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Conserved domains on  [gi|15241483|ref|NP_196416|]
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Cytochrome P450 superfamily protein [Arabidopsis thaliana]

Protein Classification

cytochrome P450 family protein; cytochrome P450( domain architecture ID 10010864)

cytochrome P450 family protein may catalyze the oxidation of organic species by molecular oxygen, by the oxidative addition of atomic oxygen into an unactivated C-H or C-C bond| 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
PLN02687 PLN02687
flavonoid 3'-monooxygenase
2-511 0e+00

flavonoid 3'-monooxygenase


:

Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 971.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    2 ATLFLTILLATVLFL-ILRIFSHRRNRS--HNNRLPPGPNPWPIIGNLPHMGTKPHRTLSAMVTTYGPILHLRLGFVDVV 78
Cdd:PLN02687   1 MDLPLPLLLGTVAVSvLVWCLLLRRGGSgkHKRPLPPGPRGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   79 VAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEVGTLTR 158
Cdd:PLN02687  81 VAASASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVALLVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  159 ELVR-VGTKPVNLGQLVNMCVVNALGREMIGRRLFGADADHKADEFRSMVTEMMALAGVFNIGDFVPSLDWLDLQGVAGK 237
Cdd:PLN02687 161 ELARqHGTAPVNLGQLVNVCTTNALGRAMVGRRVFAGDGDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLDLQGVVGK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  238 MKRLHKRFDAFLSSILKEHEMNGQD--QKHTDMLSTLISLKGTD-LDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWA 314
Cdd:PLN02687 241 MKRLHRRFDAMMNGIIEEHKAAGQTgsEEHKDLLSTLLALKREQqADGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  315 IAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLT 394
Cdd:PLN02687 321 IAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  395 NIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGV 474
Cdd:PLN02687 401 NVWAIARDPEQWPDPLEFRPDRFLPGGEHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQ 480
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 15241483  475 TPEKLNMEESYGLTLQRAVPLVVHPKPRLAPNVYGLG 511
Cdd:PLN02687 481 TPDKLNMEEAYGLTLQRAVPLMVHPRPRLLPSAYGIE 517
 
Name Accession Description Interval E-value
PLN02687 PLN02687
flavonoid 3'-monooxygenase
2-511 0e+00

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 971.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    2 ATLFLTILLATVLFL-ILRIFSHRRNRS--HNNRLPPGPNPWPIIGNLPHMGTKPHRTLSAMVTTYGPILHLRLGFVDVV 78
Cdd:PLN02687   1 MDLPLPLLLGTVAVSvLVWCLLLRRGGSgkHKRPLPPGPRGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   79 VAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEVGTLTR 158
Cdd:PLN02687  81 VAASASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVALLVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  159 ELVR-VGTKPVNLGQLVNMCVVNALGREMIGRRLFGADADHKADEFRSMVTEMMALAGVFNIGDFVPSLDWLDLQGVAGK 237
Cdd:PLN02687 161 ELARqHGTAPVNLGQLVNVCTTNALGRAMVGRRVFAGDGDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLDLQGVVGK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  238 MKRLHKRFDAFLSSILKEHEMNGQD--QKHTDMLSTLISLKGTD-LDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWA 314
Cdd:PLN02687 241 MKRLHRRFDAMMNGIIEEHKAAGQTgsEEHKDLLSTLLALKREQqADGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  315 IAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLT 394
Cdd:PLN02687 321 IAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  395 NIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGV 474
Cdd:PLN02687 401 NVWAIARDPEQWPDPLEFRPDRFLPGGEHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQ 480
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 15241483  475 TPEKLNMEESYGLTLQRAVPLVVHPKPRLAPNVYGLG 511
Cdd:PLN02687 481 TPDKLNMEEAYGLTLQRAVPLMVHPRPRLLPSAYGIE 517
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
65-502 0e+00

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: 839.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALED 144
Cdd:cd20657   1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMAYNAQDMVFAPYGPRWRLLRKLCNLHLFGGKALED 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 145 FKHVRQEEVGTLTRELVRVGTK--PVNLGQLVNMCVVNALGREMIGRRLFGADADHKADEFRSMVTEMMALAGVFNIGDF 222
Cdd:cd20657  81 WAHVRENEVGHMLKSMAEASRKgePVVLGEMLNVCMANMLGRVMLSKRVFAAKAGAKANEFKEMVVELMTVAGVFNIGDF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 223 VPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLIsLKGTDLDGDGGSLTDTEIKALLLNMFTA 302
Cdd:cd20657 161 IPSLAWMDLQGVEKKMKRLHKRFDALLTKILEEHKATAQERKGKPDFLDFV-LLENDDNGEGERLTDTNIKALLLNLFTA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 303 GTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEIN 382
Cdd:cd20657 240 GTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEACEVD 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 383 GYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGeKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATL 462
Cdd:cd20657 320 GYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGR-NAKVDVRGNDFELIPFGAGRRICAGTRMGIRMVEYILATL 398
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 15241483 463 VQGFDWELAGGVTPEKLNMEESYGLTLQRAVPLVVHPKPR 502
Cdd:cd20657 399 VHSFDWKLPAGQTPEELNMEEAFGLALQKAVPLVAHPTPR 438
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
34-501 7.25e-113

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: 341.95  E-value: 7.25e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    34 PPGPNPWPIIGNLPHMGTK--PHRTLSAMVTTYGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAY 111
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   112 NY--QDLVFApYGHRWRLLRKISSVHLFSAKALEdFKHVRQEEVGTLTRELVRVGTKP--VNLGQLVNMCVVNALGREMI 187
Cdd:pfam00067  81 PFlgKGIVFA-NGPRWRQLRRFLTPTFTSFGKLS-FEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   188 GRRLFGADaDHKADEFRSMVTEMMALAG--VFNIGDFVPSLDWLdLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKH 265
Cdd:pfam00067 159 GERFGSLE-DPKFLELVKAVQELSSLLSspSPQLLDLFPILKYF-PGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   266 TDMLSTLISLKGTDlDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNES 345
Cdd:pfam00067 237 SPRDFLDALLLAKE-EEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   346 DIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSg 425
Cdd:pfam00067 316 DLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKF- 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241483   426 vdvkGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPEKLNMEESygltlqravpLVVHPKP 501
Cdd:pfam00067 395 ----RKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPG----------LLLPPKP 456
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
47-500 2.64e-51

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: 179.70  E-value: 2.64e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  47 PHMGTKPHRTLSAMvTTYGPILHLRLGFVDVVVAASKSVAEQFLKiHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWR 126
Cdd:COG2124  15 PAFLRDPYPFYARL-REYGPVFRVRLPGGGAWLVTRYEDVREVLR-DPRTFSSDGGLPEVLRPLPLLGDSLLTLDGPEHT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 127 LLRKISSvHLFSAKALEDFKHVRQEEVGTLTRELVRVGTkpvnlgqlvnMCVVNALGR---EMIGRRLFGADADHkADEF 203
Cdd:COG2124  93 RLRRLVQ-PAFTPRRVAALRPRIREIADELLDRLAARGP----------VDLVEEFARplpVIVICELLGVPEED-RDRL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 204 RSMVTEMMALAGVFNIGDFvpsldwldlqgvaGKMKRLHKRFDAFLSSILKEHEMNGQDqkhtDMLSTLISLKGtdldgD 283
Cdd:COG2124 161 RRWSDALLDALGPLPPERR-------------RRARRARAELDAYLRELIAERRAEPGD----DLLSALLAARD-----D 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 284 GGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELdivvgrdrpvnesdiaqlPYLQAVIKENFRL 363
Cdd:COG2124 219 GERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRL 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 364 HPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERflpggeksgvdvkgSDFELIPFGAGRR 443
Cdd:COG2124 281 YPPVPL-LPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR--------------PPNAHLPFGGGPH 345
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241483 444 ICAGLSLGLRTIQFLTATLVQGF-DWELAGgvtPEKLNMEESYGLTLQRAVPLVVHPK 500
Cdd:COG2124 346 RCLGAALARLEARIALATLLRRFpDLRLAP---PEELRWRPSLTLRGPKSLPVRLRPR 400
 
Name Accession Description Interval E-value
PLN02687 PLN02687
flavonoid 3'-monooxygenase
2-511 0e+00

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 971.21  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    2 ATLFLTILLATVLFL-ILRIFSHRRNRS--HNNRLPPGPNPWPIIGNLPHMGTKPHRTLSAMVTTYGPILHLRLGFVDVV 78
Cdd:PLN02687   1 MDLPLPLLLGTVAVSvLVWCLLLRRGGSgkHKRPLPPGPRGWPVLGNLPQLGPKPHHTMAALAKTYGPLFRLRFGFVDVV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   79 VAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEVGTLTR 158
Cdd:PLN02687  81 VAASASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVALLVR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  159 ELVR-VGTKPVNLGQLVNMCVVNALGREMIGRRLFGADADHKADEFRSMVTEMMALAGVFNIGDFVPSLDWLDLQGVAGK 237
Cdd:PLN02687 161 ELARqHGTAPVNLGQLVNVCTTNALGRAMVGRRVFAGDGDEKAREFKEMVVELMQLAGVFNVGDFVPALRWLDLQGVVGK 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  238 MKRLHKRFDAFLSSILKEHEMNGQD--QKHTDMLSTLISLKGTD-LDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWA 314
Cdd:PLN02687 241 MKRLHRRFDAMMNGIIEEHKAAGQTgsEEHKDLLSTLLALKREQqADGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWA 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  315 IAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLT 394
Cdd:PLN02687 321 IAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLV 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  395 NIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGV 474
Cdd:PLN02687 401 NVWAIARDPEQWPDPLEFRPDRFLPGGEHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADGQ 480
                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 15241483  475 TPEKLNMEESYGLTLQRAVPLVVHPKPRLAPNVYGLG 511
Cdd:PLN02687 481 TPDKLNMEEAYGLTLQRAVPLMVHPRPRLLPSAYGIE 517
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
65-502 0e+00

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: 839.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALED 144
Cdd:cd20657   1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMAYNAQDMVFAPYGPRWRLLRKLCNLHLFGGKALED 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 145 FKHVRQEEVGTLTRELVRVGTK--PVNLGQLVNMCVVNALGREMIGRRLFGADADHKADEFRSMVTEMMALAGVFNIGDF 222
Cdd:cd20657  81 WAHVRENEVGHMLKSMAEASRKgePVVLGEMLNVCMANMLGRVMLSKRVFAAKAGAKANEFKEMVVELMTVAGVFNIGDF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 223 VPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLIsLKGTDLDGDGGSLTDTEIKALLLNMFTA 302
Cdd:cd20657 161 IPSLAWMDLQGVEKKMKRLHKRFDALLTKILEEHKATAQERKGKPDFLDFV-LLENDDNGEGERLTDTNIKALLLNLFTA 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 303 GTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEIN 382
Cdd:cd20657 240 GTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEACEVD 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 383 GYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGeKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATL 462
Cdd:cd20657 320 GYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGR-NAKVDVRGNDFELIPFGAGRRICAGTRMGIRMVEYILATL 398
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 15241483 463 VQGFDWELAGGVTPEKLNMEESYGLTLQRAVPLVVHPKPR 502
Cdd:cd20657 399 VHSFDWKLPAGQTPEELNMEEAFGLALQKAVPLVAHPTPR 438
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
65-495 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: 633.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALED 144
Cdd:cd20618   1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGQDIVFAPYGPHWRHLRKICTLELFSAKRLES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 145 FKHVRQEEVGTLTRELVRVGT--KPVNLGQLVNMCVVNALGREMIGRRLFGADA--DHKADEFRSMVTEMMALAGVFNIG 220
Cdd:cd20618  81 FQGVRKEELSHLVKSLLEESEsgKPVNLREHLSDLTLNNITRMLFGKRYFGESEkeSEEAREFKELIDEAFELAGAFNIG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 221 DFVPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLISLkgTDLDGDGGSLTDTEIKALLLNMF 300
Cdd:cd20618 161 DYIPWLRWLDLQGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLL--LLDLDGEGKLSDDNIKALLLDML 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 301 TAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCE 380
Cdd:cd20618 239 AAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLPHESTEDCK 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 381 INGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKsgvDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTA 460
Cdd:cd20618 319 VAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDID---DVKGQDFELLPFGSGRRMCPGMPLGLRMVQLTLA 395
                       410       420       430
                ....*....|....*....|....*....|....*
gi 15241483 461 TLVQGFDWELAgGVTPEKLNMEESYGLTLQRAVPL 495
Cdd:cd20618 396 NLLHGFDWSLP-GPKPEDIDMEEKFGLTVPRAVPL 429
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
3-508 0e+00

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 570.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    3 TLFLTILLATVLFLILRIFSHRRNRSHNNRLPPGPNPWPIIGNLPHMGTKPHRTLSAMVTTYGPILHLRLGFVDVVVAAS 82
Cdd:PLN00110   2 SLLLELAAATLLFFITRFFIRSLLPKPSRKLPPGPRGWPLLGALPLLGNMPHVALAKMAKRYGPVMFLKMGTNSMVVAST 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   83 KSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEVGTLTR---E 159
Cdd:PLN00110  82 PEAARAFLKTLDINFSNRPPNAGATHLAYGAQDMVFADYGPRWKLLRKLSNLHMLGGKALEDWSQVRTVELGHMLRamlE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  160 LVRVGtKPVNLGQLVNMCVVNALGREMIGRRLFGADADhKADEFRSMVTEMMALAGVFNIGDFVPSLDWLDLQGVAGKMK 239
Cdd:PLN00110 162 LSQRG-EPVVVPEMLTFSMANMIGQVILSRRVFETKGS-ESNEFKDMVVELMTTAGYFNIGDFIPSIAWMDIQGIERGMK 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  240 RLHKRFDAFLSSILKEHEMNGQDQK-HTDMLSTLIslkGTDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAEL 318
Cdd:PLN00110 240 HLHKKFDKLLTRMIEEHTASAHERKgNPDFLDVVM---ANQENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEM 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  319 IRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWA 398
Cdd:PLN00110 317 LKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWA 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  399 IARDPDQWSDPLAFKPERFLpGGEKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVtpeK 478
Cdd:PLN00110 397 IGRDPDVWENPEEFRPERFL-SEKNAKIDPRGNDFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGV---E 472
                        490       500       510
                 ....*....|....*....|....*....|
gi 15241483  479 LNMEESYGLTLQRAVPLVVHPKPRLAPNVY 508
Cdd:PLN00110 473 LNMDEAFGLALQKAVPLSAMVTPRLHQSAY 502
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
63-495 0e+00

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: 553.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  63 TYGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKAL 142
Cdd:cd11072   1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGKDIAFAPYGEYWRQMRKICVLELLSAKRV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 143 EDFKHVRQEEVGTLTRELVR--VGTKPVNLGQLVNMCVVNALGREMIGRRLFGADADhkadEFRSMVTEMMALAGVFNIG 220
Cdd:cd11072  81 QSFRSIREEEVSLLVKKIREsaSSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQD----KFKELVKEALELLGGFSVG 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 221 DFVPSLDWLDLQ-GVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLISLKGTDLDGDGGSLTDTEIKALLLNM 299
Cdd:cd11072 157 DYFPSLGWIDLLtGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEFPLTRDNIKAIILDM 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 300 FTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESC 379
Cdd:cd11072 237 FLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLPRECREDC 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 380 EINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggeKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLT 459
Cdd:cd11072 317 KINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFL----DSSIDFKGQDFELIPFGAGRRICPGITFGLANVELAL 392
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 15241483 460 ATLVQGFDWELAGGVTPEKLNMEESYGLTLQRAVPL 495
Cdd:cd11072 393 ANLLYHFDWKLPDGMKPEDLDMEEAFGLTVHRKNPL 428
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
63-499 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: 536.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  63 TYGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKAL 142
Cdd:cd11073   3 KYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPKRL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 143 EDFKHVRQEEVgtltRELVR-VGTK-----PVNLGQLVNMCVVNALGREMIGRRLFGADADhKADEFRSMVTEMMALAGV 216
Cdd:cd11073  83 DATQPLRRRKV----RELVRyVREKagsgeAVDIGRAAFLTSLNLISNTLFSVDLVDPDSE-SGSEFKELVREIMELAGK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 217 FNIGDFVPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHeMNGQDQKHTDMLSTLISLKGTDLDGDGGSLTDTEIKALL 296
Cdd:cd11073 158 PNVADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDER-LAEREAGGDKKKDDDLLLLLDLELDSESELTRNHIKALL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 297 LNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIAS 376
Cdd:cd11073 237 LDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAE 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 377 ESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggeKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQ 456
Cdd:cd11073 317 EDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFL----GSEIDFKGRDFELIPFGSGRRICPGLPLAERMVH 392
                       410       420       430       440
                ....*....|....*....|....*....|....*....|...
gi 15241483 457 FLTATLVQGFDWELAGGVTPEKLNMEESYGLTLQRAVPLVVHP 499
Cdd:cd11073 393 LVLASLLHSFDWKLPDGMKPEDLDMEEKFGLTLQKAVPLKAIP 435
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
65-499 1.18e-163

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: 470.54  E-value: 1.18e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALED 144
Cdd:cd20655   1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPRALER 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 145 FKHVRQEEVGTLTRELVRVGTK--PVNLG----QLVNmcvvNALGREMIGRRLfgADADHKADEFRSMVTEMMALAGVFN 218
Cdd:cd20655  81 FRPIRAQELERFLRRLLDKAEKgeSVDIGkelmKLTN----NIICRMIMGRSC--SEENGEAEEVRKLVKESAELAGKFN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 219 IGDFVPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHE---MNGQDQKHTDMLSTLIslkgtDLDGDGGS---LTDTEI 292
Cdd:cd20655 155 ASDFIWPLKKLDLQGFGKRIMDVSNRFDELLERIIKEHEekrKKRKEGGSKDLLDILL-----DAYEDENAeykITRNHI 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 293 KALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLsLP 372
Cdd:cd20655 230 KAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPL-LV 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 373 HIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLP-GGEKSGVDVKGSDFELIPFGAGRRICAGLSLG 451
Cdd:cd20655 309 RESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLAsSRSGQELDVRGQHFKLLPFGSGRRGCPGASLA 388
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 15241483 452 LRTIQFLTATLVQGFDWELAGGvtpEKLNMEESYGLTLQRAVPLVVHP 499
Cdd:cd20655 389 YQVVGTAIAAMVQCFDWKVGDG---EKVNMEEASGLTLPRAHPLKCVP 433
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
65-502 3.38e-159

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: 459.77  E-value: 3.38e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALED 144
Cdd:cd20654   1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMGYNYAMFGFAPYGPYWRELRKIATLELLSNRRLEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 145 FKHVRQEEVGTLTRELVRVGTKPVNLGQ--LVNM------CVVNALGREMIGRRLFGADA---DHKADEFRSMVTEMMAL 213
Cdd:cd20654  81 LKHVRVSEVDTSIKELYSLWSNNKKGGGgvLVEMkqwfadLTFNVILRMVVGKRYFGGTAvedDEEAERYKKAIREFMRL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 214 AGVFNIGDFVPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEH------EMNGQDQKHTDMLSTLISLKGTDLDGDGgsl 287
Cdd:cd20654 161 AGTFVVSDAIPFLGWLDFGGHEKAMKRTAKELDSILEEWLEEHrqkrssSGKSKNDEDDDDVMMLSILEDSQISGYD--- 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 288 TDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPT 367
Cdd:cd20654 238 ADTVIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYPPG 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 368 PLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGgeKSGVDVKGSDFELIPFGAGRRICAG 447
Cdd:cd20654 318 PLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTT--HKDIDVRGQNFELIPFGSGRRSCPG 395
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15241483 448 LSLGLRTIQFLTATLVQGFDWElagGVTPEKLNMEESYGLTLQRAVPLVVHPKPR 502
Cdd:cd20654 396 VSFGLQVMHLTLARLLHGFDIK---TPSNEPVDMTEGPGLTNPKATPLEVLLTPR 447
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
65-495 1.76e-154

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: 446.67  E-value: 1.76e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALED 144
Cdd:cd20653   1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAPYGDHWRNLRRITTLEIFSSHRLNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 145 FKHVRQEEVGTLTRELVRV---GTKPVNLGQLVNMCVVNALGREMIGRRLFGADADH--KADEFRSMVTEMMALAGVFNI 219
Cdd:cd20653  81 FSSIRRDEIRRLLKRLARDskgGFAKVELKPLFSELTFNNIMRMVAGKRYYGEDVSDaeEAKLFRELVSEIFELSGAGNP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 220 GDFVPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHTdMLSTLISLKGTDLDgdggSLTDTEIKALLLNM 299
Cdd:cd20653 161 ADFLPILRWFDFQGLEKRVKKLAKRRDAFLQGLIDEHRKNKESGKNT-MIDHLLSLQESQPE----YYTDEIIKGLILVM 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 300 FTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESC 379
Cdd:cd20653 236 LLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVPHESSEDC 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 380 EINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFlpggEKSGVDVkgsdFELIPFGAGRRICAGLSLGLRTIQFLT 459
Cdd:cd20653 316 KIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF----EGEEREG----YKLIPFGLGRRACPGAGLAQRVVGLAL 387
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 15241483 460 ATLVQGFDWELAGGvtpEKLNMEESYGLTLQRAVPL 495
Cdd:cd20653 388 GSLIQCFEWERVGE---EEVDMTEGKGLTMPKAIPL 420
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
1-509 6.48e-148

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 433.48  E-value: 6.48e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    1 MATLFLTILLATVLFLILRIFSHRRNRSHNNRLPPGPNPWPIIGNLPHMGTKPHRTLSAMVTTYGPILHLRLGFVDVVVA 80
Cdd:PLN03112   1 MDSFLLSLLFSVLIFNVLIWRWLNASMRKSLRLPPGPPRWPIVGNLLQLGPLPHRDLASLCKKYGPLVYLRLGSVDAITT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   81 ASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEVGTLTR-- 158
Cdd:PLN03112  81 DDPELIREILLRQDDVFASRPRTLAAVHLAYGCGDVALAPLGPHWKRMRRICMEHLLTTKRLESFAKHRAEEARHLIQdv 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  159 -ELVRVGtKPVNLGQLVNMCVVNALGREMIGRRLFGADA--DHKADEFRSMVTEMMALAGVFNIGDFVPSLDWLDLQGVA 235
Cdd:PLN03112 161 wEAAQTG-KPVNLREVLGAFSMNNVTRMLLGKQYFGAESagPKEAMEFMHITHELFRLLGVIYLGDYLPAWRWLDPYGCE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  236 GKMKRLHKRFDAFLSSILKEH----EMNGQDQKHTDMLSTLISLKGTDldgDGGSLTDTEIKALLLNMFTAGTDTSASTV 311
Cdd:PLN03112 240 KKMREVEKRVDEFHDKIIDEHrrarSGKLPGGKDMDFVDVLLSLPGEN---GKEHMDDVEIKALMQDMIAAATDTSAVTN 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  312 DWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGST 391
Cdd:PLN03112 317 EWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKTR 396
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  392 LLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELA 471
Cdd:PLN03112 397 VFINTHGLGRNTKIWDDVEEFRPERHWPAEGSRVEISHGPDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPP 476
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 15241483  472 GGVTPEKLNMEESYGLTLQRAVPLVVHPKPRLAPNVYG 509
Cdd:PLN03112 477 DGLRPEDIDTQEVYGMTMPKAKPLRAVATPRLAPHLYG 514
PLN02183 PLN02183
ferulate 5-hydroxylase
5-503 1.73e-134

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 399.22  E-value: 1.73e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    5 FLTILLATVLFLILrIFSHRRNRSHnnrlPPGPNPWPIIGNLPHMGTKPHRTLSAMVTTYGPILHLRLGFVDVVVAASKS 84
Cdd:PLN02183  14 FFLILISLFLFLGL-ISRLRRRLPY----PPGPKGLPIIGNMLMMDQLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   85 VAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRqEEVGTLTRELVRVG 164
Cdd:PLN02183  89 VARQVLQVQDSVFSNRPANIAISYLTYDRADMAFAHYGPFWRQMRKLCVMKLFSRKRAESWASVR-DEVDSMVRSVSSNI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  165 TKPVNLGQLvnmcvVNALGREMIGRRLFGADADHKADEFRSMVTEMMALAGVFNIGDFVPSLDWLDLQGVAGKMKRLHKR 244
Cdd:PLN02183 168 GKPVNIGEL-----IFTLTRNITYRAAFGSSSNEGQDEFIKILQEFSKLFGAFNVADFIPWLGWIDPQGLNKRLVKARKS 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  245 FDAFLSSILKEH--------EMNGQDQKHTDMLSTLISLKGTDLDGDGG-------SLTDTEIKALLLNMFTAGTDTSAS 309
Cdd:PLN02183 243 LDGFIDDIIDDHiqkrknqnADNDSEEAETDMVDDLLAFYSEEAKVNESddlqnsiKLTRDNIKAIIMDVMFGGTETVAS 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  310 TVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLpHIASESCEINGYHIPKG 389
Cdd:PLN02183 323 AIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLL-HETAEDAEVAGYFIPKR 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  390 STLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKsgvDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWE 469
Cdd:PLN02183 402 SRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVP---DFKGSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWE 478
                        490       500       510
                 ....*....|....*....|....*....|....
gi 15241483  470 LAGGVTPEKLNMEESYGLTLQRAVPLVVHPKPRL 503
Cdd:PLN02183 479 LPDGMKPSELDMNDVFGLTAPRATRLVAVPTYRL 512
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
64-495 1.84e-124

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: 370.66  E-value: 1.84e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALE 143
Cdd:cd20656   1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGQDLIWADYGPHYVKVRKLCTLELFTPKRLE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 144 DFKHVRQEEVGTLTRELVRVGT------KPVNLGQLVNMCVVNALGREMIGRRLFGA--DADHKADEFRSMVTEMMALAG 215
Cdd:cd20656  81 SLRPIREDEVTAMVESIFNDCMspenegKPVVLRKYLSAVAFNNITRLAFGKRFVNAegVMDEQGVEFKAIVSNGLKLGA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 216 VFNIGDFVPSLDWLDLQGVAGKMKRLHKRfDAFLSSILKEHEMNGQDQK-HTDMLSTLISLKgtdldgDGGSLTDTEIKA 294
Cdd:cd20656 161 SLTMAEHIPWLRWMFPLSEKAFAKHGARR-DRLTKAIMEEHTLARQKSGgGQQHFVALLTLK------EQYDLSEDTVIG 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 295 LLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHI 374
Cdd:cd20656 234 LLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHK 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 375 ASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggeKSGVDVKGSDFELIPFGAGRRICAGLSLGLRT 454
Cdd:cd20656 314 ASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFL----EEDVDIKGHDFRLLPFGAGRRVCPGAQLGINL 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 15241483 455 IQFLTATLVQGFDWELAGGVTPEKLNMEESYGLTLQRAVPL 495
Cdd:cd20656 390 VTLMLGHLLHHFSWTPPEGTPPEEIDMTENPGLVTFMRTPL 430
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
34-501 7.25e-113

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: 341.95  E-value: 7.25e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    34 PPGPNPWPIIGNLPHMGTK--PHRTLSAMVTTYGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAY 111
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   112 NY--QDLVFApYGHRWRLLRKISSVHLFSAKALEdFKHVRQEEVGTLTRELVRVGTKP--VNLGQLVNMCVVNALGREMI 187
Cdd:pfam00067  81 PFlgKGIVFA-NGPRWRQLRRFLTPTFTSFGKLS-FEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   188 GRRLFGADaDHKADEFRSMVTEMMALAG--VFNIGDFVPSLDWLdLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKH 265
Cdd:pfam00067 159 GERFGSLE-DPKFLELVKAVQELSSLLSspSPQLLDLFPILKYF-PGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   266 TDMLSTLISLKGTDlDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNES 345
Cdd:pfam00067 237 SPRDFLDALLLAKE-EEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   346 DIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSg 425
Cdd:pfam00067 316 DLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKF- 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241483   426 vdvkGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPEKLNMEESygltlqravpLVVHPKP 501
Cdd:pfam00067 395 ----RKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPG----------LLLPPKP 456
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
66-495 4.71e-112

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: 338.53  E-value: 4.71e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  66 PILHLRLGFVDVVVAASKSVAEQFLkiHDANFASRPPNSGAKHMAYNyQDLVFAPYGHRWRLLRKISSVHLFSAKALEDF 145
Cdd:cd11076   4 RLMAFSLGETRVVITSHPETAREIL--NSPAFADRPVKESAYELMFN-RAIGFAPYGEYWRNLRRIASNHLFSPRRIAAS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 146 KHVRQEE----VGTLTRELVRVGTKPV----NLGQLVN-MCVVnalgremIGRRLFGADADHKADEFRSMVTEMMALAGV 216
Cdd:cd11076  81 EPQRQAIaaqmVKAIAKEMERSGEVAVrkhlQRASLNNiMGSV-------FGRRYDFEAGNEEAEELGEMVREGYELLGA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 217 FNIGDFVPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLS--TLISLKGTDldgdggSLTDTEIKA 294
Cdd:cd11076 154 FNWSDHLPWLRWLDLQGIRRRCSALVPRVNTFVGKIIEEHRAKRSNRARDDEDDvdVLLSLQGEE------KLSDSDMIA 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 295 LLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPL-SLPH 373
Cdd:cd11076 228 VLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGPLlSWAR 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 374 IASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGSDFELIPFGAGRRICAGLSLGLR 453
Cdd:cd11076 308 LAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGADVSVLGSDLRLAPFGAGRRVCPGKALGLA 387
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 15241483 454 TIQFLTATLVQGFDWELAGGVTPEklnMEESYGLTLQRAVPL 495
Cdd:cd11076 388 TVHLWVAQLLHEFEWLPDDAKPVD---LSEVLKLSCEMKNPL 426
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
63-495 2.05e-101

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: 311.48  E-value: 2.05e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  63 TYGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLV-FAPYGHRWRLLRKISSVHLFSAKA 141
Cdd:cd11075   1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVLFSSNKHMVnSSPYGPLWRTLRRNLVSEVLSPSR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 142 LEDFKHVRQEEVGTLT---RELVRVGTKPVNL---------GQLVNMCvvnalgremigrrlFGADADhkADEFRSMVTE 209
Cdd:cd11075  81 LKQFRPARRRALDNLVerlREEAKENPGPVNVrdhfrhalfSLLLYMC--------------FGERLD--EETVRELERV 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 210 MMALA---GVFNIGDFVPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEH--EMNGQDQKHTDMLSTLISLKGTDLDGDG 284
Cdd:cd11075 145 QRELLlsfTDFDVRDFFPALTWLLNRRRWKKVLELRRRQEEVLLPLIRARrkRRASGEADKDYTDFLLLDLLDLKEEGGE 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 285 GSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLH 364
Cdd:cd11075 225 RKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRH 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 365 PPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGSDFELIPFGAGRRI 444
Cdd:cd11075 305 PPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAADIDTGSKEIKMMPFGAGRRI 384
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 15241483 445 CAGLSLGLRTIQFLTATLVQGFDWELAGGvtpEKLNMEESYGLTLQRAVPL 495
Cdd:cd11075 385 CPGLGLATLHLELFVARLVQEFEWKLVEG---EEVDFSEKQEFTVVMKNPL 432
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
71-503 2.05e-100

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: 309.30  E-value: 2.05e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  71 RLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQ 150
Cdd:cd20658   7 RLGNTHVIPVTCPKIAREILRKQDAVFASRPLTYATEIISGGYKTTVISPYGEQWKKMRKVLTTELMSPKRHQWLHGKRT 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 151 EEVGTLTRELVR-----VGTKPVNLGQLVNMCVVNALGREMIGRRLFG---ADADHKADEFRSMVTEMMALAGV--FNIG 220
Cdd:cd20658  87 EEADNLVAYVYNmckksNGGGLVNVRDAARHYCGNVIRKLMFGTRYFGkgmEDGGPGLEEVEHMDAIFTALKCLyaFSIS 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 221 DFVPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHT---DMLSTLISLKgtdlDGDGGSL-TDTEIKALL 296
Cdd:cd20658 167 DYLPFLRGLDLDGHEKIVREAMRIIRKYHDPIIDERIKQWREGKKKeeeDWLDVFITLK----DENGNPLlTPDEIKAQI 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 297 LNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIAS 376
Cdd:cd20658 243 KELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNVPHVAM 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 377 ESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGekSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQ 456
Cdd:cd20658 323 SDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNED--SEVTLTEPDLRFISFSTGRRGCPGVKLGTAMTV 400
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 15241483 457 FLTATLVQGFDWELAGGVTPEKLnMEESYGLTLqrAVPLVVHPKPRL 503
Cdd:cd20658 401 MLLARLLQGFTWTLPPNVSSVDL-SESKDDLFM--AKPLVLVAKPRL 444
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
65-501 5.37e-97

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: 299.90  E-value: 5.37e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAAS-KSVAEQFLKIHDaNFASRPPNSGAKHMaYNYQDLVFApYGHRWRLLRKISSVHLFSAKALE 143
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDpEIIKEAFVKNGD-NFSDRPLLPSFEII-SGGKGILFS-NGDYWKELRRFALSSLTKTKLKK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 144 DFKHVRQEEVGTLTRELVR--VGTKPVNLGQLVNMCVVNALGREMIGRRlFGADADHKADEFRSMVTEMMALAGVFNIGD 221
Cdd:cd20617  78 KMEELIEEEVNKLIESLKKhsKSGEPFDPRPYFKKFVLNIINQFLFGKR-FPDEDDGEFLKLVKPIEEIFKELGSGNPSD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 222 FVPSLDWLDLQGVAgKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLISLKgtDLDGDGGSLTDTEIKALLLNMFT 301
Cdd:cd20617 157 FIPILLPFYFLYLK-KLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLL--LKEGDSGLFDDDSIISTCLDLFL 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 302 AGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEI 381
Cdd:cd20617 234 AGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTEI 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 382 NGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDvkgSDFELIPFGAGRRICAGLSLGlRTIQFL-TA 460
Cdd:cd20617 314 GGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFL---ENDGNK---LSEQFIPFGIGKRNCVGENLA-RDELFLfFA 386
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 15241483 461 TLVQGFDWELAGGvtpEKLNMEESYGLTLqravplvvHPKP 501
Cdd:cd20617 387 NLLLNFKFKSSDG---LPIDEKEVFGLTL--------KPKP 416
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
64-489 5.84e-94

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: 292.19  E-value: 5.84e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVA-EQFLKIHDAnFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKI--SSVHLF--S 138
Cdd:cd11027   1 YGDVFSLYLGSRLVVVLNSGAAIkEALVKKSAD-FAGRPKLFTFDLFSRGGKDIAFGDYSPTWKLHRKLahSALRLYasG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 139 AKALEDfkhVRQEEVGTLTRELVRVGTKPVNLGQLVNMCVVNalgreMIGRRLFGADADHKADEFRSMV---TEMMALAG 215
Cdd:cd11027  80 GPRLEE---KIAEEAEKLLKRLASQEGQPFDPKDELFLAVLN-----VICSITFGKRYKLDDPEFLRLLdlnDKFFELLG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 216 VFNIGDFVPSLDWLDLQGVAgKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLISLK---GTDLDGDGGSLTDTEI 292
Cdd:cd11027 152 AGSLLDIFPFLKYFPNKALR-ELKELMKERDEILRKKLEEHKETFDPGNIRDLTDALIKAKkeaEDEGDEDSGLLTDDHL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 293 KALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLP 372
Cdd:cd11027 231 VMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALP 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 373 HIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDfELIPFGAGRRICAGLSLGL 452
Cdd:cd11027 311 HKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFL---DENGKLVPKPE-SFLPFSAGRRVCLGESLAK 386
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 15241483 453 RTIQFLTATLVQGFDWELAGGVTPEklNMEESYGLTL 489
Cdd:cd11027 387 AELFLFLARLLQKFRFSPPEGEPPP--ELEGIPGLVL 421
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
64-501 1.01e-93

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: 291.40  E-value: 1.01e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSvHLFSAKALE 143
Cdd:cd11065   1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGELMGWGMRLLLMPYGPRWRLHRRLFH-QLLNPSAVR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 144 DFKHVRQEEVGTLTRELVRvgtKPVNLGQLVNMCVVNALGREMIGRRLFGADADHKADEFRSMVTEMMALAGVFNIGDFV 223
Cdd:cd11065  80 KYRPLQELESKQLLRDLLE---SPDDFLDHIRRYAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGSPGAYLVDFF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 224 PSLDWL---DLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHTD-MLSTLISLKGTDldgdgGSLTDTEIKALLLNM 299
Cdd:cd11065 157 PFLRYLpswLGAPWKRKARELRELTRRLYEGPFEAAKERMASGTATPsFVKDLLEELDKE-----GGLSEEEIKYLAGSL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 300 FTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESC 379
Cdd:cd11065 232 YEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIPHALTEDD 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 380 EINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGvdvKGSDFELIPFGAGRRICAGLSLGLRTIQFLT 459
Cdd:cd11065 312 EYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTP---DPPDPPHFAFGFGRRICPGRHLAENSLFIAI 388
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 15241483 460 ATLVQGFDWELA--GGVTPEKLNMEESYGltlqravpLVVHPKP 501
Cdd:cd11065 389 ARLLWAFDIKKPkdEGGKEIPDEPEFTDG--------LVSHPLP 424
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
4-499 8.28e-93

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 291.60  E-value: 8.28e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    4 LFLTILLATVLFLILRIFSHRrnrshNNRLPPGPNPWPIIGNLPHMGT-KPHRTLSAMVTTYGPILHLRLGFVDVVVAAS 82
Cdd:PLN03234   5 LIIAALVAAAAFFFLRSTTKK-----SLRLPPGPKGLPIIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRRLAVISS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   83 KSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEVGTLTRELVR 162
Cdd:PLN03234  80 AELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQRMMDKIYK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  163 VGTKP--VNLGQLV---NMCVVnalGREMIGRRLFGADADHKadEFRSMVTEMMALAGVFNIGDFVPSLDWLD-LQGVAG 236
Cdd:PLN03234 160 AADQSgtVDLSELLlsfTNCVV---CRQAFGKRYNEYGTEMK--RFIDILYETQALLGTLFFSDLFPYFGFLDnLTGLSA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  237 KMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLISLKGTDlDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIA 316
Cdd:PLN03234 235 RLKKAFKELDTYLQELLDETLDPNRPKQETESFIDLLMQIYKD-QPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMT 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  317 ELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNI 396
Cdd:PLN03234 314 YLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNA 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  397 WAIARDPDQWSD-PLAFKPERFLpgGEKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVT 475
Cdd:PLN03234 394 WAVSRDTAAWGDnPNEFIPERFM--KEHKGVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLPKGIK 471
                        490       500
                 ....*....|....*....|....
gi 15241483  476 PEKLNMEESYGLTLQRAVPLVVHP 499
Cdd:PLN03234 472 PEDIKMDVMTGLAMHKKEHLVLAP 495
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
4-504 4.42e-87

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 277.00  E-value: 4.42e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    4 LFLTILLATVLFLILRIFSHRRnRSHNNRLPPGPNPWPIIGNLPHMGTK-PHRTLSAMVTTYGPILHLRLGFVDVVVAAS 82
Cdd:PLN02394   3 LLEKTLLGLFVAIVLALLVSKL-RGKKLKLPPGPAAVPIFGNWLQVGDDlNHRNLAEMAKKYGDVFLLRMGQRNLVVVSS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   83 KSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEVGTLTRELVR 162
Cdd:PLN02394  82 PELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGDHWRKMRRIMTVPFFTNKVVQQYRYGWEEEADLVVEDVRA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  163 ---VGTKPVNLGQLVNMCVVNALGREMIGRRlFGADADHKADEFRSMVTEMMALAGVF--NIGDFVPSLDWLdLQGVAGK 237
Cdd:PLN02394 162 npeAATEGVVIRRRLQLMMYNIMYRMMFDRR-FESEDDPLFLKLKALNGERSRLAQSFeyNYGDFIPILRPF-LRGYLKI 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  238 MKRLHKRFDAFLssilKEHemngqdqkHTDMLSTLISLKGTDLDGD------------GGSLTDTEIKALLLNMFTAGTD 305
Cdd:PLN02394 240 CQDVKERRLALF----KDY--------FVDERKKLMSAKGMDKEGLkcaidhileaqkKGEINEDNVLYIVENINVAAIE 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  306 TSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYH 385
Cdd:PLN02394 308 TTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGYD 387
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  386 IPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpgGEKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQG 465
Cdd:PLN02394 388 IPAESKILVNAWWLANNPELWKNPEEFRPERFL--EEEAKVEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQN 465
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 15241483  466 FDWELAGGVtpEKLNMEESYG-LTLQRAVPLVVHPKPRLA 504
Cdd:PLN02394 466 FELLPPPGQ--SKIDVSEKGGqFSLHIAKHSTVVFKPRSA 503
PLN02966 PLN02966
cytochrome P450 83A1
8-500 2.66e-85

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 272.39  E-value: 2.66e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    8 ILLATVLFLILRIFSHRRNRSHNNRLPPGPNPWPIIGNLPHMGT-KPHRTLSAMVTTYGPILHLRLGFVDVVVAASKSVA 86
Cdd:PLN02966   5 IIGVVALAAVLLFFLYQKPKTKRYKLPPGPSPLPVIGNLLQLQKlNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   87 EQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEVGTLTRELVRVGTK 166
Cdd:PLN02966  85 KELLKTQDVNFADRPPHRGHEFISYGRRDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAADK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  167 P--VNLGQLVnMCVVNALgremIGRRLFGADADHKADEFRSMVTEMMALAGVFN---IGDFVPSLDWL-DLQGVAGKMKR 240
Cdd:PLN02966 165 SevVDISELM-LTFTNSV----VCRQAFGKKYNEDGEEMKRFIKILYGTQSVLGkifFSDFFPYCGFLdDLSGLTAYMKE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  241 LHKRFDAFLSSILKE----HEMNGQDQKHTDMLSTLISLKGTdldgdGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIA 316
Cdd:PLN02966 240 CFERQDTYIQEVVNEtldpKRVKPETESMIDLLMEIYKEQPF-----ASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMT 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  317 ELIRHPDIMVKAQEELDIVVGRDRP--VNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLT 394
Cdd:PLN02966 315 YLMKYPQVLKKAQAEVREYMKEKGStfVTEDDVKNLPYFRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNV 394
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  395 NIWAIARDPDQWS-DPLAFKPERFLpggEKSgVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGG 473
Cdd:PLN02966 395 NAWAVSRDEKEWGpNPDEFRPERFL---EKE-VDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPNG 470
                        490       500
                 ....*....|....*....|....*..
gi 15241483  474 VTPEKLNMEESYGLTLQRAVPLVVHPK 500
Cdd:PLN02966 471 MKPDDINMDVMTGLAMHKSQHLKLVPE 497
PLN02971 PLN02971
tryptophan N-hydroxylase
6-508 1.49e-84

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 271.53  E-value: 1.49e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    6 LTILLATVLFLILRIFSHRRNRSHNNRLPPGPNPWPIIGNLPHM-GTKP-HRTL-SAMVTTYGPILHLRLGFVDVVVAAS 82
Cdd:PLN02971  31 LQALVAITLLMILKKLKSSSRNKKLHPLPPGPTGFPIVGMIPAMlKNRPvFRWLhSLMKELNTEIACVRLGNTHVIPVTC 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   83 KSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEVGTLTRELVR 162
Cdd:PLN02971 111 PKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDHLTAWLYN 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  163 V--GTKPVNLGQLVNMCVVNALGREMIGRRLFG----ADADHKADEFRSM--VTEMMALAGVFNIGDFVPSLDWLDLQGV 234
Cdd:PLN02971 191 MvkNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSektePDGGPTLEDIEHMdaMFEGLGFTFAFCISDYLPMLTGLDLNGH 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  235 AGKMKRLHKRFDAFLSSILKEHEMNGQDQKHT---DMLSTLISLKgtdlDGDGGSL-TDTEIKALLLNMFTAGTDTSAST 310
Cdd:PLN02971 271 EKIMRESSAIMDKYHDPIIDERIKMWREGKRTqieDFLDIFISIK----DEAGQPLlTADEIKPTIKELVMAAPDNPSNA 346
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  311 VDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGS 390
Cdd:PLN02971 347 VEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGS 426
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  391 TLLTNIWAIARDPDQWSDPLAFKPERFLpgGEKSGVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWEL 470
Cdd:PLN02971 427 QVLLSRYGLGRNPKVWSDPLSFKPERHL--NECSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKL 504
                        490       500       510
                 ....*....|....*....|....*....|....*...
gi 15241483  471 AGGVTPEKLnMEESYGLTLQRavPLVVHPKPRLAPNVY 508
Cdd:PLN02971 505 AGSETRVEL-MESSHDMFLSK--PLVMVGELRLSEDLY 539
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
64-502 2.78e-75

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: 243.74  E-value: 2.78e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAyNYQDLVFAPYGHRWRLLRKI--SSVHLFSAKA 141
Cdd:cd11028   1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFIS-NGKSMAFSDYGPRWKLHRKLaqNALRTFSNAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 142 ----LEDfkHVrQEEVGTLTRELVRV--GTKPVNLGQLVNMCVVNALGREMIGRRLfgadaDHKADEFR---SMVTEMMA 212
Cdd:cd11028  80 thnpLEE--HV-TEEAEELVTELTENngKPGPFDPRNEIYLSVGNVICAICFGKRY-----SRDDPEFLelvKSNDDFGA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 213 LAGVFNIGDFVPSLDWLDLQGVAgKMKRLHKRFDAFLSSILKEHeMNGQDQKHT-DMLSTLI--SLKGTDLDGDGGSLTD 289
Cdd:cd11028 152 FVGAGNPVDVMPWLRYLTRRKLQ-KFKELLNRLNSFILKKVKEH-LDTYDKGHIrDITDALIkaSEEKPEEEKPEVGLTD 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 290 TEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPL 369
Cdd:cd11028 230 EHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPF 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 370 SLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFL-PGGE--KSGVDvkgsdfELIPFGAGRRICA 446
Cdd:cd11028 310 TIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLdDNGLldKTKVD------KFLPFGAGRRRCL 383
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15241483 447 GLSLGlRTIQFL-TATLVQGFDWELAGGvtpEKLNMEESYGLTLqravplvvHPKPR 502
Cdd:cd11028 384 GEELA-RMELFLfFATLLQQCEFSVKPG---EKLDLTPIYGLTM--------KPKPF 428
PLN00168 PLN00168
Cytochrome P450; Provisional
4-502 1.15e-74

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 244.86  E-value: 1.15e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    4 LFLTILLATVLFLILRIFSHR-RNRSHNNRLPPGPNPWPIIGNL---PHMGTKPHRTLSAMVTTYGPILHLRLGFVDVVV 79
Cdd:PLN00168   6 LLLLAALLLLPLLLLLLGKHGgRGGKKGRRLPPGPPAVPLLGSLvwlTNSSADVEPLLRRLIARYGPVVSLRVGSRLSVF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   80 AASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRK--------ISSVHLFS-AKALedfkhVRQ 150
Cdd:PLN00168  86 VADRRLAHAALVERGAALADRPAVASSRLLGESDNTITRSSYGPVWRLLRRnlvaetlhPSRVRLFApARAW-----VRR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  151 EEVGTLTRELVRVGTKPV-------NLGQLVNMCvvnalgremIGRRLFGADADHKADEFRSMVTEMMALAGVFNigdFV 223
Cdd:PLN00168 161 VLVDKLRREAEDAAAPRVvetfqyaMFCLLVLMC---------FGERLDEPAVRAIAAAQRDWLLYVSKKMSVFA---FF 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  224 PSLDWLDLQGVAGKMKRLHKRF-DAFLSSILKEHEMNGQDQKH--------TDMLSTLISLKGTDLDGDGG-SLTDTEIK 293
Cdd:PLN00168 229 PAVTKHLFRGRLQKALALRRRQkELFVPLIDARREYKNHLGQGgeppkketTFEHSYVDTLLDIRLPEDGDrALTDDEIV 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  294 ALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRP-VNESDIAQLPYLQAVIKENFRLHPPTPLSLP 372
Cdd:PLN00168 309 NLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQEeVSEEDVHKMPYLKAVVLEGLRKHPPAHFVLP 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  373 HIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGS-DFELIPFGAGRRICAGLSLG 451
Cdd:PLN00168 389 HKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLAGGDGEGVDVTGSrEIRMMPFGVGRRICAGLGIA 468
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15241483  452 LRTIQFLTATLVQGFDWELAGGvtpEKLNMEESYGLTLQRAVPLVVHPKPR 502
Cdd:PLN00168 469 MLHLEYFVANMVREFEWKEVPG---DEVDFAEKREFTTVMAKPLRARLVPR 516
PLN03018 PLN03018
homomethionine N-hydroxylase
8-508 1.30e-71

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 237.22  E-value: 1.30e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    8 ILLATVLF-----LILRIFSH-RRNRSHNNRLPPGPNPWPIIGNLPHM-GTKPHRTLS--AMVTTYGPILHLRLGFVDVV 78
Cdd:PLN03018  10 ILLGFIVFiasitLLGRILSRpSKTKDRSRQLPPGPPGWPILGNLPELiMTRPRSKYFhlAMKELKTDIACFNFAGTHTI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   79 VAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEVGTL-- 156
Cdd:PLN03018  90 TINSDEIAREAFRERDADLADRPQLSIMETIGDNYKSMGTSPYGEQFMKMKKVITTEIMSVKTLNMLEAARTIEADNLia 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  157 -------------TRELVRVgtkpvnLGQLVNMcvvnalgREMIGRRLFGADaDHKADEFRSMVTEMMALAGVFNIGDFV 223
Cdd:PLN03018 170 yihsmyqrsetvdVRELSRV------YGYAVTM-------RMLFGRRHVTKE-NVFSDDGRLGKAEKHHLEVIFNTLNCL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  224 PSLD-------WLDLQGVAGKMKRLHKRFD---AFLSSILKEH----EMNGQDQKHTDMLSTLISLKgtdlDGDGGSL-T 288
Cdd:PLN03018 236 PGFSpvdyverWLRGWNIDGQEERAKVNVNlvrSYNNPIIDERvelwREKGGKAAVEDWLDTFITLK----DQNGKYLvT 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  289 DTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTP 368
Cdd:PLN03018 312 PDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAH 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  369 LSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPG-GEKSGVDVKGSDFELIPFGAGRRICAG 447
Cdd:PLN03018 392 YVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGdGITKEVTLVETEMRFVSFSTGRRGCVG 471
                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15241483  448 LSLGLRTIQFLTATLVQGFDWELAGGVTPekLNMEESyGLTLQRAVPLVVHPKPRLAPNVY 508
Cdd:PLN03018 472 VKVGTIMMVMMLARFLQGFNWKLHQDFGP--LSLEED-DASLLMAKPLLLSVEPRLAPNLY 529
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
65-477 1.27e-70

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: 231.34  E-value: 1.27e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAAS-KSVAEQFLKihdANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHL----FSA 139
Cdd:cd20651   1 GDVVGLKLGKDKVVVVSGyEAVREVLSR---EEFDGRPDGFFFRLRTFGKRLGITFTDGPFWKEQRRFVLRHLrdfgFGR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 140 KALEDfkhVRQEEVGTLTRELVRVGTKPVNLGQLVNMCVVNALGREMIGRRLfgADADHKADEFRSMVTEMMALA----G 215
Cdd:cd20651  78 RSMEE---VIQEEAEELIDLLKKGEKGPIQMPDLFNVSVLNVLWAMVAGERY--SLEDQKLRKLLELVHLLFRNFdmsgG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 216 VFNigdFVPsldWL-----DLQGVAgKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDML-STLISLKGTDLDGDggSLTD 289
Cdd:cd20651 153 LLN---QFP---WLrfiapEFSGYN-LLVELNQKLIEFLKEEIKEHKKTYDEDNPRDLIdAYLREMKKKEPPSS--SFTD 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 290 TEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPL 369
Cdd:cd20651 224 DQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPI 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 370 SLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggeksgvDVKG---SDFELIPFGAGRRICA 446
Cdd:cd20651 304 GIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFL--------DEDGkllKDEWFLPFGAGKRRCL 375
                       410       420       430
                ....*....|....*....|....*....|..
gi 15241483 447 GLSLGlRTIQFL-TATLVQGFDWELAGGVTPE 477
Cdd:cd20651 376 GESLA-RNELFLfFTGLLQNFTFSPPNGSLPD 406
PLN02655 PLN02655
ent-kaurene oxidase
35-502 1.86e-70

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 232.32  E-value: 1.86e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   35 PGpnpWPIIGNLPHMG-TKPHRTLSAMVTTYGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNY 113
Cdd:PLN02655   5 PG---LPVIGNLLQLKeKKPHRTFTKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVLTRDK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  114 QDLVFAPYGHRWRLLRKISSVHLFSAKALEDFKHVRQEEV----GTLTRELVRVGTKPVNL-----GQLVNMCVVNALGR 184
Cdd:PLN02655  82 SMVATSDYGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIenmlSGLHALVKDDPHSPVNFrdvfeNELFGLSLIQALGE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  185 EMIGRRL--FGADADhKADEFRSMVTEMMALAGVFNIGDFVPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHEM---N 259
Cdd:PLN02655 162 DVESVYVeeLGTEIS-KEEIFDVLVHDMMMCAIEVDWRDFFPYLSWIPNKSFETRVQTTEFRRTAVMKALIKQQKKriaR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  260 GQDQK-HTDMLSTlislkgtdldgDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGR 338
Cdd:PLN02655 241 GEERDcYLDFLLS-----------EATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGD 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  339 DRpVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFL 418
Cdd:PLN02655 310 ER-VTEEDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFL 388
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  419 PGGEKSgVDVkgsdFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGvtpeKLNMEESYGLTLQRAVPLVVH 498
Cdd:PLN02655 389 GEKYES-ADM----YKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLREG----DEEKEDTVQLTTQKLHPLHAH 459

                 ....
gi 15241483  499 PKPR 502
Cdd:PLN02655 460 LKPR 463
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
63-467 1.39e-69

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: 229.28  E-value: 1.39e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  63 TYGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSVHLFSAKAL 142
Cdd:cd11074   2 KFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGEHWRKMRRIMTVPFFTNKVV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 143 EDFKHVRQEEVGTLTRELVR---VGTKPVNLGQLVNMCVVNALGREMIGRRlFGADADHKADEFRSMVTEMMALAGVF-- 217
Cdd:cd11074  82 QQYRYGWEEEAARVVEDVKKnpeAATEGIVIRRRLQLMMYNNMYRIMFDRR-FESEDDPLFVKLKALNGERSRLAQSFey 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 218 NIGDFVPSLDWLdLQGVAGKMKRL-HKRFDAFlssilKEHemngqdqkHTDMLSTLISLKGTDLDG------------DG 284
Cdd:cd11074 161 NYGDFIPILRPF-LRGYLKICKEVkERRLQLF-----KDY--------FVDERKKLGSTKSTKNEGlkcaidhildaqKK 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 285 GSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLH 364
Cdd:cd11074 227 GEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLR 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 365 PPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpgGEKSGVDVKGSDFELIPFGAGRRI 444
Cdd:cd11074 307 MAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFL--EEESKVEANGNDFRYLPFGVGRRS 384
                       410       420
                ....*....|....*....|...
gi 15241483 445 CAGLSLGLRTIQFLTATLVQGFD 467
Cdd:cd11074 385 CPGIILALPILGITIGRLVQNFE 407
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
65-477 2.42e-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: 2.42e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAASKSVAEQFLkiHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKISSvHLFSAKALED 144
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVL--RDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLA-PAFTPRALAA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 145 FKHVRQEEVGTLTRELVRVGTKPVNLGQLVNmcvvnALGREMIGRRLFGADADHKADEFRSMVTEMMALAGvfnigdfvP 224
Cdd:cd00302  78 LRPVIREIARELLDRLAAGGEVGDDVADLAQ-----PLALDVIARLLGGPDLGEDLEELAELLEALLKLLG--------P 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 225 SLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLstlislkgtDLDGDGGSLTDTEIKALLLNMFTAGT 304
Cdd:cd00302 145 RLLRPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDLLLL---------ADADDGGGLSDEEIVAELLTLLLAGH 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 305 DTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPvneSDIAQLPYLQAVIKENFRLHPPTPLsLPHIASESCEINGY 384
Cdd:cd00302 216 ETTASLLAWALYLLARHPEVQERLRAEIDAVLGDGTP---EDLSKLPYLEAVVEETLRLYPPVPL-LPRVATEDVELGGY 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 385 HIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKsgvdvkgSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQ 464
Cdd:cd00302 292 TIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREE-------PRYAHLPFGAGPHRCLGARLARLELKLALATLLR 364
                       410
                ....*....|...
gi 15241483 465 GFDWELAGGVTPE 477
Cdd:cd00302 365 RFDFELVPDEELE 377
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
64-466 4.16e-65

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: 216.90  E-value: 4.16e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKI--SSVHLFSAKA 141
Cdd:cd20674   1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTGKLVSQGGQDLSLGDYSLLWKAHRKLtrSALQLGIRNS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 142 LEDfkhVRQEEVGTLTRELVRVGTKPVNLGQLVNMCVVNalgreMIGRRLFGA--DADHKADEFRSMVTEMMALAGVFNI 219
Cdd:cd20674  81 LEP---VVEQLTQELCERMRAQAGTPVDIQEEFSLLTCS-----IICCLTFGDkeDKDTLVQAFHDCVQELLKTWGHWSI 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 220 G--DFVPSLDWLDLQGVAgKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLISLKGTDLDGDG-GSLTDTEIKALL 296
Cdd:cd20674 153 QalDSIPFLRFFPNPGLR-RLKQAVENRDHIVESQLRQHKESLVAGQWRDMTDYMLQGLGQPRGEKGmGQLLEGHVHMAV 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 297 LNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIAS 376
Cdd:cd20674 232 VDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTT 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 377 ESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGvdvkgsdfELIPFGAGRRICAGLSLGLRTIQ 456
Cdd:cd20674 312 RDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAANR--------ALLPFGCGARVCLGEPLARLELF 383
                       410
                ....*....|
gi 15241483 457 FLTATLVQGF 466
Cdd:cd20674 384 VFLARLLQAF 393
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
65-477 2.57e-63

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: 211.67  E-value: 2.57e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAASKSVAEQFLKIHDANFAsrppnsgaKHMAYNYQDLVF-----APYGHRWRLLRKISSvHLFSA 139
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYV--------KGGVYERLKLLLgngllTSEGDLWRRQRRLAQ-PAFHR 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 140 KALEDFKhvrqEEVGTLTRELV-----RVGTKPVNLGQlvNMcvvNALGREMIGRRLFGADADHKADEFRSMVTEMMALA 214
Cdd:cd20620  72 RRIAAYA----DAMVEATAALLdrweaGARRGPVDVHA--EM---MRLTLRIVAKTLFGTDVEGEADEIGDALDVALEYA 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 215 gVFNIGDFVPSLDWLDLQGVAgKMKRLHKRFDAFLSSILKEHEMNGQDqkHTDMLSTLISlkgTDLDGDGGSLTDTEIKA 294
Cdd:cd20620 143 -ARRMLSPFLLPLWLPTPANR-RFRRARRRLDEVIYRLIAERRAAPAD--GGDLLSMLLA---ARDEETGEPMSDQQLRD 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 295 LLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGrDRPVNESDIAQLPYLQAVIKENFRLHPPTPLsLPHI 374
Cdd:cd20620 216 EVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLRLYPPAWI-IGRE 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 375 ASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKsgvdvKGSDFELIPFGAGRRICAGLSLGLRT 454
Cdd:cd20620 294 AVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREA-----ARPRYAYFPFGGGPRICIGNHFAMME 368
                       410       420
                ....*....|....*....|...
gi 15241483 455 IQFLTATLVQGFDWELAGGVTPE 477
Cdd:cd20620 369 AVLLLATIAQRFRLRLVPGQPVE 391
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
64-489 2.50e-62

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: 209.63  E-value: 2.50e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNyQDLVFAPYGHRWRLLRKISSVHL------- 136
Cdd:cd20666   1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKG-KGIVFAPYGPVWRQQRKFSHSTLrhfglgk 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 137 --FSAKALEDFKHVRQEevgtltreLVRVGTKPVNLGQLVNMCVVNALGREMIGRRLfgadaDHKADEFRSMVTEMM--- 211
Cdd:cd20666  80 lsLEPKIIEEFRYVKAE--------MLKHGGDPFNPFPIVNNAVSNVICSMSFGRRF-----DYQDVEFKTMLGLMSrgl 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 212 -----ALAGVFNIGDFVPSLDWldlqGVAGKMKRLHKRFDAFLSSILKEH-----EMNGQDqkHTDMLstLISLKGTDLD 281
Cdd:cd20666 147 eisvnSAAILVNICPWLYYLPF----GPFRELRQIEKDITAFLKKIIADHretldPANPRD--FIDMY--LLHIEEEQKN 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 282 GDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENF 361
Cdd:cd20666 219 NAESSFNEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQ 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 362 RLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGAG 441
Cdd:cd20666 299 RMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFL---DENGQLIKKEAF--IPFGIG 373
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 15241483 442 RRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTpeKLNMEESYGLTL 489
Cdd:cd20666 374 RRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNAP--KPSMEGRFGLTL 419
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
64-490 4.00e-60

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: 204.09  E-value: 4.00e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWRLLRKI--SSVHLF---S 138
Cdd:cd20673   1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRNGKDIAFADYSATWQLHRKLvhSAFALFgegS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 139 AKaLEDfkhVRQEEVGTLTRELVRVGTKPVNLGQLVNMCVVNalgreMIGRRLFGADADHKADEFRSMVTEMMALAGVFN 218
Cdd:cd20673  81 QK-LEK---IICQEASSLCDTLATHNGESIDLSPPLFRAVTN-----VICLLCFNSSYKNGDPELETILNYNEGIVDTVA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 219 IGDFVPSLDWL------DLQgvagKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLISLK------GTDLDGDGGS 286
Cdd:cd20673 152 KDSLVDIFPWLqifpnkDLE----KLKQCVKIRDKLLQKKLEEHKEKFSSDSIRDLLDALLQAKmnaennNAGPDQDSVG 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 287 LTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPP 366
Cdd:cd20673 228 LSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPV 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 367 TPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFELIPFGAGRRICA 446
Cdd:cd20673 308 APLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFL---DPTGSQLISPSLSYLPFGAGPRVCL 384
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 15241483 447 GLSLGLRTIQFLTATLVQGFDWELAGGVTPEKLnmEESYGLTLQ 490
Cdd:cd20673 385 GEALARQELFLFMAWLLQRFDLEVPDGGQLPSL--EGKFGVVLQ 426
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
64-490 4.50e-60

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: 203.95  E-value: 4.50e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNYQdlVFAPYGHRWRLLRKissvhlFSAKALE 143
Cdd:cd11026   1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYG--VVFSNGERWKQLRR------FSLTTLR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 144 DF----KHVR---QEEVGTLTRELVRVGTKPVNLGQLVNMCVVNalgreMIGRRLFGADADHKADEFRSMVT---EMMAL 213
Cdd:cd11026  73 NFgmgkRSIEeriQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSN-----VICSIVFGSRFDYEDKEFLKLLDlinENLRL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 214 AG-----VFNIgdFVPSLDWLdlQGVAGKMKRLHKRFDAFLSSILKEHEMN---GQDQKHTDMLstLISLKGTDLDGDGg 285
Cdd:cd11026 148 LSspwgqLYNM--FPPLLKHL--PGPHQKLFRNVEEIKSFIRELVEEHRETldpSSPRDFIDCF--LLKMEKEKDNPNS- 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 286 SLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHP 365
Cdd:cd11026 221 EFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGD 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 366 PTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGAGRRIC 445
Cdd:cd11026 301 IVPLGVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFL---DEQGKFKKNEAF--MPFSAGKRVC 375
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 15241483 446 AGLSLGlRTIQFL-TATLVQGFDweLAGGVTPEKLNME-ESYGLTLQ 490
Cdd:cd11026 376 LGEGLA-RMELFLfFTSLLQRFS--LSSPVGPKDPDLTpRFSGFTNS 419
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
55-497 4.59e-60

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: 203.58  E-value: 4.59e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  55 RTLSAMVTTYGPILHLRL-GFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKhmaynyqdLVFAPYG--------HRW 125
Cdd:cd11053   2 GFLERLRARYGDVFTLRVpGLGPVVVLSDPEAIKQIFTADPDVLHPGEGNSLLE--------PLLGPNSlllldgdrHRR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 126 RllRKISsVHLFSAKALEDFKHVRQEEVGTLTRELvRVGtKPVNLGQLVNmcvvnALGREMIGRRLFGADADHKADEFRS 205
Cdd:cd11053  74 R--RKLL-MPAFHGERLRAYGELIAEITEREIDRW-PPG-QPFDLRELMQ-----EITLEVILRVVFGVDDGERLQELRR 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 206 MVTEMMALAGvfNIGDFVPSLdWLDLQGVA--GKMKRLHKRFDAFLSSILKEHEMNGqDQKHTDMLSTLISLKgtdlDGD 283
Cdd:cd11053 144 LLPRLLDLLS--SPLASFPAL-QRDLGPWSpwGRFLRARRRIDALIYAEIAERRAEP-DAERDDILSLLLSAR----DED 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 284 GGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPvneSDIAQLPYLQAVIKENFRL 363
Cdd:cd11053 216 GQPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDP---EDIAKLPYLDAVIKETLRL 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 364 HPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggeksgvDVKGSDFELIPFGAGRR 443
Cdd:cd11053 293 YPVAPL-VPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFL--------GRKPSPYEYLPFGGGVR 363
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15241483 444 ICAGLSLGLRTIQFLTATLVQGFDWELAGGVtPEKLNmeeSYGLTL--QRAVPLVV 497
Cdd:cd11053 364 RCIGAAFALLEMKVVLATLLRRFRLELTDPR-PERPV---RRGVTLapSRGVRMVV 415
PTZ00404 PTZ00404
cytochrome P450; Provisional
5-492 5.46e-59

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 202.65  E-value: 5.46e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    5 FLTILLATVLFLILRIFSHRRNRSHNNRLPpGPNPWPIIGNLPHMGTKPHRTLSAMVTTYGPILhlRLGFVD---VVVAA 81
Cdd:PTZ00404   3 LFNIILFLFIFYIIHNAYKKYKKIHKNELK-GPIPIPILGNLHQLGNLPHRDLTKMSKKYGGIF--RIWFADlytVVLSD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   82 SKSVAEQFLKIHDaNFASRPPNSGAKHMAYnYQDLVfAPYGHRWRLLRKIssvhLFSAKALEDFKHVRQ---EEVGTLTR 158
Cdd:PTZ00404  80 PILIREMFVDNFD-NFSDRPKIPSIKHGTF-YHGIV-TSSGEYWKRNREI----VGKAMRKTNLKHIYDlldDQVDVLIE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  159 EL--VRVGTKPVNLGQLVNMCVVNALGReMIGRRLFGADAD-HKADEFRSM--VTEMMALAGVFNIGDFV-----PSLDW 228
Cdd:PTZ00404 153 SMkkIESSGETFEPRYYLTKFTMSAMFK-YIFNEDISFDEDiHNGKLAELMgpMEQVFKDLGSGSLFDVIeitqpLYYQY 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  229 LDLQGvaGKMKRLHKrfdaFLSSILKEHEMNGQDQKHTDMLSTLISLKGTDLDGDGGSLTDTeikalLLNMFTAGTDTSA 308
Cdd:PTZ00404 232 LEHTD--KNFKKIKK----FIKEKYHEHLKTIDPEVPRDLLDLLIKEYGTNTDDDILSILAT-----ILDFFLAGVDTSA 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  309 STVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEI-NGYHIP 387
Cdd:PTZ00404 301 TSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFGLPRSTSNDIIIgGGHFIP 380
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  388 KGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggeksGVDvkgSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFD 467
Cdd:PTZ00404 381 KDAQILINYYSLGRNEKYFENPEQFDPSRFL------NPD---SNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFK 451
                        490       500
                 ....*....|....*....|....*
gi 15241483  468 WELAGGvtpEKLNMEESYGLTLQRA 492
Cdd:PTZ00404 452 LKSIDG---KKIDETEEYGLTLKPN 473
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
64-490 6.89e-57

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: 195.62  E-value: 6.89e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAyNYQDLVFAP-YGHRWRLLRKI--SSVHLFSAK 140
Cdd:cd20676   1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRPDLYSFRFIS-DGQSLTFSTdSGPVWRARRKLaqNALKTFSIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 141 ---------ALEDfkHVRQEE---VGTLTRELVRVGT-KPVNlgQLVnMCVVNalgreMIGRRLFGADADHKADEFRSMV 207
Cdd:cd20676  80 ssptsssscLLEE--HVSKEAeylVSKLQELMAEKGSfDPYR--YIV-VSVAN-----VICAMCFGKRYSHDDQELLSLV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 208 T---EMMALAGVFNIGDFVPSLDWLDLQGVAgKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLI--SLKGTDLDG 282
Cdd:cd20676 150 NlsdEFGEVAGSGNPADFIPILRYLPNPAMK-RFKDINKRFNSFLQKIVKEHYQTFDKDNIRDITDSLIehCQDKKLDEN 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 283 DGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFR 362
Cdd:cd20676 229 ANIQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFR 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 363 LHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFL--PGGEKSGVDvkgSDFELIpFGA 440
Cdd:cd20676 309 HSSFVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLtaDGTEINKTE---SEKVML-FGL 384
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 15241483 441 GRRICAGLSLGLRTIQFLTATLVQGFDWELAGGvtpEKLNMEESYGLTLQ 490
Cdd:cd20676 385 GKRRCIGESIARWEVFLFLAILLQQLEFSVPPG---VKVDMTPEYGLTMK 431
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
64-501 1.63e-55

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: 191.76  E-value: 1.63e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPP------NSGAKHMAynyqdlvFAPYGHRWRLLRKI--SSVH 135
Cdd:cd20675   1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDfasfrvVSGGRSLA-------FGGYSERWKAHRRVahSTVR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 136 LFSA------KALEdfKHVRQEevgtlTRELVRV------GTKPVNLGQLVNMCVVNALGREMIGRRLfgadaDHKADEF 203
Cdd:cd20675  74 AFSTrnprtrKAFE--RHVLGE-----ARELVALflrksaGGAYFDPAPPLVVAVANVMSAVCFGKRY-----SHDDAEF 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 204 RSMVTEMMALAGVFNIGDFVPSLDWLD-----LQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLISLKGT 278
Cdd:cd20675 142 RSLLGRNDQFGRTVGAGSLVDVMPWLQyfpnpVRTVFRNFKQLNREFYNFVLDKVLQHRETLRGGAPRDMMDAFILALEK 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 279 DLDGDGGSLTDTE-IKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVI 357
Cdd:cd20675 222 GKSGDSGVGLDKEyVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFL 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 358 KENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFELIP 437
Cdd:cd20675 302 YEAMRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFL---DENGFLNKDLASSVMI 378
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15241483 438 FGAGRRICAGLSLGLRTIQFLTATLVQGFDWElagGVTPEKLNMEESYGLTLQravplvvhPKP 501
Cdd:cd20675 379 FSVGKRRCIGEELSKMQLFLFTSILAHQCNFT---ANPNEPLTMDFSYGLTLK--------PKP 431
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
122-489 6.97e-55

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: 190.04  E-value: 6.97e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 122 GHRWRLLRKISSvHLFSAKALEDFKHVRQEEVGTLTREL-VRVGTKPVNLGQLVNMCVVNALGREMIGRRLfgaDA-DHK 199
Cdd:cd20628  54 GEKWRKRRKLLT-PAFHFKILESFVEVFNENSKILVEKLkKKAGGGEFDIFPYISLCTLDIICETAMGVKL---NAqSNE 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 200 ADEFR---SMVTEMMaLAGVFNI---GDFVPSLDWLdlqgvAGKMKRLHKRFDAFLSSILKE---------HEMNGQDQ- 263
Cdd:cd20628 130 DSEYVkavKRILEII-LKRIFSPwlrFDFIFRLTSL-----GKEQRKALKVLHDFTNKVIKErreelkaekRNSEEDDEf 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 264 ---KHTDMLSTLIslkgtDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRD- 339
Cdd:cd20628 204 gkkKRKAFLDLLL-----EAHEDGGPLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDd 278
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 340 RPVNESDIAQLPYLQAVIKENFRLHPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLP 419
Cdd:cd20628 279 RRPTLEDLNKMKYLERVIKETLRLYPSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLP 357
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 420 ggEKSgvdVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFdwELAGGVTPEKLNMeeSYGLTL 489
Cdd:cd20628 358 --ENS---AKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNF--RVLPVPPGEDLKL--IAEIVL 418
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
64-473 1.04e-53

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: 186.82  E-value: 1.04e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAY--NYQDLVFAPYGHRWRLLRKissvhlFSAKA 141
Cdd:cd20663   1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFgpKSQGVVLARYGPAWREQRR------FSVST 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 142 LEDF----KHVRQ---EEVGTLTRELVRVGTKPVNLGQLVNMCVVNALGREMIGRRlFGADaDHKADEFRSMVTEMM--- 211
Cdd:cd20663  75 LRNFglgkKSLEQwvtEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARR-FEYE-DPRFIRLLKLLEESLkee 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 212 --ALAGVFNIgdfVPSLdwLDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKH----TD-MLSTLISLKGTDldgdG 284
Cdd:cd20663 153 sgFLPEVLNA---FPVL--LRIPGLAGKVFPGQKAFLALLDELLTEHRTTWDPAQPprdlTDaFLAEMEKAKGNP----E 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 285 GSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLH 364
Cdd:cd20663 224 SSFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFG 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 365 PPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGAGRRI 444
Cdd:cd20663 304 DIVPLGVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFL---DAQGHFVKPEAF--MPFSAGRRA 378
                       410       420       430
                ....*....|....*....|....*....|
gi 15241483 445 CAGLSLGlRTIQFLTAT-LVQGFDWELAGG 473
Cdd:cd20663 379 CLGEPLA-RMELFLFFTcLLQRFSFSVPAG 407
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
64-501 1.53e-53

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: 186.84  E-value: 1.53e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAyNYQDLVFAP-YGHRWRLLRKISSVHL--FS-- 138
Cdd:cd20677   1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPDFYTFSLIA-NGKSMTFSEkYGESWKLHKKIAKNALrtFSke 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 139 -AKA------LEDfkHVrQEEVGTLTRELVRVGTK-----PVNLGQLVNMCVVNALgremigrrLFGADADHKADEFRSM 206
Cdd:cd20677  80 eAKSstcsclLEE--HV-CAEASELVKTLVELSKEkgsfdPVSLITCAVANVVCAL--------CFGKRYDHSDKEFLTI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 207 V---TEMMALAGVFNIGDFVPSLDWLDLQGVAgKMKRLHKRFDAFLSSILKEHeMNGQDQKHT-DMLSTLISL-KGTDLD 281
Cdd:cd20677 149 VeinNDLLKASGAGNLADFIPILRYLPSPSLK-ALRKFISRLNNFIAKSVQDH-YATYDKNHIrDITDALIALcQERKAE 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 282 GDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENF 361
Cdd:cd20677 227 DKSAVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVF 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 362 RLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFELIPFGAG 441
Cdd:cd20677 307 RHSSFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFL---DENGQLNKSLVEKVLIFGMG 383
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 442 RRICAGLSLGLRTIQFLTATLVQGFDWElagGVTPEKLNMEESYGLTLQravplvvhPKP 501
Cdd:cd20677 384 VRKCLGEDVARNEIFVFLTTILQQLKLE---KPPGQKLDLTPVYGLTMK--------PKP 432
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
64-473 2.72e-52

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: 183.11  E-value: 2.72e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKiHDANFASRPPNSGAKHMA--YNYQDLVFAPYGHRWRLLRKISSVHLFSAKA 141
Cdd:cd11054   4 YGPIVREKLGGRDIVHLFDPDDIEKVFR-NEGKYPIRPSLEPLEKYRkkRGKPLGLLNSNGEEWHRLRSAVQKPLLRPKS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 142 LEDFKHvRQEEVGT-----LTRELVRVGTKPVNLGQLVNMCVVNALGREMIGRRL--FGADADHKADEFRSMVTEMMALa 214
Cdd:cd11054  83 VASYLP-AINEVADdfverIRRLRDEDGEEVPDLEDELYKWSLESIGTVLFGKRLgcLDDNPDSDAQKLIEAVKDIFES- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 215 gvFNIGDFVPSL-------DWldlqgvagkmKRLHKRFDAFLSSILK--------EHEMNGQDQKHTDMLSTLISLKGtd 279
Cdd:cd11054 161 --SAKLMFGPPLwkyfptpAW----------KKFVKAWDTIFDIASKyvdealeeLKKKDEEDEEEDSLLEYLLSKPG-- 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 280 ldgdggsLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKE 359
Cdd:cd11054 227 -------LSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKE 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 360 NFRLHPPTPlSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDvkgSDFELIPFG 439
Cdd:cd11054 300 SLRLYPVAP-GNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENKNI---HPFASLPFG 375
                       410       420       430
                ....*....|....*....|....*....|....
gi 15241483 440 AGRRICAGLSLGLRTIQFLTATLVQGFDWELAGG 473
Cdd:cd11054 376 FGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHE 409
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
47-500 2.64e-51

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: 179.70  E-value: 2.64e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  47 PHMGTKPHRTLSAMvTTYGPILHLRLGFVDVVVAASKSVAEQFLKiHDANFASRPPNSGAKHMAYNYQDLVFAPYGHRWR 126
Cdd:COG2124  15 PAFLRDPYPFYARL-REYGPVFRVRLPGGGAWLVTRYEDVREVLR-DPRTFSSDGGLPEVLRPLPLLGDSLLTLDGPEHT 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 127 LLRKISSvHLFSAKALEDFKHVRQEEVGTLTRELVRVGTkpvnlgqlvnMCVVNALGR---EMIGRRLFGADADHkADEF 203
Cdd:COG2124  93 RLRRLVQ-PAFTPRRVAALRPRIREIADELLDRLAARGP----------VDLVEEFARplpVIVICELLGVPEED-RDRL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 204 RSMVTEMMALAGVFNIGDFvpsldwldlqgvaGKMKRLHKRFDAFLSSILKEHEMNGQDqkhtDMLSTLISLKGtdldgD 283
Cdd:COG2124 161 RRWSDALLDALGPLPPERR-------------RRARRARAELDAYLRELIAERRAEPGD----DLLSALLAARD-----D 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 284 GGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELdivvgrdrpvnesdiaqlPYLQAVIKENFRL 363
Cdd:COG2124 219 GERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRL 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 364 HPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERflpggeksgvdvkgSDFELIPFGAGRR 443
Cdd:COG2124 281 YPPVPL-LPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR--------------PPNAHLPFGGGPH 345
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241483 444 ICAGLSLGLRTIQFLTATLVQGF-DWELAGgvtPEKLNMEESYGLTLQRAVPLVVHPK 500
Cdd:COG2124 346 RCLGAALARLEARIALATLLRRFpDLRLAP---PEELRWRPSLTLRGPKSLPVRLRPR 400
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
65-489 1.58e-50

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: 178.37  E-value: 1.58e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  65 GPILHLRLGFVDVVVAASKSVAEQFLKIHDanFASRPPNSgAKHMAYNYQDLVFAPyGHRWRLLRKISSVHLfSAKALED 144
Cdd:cd20652   1 GSIFSLKMGSVYTVVLSDPKLIRDTFRRDE--FTGRAPLY-LTHGIMGGNGIICAE-GDLWRDQRRFVHDWL-RQFGMTK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 145 FKHVRQ-------EEVGTLTRELVRVGTKPVNLGQLVNMCVVNALGREMIGRRlFGADaDHKADEFRSMVTEMMALAGVF 217
Cdd:cd20652  76 FGNGRAkmekriaTGVHELIKHLKAESGQPVDPSPVLMHSLGNVINDLVFGFR-YKED-DPTWRWLRFLQEEGTKLIGVA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 218 NIGDFVPSLDWL-DLQGVAGKMKRLHKRFDAFLSSILKEHE----MNGQDQKHTDMLSTLISLK--GTDLDGDGGSLTDT 290
Cdd:cd20652 154 GPVNFLPFLRHLpSYKKAIEFLVQGQAKTHAIYQKIIDEHKrrlkPENPRDAEDFELCELEKAKkeGEDRDLFDGFYTDE 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 291 EIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLS 370
Cdd:cd20652 234 QLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPLG 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 371 LPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGAGRRICAGLSL 450
Cdd:cd20652 314 IPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFL---DTDGKYLKPEAF--IPFQTGKRMCLGDEL 388
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 15241483 451 GlRTIQFL-TATLVQGFDWELAGGvTPEKLNMEESyGLTL 489
Cdd:cd20652 389 A-RMILFLfTARILRKFRIALPDG-QPVDSEGGNV-GITL 425
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
122-469 3.36e-49

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: 174.69  E-value: 3.36e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 122 GHRWRLLRKISSvHLFSAKALedfKHVrQEEVGTLTRELVRVGTKPVNLGQLVNMCVV-NALGREMIGRRLFGADADHKA 200
Cdd:cd11055  57 GERWKRLRTTLS-PTFSSGKL---KLM-VPIINDCCDELVEKLEKAAETGKPVDMKDLfQGFTLDVILSTAFGIDVDSQN 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 201 DEFRSMVtemMALAGVFNIGDF--------VPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQkHTDMLSTL 272
Cdd:cd11055 132 NPDDPFL---KAAKKIFRNSIIrlflllllFPLRLFLFLLFPFVFGFKSFSFLEDVVKKIIEQRRKNKSSR-RKDLLQLM 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 273 ISLKGTDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPY 352
Cdd:cd11055 208 LDAQDSDEDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKY 287
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 353 LQAVIKENFRLHPPTPLSLpHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKsgvdvKGSD 432
Cdd:cd11055 288 LDMVINETLRLYPPAFFIS-RECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKA-----KRHP 361
                       330       340       350
                ....*....|....*....|....*....|....*..
gi 15241483 433 FELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWE 469
Cdd:cd11055 362 YAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFV 398
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
64-471 1.48e-48

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: 172.85  E-value: 1.48e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRL-GFVDVVVAASKSVAEQFLKIHDANFASRPPNsgakhmaynYQDLvFAPY------GHRWRLLRKISSVHl 136
Cdd:cd11044  21 YGPVFKTHLlGRPTVFVIGAEAVRFILSGEGKLVRYGWPRS---------VRRL-LGENslslqdGEEHRRRRKLLAPA- 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 137 FSAKALEDFKHVRQEEVGTLTRELVRVGTkpvnlgqlvnMCVVNALGR---EMIGRRLFG----ADADHKADEFRSMVTE 209
Cdd:cd11044  90 FSREALESYVPTIQAIVQSYLRKWLKAGE----------VALYPELRRltfDVAARLLLGldpeVEAEALSQDFETWTDG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 210 MMALAGVFNIGDFVPSLdwldlqgVAGKmkRLHKRFDAFLSSILKEhemngQDQKHTDMLSTLISLKgtdlDGDGGSLTD 289
Cdd:cd11044 160 LFSLPVPLPFTPFGRAI-------RARN--KLLARLEQAIRERQEE-----ENAEAKDALGLLLEAK----DEDGEPLSM 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 290 TEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDiVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPL 369
Cdd:cd11044 222 DELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQD-ALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGG 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 370 SLpHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSgvdvKGSDFELIPFGAGRRICAGLS 449
Cdd:cd11044 301 GF-RKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSED----KKKPFSLIPFGGGPRECLGKE 375
                       410       420
                ....*....|....*....|..
gi 15241483 450 LGLRTIQFLTATLVQGFDWELA 471
Cdd:cd11044 376 FAQLEMKILASELLRNYDWELL 397
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
240-477 2.84e-48

cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 172.02  E-value: 2.84e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 240 RLHKRFDAFLSSILKEHEMNGqDQKHTDMLSTLISLKGTDldgdGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELI 319
Cdd:cd11042 166 RARAKLKEIFSEIIQKRRKSP-DKDEDDMLQTLMDAKYKD----GRPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELL 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 320 RHPDIMVKAQEELDIVVG-RDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASE-SCEINGYHIPKGSTLLTNIW 397
Cdd:cd11042 241 RNPEHLEALREEQKEVLGdGDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPfEVEGGGYVIPKGHIVLASPA 320
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 398 AIARDPDQWSDPLAFKPERFLPGGEksgVDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPE 477
Cdd:cd11042 321 VSHRDPEIFKNPDEFDPERFLKGRA---EDSKGGKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSPFPE 397
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
123-495 6.81e-48

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: 171.23  E-value: 6.81e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 123 HRwRLLRKISSVhlFSAKALEDFKHVRQEEVGTLTRELVR--VGTKPVNLGQLVNMCVVNALGREMIGRRlFG---ADAD 197
Cdd:cd11060  57 HA-ALRRKVASG--YSMSSLLSLEPFVDECIDLLVDLLDEkaVSGKEVDLGKWLQYFAFDVIGEITFGKP-FGfleAGTD 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 198 HkaDEFRSMVTEMMALAGVfnIGdFVPSLDWL---DLQGVAGKMKRLHKRFDAFLSSILKEH--EMNGQDQKHTDMLSTL 272
Cdd:cd11060 133 V--DGYIASIDKLLPYFAV--VG-QIPWLDRLllkNPLGPKRKDKTGFGPLMRFALEAVAERlaEDAESAKGRKDMLDSF 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 273 ISLKgtdlDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDR---PVNESDIAQ 349
Cdd:cd11060 208 LEAG----LKDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGKlssPITFAEAQK 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 350 LPYLQAVIKENFRLHPPTPLSLPHIASES-CEINGYHIPKGSTLLTNIWAIARDPDQWS-DPLAFKPERFLPGGEKSGVD 427
Cdd:cd11060 284 LPYLQAVIKEALRLHPPVGLPLERVVPPGgATICGRFIPGGTIVGVNPWVIHRDKEVFGeDADVFRPERWLEADEEQRRM 363
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241483 428 VKGSDFeliPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELaggVTPEKLNMEESYGLTLQRAVPL 495
Cdd:cd11060 364 MDRADL---TFGAGSRTCLGKNIALLELYKVIPELLRRFDFEL---VDPEKEWKTRNYWFVKQSDFDV 425
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
64-489 8.41e-48

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: 171.14  E-value: 8.41e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRpPNSGAKHMAYNYQDLVFApYGHRWRLLRKissvhlFSAKALE 143
Cdd:cd20664   1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGR-PIIPIFEDFNKGYGILFS-NGENWKEMRR------FTLTTLR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 144 DFKHVRQ-------EEVGTLTRELVRVGTKPVNLGQLVNMCVVNALGREMIGRRLfgADADHKADEFRSMVTEMMALAG- 215
Cdd:cd20664  73 DFGMGKKtsedkilEEIPYLIEVFEKHKGKPFETTLSMNVAVSNIIASIVLGHRF--EYTDPTLLRMVDRINENMKLTGs 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 216 -------VFNIGDFVPSldwlDLQGVAGKMKRLHkrfdaflsSILKEHEMNGQDQKHTDMLSTLIS---LKGTDLDGDGG 285
Cdd:cd20664 151 psvqlynMFPWLGPFPG----DINKLLRNTKELN--------DFLMETFMKHLDVLEPNDQRGFIDaflVKQQEEEESSD 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 286 SLTDTE-IKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNEsDIAQLPYLQAVIKENFRLH 364
Cdd:cd20664 219 SFFHDDnLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVE-HRKNMPYTDAVIHEIQRFA 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 365 PPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGAGRRI 444
Cdd:cd20664 298 NIVPMNLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFL---DSQGKFVKRDAF--MPFSAGRRV 372
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 15241483 445 CAGLSLGLRTIQFLTATLVQGFDWELAGGVTPEKLNMEESYGLTL 489
Cdd:cd20664 373 CIGETLAKMELFLFFTSLLQRFRFQPPPGVSEDDLDLTPGLGFTL 417
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
123-496 1.77e-46

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: 167.40  E-value: 1.77e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 123 HRWRllRKISSvHLFSAKALEDFKHVRQEEVGTLTRELVRVGTKPVnlGQLVNMCV-VNALGREMIGRRLFGADAD---- 197
Cdd:cd11061  54 HARR--RRVWS-HAFSDKALRGYEPRILSHVEQLCEQLDDRAGKPV--SWPVDMSDwFNYLSFDVMGDLAFGKSFGmles 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 198 HKADEFRSMVTEMMALAGVFNIGDFVPSLdWLDLQGVAGKMKRlHKRFDAFLSSILKEHeMNGQDQKHTDMLSTLIslkg 277
Cdd:cd11061 129 GKDRYILDLLEKSMVRLGVLGHAPWLRPL-LLDLPLFPGATKA-RKRFLDFVRAQLKER-LKAEEEKRPDIFSYLL---- 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 278 TDLDGDGGS-LTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELD-IVVGRDRPVNESDIAQLPYLQA 355
Cdd:cd11061 202 EAKDPETGEgLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDsTFPSDDEIRLGPKLKSLPYLRA 281
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 356 VIKENFRLHPPTPLSLPHIA-SESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPgGEKSGVDVKGSdfe 434
Cdd:cd11061 282 CIDEALRLSPPVPSGLPRETpPGGLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLS-RPEELVRARSA--- 357
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15241483 435 LIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPEKLnmEESYGLTLQRAVPLV 496
Cdd:cd11061 358 FIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPGEDGEAG--EGGFKDAFGRGPGDL 417
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
145-497 6.67e-44

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: 160.12  E-value: 6.67e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 145 FKHVRQEEVGTLTRELVRVGTKPVNLGQLVNMCVV-NALGREMIGRRLFGAD-ADHKADEFRSMVTEMMAlaGVFNIGDF 222
Cdd:cd11049  81 FHRSRIPAYAEVMREEAEALAGSWRPGRVVDVDAEmHRLTLRVVARTLFSTDlGPEAAAELRQALPVVLA--GMLRRAVP 158
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 223 VPSLDWLDLQGvagkmKRLHKRFDAFLSSILKE--HEMNGQDQKHTDMLSTLISLKgtdlDGDGGSLTDTEIKALLLNMF 300
Cdd:cd11049 159 PKFLERLPTPG-----NRRFDRALARLRELVDEiiAEYRASGTDRDDLLSLLLAAR----DEEGRPLSDEELRDQVITLL 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 301 TAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGrDRPVNESDIAQLPYLQAVIKENFRLHPPTPLsLPHIASESCE 380
Cdd:cd11049 230 TAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWL-LTRRTTADVE 307
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 381 INGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGgeKSGVDVKGSdfeLIPFGAGRRICAGLSLGLRTIQFLTA 460
Cdd:cd11049 308 LGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPG--RAAAVPRGA---FIPFGAGARKCIGDTFALTELTLALA 382
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 15241483 461 TLVQGFDWELAGGVTPeklnmEESYGLTLQ-RAVPLVV 497
Cdd:cd11049 383 TIASRWRLRPVPGRPV-----RPRPLATLRpRRLRMRV 415
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
64-471 7.95e-44

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: 160.51  E-value: 7.95e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLR--LGFVDVVVAASKSVAEqFLKIHDANFasrPPNSGAKHMAYN-YQDLVFAPYGHRWRLLRKISSvHLFSAK 140
Cdd:cd11069   1 YGGLIRYRglFGSERLLVTDPKALKH-ILVTNSYDF---EKPPAFRRLLRRiLGDGLLAAEGEEHKRQRKILN-PAFSYR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 141 ALEDFKHVRQEEVGTLTRELVR-VGTKPvnlGQLVNMCVVNALGR---EMIGRRLFGADADHKADE-------FRSMVTE 209
Cdd:cd11069  76 HVKELYPIFWSKAEELVDKLEEeIEESG---DESISIDVLEWLSRatlDIIGLAGFGYDFDSLENPdnelaeaYRRLFEP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 210 MMALAGVFNIGDFVPS--LDWLDLQgVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHT---DMLSTLisLKGTDLDGDG 284
Cdd:cd11069 153 TLLGSLLFILLLFLPRwlVRILPWK-ANREIRRAKDVLRRLAREIIREKKAALLEGKDDsgkDILSIL--LRANDFADDE 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 285 GsLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVV--GRDRPVNESDIAQLPYLQAVIKENFR 362
Cdd:cd11069 230 R-LSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALpdPPDGDLSYDDLDRLPYLNAVCRETLR 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 363 LHPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQW-SDPLAFKPERFLPGGEKSGVDVKGSDFELIPFGAG 441
Cdd:cd11069 309 LYPPVPL-TSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASPGGAGSNYALLTFLHG 387
                       410       420       430
                ....*....|....*....|....*....|
gi 15241483 442 RRICAGLSLGLRTIQFLTATLVQGFDWELA 471
Cdd:cd11069 388 PRSCIGKKFALAEMKVLLAALVSRFEFELD 417
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
64-489 1.35e-42

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: 156.88  E-value: 1.35e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMaYNYQDLVFAPyGHRWRLLRKISSVHL----FSA 139
Cdd:cd20662   1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERI-FNKNGLIFSS-GQTWKEQRRFALMTLrnfgLGK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 140 KALEDfkhvR-QEEVGTLTRELVRVGTKPVNLGQLVNMCVVNALGREMIGRRLFGADADHKadEFRSMVTEMMALAG--- 215
Cdd:cd20662  79 KSLEE----RiQEECRHLVEAIREEKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQ--ELLRLLDETVYLEGspm 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 216 --VFNIgdFVPSLDWLdlQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKHTDMLSTLIslkgTDLDGDGGSLTDTEIK 293
Cdd:cd20662 153 sqLYNA--FPWIMKYL--PGSHQTVFSNWKKLKLFVSDMIDKHREDWNPDEPRDFIDAYL----KEMAKYPDPTTSFNEE 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 294 ALL---LNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLS 370
Cdd:cd20662 225 NLIcstLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLN 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 371 LPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSgvdvKGSDFelIPFGAGRRICAGLSL 450
Cdd:cd20662 305 VPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQFK----KREAF--LPFSMGKRACLGEQL 378
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 15241483 451 GlRTIQFLTAT-LVQGFDWELAGGvtpEKLNMEESYGLTL 489
Cdd:cd20662 379 A-RSELFIFFTsLLQKFTFKPPPN---EKLSLKFRMGITL 414
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
254-481 6.68e-42

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: 155.02  E-value: 6.68e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 254 KEHEMNGQDQKHTDMLSTLISLKgtDLDGDGgsLTDTEIKalllN-----MFtAGTDTSASTVDWAIAELIRHPDIMVKA 328
Cdd:cd20659 194 DNKDEALSKRKYLDFLDILLTAR--DEDGKG--LTDEEIR----DevdtfLF-AGHDTTASGISWTLYSLAKHPEHQQKC 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 329 QEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPtplsLPHIA---SESCEINGYHIPKGSTLLTNIWAIARDPDQ 405
Cdd:cd20659 265 REEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPP----VPFIArtlTKPITIDGVTLPAGTLIAINIYALHHNPTV 340
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241483 406 WSDPLAFKPERFLPggEKSgvdvKGSD-FELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPEKLNM 481
Cdd:cd20659 341 WEDPEEFDPERFLP--ENI----KKRDpFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSVDPNHPVEPKPG 411
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
180-485 2.33e-41

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: 153.61  E-value: 2.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 180 NALGREMIGRRLFGADADHKADEFRSMVTEMMALAGVFNIGDFVPSL-DWLDLQGVAGKMKRLHKRFDAF----LSSILK 254
Cdd:cd11059 108 TALAMDVVSHLLFGESFGTLLLGDKDSRERELLRRLLASLAPWLRWLpRYLPLATSRLIIGIYFRAFDEIeewaLDLCAR 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 255 EHEMngQDQKHTDMLSTLISLKGTDLDGDGGsLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDI 334
Cdd:cd11059 188 AESS--LAESSDSESLTVLLLEKLKGLKKQG-LDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAG 264
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 335 VVGRDR-PVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIA-SESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAF 412
Cdd:cd11059 265 LPGPFRgPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLPRVVpEGGATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEF 344
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15241483 413 KPERFLPGGEKSGVDVKGSdfeLIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELaggVTPEKLNMEESY 485
Cdd:cd11059 345 DPERWLDPSGETAREMKRA---FWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTST---TTDDDMEQEDAF 411
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
64-473 1.14e-40

plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, cytochrome P450 family 90, subfamily B, polypeptide 1, and cytochrome P450 family 90, subfamily D, polypeptide 2; This family is composed of plant cytochrome P450s including: Arabidopsis thaliana cytochrome P450s 85A1 (CYP85A1 or brassinosteroid-6-oxidase 1), 90A1 (CYP90A1), 88A3 (CYP88A3 or ent-kaurenoic acid oxidase 1), 90B1 (CYP90B1 or Dwarf4 or steroid 22-alpha-hydroxylase), and 90C1 (CYP90C1 or 3-epi-6-deoxocathasterone 23-monooxygenase); Oryza sativa cytochrome P450s 90D2 (CYP90D2 or C6-oxidase), 87A3 (CYP87A3), and 724B1 (CYP724B1 or dwarf protein 11); and Taxus cuspidata cytochrome P450 725A2 (CYP725A2 or taxane 13-alpha-hydroxylase). These enzymes are monooxygenases that catalyze oxidation reactions involved in steroid or hormone biosynthesis. CYP85A1, CYP90D2, and CYP90C1 are involved in brassinosteroids biosynthesis, while CYP88A3 catalyzes three successive oxidations of ent-kaurenoic acid, which is a key step in the synthesis of gibberellins. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410669 [Multi-domain]  Cd Length: 408  Bit Score: 151.18  E-value: 1.14e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAynyQDLVFAPYGHRWRLLRKISSVHLFS----A 139
Cdd:cd11043   5 YGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWYPKSVRKLLG---KSSLLTVSGEEHKRLRGLLLSFLGPealkD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 140 KALEDFKHVRQEEVGTLTR---ELVRVGTKPVNLGQLVNMcvvnalgremigrrLFGADADHKADEFRSMVTEMMAlaGV 216
Cdd:cd11043  82 RLLGDIDELVRQHLDSWWRgksVVVLELAKKMTFELICKL--------------LLGIDPEEVVEELRKEFQAFLE--GL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 217 FNigdfVPsldwLDLQGVA-GKMKRLHKRFDAFLSSILKEHEMNG-QDQKHTDMLSTLISlkgtDLDGDGGSLTDTEIKA 294
Cdd:cd11043 146 LS----FP----LNLPGTTfHRALKARKRIRKELKKIIEERRAELeKASPKGDLLDVLLE----EKDEDGDSLTDEEILD 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 295 LLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEE-LDIVVGR--DRPVNESDIAQLPYLQAVIKENFRLHPPTPLSl 371
Cdd:cd11043 214 NILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEhEEIAKRKeeGEGLTWEDYKSMKYTWQVINETLRLAPIVPGV- 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 372 PHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFlpggEKSGVDVKGSdfeLIPFGAGRRICAGLSLG 451
Cdd:cd11043 293 FRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRW----EGKGKGVPYT---FLPFGGGPRLCPGAELA 365
                       410       420
                ....*....|....*....|..
gi 15241483 452 LRTIQFLTATLVQGFDWELAGG 473
Cdd:cd11043 366 KLEILVFLHHLVTRFRWEVVPD 387
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
121-447 1.54e-40

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: 151.26  E-value: 1.54e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 121 YGHRWRLLRKIssvhL---FSAKALEDFKHVRQEEVGTLTREL-VRVGTKPVNLGQLVNMCVVN-----ALGR------- 184
Cdd:cd20660  53 TGEKWHSRRKM----LtptFHFKILEDFLDVFNEQSEILVKKLkKEVGKEEFDIFPYITLCALDiicetAMGKsvnaqqn 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 185 -------------EMIGRR-------------LFGADADHKAD-----EF-RSMVTEMMALagvFNIGDFVPSLDwlDLQ 232
Cdd:cd20660 129 sdseyvkavyrmsELVQKRqknpwlwpdfiysLTPDGREHKKClkilhGFtNKVIQERKAE---LQKSLEEEEED--DED 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 233 GVAGKMKRLhkrfdAFLSSILKEHEmngqdqkhtdmlstlislkgtdldgDGGSLTDTEIKALLLN-MFTaGTDTSASTV 311
Cdd:cd20660 204 ADIGKRKRL-----AFLDLLLEASE-------------------------EGTKLSDEDIREEVDTfMFE-GHDTTAAAI 252
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 312 DWAIAELIRHPDIMVKAQEELDIVVG-RDRPVNESDIAQLPYLQAVIKENFRLHPptplSLPHIA---SESCEINGYHIP 387
Cdd:cd20660 253 NWALYLIGSHPEVQEKVHEELDRIFGdSDRPATMDDLKEMKYLECVIKEALRLFP----SVPMFGrtlSEDIEIGGYTIP 328
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 388 KGSTLLTNIWAIARDPDQWSDPLAFKPERFLPggEKSgvdVKGSDFELIPFGAGRRICAG 447
Cdd:cd20660 329 KGTTVLVLTYALHRDPRQFPDPEKFDPDRFLP--ENS---AGRHPYAYIPFSAGPRNCIG 383
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
122-480 5.86e-40

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: 149.61  E-value: 5.86e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 122 GHRWRLLRKISSvHLFSA---KALedFKHVrqEEVGtltRELVRVGTKPVNLGQLVNMC-VVNALGREMIGRRLFGADAD 197
Cdd:cd11056  58 GEKWKELRQKLT-PAFTSgklKNM--FPLM--VEVG---DELVDYLKKQAEKGKELEIKdLMARYTTDVIASCAFGLDAN 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 198 HKAD---EFRSMVTEMMA---LAGVFNIGDFV-PSL-DWLdlqgvagKMKRLHKRFDAFLSSILKE--HEMNGQDQKHTD 267
Cdd:cd11056 130 SLNDpenEFREMGRRLFEpsrLRGLKFMLLFFfPKLaRLL-------RLKFFPKEVEDFFRKLVRDtiEYREKNNIVRND 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 268 MLSTLISLKGTDL---DGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGR-DRPVN 343
Cdd:cd11056 203 FIDLLLELKKKGKiedDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKhGGELT 282
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 344 ESDIAQLPYLQAVIKENFRLHPPTPlSLPHIASESCEING--YHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGG 421
Cdd:cd11056 283 YEALQEMKYLDQVVNETLRKYPPLP-FLDRVCTKDYTLPGtdVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPEN 361
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 422 EKSGVdvkgsDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGG-VTPEKLN 480
Cdd:cd11056 362 KKKRH-----PYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKtKIPLKLS 416
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
126-472 2.75e-39

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: 147.79  E-value: 2.75e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 126 RLLRKISSvHLFSAKALEDFKHVRQEEVGTLTRELVR--VGTKPVNLGqlvnmCVVNALGREMIGRRLFGADAD-HKADE 202
Cdd:cd11062  56 RLRRKALS-PFFSKRSILRLEPLIQEKVDKLVSRLREakGTGEPVNLD-----DAFRALTADVITEYAFGRSYGyLDEPD 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 203 FRSMVTEMM-ALAGVFNIGDFVPSLDWL--DLQGVAGKMKRLH----KRFDAFLSSILKEHEMNGQDQKHTDMLSTLISL 275
Cdd:cd11062 130 FGPEFLDALrALAEMIHLLRHFPWLLKLlrSLPESLLKRLNPGlavfLDFQESIAKQVDEVLRQVSAGDPPSIVTSLFHA 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 276 kGTDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELD-IVVGRDRPVNESDIAQLPYLQ 354
Cdd:cd11062 210 -LLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKtAMPDPDSPPSLAELEKLPYLT 288
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 355 AVIKENFRLHPPTPLSLPHIASES-CEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKgsdf 433
Cdd:cd11062 289 AVIKEGLRLSYGVPTRLPRVVPDEgLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEKGKLDRY---- 364
                       330       340       350
                ....*....|....*....|....*....|....*....
gi 15241483 434 eLIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAG 472
Cdd:cd11062 365 -LVPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYE 402
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
63-473 3.41e-39

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: 147.90  E-value: 3.41e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  63 TYGPILHLRLGFVDVVVAASKSVAEQFLKihDANFASRPPNSGAKH-MAYNYQDLVFAPyGHRWRLlRKISSVHLFSAKA 141
Cdd:cd11046   9 EYGPIYKLAFGPKSFLVISDPAIAKHVLR--SNAFSYDKKGLLAEIlEPIMGKGLIPAD-GEIWKK-RRRALVPALHKDY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 142 LEDFKHVRQEEVGTLTRELVRVGTK--PVNLGQLvnMCVvnaLGREMIGRRLFGADADHKADE---FRSMVTEMM--ALA 214
Cdd:cd11046  85 LEMMVRVFGRCSERLMEKLDAAAETgeSVDMEEE--FSS---LTLDIIGLAVFNYDFGSVTEEspvIKAVYLPLVeaEHR 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 215 GVFNI--GDFVPSLDWLDLQGvagKMKRLHKRFDAFLSSILK-------EHEMNGQDQKHTDMLSTliSLKGTDLDGDGG 285
Cdd:cd11046 160 SVWEPpyWDIPAALFIVPRQR---KFLRDLKLLNDTLDDLIRkrkemrqEEDIELQQEDYLNEDDP--SLLRFLVDMRDE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 286 SLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHP 365
Cdd:cd11046 235 DVDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYP 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 366 PTPLsLPHIASESCEINGYH--IPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKgSDFELIPFGAGRR 443
Cdd:cd11046 315 QPPV-LIRRAVEDDKLPGGGvkVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNEVI-DDFAFLPFGGGPR 392
                       410       420       430
                ....*....|....*....|....*....|
gi 15241483 444 ICAGLSLGLRTIQFLTATLVQGFDWELAGG 473
Cdd:cd11046 393 KCLGDQFALLEATVALAMLLRRFDFELDVG 422
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
64-481 4.03e-39

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: 147.22  E-value: 4.03e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRppnsGAKHMAYNY---QDLVFAPyGHRWRLLRKissvhlFSAK 140
Cdd:cd20669   1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGR----GDYPVFFNFtkgNGIAFSN-GERWKILRR------FALQ 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 141 ALEDFKHVR-------QEEVGTLTRELVRVGTKPVNLGQLVNMCVVNalgreMIGRRLFGADADHKADEFRSMVT----- 208
Cdd:cd20669  70 TLRNFGMGKrsieeriLEEAQFLLEELRKTKGAPFDPTFLLSRAVSN-----IICSVVFGSRFDYDDKRLLTILNlindn 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 209 -EMMA--LAGVFNIgdFVPSLDWLdlqgvAGKMKRLHKRFDA---FLSSILKEHEMNGQDQKHTDMLSTLIslkgTDLDG 282
Cdd:cd20669 145 fQIMSspWGELYNI--FPSVMDWL-----PGPHQRIFQNFEKlrdFIAESVREHQESLDPNSPRDFIDCFL----TKMAE 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 283 DGGS-LTDTEIKALLL---NMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIK 358
Cdd:cd20669 214 EKQDpLSHFNMETLVMtthNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIH 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 359 ENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggeksgvDVKGSdFE---- 434
Cdd:cd20669 294 EIQRFADIIPMSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFL--------DDNGS-FKknda 364
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 15241483 435 LIPFGAGRRICAGLSLGLRTIQFLTATLVQGFdwELAGGVTPEKLNM 481
Cdd:cd20669 365 FMPFSAGKRICLGESLARMELFLYLTAILQNF--SLQPLGAPEDIDL 409
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
64-490 1.05e-38

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: 146.10  E-value: 1.05e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAYNyqDLVFAPYGHRWRLLRKissvhlFSAKALE 143
Cdd:cd20671   1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHG--NGVFFSSGERWRTTRR------FTVRSMK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 144 DFKHVRQ-------EEVGTLTRELVRVGTKPVNLGQLVnmCVVNALGREMigrrLFGADADHKADEFRS---MVTEMMAL 213
Cdd:cd20671  73 SLGMGKRtiedkilEELQFLNGQIDSFNGKPFPLRLLG--WAPTNITFAM----LFGRRFDYKDPTFVSlldLIDEVMVL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 214 AGVfnigdfvPSLDWLDLQGVAGKMKRLHK-------RFDAFLSSILKEHEMNGQDQKHTDMLSTLISlKGTDLDGDGGS 286
Cdd:cd20671 147 LGS-------PGLQLFNLYPVLGAFLKLHKpildkveEVCMILRTLIEARRPTIDGNPLHSYIEALIQ-KQEEDDPKETL 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 287 LTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPP 366
Cdd:cd20671 219 FHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITL 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 367 TPlSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGAGRRICA 446
Cdd:cd20671 299 LP-HVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFL---DAEGKFVKKEAF--LPFSAGRRVCV 372
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 15241483 447 GLSLGLRTIQFLTATLVQGFDWELAGGVTPEKLNMEESYGLTLQ 490
Cdd:cd20671 373 GESLARTELFIFFTGLLQKFTFLPPPGVSPADLDATPAAAFTMR 416
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
64-490 2.73e-38

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: 144.98  E-value: 2.73e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSgakhmayNYQDL-----VFAPYGHRWRLLRKISSVHL-- 136
Cdd:cd20667   1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTP-------FFRDLfgekgIICTNGLTWKQQRRFCMTTLre 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 137 --FSAKALEdfkHVRQEEVGTLTRELVRVGTKPVNLGQLVNMCVVNALGREMIGRRLFGADadhkaDEFRSMVTEM-MAL 213
Cdd:cd20667  74 lgLGKQALE---SQIQHEAAELVKVFAQENGRPFDPQDPIVHATANVIGAVVFGHRFSSED-----PIFLELIRAInLGL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 214 AGVFNI-GDFVPSLDWLdLQGVAGKMKRLHKRFDAFLSSILKE---HEMNGQDQKHtDMLSTLISLKGTDLDGDGGSLTD 289
Cdd:cd20667 146 AFASTIwGRLYDAFPWL-MRYLPGPHQKIFAYHDAVRSFIKKEvirHELRTNEAPQ-DFIDCYLAQITKTKDDPVSTFSE 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 290 TEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPL 369
Cdd:cd20667 224 ENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSV 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 370 SLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGAGRRICAGLS 449
Cdd:cd20667 304 GAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFL---DKDGNFVMNEAF--LPFSAGHRVCLGEQ 378
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 15241483 450 LGLRTIQFLTATLVQGFDWELAGGVTpeKLNMEESYGLTLQ 490
Cdd:cd20667 379 LARMELFIFFTTLLRTFNFQLPEGVQ--ELNLEYVFGGTLQ 417
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
76-495 4.90e-38

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: 144.27  E-value: 4.90e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  76 DVVVAASKSVAEQFLKihdANFASRPpnsGAKHMAYNYQDL----VFAPYGHRWRLLRKISSvHLFSAKALEDFkhvrqe 151
Cdd:cd11064  12 DGIVTADPANVEHILK---TNFDNYP---KGPEFRDLFFDLlgdgIFNVDGELWKFQRKTAS-HEFSSRALREF------ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 152 eVGTLTRELVRVGTKPV-----NLGQLVNMCVVnaLGREM---IGRRLFGADADHKADEF------RSMVTEMMALAGVF 217
Cdd:cd11064  79 -MESVVREKVEKLLVPLldhaaESGKVVDLQDV--LQRFTfdvICKIAFGVDPGSLSPSLpevpfaKAFDDASEAVAKRF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 218 NIGDFVPSL-DWLDLqGVAGKMKRLHKRFDAFLSSILKE-----HEMNGQDQKHTDMLSTLISLKgtdlDGDGGSLTDTE 291
Cdd:cd11064 156 IVPPWLWKLkRWLNI-GSEKKLREAIRVIDDFVYEVISRrreelNSREEENNVREDLLSRFLASE----EEEGEPVSDKF 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 292 IKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVV-----GRDRPVNESDIAQLPYLQAVIKENFRLHPP 366
Cdd:cd11064 231 LRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLpklttDESRVPTYEELKKLVYLHAALSESLRLYPP 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 367 TPLS---------LPhiasesceiNGYHIPKGSTLLTNIWAIARDPDQW-SDPLAFKPERFLpggEKSGVDVKGSDFELI 436
Cdd:cd11064 311 VPFDskeavnddvLP---------DGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWL---DEDGGLRPESPYKFP 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15241483 437 PFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGvtpekLNMEESYGLTLQRAVPL 495
Cdd:cd11064 379 AFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPG-----HKVEPKMSLTLHMKGGL 432
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
66-469 6.64e-38

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: 144.13  E-value: 6.64e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  66 PILHLRLGFVDVVVAASKSVAEQFLkihdanfasrppnSGAKHM--AYNYQDL-------VFAPYGHRWRLLRKISSvHL 136
Cdd:cd20680  13 PLLKLWIGPVPFVILYHAENVEVIL-------------SSSKHIdkSYLYKFLhpwlgtgLLTSTGEKWRSRRKMLT-PT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 137 FSAKALEDFKHVRQEEVGTLTRELVR-VGTKPVNLGQLVNMCVVNALGREMIGRRLfGADADHKADEFRSmvtemmalag 215
Cdd:cd20680  79 FHFTILSDFLEVMNEQSNILVEKLEKhVDGEAFNCFFDITLCALDIICETAMGKKI-GAQSNKDSEYVQA---------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 216 VFNIGDFV------PSLdWLDLQGVAGKMKRLHKR----FDAFLSSILKE--HEMNGQDQKHTDMLSTLIS--------- 274
Cdd:cd20680 148 VYRMSDIIqrrqkmPWL-WLDLWYLMFKEGKEHNKnlkiLHTFTDNVIAEraEEMKAEEDKTGDSDGESPSkkkrkafld 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 275 --LKGTDLDGDGGSLTDT--EIKALllnMFTaGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGR-DRPVNESDIAQ 349
Cdd:cd20680 227 mlLSVTDEEGNKLSHEDIreEVDTF---MFE-GHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKsDRPVTMEDLKK 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 350 LPYLQAVIKENFRLHPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKsgvdvK 429
Cdd:cd20680 303 LRYLECVIKESLRLFPSVPL-FARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSS-----G 376
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 15241483 430 GSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWE 469
Cdd:cd20680 377 RHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVE 416
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
64-466 1.48e-37

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: 143.22  E-value: 1.48e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPpnsgakhMAYNYQDLVFA---------PYGHRWRLLRKISSV 134
Cdd:cd11066   1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRP-------TFYTFHKVVSStqgftigtsPWDESCKRRRKAAAS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 135 HLfSAKALEDFKHVRQEEVGTLTRELVRV---GTKPVNLGQLVNMCVVNALGREMIGRRLFGADADHKADE--------- 202
Cdd:cd11066  74 AL-NRPAVQSYAPIIDLESKSFIRELLRDsaeGKGDIDPLIYFQRFSLNLSLTLNYGIRLDCVDDDSLLLEiievesais 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 203 -FRSMVTemmalagvfNIGDFVPSLDWLDLQGvAGKMKRLH--KRFDAFLSSIL---KEHEMNGQDQKhtdmlstliSLK 276
Cdd:cd11066 153 kFRSTSS---------NLQDYIPILRYFPKMS-KFRERADEyrNRRDKYLKKLLaklKEEIEDGTDKP---------CIV 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 277 GTDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHP--DIMVKAQEELDIVVGRDRPVNESDIA--QLPY 352
Cdd:cd11066 214 GNILKDKESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWEDCAAeeKCPY 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 353 LQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFL--PGGEKSGVDVKG 430
Cdd:cd11066 294 VVALVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLdaSGDLIPGPPHFS 373
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 15241483 431 sdfelipFGAGRRICAGLSLGLRTIQFLTATLVQGF 466
Cdd:cd11066 374 -------FGAGSRMCAGSHLANRELYTAICRLILLF 402
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
53-490 4.79e-37

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: 141.88  E-value: 4.79e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  53 PHRTLSAMVTTYGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAyNYQDLVFAPYGHRWRLLRKIS 132
Cdd:cd20661   1 PHVYMKKQSQIHGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLT-NMGGLLNSKYGRGWTEHRKLA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 133 sVHLFS--AKALEDFKHVRQEEVGTLTRELVRVGTKPVNLGQLVNMCVVNALGREMIGRRLFGADAD--HKADEFRSMVt 208
Cdd:cd20661  80 -VNCFRyfGYGQKSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDfqHMIEIFSENV- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 209 EMMALAGVFNIGDFvPSLDWLDLqgvaGKMKRLHKR----FDaFLSSILKEHEMNGQDQKHTDMLSTLISlkgtDLDGDG 284
Cdd:cd20661 158 ELAASAWVFLYNAF-PWIGILPF----GKHQQLFRNaaevYD-FLLRLIERFSENRKPQSPRHFIDAYLD----EMDQNK 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 285 GSLTDTEIKALLL----NMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKEN 360
Cdd:cd20661 228 NDPESTFSMENLIfsvgELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEV 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 361 FRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGA 440
Cdd:cd20661 308 LRFCNIVPLGIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFL---DSNGQFAKKEAF--VPFSL 382
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 15241483 441 GRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPeklNMEESYGLTLQ 490
Cdd:cd20661 383 GRRHCLGEQLARMEMFLFFTALLQRFHLHFPHGLIP---DLKPKLGMTLQ 429
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
128-473 5.22e-37

cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 141.18  E-value: 5.22e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 128 LRKISSvHLFSAKALEDFKHVRQEEVGTL---TRELVRVGTkPVNLGQLVNMCVVNALGREMIGRRlFGADADHKADEFR 204
Cdd:cd11058  61 LRRLLA-HAFSEKALREQEPIIQRYVDLLvsrLRERAGSGT-PVDMVKWFNFTTFDIIGDLAFGES-FGCLENGEYHPWV 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 205 SMVTEMMALAGVFNIGDFVPSLDWLDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQKhtDMLSTLIslkgtDLDGDG 284
Cdd:cd11058 138 ALIFDSIKALTIIQALRRYPWLLRLLRLLIPKSLRKKRKEHFQYTREKVDRRLAKGTDRP--DFMSYIL-----RNKDEK 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 285 GSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELdivvgRDRPVNESDI-----AQLPYLQAVIKE 359
Cdd:cd11058 211 KGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEI-----RSAFSSEDDItldslAQLPYLNAVIQE 285
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 360 NFRLHPPTPLSLPHIA-SESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGV-DVKGSdfeLIP 437
Cdd:cd11058 286 ALRLYPPVPAGLPRVVpAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFDnDKKEA---FQP 362
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 15241483 438 FGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGG 473
Cdd:cd11058 363 FSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPE 398
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
279-490 2.12e-36

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: 139.76  E-value: 2.12e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 279 DLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDR-PVNESDIAQLPYLQAVI 357
Cdd:cd11083 210 AEDDPDARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARvPPLLEALDRLPYLEAVA 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 358 KENFRLHPPTPLslphIASESCE---INGYHIPKGST--LLTNiwAIARDPDQWSDPLAFKPERFLPGGEKSgvdVKGSD 432
Cdd:cd11083 290 RETLRLKPVAPL----LFLEPNEdtvVGDIALPAGTPvfLLTR--AAGLDAEHFPDPEEFDPERWLDGARAA---EPHDP 360
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241483 433 FELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPEKlnmeESYGLTLQ 490
Cdd:cd11083 361 SSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPEPAPAVG----EEFAFTMS 414
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
238-467 4.24e-36

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: 138.93  E-value: 4.24e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 238 MKRLhKRFDAFLSSI----LKEHEMNGQDQKHTDMLSTLISLKGTDLDGDggsLTDTEIKALLLNMFTAGTDTSASTVDW 313
Cdd:cd20621 176 QKRV-KELRQFIEKIiqnrIKQIKKNKDEIKDIIIDLDLYLLQKKKLEQE---ITKEEIIQQFITFFFAGTDTTGHLVGM 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 314 AIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLL 393
Cdd:cd20621 252 CLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVN 331
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15241483 394 TNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGAGRRICAGLSLGLRTIQFLTATLVQGFD 467
Cdd:cd20621 332 VGYIYNHFNPKYFENPDEFNPERWL---NQNNIEDNPFVF--IPFSAGPRNCIGQHLALMEAKIILIYILKNFE 400
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
257-470 4.68e-36

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: 138.81  E-value: 4.68e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 257 EMNGQDQKHTDMLSTLISLKGTDLDGDGGSLTDteikaLLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVV 336
Cdd:cd20613 205 ALKRGEEVPNDILTHILKASEEEPDFDMEELLD-----DFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVL 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 337 GRDRPVNESDIAQLPYLQAVIKENFRLHPPTPlSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPER 416
Cdd:cd20613 280 GSKQYVEYEDLGKLEYLSQVLKETLRLYPPVP-GTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPER 358
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15241483 417 FLPGGEKsgvdvKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWEL 470
Cdd:cd20613 359 FSPEAPE-----KIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFEL 407
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
64-466 9.14e-36

cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of rats and rabbits and may have important functions for the olfactory chemosensory system. It is involved in the metabolism of sex steroids and xenobiotic compounds. In cynomolgus monkeys, CYP2G2 is a functional drug-metabolizing enzyme in nasal mucosa. In humans, two different CYP2G genes, CYP2GP1 and CYP2GP2, are pseudogenes because of loss-of-function deletions/mutations. The CYP2G subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 138.13  E-value: 9.14e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAKHmayNYQDLVFA-PYGHRWRLLRKissvhlFSAKAL 142
Cdd:cd20670   1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIER---NFQGHGVAlANGERWRILRR------FSLTIL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 143 EDFKHVR-------QEEVGTLTRELVRVGTKPVNLGQLVNMCVVNalgreMIGRRLFGADADHKADEFRSMV-------T 208
Cdd:cd20670  72 RNFGMGKrsieeriQEEAGYLLEEFRKTKGAPIDPTFFLSRTVSN-----VISSVVFGSRFDYEDKQFLSLLrminesfI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 209 EM-MALAGVFNigdfvpsLDWLDLQGVAGKMKRLH---KRFDAFLSSILKEHEMNGQDQKHTDMLSTLISLKGTDldgDG 284
Cdd:cd20670 147 EMsTPWAQLYD-------MYSGIMQYLPGRHNRIYyliEELKDFIASRVKINEASLDPQNPRDFIDCFLIKMHQD---KN 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 285 GSLTDTEIKALLL---NMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENF 361
Cdd:cd20670 217 NPHTEFNLKNLVLttlNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQ 296
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 362 RLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGAG 441
Cdd:cd20670 297 RLTDIVPLGVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFL---DEQGRFKKNEAF--VPFSSG 371
                       410       420
                ....*....|....*....|....*
gi 15241483 442 RRICAGLSLGLRTIQFLTATLVQGF 466
Cdd:cd20670 372 KRVCLGEAMARMELFLYFTSILQNF 396
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
63-470 2.13e-35

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: 137.08  E-value: 2.13e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  63 TYGPILHLRLGFVDVVVAASKSVAEQFLKIHDanFAsRPPNSgAKHMAYnYQDLVFAPYGHRWRLLRKISSVHLFSAKAL 142
Cdd:cd11070   1 KLGAVKILFVSRWNILVTKPEYLTQIFRRRDD--FP-KPGNQ-YKIPAF-YGPNVISSEGEDWKRYRKIVAPAFNERNNA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 143 EDFKH-VRQEE--VGTLTRELVRVGTKPVNLGQLVNMCVVNALGREMIGRRlFGADadhKADEFRSMVTEM----MALAG 215
Cdd:cd11070  76 LVWEEsIRQAQrlIRYLLEEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFD-LPAL---DEEESSLHDTLNaiklAIFPP 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 216 VFNIGDFVPSLDWLDLQgvagKMKRLHKRFDAFLSSIL------KEHEMNGQDQKHTDMLSTLISlkgtdlDGDGGSLTD 289
Cdd:cd11070 152 LFLNFPFLDRLPWVLFP----SRKRAFKDVDEFLSELLdeveaeLSADSKGKQGTESVVASRLKR------ARRSGGLTE 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 290 TEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNES--DIAQLPYLQAVIKENFRLHPPT 367
Cdd:cd11070 222 KELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYeeDFPKLPYLLAVIYETLRLYPPV 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 368 PLsLPHIASESCEI-----NGYHIPKGSTLLTNIWAIARDPDQW-SDPLAFKPERFLPGGEKSGVD-----VKGSdfeLI 436
Cdd:cd11070 302 QL-LNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSGEIGAAtrftpARGA---FI 377
                       410       420       430
                ....*....|....*....|....*....|....*.
gi 15241483 437 PFGAGRRICAGLSLGLrtIQFLT--ATLVQGFDWEL 470
Cdd:cd11070 378 PFSAGPRACLGRKFAL--VEFVAalAELFRQYEWRV 411
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
116-466 4.32e-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: 133.50  E-value: 4.32e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 116 LVFAPYgHRWRLLRKissvHL---FSAKALEDFKHVRQEEVGTLTRELVR-VGTKPVNLGQLVNMCV-----VNALGREM 186
Cdd:cd11057  47 LFSAPY-PIWKLQRK----ALnpsFNPKILLSFLPIFNEEAQKLVQRLDTyVGGGEFDILPDLSRCTlemicQTTLGSDV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 187 IGRRLFGADADHKADEFRSMVTEMMALAGVFNigDFVPSL--DWLDLQgvagkmkRLHKRFDAFLSSILK----EHEMNG 260
Cdd:cd11057 122 NDESDGNEEYLESYERLFELIAKRVLNPWLHP--EFIYRLtgDYKEEQ-------KARKILRAFSEKIIEkklqEVELES 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 261 QDQKHTDMLS-----TLISLKgTDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIV 335
Cdd:cd11057 193 NLDSEEDEENgrkpqIFIDQL-LELARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEV 271
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 336 VGRDRPVNE-SDIAQLPYLQAVIKENFRLHPPTPLsLPHIASESCEI-NGYHIPKGSTLLTNIWAIARDPDQW-SDPLAF 412
Cdd:cd11057 272 FPDDGQFITyEDLQQLVYLEMVLKETMRLFPVGPL-VGRETTADIQLsNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQF 350
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 15241483 413 KPERFLPggEKSGvdvKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGF 466
Cdd:cd11057 351 DPDNFLP--ERSA---QRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNY 399
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
64-466 9.10e-34

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: 132.39  E-value: 9.10e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRPPNSGAkHMAYNYQDLVFApYGHRWRLLRKISSVHLFS----A 139
Cdd:cd20665   1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIF-EKVNKGLGIVFS-NGERWKETRRFSLMTLRNfgmgK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 140 KALEDfkhvR-QEEVGTLTRELVRVGTKPVNLGQLVNMCVVNalgreMIGRRLFGADADHKADEFRS---MVTEMMALAG 215
Cdd:cd20665  79 RSIED----RvQEEARCLVEELRKTNGSPCDPTFILGCAPCN-----VICSIIFQNRFDYKDQDFLNlmeKLNENFKILS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 216 -----VFNigdFVPSLdwldLQGVAGKMKRLHKRFD---AFLSSILKEHE-----MNGQD-----------QKHT-DMLS 270
Cdd:cd20665 150 spwlqVCN---NFPAL----LDYLPGSHNKLLKNVAyikSYILEKVKEHQesldvNNPRDfidcflikmeqEKHNqQSEF 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 271 TLISLKGTdldgdggsltdteikalLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQL 350
Cdd:cd20665 223 TLENLAVT-----------------VTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHM 285
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 351 PYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGvDVKG 430
Cdd:cd20665 286 PYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFL---DENG-NFKK 361
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 15241483 431 SDFeLIPFGAGRRICAGLSLG-LRTIQFLTaTLVQGF 466
Cdd:cd20665 362 SDY-FMPFSAGKRICAGEGLArMELFLFLT-TILQNF 396
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
53-502 1.91e-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: 131.54  E-value: 1.91e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  53 PHRTLSAMVTTYGPILHLRLGFVDVVVAASKS-VAEqflkIHDANFASRPPNSGAKHMAYNYQDLVFAPYGHR--W---- 125
Cdd:cd11068   1 PVQSLLRLADELGPIFKLTLPGRRVVVVSSHDlIAE----LCDESRFDKKVSGPLEELRDFAGDGLFTAYTHEpnWgkah 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 126 RLLrkissVHLFSAKALEDFKHVRQEEVGTLTRELVRVG-TKPVNLGqlVNMcvvNALGREMIGRRLFGADAD-HKADEF 203
Cdd:cd11068  77 RIL-----MPAFGPLAMRGYFPMMLDIAEQLVLKWERLGpDEPIDVP--DDM---TRLTLDTIALCGFGYRFNsFYRDEP 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 204 RSMVTEMM-ALAGVFNIGDFVPSLDWLdlqgvagkMKRLHKRFD---AFLSS----ILKEHEMNGqDQKHTDMLSTLisL 275
Cdd:cd11068 147 HPFVEAMVrALTEAGRRANRPPILNKL--------RRRAKRQFRediALMRDlvdeIIAERRANP-DGSPDDLLNLM--L 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 276 KGTDLDgDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNEsDIAQLPYLQA 355
Cdd:cd11068 216 NGKDPE-TGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPPPYE-QVAKLRYIRR 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 356 VIKENFRLHPPTPLSLPHiASESCEING-YHIPKGSTLLTNIWAIARDPDQW-SDPLAFKPERFLPGGeksgvdvkgsdF 433
Cdd:cd11068 294 VLDETLRLWPTAPAFARK-PKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEE-----------F 361
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 434 ELI------PFGAGRRICAGLSLGLRTIQFLTATLVQGFDwelaggvtpekLNMEESYGLTLQRAV---P--LVVHPKPR 502
Cdd:cd11068 362 RKLppnawkPFGNGQRACIGRQFALQEATLVLAMLLQRFD-----------FEDDPDYELDIKETLtlkPdgFRLKARPR 430
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
238-489 7.87e-32

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: 126.90  E-value: 7.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 238 MKRLHKRFDAFLSSIL--KEHEMNGQDQKHTDMLSTLISlKGTDLdgdggsltdTEIKALLLNMFTAGTDTSASTVDWAI 315
Cdd:cd11063 171 CKVVHRFVDPYVDKALarKEESKDEESSDRYVFLDELAK-ETRDP---------KELRDQLLNILLAGRDTTASLLSFLF 240
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 316 AELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPL---------SLPHiasesceinG--- 383
Cdd:cd11063 241 YELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLnsrvavrdtTLPR---------Gggp 311
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 384 -----YHIPKGSTLLTNIWAIARDPDQW-SDPLAFKPERFLPGGEKSgvdvkgsdFELIPFGAGRRICAGLSLGLRTIQF 457
Cdd:cd11063 312 dgkspIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWEDLKRPG--------WEYLPFNGGPRICLGQQFALTEASY 383
                       250       260       270
                ....*....|....*....|....*....|..
gi 15241483 458 LTATLVQGFDWELAGGVTPeklnMEESYGLTL 489
Cdd:cd11063 384 VLVRLLQTFDRIESRDVRP----PEERLTLTL 411
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
245-469 9.06e-32

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: 126.76  E-value: 9.06e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 245 FDAFLSSILKEHEmnGQDQKH-TDMLSTLISLKGTDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPD 323
Cdd:cd20650 183 FYKSVKKIKESRL--DSTQKHrVDFLQLMIDSQNSKETESHKALSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPD 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 324 IMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPlSLPHIASESCEINGYHIPKGSTLLTNIWAIARDP 403
Cdd:cd20650 261 VQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAG-RLERVCKKDVEINGVFIPKGTVVMIPTYALHRDP 339
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241483 404 DQWSDPLAFKPERFLPgGEKSGVDvkgsDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWE 469
Cdd:cd20650 340 QYWPEPEEFRPERFSK-KNKDNID----PYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFK 400
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
169-491 1.55e-30

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: 123.24  E-value: 1.55e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 169 NLGQLvNMCVVNALGREMIGRRLFGADADHKADeFRSMVTEMMALAGV---------FNIGDFVPSLD------WLDLQG 233
Cdd:cd11040  92 GLDRL-NEAMLENLSKLLDELSLSGGTSTVEVD-LYEWLRDVLTRATTealfgpklpELDPDLVEDFWtfdrglPKLLLG 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 234 VAGKM-KRLHKRFDAFLSSILKEHEMNGQDQKHTdmlSTLISLKGTDLDGDGgsLTDTEIKALLLNMFTAGTDTSASTVD 312
Cdd:cd11040 170 LPRLLaRKAYAARDRLLKALEKYYQAAREERDDG---SELIRARAKVLREAG--LSEEDIARAELALLWAINANTIPAAF 244
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 313 WAIAELIRHPDIMVKAQEELDIVVGRDRPVN-----ESDIAQLPYLQAVIKENFRLHPpTPLSLPHIASESCEINGYHIP 387
Cdd:cd11040 245 WLLAHILSDPELLERIREEIEPAVTPDSGTNaildlTDLLTSCPLLDSTYLETLRLHS-SSTSVRLVTEDTVLGGGYLLR 323
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 388 KGSTLLTNIWAIARDPDQW-SDPLAFKPERFL-PGGEKSGVDVKGSdfeLIPFGAGRRICAGLSLGLRTIQFLTATLVQG 465
Cdd:cd11040 324 KGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLkKDGDKKGRGLPGA---FRPFGGGASLCPGRHFAKNEILAFVALLLSR 400
                       330       340
                ....*....|....*....|....*.
gi 15241483 466 FDWELAGGVTPEKLNMEESYGLTLQR 491
Cdd:cd11040 401 FDVEPVGGGDWKVPGMDESPGLGILP 426
PLN02302 PLN02302
ent-kaurenoic acid oxidase
8-469 5.63e-30

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 122.51  E-value: 5.63e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    8 ILLATVLFLILRIF------SHRRNRSHnnRLPPGPNPWPIIGNlphMGT--------KPHRTLSAMVTTYGpilhlRLG 73
Cdd:PLN02302  14 VAGVFVLKWVLRRVnswlyePKLGEGQP--PLPPGDLGWPVIGN---MWSflrafkssNPDSFIASFISRYG-----RTG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   74 FVDV-------VVAASKSVAEQFLKIHDAnFASRPPNSGAKHMAYNyqDLVFAPYGHRWRLlRKISSVHLFSAKALEDFK 146
Cdd:PLN02302  84 IYKAfmfgqptVLVTTPEACKRVLTDDDA-FEPGWPESTVELIGRK--SFVGITGEEHKRL-RRLTAAPVNGPEALSTYI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  147 HVRQEEVGTLTRELVrvgtkpvNLGQLVNMCVVNALGREMIGRRLFGADADHKADEFRSMVTEMmalagvfNIGdfVPSL 226
Cdd:PLN02302 160 PYIEENVKSCLEKWS-------KMGEIEFLTELRKLTFKIIMYIFLSSESELVMEALEREYTTL-------NYG--VRAM 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  227 DwLDLQGVA-GKMKRLHKRFDAFLSSILKEH---EMNGQDQKHTDMLSTLISLKgtdlDGDGGSLTDTEIKALLLNMFTA 302
Cdd:PLN02302 224 A-INLPGFAyHRALKARKKLVALFQSIVDERrnsRKQNISPRKKDMLDLLLDAE----DENGRKLDDEEIIDLLLMYLNA 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  303 GTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVgRDRPVNES-----DIAQLPYLQAVIKENFRLHPPTPLSLPHiASE 377
Cdd:PLN02302 299 GHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIA-KKRPPGQKgltlkDVRKMEYLSQVIDETLRLINISLTVFRE-AKT 376
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  378 SCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVdvkgsdfeLIPFGAGRRICAGLSLGLRTIQF 457
Cdd:PLN02302 377 DVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTPKAGT--------FLPFGLGSRLCPGNDLAKLEISI 448
                        490
                 ....*....|..
gi 15241483  458 LTATLVQGFDWE 469
Cdd:PLN02302 449 FLHHFLLGYRLE 460
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
70-473 6.57e-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: 118.93  E-value: 6.57e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  70 LRLGFVDVVVAASKSVAEqflkihdanFASRPPNSGAKHMAYNYQDLVFAPYGHR-------WRLLRK--ISSVHLFSAK 140
Cdd:cd11041  16 LPTPDGPLVVLPPKYLDE---------LRNLPESVLSFLEALEEHLAGFGTGGSVvldsplhVDVVRKdlTPNLPKLLPD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 141 ALEDFKHVRQEEVGTLTrelvrvGTKPVNLGQLVNMCVVNALGREMIGRRLfGADADHkADEFRSMVTEMMALAGVFNig 220
Cdd:cd11041  87 LQEELRAALDEELGSCT------EWTEVNLYDTVLRIVARVSARVFVGPPL-CRNEEW-LDLTINYTIDVFAAAAALR-- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 221 dFVPSLdwldLQGVAG-------KMKRLHKRFDAFLSSILKEHEMNGQD---QKHTDMLSTLISLKGTDLDGDGGSLTDt 290
Cdd:cd11041 157 -LFPPF----LRPLVApflpeprRLRRLLRRARPLIIPEIERRRKLKKGpkeDKPNDLLQWLIEAAKGEGERTPYDLAD- 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 291 eikaLLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLS 370
Cdd:cd11041 231 ----RQLALSFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVS 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 371 LPHIASESCEI-NGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVK------GSDFelIPFGAGRR 443
Cdd:cd11041 307 LRRKVLKDVTLsDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQEKKhqfvstSPDF--LGFGHGRH 384
                       410       420       430
                ....*....|....*....|....*....|
gi 15241483 444 ICAGLSLGLRTIQFLTATLVQGFDWELAGG 473
Cdd:cd11041 385 ACPGRFFASNEIKLILAHLLLNYDFKLPEG 414
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
181-471 4.36e-28

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: 116.29  E-value: 4.36e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 181 ALGREMIGRRLFGADADHKADEFRsMVTEMMALAGVFNIGDFVPSLDWLDLQGvAGKMKRLHKRFDAFLSSILKEHEMNG 260
Cdd:cd11052 122 ALTADIISRTAFGSSYEEGKEVFK-LLRELQKICAQANRDVGIPGSRFLPTKG-NKKIKKLDKEIEDSLLEIIKKREDSL 199
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 261 QDQKH----TDMLSTLisLKGTDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVV 336
Cdd:cd11052 200 KMGRGddygDDLLGLL--LEANQSDDQNKNMTVQEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVC 277
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 337 GRDRPVNESdIAQLPYLQAVIKENFRLHPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQW-SDPLAFKPE 415
Cdd:cd11052 278 GKDKPPSDS-LSKLKTVSMVINESLRLYPPAVF-LTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPE 355
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15241483 416 RF---LPGGEKSGVdvkgsdfELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELA 471
Cdd:cd11052 356 RFadgVAKAAKHPM-------AFLPFGLGPRNCIGQNFATMEAKIVLAMILQRFSFTLS 407
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
285-476 8.60e-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: 115.53  E-value: 8.60e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 285 GSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLH 364
Cdd:cd20646 227 GKLSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLY 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 365 PPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEksgvdVKGSDFELIPFGAGRRI 444
Cdd:cd20646 307 PVVPGNARVIVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGG-----LKHHPFGSIPFGYGVRA 381
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15241483 445 CAGLSLGLRTIQFLTATLVQGFD--WELAGG-VTP 476
Cdd:cd20646 382 CVGRRIAELEMYLALSRLIKRFEvrPDPSGGeVKA 416
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
6-497 2.26e-27

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 115.26  E-value: 2.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    6 LTILLATVLFLILRIFSHRrNRShnnrlppGPNPWPIIGNLPHMGTKPHRtLSAMVTTY---GPILHLRLGFVDVVVAAS 82
Cdd:PLN03195  12 LFIALAVLSWIFIHRWSQR-NRK-------GPKSWPIIGAALEQLKNYDR-MHDWLVEYlskDRTVVVKMPFTTYTYIAD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   83 KSVAEQFLKihdANFASRPPNSG-AKHMAYNYQDLVFAPYGHRWRLLRKISSVHlFSAKALEDFKH-VRQEEVGTLTREL 160
Cdd:PLN03195  83 PVNVEHVLK---TNFANYPKGEVyHSYMEVLLGDGIFNVDGELWRKQRKTASFE-FASKNLRDFSTvVFREYSLKLSSIL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  161 VRVGTKpvnlGQLVNMCVVNA-LGREMIGRRLFGADADHKADEFRSMvtemmALAGVFNIGDFVPSLDWLDlqgVAGKMK 239
Cdd:PLN03195 159 SQASFA----NQVVDMQDLFMrMTLDSICKVGFGVEIGTLSPSLPEN-----PFAQAFDTANIIVTLRFID---PLWKLK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  240 RLH------------KRFDAFLSSILK-------EHEMNGQDQKHtDMLSTLISLkGTDLDGDggsLTDTEIKALLLNMF 300
Cdd:PLN03195 227 KFLnigseallsksiKVVDDFTYSVIRrrkaemdEARKSGKKVKH-DILSRFIEL-GEDPDSN---FTDKSLRDIVLNFV 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  301 TAGTDTSASTVDWAIAELIRHPDIMVKAQEEL---DIVVGRDRPVNESD-----------------IAQLPYLQAVIKEN 360
Cdd:PLN03195 302 IAGRDTTATTLSWFVYMIMMNPHVAEKLYSELkalEKERAKEEDPEDSQsfnqrvtqfaglltydsLGKLQYLHAVITET 381
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  361 FRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQW-SDPLAFKPERFLpggeKSGVDVKGSDFELIPFG 439
Cdd:PLN03195 382 LRLYPAVPQDPKGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWI----KDGVFQNASPFKFTAFQ 457
                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241483  440 AGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGvTPEKLNMEESygLTLQRAVPLVV 497
Cdd:PLN03195 458 AGPRICLGKDSAYLQMKMALALLCRFFKFQLVPG-HPVKYRMMTI--LSMANGLKVTV 512
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
185-477 3.90e-27

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: 113.18  E-value: 3.90e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 185 EMIGRRLFGADADHKADEFRSMVTEMMAlAGVFNIGDFVPSLDWLdlQGVAGkmkrlHKRFDAFLSSILKEHEMNGQDqk 264
Cdd:cd11045 121 DLATRVFLGVDLGPEADKVNKAFIDTVR-ASTAIIRTPIPGTRWW--RGLRG-----RRYLEEYFRRRIPERRAGGGD-- 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 265 htDMLSTLISLKgtdlDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVvgRDRPVNE 344
Cdd:cd11045 191 --DLFSALCRAE----DEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL--GKGTLDY 262
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 345 SDIAQLPYLQAVIKENFRLHPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKS 424
Cdd:cd11045 263 EDLGQLEVTDWVFKEALRLVPPVPT-LPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAED 341
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15241483 425 GVdvkgSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPE 477
Cdd:cd11045 342 KV----HRYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWSVPGYYPP 390
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
64-480 7.75e-27

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: 112.58  E-value: 7.75e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  64 YGPILHLRLGFVDVVVAASKSVAEQFLKIHDANFASRppnsgAKHMAYNYqdlVFAPYG------HRWRLLRKissvhlF 137
Cdd:cd20668   1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGR-----GEQATFDW---LFKGYGvafsngERAKQLRR------F 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 138 SAKALEDF-------KHVRQEEVGTLTRELVRVGTKPVNLGQLVNMCVVNalgreMIGRRLFGADADHKADEFRSMVTEM 210
Cdd:cd20668  67 SIATLRDFgvgkrgiEERIQEEAGFLIDALRGTGGAPIDPTFYLSRTVSN-----VISSIVFGDRFDYEDKEFLSLLRMM 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 211 M-----ALAGVFNIGDFVPSLdwldLQGVAGKMKRLHKRFDAFLSSILKEHEmngQDQKHTD-------MLSTLISLKGT 278
Cdd:cd20668 142 LgsfqfTATSTGQLYEMFSSV----MKHLPGPQQQAFKELQGLEDFIAKKVE---HNQRTLDpnsprdfIDSFLIRMQEE 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 279 DLDGDggslTDTEIKALL---LNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQA 355
Cdd:cd20668 215 KKNPN----TEFYMKNLVmttLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEA 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 356 VIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFel 435
Cdd:cd20668 291 VIHEIQRFGDVIPMGLARRVTKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFL---DDKGQFKKSDAF-- 365
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 15241483 436 IPFGAGRRICAGLSLGLRTIQFLTATLVQGFdwELAGGVTPEKLN 480
Cdd:cd20668 366 VPFSIGKRYCFGEGLARMELFLFFTTIMQNF--RFKSPQSPEDID 408
PLN02738 PLN02738
carotene beta-ring hydroxylase
284-501 3.84e-26

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 112.31  E-value: 3.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  284 GGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNEsDIAQLPYLQAVIKENFRL 363
Cdd:PLN02738 384 GDDVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIE-DMKKLKYTTRVINESLRL 462
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  364 HPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERF-LPGGEKSGVDvkgSDFELIPFGAGR 442
Cdd:PLN02738 463 YPQPPV-LIRRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpLDGPNPNETN---QNFSYLPFGGGP 538
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241483  443 RICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPEKL----NMEESYGLTL---QRAVPLVVHPKP 501
Cdd:PLN02738 539 RKCVGDMFASFENVVATAMLVRRFDFQLAPGAPPVKMttgaTIHTTEGLKMtvtRRTKPPVIPNLP 604
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
251-447 4.47e-26

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: 110.44  E-value: 4.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 251 SILKEHEMNGQDQK-HTDMLSTLISLKgtdlDGDGGSLTDTEIKALLLN-MFtAGTDTSASTVDWAIAELIRHPDIMVKA 328
Cdd:cd20678 202 QLQDEGELEKIKKKrHLDFLDILLFAK----DENGKSLSDEDLRAEVDTfMF-EGHDTTASGISWILYCLALHPEHQQRC 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 329 QEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPP---------TPLSLPhiasesceiNGYHIPKGSTLLTNIWAI 399
Cdd:cd20678 277 REEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPvpgisrelsKPVTFP---------DGRSLPAGITVSLSIYGL 347
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15241483 400 ARDPDQWSDPLAFKPERFLPggEKSgvdVKGSDFELIPFGAGRRICAG 447
Cdd:cd20678 348 HHNPAVWPNPEVFDPLRFSP--ENS---SKRHSHAFLPFSAGPRNCIG 390
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
77-471 6.00e-26

cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus nidulans cytochrome P450 59 (CYP59), also called sterigmatocystin biosynthesis P450 monooxygenase stcS, and similar fungal proteins. CYP59 is required for the conversion of versicolorin A to sterigmatocystin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410674 [Multi-domain]  Cd Length: 403  Bit Score: 109.65  E-value: 6.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  77 VVVAASKSVAEQFLKIHdanfaSRPPNSGAKHMaynYQDLV-----FAPYGHRWRLLRKISSvHLFSAKaledfkHVRQ- 150
Cdd:cd11051  12 LLVVTDPELAEQITQVT-----NLPKPPPLRKF---LTPLTggsslISMEGEEWKRLRKRFN-PGFSPQ------HLMTl 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 151 -----EEVGTLT---RELVRVGtKPVNLGQL-VNMCVvnalgrEMIGRRLFGADADHKADEfRSMVTEM-MALAGVFNIG 220
Cdd:cd11051  77 vptilDEVEIFAailRELAESG-EVFSLEELtTNLTF------DVIGRVTLDIDLHAQTGD-NSLLTALrLLLALYRSLL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 221 DFVPslDWLDLQGVagKMKRLHKRFDAFLSSILKE-HEMNgqdqkhtdmlstlislkgtdldgdggsLTDTEIKALLLnm 299
Cdd:cd11051 149 NPFK--RLNPLRPL--RRWRNGRRLDRYLKPEVRKrFELE---------------------------RAIDQIKTFLF-- 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 300 ftAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDR-------PVNESDIAQLPYLQAVIKENFRLHPPtplslP 372
Cdd:cd11051 196 --AGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPsaaaellREGPELLNQLPYTTAVIKETLRLFPP-----A 268
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 373 HIASESCEINGYHIPKGSTLLT---NIW----AIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGSdfeLIPFGAGRRIC 445
Cdd:cd11051 269 GTARRGPPGVGLTDRDGKEYPTdgcIVYvchhAIHRDPEYWPRPDEFIPERWLVDEGHELYPPKSA---WRPFERGPRNC 345
                       410       420
                ....*....|....*....|....*.
gi 15241483 446 AGLSLGLRTIQFLTATLVQGFDWELA 471
Cdd:cd11051 346 IGQELAMLELKIILAMTVRRFDFEKA 371
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
287-476 2.65e-25

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: 108.08  E-value: 2.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 287 LTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPP 366
Cdd:cd20647 233 LTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPV 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 367 TPLSlPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGSdfelIPFGAGRRICA 446
Cdd:cd20647 313 LPGN-GRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRVDNFGS----IPFGYGIRSCI 387
                       170       180       190
                ....*....|....*....|....*....|
gi 15241483 447 GLSLGLRTIQFLTATLVQGFDWELAGGVTP 476
Cdd:cd20647 388 GRRIAELEIHLALIQLLQNFEIKVSPQTTE 417
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
264-447 3.07e-25

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: 108.24  E-value: 3.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 264 KHTDMLSTLISLKgtdlDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVgRDRPVN 343
Cdd:cd20679 221 KTLDFIDVLLLSK----DEDGKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELL-KDREPE 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 344 E---SDIAQLPYLQAVIKENFRLHPPTPLslphiASESCEIN-----GYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPE 415
Cdd:cd20679 296 EiewDDLAQLPFLTMCIKESLRLHPPVTA-----ISRCCTQDivlpdGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPF 370
                       170       180       190
                ....*....|....*....|....*....|..
gi 15241483 416 RFLPGGEKsgvdvKGSDFELIPFGAGRRICAG 447
Cdd:cd20679 371 RFDPENSQ-----GRSPLAFIPFSAGPRNCIG 397
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
287-466 4.43e-25

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: 108.00  E-value: 4.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 287 LTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPP 366
Cdd:cd20649 257 LTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPP 336
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 367 TpLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKsgvdvKGSDFELIPFGAGRRICA 446
Cdd:cd20649 337 A-FRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQ-----RRHPFVYLPFGAGPRSCI 410
                       170       180
                ....*....|....*....|
gi 15241483 447 GLSLGLRTIQFLTATLVQGF 466
Cdd:cd20649 411 GMRLALLEIKVTLLHILRRF 430
PLN02936 PLN02936
epsilon-ring hydroxylase
287-481 7.49e-25

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 107.57  E-value: 7.49e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  287 LTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGrDRPVNESDIAQLPYLQAVIKENFRLHPP 366
Cdd:PLN02936 274 VSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMRLYPH 352
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  367 TPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERF-LPGGEKSGVDvkgSDFELIPFGAGRRIC 445
Cdd:PLN02936 353 PPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdLDGPVPNETN---TDFRYIPFSGGPRKC 429
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15241483  446 AGLSLGLRTIQFLTATLVQGFDWELAGGvtpEKLNM 481
Cdd:PLN02936 430 VGDQFALLEAIVALAVLLQRLDLELVPD---QDIVM 462
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
246-460 2.11e-24

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: 105.22  E-value: 2.11e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 246 DAFLSSILKEHEMNGQDqkhTDMLSTLISLKgtdlDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIM 325
Cdd:cd20614 170 DARLSQLVATARANGAR---TGLVAALIRAR----DDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVW 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 326 VKAQEELDIVvgRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQ 405
Cdd:cd20614 243 DALCDEAAAA--GDVPRTPAELRRFPLAEALFRETLRLHPPVPF-VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPEL 319
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15241483 406 WSDPLAFKPERFLpggeksGVDVKGSDFELIPFGAGRRICAGLSLG-LRTIQFLTA 460
Cdd:cd20614 320 YPDPDRFRPERWL------GRDRAPNPVELLQFGGGPHFCLGYHVAcVELVQFIVA 369
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
262-473 1.07e-23

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: 103.36  E-value: 1.07e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 262 DQKHTDMLSTLISlkgtDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELD---IVVGR 338
Cdd:cd20638 205 EQQCKDALQLLIE----HSRRNGEPLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQekgLLSTK 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 339 DRPVNESDIA---QLPYLQAVIKENFRLHPPTPLSLpHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPE 415
Cdd:cd20638 281 PNENKELSMEvleQLKYTGCVIKETLRLSPPVPGGF-RVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPD 359
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241483 416 RFLPGGEKsgvdvKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGG 473
Cdd:cd20638 360 RFMSPLPE-----DSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQLLNG 412
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
295-447 1.56e-23

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: 102.91  E-value: 1.56e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 295 LLLnmftAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHI 374
Cdd:cd20648 242 LLL----AGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVI 317
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15241483 375 ASESCEINGYHIPKgSTLLTNI-WAIARDPDQWSDPLAFKPERFLPGGEksgvdvKGSDFELIPFGAGRRICAG 447
Cdd:cd20648 318 PDRDIQVGEYIIPK-KTLITLChYATSRDENQFPDPNSFRPERWLGKGD------THHPYASLPFGFGKRSCIG 384
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
123-499 1.03e-22

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: 100.68  E-value: 1.03e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 123 HRWRllRKISSvHLFSAKALEDFKHVRQEEVGTLTRELVRvGTKPVNLGQLVNMCVVNALGREMIGRRLFGADADHKADE 202
Cdd:cd20636  80 HRQR--RKVLA-RVFSRAALESYLPRIQDVVRSEVRGWCR-GPGPVAVYTAAKSLTFRIAVRILLGLRLEEQQFTYLAKT 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 203 FRSMVTEMMALAgvfnigdfvpsldwLDLQgVAGKMKRLHKR--FDAFLSSILKEHEMNGQDQKHTDMLSTLISlkgtDL 280
Cdd:cd20636 156 FEQLVENLFSLP--------------LDVP-FSGLRKGIKARdiLHEYMEKAIEEKLQRQQAAEYCDALDYMIH----SA 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 281 DGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELD----IVVGRDRP--VNESDIAQLPYLQ 354
Cdd:cd20636 217 RENGKELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVshglIDQCQCCPgaLSLEKLSRLRYLD 296
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 355 AVIKENFRLHPPTPLSLpHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSgvdvKGSDFE 434
Cdd:cd20636 297 CVVKEVLRLLPPVSGGY-RTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREES----KSGRFN 371
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15241483 435 LIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAggvTPEKLNMEesygltlqrAVPlVVHP 499
Cdd:cd20636 372 YIPFGGGVRSCIGKELAQVILKTLAVELVTTARWELA---TPTFPKMQ---------TVP-IVHP 423
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
181-471 1.21e-22

cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP734As function as multisubstrate and multifunctional enzymes in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis. Arabidopsis thaliana CYP734A1/BAS1 (formerly CYP72B1) inactivates bioactive brassinosteroids such as castasterone (CS) and brassinolide (BL) by C-26 hydroxylation. Rice CYP734As can catalyze C-22 hydroxylation as well as second and third oxidations to produce aldehyde and carboxylate groups at C-26. CYP734 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 100.22  E-value: 1.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 181 ALGREMIGRRLFGADADHKADEFRsMVTEMMALAGVFNIGDFVPSLDWLdlqgvAGKMKRLHKRFDAFL-SSILKEHEMN 259
Cdd:cd20639 123 NLTEDVISRTAFGSSYEDGKAVFR-LQAQQMLLAAEAFRKVYIPGYRFL-----PTKKNRKSWRLDKEIrKSLLKLIERR 196
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 260 GQ-------DQKHTDMLSTLISLKGtdlDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEEL 332
Cdd:cd20639 197 QTaaddekdDEDSKDLLGLMISAKN---ARNGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREV 273
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 333 DIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTpLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLA- 411
Cdd:cd20639 274 LAVCGKGDVPTKDHLPKLKTLGMILNETLRLYPPA-VATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWGNDAAe 352
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 412 FKPERFLPGgeKSGVDVKGSDFelIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELA 471
Cdd:cd20639 353 FNPARFADG--VARAAKHPLAF--IPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRLS 408
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
296-481 1.37e-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: 100.24  E-value: 1.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 296 LLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIA 375
Cdd:cd20672 231 VLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRV 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 376 SESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLpggEKSGVDVKGSDFelIPFGAGRRICAGLSLGLRTI 455
Cdd:cd20672 311 TKDTLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFL---DANGALKKSEAF--MPFSTGKRICLGEGIARNEL 385
                       170       180
                ....*....|....*....|....*.
gi 15241483 456 QFLTATLVQGFdwELAGGVTPEKLNM 481
Cdd:cd20672 386 FLFFTTILQNF--SVASPVAPEDIDL 409
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
288-469 2.27e-22

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: 99.24  E-value: 2.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 288 TDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEEldivVGRDRPVNESDI-----AQLPYLQAVIKENFR 362
Cdd:cd11082 217 SDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREE----QARLRPNDEPPLtldllEEMKYTRQVVKEVLR 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 363 LHPPTPLsLPHIASESCEIN-GYHIPKGSTLLTNIWAIARDPdqWSDPLAFKPERFLPGGEKSGVDVKGSdfelIPFGAG 441
Cdd:cd11082 293 YRPPAPM-VPHIAKKDFPLTeDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQEDRKYKKNF----LVFGAG 365
                       170       180
                ....*....|....*....|....*...
gi 15241483 442 RRICAGLSLGLRTIQFLTATLVQGFDWE 469
Cdd:cd11082 366 PHQCVGQEYAINHLMLFLALFSTLVDWK 393
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
284-467 1.09e-21

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


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 97.18  E-value: 1.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 284 GGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNESDIAQLPYLQAVIKENFRL 363
Cdd:cd20645 219 DNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRL 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 364 HPPTPLSLPHIaSESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPggEKSGVDvkgsDFELIPFGAGRR 443
Cdd:cd20645 299 TPSVPFTSRTL-DKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQ--EKHSIN----PFAHVPFGIGKR 371
                       170       180
                ....*....|....*....|....
gi 15241483 444 ICAGLSLGLRTIQFLTATLVQGFD 467
Cdd:cd20645 372 MCIGRRLAELQLQLALCWIIQKYQ 395
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
219-477 7.26e-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: 7.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 219 IGDFVPSLDwlDLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDqkhtDMLSTLislkgTDLDGDGGSLTDTEIKALLLN 298
Cdd:cd11080 132 VAAFITSLS--QDPEARAHGLRCAEQLSQYLLPVIEERRVNPGS----DLISIL-----CTAEYEGEALSDEDIKALILN 200
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 299 MFTAGTDTSASTVDWAIAELIRHPDIMVKAQEeldivvgrDRpvnesdiaqlPYLQAVIKENFRLHPPTPLsLPHIASES 378
Cdd:cd11080 201 VLLAATEPADKTLALMIYHLLNNPEQLAAVRA--------DR----------SLVPRAIAETLRYHPPVQL-IPRQASQD 261
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 379 CEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERfLPGGEKSGVDVKGSDfelIPFGAGRRICAGLSLGLRTIQFL 458
Cdd:cd11080 262 VVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHR-EDLGIRSAFSGAADH---LAFGSGRHFCVGAALAKREIEIV 337
                       250       260
                ....*....|....*....|
gi 15241483 459 TATLVQGF-DWELAGGVTPE 477
Cdd:cd11080 338 ANQVLDALpNIRLEPGFEYA 357
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
185-489 2.80e-20

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: 93.25  E-value: 2.80e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 185 EMIGRRLFGADADhKADEFRSMVTEMMALAGVFNIGDFVPSLDWLDLQGvAGKMKRLHKRFDAFLSSILKEHEMNGQDQK 264
Cdd:cd20640 130 DVISRACFGSSYS-KGKEIFSKLRELQKAVSKQSVLFSIPGLRHLPTKS-NRKIWELEGEIRSLILEIVKEREEECDHEK 207
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 265 htDMLSTLIslkgtDLDGDGGSLTDTEIKALLLN---MFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELdIVVGRDRP 341
Cdd:cd20640 208 --DLLQAIL-----EGARSSCDKKAEAEDFIVDNcknIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEV-LEVCKGGP 279
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 342 VNESDIAQLPYLQAVIKENFRLHPPTPLsLPHIASESCEINGYHIPKGstllTNIW----AIARDPDQW-SDPLAFKPER 416
Cdd:cd20640 280 PDADSLSRMKTVTMVIQETLRLYPPAAF-VSREALRDMKLGGLVVPKG----VNIWvpvsTLHLDPEIWgPDANEFNPER 354
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 417 FLPGGEKSgvdvKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELaggvTPE-------KLNMEESYGLTL 489
Cdd:cd20640 355 FSNGVAAA----CKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLILSKFSFTL----SPEyqhspafRLIVEPEFGVRL 426
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
291-469 9.33e-20

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: 91.70  E-value: 9.33e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 291 EIKALLLNMFTAGTDTSASTVDWAIAELIRHPDImvkaQEELDIVVGRDRPVNESDIAQL----PYLQAVIKENFRLHPp 366
Cdd:cd20643 234 DIKASVTELMAGGVDTTSMTLQWTLYELARNPNV----QEMLRAEVLAARQEAQGDMVKMlksvPLLKAAIKETLRLHP- 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 367 TPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSgvdvkgsdFELIPFGAGRRICA 446
Cdd:cd20643 309 VAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITH--------FRNLGFGFGPRQCL 380
                       170       180
                ....*....|....*....|...
gi 15241483 447 GLSLGLRTIQFLTATLVQGFDWE 469
Cdd:cd20643 381 GRRIAETEMQLFLIHMLENFKIE 403
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
237-471 1.44e-19

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: 91.19  E-value: 1.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 237 KMKRLHKRFDAFLSSIL--KEHEMNGQDQKHTDML-----STLISLKGTDLDGDGGSLTDT--EIKALLLnmftAGTDTS 307
Cdd:cd20642 175 RMKEIEKEIRSSLRGIInkREKAMKAGEATNDDLLgilleSNHKEIKEQGNKNGGMSTEDVieECKLFYF----AGQETT 250
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 308 ASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNEsDIAQLPYLQAVIKENFRLHPPTpLSLPHIASESCEINGYHIP 387
Cdd:cd20642 251 SVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKPDFE-GLNHLKVVTMILYEVLRLYPPV-IQLTRAIHKDTKLGDLTLP 328
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 388 KGSTLLTNIWAIARDPDQW-SDPLAFKPERFLPGGEKSgvdVKGSdFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGF 466
Cdd:cd20642 329 AGVQVSLPILLVHRDPELWgDDAKEFNPERFAEGISKA---TKGQ-VSYFPFGWGPRICIGQNFALLEAKMALALILQRF 404

                ....*
gi 15241483 467 DWELA 471
Cdd:cd20642 405 SFELS 409
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
2-476 1.71e-19

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 91.15  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    2 ATLFLTILLATVLFLILRIFSH-RRNRSHNNRLPPGPNPWPIIGNLPHMGTK-PHRTLSAMVTTYGPILHLRLGFVDVVV 79
Cdd:PLN02196   4 SALFLTLFAGALFLCLLRFLAGfRRSSSTKLPLPPGTMGWPYVGETFQLYSQdPNVFFASKQKRYGSVFKTHVLGCPCVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   80 AASKSVAEQFLKIHDANFASRPPNSGAKHMAynyQDLVFAPYGHRWRLLRKISsVHLFSAKALE----DFKHVRQEEV-- 153
Cdd:PLN02196  84 ISSPEAAKFVLVTKSHLFKPTFPASKERMLG---KQAIFFHQGDYHAKLRKLV-LRAFMPDAIRnmvpDIESIAQESLns 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  154 --GTLTRELVRVGTKPVNLGQLVNMCVVNALGREMIGRRLFGADADhkadeFRSMVtemMALAG-VFNigdfvpsldwld 230
Cdd:PLN02196 160 weGTQINTYQEMKTYTFNVALLSIFGKDEVLYREDLKRCYYILEKG-----YNSMP---INLPGtLFH------------ 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  231 lqgvagKMKRLHKRFDAFLSSILKEHEMNGQDqkHTDMLSTLIslkgtdldGDGGSLTDTEIKALLLNMFTAGTDTSAST 310
Cdd:PLN02196 220 ------KSMKARKELAQILAKILSKRRQNGSS--HNDLLGSFM--------GDKEGLTDEQIADNIIGVIFAARDTTASV 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  311 VDWAIAELIRHPDIMVKAQEELDIVVgRDRPVNES----DIAQLPYLQAVIKENFRLhpPTPLSLP-HIASESCEINGYH 385
Cdd:PLN02196 284 LTWILKYLAENPSVLEAVTEEQMAIR-KDKEEGESltweDTKKMPLTSRVIQETLRV--ASILSFTfREAVEDVEYEGYL 360
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  386 IPKGSTLLTNIWAIARDPDQWSDPLAFKPERFlpggeksGVDVKGSDFelIPFGAGRRICAGLSLGLRTIQFLTATLVQG 465
Cdd:PLN02196 361 IPKGWKVLPLFRNIHHSADIFSDPGKFDPSRF-------EVAPKPNTF--MPFGNGTHSCPGNELAKLEISVLIHHLTTK 431
                        490
                 ....*....|.
gi 15241483  466 FDWELAGGVTP 476
Cdd:PLN02196 432 YRWSIVGTSNG 442
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
290-488 1.35e-18

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


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 88.51  E-value: 1.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 290 TEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVV------GRDRPVNESDIAQLPYLQAVIKENFRL 363
Cdd:cd20622 261 QVIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHpeavaeGRLPTAQEIAQARIPYLDAVIEEILRC 340
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 364 HPPTPlSLPHIASESCEINGYHIPKGstllTNIWAIARDPDQWSDPL---------------------------AFKPER 416
Cdd:cd20622 341 ANTAP-ILSREATVDTQVLGYSIPKG----TNVFLLNNGPSYLSPPIeidesrrssssaakgkkagvwdskdiaDFDPER 415
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15241483 417 FLPGGEKSG-VDVKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWElaggVTPEKL-NMEESYGLT 488
Cdd:cd20622 416 WLVTDEETGeTVFDPSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELL----PLPEALsGYEAIDGLT 485
PLN02290 PLN02290
cytokinin trans-hydroxylase
300-508 3.09e-18

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 87.56  E-value: 3.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  300 FTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNEsDIAQLPYLQAVIKENFRLHPPTPLsLPHIASESC 379
Cdd:PLN02290 325 FFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVD-HLSKLTLLNMVINESLRLYPPATL-LPRMAFEDI 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  380 EINGYHIPKGSTLLTNIWAIARDPDQW-SDPLAFKPERFLPGGEKSGVdvkgsdfELIPFGAGRRICAGLSLGLRTIQFL 458
Cdd:PLN02290 403 KLGDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGR-------HFIPFAAGPRNCIGQAFAMMEAKII 475
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15241483  459 TATLVQGFdwelaggvtpeKLNMEESYgltlqRAVPLVVHP-KPRLAPNVY 508
Cdd:PLN02290 476 LAMLISKF-----------SFTISDNY-----RHAPVVVLTiKPKYGVQVC 510
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
313-470 5.59e-18

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: 85.83  E-value: 5.59e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 313 WAIAELIRHPDIMVKAQEELDIVVGRDR----PVNESDIAQLPYLQAVIKENFRLHPPTplSLPHIASESCEINGYHIPK 388
Cdd:cd20635 232 WTLAFILSHPSVYKKVMEEISSVLGKAGkdkiKISEDDLKKMPYIKRCVLEAIRLRSPG--AITRKVVKPIKIKNYTIPA 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 389 GSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGsdfeLIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDW 468
Cdd:cd20635 310 GDMLMLSPYWAHRNPKYFPDPELFKPERWKKADLEKNVFLEG----FVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDF 385

                ..
gi 15241483 469 EL 470
Cdd:cd20635 386 TL 387
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
123-499 7.49e-18

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: 85.67  E-value: 7.49e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 123 HRWRllRKISSvHLFSAKALEDFkhvrQEEVGTLTRELVRVGT---KPVNLGQLVNMCVVNALGREMIGRRLFGADADHK 199
Cdd:cd20637  79 HRHK--RKVFS-KLFSHEALESY----LPKIQQVIQDTLRVWSsnpEPINVYQEAQKLTFRMAIRVLLGFRVSEEELSHL 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 200 ADEFRSMVTEMMALAgvfnigdfvpsldwLDLQgVAGKMKRLHKR--FDAFLSSILKEHEMNGQDQKHTDMLSTLISlkg 277
Cdd:cd20637 152 FSVFQQFVENVFSLP--------------LDLP-FSGYRRGIRARdsLQKSLEKAIREKLQGTQGKDYADALDILIE--- 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 278 tDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEEL--DIVVGRDRPVNES----DIAQLP 351
Cdd:cd20637 214 -SAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELrsNGILHNGCLCEGTlrldTISSLK 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 352 YLQAVIKENFRLHPPTPLSLpHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFlpGGEKSgvDVKGS 431
Cdd:cd20637 293 YLDCVIKEVLRLFTPVSGGY-RTALQTFELDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRF--GQERS--EDKDG 367
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241483 432 DFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPEKLnmeesygltlqrAVPlVVHP 499
Cdd:cd20637 368 RFHYLPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFELATRTFPRMT------------TVP-VVHP 422
PLN02774 PLN02774
brassinosteroid-6-oxidase
243-475 9.37e-18

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 85.60  E-value: 9.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  243 KRFDAFLSSILKEHEMNGQdqKHTDMLSTLISLKGTDLdgdggSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHP 322
Cdd:PLN02774 223 KNIVRMLRQLIQERRASGE--THTDMLGYLMRKEGNRY-----KLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHP 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  323 DIMVKAQEE-LDIVVGR--DRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHIASEsCEINGYHIPKGSTLLTNIWAI 399
Cdd:PLN02774 296 KALQELRKEhLAIRERKrpEDPIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQD-MELNGYVIPKGWRIYVYTREI 374
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241483  400 ARDPDQWSDPLAFKPERFLpggEKSgvdvKGSDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVT 475
Cdd:PLN02774 375 NYDPFLYPDPMTFNPWRWL---DKS----LESHNYFFLFGGGTRLCPGKELGIVEISTFLHYFVTRYRWEEVGGDK 443
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
287-478 1.39e-17

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


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 84.65  E-value: 1.39e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 287 LTDTEIKALLLNMftagtDTSASTVDWAIAELIRHPDIMVKAQEEldIVVGRDRPVNESD--IA-QLPYLQAVIKENFRL 363
Cdd:cd20615 216 LLQTLDEMLFANL-----DVTTGVLSWNLVFLAANPAVQEKLREE--ISAAREQSGYPMEdyILsTDTLLAYCVLESLRL 288
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 364 HPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAI-ARDPDQWSDPLAFKPERFLpggeksgvDVKGSDFE--LIPFGA 440
Cdd:cd20615 289 RPLLAFSVPESSPTDKIIGGYRIPANTPVVVDTYALnINNPFWGPDGEAYRPERFL--------GISPTDLRynFWRFGF 360
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 15241483 441 GRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPEK 478
Cdd:cd20615 361 GPRKCLGQHVADVILKALLAHLLEQYELKLPDQGENEE 398
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
254-468 6.16e-17

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 83.10  E-value: 6.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  254 KEHEMNGQDQKHtDMLSTLislkgtdLDGDGGsLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELD 333
Cdd:PLN02987 239 RKEEEEGAEKKK-DMLAAL-------LASDDG-FSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHE 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  334 IVVGR--DRPVNE-SDIAQLPYLQAVIKENFRLHPPTPLSLPHIASEsCEINGYHIPKGSTLLTNIWAIARDPDQWSDPL 410
Cdd:PLN02987 310 KIRAMksDSYSLEwSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTD-IEVKGYTIPKGWKVFASFRAVHLDHEYFKDAR 388
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15241483  411 AFKPERFlpgGEKSGVDVKGSDFelIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDW 468
Cdd:PLN02987 389 TFNPWRW---QSNSGTTVPSNVF--TPFGGGPRLCPGYELARVALSVFLHRLVTRFSW 441
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
282-473 6.39e-17

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 83.20  E-value: 6.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  282 GDGGSLTDTEIKALLlnmftAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVG-RDRPVNESDIAQLPYLQAVIKEN 360
Cdd:PLN02426 289 NDDKYLRDIVVSFLL-----AGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGpNQEAASFEEMKEMHYLHAALYES 363
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  361 FRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQW-SDPLAFKPERFLpggeKSGVDVKGSDFELIPFG 439
Cdd:PLN02426 364 MRLFPPVQFDSKFAAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWL----KNGVFVPENPFKYPVFQ 439
                        170       180       190
                 ....*....|....*....|....*....|....
gi 15241483  440 AGRRICAGLSLGLRTIQFLTATLVQGFDWELAGG 473
Cdd:PLN02426 440 AGLRVCLGKEMALMEMKSVAVAVVRRFDIEVVGR 473
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
289-473 1.68e-16

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 81.98  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  289 DTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIvvgrdrPVNESDIAQLPYLQAVIKENFRLHPPTP 368
Cdd:PLN02169 299 DKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINT------KFDNEDLEKLVYLHAALSESMRLYPPLP 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  369 LSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQW-SDPLAFKPERFLpgGEKSGVDVKGSdFELIPFGAGRRICAG 447
Cdd:PLN02169 373 FNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWI--SDNGGLRHEPS-YKFMAFNSGPRTCLG 449
                        170       180
                 ....*....|....*....|....*.
gi 15241483  448 LSLGLRTIQFLTATLVQGFDWELAGG 473
Cdd:PLN02169 450 KHLALLQMKIVALEIIKNYDFKVIEG 475
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
254-490 5.61e-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: 5.61e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 254 KEHEMNGQDQK--HTDMLSTLIslkgtdLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEE 331
Cdd:cd20616 191 KRRRISTAEKLedHMDFATELI------FAQKRGELTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKE 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 332 LDIVVGrDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPHiASESCEINGYHIPKGSTLLTNIWAIARDPdQWSDPLA 411
Cdd:cd20616 265 IQTVLG-ERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRK-ALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNE 341
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15241483 412 FKPERFlpggEKSgvdVKGSDFEliPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELAGGVTPEklNMEESYGLTLQ 490
Cdd:cd20616 342 FTLENF----EKN---VPSRYFQ--PFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVE--NIQKTNDLSLH 409
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
260-494 8.90e-16

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: 79.50  E-value: 8.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 260 GQDQKHTDMLSTLIslkgtdldgDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDImvkaQEELDIVVGRD 339
Cdd:cd20644 210 GRPQHYTGIVAELL---------LQAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDV----QQILRQESLAA 276
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 340 RPVNESDIAQ----LPYLQAVIKENFRLHPpTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPE 415
Cdd:cd20644 277 AAQISEHPQKalteLPLLKAALKETLRLYP-VGITVQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQ 355
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 416 RFLpggeksgvDVKGSD--FELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELaggVTPEKLNMeeSYGLTLQRAV 493
Cdd:cd20644 356 RWL--------DIRGSGrnFKHLAFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLVET---LSQEDIKT--VYSFILRPEK 422

                .
gi 15241483 494 P 494
Cdd:cd20644 423 P 423
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
182-471 2.17e-15

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: 78.26  E-value: 2.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 182 LGREMIGRRLFGADADHKADEFRSMvTEM--MALAGVFNIgdFVPSLDWLDLQGVAgKMKRLHKRFDAFLSSILKEHEMN 259
Cdd:cd20641 126 LTADIIATTAFGSSYAEGIEVFLSQ-LELqkCAAASLTNL--YIPGTQYLPTPRNL-RVWKLEKKVRNSIKRIIDSRLTS 201
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 260 GQDQKHTDMLSTLIslkgTDLDGDGGSLTDT------EIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELD 333
Cdd:cd20641 202 EGKGYGDDLLGLML----EAASSNEGGRRTErkmsidEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVF 277
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 334 IVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQW-SDPLAF 412
Cdd:cd20641 278 RECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVIN-IARRASEDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEF 356
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15241483 413 KPERFLPGGEKSGVDVKGsdfeLIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELA 471
Cdd:cd20641 357 NPLRFANGVSRAATHPNA----LLSFSLGPRACIGQNFAMIEAKTVLAMILQRFSFSLS 411
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
243-450 1.88e-14

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


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 74.55  E-value: 1.88e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 243 KRFDAFLSSILKEHEMNGQDqkhtDMLSTLISLkgtdlDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHP 322
Cdd:cd11035 151 QAVLDYLTPLIAERRANPGD----DLISAILNA-----EIDGRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHP 221
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 323 DimvkAQEELdivvgRDRPvneSDIaqlpylQAVIKENFRLHPptPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARD 402
Cdd:cd11035 222 E----DRRRL-----REDP---ELI------PAAVEELLRRYP--LVNVARIVTRDVEFHGVQLKAGDMVLLPLALANRD 281
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15241483 403 PDQWSDPLAFKPERflpggeksgvdvkgSDFELIPFGAGRRICAGLSL 450
Cdd:cd11035 282 PREFPDPDTVDFDR--------------KPNRHLAFGAGPHRCLGSHL 315
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
267-472 9.04e-14

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: 72.84  E-value: 9.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 267 DMLSTLISlkgTDLDGDGgsLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIM--VKAQEELdivvgrdrpvne 344
Cdd:cd20630 184 DLLTTLLR---AEEDGER--LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALrkVKAEPEL------------ 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 345 sdiaqlpyLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERflpggeks 424
Cdd:cd20630 247 --------LRNALEEVLRWDNFGKMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR-------- 310
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15241483 425 gvDVKGSdfelIPFGAGRRICAGLSLGLRTIQFLTATLVQGF-DWELAG 472
Cdd:cd20630 311 --DPNAN----IAFGYGPHFCIGAALARLELELAVSTLLRRFpEMELAE 353
PLN02500 PLN02500
cytochrome P450 90B1
3-472 1.89e-13

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 72.59  E-value: 1.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483    3 TLFLTILLATVLFLILR-IFSHRRNRSHNNRLPPGPNPWPIIGNL-----PHMGTKPHRTLSAMVTTYGPILHLRLGFVD 76
Cdd:PLN02500   8 TELLLFLLPSILSLLLVfILTKRRPKQKRFNLPPGNMGWPFLGETigylkPYSATSIGEFMEQHISRYGKIYRSNLFGEP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483   77 VVVAASKSVAEQFLKIHDANFASRPPNSGAKHMAynyqdlvfapyghRWRLLRKISSVHL-FSAKALEDFKHVRQEEVgt 155
Cdd:PLN02500  88 TIVSADAGLNRFILQNEGRLFECSYPRSIGGILG-------------KWSMLVLVGDMHRdMRSISLNFLSHARLRTH-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  156 LTRELVRVgtkpvnlgqlvNMCVVNALGREMIgrrlFGADADHKADEFRSMVTEMMAL------------------AGVF 217
Cdd:PLN02500 153 LLKEVERH-----------TLLVLDSWKENST----FSAQDEAKKFTFNLMAKHIMSMdpgeeeteqlkkeyvtfmKGVV 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  218 NigdfVPsldwLDLQGVAGKmKRLHKRfdaflSSILKEHEMNGQDQKhTDMLSTLISLKGTDLDG---DGGSLTDTEIKA 294
Cdd:PLN02500 218 S----AP----LNFPGTAYR-KALKSR-----ATILKFIERKMEERI-EKLKEEDESVEEDDLLGwvlKHSNLSTEQILD 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  295 LLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVGRDRPVNES-----DIAQLPYLQAVIKENFRLHPPTPL 369
Cdd:PLN02500 283 LILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIARAKKQSGESelnweDYKKMEFTQCVINETLRLGNVVRF 362
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  370 sLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVKGSDFE--LIPFGAGRRICAG 447
Cdd:PLN02500 363 -LHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRGGSSGSSSATTnnFMPFGGGPRLCAG 441
                        490       500
                 ....*....|....*....|....*
gi 15241483  448 LSLGLRTIQFLTATLVQGFDWELAG 472
Cdd:PLN02500 442 SELAKLEMAVFIHHLVLNFNWELAE 466
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
311-459 8.02e-13

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: 69.87  E-value: 8.02e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 311 VDWAIAELIRHPDImvkaqeeldivvgRDRPVNESDiaqlPYLQAVIKENFRLHPPTPLsLPHIASESCEINGYHIPKGS 390
Cdd:cd11067 240 VTFAALALHEHPEW-------------RERLRSGDE----DYAEAFVQEVRRFYPFFPF-VGARARRDFEWQGYRFPKGQ 301
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15241483 391 TLLTNIWAIARDPDQWSDPLAFKPERFLpggeksgvDVKGSDFELIPFGAGR-----RiCAG--LSLGL--RTIQFLT 459
Cdd:cd11067 302 RVLLDLYGTNHDPRLWEDPDRFRPERFL--------GWEGDPFDFIPQGGGDhatghR-CPGewITIALmkEALRLLA 370
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
283-466 1.15e-12

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: 69.25  E-value: 1.15e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 283 DGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIM--VKAQEELdivvgrdrpvnesdiaqlpyLQAVIKEN 360
Cdd:cd20629 184 EGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLerVRRDRSL--------------------IPAAIEEG 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 361 FRLHPPTpLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDplafkPERFlpggeksgvDVKGSDFELIPFGA 440
Cdd:cd20629 244 LRWEPPV-ASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPD-----PDVF---------DIDRKPKPHLVFGG 308
                       170       180
                ....*....|....*....|....*.
gi 15241483 441 GRRICAGLSLGLRTIQFLTATLVQGF 466
Cdd:cd20629 309 GAHRCLGEHLARVELREALNALLDRL 334
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
267-450 3.77e-12

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: 67.94  E-value: 3.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 267 DMLSTLISLKGtdldgDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIM--VKAQEELdivvgrdrpvne 344
Cdd:cd11029 192 DLLSALVAARD-----EGDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLalLRADPEL------------ 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 345 sdiaqlpyLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDplafkPERFlpggeks 424
Cdd:cd11029 255 --------WPAAVEELLRYDGPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPD-----PDRL------- 314
                       170       180
                ....*....|....*....|....*.
gi 15241483 425 gvDVKGSDFELIPFGAGRRICAGLSL 450
Cdd:cd11029 315 --DITRDANGHLAFGHGIHYCLGAPL 338
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
267-479 1.01e-11

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


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 66.43  E-value: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 267 DMLSTLISLKGtdldgDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMvkaqEELdivvgRDRPvnesd 346
Cdd:cd11031 187 DLLSALVAARD-----DDDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQL----ARL-----RADP----- 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 347 iAQLPylQAViKENFRLHPPTPLS-LPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDplafkPERFLPggeksg 425
Cdd:cd11031 248 -ELVP--AAV-EELLRYIPLGAGGgFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPD-----PDRLDL------ 312
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15241483 426 vdvkgsDFELIP---FGAGRRICAGLSLGLRTIQFLTATLVQGFDwELAGGVTPEKL 479
Cdd:cd11031 313 ------DREPNPhlaFGHGPHHCLGAPLARLELQVALGALLRRLP-GLRLAVPEEEL 362
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
245-450 1.52e-11

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: 66.04  E-value: 1.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 245 FDAFLSSILKEHEMNGQDqkhtDMLSTLIslkgtDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDI 324
Cdd:cd20625 164 LAAYFRDLIARRRADPGD----DLISALV-----AAEEDGDRLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQ 234
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 325 MvkaqEELdivvgRDRPvneSDIAqlpylqAVIKENFRLHPPTPLSlPHIASESCEINGYHIPKGSTLLTNIWAIARDPD 404
Cdd:cd20625 235 L----ALL-----RADP---ELIP------AAVEELLRYDSPVQLT-ARVALEDVEIGGQTIPAGDRVLLLLGAANRDPA 295
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15241483 405 QWSDPLAFKPERflpggeksgvdvkgSDFELIPFGAGRRICAGLSL 450
Cdd:cd20625 296 VFPDPDRFDITR--------------APNRHLAFGAGIHFCLGAPL 327
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
224-484 6.17e-11

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 63.91  E-value: 6.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 224 PSLDWL------DLQGVAGKMKRLHKRFDAFLSSILKEHEMNGQDQkhTDMLSTLISLKGTDldgdGGSLTDTEIKALLL 297
Cdd:cd11079 116 PLAEWVnknhaaTRSGDRAATAEVAEEFDGIIRDLLADRRAAPRDA--DDDVTARLLRERVD----GRPLTDEEIVSILR 189
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 298 NMFTAGTDTSASTVDWAIAELIRHPDImvkaQEELdivvgRDRPvnesdiAQLPylqAVIKENFRLHPPTPlSLPHIASE 377
Cdd:cd11079 190 NWTVGELGTIAACVGVLVHYLARHPEL----QARL-----RANP------ALLP---AAIDEILRLDDPFV-ANRRITTR 250
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 378 SCEINGYHIPKGSTLLTNiWAIA-RDPDQWSDPLAFKPERflpggeksgvdvkGSDFELIpFGAGRRICAGLSLGLRTIQ 456
Cdd:cd11079 251 DVELGGRTIPAGSRVTLN-WASAnRDERVFGDPDEFDPDR-------------HAADNLV-YGRGIHVCPGAPLARLELR 315
                       250       260
                ....*....|....*....|....*....
gi 15241483 457 FLTATLVQGFDW-ELAGGVTPEKLNMEES 484
Cdd:cd11079 316 ILLEELLAQTEAiTLAAGGPPERATYPVG 344
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
262-450 2.12e-10

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: 62.24  E-value: 2.12e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 262 DQKHTDMLSTLIslkgTDLDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDImvkaQEELdivvgRDRP 341
Cdd:cd11078 184 REPRDDLISDLL----AAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQ----WRRL-----RADP 250
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 342 vnesdiAQLPylqAVIKENFRLHPPTPlSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERflPGG 421
Cdd:cd11078 251 ------SLIP---NAVEETLRYDSPVQ-GLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR--PNA 318
                       170       180
                ....*....|....*....|....*....
gi 15241483 422 EKSgvdvkgsdfelIPFGAGRRICAGLSL 450
Cdd:cd11078 319 RKH-----------LTFGHGIHFCLGAAL 336
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
249-417 8.58e-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: 60.60  E-value: 8.58e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 249 LSSILKE--HEMNGQDQKHTDMLSTLISlkgtdldgdgGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMV 326
Cdd:cd20627 168 MESVLKKviKERKGKNFSQHVFIDSLLQ----------GNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQK 237
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 327 KAQEELDIVVGrDRPVNESDIAQLPYLQAVIKENFRLHPPTPlslphIASESCEING----YHIPKGSTLLTNIWAIARD 402
Cdd:cd20627 238 KLYKEVDQVLG-KGPITLEKIEQLRYCQQVLCETVRTAKLTP-----VSARLQELEGkvdqHIIPKETLVLYALGVVLQD 311
                       170
                ....*....|....*
gi 15241483 403 PDQWSDPLAFKPERF 417
Cdd:cd20627 312 NTTWPLPYRFDPDRF 326
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
287-480 3.35e-09

cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also called 25-hydroxycholesterol 7-alpha-hydroxylase (EC 1.14.14.29) or oxysterol 7-alpha-hydroxylase. It catalyzes the 7alpha-hydroxylation of both steroids and oxysterols, and is thus implicated in the metabolism of neurosteroids and bile acid synthesis, respectively. It participates in the alternative (or acidic) pathway of cholesterol catabolism and bile acid biosynthesis. It also mediates the formation of 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) from 25-hydroxycholesterol; 7-alpha,25-OHC acts as a ligand for the G protein-coupled receptor GPR183/EBI2, a chemotactic receptor in lymphoid cells. CYP7B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410725  Cd Length: 438  Bit Score: 58.85  E-value: 3.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 287 LTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEELDIVVG----RDRPvnESDIA-------QLPYLQA 355
Cdd:cd20632 211 LQDYDKAAHHFAFLWASVGNTIPATFWAMYYLLRHPEALAAVRDEIDHVLQstgqELGP--DFDIHltreqldSLVYLES 288
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 356 VIKENFRLhppTPLSLP-HIASESCEIN-----GYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFLPGGEKSGVDVK 429
Cdd:cd20632 289 AINESLRL---SSASMNiRVVQEDFTLKlesdgSVNLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKKTTFYK 365
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15241483 430 GSD---FELIPFGAGRRICAGLSLGLRTI-QFLTATLVQgFDWELAGGVTPEKLN 480
Cdd:cd20632 366 RGQklkYYLMPFGSGSSKCPGRFFAVNEIkQFLSLLLLY-FDLELLEEQKPPGLD 419
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
239-470 7.40e-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: 57.77  E-value: 7.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 239 KRLHKRFDAFLSSILKEHemngqdQKHTDMLSTLISLKgtDLDGDGGS-LTDTEIKALLLNMFTAGTDTSASTVDWAIAE 317
Cdd:cd20631 182 KTAKSAREALAERLLHEN------LQKRENISELISLR--MLLNDTLStLDEMEKARTHVAMLWASQANTLPATFWSLFY 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 318 LIRHPDIMVKAQEELDIVVG----RDRPVNES------DIAQLPYLQAVIKENFRLhppTPLSLP-HIASESCEI---NG 383
Cdd:cd20631 254 LLRCPEAMKAATKEVKRTLEktgqKVSDGGNPivltreQLDDMPVLGSIIKEALRL---SSASLNiRVAKEDFTLhldSG 330
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 384 --YHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFL-PGGEKSGVDVKGS---DFELIPFGAGRRICAGLSLGLRTI-Q 456
Cdd:cd20631 331 esYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLdENGKEKTTFYKNGrklKYYYMPFGSGTSKCPGRFFAINEIkQ 410
                       250
                ....*....|....
gi 15241483 457 FLTATLVQgFDWEL 470
Cdd:cd20631 411 FLSLMLCY-FDMEL 423
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
253-497 1.13e-08

P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome P450cin (P450cin, also called CYP176A1) and similar proteins. P450cin is a bacterial P450 enzyme that catalyzes the enantiospecific hydroxylation of 1,8-cineole to (1R)-6beta-hydroxycineole; its natural reduction-oxidation partner is cindoxin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 56.96  E-value: 1.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 253 LKEHEMNGQDqkhtDMLSTLISLKGtdldgDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDImvkaqeel 332
Cdd:cd11034 161 IAERRANPRD----DLISRLIEGEI-----DGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPED-------- 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 333 divvgRDRPVNESDIaqlpyLQAVIKENFRLHPPTpLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDP--- 409
Cdd:cd11034 224 -----RRRLIADPSL-----IPNAVEEFLRFYSPV-AGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPdri 292
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 410 -LAFKPERFLpggeksgvdvkgsdfeliPFGAGRRICAGLSLGLRTIQFLTATLVQGF-DWELAGGVTPEKLNMEESYGL 487
Cdd:cd11034 293 dIDRTPNRHL------------------AFGSGVHRCLGSHLARVEARVALTEVLKRIpDFELDPGATCEFLDSGTVRGL 354
                       250
                ....*....|
gi 15241483 488 tlqRAVPLVV 497
Cdd:cd11034 355 ---RTLPVIF 361
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
314-470 2.08e-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: 56.32  E-value: 2.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 314 AIAELIRHPDIMVKAQEELDIVvgrDRPVNesdiaqLPYLQAVIKENFRLHPPTPLSLPHiASESCEINGYHIPKGSTLL 393
Cdd:cd20624 214 ALALLAAHPEQAARAREEAAVP---PGPLA------RPYLRACVLDAVRLWPTTPAVLRE-STEDTVWGGRTVPAGTGFL 283
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15241483 394 TNIWAIARDPDQWSDPLAFKPERFLPGGEKSgvdvkgsDFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWEL 470
Cdd:cd20624 284 IFAPFFHRDDEALPFADRFVPEIWLDGRAQP-------DEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDP 353
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
286-468 2.23e-08

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 56.29  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  286 SLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMVKAQEElDIVVGRDR-----PVNESDIAQLPYLQAVIKEN 360
Cdd:PLN03141 246 ELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVALQQLTEE-NMKLKRLKadtgePLYWTDYMSLPFTQNVITET 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  361 FRLhPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERFlpggEKSgvDVKGSDFEliPFGA 440
Cdd:PLN03141 325 LRM-GNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRW----QEK--DMNNSSFT--PFGG 395
                        170       180
                 ....*....|....*....|....*...
gi 15241483  441 GRRICAGLSLGLRTIQFLTATLVQGFDW 468
Cdd:PLN03141 396 GQRLCPGLDLARLEASIFLHHLVTRFRW 423
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
267-447 6.34e-08

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: 54.68  E-value: 6.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 267 DMLSTLISlkgTDLDGDGgsLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPD--IMVKAQEELDivvgrdrpvne 344
Cdd:cd11038 195 DLISTLVA---AEQDGDR--LSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDqwRALREDPELA----------- 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 345 sdiaqlpylQAVIKENFRLHPPTPLsLPHIASESCEINGYHIPKGSTLLTNIWAIARdpdqwsDPLAFKPERFlpggeks 424
Cdd:cd11038 259 ---------PAAVEEVLRWCPTTTW-ATREAVEDVEYNGVTIPAGTVVHLCSHAANR------DPRVFDADRF------- 315
                       170       180
                ....*....|....*....|...
gi 15241483 425 gvDVKGSDFELIPFGAGRRICAG 447
Cdd:cd11038 316 --DITAKRAPHLGFGGGVHHCLG 336
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
232-416 1.38e-07

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: 53.76  E-value: 1.38e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 232 QGVAGKMKRLHKRFDAFLSSILKEHEMNGQDqkhtDMLSTLISLkgtdlDGDGGSLTDTEIKALLLNMFTAGTDTSASTV 311
Cdd:cd11032 148 EEEVEEMAEALRELNAYLLEHLEERRRNPRD----DLISRLVEA-----EVDGERLTDEEIVGFAILLLIAGHETTTNLL 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 312 DWAIAELIRHPDIMVKAQEeldivvgrdrpvnesDIAQLPylqAVIKENFRLHPPTPlSLPHIASESCEINGYHIPKGST 391
Cdd:cd11032 219 GNAVLCLDEDPEVAARLRA---------------DPSLIP---GAIEEVLRYRPPVQ-RTARVTTEDVELGGVTIPAGQL 279
                       170       180
                ....*....|....*....|....*
gi 15241483 392 LLTNIWAIARDPDQWSDPLAFKPER 416
Cdd:cd11032 280 VIAWLASANRDERQFEDPDTFDIDR 304
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
313-477 2.58e-07

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: 53.14  E-value: 2.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 313 WAIAELIRHPDIMVKAQEELDIVVGRDRP---------VNESDIA-QLPYLQAVIKENFRLH-PPTPLSLPHIASESCEI 381
Cdd:cd20633 246 WLLLYLLKHPEAMKAVREEVEQVLKETGQevkpggpliNLTRDMLlKTPVLDSAVEETLRLTaAPVLIRAVVQDMTLKMA 325
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 382 NG--YHIPKGSTL-LTNIWAIARDPDQWSDPLAFKPERFL-PGGE------KSGVDVKgsdFELIPFGAGRRICAGLSLG 451
Cdd:cd20633 326 NGreYALRKGDRLaLFPYLAVQMDPEIHPEPHTFKYDRFLnPDGGkkkdfyKNGKKLK---YYNMPWGAGVSICPGRFFA 402
                       170       180
                ....*....|....*....|....*.
gi 15241483 452 LRTIQFLTATLVQGFDWELaggVTPE 477
Cdd:cd20633 403 VNEMKQFVFLMLTYFDLEL---VNPD 425
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
330-467 1.73e-06

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: 50.34  E-value: 1.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 330 EELDIVVGRDRPVNESDIAQLPYLQAVIKENFRLHPPTPLSLPH------IASESCeinGYHIPKGSTLLTNIWAIARDP 403
Cdd:cd11071 265 EEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPLQYGRarkdfvIESHDA---SYKIKKGELLVGYQPLATRDP 341
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15241483 404 DQWSDPLAFKPERFLpggeksgvdvkGSDFELIP---FGAGR---------RICAGLSLGLRTIQFLTATLVQGFD 467
Cdd:cd11071 342 KVFDNPDEFVPDRFM-----------GEEGKLLKhliWSNGPeteeptpdnKQCPGKDLVVLLARLFVAELFLRYD 406
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
281-416 1.88e-06

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: 50.22  E-value: 1.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 281 DGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDimvkaqeELDIVvgRDRPvnesdiAQLPylqAVIKEN 360
Cdd:cd11033 199 EVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPD-------QWERL--RADP------SLLP---TAVEEI 260
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15241483 361 FRLHPPTplslPH---IASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPER 416
Cdd:cd11033 261 LRWASPV----IHfrrTATRDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR 315
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
267-409 1.90e-06

cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains bacterial cytochrome P450s, including those belonging to families 105 (CYP105) and 165 (CYP165). Also included in this group are fungal family 55 proteins (CYP55). CYP105s are predominantly found in bacteria belonging to the phylum Actinobacteria and the order Actinomycetales, and are associated with a wide variety of pathways and processes, from steroid biotransformation to production of macrolide metabolites. CYP105A1 catalyzes two sequential hydroxylations of vitamin D3 with differing specificity and cytochrome P450-SOY (also known as CYP105D1) has been shown to be capable of both oxidation and dealkylation reactions. CYP105D6 and CYP105P1, from the filipin biosynthetic pathway, perform highly regio- and stereospecific hydroxylations. Other members of this group include, but are not limited to: CYP165D3 (also called OxyE) from the teicoplanin biosynthetic gene cluster of Actinoplanes teichomyceticus, which is responsible for the phenolic coupling of the aromatic side chains of the first and third peptide residues in the teicoplanin peptide; Micromonospora griseorubida cytochrome P450 MycCI that catalyzes hydroxylation at the C21 methyl group of mycinamicin VIII, the earliest macrolide form in the postpolyketide synthase tailoring pathway; and Fusarium oxysporum CYP55A1 (also called nitric oxide reductase cytochrome P450nor) that catalyzes an unusual reaction, the direct electron transfer from NAD(P)H to bound heme. The CYP105-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 50.21  E-value: 1.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 267 DMLSTLIslkgTDlDGDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMvkaqEELdivvgRDRPVnesd 346
Cdd:cd11030 189 DLLSRLV----AE-HGAPGELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPEQL----AAL-----RADPS---- 250
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15241483 347 iaqlpYLQAVIKENFRLHPPTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDP 409
Cdd:cd11030 251 -----LVPGAVEELLRYLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDP 308
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
289-471 2.62e-06

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 49.76  E-value: 2.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 289 DTEIKALLLNMFTAGTDTSASTVdWAIAELIRHPDIMVKAQEELDIVVGRDRP-------VNESDIAQLPYLQAVIKENF 361
Cdd:cd20634 220 EMQARAMLLQLWATQGNAGPAAF-WLLLFLLKHPEAMAAVRGEIQRIKHQRGQpvsqtltINQELLDNTPVFDSVLSETL 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 362 RLhpptpLSLPHIASES------CEING--YHIPKGSTLLTNIW-AIARDPDQWSDPLAFKPERFL--PGGEK-----SG 425
Cdd:cd20634 299 RL-----TAAPFITREVlqdmklRLADGqeYNLRRGDRLCLFPFlSPQMDPEIHQEPEVFKYDRFLnaDGTEKkdfykNG 373
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15241483 426 VDVKgsdFELIPFGAGRRICAGLSLGLRTIQFLTATLVQGFDWELA 471
Cdd:cd20634 374 KRLK---YYNMPWGAGDNVCIGRHFAVNSIKQFVFLILTHFDVELK 416
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
282-480 3.63e-06

cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Rhodopseudomonas palustris CYP199A2 and CYP199A4. CYP199A2 catalyzes the oxidation of aromatic carboxylic acids including indole-2-carboxylic acid, 2-naphthoic acid and 4-ethylbenzoic acid. CYP199A4 catalyzes the hydroxylation of para-substituted benzoic acids. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 49.12  E-value: 3.63e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 282 GDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDI--MVKAQEELdivvgrdrpvnesdiaqlpyLQAVIKE 359
Cdd:cd11037 193 ADRGEITEDEAPLLMRDYLSAGLDTTISAIGNALWLLARHPDQweRLRADPSL--------------------APNAFEE 252
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 360 NFRLHPPTPlSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERflpggeksgvDVKGSdfelIPFG 439
Cdd:cd11037 253 AVRLESPVQ-TFSRTTTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR----------NPSGH----VGFG 317
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15241483 440 AGRRICAGLSLGLRTIQFLTATLVQGFD-WELAGGVTPeKLN 480
Cdd:cd11037 318 HGVHACVGQHLARLEGEALLTALARRVDrIELAGPPVR-ALN 358
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
282-447 1.18e-04

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 44.34  E-value: 1.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 282 GDGGSLTDTEIKALLLNMFTAGTDTSASTVDWAIAELIRHPDIMvkaqeELdivvGRDRPVNESdiaqlpylqAVIKENF 361
Cdd:cd20619 181 ARAGEITESEAIATILVFYAVGHMAIGYLIASGIELFARRPEVF-----TA----FRNDESARA---------AIINEMV 242
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 362 RLHPpTPLSLPHIASESCEINGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERflpgGEKSGVDvkgsdfelIPFGAG 441
Cdd:cd20619 243 RMDP-PQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTR----PPAASRN--------LSFGLG 309

                ....*.
gi 15241483 442 RRICAG 447
Cdd:cd20619 310 PHSCAG 315
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
354-472 4.59e-04

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: 42.39  E-value: 4.59e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 354 QAVIKENFRLHPPTplslPHIASESCEINGyhiPKGSTLLTNIWAIARDPDQW-SDPLAFKPERFlpggeKSGVDVKGSD 432
Cdd:cd20626 259 KNLVKEALRLYPPT----RRIYRAFQRPGS---SKPEIIAADIEACHRSESIWgPDALEFNPSRW-----SKLTPTQKEA 326
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15241483 433 FelIPFGAGRRIC-AGLSLGLRTIQFLTATLVQGFD--WELAG 472
Cdd:cd20626 327 F--LPFGSGPFRCpAKPVFGPRMIALLVGALLDALGdeWELVS 367
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
302-450 7.29e-04

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: 41.71  E-value: 7.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483 302 AGTDTSASTVDWAIAELIRHPDIMVkaqeeldivvgRDRPVNESdiaqlpyLQAVIKENFRLHPPTPLSlPHIASESCEI 381
Cdd:cd11036 188 QGAEAAAGLVGNAVLALLRRPAQWA-----------RLRPDPEL-------AAAAVAETLRYDPPVRLE-RRFAAEDLEL 248
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15241483 382 NGYHIPKGSTLLTNIWAIARDPDQWSDPLAFKPERflPGGEKSgvdvkgsdfeliPFGAGRRICAGLSL 450
Cdd:cd11036 249 AGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR--PTARSA------------HFGLGRHACLGAAL 303
PLN02648 PLN02648
allene oxide synthase
322-423 3.38e-03

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 39.92  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15241483  322 PDIMVKAQEELDIVVGRDRP-VNESDIAQLPYLQAVIKENFRLHPPTPLSLPHiASESCEI----NGYHIPKGStLLTNI 396
Cdd:PLN02648 304 EELQARLAEEVRSAVKAGGGgVTFAALEKMPLVKSVVYEALRIEPPVPFQYGR-AREDFVIeshdAAFEIKKGE-MLFGY 381
                         90       100
                 ....*....|....*....|....*....
gi 15241483  397 WAIA-RDPDQWSDPLAFKPERFL-PGGEK 423
Cdd:PLN02648 382 QPLVtRDPKVFDRPEEFVPDRFMgEEGEK 410
 
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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