYGLTL-KPKP 431
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
74-453 2.78e-37

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: 142.05  E-value: 2.78e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  74 VVISSPHPAKQIFKTHDRKFSSRPVPLAAKtlsYGGNSLVWAAYGHHWRLLRRLsFTELFS--TKRLNSMEKFRKAEVSK 151
Cdd:cd11059   11 VSVNDLDAVREIYGGGFGKTKSYWYFTLRG---GGGPNLFSTLDPKEHSARRRL-LSGVYSksSLLRAAMEPIIRERVLP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 152 TMASIYEESIKGNSVNIGSTVFSTMLGIVenmvcGNYVFkkGDELATELKGMVRDVLKLSGEPNASDFFPFLRglDLQGV 231
Cdd:cd11059   87 LIDRIAKEAGKSGSVDVYPLFTALAMDVV-----SHLLF--GESFGTLLLGDKDSRERELLRRLLASLAPWLR--WLPRY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 232 ERRAQKLRERFdgifseMIERRLKDMRE--KGMVN--ERDEESGRGIKESDFLGVLLELMDHNEGLQMEHVKGMLMDMFI 307
Cdd:cd11059  158 LPLATSRLIIG------IYFRAFDEIEEwaLDLCAraESSLAESSDSESLTVLLLEKLKGLKKQGLDDLEIASEALDHIV 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 308 AGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPD-VPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQ 386
Cdd:cd11059  232 AGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPFRGPPDLEDLDkLPYLNAVIRETLRLYPPIPGSLPRVVPEGGA 311
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 387 -IDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRF-VGTNLEFKGNDYELLPFGAGRRICIGMPLA 453
Cdd:cd11059  312 tIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWlDPSGETAREMKRAFWPFGSGSRMCIGMNLA 380
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
60-486 3.43e-37

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: 141.86  E-value: 3.43e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPV-PLAAKTlsYGGNSLVWAAyGHHWRLLRRLSFTEL--FSTK 136
Cdd:cd20662    1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPEtPLRERI--FNKNGLIFSS-GQTWKEQRRFALMTLrnFGLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 137 RlNSMEKFRKAEVSKTMASIYEEsiKGNSVNigsTVFStMLGIVENMVC----GNYvFKKGDELATELKGMVRDVLKLSG 212
Cdd:cd20662   78 K-KSLEERIQEECRHLVEAIREE--KGNPFN---PHFK-INNAVSNIICsvtfGER-FEYHDEWFQELLRLLDETVYLEG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 213 EPNAS--DFFP----FLRGlDLQGVERRAQKLRErfdgIFSEMIERRLKDMrekgmvnerDEESGRgikesDFLGVLLEL 286
Cdd:cd20662  150 SPMSQlyNAFPwimkYLPG-SHQTVFSNWKKLKL----FVSDMIDKHREDW---------NPDEPR-----DFIDAYLKE 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 287 M----DHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAI 362
Cdd:cd20662  211 MakypDPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAV 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 363 VKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVgTNLEFKGNDyELLPFGA 442
Cdd:cd20662  291 IHEVQRMGNIIPLNVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFL-ENGQFKKRE-AFLPFSM 368
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 586644824 443 GRRICIGMPLASSMVHLVLGSLLHYFNWK--VEGEVDMTEEFGITL 486
Cdd:cd20662  369 GKRACLGEQLARSELFIFFTSLLQKFTFKppPNEKLSLKFRMGITL 414
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
48-472 9.08e-37

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: 140.55  E-value: 9.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  48 LPHqsLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSygGNSLVwAAYGHHWRLLRRL 127
Cdd:cd11052    1 LPH--YYHWIKQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEGYFGKSPLQPGLKKLL--GRGLV-MSNGEKWAKHRRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 128 SfTELFSTKRLNSMEKFRKAEVSKtMASIYEESIKGNSVNIgsTVFSTMLGIVENmVCGNYVFKKGDELATELKGMVRDV 207
Cdd:cd11052   76 A-NPAFHGEKLKGMVPAMVESVSD-MLERWKKQMGEEGEEV--DVFEEFKALTAD-IISRTAFGSSYEEGKEVFKLLREL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 208 LKLSGEPNASDFFPFLRGLDLQGvERRAQKLRERFDGIFSEMIERRLKDMrekgmvnerdEESGRGIKESDFLGVLLELM 287
Cdd:cd11052  151 QKICAQANRDVGIPGSRFLPTKG-NKKIKKLDKEIEDSLLEIIKKREDSL----------KMGRGDDYGDDLLGLLLEAN 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 288 DHNEGLQMEHVKgMLMD----MFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKmMEESHIPDVPFLQAIV 363
Cdd:cd11052  220 QSDDQNKNMTVQ-EIVDecktFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDK-PPSDSLSKLKTVSMVI 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 364 KEVLRLHPAAPLLiPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLEFKGNDYELLPFGA 442
Cdd:cd11052  298 NESLRLYPPAVFL-TRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGVAKAAKHPMAFLPFGL 376
                        410       420       430
                 ....*....|....*....|....*....|
gi 586644824 443 GRRICIGMPLASSMVHLVLGSLLHYFNWKV 472
Cdd:cd11052  377 GPRNCIGQNFATMEAKIVLAMILQRFSFTL 406
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
60-471 2.90e-36

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: 139.33  E-value: 2.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFK-LGMRKAVVISSPHPAKQIFKTHDRKFssRPVPLAAKTLS-YGGNSLVWAaYGHHWRLLRRLsFTELFSTKR 137
Cdd:cd11069    1 YGGLIRYRgLFGSERLLVTDPKALKHILVTNSYDF--EKPPAFRRLLRrILGDGLLAA-EGEEHKRQRKI-LNPAFSYRH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 138 LNSMEK--FRKAE--VSKTMASIYEESIKGNSVNIGSTVFSTMLGIVenmvcGNYVF--------KKGDELATELKGMVR 205
Cdd:cd11069   77 VKELYPifWSKAEelVDKLEEEIEESGDESISIDVLEWLSRATLDII-----GLAGFgydfdsleNPDNELAEAYRRLFE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 206 DVLKLSG--EPNASDFFPFLRGLDLQgVERRAQKLRERFDGIFSEMIERRLKDmrekgmVNERDEESGRgikesDFLGVL 283
Cdd:cd11069  152 PTLLGSLlfILLLFLPRWLVRILPWK-ANREIRRAKDVLRRLAREIIREKKAA------LLEGKDDSGK-----DILSIL 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 284 LELMDHNEGLQM--EHVKGMLMdMFI-AGTDTTSATVEWAMAELLNHPYVMEEARDELRRVI--GKDKMMEESHIPDVPF 358
Cdd:cd11069  220 LRANDFADDERLsdEELIDQIL-TFLaAGHETTSTALTWALYLLAKHPDVQERLREEIRAALpdPPDGDLSYDDLDRLPY 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 359 LQAIVKEVLRLHPAAPLLiPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRF----VGTNLEFKGN 433
Cdd:cd11069  299 LNAVCRETLRLYPPVPLT-SREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWlepdGAASPGGAGS 377
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 586644824 434 DYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWK 471
Cdd:cd11069  378 NYALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFE 415
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
119-484 3.47e-36

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: 138.93  E-value: 3.47e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 119 HHwRLLRRLsFTELFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNIgSTVFSTMLG-IVENMVCG-NYVFKKGDEL 196
Cdd:cd11062   54 LH-RLRRKA-LSPFFSKRSILRLEPLIQEKVDKLVSRLREAKGTGEPVNL-DDAFRALTAdVITEYAFGrSYGYLDEPDF 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 197 ATELKGMVRDVLKLSgepNASDFFPFLRGLdlqgVERRAQKLRERFDGIFSEMIERRlKDMREKgmVNERDEESGRGIKE 276
Cdd:cd11062  131 GPEFLDALRALAEMI---HLLRHFPWLLKL----LRSLPESLLKRLNPGLAVFLDFQ-ESIAKQ--VDEVLRQVSAGDPP 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 277 SDFLGVLLELMDHN---EGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVI-GKDKMMEESH 352
Cdd:cd11062  201 SIVTSLFHALLNSDlppSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMpDPDSPPSLAE 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 353 IPDVPFLQAIVKEVLRLHPAAPLLIPRLC-DSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFK 431
Cdd:cd11062  281 LEKLPYLTAVIKEGLRLSYGVPTRLPRVVpDEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEKGK 360
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 586644824 432 GNDYeLLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWK----VEGEVDMTEEFGI 484
Cdd:cd11062  361 LDRY-LVPFSKGSRSCLGINLAYAELYLALAALFRRFDLElyetTEEDVEIVHDFFL 416
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
60-487 6.46e-36

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: 138.07  E-value: 6.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFklgmrkaVVISSPHPAKQIFKTHDRKFSSRPVPLaaktLSYGGNSLVWAAyGHHWRLLRRL-----------S 128
Cdd:cd20659    8 LGPFRPI-------LVLNHPDTIKAVLKTSEPKDRDSYRFL----KPWLGDGLLLSN-GKKWKRNRRLltpafhfdilkP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 129 FTELF--STKRLnsMEKFRKAEVSKTMASIYEesikgnsvNIGSTVFSTMLGivenmvCgnyVFKKGDELATELK----- 201
Cdd:cd20659   76 YVPVYneCTDIL--LEKWSKLAETGESVEVFE--------DISLLTLDIILR------C---AFSYKSNCQQTGKnhpyv 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 202 GMVRDVLKLSGEP--NASDFFPFLRGLDLQGVE-RRAQKLRERFDGifsEMIERRLKDMREkgmvNERDEESGRgiKESD 278
Cdd:cd20659  137 AAVHELSRLVMERflNPLLHFDWIYYLTPEGRRfKKACDYVHKFAE---EIIKKRRKELED----NKDEALSKR--KYLD 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 279 FLGVLLELMDhneglqmEHVKGMLMD---------MFiAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMME 349
Cdd:cd20659  208 FLDILLTARD-------EDGKGLTDEeirdevdtfLF-AGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIE 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 350 ESHIPDVPFLQAIVKEVLRLHPAAPLlIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNle 429
Cdd:cd20659  280 WDDLSKLPYLTMCIKESLRLYPPVPF-IARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPEN-- 356
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 430 FKGND-YELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEGEVDMTEEFGITLQ 487
Cdd:cd20659  357 IKKRDpFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNHPVEPKPGLVLR 415
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
248-469 2.53e-35

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: 136.62  E-value: 2.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 248 EMIERRLKDMREKGMVNERDEESG--RGIKESDFLGVLLELmdHNEGLQMEHvkgmlMD--------MFiAGTDTTSATV 317
Cdd:cd20660  181 KVIQERKAELQKSLEEEEEDDEDAdiGKRKRLAFLDLLLEA--SEEGTKLSD-----EDireevdtfMF-EGHDTTAAAI 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 318 EWAMAELLNHPYVMEEARDELRRVIGK-DKMMEESHIPDVPFLQAIVKEVLRLHPAAPLlIPRLCDSDCQIDGHIIEKNT 396
Cdd:cd20660  253 NWALYLIGSHPEVQEKVHEELDRIFGDsDRPATMDDLKEMKYLECVIKEALRLFPSVPM-FGRTLSEDIEIGGYTIPKGT 331
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586644824 397 EVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEfKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFN 469
Cdd:cd20660  332 TVLVLTYALHRDPRQFPDPEKFDPDRFLPENSA-GRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFR 403
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
60-471 6.91e-35

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: 135.47  E-value: 6.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSR-PVPLAAKTLSygGNSLVWAAyGHHWRLLRRLSFTELfstkRL 138
Cdd:cd20665    1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRgRFPIFEKVNK--GLGIVFSN-GERWKETRRFSLMTL----RN 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 139 NSMEKfRKAE--VSKTMASIYEESIKGNSVNIGSTVFstmLGIVE-NMVCgNYVFKK----GDELATELKGMVRDVLKLS 211
Cdd:cd20665   74 FGMGK-RSIEdrVQEEARCLVEELRKTNGSPCDPTFI---LGCAPcNVIC-SIIFQNrfdyKDQDFLNLMEKLNENFKIL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 212 GEP--NASDFFPFLrgLD-LQGVERRAQKlreRFDGIFSEMIERrLKDMREKgmvneRDEESGRgikesDFLGVLLELM- 287
Cdd:cd20665  149 SSPwlQVCNNFPAL--LDyLPGSHNKLLK---NVAYIKSYILEK-VKEHQES-----LDVNNPR-----DFIDCFLIKMe 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 288 --DHNEGLQ--MEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDK---MMEESHIpdvPFLQ 360
Cdd:cd20665  213 qeKHNQQSEftLENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRspcMQDRSHM---PYTD 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 361 AIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYeLLPF 440
Cdd:cd20665  290 AVIHEIQRYIDLVPNNLPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDY-FMPF 368
                        410       420       430
                 ....*....|....*....|....*....|.
gi 586644824 441 GAGRRICIGMPLASSMVHLVLGSLLHYFNWK 471
Cdd:cd20665  369 SAGKRICAGEGLARMELFLFLTTILQNFNLK 399
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
64-486 1.46e-34

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: 134.65  E-value: 1.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  64 MPFK--LGMRKAVVISSPHPAKQIFktHDRKFSSRPVPLAAKTLSYGgnslVWAAYGHHWRLLRR-LSFTelFSTKRLNS 140
Cdd:cd11057    2 SPFRawLGPRPFVITSDPEIVQVVL--NSPHCLNKSFFYDFFRLGRG----LFSAPYPIWKLQRKaLNPS--FNPKILLS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 141 -MEKFrkAEVSKTMASIYEESIKGNSVNIgstvFSTMLGIVENMVCGN---YVFKKGDELATELKGMVRDVLKLSGEpna 216
Cdd:cd11057   74 fLPIF--NEEAQKLVQRLDTYVGGGEFDI----LPDLSRCTLEMICQTtlgSDVNDESDGNEEYLESYERLFELIAK--- 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 SDFFPFLRgLD----LQGVERRAQKLRERFDGIFSEMIERRLKDMREKGMVNERDEESGRGIKESdFLGVLLELMDHNEG 292
Cdd:cd11057  145 RVLNPWLH-PEfiyrLTGDYKEEQKARKILRAFSEKIIEKKLQEVELESNLDSEEDEENGRKPQI-FIDQLLELARNGEE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 293 LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKmmEESHIPDVP---FLQAIVKEVLRL 369
Cdd:cd11057  223 FTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDG--QFITYEDLQqlvYLEMVLKETMRL 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 370 HPAAPlLIPRLCDSDCQID-GHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLEfKGNDYELLPFGAGRRIC 447
Cdd:cd11057  301 FPVGP-LVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSA-QRHPYAFIPFSAGPRNC 378
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 586644824 448 IGMPLASSMVHLVLGSLLHYFNWKVEGEV-DMTEEFGITL 486
Cdd:cd11057  379 IGWRYAMISMKIMLAKILRNYRLKTSLRLeDLRFKFNITL 418
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
60-472 1.97e-34

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: 134.05  E-value: 1.97e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNS--LVWAAYGHHWRLLRRLSFTEL--FST 135
Cdd:cd20663    1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGPKSqgVVLARYGPAWREQRRFSVSTLrnFGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 136 KRlNSMEKFRKAEVSKTMASIYEESikGNSVNIGSTVFSTMLGIVENMVCGNYvFKKGD-----------ELATELKGMV 204
Cdd:cd20663   81 GK-KSLEQWVTEEAGHLCAAFTDQA--GRPFNPNTLLNKAVCNVIASLIFARR-FEYEDprfirllklleESLKEESGFL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 205 RDVLK----LSGEPN-ASDFFP----FLRGLDLQGVERR-----AQKLRERFDGIFSEMierrlkdmrekgmvnerdeES 270
Cdd:cd20663  157 PEVLNafpvLLRIPGlAGKVFPgqkaFLALLDELLTEHRttwdpAQPPRDLTDAFLAEM-------------------EK 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 271 GRGIKESDFlgvllelmdHNEGLQMehvkgMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEE 350
Cdd:cd20663  218 AKGNPESSF---------NDENLRL-----VVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEM 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 351 SHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEF 430
Cdd:cd20663  284 ADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHF 363
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 586644824 431 KGNDyELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV 472
Cdd:cd20663  364 VKPE-AFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSV 404
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
76-475 3.10e-34

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: 133.48  E-value: 3.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  76 ISSPHPAKQIFKTHDRKFSSRPVPlaaktlsyGGNSLVWAAYGHHWRLlRRLsFTELFSTKRLNSMEKFRKAEVSKTMAS 155
Cdd:cd11058   22 IYGHRPGGPKFPKKDPRFYPPAPN--------GPPSISTADDEDHARL-RRL-LAHAFSEKALREQEPIIQRYVDLLVSR 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 156 IYEESIKGNSVN------------IGSTVFSTMLGIVENMVCGNYVfkkgdelatelkGMVRDVLKLSGEPNASDFFPFL 223
Cdd:cd11058   92 LRERAGSGTPVDmvkwfnfttfdiIGDLAFGESFGCLENGEYHPWV------------ALIFDSIKALTIIQALRRYPWL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 224 RGLDLQGVERRAQKLRERFDGIFSEMIERRLkdmrekgmvnerdeesGRGIKESDFLGVLLELMDHNEGLQMEHVKGMLM 303
Cdd:cd11058  160 LRLLRLLIPKSLRKKRKEHFQYTREKVDRRL----------------AKGTDRPDFMSYILRNKDEKKGLTREELEANAS 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 304 DMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRrvigkDKMMEESHI-----PDVPFLQAIVKEVLRLHPAAPLLIP 378
Cdd:cd11058  224 LLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIR-----SAFSSEDDItldslAQLPYLNAVIQEALRLYPPVPAGLP 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 379 RLCDSD-CQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTN-LEFKGNDYELL-PFGAGRRICIGMPLASS 455
Cdd:cd11058  299 RVVPAGgATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPrFEFDNDKKEAFqPFSVGPRNCIGKNLAYA 378
                        410       420
                 ....*....|....*....|
gi 586644824 456 MVHLVLGSLLHYFNWKVEGE 475
Cdd:cd11058  379 EMRLILAKLLWNFDLELDPE 398
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
61-487 3.18e-34

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: 133.60  E-value: 3.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  61 GPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSsRPVPLAAKTLSYGGNSlVWAAYGHHWRLLRRLSfTELFSTKRLNS 140
Cdd:cd11083    1 GSAYRFRLGRQPVLVISDPELIREVLRRRPDEFR-RISSLESVFREMGING-VFSAEGDAWRRQRRLV-MPAFSPKHLRY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 141 MEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCG---NYVFKKGDELATELKGMVRDVLKLSGEPnas 217
Cdd:cd11083   78 FFPTLRQITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGydlNTLERGGDPLQEHLERVFPMLNRRVNAP--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 218 dfFPFLRGLdlqgverRAQKLReRFDGIFSEmIERRLKDMREKGMVnERDEESGRGIKESDFLGVLLELMDHNEGLQMEH 297
Cdd:cd11083  155 --FPYWRYL-------RLPADR-ALDRALVE-VRALVLDIIAAARA-RLAANPALAEAPETLLAMMLAEDDPDARLTDDE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 298 VKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMME-ESHIPDVPFLQAIVKEVLRLHPAAPLL 376
Cdd:cd11083  223 IYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPlLEALDRLPYLEAVARETLRLKPVAPLL 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 377 iPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLE-FKGNDYELLPFGAGRRICIGMPLASS 455
Cdd:cd11083  303 -FLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAaEPHDPSSLLPFGAGPRLCPGRSLALM 381
                        410       420       430
                 ....*....|....*....|....*....|...
gi 586644824 456 MVHLVLGSLLHYFNWK-VEGEVDMTEEFGITLQ 487
Cdd:cd11083  382 EMKLVFAMLCRNFDIElPEPAPAVGEEFAFTMS 414
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
49-469 1.18e-33

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: 131.92  E-value: 1.18e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  49 PHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFkthDRKFSSRPVPLAAKTL-SYGGNSLvWAAYGH--HWRLLR 125
Cdd:cd11068    1 PVQSLLRLADELGPIFKLTLPGRRVVVVSSHDLIAELC---DESRFDKKVSGPLEELrDFAGDGL-FTAYTHepNWGKAH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 126 RLsFTELFSTKRLNSMekfrkaevsktmasiyeesikgnsvnigstvFSTMLGIVENMvCGNYVFKKGDE--LATELkgM 203
Cdd:cd11068   77 RI-LMPAFGPLAMRGY-------------------------------FPMMLDIAEQL-VLKWERLGPDEpiDVPDD--M 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 204 VR---DVLKLSG------EPNASDFFPFLRGLD--LQGVERRAQKLrerfdGIFSEMIERRLKDMRE---------KGMV 263
Cdd:cd11068  122 TRltlDTIALCGfgyrfnSFYRDEPHPFVEAMVraLTEAGRRANRP-----PILNKLRRRAKRQFREdialmrdlvDEII 196
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 264 NERDEESGRGIKesDFLGVLLELMD--HNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRV 341
Cdd:cd11068  197 AERRANPDGSPD--DLLNLMLNGKDpeTGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEV 274
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 342 IGKDKMMEEsHIPDVPFLQAIVKEVLRLHPAAPlLIPRLCDSDCQIDG-HIIEKNTEVLVNVWAIGRDPKVW-SDPLKFD 419
Cdd:cd11068  275 LGDDPPPYE-QVAKLRYIRRVLDETLRLWPTAP-AFARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFR 352
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 586644824 420 PSRFVGTNLE-FKGNDYEllPFGAGRRICIGMPLASSMVHLVLGSLLHYFN 469
Cdd:cd11068  353 PERFLPEEFRkLPPNAWK--PFGNGQRACIGRQFALQEATLVLAMLLQRFD 401
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
233-483 1.28e-33

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: 131.58  E-value: 1.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 233 RRAQKLRERFDGIFSEMIERRLKDMREKGmvnerdeesgrgikeSDFLGVLLELMDHNEGLQMEHvkGMLMD----MFIA 308
Cdd:cd11061  165 PGATKARKRFLDFVRAQLKERLKAEEEKR---------------PDIFSYLLEAKDPETGEGLDL--EELVGearlLIVA 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 309 GTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDkmmEESHIPD----VPFLQAIVKEVLRLHPAAPLLIPRLCDSD 384
Cdd:cd11061  228 GSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSD---DEIRLGPklksLPYLRACIDEALRLSPPVPSGLPRETPPG 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 385 -CQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGS 463
Cdd:cd11061  305 gLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVRARSAFIPFSIGPRGCIGKNLAYMELRLVLAR 384
                        250       260
                 ....*....|....*....|....*..
gi 586644824 464 LLH-------YFNWKVEGEVDMTEEFG 483
Cdd:cd11061  385 LLHrydfrlaPGEDGEAGEGGFKDAFG 411
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
262-492 1.55e-32

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: 128.85  E-value: 1.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 262 MVNERDEESGRGIK-ESDFLGVLLELMD-HNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELr 339
Cdd:cd11060  185 AVAERLAEDAESAKgRKDMLDSFLEAGLkDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEI- 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 340 rvigkDKMMEESHIPDV---------PFLQAIVKEVLRLHPAAPLLIPRLC-DSDCQIDGHIIEKNTEVLVNVWAIGRDP 409
Cdd:cd11060  264 -----DAAVAEGKLSSPitfaeaqklPYLQAVIKEALRLHPPVGLPLERVVpPGGATICGRFIPGGTIVGVNPWVIHRDK 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 410 KVWS-DPLKFDPSRFvgtnLEFKGNDYE-----LLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV---EGEVDmTE 480
Cdd:cd11060  339 EVFGeDADVFRPERW----LEADEEQRRmmdraDLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELvdpEKEWK-TR 413
                        250
                 ....*....|..
gi 586644824 481 EFGITLQKALPL 492
Cdd:cd11060  414 NYWFVKQSDFDV 425
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
60-487 3.24e-32

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: 128.03  E-value: 3.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSygGNSLVWAAYGHHWRLLRRLSFTEL----FST 135
Cdd:cd20667    1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLF--GEKGIICTNGLTWKQQRRFCMTTLrelgLGK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 136 KRLNSMEKFRKAEVSKTMASIyeesiKGNSVNIGSTVFSTMLGIVENMVCGNYvFKKGDELATELKGMVRDVLKLSGEP- 214
Cdd:cd20667   79 QALESQIQHEAAELVKVFAQE-----NGRPFDPQDPIVHATANVIGAVVFGHR-FSSEDPIFLELIRAINLGLAFASTIw 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 215 -NASDFFPFLrgldLQGVERRAQKlrerfdgIFSEMIERRLKDMREKGMVNERDEESGRGIKESDFLGVLLELMDHNEGL 293
Cdd:cd20667  153 gRLYDAFPWL----MRYLPGPHQK-------IFAYHDAVRSFIKKEVIRHELRTNEAPQDFIDCYLAQITKTKDDPVSTF 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 294 QMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAA 373
Cdd:cd20667  222 SEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVV 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 374 PLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDyELLPFGAGRRICIGMPLA 453
Cdd:cd20667  302 SVGAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNE-AFLPFSAGHRVCLGEQLA 380
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 586644824 454 SSMVHLVLGSLLHYFNWKV-EGEVDMTEE--FGITLQ 487
Cdd:cd20667  381 RMELFIFFTTLLRTFNFQLpEGVQELNLEyvFGGTLQ 417
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
60-487 3.52e-32

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: 127.61  E-value: 3.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPvPLAAKTLSYGGNSLVWAAyGHHWRLLRRlsftelFSTKRLN 139
Cdd:cd20671    1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRP-PIPIFQAIQHGNGVFFSS-GERWRTTRR------FTVRSMK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 140 SMEKFRKAEVSKTMASIyeESIKGNSVNIGSTVFSTML------GIVENMVCGNYvFKKGDELATELKGMVRDVLKLSGE 213
Cdd:cd20671   73 SLGMGKRTIEDKILEEL--QFLNGQIDSFNGKPFPLRLlgwaptNITFAMLFGRR-FDYKDPTFVSLLDLIDEVMVLLGS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 214 PNAS--DFFPFLrgldlqgverraqklrerfdGIFSEMIERRLKDMREKGMVNERDEESGRGIKESDFLGVLLELM---- 287
Cdd:cd20671  150 PGLQlfNLYPVL--------------------GAFLKLHKPILDKVEEVCMILRTLIEARRPTIDGNPLHSYIEALiqkq 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 288 ---DHNEGLQME-HVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIV 363
Cdd:cd20671  210 eedDPKETLFHDaNVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVI 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 364 KEVLRLHPAAPlLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDyELLPFGAG 443
Cdd:cd20671  290 HEVQRFITLLP-HVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKE-AFLPFSAG 367
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 586644824 444 RRICIGMPLASSMVHLVLGSLLHYFNW-----KVEGEVDMTEEFGITLQ 487
Cdd:cd20671  368 RRVCVGESLARTELFIFFTGLLQKFTFlpppgVSPADLDATPAAAFTMR 416
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
60-471 3.79e-32

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: 127.73  E-value: 3.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPvPLAAKTLSYGGNSLVWAAyGHHWRLLRRLSFTELfstkRLN 139
Cdd:cd20670    1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRG-ELATIERNFQGHGVALAN-GERWRILRRFSLTIL----RNF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 140 SMEKfRKAE--VSKTMASIYEESIKGNSVNIGSTVFSTMlgIVENMVCgNYVFkkGDELATELKgMVRDVLKLSGEPNAS 217
Cdd:cd20670   75 GMGK-RSIEerIQEEAGYLLEEFRKTKGAPIDPTFFLSR--TVSNVIS-SVVF--GSRFDYEDK-QFLSLLRMINESFIE 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 218 DFFPFLRGLDL-QGVerrAQKLRERFDGIFSeMIERrLKD-MREKGMVNER--DEESGRgikesDFLGVLLELMDHNEG- 292
Cdd:cd20670  148 MSTPWAQLYDMySGI---MQYLPGRHNRIYY-LIEE-LKDfIASRVKINEAslDPQNPR-----DFIDCFLIKMHQDKNn 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 293 ----LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLR 368
Cdd:cd20670  218 phteFNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQR 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 369 LHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDyELLPFGAGRRICI 448
Cdd:cd20670  298 LTDIVPLGVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNE-AFVPFSSGKRVCL 376
                        410       420
                 ....*....|....*....|...
gi 586644824 449 GMPLASSMVHLVLGSLLHYFNWK 471
Cdd:cd20670  377 GEAMARMELFLYFTSILQNFSLR 399
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
65-487 9.17e-32

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: 126.55  E-value: 9.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  65 PFKLGMRkAVVISSPHPAKQIFKTHdrkFSSRPVPLAAKTLSYG--GNSLVwAAYGHHWRLLRRLsFTELFSTKRL-NSM 141
Cdd:cd11064    6 PWPGGPD-GIVTADPANVEHILKTN---FDNYPKGPEFRDLFFDllGDGIF-NVDGELWKFQRKT-ASHEFSSRALrEFM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 142 EKFRKAEVSKTMASIYEESIKGNSV-------------NIGSTVFSTMLGIVENMVCGNYVFKKGDElATELkGMVRDVl 208
Cdd:cd11064   80 ESVVREKVEKLLVPLLDHAAESGKVvdlqdvlqrftfdVICKIAFGVDPGSLSPSLPEVPFAKAFDD-ASEA-VAKRFI- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 209 klsgepnasdFFPFL----RGLDLqGVERRAQKLRERFDGIFSEMIERRlkdMREKGMVNERDEESgrgikeSDFLGVLL 284
Cdd:cd11064  157 ----------VPPWLwklkRWLNI-GSEKKLREAIRVIDDFVYEVISRR---REELNSREEENNVR------EDLLSRFL 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 285 ELMDHNEGLQM-EHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKdKMMEESHIPD------VP 357
Cdd:cd11064  217 ASEEEEGEPVSdKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPK-LTTDESRVPTyeelkkLV 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 358 FLQAIVKEVLRLHPAAPLlIPRLC-DSDCQIDGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLEFKG-ND 434
Cdd:cd11064  296 YLHAALSESLRLYPPVPF-DSKEAvNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDGGLRPeSP 374
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 586644824 435 YELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEGEVDMTEEFGITLQ 487
Cdd:cd11064  375 YKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVEPKMSLTLH 427
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
240-492 2.85e-31

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: 125.21  E-value: 2.85e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 240 ERFDGIFSEM---IERRLKDMREKGmvnerdeesgrgIKESDFLGVLLELMdHNEGLQMEHVKGMLMDMFIAGTDTTSAT 316
Cdd:cd20643  187 EAWDVIFNHAdkcIQNIYRDLRQKG------------KNEHEYPGILANLL-LQDKLPIEDIKASVTELMAGGVDTTSMT 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 317 VEWAMAELLNHPYVMEEARDEL---RRVIGKD--KMMEEshipdVPFLQAIVKEVLRLHPAApLLIPRLCDSDCQIDGHI 391
Cdd:cd20643  254 LQWTLYELARNPNVQEMLRAEVlaaRQEAQGDmvKMLKS-----VPLLKAAIKETLRLHPVA-VSLQRYITEDLVLQNYH 327
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 392 IEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLE-FKGndyelLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNW 470
Cdd:cd20643  328 IPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDIThFRN-----LGFGFGPRQCLGRRIAETEMQLFLIHMLENFKI 402
                        250       260
                 ....*....|....*....|..
gi 586644824 471 KVEGEVDMTEEFGITLQKALPL 492
Cdd:cd20643  403 ETQRLVEVKTTFDLILVPEKPI 424
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
60-479 3.07e-31

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: 125.26  E-value: 3.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSR---PVPLAAKTlsygGNSLVWAAyGHHWRLLRRLSFTEL--FS 134
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRgdyPVFFNFTK----GNGIAFSN-GERWKILRRFALQTLrnFG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 135 TKRlNSMEKFRKAEVSKTMASIyeESIKGNSVNIGSTVFSTMLGIVENMVCGNYvFKKGDELATELKGMVRDVLKLSGEP 214
Cdd:cd20669   76 MGK-RSIEERILEEAQFLLEEL--RKTKGAPFDPTFLLSRAVSNIICSVVFGSR-FDYDDKRLLTILNLINDNFQIMSSP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 215 NAS--DFFPFLrgLD-LQGVERRaqkLRERFDGIfSEMIERRLKDMREkgmvnERDEESGRgikesDFLGVLLELMDHNE 291
Cdd:cd20669  152 WGElyNIFPSV--MDwLPGPHQR---IFQNFEKL-RDFIAESVREHQE-----SLDPNSPR-----DFIDCFLTKMAEEK 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 292 GLQMEH--VKGMLM---DMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEV 366
Cdd:cd20669  216 QDPLSHfnMETLVMtthNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEI 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 367 LRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDyELLPFGAGRRI 446
Cdd:cd20669  296 QRFADIIPMSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKND-AFMPFSAGKRI 374
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 586644824 447 CIGMPLASSMVHLVLGSLLHYFNWKVEG---EVDMT 479
Cdd:cd20669  375 CLGESLARMELFLYLTAILQNFSLQPLGapeDIDLT 410
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
236-473 6.88e-31

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: 124.10  E-value: 6.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 236 QKLRERFDGIFS---EMIERRLKDMREKgmVNERDEESGRGIkeSDFLGvllelmdhNEGLQMEHVKGMLMDMFIAGTDT 312
Cdd:cd20648  182 QRFCRSWDQMFAfakGHIDRRMAEVAAK--LPRGEAIEGKYL--TYFLA--------REKLPMKSIYGNVTELLLAGVDT 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 313 TSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHII 392
Cdd:cd20648  250 ISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPDRDIQVGEYII 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 393 EKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTnlEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV 472
Cdd:cd20648  330 PKKTLITLCHYATSRDENQFPDPNSFRPERWLGK--GDTHHPYASLPFGFGKRSCIGRRIAELEVYLALARILTHFEVRP 407

                 .
gi 586644824 473 E 473
Cdd:cd20648  408 E 408
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
59-472 9.14e-30

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: 121.02  E-value: 9.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  59 TYGPIMPFKLGMRKAVVISSPHPAKQIFKT---HDRKFSSRPvpLAAKTLSYGGNSLVWAAYGHHWRLLrrlsfTELFST 135
Cdd:cd20639   10 IYGKTFLYWFGPTPRLTVADPELIREILLTradHFDRYEAHP--LVRQLEGDGLVSLRGEKWAHHRRVI-----TPAFHM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 136 KRLNS------------MEKFRK---------AEVSKTMASIYEESIK----GNSVNIGSTVFstmlgivenmvcgnyvf 190
Cdd:cd20639   83 ENLKRlvphvvksvadmLDKWEAmaeaggegeVDVAEWFQNLTEDVISrtafGSSYEDGKAVF----------------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 191 kkgdELATELkgmvrdvLKLSGEPNASDFFPFLRGLDLQGvERRAQKLRERFDGIFSEMIERRlkdmrEKGMVNERDEES 270
Cdd:cd20639  146 ----RLQAQQ-------MLLAAEAFRKVYIPGYRFLPTKK-NRKSWRLDKEIRKSLLKLIERR-----QTAADDEKDDED 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 271 GRgikesDFLGVLLELMDHNEGLQM--EHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMM 348
Cdd:cd20639  209 SK-----DLLGLMISAKNARNGEKMtvEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVP 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 349 EESHIPDVPFLQAIVKEVLRLHPAAPLLIpRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTN 427
Cdd:cd20639  284 TKDHLPKLKTLGMILNETLRLYPPAVATI-RRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGV 362
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 586644824 428 LEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV 472
Cdd:cd20639  363 ARAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRL 407
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
233-475 1.33e-29

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: 120.86  E-value: 1.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 233 RRAQKLRERFDGIFSEMIERRLKDMREKGmvnerdeesgrGIKESDFLGVLLELMDHNEGLQMEHVKGMLMDMFIAGTDT 312
Cdd:cd11041  174 RRLRRLLRRARPLIIPEIERRRKLKKGPK-----------EDKPNDLLQWLIEAAKGEGERTPYDLADRQLALSFAAIHT 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 313 TSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQI-DGHI 391
Cdd:cd11041  243 TSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVTLsDGLT 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 392 IEKNTEVLVNVWAIGRDPKVWSDPLKFDP---------------SRFVGTNLEFkgndyelLPFGAGRRICIGMPLASSM 456
Cdd:cd11041  323 LPKGTRIAVPAHAIHRDPDIYPDPETFDGfrfyrlreqpgqekkHQFVSTSPDF-------LGFGHGRHACPGRFFASNE 395
                        250
                 ....*....|....*....
gi 586644824 457 VHLVLGSLLHYFNWKVEGE 475
Cdd:cd11041  396 IKLILAHLLLNYDFKLPEG 414
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
233-468 1.47e-29

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: 120.57  E-value: 1.47e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 233 RRAQKLRERFDgifSEMIERRLKDMREKGMvnerDEESGRGIKES--DFLGVLLELMD-HNEGLQMEHVKGMlMDMFI-A 308
Cdd:cd20679  184 RRACRLVHDFT---DAVIQERRRTLPSQGV----DDFLKAKAKSKtlDFIDVLLLSKDeDGKELSDEDIRAE-ADTFMfE 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 309 GTDTTSATVEWAMAELLNHPYVMEEARDELRRVIgKDKMMEE---SHIPDVPFLQAIVKEVLRLHPAAPLlIPRLCDSDC 385
Cdd:cd20679  256 GHDTTASGLSWILYNLARHPEYQERCRQEVQELL-KDREPEEiewDDLAQLPFLTMCIKESLRLHPPVTA-ISRCCTQDI 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 386 QI-DGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEfKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSL 464
Cdd:cd20679  334 VLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQ-GRSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALT 412

                 ....
gi 586644824 465 LHYF 468
Cdd:cd20679  413 LLRF 416
PLN02738 PLN02738
carotene beta-ring hydroxylase
53-504 3.01e-29

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 121.56  E-value: 3.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  53 LAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSrpvPLAAKTLSY-GGNSLVwAAYGHHWRLLRRlSFTE 131
Cdd:PLN02738 157 LYELFLTYGGIFRLTFGPKSFLIVSDPSIAKHILRDNSKAYSK---GILAEILEFvMGKGLI-PADGEIWRVRRR-AIVP 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 132 LFSTKRLNSMEKFRKAEVSKTMASIYEESIKGNSVNIGStVFSTM-LGIVENMVCgNYVFkkgDELATElKGMVRDVLKL 210
Cdd:PLN02738 232 ALHQKYVAAMISLFGQASDRLCQKLDAAASDGEDVEMES-LFSRLtLDIIGKAVF-NYDF---DSLSND-TGIVEAVYTV 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 211 --SGEPNASDFFPFLRGLDLQGVERRAQKLRERFdgifsEMIERRLKDMRE--KGMVNERD---EESGRGIKESDFLGVL 283
Cdd:PLN02738 306 lrEAEDRSVSPIPVWEIPIWKDISPRQRKVAEAL-----KLINDTLDDLIAicKRMVEEEElqfHEEYMNERDPSILHFL 380
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 284 LELMDHNEGLQMehvKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGkDKMMEESHIPDVPFLQAIV 363
Cdd:PLN02738 381 LASGDDVSSKQL---RDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLG-DRFPTIEDMKKLKYTTRVI 456
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 364 KEVLRLHPAAPLLIPRLCDSDcQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFV--GTNLEFKGNDYELLPFG 441
Cdd:PLN02738 457 NESLRLYPQPPVLIRRSLEND-MLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWPldGPNPNETNQNFSYLPFG 535
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586644824 442 AGRRICIGMPLASSMVHLVLGSLLHYFNWKV---EGEVDMTEEFGITLQKALPLVVV------ATPSLPLNP 504
Cdd:PLN02738 536 GGPRKCVGDMFASFENVVATAMLVRRFDFQLapgAPPVKMTTGATIHTTEGLKMTVTrrtkppVIPNLPMTP 607
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
60-471 4.12e-29

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: 119.13  E-value: 4.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTL--SYGgnslVWAAYGHHWRLLRRLSFTELfstkR 137
Cdd:cd20668    1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGRGEQATFDWLfkGYG----VAFSNGERAKQLRRFSIATL----R 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 138 LNSMEKFRKAEVSKTMASIYEESIKG-NSVNIGSTVF--STMLGIVENMVCGNYvFKKGDELATELKGMVRDVLKLSGEP 214
Cdd:cd20668   73 DFGVGKRGIEERIQEEAGFLIDALRGtGGAPIDPTFYlsRTVSNVISSIVFGDR-FDYEDKEFLSLLRMMLGSFQFTATS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 215 NASDFFPFLRGLD-LQGVERRAQKLRERFDGIFSEMIERrlkdmrekgmvNER--DEESGRGIKESDFLGVLLELMDHNE 291
Cdd:cd20668  152 TGQLYEMFSSVMKhLPGPQQQAFKELQGLEDFIAKKVEH-----------NQRtlDPNSPRDFIDSFLIRMQEEKKNPNT 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 292 GLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHP 371
Cdd:cd20668  221 EFYMKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGD 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 372 AAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDyELLPFGAGRRICIGMP 451
Cdd:cd20668  301 VIPMGLARRVTKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSD-AFVPFSIGKRYCFGEG 379
                        410       420
                 ....*....|....*....|
gi 586644824 452 LASSMVHLVLGSLLHYFNWK 471
Cdd:cd20668  380 LARMELFLFFTTIMQNFRFK 399
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
49-487 2.09e-28

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: 117.22  E-value: 2.09e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  49 PHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRP-VPLAAKTLSYGGnsLVWAAYGHHWRLLRRL 127
Cdd:cd20661    1 PHVYMKKQSQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPsLPLFMKLTNMGG--LLNSKYGRGWTEHRKL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 128 SFT--ELFSTKRlNSMEKFRKAEVSKTMASIyeESIKGNSVNIGSTVFSTMLGIVeNMVCGNYVFKKGDelaTELKGMVr 205
Cdd:cd20661   79 AVNcfRYFGYGQ-KSFESKISEECKFFLDAI--DTYKGKPFDPKHLITNAVSNIT-NLIIFGERFTYED---TDFQHMI- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 206 DVLKLSGEPNAS------DFFPFLRGLDLQGVERRAQKLRERFDgIFSEMIERrlkdmrekgMVNERDEESGRgikesDF 279
Cdd:cd20661  151 EIFSENVELAASawvflyNAFPWIGILPFGKHQQLFRNAAEVYD-FLLRLIER---------FSENRKPQSPR-----HF 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 280 LGVLLELMDHNEG-----LQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIP 354
Cdd:cd20661  216 IDAYLDEMDQNKNdpestFSMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKC 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 355 DVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGND 434
Cdd:cd20661  296 KMPYTEAVLHEVLRFCNIVPLGIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKE 375
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 586644824 435 yELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEGEV--DMTEEFGITLQ 487
Cdd:cd20661  376 -AFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHGLipDLKPKLGMTLQ 429
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
59-468 3.78e-28

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: 116.30  E-value: 3.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  59 TYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPL-----AAKTLSYGgnslVWAAYGHHWRLLRRLSFTELF 133
Cdd:cd20646    3 IYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHwkehrDLRGHAYG----PFTEEGEKWYRLRSVLNQRML 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 134 STKRLNSMEKFRKAEVSKTMASIY---EESIKGNSVN-------------IGSTVFSTMLGIVENMVCgnyvfKKGDELA 197
Cdd:cd20646   79 KPKEVSLYADAINEVVSDLMKRIEylrERSGSGVMVSdlanelykfafegISSILFETRIGCLEKEIP-----EETQKFI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 198 TELKGMVRDVLKLSGEPNAS-DFFPFLrgldlqgverraQKLRERFDGIFS---EMIERRLKDMREKgmvNERDEESgrg 273
Cdd:cd20646  154 DSIGEMFKLSEIVTLLPKWTrPYLPFW------------KRYVDAWDTIFSfgkKLIDKKMEEIEER---VDRGEPV--- 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 274 ikESDFLGVLLElmdhNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHI 353
Cdd:cd20646  216 --EGEYLTYLLS----SGKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDI 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 354 PDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVgTNLEFKGN 433
Cdd:cd20646  290 AKMPLLKAVIKETLRLYPVVPGNARVIVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWL-RDGGLKHH 368
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 586644824 434 DYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYF 468
Cdd:cd20646  369 PFGSIPFGYGVRACVGRRIAELEMYLALSRLIKRF 403
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
296-486 9.66e-27

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: 112.27  E-value: 9.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 296 EHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPL 375
Cdd:cd11063  215 KELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPL 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 376 LIpRLCDSDCQI------DGH---IIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFvgtnLEFKGNDYELLPFGAGRR 445
Cdd:cd11063  295 NS-RVAVRDTTLprgggpDGKspiFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERW----EDLKRPGWEYLPFNGGPR 369
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 586644824 446 ICIGMPLASSMVHLVLGSLLHYFNWKVEGEV-DMTEEFGITL 486
Cdd:cd11063  370 ICLGQQFALTEASYVLVRLLQTFDRIESRDVrPPEERLTLTL 411
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
242-472 2.21e-26

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: 111.16  E-value: 2.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 242 FDGIF--SEM-IERRLKDMREKgmvnerdEESGRGIKesdflGVLLELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVE 318
Cdd:cd20647  191 WDGLFkfSQIhVDNRLREIQKQ-------MDRGEEVK-----GGLLTYLLVSKELTLEEIYANMTEMLLAGVDTTSFTLS 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 319 WAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPlLIPRLCDSDCQIDGHIIEKNTEV 398
Cdd:cd20647  259 WATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLP-GNGRVTQDDLIVGGYLIPKGTQL 337
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586644824 399 LVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV 472
Cdd:cd20647  338 ALCHYSTSYDEENFPRAEEFRPERWLRKDALDRVDNFGSIPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIKV 411
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
59-471 2.67e-26

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: 111.47  E-value: 2.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  59 TYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVP-LAAKTLSyggNSLVWAAyGHHWRLLRRLsFTELFSTKR 137
Cdd:cd20649    1 KYGPICGYYIGRRMFVVIAEPDMIKQVLVKDFNNFTNRMKAnLITKPMS---DSLLCLR-DERWKRVRSI-LTPAFSAAK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 138 LNSMEKFRKAEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMVCGNYVFKKGD-------------ELATELKGMV 204
Cdd:cd20649   76 MKEMVPLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQVDSQKNpddpfvknckrffEFSFFRPILI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 205 rdvLKLSgepnasdfFPFLrgldLQGVERR-AQKLRERFDGIFSEMIERRLKdMREKGMVNERdeesgrgikESDFLGVL 283
Cdd:cd20649  156 ---LFLA--------FPFI----MIPLARIlPNKSRDELNSFFTQCIRNMIA-FRDQQSPEER---------RRDFLQLM 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 284 LELMDHNEGLQMEH-------------------------------------VKGMLMDMFIAGTDTTSATVEWAMAELLN 326
Cdd:cd20649  211 LDARTSAKFLSVEHfdivndadesaydghpnspaneqtkpskqkrmltedeIVGQAFIFLIAGYETTTNTLSFATYLLAT 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 327 HPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAApLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIG 406
Cdd:cd20649  291 HPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPA-FRFAREAAEDCVVLGQRIPAGAVLEIPVGFLH 369
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586644824 407 RDPKVWSDPLKFDPSRFVGTNLEfKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWK 471
Cdd:cd20649  370 HDPEHWPEPEKFIPERFTAEAKQ-RRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQ 433
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
252-493 3.02e-26

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: 110.97  E-value: 3.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 252 RRLKDMREKGMVNERdeesgrgikeSDFLgvllELMDHNEGLQMEHVKGMLMDM--------FI-AGTDTTSATVEWAMA 322
Cdd:cd20650  188 KKIKESRLDSTQKHR----------VDFL----QLMIDSQNSKETESHKALSDLeilaqsiiFIfAGYETTSSTLSFLLY 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 323 ELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLiPRLCDSDCQIDGHIIEKNTEVLVNV 402
Cdd:cd20650  254 ELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRL-ERVCKKDVEINGVFIPKGTVVMIPT 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 403 WAIGRDPKVWSDPLKFDPSRFVGTNlefKGN--DYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV--EGEVDM 478
Cdd:cd20650  333 YALHRDPQYWPEPEEFRPERFSKKN---KDNidPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPckETQIPL 409
                        250
                 ....*....|....*
gi 586644824 479 TEEFGITLQKALPLV 493
Cdd:cd20650  410 KLSLQGLLQPEKPIV 424
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
252-468 1.05e-25

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: 109.46  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 252 RRLKDMREKGMVNERDEESGRgiKESDFLGVLLELMDHN-EGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYV 330
Cdd:cd20680  199 EEMKAEEDKTGDSDGESPSKK--KRKAFLDMLLSVTDEEgNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEV 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 331 MEEARDELRRVIGK-DKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDsDCQIDGHIIEKNTEVLVNVWAIGRDP 409
Cdd:cd20680  277 QRKVHKELDEVFGKsDRPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCE-DCEIRGFKVPKGVNAVIIPYALHRDP 355
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 410 KVWSDPLKFDPSRFVGTNLEfKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYF 468
Cdd:cd20680  356 RYFPEPEEFRPERFFPENSS-GRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHF 413
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
59-469 3.26e-25

cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome P450 family 7, subfamily B, polypeptide 1, cytochrome P450 family 8, subfamily A, polypeptide 1; This family is composed of cytochrome P450s (CYPs) with similarity to the human P450s CYP7A1, CYP7B1, CYP8B1, CYP39A1 and prostacyclin synthase (CYP8A1). CYP7A1, CYP7B1, CYP8B1, and CYP39A1 are involved in the catabolism of cholesterol to bile acids (BAs) in two major pathways. CYP7A1 (cholesterol 7alpha-hydroxylase) and CYP8B1 (sterol 12-alpha-hydroxylase) function in the classic (or neutral) pathway, which leads to two bile acids: cholic acid (CA) and chenodeoxycholic acid (CDCA). CYP7B1 and CYP39A1 are 7-alpha-hydroxylases involved in the alternative (or acidic) pathway, which leads mainly to the formation of CDCA. Prostacyclin synthase (CYP8A1) catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 107.84  E-value: 3.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  59 TYGPIMPFKLGMRKAVVISSPHPAKQIFKtHDRKFSSRP--VPLAAKTLSYGGNSLVWAAYGHHWRL---LRRLSFTELF 133
Cdd:cd11040   10 SGGPIFTIRLGGQKIYVITDPELISAVFR-NPKTLSFDPivIVVVGRVFGSPESAKKKEGEPGGKGLirlLHDLHKKALS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 134 STKRLNSMEKFRKAEVSKTMAsiyEESIKGNS----VNIGSTVFSTMLGIVENMVCGNYVFKKGDELATELKGMVRDVLK 209
Cdd:cd11040   89 GGEGLDRLNEAMLENLSKLLD---ELSLSGGTstveVDLYEWLRDVLTRATTEALFGPKLPELDPDLVEDFWTFDRGLPK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 210 LsgepnASDFFPFL-------RGLDLQGVERRAQKLRERFDGIfSEMIERRLKDMREKGMvneRDEESGRgikesdflgv 282
Cdd:cd11040  166 L-----LLGLPRLLarkayaaRDRLLKALEKYYQAAREERDDG-SELIRARAKVLREAGL---SEEDIAR---------- 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 283 llelmdhneglqmehvkgMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKmmEESHIPDV------ 356
Cdd:cd11040  227 ------------------AELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDS--GTNAILDLtdllts 286
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 357 -PFLQAIVKEVLRLHPAAPllIPRLCDSDC-QIDGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLEFKGN 433
Cdd:cd11040  287 cPLLDSTYLETLRLHSSST--SVRLVTEDTvLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKKGR 364
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 586644824 434 D--YELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFN 469
Cdd:cd11040  365 GlpGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFD 402
PLN02290 PLN02290
cytokinin trans-hydroxylase
217-472 1.02e-24

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 107.21  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 SDFFPflrgldlQGVERRAQKLRERFDGIFSEMIERRlKDMREKGmvneRDEESGRgikesDFLGVLLELMDHNEGLQME 296
Cdd:PLN02290 249 SRFFP-------SKYNREIKSLKGEVERLLMEIIQSR-RDCVEIG----RSSSYGD-----DLLGMLLNEMEKKRSNGFN 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 297 HVKGMLMD----MFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEEsHIPDVPFLQAIVKEVLRLHPA 372
Cdd:PLN02290 312 LNLQLIMDecktFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVD-HLSKLTLLNMVINESLRLYPP 390
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 373 APLLiPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLEFKGNdyeLLPFGAGRRICIGMP 451
Cdd:PLN02290 391 ATLL-PRMAFEDIKLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRH---FIPFAAGPRNCIGQA 466
                        250       260
                 ....*....|....*....|.
gi 586644824 452 LASSMVHLVLGSLLHYFNWKV 472
Cdd:PLN02290 467 FAMMEAKIILAMLISKFSFTI 487
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
295-473 1.35e-24

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: 105.48  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 295 MEHVKGMLMdmfiAGTDTTSATVEWAMAELLNHPYVMEEARDELRRvIGKDKMMEEShIPDVPFLQAIVKEVLRLHPAAP 374
Cdd:cd11045  213 VNHMIFLMM----AAHDTTTSTLTSMAYFLARHPEWQERLREESLA-LGKGTLDYED-LGQLEVTDWVFKEALRLVPPVP 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 375 LLiPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGMPLAS 454
Cdd:cd11045  287 TL-PRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRYAWAPFGGGAHKCIGLHFAG 365
                        170
                 ....*....|....*....
gi 586644824 455 SMVHLVLGSLLHYFNWKVE 473
Cdd:cd11045  366 MEVKAILHQMLRRFRWWSV 384
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
257-453 1.71e-24

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: 105.82  E-value: 1.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 257 MREKGMVNERDEESGRGIKESDFLGVLLELMDHNE-GLQMEHVKGMLmDMFI-AGTDTTSATVEWAMAELLNHPYVMEEA 334
Cdd:cd20678  198 QRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGkSLSDEDLRAEV-DTFMfEGHDTTASGISWILYCLALHPEHQQRC 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 335 RDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSD 414
Cdd:cd20678  277 REEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPN 356
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 586644824 415 PLKFDPSRFVGTNLEfKGNDYELLPFGAGRRICIGMPLA 453
Cdd:cd20678  357 PEVFDPLRFSPENSS-KRHSHAFLPFSAGPRNCIGQQFA 394
PLN02936 PLN02936
epsilon-ring hydroxylase
60-449 2.30e-24

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 106.03  E-value: 2.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVPLAAKTLSYGGNSLvwaAYGHHWRLLRRLSFTELFStKRLN 139
Cdd:PLN02936  49 YGPVYRLAAGPRNFVVVSDPAIAKHVLRNYGSKYAKGLVAEVSEFLFGSGFAI---AEGELWTARRRAVVPSLHR-RYLS 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 140 SMEKFRKAEVSKTMASIYEESI-KGNSVNIGSTvFSTMLGIVENMVCGNYVFkkgDELATE--LKGMVRDVLKlSGEPNA 216
Cdd:PLN02936 125 VMVDRVFCKCAERLVEKLEPVAlSGEAVNMEAK-FSQLTLDVIGLSVFNYNF---DSLTTDspVIQAVYTALK-EAETRS 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 SDFFPFLRGLDLQGVERRaQKLRERFDGIFSEMIERRLKDMREkgMVnERDEESGRG---IKESDfLGVLLELMDHNEGL 293
Cdd:PLN02936 200 TDLLPYWKVDFLCKISPR-QIKAEKAVTVIRETVEDLVDKCKE--IV-EAEGEVIEGeeyVNDSD-PSVLRFLLASREEV 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 294 QMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGkDKMMEESHIPDVPFLQAIVKEVLRLHPAA 373
Cdd:PLN02936 275 SSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMRLYPHP 353
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586644824 374 PLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRF--VGTNLEFKGNDYELLPFGAGRRICIG 449
Cdd:PLN02936 354 PVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdlDGPVPNETNTDFRYIPFSGGPRKCVG 431
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
275-491 7.69e-24

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: 103.77  E-value: 7.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 275 KESDFLGVLLELMDHNEgLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIP 354
Cdd:cd20644  211 RPQHYTGIVAELLLQAE-LSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALT 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 355 DVPFLQAIVKEVLRLHPAApLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVgtNLEFKGND 434
Cdd:cd20644  290 ELPLLKAALKETLRLYPVG-ITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWL--DIRGSGRN 366
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 586644824 435 YELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEGEVDMTEEFGITLQKALP 491
Cdd:cd20644  367 FKHLAFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLVETLSQEDIKTVYSFILRPEKP 423
P450_cycloAA_1 TIGR04538
cytochrome P450, cyclodipeptide synthase-associated; Members of this subfamily are cytochrome ...
218-473 1.80e-23

cytochrome P450, cyclodipeptide synthase-associated; Members of this subfamily are cytochrome P450 enzymes that occur next to tRNA-dependent cyclodipeptide synthases. This group does NOT include CYP121 (Rv2275) from Mycobacterium tuberculosis, adjacent to the cyclodityrosine synthetase Rv2276.


Pssm-ID: 275331  Cd Length: 395  Bit Score: 102.11  E-value: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  218 DF---FPFLRGLDLQGV-ERRAQKLRERFDGI--F-------SEMIERRLKDMRE-----KGMVNERdeesgRGIKESDF 279
Cdd:TIGR04538 122 DFgktFAVCVTMDLLGLdKRDHEKIREWHSGIakFitslnqsPEERMHSLECSEKlreylMPIIEER-----RKNPGSDL 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  280 LGVLLELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPyvmeearDELRRVIgKDKmmeeshipdvPFL 359
Cdd:TIGR04538 197 ISILCTSEDEGNAMSDTEILALILNILLAATEPADKTLAYMIYHLLNNP-------EQLNDVL-DDR----------KLL 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  360 QAIVKEVLRLHPaaPL-LIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELL 438
Cdd:TIGR04538 259 RRAIAETLRLHS--PVqLIPRQLSQDVTISGKEIKKGDTVFCMIGAANRDPEAFEDPDEFNIHRKDLVNKSAFTGAARHL 336
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 586644824  439 PFGAGRRICIGMPLASSMVHLVLGSLLHYF-NWKVE 473
Cdd:TIGR04538 337 AFGSGVHNCVGAAFAKRQLEIVANILLDLLkNIRLE 372
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
60-468 1.90e-22

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: 99.47  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFSSRPVpLAAKTLSYGGNSLVWAAyGHHWRLLRRLSFTelfsTKRLN 139
Cdd:cd20672    1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGT-IAVVDPIFQGYGVIFAN-GERWKTLRRFSLA----TMRDF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 140 SMEKFRKAEVSKTMAS-IYEESIKGNSVNIGSTVFstMLGIVENMVCgNYVFKK----GDELATELKGMVRDVLKLSGEp 214
Cdd:cd20672   75 GMGKRSVEERIQEEAQcLVEELRKSKGALLDPTFL--FQSITANIIC-SIVFGErfdyKDPQFLRLLDLFYQTFSLISS- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 215 NASDFFPFLRGL--DLQGVERRAQK-LRERFDGIfSEMIERRLKDMrekgmvnerDEESGRgikesDFLGVLLELMDH-- 289
Cdd:cd20672  151 FSSQVFELFSGFlkYFPGAHRQIYKnLQEILDYI-GHSVEKHRATL---------DPSAPR-----DFIDTYLLRMEKek 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 290 -NEGLQMEHVKGML--MDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEV 366
Cdd:cd20672  216 sNHHTEFHHQNLMIsvLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEI 295
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 367 LRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDyELLPFGAGRRI 446
Cdd:cd20672  296 QRFSDLIPIGVPHRVTKDTLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSE-AFMPFSTGKRI 374
                        410       420
                 ....*....|....*....|..
gi 586644824 447 CIGMPLASSMVHLVLGSLLHYF 468
Cdd:cd20672  375 CLGEGIARNELFLFFTTILQNF 396
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
233-453 4.98e-22

cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins including Sinorhizobium fredii CYPBJ-4 homolog. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 97.90  E-value: 4.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 233 RRAQKLRERFDgifsEMIERRLKDMREKG--------MVNERDEEsGRGIKESDFLGVLLELMdhneglqmehvkgmlmd 304
Cdd:cd20614  160 RRSRRARAWID----ARLSQLVATARANGartglvaaLIRARDDN-GAGLSEQELVDNLRLLV----------------- 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 305 mfIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVigKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLlIPRLCDSD 384
Cdd:cd20614  218 --LAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA--GDVPRTPAELRRFPLAEALFRETLRLHPPVPF-VFRRVLEE 292
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 385 CQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLefKGNDYELLPFGAGRRICIGMPLA 453
Cdd:cd20614  293 IELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDR--APNPVELLQFGGGPHFCLGYHVA 359
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
302-471 4.16e-21

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: 95.39  E-value: 4.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 302 LMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKD------KMMEEshipdVPFLQAIVKEVLRLHPAAPl 375
Cdd:cd11082  225 LLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDeppltlDLLEE-----MKYTRQVVKEVLRYRPPAP- 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 376 LIPRLCDSDCQI-DGHIIEKNTEVLVNVWAIGRDPkvWSDPLKFDPSRFVGTNLE---FKGNdyeLLPFGAGRRICIGMP 451
Cdd:cd11082  299 MVPHIAKKDFPLtEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQEdrkYKKN---FLVFGAGPHQCVGQE 373
                        170       180
                 ....*....|....*....|
gi 586644824 452 LASSMVHLVLGSLLHYFNWK 471
Cdd:cd11082  374 YAINHLMLFLALFSTLVDWK 393
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
59-465 5.42e-21

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: 95.17  E-value: 5.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  59 TYGPIMPFKLGMRKAVVISSPHPAKQIfkthdrkfsSRPVPLAAKTLSYGGNSL-------VWAAYGHHWRLLRRLSFTE 131
Cdd:cd20640   10 QYGPIFTYSTGNKQFLYVSRPEMVKEI---------NLCVSLDLGKPSYLKKTLkplfgggILTSNGPHWAHQRKIIAPE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 132 LFstkrlnsMEKFRK-----AEVSKTMASIYEESIKGNSVNIGSTVFSTMLGIVENMV----CGNYVFKKGDELATelkg 202
Cdd:cd20640   81 FF-------LDKVKGmvdlmVDSAQPLLSSWEERIDRAGGMAADIVVDEDLRAFSADVisraCFGSSYSKGKEIFS---- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 203 MVRDVLKLSGEPNASDFFPFLRGLDLQGvERRAQKLRERFDGIFSEMIErrlkdmrekgmvnERDEEsgrGIKESDFLGV 282
Cdd:cd20640  150 KLRELQKAVSKQSVLFSIPGLRHLPTKS-NRKIWELEGEIRSLILEIVK-------------EREEE---CDHEKDLLQA 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 283 LLElmdhneGLQMEHVKGMLMDMFI---------AGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEEShI 353
Cdd:cd20640  213 ILE------GARSSCDKKAEAEDFIvdnckniyfAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPPDADS-L 285
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 354 PDVPFLQAIVKEVLRLHPAAPLlIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLEFKG 432
Cdd:cd20640  286 SRMKTVTMVIQETLRLYPPAAF-VSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACK 364
                        410       420       430
                 ....*....|....*....|....*....|....
gi 586644824 433 NDYELLPFGAGRRICIGMPLAssMVHL-VLGSLL 465
Cdd:cd20640  365 PPHSYMPFGAGARTCLGQNFA--MAELkVLVSLI 396
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
222-473 7.18e-21

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: 94.08  E-value: 7.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 222 FLRGLDlQGVERRAQKLR--ERFDGIFSEMIERRLKDMREkgmvnerdeesgrgikesDFLGVLLELMDHNEGLQMEHVK 299
Cdd:cd11080  135 FITSLS-QDPEARAHGLRcaEQLSQYLLPVIEERRVNPGS------------------DLISILCTAEYEGEALSDEDIK 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 300 GMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDelrrvigkdkmmeeshipDVPFLQAIVKEVLRLHPaaPL-LIP 378
Cdd:cd11080  196 ALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRA------------------DRSLVPRAIAETLRYHP--PVqLIP 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 379 RLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRF-VGTNLEFKGNdYELLPFGAGRRICIGMPLASSMV 457
Cdd:cd11080  256 RQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREdLGIRSAFSGA-ADHLAFGSGRHFCVGAALAKREI 334
                        250
                 ....*....|....*..
gi 586644824 458 HLVLGSLLHYF-NWKVE 473
Cdd:cd11080  335 EIVANQVLDALpNIRLE 351
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
250-450 1.05e-20

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: 94.27  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 250 IERRLKDMReKGMVNERDEESGRGI-KESDFLGVLLElMDHNE---------GLQMEHVKGMLMDMFIAGTDTTSATVEW 319
Cdd:cd20642  179 IEKEIRSSL-RGIINKREKAMKAGEaTNDDLLGILLE-SNHKEikeqgnkngGMSTEDVIEECKLFYFAGQETTSVLLVW 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 320 AMAELLNHPYVMEEARDELRRVIGKDKMMEE--SHIPDVPFlqaIVKEVLRLHPAAPLLIpRLCDSDCQIDGHIIEKNTE 397
Cdd:cd20642  257 TMVLLSQHPDWQERAREEVLQVFGNNKPDFEglNHLKVVTM---ILYEVLRLYPPVIQLT-RAIHKDTKLGDLTLPAGVQ 332
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 586644824 398 VLVNVWAIGRDPKVWSDPLK-FDPSRFVGTNLEFKGNDYELLPFGAGRRICIGM 450
Cdd:cd20642  333 VSLPILLVHRDPELWGDDAKeFNPERFAEGISKATKGQVSYFPFGWGPRICIGQ 386
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
249-468 2.22e-20

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: 92.87  E-value: 2.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 249 MIERRLKDMRE---------KGMVNERDEESGrgikESDFLGVLLELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEW 319
Cdd:cd20630  150 LDPEELETAAPdvteglaliEEVIAERRQAPV----EDDLLTTLLRAEEDGERLSEDELMALVAALIVAGTDTTVHLITF 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 320 AMAELLNHPYVMEEARDElrrvigkdkmmeeshiPDVpfLQAIVKEVLRLHPAAPLLIPRLCDSDCQIDGHIIEKNTEVL 399
Cdd:cd20630  226 AVYNLLKHPEALRKVKAE----------------PEL--LRNALEEVLRWDNFGKMGTARYATEDVELCGVTIRKGQMVL 287
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 400 VNVWAIGRDPKVWSDPLKFDPSRfvgtnlEFKGNdyelLPFGAGRRICIGMPLASSMVHLVLGSLLHYF 468
Cdd:cd20630  288 LLLPSALRDEKVFSDPDRFDVRR------DPNAN----IAFGYGPHFCIGAALARLELELAVSTLLRRF 346
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
216-468 5.31e-20

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: 91.46  E-value: 5.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 216 ASDFFPFLRGLDLQGVERRAQKLRERFDGIFSEMIERRLKDMREkgmvnerdeesgrgikesDFLGVLLELMDHNEGLQM 295
Cdd:cd20625  138 SAALARALDPGPLLEELARANAAAAELAAYFRDLIARRRADPGD------------------DLISALVAAEEDGDRLSE 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 296 EHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPyvmeEARDELRRvigkdkmmEESHIPDVpflqaiVKEVLRLHPAApL 375
Cdd:cd20625  200 DELVANCILLLVAGHETTVNLIGNGLLALLRHP----EQLALLRA--------DPELIPAA------VEELLRYDSPV-Q 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 376 LIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefKGNDYelLPFGAGRRICIGMPLASS 455
Cdd:cd20625  261 LTARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITR--------APNRH--LAFGAGIHFCLGAPLARL 330
                        250
                 ....*....|...
gi 586644824 456 MVHLVLGSLLHYF 468
Cdd:cd20625  331 EAEIALRALLRRF 343
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
60-491 6.75e-20

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: 92.13  E-value: 6.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  60 YGPIMPFKLGMRKAVVISSPHPAKQIFkTHDRKFSSRPVPLAAkTLSYGGNSLVWAAyGHHWRLLRRLsFTELFSTKRLN 139
Cdd:cd20641   11 YGETFLYWQGTTPRICISDHELAKQVL-SDKFGFFGKSKARPE-ILKLSGKGLVFVN-GDDWVRHRRV-LNPAFSMDKLK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 140 SMekfrkaevSKTMASIYEESIKG------NSVNIGSTV-FSTMLGIVENMVCGNYVFKKGDELATELKGMVRDVLKLSG 212
Cdd:cd20641   87 SM--------TQVMADCTERMFQEwrkqrnNSETERIEVeVSREFQDLTADIIATTAFGSSYAEGIEVFLSQLELQKCAA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 213 EPNASDFFPFLRGLDLQGvERRAQKLRERFDGIFSEMIERRLKDmrekgmvnerdEESGRGikeSDFLGVLLELMDHNEG 292
Cdd:cd20641  159 ASLTNLYIPGTQYLPTPR-NLRVWKLEKKVRNSIKRIIDSRLTS-----------EGKGYG---DDLLGLMLEAASSNEG 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 293 LQMEHVKgMLMD--------MFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDVPFLQAIVK 364
Cdd:cd20641  224 GRRTERK-MSIDeiidecktFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLM 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 365 EVLRLHPAAPlLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLEFKGNDYELLPFGAG 443
Cdd:cd20641  303 ETLRLYGPVI-NIARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHPNALLSFSLG 381
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 586644824 444 RRICIGMPLASSMVHLVLGSLLHYFNWKVEGEVDMTEEFGITLQ--KALP 491
Cdd:cd20641  382 PRACIGQNFAMIEAKTVLAMILQRFSFSLSPEYVHAPADHLTLQpqYGLP 431
PLN02302 PLN02302
ent-kaurenoic acid oxidase
234-471 1.87e-19

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 90.93  E-value: 1.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 234 RAQKLRERFDGIFsemierrlkdmreKGMVNER--DEESGRGIKESDFLGVLLELMDHN-EGLQMEHVKGMLMDMFIAGT 310
Cdd:PLN02302 234 RALKARKKLVALF-------------QSIVDERrnSRKQNISPRKKDMLDLLLDAEDENgRKLDDEEIIDLLLMYLNAGH 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 311 DTTSATVEWAMAELLNHPYVMEEARDELRRVIGK----DKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIpRLCDSDCQ 386
Cdd:PLN02302 301 ESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKKrppgQKGLTLKDVRKMEYLSQVIDETLRLINISLTVF-REAKTDVE 379
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 387 IDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGtnleFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLH 466
Cdd:PLN02302 380 VNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDN----YTPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLL 455

                 ....*
gi 586644824 467 YFNWK 471
Cdd:PLN02302 456 GYRLE 460
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
205-484 2.97e-19

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: 88.90  E-value: 2.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 205 RDVLKLSGEPNaSDFFPflrglDLQGVERRAQKLRERFDGIfsemIERRLKDMREkgmvnerdeesgrgikesDFLGVLL 284
Cdd:cd20629  128 RLALAMLRGLS-DPPDP-----DVPAAEAAAAELYDYVLPL----IAERRRAPGD------------------DLISRLL 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 285 ELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEardeLRRvigkdkmmEESHIPdvpflqAIVK 364
Cdd:cd20629  180 RAEVEGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLER----VRR--------DRSLIP------AAIE 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 365 EVLRLHPAApLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefkgNDYELLPFGAGR 444
Cdd:cd20629  242 EGLRWEPPV-ASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR----------KPKPHLVFGGGA 310
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 586644824 445 RICIGMPLASSMVHLVLGSLLHYF-NWKVEGEVDMTEEFGI 484
Cdd:cd20629  311 HRCLGEHLARVELREALNALLDRLpNLRLDPDAPAPEISGG 351
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
233-453 3.13e-19

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: 90.44  E-value: 3.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 233 RRAQKLRERFdgifseMIERRLKDMREKgmvnERDEESGRgIKESDFLGVLLELMDH-NEGLQMEHVKGMLMD-MF---I 307
Cdd:cd20622  204 RRAAKIKDDF------LQREIQAIARSL----ERKGDEGE-VRSAVDHMVRRELAAAeKEGRKPDYYSQVIHDeLFgylI 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 308 AGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKmmEESHIP--------DVPFLQAIVKEVLRLHPAAPLLIpR 379
Cdd:cd20622  273 AGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEAV--AEGRLPtaqeiaqaRIPYLDAVIEEILRCANTAPILS-R 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 380 LCDSDCQIDGHIIEKNTEVLVNVW---------------------AIGRDPKVWS--DPLKFDPSRFVGT-----NLEFK 431
Cdd:cd20622  350 EATVDTQVLGYSIPKGTNVFLLNNgpsylsppieidesrrssssaAKGKKAGVWDskDIADFDPERWLVTdeetgETVFD 429
                        250       260
                 ....*....|....*....|..
gi 586644824 432 GNDYELLPFGAGRRICIGMPLA 453
Cdd:cd20622  430 PSAGPTLAFGLGPRGCFGRRLA 451
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
305-498 5.12e-19

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: 88.85  E-value: 5.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 305 MFI-AGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKD------KMMEESH-IPDVPFLQAIVKEVLRLHPAA--- 373
Cdd:cd11051  192 TFLfAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDpsaaaeLLREGPElLNQLPYTTAVIKETLRLFPPAgta 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 374 -------PLLIP---RLCDSDCqidghiiekntEVLVNVWAIGRDPKVWSDPLKFDPSRFV---GTNLEFKGNDYelLPF 440
Cdd:cd11051  272 rrgppgvGLTDRdgkEYPTDGC-----------IVYVCHHAIHRDPEYWPRPDEFIPERWLvdeGHELYPPKSAW--RPF 338
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 441 GAGRRICIGMPLASSMVHLVLGSLLHYFNW-KVEGEVDMTEEFGITLQKALPLVVVATP 498
Cdd:cd11051  339 ERGPRNCIGQELAMLELKIILAMTVRRFDFeKAYDEWDAKGGYKGLKELFVTGQGTAHP 397
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
305-482 6.55e-19

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: 88.88  E-value: 6.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 305 MFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDV-PFLQAIVKEVLRLHPAAPLLIPRLCDS 383
Cdd:cd20615  223 MLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPMEDYILSTdTLLAYCVLESLRLRPLLAFSVPESSPT 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 384 DCQIDGHIIEKNTEVLVNVWAIG-RDPKVWSDPLKFDPSRFvgtnLEFKGND--YELLPFGAGRRICIGMPLASSMVHLV 460
Cdd:cd20615  303 DKIIGGYRIPANTPVVVDTYALNiNNPFWGPDGEAYRPERF----LGISPTDlrYNFWRFGFGPRKCLGQHVADVILKAL 378
                        170       180
                 ....*....|....*....|..
gi 586644824 461 LGSLLHYFNWKVEGEVDMTEEF 482
Cdd:cd20615  379 LAHLLEQYELKLPDQGENEEDT 400
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
262-494 1.48e-18

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 88.11  E-value: 1.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 262 MVNERDEESGRGI-KESDFLGVLLelmDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVM---EEARDE 337
Cdd:PLN02987 234 VVMKRRKEEEEGAeKKKDMLAALL---ASDDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALaqlKEEHEK 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 338 LRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLhpaAPLL--IPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDP 415
Cdd:PLN02987 311 IRAMKSDSYSLEWSDYKSMPFTQCVVNETLRV---ANIIggIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDA 387
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 416 LKFDPSRFvGTNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWkVEGEVDMTEEFGIT-LQKALPLVV 494
Cdd:PLN02987 388 RTFNPWRW-QSNSGTTVPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSW-VPAEQDKLVFFPTTrTQKRYPINV 465
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
260-461 1.82e-18

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: 87.55  E-value: 1.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 260 KGMVNERDEESGRGiKESDFLGVLLelmdHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELR 339
Cdd:cd20645  194 KHCIDKRLQRYSQG-PANDFLCDIY----HDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQ 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 340 RVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPlLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFD 419
Cdd:cd20645  269 SVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVP-FTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFK 347
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 586644824 420 PSRFVGTnlEFKGNDYELLPFGAGRRICIGMPLASSMVHLVL 461
Cdd:cd20645  348 PERWLQE--KHSINPFAHVPFGIGKRMCIGRRLAELQLQLAL 387
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
216-453 5.73e-18

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: 85.34  E-value: 5.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 216 ASDF---FP---FLRGLDLQgVERRAQkLRERFDGIF-SEMIERRLKDMRE-----KGMVNERDEESGrgikeSDFLGVL 283
Cdd:cd11035  104 VADFaepFPtrvFLELMGLP-LEDLDR-FLEWEDAMLrPDDAEERAAAAQAvldylTPLIAERRANPG-----DDLISAI 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 284 LELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPyvmeEARDELRRvigkdkmmEESHIPDVpflqaiV 363
Cdd:cd11035  177 LNAEIDGRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHP----EDRRRLRE--------DPELIPAA------V 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 364 KEVLRLHPaaPLLIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefKGNDYelLPFGAG 443
Cdd:cd11035  239 EELLRRYP--LVNVARIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR--------KPNRH--LAFGAG 306
                        250
                 ....*....|
gi 586644824 444 RRICIGMPLA 453
Cdd:cd11035  307 PHRCLGSHLA 316
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
25-474 2.96e-16

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 81.14  E-value: 2.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824  25 SAKAQAPSPPK---WPIIGH-LHLLGKLPHQSLAALSLTYGPIMPFKLGMRKAVVISSPHPAKQIFKTHDRKFssRPVPL 100
Cdd:PLN02196  29 SSSTKLPLPPGtmgWPYVGEtFQLYSQDPNVFFASKQKRYGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLF--KPTFP 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 101 AAKTLSYGGNSLVWAAYGHHWRLlRRLSFtELFSTKRLNSMekfrkaeVSKtMASIYEESIK---GNSVNigstVFSTML 177
Cdd:PLN02196 107 ASKERMLGKQAIFFHQGDYHAKL-RKLVL-RAFMPDAIRNM-------VPD-IESIAQESLNsweGTQIN----TYQEMK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 178 GIVENMVCGNyVFKKgDELatelkgMVRDVLKLSgepnasdFFPFLRG-----LDLQG-VERRAQKLRERFDGIFSEMIE 251
Cdd:PLN02196 173 TYTFNVALLS-IFGK-DEV------LYREDLKRC-------YYILEKGynsmpINLPGtLFHKSMKARKELAQILAKILS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 252 RRLKDmrekgmvnerdeesgrGIKESDFLGvllELMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVM 331
Cdd:PLN02196 238 KRRQN----------------GSSHNDLLG---SFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVL 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 332 EEARDElRRVIGKDKMMEES----HIPDVPFLQAIVKEVLRlhpAAPLL--IPRLCDSDCQIDGHIIEKNTEVLVNVWAI 405
Cdd:PLN02196 299 EAVTEE-QMAIRKDKEEGESltweDTKKMPLTSRVIQETLR---VASILsfTFREAVEDVEYEGYLIPKGWKVLPLFRNI 374
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 406 GRDPKVWSDPLKFDPSRFvgtNLEFKGNDYelLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEG 474
Cdd:PLN02196 375 HHSADIFSDPGKFDPSRF---EVAPKPNTF--MPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIVG 438
PLN02774 PLN02774
brassinosteroid-6-oxidase
217-475 4.41e-16

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 80.59  E-value: 4.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 217 SDFFPFLRG-----LDLQGVE-RRAQKLRERFDGIFSEMIERRlkdmREKGMVnerdeesgrgikESDFLGVLLELMDHN 290
Cdd:PLN02774 194 TEFFKLVLGtlslpIDLPGTNyRSGVQARKNIVRMLRQLIQER----RASGET------------HTDMLGYLMRKEGNR 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 291 EGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDE---LRRVIGKDKMMEESHIPDVPFLQAIVKEVL 367
Cdd:PLN02774 258 YKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEhlaIRERKRPEDPIDWNDYKSMRFTRAVIFETS 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 368 RLHPAAPLLIpRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEfkgNDYELLPFGAGRRIC 447
Cdd:PLN02774 338 RLATIVNGVL-RKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKSLE---SHNYFFLFGGGTRLC 413
                        250       260       270
                 ....*....|....*....|....*....|..
gi 586644824 448 IGMPLASSMVhlvlGSLLHYF----NWKVEGE 475
Cdd:PLN02774 414 PGKELGIVEI----STFLHYFvtryRWEEVGG 441
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
276-468 5.85e-16

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: 79.71  E-value: 5.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 276 ESDFLGVLLELMDHNEgLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGkDKMMEESHIPD 355
Cdd:cd20616  204 HMDFATELIFAQKRGE-LTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQK 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 356 VPFLQAIVKEVLRLHPAAPLLIPRLCDSDcQIDGHIIEKNTEVLVNVWAIGRDPkVWSDPLKFD--------PSRFvgtn 427
Cdd:cd20616  282 LKVLENFINESMRYQPVVDFVMRKALEDD-VIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTlenfeknvPSRY---- 355
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 586644824 428 lefkgndyeLLPFGAGRRICIGMPLASSMVHLVLGSLLHYF 468
Cdd:cd20616  356 ---------FQPFGFGPRSCVGKYIAMVMMKAILVTLLRRF 387
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
249-474 2.30e-15

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 78.67  E-value: 2.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 249 MIERRLKDMREKgmvnerdEESGRGIKeSDFLGVLLEL-MDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNH 327
Cdd:PLN03195 251 VIRRRKAEMDEA-------RKSGKKVK-HDILSRFIELgEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMN 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 328 PYVMEEARDELR--------------------RVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLIPRLCDSDCQI 387
Cdd:PLN03195 323 PHVAEKLYSELKalekerakeedpedsqsfnqRVTQFAGLLTYDSLGKLQYLHAVITETLRLYPAVPQDPKGILEDDVLP 402
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 388 DGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLH 466
Cdd:PLN03195 403 DGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKDGVFQNASPFKFTAFQAGPRICLGKDSAYLQMKMALALLCR 482

                 ....*....
gi 586644824 467 YFNWK-VEG 474
Cdd:PLN03195 483 FFKFQlVPG 491
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
253-453 2.46e-15

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: 77.97  E-value: 2.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 253 RLKDMREKGMVNERDE--ESGRGIKESDFLGVLLE-LMDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPY 329
Cdd:cd20637  179 RARDSLQKSLEKAIREklQGTQGKDYADALDILIEsAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 330 VMEEARDELRR--VIGKDKMMEES----HIPDVPFLQAIVKEVLRLHPaaplliP-----RLCDSDCQIDGHIIEKNTEV 398
Cdd:cd20637  259 VLEKLREELRSngILHNGCLCEGTlrldTISSLKYLDCVIKEVLRLFT------PvsggyRTALQTFELDGFQIPKGWSV 332
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 586644824 399 LVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGMPLA 453
Cdd:cd20637  333 LYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGRFHYLPFGGGVRTCLGKQLA 387
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
239-468 4.55e-15

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: 76.84  E-value: 4.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 239 RERF----DGIFS------EMIERRLKDMRE--KGMVNERDEESGrgikeSDFLGVLLELMDHNEGLQMEHVKGMLMDMF 306
Cdd:cd11031  141 RERFrawsDALLStsaltpEEAEAARQELRGymAELVAARRAEPG-----DDLLSALVAARDDDDRLSEEELVTLAVGLL 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 307 IAGTDTTSATVEWAMAELLNHPyvmeEARDELRRvigkdkmmEESHIPDVpflqaiVKEVLRLHPAAPL-LIPRLCDSDC 385
Cdd:cd11031  216 VAGHETTASQIGNGVLLLLRHP----EQLARLRA--------DPELVPAA------VEELLRYIPLGAGgGFPRYATEDV 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 386 QIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefkgndyELLP---FGAGRRICIGMPLASSMVHLVLG 462
Cdd:cd11031  278 ELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDR-------------EPNPhlaFGHGPHHCLGAPLARLELQVALG 344

                 ....*.
gi 586644824 463 SLLHYF 468
Cdd:cd11031  345 ALLRRL 350
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
298-472 9.27e-15

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 76.58  E-value: 9.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 298 VKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELrrvigkDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLLI 377
Cdd:PLN02169 302 IRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEI------NTKFDNEDLEKLVYLHAALSESMRLYPPLPFNH 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 378 PRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLEFKGN-DYELLPFGAGRRICIGMPLASS 455
Cdd:PLN02169 376 KAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGLRHEpSYKFMAFNSGPRTCLGKHLALL 455
                        170
                 ....*....|....*..
gi 586644824 456 MVHLVLGSLLHYFNWKV 472
Cdd:PLN02169 456 QMKIVALEIIKNYDFKV 472
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
227-453 9.13e-14

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: 72.95  E-value: 9.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 227 DLQGV-ERRAQKLRERFDGIFS-----EMIERRLKDMRE--KGMVNERDEESGrgikeSDFLGVLLELMDHNEGLQMEHV 298
Cdd:cd11029  138 ELLGVpEEDRDRFRRWSDALVDtdpppEEAAAALRELVDylAELVARKRAEPG-----DDLLSALVAARDEGDRLSEEEL 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 299 KGMLMDMFIAGTDTTSATVEWAMAELLNHPyvmeEARDELRRvigkdkmmEESHIPDVpflqaiVKEVLRLHPAAPLLIP 378
Cdd:cd11029  213 VSTVFLLLVAGHETTVNLIGNGVLALLTHP----DQLALLRA--------DPELWPAA------VEELLRYDGPVALATL 274
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586644824 379 RLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefkgNDYELLPFGAGRRICIGMPLA 453
Cdd:cd11029  275 RFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR----------DANGHLAFGHGIHYCLGAPLA 339
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
227-468 2.24e-13

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: 71.40  E-value: 2.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 227 DLQGVERRAQKLRERfdgifSEMIERRLKDMRE-----KGMVNERDEESGRgikesDFLGVLLELMDHNEGLQMEHVKGM 301
Cdd:cd11030  143 DREFFQRRSARLLDL-----SSTAEEAAAAGAElraylDELVARKRREPGD-----DLLSRLVAEHGAPGELTDEELVGI 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 302 LMDMFIAGTDTTSATVEWAMAELLNHPyvmeEARDELRRvigkdkmmEESHIPDVpflqaiVKEVLRLHPAAPLLIPRLC 381
Cdd:cd11030  213 AVLLLVAGHETTANMIALGTLALLEHP----EQLAALRA--------DPSLVPGA------VEELLRYLSIVQDGLPRVA 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 382 DSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefKGNDYelLPFGAGRRICIGMPLASSMVHLVL 461
Cdd:cd11030  275 TEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR--------PARRH--LAFGHGVHQCLGQNLARLELEIAL 344

                 ....*..
gi 586644824 462 GSLLHYF 468
Cdd:cd11030  345 PTLFRRF 351
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
222-475 2.44e-13

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


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 71.48  E-value: 2.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 222 FLRGLDLQGVERRAQKLRerFDGIFSEMIERRLKDMREKGMVNERDEESGRGikesdflgvllelmdhnEGLQMEHVKGM 301
Cdd:cd11078  153 WGRPSEEEQVEAAAAVGE--LWAYFADLVAERRREPRDDLISDLLAAADGDG-----------------ERLTDEELVAF 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 302 LMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRvigkdkmmeeshIPDvpflqaIVKEVLRLHPAAPLLiPRLC 381
Cdd:cd11078  214 LFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRADPSL------------IPN------AVEETLRYDSPVQGL-RRTA 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 382 DSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefkGNDYELLPFGAGRRICIGMPLASSMVHLVL 461
Cdd:cd11078  275 TRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR---------PNARKHLTFGHGIHFCLGAALARMEARIAL 345
                        250
                 ....*....|....*
gi 586644824 462 GSLLHYF-NWKVEGE 475
Cdd:cd11078  346 EELLRRLpGMRVPGQ 360
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
251-494 2.55e-13

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 72.03  E-value: 2.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 251 ERRLKDMrekgmVNERDEESGRGIKESDFLGVllelMDHNEGLQ--MEHVKG--MLMDMFI----AGTDTTSATVEWAMA 322
Cdd:PLN02426 248 ERKLKEA-----IKLVDELAAEVIRQRRKLGF----SASKDLLSrfMASINDdkYLRDIVVsfllAGRDTVASALTSFFW 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 323 ELLNHPYVMEEARDELRRVIGKDKMMEES-HIPDVPFLQAIVKEVLRLHPaaplliPRLCDS------DCQIDGHIIEKN 395
Cdd:PLN02426 319 LLSKHPEVASAIREEADRVMGPNQEAASFeEMKEMHYLHAALYESMRLFP------PVQFDSkfaaedDVLPDGTFVAKG 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 396 TEVLVNVWAIGRDPKVW-SDPLKFDPSRFVGTNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVEG 474
Cdd:PLN02426 393 TRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGVFVPENPFKYPVFQAGLRVCLGKEMALMEMKSVAVAVVRRFDIEVVG 472
                        250       260
                 ....*....|....*....|....
gi 586644824 475 EVDMTEEF--GIT--LQKALPLVV 494
Cdd:PLN02426 473 RSNRAPRFapGLTatVRGGLPVRV 496
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
239-492 3.10e-12

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: 68.01  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 239 RERFDGIFSEMIERRLKDMRE--KGMVNERDEESGrgikeSDFLGVLLELMDHNEGLQMEHVKGMLMDMFIAGTDTTSAT 316
Cdd:cd11032  143 DDSFEEEEVEEMAEALRELNAylLEHLEERRRNPR-----DDLISRLVEAEVDGERLTDEEIVGFAILLLIAGHETTTNL 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 317 VEWAMAELLNHPyvmeEARDELRrvigkdkmMEESHIPDVpflqaiVKEVLRLHPAAPLlIPRLCDSDCQIDGHIIEKNt 396
Cdd:cd11032  218 LGNAVLCLDEDP----EVAARLR--------ADPSLIPGA------IEEVLRYRPPVQR-TARVTTEDVELGGVTIPAG- 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 397 eVLVNVW--AIGRDPKVWSDPLKFDPSRfvgtnlefKGNDYelLPFGAGRRICIGMPLASSMVHLVLGSLL-HYFNWKV- 472
Cdd:cd11032  278 -QLVIAWlaSANRDERQFEDPDTFDIDR--------NPNPH--LSFGHGIHFCLGAPLARLEARIALEALLdRFPRIRVd 346
                        250       260
                 ....*....|....*....|.
gi 586644824 473 -EGEVDMTEEFGITLQKALPL 492
Cdd:cd11032  347 pDVPLELIDSPVVFGVRSLPV 367
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
306-466 3.15e-12

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: 67.90  E-value: 3.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 306 FIAGTDTTSATVEWAMAELLNHPyvmeEARDELRrvigkdkmmeeshiPDVPFLQAIVKEVLRLhpAAPL-LIPRLCDSD 384
Cdd:cd11036  186 AVQGAEAAAGLVGNAVLALLRRP----AQWARLR--------------PDPELAAAAVAETLRY--DPPVrLERRFAAED 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 385 CQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefkgNDYELLPFGAGRRICIGMPLASSMVHLVLGSL 464
Cdd:cd11036  246 LELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR----------PTARSAHFGLGRHACLGAALARAAAAAALRAL 315

                 ..
gi 586644824 465 LH 466
Cdd:cd11036  316 AA 317
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
242-472 3.91e-12

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: 67.92  E-value: 3.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 242 FDGIFSEMIERRL------KDMREKgMVNERDEEsgrgiKESDFLGVLLELMDHN-EGLQMEHVKGMLMDMFIAGTDTTS 314
Cdd:cd20638  174 FSGLYRGLRARNLihakieENIRAK-IQREDTEQ-----QCKDALQLLIEHSRRNgEPLNLQALKESATELLFGGHETTA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 315 ATVEWAMAELLNHPYVMEEARDELR-RVIGKDKMMEESHIpDVPFLQ------AIVKEVLRLHPAAPLLIpRLCDSDCQI 387
Cdd:cd20638  248 SAATSLIMFLGLHPEVLQKVRKELQeKGLLSTKPNENKEL-SMEVLEqlkytgCVIKETLRLSPPVPGGF-RVALKTFEL 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 388 DGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEfKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHY 467
Cdd:cd20638  326 NGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPE-DSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELARH 404

                 ....*
gi 586644824 468 FNWKV 472
Cdd:cd20638  405 CDWQL 409
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
252-473 4.02e-12

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 68.23  E-value: 4.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 252 RRLKDMREKGMVNERDEESGRgikESDFLGVLLElmDHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYV- 330
Cdd:PLN03141 211 KKIIEEKRRAMKNKEEDETGI---PKDVVDVLLR--DGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVAl 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 331 --MEEARDELRRviGKDKMMEESHIPD---VPFLQAIVKEVLRLhpaAPLLIP--RLCDSDCQIDGHIIEKNTEVLVNVW 403
Cdd:PLN03141 286 qqLTEENMKLKR--LKADTGEPLYWTDymsLPFTQNVITETLRM---GNIINGvmRKAMKDVEIKGYLIPKGWCVLAYFR 360
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 404 AIGRDPKVWSDPLKFDPSRFVGTNLefkgNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVE 473
Cdd:PLN03141 361 SVHLDEENYDNPYQFNPWRWQEKDM----NNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFRWVAE 426
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
317-443 4.51e-12

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


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 67.55  E-value: 4.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 317 VEWAMAELLNHPyvmeEARDELRRvigkdkmmeeshiPDVPFLQAIVKEVLRLHPAAPLLIPRLCDsDCQIDGHIIEKNT 396
Cdd:cd11067  240 VTFAALALHEHP----EWRERLRS-------------GDEDYAEAFVQEVRRFYPFFPFVGARARR-DFEWQGYRFPKGQ 301
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 586644824 397 EVLVNVWAIGRDPKVWSDPLKFDPSRFvgtnLEFKGNDYELLPFGAG 443
Cdd:cd11067  302 RVLLDLYGTNHDPRLWEDPDRFRPERF----LGWEGDPFDFIPQGGG 344
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
288-472 6.96e-12

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: 67.17  E-value: 6.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 288 DHNEGLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELrrvIGKDKMMEESHIPD---------VPF 358
Cdd:cd20636  218 ENGKELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQEL---VSHGLIDQCQCCPGalsleklsrLRY 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 359 LQAIVKEVLRLHPaaplliP-----RLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEFKGN 433
Cdd:cd20636  295 LDCVVKEVLRLLP------PvsggyRTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSG 368
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 586644824 434 DYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKV 472
Cdd:cd20636  369 RFNYIPFGGGVRSCIGKELAQVILKTLAVELVTTARWEL 407
PLN02500 PLN02500
cytochrome P450 90B1
195-494 8.77e-12

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 67.20  E-value: 8.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 195 ELATELKGMVRDVLKLSGEPnasdffpflrgldlqgvERRAQKLRERFDGIFSEMIERRLKDMREKGMVNERDEESGRGI 274
Cdd:PLN02500 208 EYVTFMKGVVSAPLNFPGTA-----------------YRKALKSRATILKFIERKMEERIEKLKEEDESVEEDDLLGWVL 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 275 KESDflgvllelmdhnegLQMEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHI- 353
Cdd:PLN02500 271 KHSN--------------LSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIARAKKQSGESELn 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 354 ----PDVPFLQAIVKEVLRLHPAAPLLiPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFV----- 424
Cdd:PLN02500 337 wedyKKMEFTQCVINETLRLGNVVRFL-HRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQqnnnr 415
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586644824 425 -GTNLEFKGNDYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWKVegeVDMTEEFG---ITLQKALPLVV 494
Cdd:PLN02500 416 gGSSGSSSATTNNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWEL---AEADQAFAfpfVDFPKGLPIRV 486
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
232-465 1.72e-11

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: 65.82  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 232 ERRAQKLRERFDGIFSEMIERRlkdmrekgmVNERDeesgrgikesDFLGVLLELMDHNEGLQMEHVKGMLMDMFIAGTD 311
Cdd:cd11034  144 EEGAAAFAELFGHLRDLIAERR---------ANPRD----------DLISRLIEGEIDGKPLSDGEVIGFLTLLLLGGTD 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 312 TTSATVEWAMAELLNHPyvmeEARDELRRvigkdkmmEESHIPdvpflqAIVKEVLRLhpAAPLL-IPRLCDSDCQIDGH 390
Cdd:cd11034  205 TTSSALSGALLWLAQHP----EDRRRLIA--------DPSLIP------NAVEEFLRF--YSPVAgLARTVTQEVEVGGC 264
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586644824 391 IIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFvgtnlefkGNDYelLPFGAGRRICIGMPLASSMVHLVLGSLL 465
Cdd:cd11034  265 RLKPGDRVLLAFASANRDEEKFEDPDRIDIDRT--------PNRH--LAFGSGVHRCLGSHLARVEARVALTEVL 329
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
319-468 1.37e-10

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


Pssm-ID: 410728  Cd Length: 410  Bit Score: 63.10  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 319 WAMAELLNHPYVMEEARDELRRVIG---KDKM-MEESHIPDVPFLQAIVKEVLRLHpaAPLLIPRLCDSDCQIDGHIIEK 394
Cdd:cd20635  232 WTLAFILSHPSVYKKVMEEISSVLGkagKDKIkISEDDLKKMPYIKRCVLEAIRLR--SPGAITRKVVKPIKIKNYTIPA 309
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586644824 395 NTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLE----FKGndyeLLPFGAGRRICIGMPLASSMVHLVLGSLLHYF 468
Cdd:cd20635  310 GDMLMLSPYWAHRNPKYFPDPELFKPERWKKADLEknvfLEG----FVAFGGGRYQCPGRWFALMEIQMFVAMFLYKY 383
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
268-476 3.18e-10

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: 61.76  E-value: 3.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 268 EESGRGIKESDFLGVLLElMDHNEGLQMEhvKGMLMDMfiAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKM 347
Cdd:cd20627  178 ERKGKNFSQHVFIDSLLQ-GNLSEQQVLE--DSMIFSL--AGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQVLGKGPI 252
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 348 MEEShIPDVPFLQAIVKEVLRLHPAAPLlIPRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFvgtN 427
Cdd:cd20627  253 TLEK-IEQLRYCQQVLCETVRTAKLTPV-SARLQELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRF---D 327
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 586644824 428 LEFKGNDYELLPFgAGRRICIGMPLASSMVHLVLGSLLHYFNW-KVEGEV 476
Cdd:cd20627  328 DESVMKSFSLLGF-SGSQECPELRFAYMVATVLLSVLVRKLRLlPVDGQV 376
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
225-453 1.25e-09

cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus P450 monooxygenase AurH which is uniquely capable of forming a homochiral tetrahydrofuran ring, a vital component of the polyketide antibiotic aureothin. AurH catalyzes an unprecedented tandem oxygenation process: first, it catalyzes an asymmetric hydroxylation of deoxyaureothin to yield (7R)-7-hydroxydeoxyaureothin as an intermediate; and second, it mediates another C-O bond formation that leads to O-heterocyclization. The AurH-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410664 [Multi-domain]  Cd Length: 382  Bit Score: 60.07  E-value: 1.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 225 GLDLQGVERRAQKLRERFDGIFSEMIERRLKDMREkgmvnerdeesgrgikesDFLGVLLELMDHNEGLQMEHVKGMLMD 304
Cdd:cd11038  160 GLEVKDHLPRIEAAVEELYDYADALIEARRAEPGD------------------DLISTLVAAEQDGDRLSDEELRNLIVA 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 305 MFIAGTDTTSATVEWAMAELLNHPyvmeeardELRRVIGKDkmmeeshiPDVPflQAIVKEVLRLHPAAPLLIpRLCDSD 384
Cdd:cd11038  222 LLFAGVDTTRNQLGLAMLTFAEHP--------DQWRALRED--------PELA--PAAVEEVLRWCPTTTWAT-REAVED 282
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 385 CQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPlKFDPSRfvgtnlefKGNDYelLPFGAGRRICIGMPLA 453
Cdd:cd11038  283 VEYNGVTIPAGTVVHLCSHAANRDPRVFDAD-RFDITA--------KRAPH--LGFGGGVHHCLGAFLA 340
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
301-469 1.45e-09

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 60.07  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 301 MLMdMFIAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKDKMMEESHIPDV----------PFLQAIVKEVLRLH 370
Cdd:cd20633  229 MFL-LLWASQGNTGPASFWLLLYLLKHPEAMKAVREEVEQVLKETGQEVKPGGPLInltrdmllktPVLDSAVEETLRLT 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 371 pAAPLLIpRLCDSDCQI---DG--HIIEKNTEVLVNVW-AIGRDPKVWSDPLKFDPSRFV----GTNLEF----KGNDYE 436
Cdd:cd20633  308 -AAPVLI-RAVVQDMTLkmaNGreYALRKGDRLALFPYlAVQMDPEIHPEPHTFKYDRFLnpdgGKKKDFykngKKLKYY 385
                        170       180       190
                 ....*....|....*....|....*....|...
gi 586644824 437 LLPFGAGRRICIGMPLASSMVHLVLGSLLHYFN 469
Cdd:cd20633  386 NMPWGAGVSICPGRFFAVNEMKQFVFLMLTYFD 418
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
229-479 2.66e-09

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: 59.08  E-value: 2.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 229 QGVERRAQKLRERFDgIFSEMIERRLKDMREkgmvnerdeesgrgikesDFLGVLLELMDHNEGLQMEHVKGMLMDMFIA 308
Cdd:cd11033  160 EAEEELAAALAELFA-YFRELAEERRANPGD------------------DLISVLANAEVDGEPLTDEEFASFFILLAVA 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 309 GTDTTSATVEWAMAELLNHPyvmeEARDELRRvigkdkmmEESHIPdvpflqAIVKEVLRLhpAAPLL-IPRLCDSDCQI 387
Cdd:cd11033  221 GNETTRNSISGGVLALAEHP----DQWERLRA--------DPSLLP------TAVEEILRW--ASPVIhFRRTATRDTEL 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 388 DGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefKGNDYelLPFGAGRRICIGMPLASSMVHLVLGSLLHY 467
Cdd:cd11033  281 GGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR--------SPNPH--LAFGGGPHFCLGAHLARLELRVLFEELLDR 350
                        250
                 ....*....|...
gi 586644824 468 F-NWKVEGEVDMT 479
Cdd:cd11033  351 VpDIELAGEPERL 363
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
241-468 6.50e-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: 58.16  E-value: 6.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 241 RFDGIFSEMIE-------RRLKDMREKGMVNERDEESGRGIKESDFLGVLLELMDHNEGL-QMEHVKGMLMDMFIAGTDT 312
Cdd:cd20631  164 EFDKVFPALVAglpihmfKTAKSAREALAERLLHENLQKRENISELISLRMLLNDTLSTLdEMEKARTHVAMLWASQANT 243
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 313 TSATVeWAMAELLNHPYVMEEARDELRRVIGKDKM---MEESHI-------PDVPFLQAIVKEVLRLHPAAPLLIPRLCD 382
Cdd:cd20631  244 LPATF-WSLFYLLRCPEAMKAATKEVKRTLEKTGQkvsDGGNPIvltreqlDDMPVLGSIIKEALRLSSASLNIRVAKED 322
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 383 SDCQIDG---HIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLE----FKGN----DYELLPFGAGRRICIGMP 451
Cdd:cd20631  323 FTLHLDSgesYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKekttFYKNgrklKYYYMPFGSGTSKCPGRF 402
                        250
                 ....*....|....*..
gi 586644824 452 LASSMVHLVLGSLLHYF 468
Cdd:cd20631  403 FAINEIKQFLSLMLCYF 419
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
359-465 8.50e-09

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: 57.37  E-value: 8.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 359 LQAIVKEVLRLHpaAPLLI-PRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefkgNDYEL 437
Cdd:cd11079  227 LPAAIDEILRLD--DPFVAnRRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR----------HAADN 294
                         90       100
                 ....*....|....*....|....*...
gi 586644824 438 LPFGAGRRICIGMPLASSMVHLVLGSLL 465
Cdd:cd11079  295 LVYGRGIHVCPGAPLARLELRILLEELL 322
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
281-464 1.25e-08

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: 56.67  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 281 GVLLELMDhnEGLQMEHVKGMLMDMFIAGTDTTSATVewaMAELLNHpYVMEEARDELRRVIGKDKmmeeshipdvpflQ 360
Cdd:cd20619  175 DSLLDAAR--AGEITESEAIATILVFYAVGHMAIGYL---IASGIEL-FARRPEVFTAFRNDESAR-------------A 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 361 AIVKEVLRLHPAAPLLIpRLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEfkgndyelLPF 440
Cdd:cd20619  236 AIINEMVRMDPPQLSFL-RFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTRPPAASRN--------LSF 306
                        170       180
                 ....*....|....*....|....
gi 586644824 441 GAGRRICIGMPLASSMVHLVLGSL 464
Cdd:cd20619  307 GLGPHSCAGQIISRAEATTVFAVL 330
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
300-465 2.56e-08

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: 55.67  E-value: 2.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 300 GMLMDMFIAGTDTTSATVEWAMAELLNHPyvmeearDELRRVigKDkmmEESHIPdvpflqAIVKEVLRLhpAAPLLI-P 378
Cdd:cd11037  205 LLMRDYLSAGLDTTISAIGNALWLLARHP-------DQWERL--RA---DPSLAP------NAFEEAVRL--ESPVQTfS 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 379 RLCDSDCQIDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFD----PSRFVGtnlefkgndyellpFGAGRRICIGMPLAS 454
Cdd:cd11037  265 RTTTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDitrnPSGHVG--------------FGHGVHACVGQHLAR 330
                        170
                 ....*....|.
gi 586644824 455 SMVHLVLGSLL 465
Cdd:cd11037  331 LEGEALLTALA 341
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
295-462 4.70e-08

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: 55.04  E-value: 4.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 295 MEHVKGMLMDMFIAGTDTTSATVEWAMAELLNHPYvmEEARDELRRVIGKDKMMEEShipdvpfLQAIVKEVLRLHPAAP 374
Cdd:cd20612  185 ADEVRDNVLGTAVGGVPTQSQAFAQILDFYLRRPG--AAHLAEIQALARENDEADAT-------LRGYVLEALRLNPIAP 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 375 LLiPRLCDSDCQID-----GHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSRfvgtnlefKGNDYelLPFGAGRRICIG 449
Cdd:cd20612  256 GL-YRRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR--------PLESY--IHFGHGPHQCLG 324
                        170
                 ....*....|....*..
gi 586644824 450 MPLA----SSMVHLVLG 462
Cdd:cd20612  325 EEIAraalTEMLRVVLR 341
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
307-465 8.71e-08

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: 54.39  E-value: 8.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 307 IAGTDTTSATVEWAMAELLNHPYVMEEARDELRRVIGKdkmmeeshiPDVPFLQAIVKEVLRLHPAAPLLIpRLCDSDCQ 386
Cdd:cd20624  201 LFAFDAAGMALLRALALLAAHPEQAARAREEAAVPPGP---------LARPYLRACVLDAVRLWPTTPAVL-RESTEDTV 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 387 IDGHIIEKNTEVLVNVWAIGRDPKVWSDPLKFDPSrfvgTNLEFKGNDYE-LLPFGAGRRICIGMPLASSMVHLVLGSLL 465
Cdd:cd20624  271 WGGRTVPAGTGFLIFAPFFHRDDEALPFADRFVPE----IWLDGRAQPDEgLVPFSAGPARCPGENLVLLVASTALAALL 346
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
289-471 1.84e-07

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 53.61  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 289 HNEGLQME-HVKGMLMDMFIAGTDTTSATVeWAMAELLNHPYVMEEARDELRRVIGKDKM-------MEESHIPDVPFLQ 360
Cdd:cd20634  213 EEEGVDEEmQARAMLLQLWATQGNAGPAAF-WLLLFLLKHPEAMAAVRGEIQRIKHQRGQpvsqtltINQELLDNTPVFD 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 361 AIVKEVLRLhPAAPlLIPRLCDSD---CQIDG--HIIEKNTEVLVNVW-AIGRDPKVWSDPLKFDPSRFVGTNLEFKGN- 433
Cdd:cd20634  292 SVLSETLRL-TAAP-FITREVLQDmklRLADGqeYNLRRGDRLCLFPFlSPQMDPEIHQEPEVFKYDRFLNADGTEKKDf 369
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 586644824 434 -------DYELLPFGAGRRICIGMPLASSMVHLVLGSLLHYFNWK 471
Cdd:cd20634  370 ykngkrlKYYNMPWGAGDNVCIGRHFAVNSIKQFVFLILTHFDVE 414
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
349-483 6.53e-07

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: 51.64  E-value: 6.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 349 EESHIPDVPFLQAIVKEVLRLHPAAPLlIPRLCDSDcQIDGHIIEKntevlVNVWAIGRDPKVW-SDPLKFDPSRFVGTN 427
Cdd:cd20626  248 AKSATKDGISAKNLVKEALRLYPPTRR-IYRAFQRP-GSSKPEIIA-----ADIEACHRSESIWgPDALEFNPSRWSKLT 320
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 586644824 428 LEFKGndyELLPFGAGRRICIGMP-LASSMVHLVLGSLLHYF--NWKVEGEVDMTEEFG 483
Cdd:cd20626  321 PTQKE---AFLPFGSGPFRCPAKPvFGPRMIALLVGALLDALgdEWELVSVDGRNVIFG 376
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
331-425 8.94e-07

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: 51.11  E-value: 8.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 331 MEEARDELRRVIGKDKMMEESHIPDVPFLQAIVKEVLRLHPAAPLlIPRLCDSDCQIDGH----IIEKNtEVLVNV--WA 404
Cdd:cd11071  260 HARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPL-QYGRARKDFVIESHdasyKIKKG-ELLVGYqpLA 337
                         90       100
                 ....*....|....*....|.
gi 586644824 405 IgRDPKVWSDPLKFDPSRFVG 425
Cdd:cd11071  338 T-RDPKVFDNPDEFVPDRFMG 357
PLN02648 PLN02648
allene oxide synthase
328-425 3.30e-05

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 46.47  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 328 PYVMEEARDELRRVIGKD------KMMEEshipdVPFLQAIVKEVLRLHPAAPLLIPRlCDSDCQIDGH-----IieKNT 396
Cdd:PLN02648 304 EELQARLAEEVRSAVKAGgggvtfAALEK-----MPLVKSVVYEALRIEPPVPFQYGR-AREDFVIESHdaafeI--KKG 375
                         90       100       110
                 ....*....|....*....|....*....|
gi 586644824 397 EVLVNVWAIG-RDPKVWSDPLKFDPSRFVG 425
Cdd:PLN02648 376 EMLFGYQPLVtRDPKVFDRPEEFVPDRFMG 405
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
319-468 6.07e-05

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: 45.37  E-value: 6.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 319 WAMAELLNHPYVMEEARDELRRVIGK------------------DKMMeeshipdvpFLQAIVKEVLRLHPAAplLIPRL 380
Cdd:cd20632  237 WAMYYLLRHPEALAAVRDEIDHVLQStgqelgpdfdihltreqlDSLV---------YLESAINESLRLSSAS--MNIRV 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 381 CDSDCQI----DGHI-IEKNTEVLVNVWAIGRDPKVWSDP--LKFDpsRFVGTNLE----FKGND---YELLPFGAGRRI 446
Cdd:cd20632  306 VQEDFTLklesDGSVnLRKGDIVALYPQSLHMDPEIYEDPevFKFD--RFVEDGKKkttfYKRGQklkYYLMPFGSGSSK 383
                        170       180
                 ....*....|....*....|..
gi 586644824 447 CIGMPLASSMVHLVLGSLLHYF 468
Cdd:cd20632  384 CPGRFFAVNEIKQFLSLLLLYF 405
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
315-457 2.77e-03

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 40.18  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586644824 315 ATVEWAmaeLLNHPyvmeEARDELRRvigkdkmmeeshiPDVPFLQAIvKEVLRLhpAAPL-LIPRLCDSDCQIDGHIIE 393
Cdd:cd11039  223 AGTCWG---LLSNP----EQLAEVMA-------------GDVHWLRAF-EEGLRW--ISPIgMSPRRVAEDFEIRGVTLP 279
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586644824 394 KNTEVLVNVWAIGRDPKVWSDPLKFDPSRFVGTNLEfkgndyellpFGAGRRICIGMPLASSMV 457
Cdd:cd11039  280 AGDRVFLMFGSANRDEARFENPDRFDVFRPKSPHVS----------FGAGPHFCAGAWASRQMV 333
 
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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