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Conserved domains on  [gi|86198312|ref|NP_803125|]
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cytochrome P450 4A12A precursor [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 70-503 0e+00

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: 896.64  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  70 LQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRSDPKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFH 149
Cdd:cd20678   1 LQKILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 150 YDILKPYTEIMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNDLVFSR 229
Cdd:cd20678  81 YDILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 230 VRNIFHQNDIIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDL 309
Cdd:cd20678 161 LRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 310 RAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSR 389
Cdd:cd20678 241 RAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISR 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 390 ELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKV 467
Cdd:cd20678 321 ELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSskRHSHAFLPFSAGPRNCIGQQFAMNEMKV 400

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 86198312 468 AVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIHLH 503
Cdd:cd20678 401 AVALTLLRFELLPDPTRIPIPIPQLVLKSKNGIHLY 436
 
Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 70-503 0e+00

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: 896.64  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  70 LQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRSDPKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFH 149
Cdd:cd20678   1 LQKILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 150 YDILKPYTEIMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNDLVFSR 229
Cdd:cd20678  81 YDILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 230 VRNIFHQNDIIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDL 309
Cdd:cd20678 161 LRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 310 RAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSR 389
Cdd:cd20678 241 RAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISR 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 390 ELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKV 467
Cdd:cd20678 321 ELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSskRHSHAFLPFSAGPRNCIGQQFAMNEMKV 400

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 86198312 468 AVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIHLH 503
Cdd:cd20678 401 AVALTLLRFELLPDPTRIPIPIPQLVLKSKNGIHLY 436
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 52-502 4.38e-150

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: 437.10  E-value: 4.38e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312    52 PSPPSHWLFGHKILKDQD--LQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRS--DPKANGSYRFLA----P 123
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKgeEFSGRPDEPWFAtsrgP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   124 WIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHE 203
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   204 GSVQLDRKYKSYIQAVEDLNDLV-FSRVRNIFHQNDIIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKlk 282
Cdd:pfam00067 162 FGSLEDPKFLELVKAVQELSSLLsSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKKSPR-- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   283 kkrrlDFLDILLFARM-ENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITW 361
Cdd:pfam00067 240 -----DFLDALLLAKEeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   362 NDLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFPdGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAP--GS 438
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIP-GYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDenGK 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86198312   439 SRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPR---IVLKSKNGIHL 502
Cdd:pfam00067 394 FRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDEtpgLLLPPKPYKLK 460
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 97-494 6.89e-64

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: 212.83  E-value: 6.89e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  97 VYDPDYMKLILGRSD--PKANGSYRFLAP--WIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWE 172
Cdd:COG2124  47 VTRYEDVREVLRDPRtfSSDGGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIREIADELLDRLA 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 173 QivgqDSTLEIFRHITLMTLDTIMKCAFSHEGSvqlDRkyksyiQAVEDLNDLVFSRVRNIFHQNDIiyrvssngcKANS 252
Cdd:COG2124 127 A----RGPVDLVEEFARPLPVIVICELLGVPEE---DR------DRLRRWSDALLDALGPLPPERRR---------RARR 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 253 ACKLAHDHTDQVIKSRRIQLQDeeeleklkkkrrlDFLDILLFARmENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIF 332
Cdd:COG2124 185 ARAELDAYLRELIAERRAEPGD-------------DLLSALLAAR-DDGERLSDEELRDELLLLLLAGHETTANALAWAL 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 333 YALATNPEHQQRCRKEIqsllgdgtsitwndldkmPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLS 412
Cdd:COG2124 251 YALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTATEDVEL-GGVTIPAGDRVLLS 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 413 FYGLHHNPTVWPNPEVFDPsrfapgsSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELL-PDPTRVPIPIPR 491
Cdd:COG2124 312 LAAANRDPRVFPDPDRFDP-------DRPPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPDLrLAPPEELRWRPS 384


                ...
gi 86198312 492 IVL 494
Cdd:COG2124 385 LTL 387
PLN02290 PLN02290
cytokinin trans-hydroxylase
 90-507 2.34e-47

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 171.92  E-value: 2.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   90 GSKVRIQVYDPDYMKLIL-------GRSDPKANGSYRFlapwIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMAD 162
Cdd:PLN02290 102 GTEPRLCLTETELIKELLtkyntvtGKSWLQQQGTKHF----IGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  163 SVRVMLDKWEQIVGQDST-LEIFRHITLMTLDTIMKCAF--SHEgsvqldrKYKSYIQAVEDLNDLVFSRVRNIFHQNDI 239
Cdd:PLN02290 178 CTKQMLQSLQKAVESGQTeVEIGEYMTRLTADIISRTEFdsSYE-------KGKQIFHLLTVLQRLCAQATRHLCFPGSR 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  240 IYRvssngCKANSACKLAHDHTDQVIKsRRIQLQDEEELEKLKKKRRLDFLDILLfARME----NGKSLSDKDLRAEVDT 315
Cdd:PLN02290 251 FFP-----SKYNREIKSLKGEVERLLM-EIIQSRRDCVEIGRSSSYGDDLLGMLL-NEMEkkrsNGFNLNLQLIMDECKT 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  316 FMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSiTWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPV 395
Cdd:PLN02290 324 FFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETP-SVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDI 402

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  396 TFPDGRsLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFA---PGSSRHshsFLPFSGGARNCIGKQFAMNELKVAVAL 471
Cdd:PLN02290 403 KLGDLH-IPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAgrpFAPGRH---FIPFAAGPRNCIGQAFAMMEAKIILAM 478

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 86198312  472 TLLRFELLPDPTRVPIPIPRIVLKSKNGIHLHLKKL 507
Cdd:PLN02290 479 LISKFSFTISDNYRHAPVVVLTIKPKYGVQVCLKPL 514
 
Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 70-503 0e+00

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: 896.64  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  70 LQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRSDPKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFH 149
Cdd:cd20678   1 LQKILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFH 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 150 YDILKPYTEIMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNDLVFSR 229
Cdd:cd20678  81 YDILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 230 VRNIFHQNDIIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDL 309
Cdd:cd20678 161 LRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDL 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 310 RAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSR 389
Cdd:cd20678 241 RAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISR 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 390 ELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKV 467
Cdd:cd20678 321 ELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSskRHSHAFLPFSAGPRNCIGQQFAMNEMKV 400

                       410       420       430
                ....*....|....*....|....*....|....*.
gi 86198312 468 AVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIHLH 503
Cdd:cd20678 401 AVALTLLRFELLPDPTRIPIPIPQLVLKSKNGIHLY 436
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 81-502 0e+00

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: 615.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  81 PSACPQWLWGSKVRIQVYDPDYMKLILGRSDPKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIM 160
Cdd:cd20659   1 PRAYVFWLGPFRPILVLNHPDTIKAVLKTSEPKDRDSYRFLKPWLGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 161 ADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNDLVFSRVRNIFHQNDII 240
Cdd:cd20659  81 NECTDILLEKWSKLAETGESVEVFEDISLLTLDIILRCAFSYKSNCQQTGKNHPYVAAVHELSRLVMERFLNPLLHFDWI 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 241 YRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDeEELEKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEG 320
Cdd:cd20659 161 YYLTPEGRRFKKACDYVHKFAEEIIKKRRKELED-NKDEALSKRKYLDFLDILLTARDEDGKGLTDEEIRDEVDTFLFAG 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 321 HDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDG 400
Cdd:cd20659 240 HDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITI-DG 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 401 RSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFEL 478
Cdd:cd20659 319 VTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIkkRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFEL 398

                       410       420
                ....*....|....*....|....
gi 86198312 479 LPDPTRVPIPIPRIVLKSKNGIHL 502
Cdd:cd20659 399 SVDPNHPVEPKPGLVLRSKNGIKL 422
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 70-503 2.67e-178

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: 508.08  E-value: 2.67e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  70 LQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRSD---PKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTP 146
Cdd:cd20679   1 LQVVTQLVATYPQGCLWWLGPFYPIIRLFHPDYIRPVLLASAavaPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 147 AFHYDILKPYTEIMADSVRVMLDKWEQIVGQDST-LEIFRHITLMTLDTIMKCAFSHEGSVQldRKYKSYIQAVEDLNDL 225
Cdd:cd20679  81 AFHFNILKPYVKIFNQSTNIMHAKWRRLASEGSArLDMFEHISLMTLDSLQKCVFSFDSNCQ--EKPSEYIAAILELSAL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 226 VFSRVRNIFHQNDIIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKR---RLDFLDILLFARMENGK 302
Cdd:cd20679 159 VVKRQQQLLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLKAKAkskTLDFIDVLLLSKDEDGK 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 303 SLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTS--ITWNDLDKMPYTTMCIKEALRI 380
Cdd:cd20679 239 ELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPeeIEWDDLAQLPFLTMCIKESLRL 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 381 YPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGK 458
Cdd:cd20679 319 HPPVTAISRCCTQDIVLPDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSqgRSPLAFIPFSAGPRNCIGQ 398

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 86198312 459 QFAMNELKVAVALTLLRFELLPDpTRVPIPIPRIVLKSKNGIHLH 503
Cdd:cd20679 399 TFAMAEMKVVLALTLLRFRVLPD-DKEPRRKPELILRAEGGLWLR 442
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 88-502 3.15e-159

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: 458.91  E-value: 3.15e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  88 LW-GSKVRIQVYDPDYMKLILGRSDPKANGS-YRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVR 165
Cdd:cd20628   6 LWiGPKPYVVVTNPEDIEVILSSSKLITKSFlYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFNENSK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 166 VMLDKWEQIVGQDStLEIFRHITLMTLDTIMKCAFSHEGSVQLDrKYKSYIQAVEDLNDLVFSRVRNIFHQNDIIYRVSS 245
Cdd:cd20628  86 ILVEKLKKKAGGGE-FDIFPYISLCTLDIICETAMGVKLNAQSN-EDSEYVKAVKRILEIILKRIFSPWLRFDFIFRLTS 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 246 NGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKRRL----DFLDILLFARMENGkSLSDKDLRAEVDTFMFEGH 321
Cdd:cd20628 164 LGKEQRKALKVLHDFTNKVIKERREELKAEKRNSEEDDEFGKkkrkAFLDLLLEAHEDGG-PLTDEDIREEVDTFMFAGH 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 322 DTTASGISWIFYALATNPEHQQRCRKEIQSLLG-DGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDG 400
Cdd:cd20628 243 DTTASAISFTLYLLGLHPEVQEKVYEELDEIFGdDDRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKL-DG 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 401 RSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFEL 478
Cdd:cd20628 322 YTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSakRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRV 401

                       410       420
                ....*....|....*....|....*
gi 86198312 479 LPDPTR-VPIPIPRIVLKSKNGIHL 502
Cdd:cd20628 402 LPVPPGeDLKLIAEIVLRSKNGIRV 426
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 52-502 4.38e-150

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: 437.10  E-value: 4.38e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312    52 PSPPSHWLFGHKILKDQD--LQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRS--DPKANGSYRFLA----P 123
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKgeEFSGRPDEPWFAtsrgP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   124 WIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHE 203
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   204 GSVQLDRKYKSYIQAVEDLNDLV-FSRVRNIFHQNDIIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKlk 282
Cdd:pfam00067 162 FGSLEDPKFLELVKAVQELSSLLsSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKKSPR-- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   283 kkrrlDFLDILLFARM-ENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITW 361
Cdd:pfam00067 240 -----DFLDALLLAKEeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   362 NDLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFPdGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAP--GS 438
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIP-GYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDenGK 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86198312   439 SRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPR---IVLKSKNGIHL 502
Cdd:pfam00067 394 FRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDEtpgLLLPPKPYKLK 460
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 87-502 2.62e-118

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: 354.65  E-value: 2.62e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  87 WLwGSKVRIQVYDPDYMKLILGRSD--PKANgSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSV 164
Cdd:cd20660   7 WL-GPKPIVVLYSAETVEVILSSSKhiDKSF-EYDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDFLDVFNEQS 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 165 RVMLDKWEQIVGqDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDrKYKSYIQAVEDLNDLVFSRVRNIFHQNDIIYRVS 244
Cdd:cd20660  85 EILVKKLKKEVG-KEEFDIFPYITLCALDIICETAMGKSVNAQQN-SDSEYVKAVYRMSELVQKRQKNPWLWPDFIYSLT 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 245 SNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKRRL-------DFLDILLFARmENGKSLSDKDLRAEVDTFM 317
Cdd:cd20660 163 PDGREHKKCLKILHGFTNKVIQERKAELQKSLEEEEEDDEDADigkrkrlAFLDLLLEAS-EEGTKLSDEDIREEVDTFM 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 318 FEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGT-SITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVT 396
Cdd:cd20660 242 FEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSDrPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIE 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 397 FpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLL 474
Cdd:cd20660 322 I-GGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSagRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILR 400

                       410       420
                ....*....|....*....|....*....
gi 86198312 475 RFELLPDPTRVPI-PIPRIVLKSKNGIHL 502
Cdd:cd20660 401 NFRIESVQKREDLkPAGELILRPVDGIRV 429
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 97-502 2.77e-100

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: 307.58  E-value: 2.77e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  97 VYDPDYMKLIL---GRSDPKaNGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQ 173
Cdd:cd20620  16 VTHPDHIQHVLvtnARNYVK-GGVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAMVEATAALLDRWEA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 174 ivGQDS-TLEIFRHITLMTLDTIMKCAFShegsVQLDRKYKSYIQAVEDLNDLVFSRVRNIFHqndIIYRVSSngcKANS 252
Cdd:cd20620  95 --GARRgPVDVHAEMMRLTLRIVAKTLFG----TDVEGEADEIGDALDVALEYAARRMLSPFL---LPLWLPT---PANR 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 253 ACKLAHDHTDQV----IKSRRIQLQDEEeleklkkkrrlDFLDILLFARM-ENGKSLSDKDLRAEVDTFMFEGHDTTASG 327
Cdd:cd20620 163 RFRRARRRLDEViyrlIAERRAAPADGG-----------DLLSMLLAARDeETGEPMSDQQLRDEVMTLFLAGHETTANA 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 328 ISWIFYALATNPEHQQRCRKEIQSLLGDGTsITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRsLPKGI 407
Cdd:cd20620 232 LSWTWYLLAQHPEVAARLRAEVDRVLGGRP-PTAEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYR-IPAGS 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 408 HVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRV 485
Cdd:cd20620 310 TVLISPYVTHRDPRFWPDPEAFDPERFTPEREaaRPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPGQP 389

                       410
                ....*....|....*..
gi 86198312 486 PIPIPRIVLKSKNGIHL 502
Cdd:cd20620 390 VEPEPLITLRPKNGVRM 406
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 97-500 2.23e-89

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: 280.49  E-value: 2.23e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  97 VYDPDYMKLILGRSDP-KANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQIV 175
Cdd:cd20680  27 LYHAENVEVILSSSKHiDKSYLYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFHFTILSDFLEVMNEQSNILVEKLEKHV 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 176 GQDStLEIFRHITLMTLDTIMKCAFSHEGSVQlDRKYKSYIQAVEDLNDLVFSRVRNIFHQNDIIYRVSSNGCKANSACK 255
Cdd:cd20680 107 DGEA-FNCFFDITLCALDIICETAMGKKIGAQ-SNKDSEYVQAVYRMSDIIQRRQKMPWLWLDLWYLMFKEGKEHNKNLK 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 256 LAHDHTDQVIKSRRIQLQ------DEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGIS 329
Cdd:cd20680 185 ILHTFTDNVIAERAEEMKaeedktGDSDGESPSKKKRKAFLDMLLSVTDEEGNKLSHEDIREEVDTFMFEGHDTTAAAMN 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 330 WIFYALATNPEHQQRCRKEIQSLLGDGT-SITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIH 408
Cdd:cd20680 265 WSLYLLGSHPEVQRKVHKELDEVFGKSDrPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEI-RGFKVPKGVN 343

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 409 VMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVP 486
Cdd:cd20680 344 AVIIPYALHRDPRYFPEPEEFRPERFFPENSsgRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVEANQKREE 423

                       410
                ....*....|....*
gi 86198312 487 I-PIPRIVLKSKNGI 500
Cdd:cd20680 424 LgLVGELILRPQNGI 438
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 87-494 2.51e-88

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: 276.32  E-value: 2.51e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  87 WLWGSKVRIqVYDPDYMKLIL---GRSDPKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADS 163
Cdd:cd00302   7 RLGGGPVVV-VSDPELVREVLrdpRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVIREI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 164 VRVMLDKWEQIVGQDstLEIFRHITLMTLDTIMKCAFSHEGSVQLDRkyksYIQAVEDLNDLVFSRVRNIFHQNDIIyrv 243
Cdd:cd00302  86 ARELLDRLAAGGEVG--DDVADLAQPLALDVIARLLGGPDLGEDLEE----LAELLEALLKLLGPRLLRPLPSPRLR--- 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 244 ssngcKANSACKLAHDHTDQVIKSRRIQLQDEeeleklkkkrrldfLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDT 323
Cdd:cd00302 157 -----RLRRARARLRDYLEELIARRRAEPADD--------------LDLLLLADADDGGGLSDEEIVAELLTLLLAGHET 217

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 324 TASGISWIFYALATNPEHQQRCRKEIQSLLGDGTsitWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSL 403
Cdd:cd00302 218 TASLLAWALYLLARHPEVQERLRAEIDAVLGDGT---PEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVEL-GGYTI 293

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 404 PKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPT 483
Cdd:cd00302 294 PAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPD 373

                       410
                ....*....|.
gi 86198312 484 RVPIPIPRIVL 494
Cdd:cd00302 374 EELEWRPSLGT 384
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 126-500 4.18e-87

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: 274.08  E-value: 4.18e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 126 GRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGS 205
Cdd:cd11055  49 DSSLLFLKGERWKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVD 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 206 VQLDRKyksyiqavedlnDLVFSRVRNIFHQNDIIY----------------RVSSNGCKANSACKlahDHTDQVIKSRR 269
Cdd:cd11055 129 SQNNPD------------DPFLKAAKKIFRNSIIRLflllllfplrlflfllFPFVFGFKSFSFLE---DVVKKIIEQRR 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 270 IQLQdeeeleklkkKRRLDFLDILLFAR----MENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRC 345
Cdd:cd11055 194 KNKS----------SRRKDLLQLMLDAQdsdeDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKL 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 346 RKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPN 425
Cdd:cd11055 264 IEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFISRECKEDCTI-NGVFIPKGVDVVIPVYAIHHDPEFWPD 342

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 86198312 426 PEVFDPSRFAPGS--SRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDP-TRVPIPI-PRIVLKSKNGI 500
Cdd:cd11055 343 PEKFDPERFSPENkaKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKeTEIPLKLvGGATLSPKNGI 421
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 87-478 1.60e-84

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: 267.55  E-value: 1.60e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  87 WLwGSKVRIQVYDPDYMKLILgrSDP----KANgSYRFLapWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMAD 162
Cdd:cd11057   7 WL-GPRPFVITSDPEIVQVVL--NSPhclnKSF-FYDFF--RLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIFNE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 163 SVRVMLDKWEQIVGQDsTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKyKSYIQAVEDLNDLVFSRVRNIFHQNDIIYR 242
Cdd:cd11057  81 EAQKLVQRLDTYVGGG-EFDILPDLSRCTLEMICQTTLGSDVNDESDGN-EEYLESYERLFELIAKRVLNPWLHPEFIYR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 243 VSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKRRLD----FLDiLLFARMENGKSLSDKDLRAEVDTFMF 318
Cdd:cd11057 159 LTGDYKEEQKARKILRAFSEKIIEKKLQEVELESNLDSEEDEENGRkpqiFID-QLLELARNGEEFTDEEIMDEIDTMIF 237

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 319 EGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGD-GTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTF 397
Cdd:cd11057 238 AGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDdGQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQL 317

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 398 PDGRSLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLL 474
Cdd:cd11057 318 SNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSaqRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILR 397


                ....
gi 86198312 475 RFEL 478
Cdd:cd11057 398 NYRL 401
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 87-501 9.67e-79

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: 252.65  E-value: 9.67e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  87 WLwGSKVRIQVYDPDYMKLILGRSDPKANGSY--RFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSV 164
Cdd:cd11052  18 WY-GTDPRLYVTEPELIKELLSKKEGYFGKSPlqPGLKKLLGRGLVMSNGEKWAKHRRIANPAFHGEKLKGMVPAMVESV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 165 RVMLDKWEQIVG-QDSTLEIFRHITLMTLDTIMKCAFsheGSvqldrkykSYIQAVEdlndlVFSRVRN----IFHQNDI 239
Cdd:cd11052  97 SDMLERWKKQMGeEGEEVDVFEEFKALTADIISRTAF---GS--------SYEEGKE-----VFKLLRElqkiCAQANRD 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 240 IYRVSSNGCKANS---ACKLAHDHTD---QVIKSRRIQLQDeeeleKLKKKRRLDFLDILLFARM--ENGKSLSDKDLRA 311
Cdd:cd11052 161 VGIPGSRFLPTKGnkkIKKLDKEIEDsllEIIKKREDSLKM-----GRGDDYGDDLLGLLLEANQsdDQNKNMTVQEIVD 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 312 EVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGtSITWNDLDKMPYTTMCIKEALRIYPPVPSVSREL 391
Cdd:cd11052 236 ECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKD-KPPSDSLSKLKTVSMVINESLRLYPPAVFLTRKA 314

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 392 SSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPN-PEVFDPSRFAPGSSR---HSHSFLPFSGGARNCIGKQFAMNELKV 467
Cdd:cd11052 315 KEDIKL-GGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGVAKaakHPMAFLPFGLGPRNCIGQNFATMEAKI 393

                       410       420       430
                ....*....|....*....|....*....|....
gi 86198312 468 AVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIH 501
Cdd:cd11052 394 VLAMILQRFSFTLSPTYRHAPTVVLTLRPQYGLQ 427
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 94-499 1.27e-77

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: 249.88  E-value: 1.27e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  94 RIQVYDPDYMKLILGRSD---PKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDK 170
Cdd:cd11069  15 RLLVTDPKALKHILVTNSydfEKPPAFRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKELYPIFWSKAEELVDK 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 171 WEQIV----GQDSTLEIFRHITLMTLDTIMKCAFSHE-GSvqLDRKYKSYIQAVEDLND-----LVFSRVRNIFHQNDII 240
Cdd:cd11069  95 LEEEIeesgDESISIDVLEWLSRATLDIIGLAGFGYDfDS--LENPDNELAEAYRRLFEptllgSLLFILLLFLPRWLVR 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 241 YRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLkkkrrlDFLDILLFARME-NGKSLSDKDLRAEVDTFMFE 319
Cdd:cd11069 173 ILPWKANREIRRAKDVLRRLAREIIREKKAALLEGKDDSGK------DILSILLRANDFaDDERLSDEELIDQILTFLAA 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 320 GHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGD--GTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPvTF 397
Cdd:cd11069 247 GHETTSTALTWALYLLAKHPDVQERLREEIRAALPDppDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKD-TV 325

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 398 PDGRSLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRF-APGSSRHS------HSFLPFSGGARNCIGKQFAMNELKVAV 469
Cdd:cd11069 326 IKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWlEPDGAASPggagsnYALLTFLHGPRSCIGKKFALAEMKVLL 405

                       410       420       430
                ....*....|....*....|....*....|.
gi 86198312 470 ALTLLRFELLPDP-TRVPIPIPRIVLKSKNG 499
Cdd:cd11069 406 AALVSRFEFELDPdAEVERPIGIITRPPVDG 436
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 97-493 2.65e-76

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: 245.96  E-value: 2.65e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  97 VYDPDYMKLILgRSDP------KANGSyrfLAPWIG-RGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLD 169
Cdd:cd11053  28 LSDPEAIKQIF-TADPdvlhpgEGNSL---LEPLLGpNSLLLLDGDRHRRRRKLLMPAFHGERLRAYGELIAEITEREID 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 170 KWeqIVGQD-STLEIFRHITLmtlDTIMKCAFSHEGSVQLDRkyksYIQAVEDLNDLVFSRVRNIFHQNDIIYRVSSNGc 248
Cdd:cd11053 104 RW--PPGQPfDLRELMQEITL---EVILRVVFGVDDGERLQE----LRRLLPRLLDLLSSPLASFPALQRDLGPWSPWG- 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 249 KANSACKLAHDHTDQVIKSRRIQlqdeeeleklKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGI 328
Cdd:cd11053 174 RFLRARRRIDALIYAEIAERRAE----------PDAERDDILSLLLSARDEDGQPLSDEELRDELMTLLFAGHETTATAL 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 329 SWIFYALATNPEHQQRCRKEIQSLLGDGTSitwNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIH 408
Cdd:cd11053 244 AWAFYWLHRHPEVLARLLAELDALGGDPDP---EDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVEL-GGYTLPAGTT 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 409 VMLSFYGLHHNPTVWPNPEVFDPSRFApGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIP 488
Cdd:cd11053 320 VAPSIYLTHHRPDLYPDPERFRPERFL-GRKPSPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPERP 398


                ....*
gi 86198312 489 IPRIV 493
Cdd:cd11053 399 VRRGV 403
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 90-500 3.29e-76

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: 246.51  E-value: 3.29e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  90 GSKVRIQVYDPDYMKLIL---GRSDPKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRV 166
Cdd:cd11046  19 GPKSFLVISDPAIAKHVLrsnAFSYDKKGLLAEILEPIMGKGLIPADGEIWKKRRRALVPALHKDYLEMMVRVFGRCSER 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 167 MLDKWEQIVGQDSTLEI---FRHitlMTLDTIMKCAFSHE-GSVQLDrkyKSYIQAVedLNDLVFSRVRNIFH----QND 238
Cdd:cd11046  99 LMEKLDAAAETGESVDMeeeFSS---LTLDIIGLAVFNYDfGSVTEE---SPVIKAV--YLPLVEAEHRSVWEppywDIP 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 239 IIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMF 318
Cdd:cd11046 171 AALFIVPRQRKFLRDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDYLNEDDPSLLRFLVDMRDEDVDSKQLRDDLMTMLI 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 319 EGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFP 398
Cdd:cd11046 251 AGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLP 330

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 399 DGR-SLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSH------SFLPFSGGARNCIGKQFAMNELKVAVAL 471
Cdd:cd11046 331 GGGvKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNeviddfAFLPFGGGPRKCLGDQFALLEATVALAM 410

                       410       420       430
                ....*....|....*....|....*....|
gi 86198312 472 TLLRFELLPDPTRVPIP-IPRIVLKSKNGI 500
Cdd:cd11046 411 LLRRFDFELDVGPRHVGmTTGATIHTKNGL 440
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 129-501 7.43e-71

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: 232.04  E-value: 7.43e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 129 LLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFShegsvqL 208
Cdd:cd11056  53 LFSLDGEKWKELRQKLTPAFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFG------L 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 209 DrkyksyIQAVEDLNDLVFSRVRNIFHQN--DIIYRVSSNGCKansacKLAH---------DHTD-------QVIKSRRi 270
Cdd:cd11056 127 D------ANSLNDPENEFREMGRRLFEPSrlRGLKFMLLFFFP-----KLARllrlkffpkEVEDffrklvrDTIEYRE- 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 271 qlqdeeelekLKKKRRLDFLDILLFAR-------MENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQ 343
Cdd:cd11056 195 ----------KNNIVRNDFIDLLLELKkkgkiedDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQE 264

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 344 RCRKEIQSLL--GDGtSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGR-SLPKGIHVMLSFYGLHHNP 420
Cdd:cd11056 265 KLREEIDEVLekHGG-ELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDvVIEKGTPVIIPVYALHHDP 343

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 421 TVWPNPEVFDPSRFAPG--SSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDP-TRVPIPI--PRIVLK 495
Cdd:cd11056 344 KYYPEPEKFDPERFSPEnkKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSkTKIPLKLspKSFVLS 423


                ....*.
gi 86198312 496 SKNGIH 501
Cdd:cd11056 424 PKGGIW 429
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 118-494 1.98e-69

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: 227.91  E-value: 1.98e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 118 YRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQivGQdsTLEIFRHITLMTLDTIMK 197
Cdd:cd11049  51 FDRARPLLGNGLATCPGEDHRRQRRLMQPAFHRSRIPAYAEVMREEAEALAGSWRP--GR--VVDVDAEMHRLTLRVVAR 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 198 CAFShegsVQLDRKYKSYIQavEDLNDLVfsrvRNIFHQN---DIIYRVSSngcKANSACKLA----HDHTDQVIKSRRI 270
Cdd:cd11049 127 TLFS----TDLGPEAAAELR--QALPVVL----AGMLRRAvppKFLERLPT---PGNRRFDRAlarlRELVDEIIAEYRA 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 271 QLQDEEeleklkkkrrlDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQ 350
Cdd:cd11049 194 SGTDRD-----------DLLSLLLAARDEEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELD 262

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 351 SLLGdGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFD 430
Cdd:cd11049 263 AVLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVEL-GGHRLPAGTEVAFSPYALHRDPEVYPDPERFD 340

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86198312 431 PSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPRIVL 494
Cdd:cd11049 341 PDRWLPGRAaaVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPVPGRPVRPRPLATL 406
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 92-481 7.09e-68

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: 224.32  E-value: 7.09e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  92 KVRIQVYDPDYMKLILGRSD-PKANGSYRFLA-----PWIGRGLLM-LDGQTWFQHRRMLTPAFHYDILKPYTEIMADSV 164
Cdd:cd20613  22 RPIVVVSDPEAVKEVLITLNlPKPPRVYSRLAflfgeRFLGNGLVTeVDHEKWKKRRAILNPAFHRKYLKNLMDEFNESA 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 165 RVMLDKWEQIVgqDSTLEI--FRHITLMTLDTIMKCAFSHE-GSV-QLDRKYKSYIQAVedLNDLVFSRvRNIFHQ---N 237
Cdd:cd20613 102 DLLVEKLSKKA--DGKTEVnmLDEFNRVTLDVIAKVAFGMDlNSIeDPDSPFPKAISLV--LEGIQESF-RNPLLKynpS 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 238 DIIYRVssngcKANSACKLAHDHTDQVIKSRRIQLQDEEELEKlkkkrrldflDIL--LFARMENGKSLSDKDLRAEVDT 315
Cdd:cd20613 177 KRKYRR-----EVREAIKFLRETGRECIEERLEALKRGEEVPN----------DILthILKASEEEPDFDMEELLDDFVT 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 316 FMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPV 395
Cdd:cd20613 242 FFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDI 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 396 TFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS--RHSHSFLPFSGGARNCIGKQFAMNELKVAVA--L 471
Cdd:cd20613 322 EL-GGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPekIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAklL 400

                       410
                ....*....|
gi 86198312 472 TLLRFELLPD 481
Cdd:cd20613 401 QNFKFELVPG 410
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 97-494 6.89e-64

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: 212.83  E-value: 6.89e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  97 VYDPDYMKLILGRSD--PKANGSYRFLAP--WIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWE 172
Cdd:COG2124  47 VTRYEDVREVLRDPRtfSSDGGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIREIADELLDRLA 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 173 QivgqDSTLEIFRHITLMTLDTIMKCAFSHEGSvqlDRkyksyiQAVEDLNDLVFSRVRNIFHQNDIiyrvssngcKANS 252
Cdd:COG2124 127 A----RGPVDLVEEFARPLPVIVICELLGVPEE---DR------DRLRRWSDALLDALGPLPPERRR---------RARR 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 253 ACKLAHDHTDQVIKSRRIQLQDeeeleklkkkrrlDFLDILLFARmENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIF 332
Cdd:COG2124 185 ARAELDAYLRELIAERRAEPGD-------------DLLSALLAAR-DDGERLSDEELRDELLLLLLAGHETTANALAWAL 250

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 333 YALATNPEHQQRCRKEIqsllgdgtsitwndldkmPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLS 412
Cdd:COG2124 251 YALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTATEDVEL-GGVTIPAGDRVLLS 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 413 FYGLHHNPTVWPNPEVFDPsrfapgsSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELL-PDPTRVPIPIPR 491
Cdd:COG2124 312 LAAANRDPRVFPDPDRFDP-------DRPPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPDLrLAPPEELRWRPS 384


                ...
gi 86198312 492 IVL 494
Cdd:COG2124 385 LTL 387
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 137-482 8.64e-64

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: 213.59  E-value: 8.64e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 137 WFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQIvGQDSTLEIFRHITLMTLDTIMKCAFSHE-GSVQLDRKYkSY 215
Cdd:cd11068  72 WGKAHRILMPAFGPLAMRGYFPMMLDIAEQLVLKWERL-GPDEPIDVPDDMTRLTLDTIALCGFGYRfNSFYRDEPH-PF 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 216 IQAVEDLNDLVFSRVRNIFHQNDIiYRVSSNGCKANSAckLAHDHTDQVIKSRRiqlqdeeeleKLKKKRRLDFLDILLF 295
Cdd:cd11068 150 VEAMVRALTEAGRRANRPPILNKL-RRRAKRQFREDIA--LMRDLVDEIIAERR----------ANPDGSPDDLLNLMLN 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 296 AR-MENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTsITWNDLDKMPYTTMCI 374
Cdd:cd11068 217 GKdPETGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDP-PPYEQVAKLRYIRRVL 295

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 375 KEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFAPG--SSRHSHSFLPFSGG 451
Cdd:cd11068 296 DETLRLWPTAPAFARKPKEDTVLGGKYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEefRKLPPNAWKPFGNG 375

                       330       340       350
                ....*....|....*....|....*....|.
gi 86198312 452 ARNCIGKQFAMNELKVAVALTLLRFELLPDP 482
Cdd:cd11068 376 QRACIGRQFALQEATLVLAMLLQRFDFEDDP 406
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 128-491 5.52e-61

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: 205.98  E-value: 5.52e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 128 GLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQivgqDSTLEIFRHITLMTLDTIMK--CAFSHEGS 205
Cdd:cd11044  70 SLSLQDGEEHRRRRKLLAPAFSREALESYVPTIQAIVQSYLRKWLK----AGEVALYPELRRLTFDVAARllLGLDPEVE 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 206 V-QLDRKYKSYIQAVEDLN-DLVFSRVRnifhqndiiyrvssngcKANSACKLAHDHTDQVIKSRRIQLQdeeeleklkk 283
Cdd:cd11044 146 AeALSQDFETWTDGLFSLPvPLPFTPFG-----------------RAIRARNKLLARLEQAIRERQEEEN---------- 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 284 KRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEiQSLLGDGTSITWND 363
Cdd:cd11044 199 AEAKDALGLLLEAKDEDGEPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQE-QDALGLEEPLTLES 277

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 364 LDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS---R 440
Cdd:cd11044 278 LKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFEL-GGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSedkK 356

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 86198312 441 HSHSFLPFSGGARNCIGKQFAMNELKVaVALTLLR---FELLP--DPTRVPIPIPR 491
Cdd:cd11044 357 KPFSLIPFGGGPRECLGKEFAQLEMKI-LASELLRnydWELLPnqDLEPVVVPTPR 411
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 87-491 2.15e-60

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: 204.09  E-value: 2.15e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  87 WLWGSKVR-IQVYDPDYMKLILgRSDPKA----NGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMA 161
Cdd:cd11045  15 WTGMLGLRvVALLGPDANQLVL-RNRDKAfsskQGWDPVIGPFFHRGLMLLDFDEHRAHRRIMQQAFTRSALAGYLDRMT 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 162 DSVRVMLDKWeqiVGQDStLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNDLVFSRVRNIfhqndIIY 241
Cdd:cd11045  94 PGIERALARW---PTGAG-FQFYPAIKELTLDLATRVFLGVDLGPEADKVNKAFIDTVRASTAIIRTPIPGT-----RWW 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 242 RvssnGCKANSA-CKLAHDHtdqvIKSRRIQLQDeeeleklkkkrrlDFLDILLFARMENGKSLSDKDLRAEVDTFMFEG 320
Cdd:cd11045 165 R----GLRGRRYlEEYFRRR----IPERRAGGGD-------------DLFSALCRAEDEDGDRFSDDDIVNHMIFLMMAA 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 321 HDTTASGISWIFYALATNPEHQQRCRKEIQSlLGDGTsITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDG 400
Cdd:cd11045 224 HDTTTSTLTSMAYFLARHPEWQERLREESLA-LGKGT-LDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEV-LG 300

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 401 RSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS---RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFE 477
Cdd:cd11045 301 YRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAedkVHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFR 380

                       410       420
                ....*....|....*....|
gi 86198312 478 LL------PDPTRVPIPIPR 491
Cdd:cd11045 381 WWsvpgyyPPWWQSPLPAPK 400
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 97-481 4.66e-60

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: 203.60  E-value: 4.66e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  97 VYDPDYMKLILgrSDPKANGSYRFLAP---WI--GRGLLMLDGQTWFQHRRMLTPAF--HYDIlKPYTEIMADSVRVMLD 169
Cdd:cd20617  16 LSDPEIIKEAF--VKNGDNFSDRPLLPsfeIIsgGKGILFSNGDYWKELRRFALSSLtkTKLK-KKMEELIEEEVNKLIE 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 170 KWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNDLV-FSRVRNIFHQNDIIYRVSSNgc 248
Cdd:cd20617  93 SLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDDGEFLKLVKPIEEIFKELgSGNPSDFIPILLPFYFLYLK-- 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 249 KANSACKLAHDHTDQVIKSRRIQLQDEEELeklkkkrrlDFLDILLFARMENGKS--LSDKDLRAEVDTFMFEGHDTTAS 326
Cdd:cd20617 171 KLKKSYDKIKDFIEKIIEEHLKTIDPNNPR---------DLIDDELLLLLKEGDSglFDDDSIISTCLDLFLAGTDTTST 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 327 GISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPK 405
Cdd:cd20617 242 TLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPlGLPRVTTEDTEI-GGYFIPK 320

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86198312 406 GIHVMLSFYGLHHNPTVWPNPEVFDPSRF-APGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPD 481
Cdd:cd20617 321 GTQIIINIYSLHRDEKYFEDPEEFNPERFlENDGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLNFKFKSS 397
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 90-477 7.04e-58

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: 197.91  E-value: 7.04e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  90 GSKVRI-----QVYDPDYMKLILGRSDPKANG-SYRFLAPWIGRGLL-MLDGQTWFQHRRMLTPAFH--YDILKPYTEIM 160
Cdd:cd11059   1 GPVVRLgpnevSVNDLDAVREIYGGGFGKTKSyWYFTLRGGGGPNLFsTLDPKEHSARRRLLSGVYSksSLLRAAMEPII 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 161 ADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAF-SHEGSVQLDRKYKSYIQAVEDLNDLVFSRVRNIFHQNDI 239
Cdd:cd11059  81 RERVLPLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFgESFGTLLLGDKDSRERELLRRLLASLAPWLRWLPRYLPL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 240 IYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEklkkkrrlDFLDILLFARMENGKSLSDKDLRAEVDTFMFE 319
Cdd:cd11059 161 ATSRLIIGIYFRAFDEIEEWALDLCARAESSLAESSDSES--------LTVLLLEKLKGLKKQGLDDLEIASEALDHIVA 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 320 GHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGD-GTSITWNDLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTF 397
Cdd:cd11059 233 GHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPfRGPPDLEDLDKLPYLNAVIRETLRLYPPIPgSLPRVVPEGGAT 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 398 PDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSH----SFLPFSGGARNCIGKQFAMNELKVAVALTL 473
Cdd:cd11059 313 IGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETARemkrAFWPFGSGSRMCIGMNLALMEMKLALAAIY 392


                ....
gi 86198312 474 LRFE 477
Cdd:cd11059 393 RNYR 396
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 89-501 3.91e-56

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: 193.44  E-value: 3.91e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  89 W-GSKVRIQVYDPDYMKLIL--GRSDPKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVR 165
Cdd:cd20639  18 WfGPTPRLTVADPELIREILltRADHFDRYEAHPLVRQLEGDGLVSLRGEKWAHHRRVITPAFHMENLKRLVPHVVKSVA 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 166 VMLDKWEQIVGQDSTLEIFRHITLMTL--DTIMKCAFsheGSVQLDRKYKSYIQavEDLNDLVFSRVRNIFHQNdiiYRV 243
Cdd:cd20639  98 DMLDKWEAMAEAGGEGEVDVAEWFQNLteDVISRTAF---GSSYEDGKAVFRLQ--AQQMLLAAEAFRKVYIPG---YRF 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 244 SSNgcKAN-SACKLahdhtDQVIKSRRIQLQDEEELEKLKKKRRLDFLDIL----LFARMENGKSLSDKDLRAEVDTFMF 318
Cdd:cd20639 170 LPT--KKNrKSWRL-----DKEIRKSLLKLIERRQTAADDEKDDEDSKDLLglmiSAKNARNGEKMTVEEIIEECKTFFF 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 319 EGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFp 398
Cdd:cd20639 243 AGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLYPPAVATIRRAKKDVKL- 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 399 DGRSLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFAPGSSR---HSHSFLPFSGGARNCIGKQFAMNELKVAVALTLL 474
Cdd:cd20639 322 GGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARaakHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQ 401

                       410       420
                ....*....|....*....|....*..
gi 86198312 475 RFELLPDPTRVPIPIPRIVLKSKNGIH 501
Cdd:cd20639 402 RFEFRLSPSYAHAPTVLMLLQPQHGAP 428
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 121-499 1.99e-55

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: 191.23  E-value: 1.99e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 121 LAPWIGRGLLMLDGQTWFQHRRMLTPAF---HYDILkpytEIMADSVRVMLdkwEQIVGQDSTLEIFRHITLMTLDTIMK 197
Cdd:cd11063  44 FKPLLGDGIFTSDGEEWKHSRALLRPQFsrdQISDL----ELFERHVQNLI---KLLPRDGSTVDLQDLFFRLTLDSATE 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 198 CAFSHegSVQLDRKYKSYIQAVEDLNDLVFS----RVRNIFHQNDIIYRVSsngcKANSACKLAHDHTDQVIkSRRIQLQ 273
Cdd:cd11063 117 FLFGE--SVDSLKPGGDSPPAARFAEAFDYAqkylAKRLRLGKLLWLLRDK----KFREACKVVHRFVDPYV-DKALARK 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 274 DEEELEKLKKKRrlDFLDILLfarmengKSLSD-KDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSL 352
Cdd:cd11063 190 EESKDEESSDRY--VFLDELA-------KETRDpKELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSL 260

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 353 LGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFP-----DGRS---LPKGIHVMLSFYGLHHNPTVW- 423
Cdd:cd11063 261 FGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLPrgggpDGKSpifVPKGTRVLYSVYAMHRRKDIWg 340

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 424 PNPEVFDPSRFAPGsSRHSHSFLPFSGGARNCIGKQFAMNElkvaVALTLLRF-----ELLPDPTRVPIPIPRIVLKSKN 498
Cdd:cd11063 341 PDAEEFRPERWEDL-KRPGWEYLPFNGGPRICLGQQFALTE----ASYVLVRLlqtfdRIESRDVRPPEERLTLTLSNAN 415


                .
gi 86198312 499 G 499
Cdd:cd11063 416 G 416
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 126-499 3.28e-55

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: 190.88  E-value: 3.28e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 126 GRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTE-IMADSVRVMLDKWEQIV-GQDSTLEIFRHITLMTLDTIMKCAFSHE 203
Cdd:cd11064  48 GDGIFNVDGELWKFQRKTASHEFSSRALREFMEsVVREKVEKLLVPLLDHAaESGKVVDLQDVLQRFTFDVICKIAFGVD 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 204 -GSVQLDRKYKSYIQAVEDLNDLVFSRvrniFHQNDIIYR------VSSnGCKANSACKLAHDHTDQVIKSRRIQLqdee 276
Cdd:cd11064 128 pGSLSPSLPEVPFAKAFDDASEAVAKR----FIVPPWLWKlkrwlnIGS-EKKLREAIRVIDDFVYEVISRRREEL---- 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 277 ELEKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDG 356
Cdd:cd11064 199 NSREEENNVREDLLSRFLASEEEEGEPVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKL 278

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 357 TSITW-----NDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVW-PNPEVFD 430
Cdd:cd11064 279 TTDESrvptyEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWgEDALEFK 358

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86198312 431 PSRF--APGSSRH--SHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPRIVLKSKNG 499
Cdd:cd11064 359 PERWldEDGGLRPesPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVEPKMSLTLHMKGG 431
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 90-502 4.03e-55

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: 190.70  E-value: 4.03e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  90 GSKVRIQVYDPDYMK-------LILGRSdpkangSY--RFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIM 160
Cdd:cd20640  20 GNKQFLYVSRPEMVKeinlcvsLDLGKP------SYlkKTLKPLFGGGILTSNGPHWAHQRKIIAPEFFLDKVKGMVDLM 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 161 ADSVRVMLDKWEQIV--GQDSTLEIF--RHITLMTLDTIMKCAFsheGSvqldrkykSYIQAVEdlndlVFSRVRN---- 232
Cdd:cd20640  94 VDSAQPLLSSWEERIdrAGGMAADIVvdEDLRAFSADVISRACF---GS--------SYSKGKE-----IFSKLRElqka 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 233 IFHQNDIIYRVSSNGCKANSACKLAHDHTD------QVIKSRRIQLQDEEEleklkkkrrldfldiLLFARMENGKSLSD 306
Cdd:cd20640 158 VSKQSVLFSIPGLRHLPTKSNRKIWELEGEirslilEIVKEREEECDHEKD---------------LLQAILEGARSSCD 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 307 KDLRAE---VD---TFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGdGTSITWNDLDKMPYTTMCIKEALRI 380
Cdd:cd20640 223 KKAEAEdfiVDnckNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCK-GGPPDADSLSRMKTVTMVIQETLRL 301

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 381 YPPVPSVSRELSSPVTFPDGRsLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFA---PGSSRHSHSFLPFSGGARNCI 456
Cdd:cd20640 302 YPPAAFVSREALRDMKLGGLV-VPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSngvAAACKPPHSYMPFGAGARTCL 380

                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*.
gi 86198312 457 GKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIHL 502
Cdd:cd20640 381 GQNFAMAELKVLVSLILSKFSFTLSPEYQHSPAFRLIVEPEFGVRL 426
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 97-478 1.88e-54

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: 188.89  E-value: 1.88e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  97 VYDPDYMKLILgRSDpkanGSY---RFLAPWI--------GRGLLMLDGQTWFQHRRMLTPafhyDILKP-----YTEIM 160
Cdd:cd11054  20 LFDPDDIEKVF-RNE----GKYpirPSLEPLEkyrkkrgkPLGLLNSNGEEWHRLRSAVQK----PLLRPksvasYLPAI 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 161 ADSVRVMLDKWEQIVGQDSTL------EIFRH----ITLMTLDTIMKCaFSHEGSVQLDRkyksYIQAVEDLNDLVF--- 227
Cdd:cd11054  91 NEVADDFVERIRRLRDEDGEEvpdledELYKWslesIGTVLFGKRLGC-LDDNPDSDAQK----LIEAVKDIFESSAklm 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 228 -----------SRVRNIFHQNDIIYRVssngckansacklAHDHTDQVIKSRRIQLQDEEELEklkkkrrlDFLDILLfa 296
Cdd:cd11054 166 fgpplwkyfptPAWKKFVKAWDTIFDI-------------ASKYVDEALEELKKKDEEDEEED--------SLLEYLL-- 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 297 rmeNGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKE 376
Cdd:cd11054 223 ---SKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKE 299

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 377 ALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSR----HSHSFLPFSGGA 452
Cdd:cd11054 300 SLRLYPVAPGNGRILPKDIVL-SGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSEnkniHPFASLPFGFGP 378

                       410       420
                ....*....|....*....|....*.
gi 86198312 453 RNCIGKQFAMNELKVAVALTLLRFEL 478
Cdd:cd11054 379 RMCIGRRFAELEMYLLLAKLLQNFKV 404
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 114-482 5.32e-53

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: 184.73  E-value: 5.32e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 114 ANGSYRFLAPWIGRGLL---MLDGQtwFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWeqivGQDSTLEIFRHITLM 190
Cdd:cd11042  40 AEEVYGFLTPPFGGGVVyyaPFAEQ--KEQLKFGLNILRRGKLRGYVPLIVEEVEKYFAKW----GESGEVDLFEEMSEL 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 191 TLDTIMKCAFSHEGSVQLDrkyKSYIQAVEDLnDLVFSRVrNIFHQNDII--YRvssngcKANSACKLAHDHTDQVIKSR 268
Cdd:cd11042 114 TILTASRCLLGKEVRELLD---DEFAQLYHDL-DGGFTPI-AFFFPPLPLpsFR------RRDRARAKLKEIFSEIIQKR 182

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 269 RiqlqdeeeleKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKE 348
Cdd:cd11042 183 R----------KSPDKDEDDMLQTLMDAKYKDGRPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREE 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 349 IQSLLGD-GTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGR-SLPKGIHVMLSFYGLHHNPTVWPNP 426
Cdd:cd11042 253 QKEVLGDgDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVEGGGyVIPKGHIVLASPAVSHRDPEIFKNP 332

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86198312 427 EVFDPSRFAPGSSRHSH----SFLPFSGGARNCIGKQFAMNELKVAVAlTLLR---FELLPDP 482
Cdd:cd11042 333 DEFDPERFLKGRAEDSKggkfAYLPFGAGRHRCIGENFAYLQIKTILS-TLLRnfdFELVDSP 394
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 95-485 5.56e-52

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: 182.53  E-value: 5.56e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  95 IQVYDPDYMKLILGRSD--PKANGSYRFLAPwIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKW- 171
Cdd:cd11070  15 ILVTKPEYLTQIFRRRDdfPKPGNQYKIPAF-YGPNVISSEGEDWKRYRKIVAPAFNERNNALVWEESIRQAQRLIRYLl 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 172 -EQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYkSYIQAVEDLNDLVFSRVRNIFHQNDIIyrvssnGCKA 250
Cdd:cd11070  94 eEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEEES-SLHDTLNAIKLAIFPPLFLNFPFLDRL------PWVL 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 251 NSACKLAHDHTDQVIKS-RRIQLQDEEELEKLKKKRRLDFLDILLFARmeNGKSLSDKDLRAEVDTFMFEGHDTTASGIS 329
Cdd:cd11070 167 FPSRKRAFKDVDEFLSElLDEVEAELSADSKGKQGTESVVASRLKRAR--RSGGLTEKELLGNLFIFFIAGHETTANTLS 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 330 WIFYALATNPEHQQRCRKEIQSLLGDgTSITWN---DLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRS---- 402
Cdd:cd11070 245 FALYLLAKHPEVQDWLREEIDSVLGD-EPDDWDyeeDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVITGLGqeiv 323

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 403 LPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFAPGSS------RHSH---SFLPFSGGARNCIGKQFAMNELKVAVALT 472
Cdd:cd11070 324 IPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSGeigaatRFTPargAFIPFSAGPRACLGRKFALVEFVAALAEL 403

                       410
                ....*....|...
gi 86198312 473 LLRFELLPDPTRV 485
Cdd:cd11070 404 FRQYEWRVDPEWE 416
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 141-506 1.45e-51

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: 180.45  E-value: 1.45e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 141 RRMLTPAFHYDILKP-YTEIMADSVRVMLDKWEQivgqDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYiqav 219
Cdd:cd11043  67 RGLLLSFLGPEALKDrLLGDIDELVRQHLDSWWR----GKSVVVLELAKKMTFELICKLLLGIDPEEVVEELRKEF---- 138

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 220 EDLNDLVFSRVRNI----FHqndiiyrvssngcKANSACKLAHDHTDQVIKSRRIQLqdeeelekLKKKRRLDFLDILLF 295
Cdd:cd11043 139 QAFLEGLLSFPLNLpgttFH-------------RALKARKRIRKELKKIIEERRAEL--------EKASPKGDLLDVLLE 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 296 ARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKE---IQSLLGDGTSITWNDLDKMPYTTM 372
Cdd:cd11043 198 EKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEheeIAKRKEEGEGLTWEDYKSMKYTWQ 277

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 373 CIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSFLPFSGGA 452
Cdd:cd11043 278 VINETLRLAPIVPGVFRKALQDVEY-KGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGVPYTFLPFGGGP 356

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 453 RNCIGKQFAmnELKVAVAL----TLLRFELLPD--PTRVPIPIPrivlksKNGIHLHLKK 506
Cdd:cd11043 357 RLCPGAELA--KLEILVFLhhlvTRFRWEVVPDekISRFPLPRP------PKGLPIRLSP 408
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 97-477 1.51e-50

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: 177.83  E-value: 1.51e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  97 VYDPDYMKLILG-RSDPKANGSYRFLAPWIGRGLLM-LDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQI 174
Cdd:cd11051  15 VTDPELAEQITQvTNLPKPPPLRKFLTPLTGGSSLIsMEGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVEIFAAILREL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 175 VGQDSTLEIFRHITLMTLDTImkcafsheGSVQLDrkyksyiqavEDLNdlvfsrvrnifhqndiiyrvssngckansaC 254
Cdd:cd11051  95 AESGEVFSLEELTTNLTFDVI--------GRVTLD----------IDLH------------------------------A 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 255 KLAhDHTDQVIKSRRIQLQDEEELEKLkkkrrlDFLDILLFARMENGKSLsDKDLRAEVD-------------TFMFEGH 321
Cdd:cd11051 127 QTG-DNSLLTALRLLLALYRSLLNPFK------RLNPLRPLRRWRNGRRL-DRYLKPEVRkrfeleraidqikTFLFAGH 198

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 322 DTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITW-------NDLDKMPYTTMCIKEALRIYPPVpSVSRElSSP 394
Cdd:cd11051 199 DTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPSAAAellregpELLNQLPYTTAVIKETLRLFPPA-GTARR-GPP 276

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 395 ---VTFPDGRSLP-KGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSH----SFLPFSGGARNCIGKQFAMNELK 466
Cdd:cd11051 277 gvgLTDRDGKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHELYppksAWRPFERGPRNCIGQELAMLELK 356

                       410
                ....*....|.
gi 86198312 467 VAVALTLLRFE 477
Cdd:cd11051 357 IILAMTVRRFD 367
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 90-482 3.25e-50

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: 177.45  E-value: 3.25e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  90 GSKVRIQVYDPDYMKLILGR----SDPKANGSYRFLapwIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVR 165
Cdd:cd20621  11 GSKPLISLVDPEYIKEFLQNhhyyKKKFGPLGIDRL---FGKGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINEITK 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 166 VMLDKWEQIVGQdstleIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNDLVFSRVRN--------IFHQN 237
Cdd:cd20621  88 EKIKKLDNQNVN-----IIQFLQKITGEVVIRSFFGEEAKDLKINGKEIQVELVEILIESFLYRFSSpyfqlkrlIFGRK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 238 DIIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKrrldFLDILLFARMENGKSLSDKDLRAEVDTFM 317
Cdd:cd20621 163 SWKLFPTKKEKKLQKRVKELRQFIEKIIQNRIKQIKKNKDEIKDIII----DLDLYLLQKKKLEQEITKEEIIQQFITFF 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 318 FEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSV-SRELSSPVT 396
Cdd:cd20621 239 FAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLfPRVATQDHQ 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 397 FPDgRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLL 474
Cdd:cd20621 319 IGD-LKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWlnQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILK 397


                ....*...
gi 86198312 475 RFELLPDP 482
Cdd:cd20621 398 NFEIEIIP 405
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 70-502 6.40e-50

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: 176.70  E-value: 6.40e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  70 LQDILTRIKNFpsacpqWLW-GSKVRIQVYDPDYMKLILGRSD----PKANGSYRFLApwigRGLLMLDGQTWFQHRRML 144
Cdd:cd20642   5 HHTVKTYGKNS------FTWfGPIPRVIIMDPELIKEVLNKVYdfqkPKTNPLTKLLA----TGLASYEGDKWAKHRKII 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 145 TPAFHYDILKPYTEIMADSVRVMLDKWEQIVGQDSTLE--IFRHITLMTLDTIMKCAF--SHE------------GSVQL 208
Cdd:cd20642  75 NPAFHLEKLKNMLPAFYLSCSEMISKWEKLVSSKGSCEldVWPELQNLTSDVISRTAFgsSYEegkkifelqkeqGELII 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 209 DRKYKSYIQA-----------VEDLNDLVFSRVRNIfhqndIIYRVssngcKANSACKLAHDhtdqviksrriqlqdeee 277
Cdd:cd20642 155 QALRKVYIPGwrflptkrnrrMKEIEKEIRSSLRGI-----INKRE-----KAMKAGEATND------------------ 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 278 leklkkkrrlDFLDILLFARMENGKS-------LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQ 350
Cdd:cd20642 207 ----------DLLGILLESNHKEIKEqgnknggMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVL 276

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 351 SLLGDGTSiTWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDgRSLPKGIHVMLSFYGLHHNPTVWPN-PEVF 429
Cdd:cd20642 277 QVFGNNKP-DFEGLNHLKVVTMILYEVLRLYPPVIQLTRAIHKDTKLGD-LTLPAGVQVSLPILLVHRDPELWGDdAKEF 354

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86198312 430 DPSRFAPGSSRHSH---SFLPFSGGARNCIGKQFAMNELKVAVALTLLRF--ELLPDPTRVPIPIprIVLKSKNGIHL 502
Cdd:cd20642 355 NPERFAEGISKATKgqvSYFPFGWGPRICIGQNFALLEAKMALALILQRFsfELSPSYVHAPYTV--LTLQPQFGAHL 430
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 90-500 4.80e-48

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: 171.86  E-value: 4.80e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  90 GSKVRIQVYDPDYMKLIL-------GRSDPKANgsyrfLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMAD 162
Cdd:cd20641  20 GTTPRICISDHELAKQVLsdkfgffGKSKARPE-----ILKLSGKGLVFVNGDDWVRHRRVLNPAFSMDKLKSMTQVMAD 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 163 SVRVMLDKWEQIVGQDSTLEIF----RHITLMTLDTIMKCAFsheGSvqldrkykSYIQAVE------DLNDLVFSRVRN 232
Cdd:cd20641  95 CTERMFQEWRKQRNNSETERIEvevsREFQDLTADIIATTAF---GS--------SYAEGIEvflsqlELQKCAAASLTN 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 233 IFHQNDIIYRVSSNGCKANSACKLahDHTDQVIKSRRIQlqdeeeleKLKKKRRLDFLDILLFARMENG------KSLSD 306
Cdd:cd20641 164 LYIPGTQYLPTPRNLRVWKLEKKV--RNSIKRIIDSRLT--------SEGKGYGDDLLGLMLEAASSNEggrrteRKMSI 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 307 KDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGdGTSITWND-LDKMPYTTMCIKEALRIYPPVP 385
Cdd:cd20641 234 DEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECG-KDKIPDADtLSKLKLMNMVLMETLRLYGPVI 312

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 386 SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFAPGSSR---HSHSFLPFSGGARNCIGKQFA 461
Cdd:cd20641 313 NIARRASEDMKL-GGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRaatHPNALLSFSLGPRACIGQNFA 391

                       410       420       430
                ....*....|....*....|....*....|....*....
gi 86198312 462 MNELKVAVALTLLRFELLPDPTRVPIPIPRIVLKSKNGI 500
Cdd:cd20641 392 MIEAKTVLAMILQRFSFSLSPEYVHAPADHLTLQPQYGL 430
PLN02290 PLN02290
cytokinin trans-hydroxylase
 90-507 2.34e-47

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 171.92  E-value: 2.34e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   90 GSKVRIQVYDPDYMKLIL-------GRSDPKANGSYRFlapwIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMAD 162
Cdd:PLN02290 102 GTEPRLCLTETELIKELLtkyntvtGKSWLQQQGTKHF----IGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  163 SVRVMLDKWEQIVGQDST-LEIFRHITLMTLDTIMKCAF--SHEgsvqldrKYKSYIQAVEDLNDLVFSRVRNIFHQNDI 239
Cdd:PLN02290 178 CTKQMLQSLQKAVESGQTeVEIGEYMTRLTADIISRTEFdsSYE-------KGKQIFHLLTVLQRLCAQATRHLCFPGSR 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  240 IYRvssngCKANSACKLAHDHTDQVIKsRRIQLQDEEELEKLKKKRRLDFLDILLfARME----NGKSLSDKDLRAEVDT 315
Cdd:PLN02290 251 FFP-----SKYNREIKSLKGEVERLLM-EIIQSRRDCVEIGRSSSYGDDLLGMLL-NEMEkkrsNGFNLNLQLIMDECKT 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  316 FMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSiTWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPV 395
Cdd:PLN02290 324 FFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETP-SVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDI 402

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  396 TFPDGRsLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFA---PGSSRHshsFLPFSGGARNCIGKQFAMNELKVAVAL 471
Cdd:PLN02290 403 KLGDLH-IPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAgrpFAPGRH---FIPFAAGPRNCIGQAFAMMEAKIILAM 478

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 86198312  472 TLLRFELLPDPTRVPIPIPRIVLKSKNGIHLHLKKL 507
Cdd:PLN02290 479 LISKFSFTISDNYRHAPVVVLTIKPKYGVQVCLKPL 514
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 90-484 4.45e-45

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: 163.52  E-value: 4.45e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  90 GSKVRI---QVY--DPDYMKLILGRSDPKA-NGSYRFLAPWIGR--GLL-MLDGQTWFQHRRMLTPAFHYDILKPYtEIM 160
Cdd:cd11060   1 GPVVRIgpnEVSisDPEAIKTIYGTRSPYTkSDWYKAFRPKDPRkdNLFsERDEKRHAALRRKVASGYSMSSLLSL-EPF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 161 ADS-VRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHE-GSVQLDRKYKSYIQAVEDLND-----LVFSRVRNI 233
Cdd:cd11060  80 VDEcIDLLVDLLDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPfGFLEAGTDVDGYIASIDKLLPyfavvGQIPWLDRL 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 234 FHQNDI-IYRVSSNGckansackLAH--DHTDQVIKSRRIQLQDEEELEKlkkkrrlDFLDILLFARMENGKSLSDKDLR 310
Cdd:cd11060 160 LLKNPLgPKRKDKTG--------FGPlmRFALEAVAERLAEDAESAKGRK-------DMLDSFLEAGLKDPEKVTDREVV 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 311 AEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDG---TSITWNDLDKMPYTTMCIKEALRIYPPVPSv 387
Cdd:cd11060 225 AEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGklsSPITFAEAQKLPYLQAVIKEALRLHPPVGL- 303

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 388 SRELSSP---VTFPdGRSLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRF--APGSSR--HSHSFLPFSGGARNCIGKQ 459
Cdd:cd11060 304 PLERVVPpggATIC-GRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWleADEEQRrmMDRADLTFGAGSRTCLGKN 382

                       410       420
                ....*....|....*....|....*..
gi 86198312 460 FAMNEL-KVAVALtLLRFEL-LPDPTR 484
Cdd:cd11060 383 IALLELyKVIPEL-LRRFDFeLVDPEK 408
PLN02936 PLN02936
epsilon-ring hydroxylase
 97-481 2.21e-44

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 163.04  E-value: 2.21e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   97 VYDPDYMKLILGRSDPK-ANGSYRFLAPWI-GRGLLMLDGQTWFQHRRMLTPAFHydilKPYTEIMADSV-----RVMLD 169
Cdd:PLN02936  65 VSDPAIAKHVLRNYGSKyAKGLVAEVSEFLfGSGFAIAEGELWTARRRAVVPSLH----RRYLSVMVDRVfckcaERLVE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  170 KWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHE-GSVQLDrkyKSYIQAVEDLNDLVFSRVRNI--FHQNDIIYRVSSN 246
Cdd:PLN02936 141 KLEPVALSGEAVNMEAKFSQLTLDVIGLSVFNYNfDSLTTD---SPVIQAVYTALKEAETRSTDLlpYWKVDFLCKISPR 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  247 GCKANSACKLAHDHTDQVI-KSRRIQLQDEEELEKLKKKRRLD--FLDILLFARMEngksLSDKDLRAEVDTFMFEGHDT 323
Cdd:PLN02936 218 QIKAEKAVTVIRETVEDLVdKCKEIVEAEGEVIEGEEYVNDSDpsVLRFLLASREE----VSSVQLRDDLLSMLVAGHET 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  324 TASGISWIFYALATNPEHQQRCRKEIQSLLGdGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSL 403
Cdd:PLN02936 294 TGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKV 372

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  404 PKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF-----APGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLR--F 476
Cdd:PLN02936 373 NAGQDIMISVYNIHRSPEVWERAEEFVPERFdldgpVPNETNTDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRldL 452


                 ....*
gi 86198312  477 ELLPD 481
Cdd:PLN02936 453 ELVPD 457
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 90-478 3.04e-44

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: 161.24  E-value: 3.04e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  90 GSKVRIQ-----VYDPDYMKLILGRSDP--KANgSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMAD 162
Cdd:cd11061   1 GDVVRIGpnelsINDPDALKDIYGHGSNclKGP-FYDALSPSASLTFTTRDKAEHARRRRVWSHAFSDKALRGYEPRILS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 163 SVRVMLDKWEQIVGQDS--TLEIFRHITLMTLDTIMKCAFSHegSVQ-LDRKYKSYIQAVeDLNDLVFSrvrNIFHQNDI 239
Cdd:cd11061  80 HVEQLCEQLDDRAGKPVswPVDMSDWFNYLSFDVMGDLAFGK--SFGmLESGKDRYILDL-LEKSMVRL---GVLGHAPW 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 240 IYRVSSNGC---KANSACKLAHDHTDQVIKsRRIQLQDEEELeklkkkrrlDFLDILLFARM-ENGKSLSDKDLRAEVDT 315
Cdd:cd11061 154 LRPLLLDLPlfpGATKARKRFLDFVRAQLK-ERLKAEEEKRP---------DIFSYLLEAKDpETGEGLDLEELVGEARL 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 316 FMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSI-TWNDLDKMPYTTMCIKEALRIYPPVPSV-SRE-LS 392
Cdd:cd11061 224 LIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIrLGPKLKSLPYLRACIDEALRLSPPVPSGlPREtPP 303

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 393 SPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSH---SFLPFSGGARNCIGKQFAMNELKVAV 469
Cdd:cd11061 304 GGLTI-DGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVRarsAFIPFSIGPRGCIGKNLAYMELRLVL 382


                ....*....
gi 86198312 470 ALTLLRFEL 478
Cdd:cd11061 383 ARLLHRYDF 391
PLN02738 PLN02738
carotene beta-ring hydroxylase
 89-487 9.49e-44

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 163.93  E-value: 9.49e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   89 WGSKVRIQVYDPDYMKLILgRSDPKANgSYRFLAPWI----GRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSV 164
Cdd:PLN02738 172 FGPKSFLIVSDPSIAKHIL-RDNSKAY-SKGILAEILefvmGKGLIPADGEIWRVRRRAIVPALHQKYVAAMISLFGQAS 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  165 RVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHE-GSVQLDrkyKSYIQAVEDLNDLVFSRVRNIFHQNDI-IYR 242
Cdd:PLN02738 250 DRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNYDfDSLSND---TGIVEAVYTVLREAEDRSVSPIPVWEIpIWK 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  243 -VSSNGCKANSACKLAHDHTDQVIK--SRRIQLQDEEELEKLKKKRRLDFLDILLFArmenGKSLSDKDLRAEVDTFMFE 319
Cdd:PLN02738 327 dISPRQRKVAEALKLINDTLDDLIAicKRMVEEEELQFHEEYMNERDPSILHFLLAS----GDDVSSKQLRDDLMTMLIA 402

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  320 GHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSiTWNDLDKMPYTTMCIKEALRIYPPVPS-VSRELSSPV--T 396
Cdd:PLN02738 403 GHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFP-TIEDMKKLKYTTRVINESLRLYPQPPVlIRRSLENDMlgG 481

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  397 FPDGRslpkGIHVMLSFYGLHHNPTVWPNPEVFDPSRFA-----PGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVAL 471
Cdd:PLN02738 482 YPIKR----GEDIFISVWNLHRSPKHWDDAEKFNPERWPldgpnPNETNQNFSYLPFGGGPRKCVGDMFASFENVVATAM 557

                        410
                 ....*....|....*.
gi 86198312  472 TLLRFELLPDPTRVPI 487
Cdd:PLN02738 558 LVRRFDFQLAPGAPPV 573
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 288-495 4.20e-41

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: 152.57  E-value: 4.20e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMENG----KSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWND 363
Cdd:cd20650 204 DFLQLMIDSQNSKEteshKALSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDT 283

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 364 LDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAP--GSSRH 441
Cdd:cd20650 284 VMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEI-NGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKknKDNID 362

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86198312 442 SHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLP-DPTRVPI---------PIPRIVLK 495
Cdd:cd20650 363 PYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPcKETQIPLklslqgllqPEKPIVLK 426
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 126-497 6.87e-41

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: 151.98  E-value: 6.87e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 126 GRGLLMLD-GQTWFQHRRMLTPAFHY--DILKPYTEIMADSVRVMLDKWEQIVGQdsTLEIFRHITLMTLDTIMKCAFSH 202
Cdd:cd11027  50 GKDIAFGDySPTWKLHRKLAHSALRLyaSGGPRLEEKIAEEAEKLLKRLASQEGQ--PFDPKDELFLAVLNVICSITFGK 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 203 EGSVqLDRKYKSYIQAVEDLNDLvfsrvrniFHQNDIIYRVSSNG---CKANSACKLAHDHTDQVIKSRRIQLQDEEELE 279
Cdd:cd11027 128 RYKL-DDPEFLRLLDLNDKFFEL--------LGAGSLLDIFPFLKyfpNKALRELKELMKERDEILRKKLEEHKETFDPG 198

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 280 KLKkkrrlDFLDILLFARMENGK-------SLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSL 352
Cdd:cd11027 199 NIR-----DLTDALIKAKKEAEDegdedsgLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDV 273

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 353 LGDGTSITWNDLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDP 431
Cdd:cd11027 274 IGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPlALPHKTTCDTTL-RGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRP 352

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86198312 432 SRF--APGSSR-HSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPI---PIPRIVLKSK 497
Cdd:cd11027 353 ERFldENGKLVpKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEPPPeleGIPGLVLYPL 424
PTZ00404 PTZ00404
cytochrome P450; Provisional
 97-478 2.26e-39

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 149.10  E-value: 2.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312   97 VYDPDYMKLILgrSDPKANGSYRFLAPWI-----GRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKW 171
Cdd:PTZ00404  77 LSDPILIREMF--VDNFDNFSDRPKIPSIkhgtfYHGIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQVDVLIESM 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  172 EQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLD---RKYKSYIQAVEDL-NDL-------VFSRVRNIFHQndii 240
Cdd:PTZ00404 155 KKIESSGETFEPRYYLTKFTMSAMFKYIFNEDISFDEDihnGKLAELMGPMEQVfKDLgsgslfdVIEITQPLYYQ---- 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  241 YRVSSNGCkANSACKLAHDHTDQVIKSRRIQLQdeeeleklkkkrrLDFLDILLfarMENGKSLSDKDLR--AEVDTFMF 318
Cdd:PTZ00404 231 YLEHTDKN-FKKIKKFIKEKYHEHLKTIDPEVP-------------RDLLDLLI---KEYGTNTDDDILSilATILDFFL 293

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  319 EGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTF 397
Cdd:PTZ00404 294 AGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPfGLPRSTSNDIII 373

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  398 PDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSrhSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFE 477
Cdd:PTZ00404 374 GGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDS--NDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFK 451


                 .
gi 86198312  478 L 478
Cdd:PTZ00404 452 L 452
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 140-485 3.36e-38

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: 144.65  E-value: 3.36e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 140 HRRMLTPAF-------HYDILKPYteimadsVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHE-GSVQlDRK 211
Cdd:cd11058  61 LRRLLAHAFsekalreQEPIIQRY-------VDLLVSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFGESfGCLE-NGE 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 212 YKSYIQAVEDLndLVFSRVRNIFHQNDIIYRVSSNGCKANSACKLAhDHTDQVIK--SRRIQLQDEEEleklkkkrrlDF 289
Cdd:cd11058 133 YHPWVALIFDS--IKALTIIQALRRYPWLLRLLRLLIPKSLRKKRK-EHFQYTREkvDRRLAKGTDRP----------DF 199

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 290 LDILLfARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPY 369
Cdd:cd11058 200 MSYIL-RNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQLPY 278

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 370 TTMCIKEALRIYPPVPS-VSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHS---- 444
Cdd:cd11058 279 LNAVIQEALRLYPPVPAgLPRVVPAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFDNdkke 358

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 86198312 445 -FLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRV 485
Cdd:cd11058 359 aFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPESE 400
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 294-490 1.22e-37

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: 143.10  E-value: 1.22e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 294 LFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMC 373
Cdd:cd11065 209 LLEELDKEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAI 288

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 374 IKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF----APGSSRHSHSFLPF 448
Cdd:cd11065 289 VKEVLRWRPVAPlGIPHALTEDDEY-EGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYlddpKGTPDPPDPPHFAF 367

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 86198312 449 SGGARNCIGKQFAMNELKVAVALTLLRFELLP--DPTRVPIPIP 490
Cdd:cd11065 368 GFGRRICPGRHLAENSLFIAIARLLWAFDIKKpkDEGGKEIPDE 411
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 304-483 2.36e-35

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: 136.61  E-value: 2.36e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 304 LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSI-TWNDLDKMPYTTMCIKEALRIYP 382
Cdd:cd11062 220 KTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDPDSPpSLAELEKLPYLTAVIKEGLRLSY 299

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 383 PVPS----VSRElsSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSRHSHSFLPFSGGARNCI 456
Cdd:cd11062 300 GVPTrlprVVPD--EGLYY-KGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWlgAAEKGKLDRYLVPFSKGSRSCL 376

                       170       180
                ....*....|....*....|....*..
gi 86198312 457 GKQFAMNELKVAVALTLLRFELLPDPT 483
Cdd:cd11062 377 GINLAYAELYLALAALFRRFDLELYET 403
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 265-482 3.74e-35

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: 136.22  E-value: 3.74e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 265 IKSRRIQLQDEEELEKLKKKRRLDFLDILLfarMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQR 344
Cdd:cd11075 191 IRARRKRRASGEADKDYTDFLLLDLLDLKE---EGGERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEK 267

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 345 CRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVW 423
Cdd:cd11075 268 LYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHfLLPHAVTEDTVL-GGYDIPAGAEVNFNVAAIGRDPKVW 346

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86198312 424 PNPEVFDPSRFAPG--------SSRhSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDP 482
Cdd:cd11075 347 EDPEEFKPERFLAGgeaadidtGSK-EIKMMPFGAGRRICPGLGLATLHLELFVARLVQEFEWKLVE 412
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 99-487 5.04e-33

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: 130.13  E-value: 5.04e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  99 DPDYMKLILgRSDPKangSYRFLAPWI-------GRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKW 171
Cdd:cd11083  18 DPELIREVL-RRRPD---EFRRISSLEsvfremgINGVFSAEGDAWRRQRRLVMPAFSPKHLRYFFPTLRQITERLRERW 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 172 EQIVGQDSTLEIFRHITLMTLDTIMKCAFShegsvqldrkyksyiqavEDLNDLvfSRVRNIFHQN-DIIYRVSSNGCKA 250
Cdd:cd11083  94 ERAAAEGEAVDVHKDLMRYTVDVTTSLAFG------------------YDLNTL--ERGGDPLQEHlERVFPMLNRRVNA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 251 ----------------NSACKLAHDHTDQVIKSRRIQLQDEEELEKLKKKrrldfLDILLFARMENGKSLSDKDLRAEVD 314
Cdd:cd11083 154 pfpywrylrlpadralDRALVEVRALVLDIIAAARARLAANPALAEAPET-----LLAMMLAEDDPDARLTDDEIYANVL 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 315 TFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDG-TSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSS 393
Cdd:cd11083 229 TLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGArVPPLLEALDRLPYLEAVARETLRLKPVAPLLFLEPNE 308

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 394 PVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSR----HSHSFLPFSGGARNCIGKQFAMNELKVAV 469
Cdd:cd11083 309 DTVV-GDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAaephDPSSLLPFGAGPRLCPGRSLALMEMKLVF 387

                       410
                ....*....|....*....
gi 86198312 470 ALTLLRFEL-LPDPTRVPI 487
Cdd:cd11083 388 AMLCRNFDIeLPEPAPAVG 406
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 300-502 1.20e-32

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: 129.39  E-value: 1.20e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 300 NGKsLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALR 379
Cdd:cd20646 226 SGK-LSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLR 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 380 IYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSRHSHSFLPFSGGARNCIG 457
Cdd:cd20646 305 LYPVVPGNARVIVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWlrDGGLKHHPFGSIPFGYGVRACVG 384

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 86198312 458 KQFAMNELKVAVALTLLRFELLPDPTRVPI-PIPRIVLKSKNGIHL 502
Cdd:cd20646 385 RRIAELEMYLALSRLIKRFEVRPDPSGGEVkAITRTLLVPNKPINL 430
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 288-492 1.55e-32

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: 128.87  E-value: 1.55e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLfARMENGK----SLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWND 363
Cdd:cd20651 202 DLIDAYL-REMKKKEppssSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDD 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 364 LDKMPYTTMCIKEALRIYPPVPS-VSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSR 440
Cdd:cd20651 281 RSKLPYTEAVILEVLRIFTLVPIgIPHRALKDTTL-GGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFldEDGKLL 359

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 86198312 441 HSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIPIPRI 492
Cdd:cd20651 360 KDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQNFTFSPPNGSLPDLEGIP 411
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 302-501 3.12e-32

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: 128.42  E-value: 3.12e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 302 KSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIY 381
Cdd:cd20649 255 RMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMY 334

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 382 PPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGS--SRHSHSFLPFSGGARNCIGKQ 459
Cdd:cd20649 335 PPAFRFAREAAEDCVV-LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAkqRRHPFVYLPFGAGPRSCIGMR 413

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 86198312 460 FAMNELKVAVALTLLRFELLPDP-TRVPIPI-PRIVLKSKNGIH 501
Cdd:cd20649 414 LALLEIKVTLLHILRRFRFQACPeTEIPLQLkSKSTLGPKNGVY 457
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 320-486 7.69e-32

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: 127.14  E-value: 7.69e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 320 GHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVP-----SVSRElssp 394
Cdd:cd20652 246 GVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPlgiphGCTED---- 321

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 395 vTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALT 472
Cdd:cd20652 322 -AVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFldTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARI 400

                       170
                ....*....|....*
gi 86198312 473 LLRFEL-LPDPTRVP 486
Cdd:cd20652 401 LRKFRIaLPDGQPVD 415
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 318-478 8.08e-31

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: 124.33  E-value: 8.08e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 318 FEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVT 396
Cdd:cd11041 237 FAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLvSLRRKVLKDVT 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 397 FPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRH-----------SHSFLPFSGGARNCIGKQFAMNEL 465
Cdd:cd11041 317 LSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPgqekkhqfvstSPDFLGFGHGRHACPGRFFASNEI 396

                       170
                ....*....|...
gi 86198312 466 KVAVALTLLRFEL 478
Cdd:cd11041 397 KLILAHLLLNYDF 409
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 288-486 1.96e-30

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: 122.81  E-value: 1.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARM----------ENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGT 357
Cdd:cd20673 202 DLLDALLQAKMnaennnagpdQDSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSR 281

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 358 SITWNDLDKMPYTTMCIKEALRIYP--P--VPSVSRELSSPVTFpdgrSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSR 433
Cdd:cd20673 282 TPTLSDRNHLPLLEATIREVLRIRPvaPllIPHVALQDSSIGEF----TIPKGTRVVINLWALHHDEKEWDQPDQFMPER 357

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 86198312 434 F--APGSSRH--SHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFEL-LPDPTRVP 486
Cdd:cd20673 358 FldPTGSQLIspSLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLeVPDGGQLP 415
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 159-485 2.75e-30

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: 122.57  E-value: 2.75e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 159 IMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFsheGSVQLDRKYKSYIQAVEDLNDLV--F--------- 227
Cdd:cd11072  86 IREEEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAF---GRKYEGKDQDKFKELVKEALELLggFsvgdyfpsl 162

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 228 ----------SRVRNIFHQNDIIYrvssngckansacklahdhtDQVIKSRRIQLQDEEELeklkkkrrlDFLDILLFAR 297
Cdd:cd11072 163 gwidlltgldRKLEKVFKELDAFL--------------------EKIIDEHLDKKRSKDED---------DDDDDLLDLR 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 298 MENGKSLSDK----DLRAEV-DtfMFE-GHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTT 371
Cdd:cd11072 214 LQKEGDLEFPltrdNIKAIIlD--MFLaGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLK 291

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 372 MCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFApGSS---RHSH-SFL 446
Cdd:cd11072 292 AVIKETLRLHPPAPlLLPRECREDCKI-NGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFL-DSSidfKGQDfELI 369

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 86198312 447 PFSGGARNCIGKQFAMNELKVAVALTLLRFEL-LPDPTRV 485
Cdd:cd11072 370 PFGAGRRICPGITFGLANVELALANLLYHFDWkLPDGMKP 409
PLN02655 PLN02655
ent-kaurene oxidase
 289-477 4.23e-30

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 122.54  E-value: 4.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  289 FLDILLfarmENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTsITWNDLDKMP 368
Cdd:PLN02655 247 YLDFLL----SEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDER-VTEEDLPNLP 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  369 YTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHS--HSFL 446
Cdd:PLN02655 322 YLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESAdmYKTM 401

                        170       180       190
                 ....*....|....*....|....*....|.
gi 86198312  447 PFSGGARNCIGKQFAMNELKVAVALTLLRFE 477
Cdd:PLN02655 402 AFGAGKRVCAGSLQAMLIACMAIARLVQEFE 432
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 139-467 6.31e-30

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: 121.46  E-value: 6.31e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 139 QHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWeqiVGQDSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQA 218
Cdd:cd20638  81 HRKKVIMRAFSREALENYVPVIQEEVRSSVNQW---LQSGPCVLVYPEVKRLMFRIAMRILLGFEPQQTDREQEQQLVEA 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 219 VEDLndlvfsrVRNIFHQN-DIIYRVSSNGCKANSackLAHDHTDQVIKSRRIQLQDEEELEklkkkrrlDFLDILLFAR 297
Cdd:cd20638 158 FEEM-------IRNLFSLPiDVPFSGLYRGLRARN---LIHAKIEENIRAKIQREDTEQQCK--------DALQLLIEHS 219

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 298 MENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQS--LLG----DGTSITWNDLDKMPYTT 371
Cdd:cd20638 220 RRNGEPLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEkgLLStkpnENKELSMEVLEQLKYTG 299

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 372 MCIKEALRIYPPVPSVSRelSSPVTFP-DGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSH--SFLPF 448
Cdd:cd20638 300 CVIKETLRLSPPVPGGFR--VALKTFElNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSrfSFIPF 377

                       330
                ....*....|....*....
gi 86198312 449 SGGARNCIGKQFAMNELKV 467
Cdd:cd20638 378 GGGSRSCVGKEFAKVLLKI 396
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 288-483 1.49e-29

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: 120.35  E-value: 1.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMENGKS-LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDK 366
Cdd:cd20618 208 DDDDDLLLLLDLDGEGkLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPK 287

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 367 MPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS---RHS 442
Cdd:cd20618 288 LPYLQAVVKETLRLHPPGPlLLPHESTEDCKV-AGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIddvKGQ 366

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 86198312 443 H-SFLPFSGGARNCIGKQFAMNELKVAVAlTLL-RFEL-LPDPT 483
Cdd:cd20618 367 DfELLPFGSGRRMCPGMPLGLRMVQLTLA-NLLhGFDWsLPGPK 409
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 305-488 1.71e-29

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: 120.04  E-value: 1.71e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 305 SDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDG-TSITWNDLDKMPYTTMCIKEALRIYPP 383
Cdd:cd11082 217 SDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDePPLTLDLLEEMKYTRQVVKEVLRYRPP 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 384 VPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPtvWPNPEVFDPSRFAPG---SSRHSHSFLPFSGGARNCIGKQF 460
Cdd:cd11082 297 APMVPHIAKKDFPLTEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPErqeDRKYKKNFLVFGAGPHQCVGQEY 374

                       170       180
                ....*....|....*....|....*...
gi 86198312 461 AMNELKVAVALtllrFELLPDPTRVPIP 488
Cdd:cd11082 375 AINHLMLFLAL----FSTLVDWKRHRTP 398
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 311-483 2.63e-29

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: 119.83  E-value: 2.63e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 311 AEVDTFMfEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRE 390
Cdd:cd20674 230 AVVDLFI-GGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPH 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 391 LSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFA-PGSSrhSHSFLPFSGGARNCIGKQFAMNELKVAV 469
Cdd:cd20674 309 RTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLePGAA--NRALLPFGCGARVCLGEPLARLELFVFL 386

                       170
                ....*....|....
gi 86198312 470 ALTLLRFELLPDPT 483
Cdd:cd20674 387 ARLLQAFTLLPPSD 400
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 126-471 1.39e-28

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: 117.60  E-value: 1.39e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 126 GRGLLMLDGQTWFQHRRmltpAFHYDILKP---------YTEIMADsvrvMLDKWEQIVGQDSTLE-IFRHITLMTLDTI 195
Cdd:cd20645  55 AYGLLILEGQEWQRVRS----AFQKKLMKPkevmkldgkINEVLAD----FMGRIDELCDETGRVEdLYSELNKWSFETI 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 196 mkCAfshegsVQLDRKYKSYIQAVEDLNDLVFSRVRNIFHQNDIIYrVSSNGCKANSACKLAHDHT---DQVIKS----- 267
Cdd:cd20645 127 --CL------VLYDKRFGLLQQNVEEEALNFIKAIKTMMSTFGKMM-VTPVELHKRLNTKVWQDHTeawDNIFKTakhci 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 268 -RRIQLQDEEELEklkkkrrlDFL-DILlfarmeNGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRC 345
Cdd:cd20645 198 dKRLQRYSQGPAN--------DFLcDIY------HDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKL 263

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 346 RKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDgRSLPKGIHVMLSFYGLHHNPTVWPN 425
Cdd:cd20645 264 LQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGD-YLLPKGTVLMINSQALGSSEEYFED 342

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 86198312 426 PEVFDPSRF-APGSSRHSHSFLPFSGGARNCIGKQFAmnELKVAVAL 471
Cdd:cd20645 343 GRQFKPERWlQEKHSINPFAHVPFGIGKRMCIGRRLA--ELQLQLAL 387
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 304-498 1.61e-28

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: 117.40  E-value: 1.61e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 304 LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIypp 383
Cdd:cd11028 227 LTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRH--- 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 384 vpsvsrelSS--PVTFP---------DGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGS----SRHSHSFLPF 448
Cdd:cd11028 304 --------SSfvPFTIPhattrdttlNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNglldKTKVDKFLPF 375

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 86198312 449 SGGARNCIGKQFAMNE--LKVAVALTLLRFELLPDPTRVPIPIPRIVLKSKN 498
Cdd:cd11028 376 GAGRRRCLGEELARMElfLFFATLLQQCEFSVKPGEKLDLTPIYGLTMKPKP 427
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 293-467 2.04e-28

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 117.73  E-value: 2.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  293 LLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGD---GTSITWNDLDKMPY 369
Cdd:PLN02196 249 LLGSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDkeeGESLTWEDTKKMPL 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  370 TTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APgssrHSHSFLP 447
Cdd:PLN02196 329 TSRVIQETLRVASILSFTFREAVEDVEY-EGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFevAP----KPNTFMP 403

                        170       180
                 ....*....|....*....|
gi 86198312  448 FSGGARNCIGKQFAMNELKV 467
Cdd:PLN02196 404 FGNGTHSCPGNELAKLEISV 423
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 288-483 2.07e-28

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: 117.04  E-value: 2.07e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLfaRMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKM 367
Cdd:cd11076 206 DDVDVLL--SLQGEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKL 283

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 368 PYTTMCIKEALRIYPPVP--SVSReLSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSF 445
Cdd:cd11076 284 PYLQAVVKETLRLHPPGPllSWAR-LAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGADVSV 362

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 86198312 446 L-------PFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPT 483
Cdd:cd11076 363 LgsdlrlaPFGAGRRVCPGKALGLATVHLWVAQLLHEFEWLPDDA 407
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 304-502 1.46e-27

cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; Cytochrome p450 27B1 (CYP27B1) is also called calcidiol 1-monooxygenase (EC 1.14.15.18), 25-hydroxyvitamin D(3) 1-alpha-hydroxylase (VD3 1A hydroxylase), 25-hydroxyvitamin D-1 alpha hydroxylase, 25-OHD-1 alpha-hydroxylase, 25-hydroxycholecalciferol 1-hydroxylase, or 25-hydroxycholecalciferol 1-monooxygenase. It catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3 or calcitriol), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). It is also active with 25-hydroxy-24-oxo-vitamin D3, and has an important role in normal bone growth, calcium metabolism, and tissue differentiation. CYP27B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 114.85  E-value: 1.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 304 LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPP 383
Cdd:cd20648 230 LPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPV 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 384 VPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF-APGSSRHSHSFLPFSGGARNCIGKQFAM 462
Cdd:cd20648 310 IPGNARVIPDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWlGKGDTHHPYASLPFGFGKRSCIGRRIAE 389

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 86198312 463 NELKVAVALTLLRFELLPDPTRVPI-PIPRIVLKSKNGIHL 502
Cdd:cd20648 390 LEVYLALARILTHFEVRPEPGGSPVkPMTRTLLVPERSINL 430
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 288-465 1.48e-27

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: 114.58  E-value: 1.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLfARMENGK-----SLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWN 362
Cdd:cd11026 202 DFIDCFL-LKMEKEKdnpnsEFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLE 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 363 DLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSS 439
Cdd:cd11026 281 DRAKMPYTDAVIHEVQRFGDIVPlGVPHAVTRDTKF-RGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFldEQGKF 359

                       170       180
                ....*....|....*....|....*.
gi 86198312 440 RHSHSFLPFSGGARNCIGKQFAMNEL 465
Cdd:cd11026 360 KKNEAFMPFSAGKRVCLGEGLARMEL 385
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 112-480 3.64e-27

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 114.49  E-value: 3.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  112 PKANGSYRFLAPWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMadsVRVMLDKWEQIVGQDSTLEifRHITL-- 189
Cdd:PLN03195  98 PKGEVYHSYMEVLLGDGIFNVDGELWRKQRKTASFEFASKNLRDFSTVV---FREYSLKLSSILSQASFAN--QVVDMqd 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  190 ----MTLDTIMKCAFSHE-GSVQLDRKYKSYIQAVEDLNDLVFSRVRNIFHQNDIIYRVSSNGCKANSAcKLAHDHTDQV 264
Cdd:PLN03195 173 lfmrMTLDSICKVGFGVEiGTLSPSLPENPFAQAFDTANIIVTLRFIDPLWKLKKFLNIGSEALLSKSI-KVVDDFTYSV 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  265 IKSRRIQLQDEEELEKLKKKrrldflDIL-LFARM-ENGKS-LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEH 341
Cdd:PLN03195 252 IRRRKAEMDEARKSGKKVKH------DILsRFIELgEDPDSnFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHV 325

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  342 QQRCRKEIQSL--------------------LGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGR 401
Cdd:PLN03195 326 AEKLYSELKALekerakeedpedsqsfnqrvTQFAGLLTYDSLGKLQYLHAVITETLRLYPAVPQDPKGILEDDVLPDGT 405

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  402 SLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSR------FAPGSsrhSHSFLPFSGGARNCIGKQFAMNELKVAVAL--T 472
Cdd:PLN03195 406 KVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERwikdgvFQNAS---PFKFTAFQAGPRICLGKDSAYLQMKMALALlcR 482


                 ....*...
gi 86198312  473 LLRFELLP 480
Cdd:PLN03195 483 FFKFQLVP 490
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 330-491 1.17e-26

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: 112.07  E-value: 1.17e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 330 WIFYALATNPEHQQRCRKEIQSLLGDG-----TSITWNDLDKMPYTTMCIKEALRIYPPVPSVsRELSSPVTFPDGRSLP 404
Cdd:cd11040 245 WLLAHILSDPELLERIREEIEPAVTPDsgtnaILDLTDLLTSCPLLDSTYLETLRLHSSSTSV-RLVTEDTVLGGGYLLR 323

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 405 KGIHVMLSFYGLHHNPTVW-PNPEVFDPSRF-----APGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFEL 478
Cdd:cd11040 324 KGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkkdgDKKGRGLPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDV 403

                       170
                ....*....|...
gi 86198312 479 LPDPTRvPIPIPR 491
Cdd:cd11040 404 EPVGGG-DWKVPG 415
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 141-491 2.08e-26

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 112.11  E-value: 2.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  141 RRMLTPAFH-YDILKPYTEIMADSVRVMLDKWEQIvgqdSTLEIFRHITLMTLDTIMKCAFSHEGSVQLDRKYKSYiqav 219
Cdd:PLN02302 142 RRLTAAPVNgPEALSTYIPYIEENVKSCLEKWSKM----GEIEFLTELRKLTFKIIMYIFLSSESELVMEALEREY---- 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  220 EDLNDLVFSRVRNI----FHqndiiyrvssNGCKANSacKLAHDHTDqVIKSRRIQLQDEEELEKLkkkrrlDFLDILLF 295
Cdd:PLN02302 214 TTLNYGVRAMAINLpgfaYH----------RALKARK--KLVALFQS-IVDERRNSRKQNISPRKK------DMLDLLLD 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  296 ARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKE----IQSLLGDGTSITWNDLDKMPYTT 371
Cdd:PLN02302 275 AEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEqeeiAKKRPPGQKGLTLKDVRKMEYLS 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  372 MCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRhSHSFLPFSGG 451
Cdd:PLN02302 355 QVIDETLRLINISLTVFREAKTDVEV-NGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTPK-AGTFLPFGLG 432

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 86198312  452 ARNCIGKQFAMNELKVAVALTLLRFELL---PDPTRVPIPIPR 491
Cdd:PLN02302 433 SRLCPGNDLAKLEISIFLHHFLLGYRLErlnPGCKVMYLPHPR 475
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 293-490 2.72e-26

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: 110.61  E-value: 2.72e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 293 LLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLlgDGTSITWNDLDKMPYTTM 372
Cdd:cd20614 193 LIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA--GDVPRTPAELRRFPLAEA 270

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 373 CIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSH-SFLPFSGG 451
Cdd:cd20614 271 LFRETLRLHPPVPFVFRRVLEEIEL-GGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDRAPNPvELLQFGGG 349

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 86198312 452 ARNCIGKQFAMNEL---KVAVALTL----LRFEL---LPDPTRVPIPIP 490
Cdd:cd20614 350 PHFCLGYHVACVELvqfIVALARELgaagIRPLLvgvLPGRRYFPTLHP 398
PLN02183 PLN02183
ferulate 5-hydroxylase
 295-481 4.92e-26

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 111.10  E-value: 4.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  295 FARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCI 374
Cdd:PLN02183 291 SDDLQNSIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTL 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  375 KEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF----APGSSRHSHSFLPFSG 450
Cdd:PLN02183 371 KETLRLHPPIPLLLHETAEDAEV-AGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFlkpgVPDFKGSHFEFIPFGS 449

                        170       180       190
                 ....*....|....*....|....*....|..
gi 86198312  451 GARNCIGKQFAMNELKVAVALTLLRFEL-LPD 481
Cdd:PLN02183 450 GRRSCPGMQLGLYALDLAVAHLLHCFTWeLPD 481
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 139-490 7.76e-26

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: 109.54  E-value: 7.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 139 QHRRMLTPAFHYDILKPYTEIMADSVRVMLDKWEQIVGQDSTLEIFRHITLMTLDTIMKCAFSHEGsvQLDRKYKSYIQA 218
Cdd:cd20636  82 QRRKVLARVFSRAALESYLPRIQDVVRSEVRGWCRGPGPVAVYTAAKSLTFRIAVRILLGLRLEEQ--QFTYLAKTFEQL 159

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 219 VEDLN----DLVFSRVRNifhqndiiyrvssnGCKANSACklaHDHTDQVIKsRRIQLQDEEELEklkkkrrlDFLDILL 294
Cdd:cd20636 160 VENLFslplDVPFSGLRK--------------GIKARDIL---HEYMEKAIE-EKLQRQQAAEYC--------DALDYMI 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 295 FARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSL-LGDG-----TSITWNDLDKMP 368
Cdd:cd20636 214 HSARENGKELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVSHgLIDQcqccpGALSLEKLSRLR 293

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 369 YTTMCIKEALRIYPPVPSVSRelSSPVTFP-DGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHS---HS 444
Cdd:cd20636 294 YLDCVVKEVLRLLPPVSGGYR--TALQTFElDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKsgrFN 371

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 86198312 445 FLPFSGGARNCIGKQFAMNELKV-AVAL-TLLRFEL----LPDPTRVPIPIP 490
Cdd:cd20636 372 YIPFGGGVRSCIGKELAQVILKTlAVELvTTARWELatptFPKMQTVPIVHP 423
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 288-481 2.08e-25

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: 108.39  E-value: 2.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMENGKsLSDKDLRAevdtFMFE----GHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWND 363
Cdd:cd11073 212 DLLLLLDLELDSESE-LTRNHIKA----LLLDlfvaGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESD 286

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 364 LDKMPYTTMCIKEALRIYPPVPS-VSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFApGSSR-- 440
Cdd:cd11073 287 ISKLPYLQAVVKETLRLHPPAPLlLPRKAEEDVEV-MGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFL-GSEIdf 364

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 86198312 441 --HSHSFLPFSGGARNCIGKQFAMNELKVAVAlTLLR-FEL-LPD 481
Cdd:cd11073 365 kgRDFELIPFGSGRRICPGLPLAERMVHLVLA-SLLHsFDWkLPD 408
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 288-482 3.67e-25

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


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 107.55  E-value: 3.67e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMENGKSLSDKDLRAE-----VDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWN 362
Cdd:cd20666 203 DFIDMYLLHIEEEQKNNAESSFNEDylfyiIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLT 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 363 DLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAP--GSSR 440
Cdd:cd20666 283 DKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDenGQLI 362

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 86198312 441 HSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDP 482
Cdd:cd20666 363 KKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPP 404
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 288-457 5.20e-25

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: 107.45  E-value: 5.20e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMENGKSL-SDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDK 366
Cdd:cd20658 216 DWLDVFITLKDENGNPLlTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPN 295

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 367 MPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS-----RH 441
Cdd:cd20658 296 LNYVKACAREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSevtltEP 375

                       170
                ....*....|....*.
gi 86198312 442 SHSFLPFSGGARNCIG 457
Cdd:cd20658 376 DLRFISFSTGRRGCPG 391
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 288-486 1.37e-24

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: 106.04  E-value: 1.37e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLfARMEN----GKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWND 363
Cdd:cd20662 202 DFIDAYL-KEMAKypdpTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLAD 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 364 LDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF-APGSSRH 441
Cdd:cd20662 281 RESMPYTNAVIHEVQRMGNIIPlNVPREVAVDTKL-AGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFlENGQFKK 359

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 86198312 442 SHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVP 486
Cdd:cd20662 360 REAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKPPPNEKL 404
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 288-457 2.26e-24

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: 105.58  E-value: 2.26e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMEN--GKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLD 365
Cdd:cd20657 206 DFLDFVLLENDDNgeGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIP 285

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 366 KMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS----- 439
Cdd:cd20657 286 NLPYLQAICKETFRLHPSTPlNLPRIASEACEV-DGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGRNakvdv 364

                       170
                ....*....|....*....
gi 86198312 440 RHSH-SFLPFSGGARNCIG 457
Cdd:cd20657 365 RGNDfELIPFGAGRRICAG 383
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 306-486 2.86e-24

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 105.93  E-value: 2.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  306 DKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDG-TSITWNDLDKMPYTTMCIKEALRIYPPV 384
Cdd:PLN02426 291 DKYLRDIVVSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNqEAASFEEMKEMHYLHAALYESMRLFPPV 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  385 PSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFAPGSsrhshSFLP--------FSGGARNC 455
Cdd:PLN02426 371 QFDSKFAAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNG-----VFVPenpfkypvFQAGLRVC 445

                        170       180       190
                 ....*....|....*....|....*....|....
gi 86198312  456 IGKQFAMNELKvAVALTLLR---FELLPDPTRVP 486
Cdd:PLN02426 446 LGKEMALMEMK-SVAVAVVRrfdIEVVGRSNRAP 478
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 288-478 3.52e-24

cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in flowering plants and could be classified into ten subfamilies, CYP93A-K. CYP93A appears to be the ancestor that was derived in flowering plants, and the remaining subfamiles show lineage-specific distribution: CYP93B and CYP93C are present in dicots; CYP93F is distributed only in Poaceae; CYP93G and CYP93J are monocot-specific; CYP93E is unique to legumes; CYP93H and CYP93K are only found in Aquilegia coerulea; and CYP93D is Brassicaceae-specific. Members of this family include: Glycyrrhiza echinata CYP93B1, also called licodione synthase (EC 1.14.14.140), that catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively; and Glycine max CYP93A1, also called 3,9-dihydroxypterocarpan 6A-monooxygenase (EC 1.14.14.93), that is involved in the biosynthesis of the phytoalexin glyceollin. CYP93 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 104.99  E-value: 3.52e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILL-FAR---------MENGKSLSdkdlraeVDTFMfEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGT 357
Cdd:cd20655 206 DLLDILLdAYEdenaeykitRNHIKAFI-------LDLFI-AGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTR 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 358 SITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPG 437
Cdd:cd20655 278 LVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKI-NGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLAS 356

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 86198312 438 SS--------RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFEL 478
Cdd:cd20655 357 SRsgqeldvrGQHFKLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCFDW 405
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 141-497 7.27e-24

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: 103.78  E-value: 7.27e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 141 RRMLTPAFHYDILKPY----TEIMADSVRVMLDKWEQI-VGQDSTLEIFRhitlMTLDTIMKCAFSHEGSVQLDRKYKSY 215
Cdd:cd20637  83 RKVFSKLFSHEALESYlpkiQQVIQDTLRVWSSNPEPInVYQEAQKLTFR----MAIRVLLGFRVSEEELSHLFSVFQQF 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 216 IQAVEDLN-DLVFSRVRNIFHQNDIIYRVSSNGCKANSACKLAHDHTDQviksrriqlqdeeeleklkkkrrldfLDILL 294
Cdd:cd20637 159 VENVFSLPlDLPFSGYRRGIRARDSLQKSLEKAIREKLQGTQGKDYADA--------------------------LDILI 212

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 295 FARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEI--QSLLGDGT----SITWNDLDKMP 368
Cdd:cd20637 213 ESAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELrsNGILHNGClcegTLRLDTISSLK 292

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 369 YTTMCIKEALRIYPPVPSVSRelSSPVTFP-DGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHS--- 444
Cdd:cd20637 293 YLDCVIKEVLRLFTPVSGGYR--TALQTFElDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGrfh 370

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 86198312 445 FLPFSGGARNCIGKQFAMNELKV-AVALTLL-RFEL----LPDPTRVPIPIPRIVLKSK 497
Cdd:cd20637 371 YLPFGGGVRTCLGKQLAKLFLKVlAVELASTsRFELatrtFPRMTTVPVVHPVDGLRVK 429
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 322-482 9.51e-24

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 104.43  E-value: 9.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  322 DTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGR 401
Cdd:PLN02394 307 ETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGY 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  402 SLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHS-----FLPFSGGARNCIGKQFAMNELKVAVALTLLRF 476
Cdd:PLN02394 387 DIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAKVEANgndfrFLPFGVGRRSCPGIILALPILGIVLGRLVQNF 466


                 ....*.
gi 86198312  477 ELLPDP 482
Cdd:PLN02394 467 ELLPPP 472
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 288-479 1.62e-23

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: 103.08  E-value: 1.62e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMEnGKSLS--DKD--LRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWND 363
Cdd:cd20654 218 DDDDVMMLSILE-DSQISgyDADtvIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESD 296

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 364 LDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSR-- 440
Cdd:cd20654 297 IKNLVYLQAIVKETLRLYPPGPlLGPREATEDCTV-GGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHKDid 375

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 86198312 441 ---HSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELL 479
Cdd:cd20654 376 vrgQNFELIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIK 417
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 302-487 5.14e-23

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: 101.53  E-value: 5.14e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 302 KSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIY 381
Cdd:cd20647 231 KELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLF 310

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 382 PPVPSVSRelsspVTFPD----GRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFApgssRHSHS-------FLPFSG 450
Cdd:cd20647 311 PVLPGNGR-----VTQDDlivgGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWL----RKDALdrvdnfgSIPFGY 381

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 86198312 451 GARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPI 487
Cdd:cd20647 382 GIRSCIGRRIAELEIHLALIQLLQNFEIKVSPQTTEV 418
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 304-487 6.50e-23

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: 101.24  E-value: 6.50e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 304 LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNP--EHQQRCRKEIQSLLGDGTSITWNDLD--KMPYTTMCIKEALR 379
Cdd:cd11066 224 LTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWEDCAAeeKCPYVVALVKETLR 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 380 IYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSRHSHSFLPFSGGARNCI 456
Cdd:cd11066 304 YFTVLPlGLPRKTTKDIVY-NGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWldASGDLIPGPPHFSFGAGSRMCA 382

                       170       180       190
                ....*....|....*....|....*....|.
gi 86198312 457 GKQFAMNELKVAVALTLLRFELLPDPTRVPI 487
Cdd:cd11066 383 GSHLANRELYTAICRLILLFRIGPKDEEEPM 413
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 320-500 1.30e-22

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: 100.25  E-value: 1.30e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 320 GHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPD 399
Cdd:cd20656 242 GMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHKASENVKIG 321

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 400 GRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSR---HSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRF 476
Cdd:cd20656 322 GYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDikgHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHF 401

                       170       180
                ....*....|....*....|....
gi 86198312 477 ELLPDPtrvPIPIPRIVLKSKNGI 500
Cdd:cd20656 402 SWTPPE---GTPPEEIDMTENPGL 422
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 322-482 1.38e-22

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: 100.24  E-value: 1.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 322 DTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGR 401
Cdd:cd11074 247 ETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLRMAIPLLVPHMNLHDAKLGGY 326

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 402 SLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHS-----FLPFSGGARNCIGKQFAMNELKVAVALTLLRF 476
Cdd:cd11074 327 DIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKVEANgndfrYLPFGVGRRSCPGIILALPILGITIGRLVQNF 406


                ....*.
gi 86198312 477 ELLPDP 482
Cdd:cd11074 407 ELLPPP 412
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 289-486 1.79e-22

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: 99.49  E-value: 1.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 289 FLDILLFARMENGKS---LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLD 365
Cdd:cd20671 201 YIEALIQKQEEDDPKetlFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRK 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 366 KMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSRHSH 443
Cdd:cd20671 281 ALPYTSAVIHEVQRFITLLPHVPRCTAADTQF-KGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFldAEGKFVKKE 359

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 86198312 444 SFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVP 486
Cdd:cd20671 360 AFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLPPPGVSP 402
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 297-497 1.06e-21

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: 97.47  E-value: 1.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 297 RMENGKS--LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCI 374
Cdd:cd20677 223 RKAEDKSavLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFI 302

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 375 KEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSF----LPFSG 450
Cdd:cd20677 303 NEVFRHSSFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLvekvLIFGM 382

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 86198312 451 GARNCIGKQFAMNELKVAVALTL--LRFELLPDPTRVPIPIPRIVLKSK 497
Cdd:cd20677 383 GVRKCLGEDVARNEIFVFLTTILqqLKLEKPPGQKLDLTPVYGLTMKPK 431
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 288-457 1.17e-21

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 97.96  E-value: 1.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  288 DFLDILLfARMEN------GKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITW 361
Cdd:PLN02687 272 DLLSTLL-ALKREqqadgeGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSE 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  362 NDLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSR 440
Cdd:PLN02687 351 SDLPQLTYLQAVIKETFRLHPSTPlSLPRMAAEECEI-NGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPGGEH 429

                        170       180
                 ....*....|....*....|....
gi 86198312  441 -------HSHSFLPFSGGARNCIG 457
Cdd:PLN02687 430 agvdvkgSDFELIPFGAGRRICAG 453
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 288-486 1.84e-21

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 97.20  E-value: 1.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  288 DFLDILLFARMENGKS-LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDK 366
Cdd:PLN03112 275 DFVDVLLSLPGENGKEhMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVH 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  367 MPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSR----- 440
Cdd:PLN03112 355 LNYLRCVVRETFRMHPAGPfLIPHESLRATTI-NGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAEGSrveis 433

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 86198312  441 HSHSF--LPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVP 486
Cdd:PLN03112 434 HGPDFkiLPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDGLRP 481
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 303-492 2.06e-21

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: 96.42  E-value: 2.06e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 303 SLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYP 382
Cdd:cd20661 233 TFSMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCN 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 383 PVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSRHSHSFLPFSGGARNCIGKQF 460
Cdd:cd20661 313 IVPLGIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFldSNGQFAKKEAFVPFSLGRRHCLGEQL 392

                       170       180       190
                ....*....|....*....|....*....|..
gi 86198312 461 AMNELKVAVALTLLRFELLPDPTRVPIPIPRI 492
Cdd:cd20661 393 ARMEMFLFFTALLQRFHLHFPHGLIPDLKPKL 424
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 302-506 2.27e-20

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 93.92  E-value: 2.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  302 KSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQsllgdgTSITWNDLDKMPYTTMCIKEALRIY 381
Cdd:PLN02169 295 KPKKDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEIN------TKFDNEDLEKLVYLHAALSESMRLY 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  382 PPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEV-FDPSRFAP--GSSRH--SHSFLPFSGGARNCI 456
Cdd:PLN02169 369 PPLPFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWGEDALdFKPERWISdnGGLRHepSYKFMAFNSGPRTCL 448

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 86198312  457 GKQFAMNELKVaVALTLLR---FELLpDPTRVPiPIPRIVLKSKNGIHLHLKK 506
Cdd:PLN02169 449 GKHLALLQMKI-VALEIIKnydFKVI-EGHKIE-AIPSILLRMKHGLKVTVTK 498
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 288-480 5.41e-20

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: 92.13  E-value: 5.41e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLfARM--ENGKSLS---DKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWN 362
Cdd:cd20669 202 DFIDCFL-TKMaeEKQDPLShfnMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLE 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 363 DLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSS 439
Cdd:cd20669 281 DRARMPYTDAVIHEIQRFADIIPmSLPHAVTRDTNF-RGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFldDNGSF 359

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 86198312 440 RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLP 480
Cdd:cd20669 360 KKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 120-487 7.01e-20

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: 90.82  E-value: 7.01e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 120 FLAPWIGRGLLMLDGQTWFQHRRMLTPAFhydilkpyteimadsVRVMLDKWEQivgqdstlEIFRHITLMTLDTIMKca 199
Cdd:cd20629  39 LGGPFLGHSILAMDGEEHRRRRRLLQPAF---------------APRAVARWEE--------PIVRPIAEELVDDLAD-- 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 200 fshEGSVQLDRKYKSYIQAV----------EDLNDlvFSR-VRNIFHQNDIIYRVSSNGCKAnSACKLaHDHTDQVIKSR 268
Cdd:cd20629  94 ---LGRADLVEDFALELPARviyallglpeEDLPE--FTRlALAMLRGLSDPPDPDVPAAEA-AAAEL-YDYVLPLIAER 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 269 RIQLQDeeeleklkkkrrlDFLDILLFARMENGKsLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKE 348
Cdd:cd20629 167 RRAPGD-------------DLISRLLRAEVEGEK-LDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRRD 232

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 349 iQSLLGdgtsitwndldkmpyttMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEV 428
Cdd:cd20629 233 -RSLIP-----------------AAIEEGLRWEPPVASVPRMALRDVEL-DGVTIPAGSLLDLSVGSANRDEDVYPDPDV 293

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86198312 429 FDPSRfapgsSRHSHsfLPFSGGARNCIGKQFAMNELKVAVALTLLRF---ELLPDPTRVPI 487
Cdd:cd20629 294 FDIDR-----KPKPH--LVFGGGAHRCLGEHLARVELREALNALLDRLpnlRLDPDAPAPEI 348
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 298-478 1.25e-19

cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes catalyze the final steps in the production of glucocorticoids and mineralocorticoids that takes place in the adrenal gland. There are two human CYP11B isoforms: Cyb11B1 (11-beta-hydroxylase or P45011beta), which catalyzes the final step of cortisol synthesis by a one-step reaction from 11-deoxycortisol; and CYP11B2 (aldosterone synthase or P450aldo), which catalyzes three steps in the synthesis of aldosterone. The CYP11B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 91.06  E-value: 1.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 298 MENGKsLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEA 377
Cdd:cd20644 223 LLQAE-LSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKET 301

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 378 LRIYPPVPSVSRELSSPVTFPDGRsLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAP--GSSRHSHSfLPFSGGARNC 455
Cdd:cd20644 302 LRLYPVGITVQRVPSSDLVLQNYH-IPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDirGSGRNFKH-LAFGFGMRQC 379

                       170       180
                ....*....|....*....|...
gi 86198312 456 IGKQFAMNELKVAVALTLLRFEL 478
Cdd:cd20644 380 LGRRLAEAEMLLLLMHVLKNFLV 402
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 288-482 2.61e-19

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: 90.25  E-value: 2.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMENGKSLS----DKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITwND 363
Cdd:cd20664 201 GFIDAFLVKQQEEEESSDsffhDDNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQV-EH 279

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 364 LDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSR 440
Cdd:cd20664 280 RKNMPYTDAVIHEIQRFANIVPmNLPHATTRDVTF-RGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFldSQGKFV 358

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 86198312 441 HSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDP 482
Cdd:cd20664 359 KRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQPPP 400
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 304-465 2.63e-19

cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain cleavage enzyme; Cytochrome P450 11A1 (CYP11A1, EC 1.14.15.6) is also called cholesterol side-chain cleavage enzyme, cholesterol desmolase, or cytochrome P450(scc). It catalyzes the side-chain cleavage reaction of cholesterol to form pregnenolone, the precursor of all steroid hormones. Missense or nonsense mutations of the CYP11A1 gene cause mild to severe early-onset adrenal failure depending on the severity of the enzyme dysfunction/deficiency. CYP11A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 90.16  E-value: 2.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 304 LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEI----QSLLGDGTSItwndLDKMPYTTMCIKEALR 379
Cdd:cd20643 230 LPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVlaarQEAQGDMVKM----LKSVPLLKAAIKETLR 305

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 380 IYPPVPSVSRELSSPVTFPDGRsLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSfLPFSGGARNCIGKQ 459
Cdd:cd20643 306 LHPVAVSLQRYITEDLVLQNYH-IPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRN-LGFGFGPRQCLGRR 383


                ....*.
gi 86198312 460 FAMNEL 465
Cdd:cd20643 384 IAETEM 389
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 288-494 3.30e-19

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: 89.19  E-value: 3.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMEnGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRkeiqsllgdgtsitwNDLDKM 367
Cdd:cd11035 171 DLISAILNAEID-GRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLR---------------EDPELI 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 368 PyttMCIKEALRIYPPVpSVSRELSSPVTFpDGRSLPKG--IHVMLSFYGLhhNPTVWPNPEVFDPSRfapgsSRHSHsf 445
Cdd:cd11035 235 P---AAVEELLRRYPLV-NVARIVTRDVEF-HGVQLKAGdmVLLPLALANR--DPREFPDPDTVDFDR-----KPNRH-- 300

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 86198312 446 LPFSGGARNCIGKQFAMNELKVAVALTLLR---FELlpDPTRVPIPIPRIVL 494
Cdd:cd11035 301 LAFGAGPHRCLGSHLARLELRIALEEWLKRipdFRL--APGAQPTYHGGSVM 350
PLN03018 PLN03018
homomethionine N-hydroxylase
 288-476 4.32e-19

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 90.07  E-value: 4.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  288 DFLDILLFARMENGKSLSDKD-LRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDK 366
Cdd:PLN03018 293 DWLDTFITLKDQNGKYLVTPDeIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPN 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  367 MPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSS------- 439
Cdd:PLN03018 373 LNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDGitkevtl 452

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 86198312  440 -RHSHSFLPFSGGARNCIGKQFAmnelKVAVALTLLRF 476
Cdd:PLN03018 453 vETEMRFVSFSTGRRGCVGVKVG----TIMMVMMLARF 486
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 288-462 5.52e-19

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 89.91  E-value: 5.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  288 DFLDILLfARMEN--GKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLD 365
Cdd:PLN00110 268 DFLDVVM-ANQENstGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLP 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  366 KMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFApgSSRHSH-- 443
Cdd:PLN00110 347 KLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFL--SEKNAKid 424

                        170       180
                 ....*....|....*....|....*
gi 86198312  444 ------SFLPFSGGARNCIGKQFAM 462
Cdd:PLN00110 425 prgndfELIPFGAGRRICAGTRMGI 449
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 313-481 6.61e-19

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: 88.74  E-value: 6.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 313 VDTFMfEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRiYPPVPSVS--RE 390
Cdd:cd20667 231 IDLFL-GGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQR-LSNVVSVGavRQ 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 391 LSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSRHSHSFLPFSGGARNCIGKQFAMNELKVA 468
Cdd:cd20667 309 CVTSTTM-HGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFldKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIF 387

                       170
                ....*....|....
gi 86198312 469 VALTLLRFEL-LPD 481
Cdd:cd20667 388 FTTLLRTFNFqLPE 401
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 258-486 7.96e-19

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: 88.04  E-value: 7.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 258 HDHTDQVIKSRRIQLQDeeeleklkkkrrlDFLDILLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALAT 337
Cdd:cd11078 172 WAYFADLVAERRREPRD-------------DLISDLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLE 238

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 338 NPEHQQRCRkEIQSLLGDGtsitwndldkmpyttmcIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLH 417
Cdd:cd11078 239 HPDQWRRLR-ADPSLIPNA-----------------VEETLRYDSPVQGLRRTATRDVEI-GGVTIPAGARVLLLFGSAN 299

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86198312 418 HNPTVWPNPEVFDPSRfaPGSSRHshsfLPFSGGARNCIGKQFAMNELKVAVALTLLRFE----LLPDPTRVP 486
Cdd:cd11078 300 RDERVFPDPDRFDIDR--PNARKH----LTFGHGIHFCLGAALARMEARIALEELLRRLPgmrvPGQEVVYSP 366
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 322-480 9.99e-19

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


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 88.11  E-value: 9.99e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 322 DTTASGISWIFYALATNPEHQQRCRKEIQSLLGDgTSITWND--LDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPD 399
Cdd:cd20615 229 DVTTGVLSWNLVFLAANPAVQEKLREEISAAREQ-SGYPMEDyiLSTDTLLAYCVLESLRLRPLLAFSVPESSPTDKIIG 307

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 400 GRSLPKGIHVMLSFYGLHHN-PTVWPNPEVFDPSRFA---PGSSRhsHSFLPFSGGARNCIGKQFAMNELKVAVALTLLR 475
Cdd:cd20615 308 GYRIPANTPVVVDTYALNINnPFWGPDGEAYRPERFLgisPTDLR--YNFWRFGFGPRKCLGQHVADVILKALLAHLLEQ 385


                ....*
gi 86198312 476 FELLP 480
Cdd:cd20615 386 YELKL 390
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 309-482 1.24e-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: 1.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 309 LRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLL----GDGTSITWNDLDKM--PYTTMCIKEALRIYP 382
Cdd:cd20622 263 IHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHpeavAEGRLPTAQEIAQAriPYLDAVIEEILRCAN 342

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 383 PVPSVSRELSSPVTFPdGRSLPKGIHVMLSFYGlhhnPTVW-PNPEV--------------------------FDPSR-- 433
Cdd:cd20622 343 TAPILSREATVDTQVL-GYSIPKGTNVFLLNNG----PSYLsPPIEIdesrrssssaakgkkagvwdskdiadFDPERwl 417

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 86198312 434 ----------FAPGSSRHshsfLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDP 482
Cdd:cd20622 418 vtdeetgetvFDPSAGPT----LAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPLP 472
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 325-490 1.83e-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: 87.37  E-value: 1.83e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 325 ASGISWIFYALA---TNPEHQQRCRKEIQSLLGDG----TSITWNDLDKMPYTTMCIKEALRIYPPvPSVSRELSSPVTF 397
Cdd:cd20635 224 ANAIPITFWTLAfilSHPSVYKKVMEEISSVLGKAgkdkIKISEDDLKKMPYIKRCVLEAIRLRSP-GAITRKVVKPIKI 302

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 398 PDgRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSR----------FAPGssrhshsFLPFSGGARNCIGKQFAMNELKV 467
Cdd:cd20635 303 KN-YTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERwkkadleknvFLEG-------FVAFGGGRYQCPGRWFALMEIQM 374

                       170       180
                ....*....|....*....|....
gi 86198312 468 AVALTLLRFEL-LPDPtrVPIPIP 490
Cdd:cd20635 375 FVAMFLYKYDFtLLDP--VPKPSP 396
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
 288-465 8.84e-18

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: 85.60  E-value: 8.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFaRMENGKS-----LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWN 362
Cdd:cd20672 202 DFIDTYLL-RMEKEKSnhhteFHHQNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLD 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 363 DLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSS 439
Cdd:cd20672 281 DRAKMPYTDAVIHEIQRFSDLIPiGVPHRVTKDTLF-RGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFldANGAL 359

                       170       180
                ....*....|....*....|....*.
gi 86198312 440 RHSHSFLPFSGGARNCIGKQFAMNEL 465
Cdd:cd20672 360 KKSEAFMPFSTGKRICLGEGIARNEL 385
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 157-484 1.14e-17

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: 85.10  E-value: 1.14e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 157 TEIMADSVRVMLDKWEQIVGQDSTLEIFrhitlmtldTIMKCafshegsVQLDRKYKSYIQAVEDLNDLVFsRVRNIFH- 235
Cdd:cd20616  90 VTVCVESTNTHLDNLEEVTNESGYVDVL---------TLMRR-------IMLDTSNRLFLGVPLNEKAIVL-KIQGYFDa 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 236 ------QNDIIYRVSSNGCKANSACKLAHDHTDQVIKSRRIQLQdeeelEKLKKKRRLDFLDILLFArmENGKSLSDKDL 309
Cdd:cd20616 153 wqalliKPDIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRIS-----TAEKLEDHMDFATELIFA--QKRGELTAENV 225

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 310 RAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDgTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSR 389
Cdd:cd20616 226 NQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGE-RDIQNDDLQKLKVLENFINESMRYQPVVDFVMR 304

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 390 E-LSSPVTfpDGRSLPKGIHVMLSFYGLHHNPtVWPNPEVFDPSRFA-PGSSRHshsFLPFSGGARNCIGKQFAMNELKV 467
Cdd:cd20616 305 KaLEDDVI--DGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFEkNVPSRY---FQPFGFGPRSCVGKYIAMVMMKA 378

                       330
                ....*....|....*..
gi 86198312 468 AVALTLLRFELLPDPTR 484
Cdd:cd20616 379 ILVTLLRRFQVCTLQGR 395
PLN00168 PLN00168
Cytochrome P450; Provisional
 289-477 1.26e-17

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 85.77  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  289 FLDILLFARM--ENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGT-SITWNDLD 365
Cdd:PLN00168 285 YVDTLLDIRLpeDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQeEVSEEDVH 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  366 KMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPG-------- 437
Cdd:PLN00168 365 KMPYLKAVVLEGLRKHPPAHFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLAGgdgegvdv 444

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 86198312  438 SSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFE 477
Cdd:PLN00168 445 TGSREIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREFE 484
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 317-473 1.51e-17

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: 84.58  E-value: 1.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 317 MFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPS-VSRELSSPV 395
Cdd:cd20653 236 LLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLlVPHESSEDC 315

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86198312 396 TFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFApGSSRHSHSFLPFSGGARNCIGKQFAMNelkvAVALTL 473
Cdd:cd20653 316 KI-GGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFE-GEEREGYKLIPFGLGRRACPGAGLAQR----VVGLAL 387
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 263-491 2.00e-17

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: 84.01  E-value: 2.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 263 QVIKSRRIQLQDEeeleklkkkrrlDFLDILLFARmENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQ 342
Cdd:cd20630 171 EVIAERRQAPVED------------DLLTTLLRAE-EDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEAL 237

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 343 QRCRKEiQSLLGDGTS--ITWNDLDKMpyttmcikealriyppvpSVSRELSSPVTFPdGRSLPKGIHVMLSFYGLHHNP 420
Cdd:cd20630 238 RKVKAE-PELLRNALEevLRWDNFGKM------------------GTARYATEDVELC-GVTIRKGQMVLLLLPSALRDE 297

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86198312 421 TVWPNPEVFDPsrfapgsSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRF---ELLPDPTRVPIPIPR 491
Cdd:cd20630 298 KVFSDPDRFDV-------RRDPNANIAFGYGPHFCIGAALARLELELAVSTLLRRFpemELAEPPVFDPHPVLR 364
PLN02971 PLN02971
tryptophan N-hydroxylase
 288-487 2.21e-17

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 85.09  E-value: 2.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  288 DFLDILLFARMENGKSLSDKD-LRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDK 366
Cdd:PLN02971 306 DFLDIFISIKDEAGQPLLTADeIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPK 385

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  367 MPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHS-- 444
Cdd:PLN02971 386 LNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTen 465

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 86198312  445 ---FLPFSGGARNCIGKQF--AMNELKVAVALTLLRFELLPDPTRVPI 487
Cdd:PLN02971 466 dlrFISFSTGKRGCAAPALgtAITTMMLARLLQGFKWKLAGSETRVEL 513
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 288-465 2.51e-17

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: 84.29  E-value: 2.51e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFA-----RMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWN 362
Cdd:cd20675 210 DMMDAFILAlekgkSGDSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIE 289

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 363 DLDKMPYTTMCIKEALRiyppvpsvsreLSS--PVTFP---------DGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDP 431
Cdd:cd20675 290 DQPNLPYVMAFLYEAMR-----------FSSfvPVTIPhattadtsiLGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDP 358

                       170       180       190
                ....*....|....*....|....*....|....*...
gi 86198312 432 SRF--APGS--SRHSHSFLPFSGGARNCIGKQFAMNEL 465
Cdd:cd20675 359 TRFldENGFlnKDLASSVMIFSVGKRRCIGEELSKMQL 396
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 259-483 3.13e-17

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: 83.15  E-value: 3.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 259 DHTDQVIKSRRIQLQDeeeleklkkkrrlDFLDILLFARMeNGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATN 338
Cdd:cd11034 155 GHLRDLIAERRANPRD-------------DLISRLIEGEI-DGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQH 220

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 339 PEHQQRCRkeiqsllgdgtsitwNDLDKMPyttMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHH 418
Cdd:cd11034 221 PEDRRRLI---------------ADPSLIP---NAVEEFLRFYSPVAGLARTVTQEVEV-GGCRLKPGDRVLLAFASANR 281

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86198312 419 NPTVWPNPEVFDPSRFApgsSRHshsfLPFSGGARNCIGKQFAMNELKVAVALTLLR---FELLPDPT 483
Cdd:cd11034 282 DEEKFEDPDRIDIDRTP---NRH----LAFGSGVHRCLGSHLARVEARVALTEVLKRipdFELDPGAT 342
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 129-491 3.67e-17

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 83.88  E-value: 3.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  129 LLMLDGQTwfqHRRM--LTPAF-HYDILKPYTEIMADS-VRVMLDKWEqivgqdSTLEIFRHITLMTLDTIMKCAFSHEG 204
Cdd:PLN02987 117 LLLMKGNL---HKKMhsLTMSFaNSSIIKDHLLLDIDRlIRFNLDSWS------SRVLLMEEAKKITFELTVKQLMSFDP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  205 SVQLDRKYKSYIQAVEDLndlvFSRVRNIFHQNdiiYRvssngcKANSACKLAHDHTDQVIKSRRIQLQDEEELEKLkkk 284
Cdd:PLN02987 188 GEWTESLRKEYVLVIEGF----FSVPLPLFSTT---YR------RAIQARTKVAEALTLVVMKRRKEEEEGAEKKKD--- 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  285 rrldfldiLLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKE---IQSLLGDGTSITW 361
Cdd:PLN02987 252 --------MLAALLASDDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEhekIRAMKSDSYSLEW 323

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  362 NDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFA--PGSS 439
Cdd:PLN02987 324 SDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEV-KGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQsnSGTT 402

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86198312  440 RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPD--------PT-----RVPIPIPR 491
Cdd:PLN02987 403 VPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSWVPAeqdklvffPTtrtqkRYPINVKR 467
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 288-482 7.04e-17

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: 82.69  E-value: 7.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFaRMENGKSLSDKDLRAE------VDTFmFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITW 361
Cdd:cd20665 202 DFIDCFLI-KMEQEKHNQQSEFTLEnlavtvTDLF-GAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCM 279

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 362 NDLDKMPYTTMCIKEALRIYPPVPS-VSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGS 438
Cdd:cd20665 280 QDRSHMPYTDAVIHEIQRYIDLVPNnLPHAVTCDTKF-RNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFldENGN 358

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 86198312 439 SRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLP--DP 482
Cdd:cd20665 359 FKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSlvDP 404
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 288-465 9.79e-17

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: 82.15  E-value: 9.79e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFaRMENGKSLSD-----KDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWN 362
Cdd:cd20668 202 DFIDSFLI-RMQEEKKNPNtefymKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFE 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 363 DLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFA--PGSS 439
Cdd:cd20668 281 DRAKMPYTEAVIHEIQRFGDVIPmGLARRVTKDTKF-RDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLddKGQF 359

                       170       180
                ....*....|....*....|....*.
gi 86198312 440 RHSHSFLPFSGGARNCIGKQFAMNEL 465
Cdd:cd20668 360 KKSDAFVPFSIGKRYCFGEGLARMEL 385
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 288-476 2.54e-16

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: 80.89  E-value: 2.54e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLfARMENGK-----SLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWN 362
Cdd:cd20663 206 DLTDAFL-AEMEKAKgnpesSFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMA 284

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 363 DLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSSR 440
Cdd:cd20663 285 DQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFldAQGHFV 364

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 86198312 441 HSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRF 476
Cdd:cd20663 365 KPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRF 400
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 288-476 3.37e-16

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: 80.30  E-value: 3.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMENGKsLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKeiqsllgdgtsitwnDLDKM 367
Cdd:cd11031 187 DLLSALVAARDDDDR-LSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRA---------------DPELV 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 368 PYTtmcIKEALRIYPPVPSVS--RELSSPVTFPDGRsLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPgssrhSHsf 445
Cdd:cd11031 251 PAA---VEELLRYIPLGAGGGfpRYATEDVELGGVT-IRAGEAVLVSLNAANRDPEVFPDPDRLDLDREPN-----PH-- 319

                       170       180       190
                ....*....|....*....|....*....|.
gi 86198312 446 LPFSGGARNCIGKQFAMNELKVAVALTLLRF 476
Cdd:cd11031 320 LAFGHGPHHCLGAPLARLELQVALGALLRRL 350
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 291-483 4.07e-16

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: 79.90  E-value: 4.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 291 DIL--LFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRkeiqsllgdgtsitwNDLDKMP 368
Cdd:cd20625 182 DLIsaLVAAEEDGDRLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQLALLR---------------ADPELIP 246

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 369 YTtmcIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRfAPGssRHshsfLPF 448
Cdd:cd20625 247 AA---VEELLRYDSPVQLTARVALEDVEI-GGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITR-APN--RH----LAF 315

                       170       180       190
                ....*....|....*....|....*....|....*
gi 86198312 449 SGGARNCIGKQFAMneLKVAVALTLLrFELLPDPT 483
Cdd:cd20625 316 GAGIHFCLGAPLAR--LEAEIALRAL-LRRFPDLR 347
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 288-480 1.55e-15

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: 78.43  E-value: 1.55e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFaRMENGKS-----LSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWN 362
Cdd:cd20670 202 DFIDCFLI-KMHQDKNnphteFNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVD 280

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 363 DLDKMPYTTMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSS 439
Cdd:cd20670 281 DRVKMPYTDAVIHEIQRLTDIVPlGVPHNVIRDTQF-RGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFldEQGRF 359

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 86198312 440 RHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLP 480
Cdd:cd20670 360 KKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSLRS 400
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 249-484 2.85e-15

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: 77.41  E-value: 2.85e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 249 KANSACKLAHDHTDQVIKSRRIQLQDeeeleklkkkrrlDFLDILLFARmENGKSLSDKDLRAEVDTFMFEGHDTTASGI 328
Cdd:cd11038 169 RIEAAVEELYDYADALIEARRAEPGD-------------DLISTLVAAE-QDGDRLSDEELRNLIVALLFAGVDTTRNQL 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 329 SWIFYALATNPEhQQRCRKEIQSLLGDGtsitwndldkmpyttmcIKEALRIYPPVPSVSRELSSPVTFPDGRsLPKGIH 408
Cdd:cd11038 235 GLAMLTFAEHPD-QWRALREDPELAPAA-----------------VEEVLRWCPTTTWATREAVEDVEYNGVT-IPAGTV 295

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86198312 409 VMLSFYGLHHnptvwpNPEVFDPSRFAPGSSRHSHsfLPFSGGARNCIGKQFAMNELkvAVALTLLRfELLPDPTR 484
Cdd:cd11038 296 VHLCSHAANR------DPRVFDADRFDITAKRAPH--LGFGGGVHHCLGAFLARAEL--AEALTVLA-RRLPTPAI 360
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
 288-486 1.31e-14

cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces sp. P450sky (also called CYP163B3), Sphingopyxis macrogoltabida P450pyr hydroxylase, Novosphingobium aromaticivorans CYP108D1, Pseudomonas sp. cytochrome P450-Terp (P450terp), and Amycolatopsis balhimycina P450 OxyD, as well as several Mycobacterium proteins CYP124, CYP125, CYP126, and CYP142. P450sky is involved in the hydroxylation of three beta-hydroxylated amino acid precursors required for the biosynthesis of the cyclic depsipeptide skyllamycin. P450pyr hydroxylase is an active and selective catalyst for the regio- and stereo-selective hydroxylation at non-activated carbon atoms with a broad substrate range. P450terp catalyzes the hydroxylation of alpha-terpineol as part of its catabolic assimilation. OxyD is involved in beta-hydroxytyrosine formation during vancomycin biosynthesis. CYP124 is a methyl-branched lipid omega-hydroxylase while CYP142 is a cholesterol 27-oxidase with likely roles in host response modulation and cholesterol metabolism. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 75.26  E-value: 1.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMeNGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRkeiqsllgdgtsitwNDLDKM 367
Cdd:cd11033 190 DLISVLANAEV-DGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLR---------------ADPSLL 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 368 PytTMcIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRfAPGssRHshsfLP 447
Cdd:cd11033 254 P--TA-VEEILRWASPVIHFRRTATRDTEL-GGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR-SPN--PH----LA 322

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 86198312 448 FSGGARNCIGKQFAMNELKVAVA--LTLL-RFELLPDPTRVP 486
Cdd:cd11033 323 FGGGPHFCLGAHLARLELRVLFEelLDRVpDIELAGEPERLR 364
PLN02774 PLN02774
brassinosteroid-6-oxidase
 288-506 2.69e-14

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 74.81  E-value: 2.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  288 DFLDILLfaRMENGK-SLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKE---IQSLLGDGTSITWND 363
Cdd:PLN02774 245 DMLGYLM--RKEGNRyKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKALQELRKEhlaIRERKRPEDPIDWND 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  364 LDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSH 443
Cdd:PLN02774 323 YKSMRFTRAVIFETSRLATIVNGVLRKTTQDMEL-NGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKSLESHN 401

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86198312  444 SFLPFSGGARNCIGKQFAMNELKVAVA--LTLLRFELLPDPTRVpiPIPRIvlKSKNGIHLHLKK 506
Cdd:PLN02774 402 YFFLFGGGTRLCPGKELGIVEISTFLHyfVTRYRWEEVGGDKLM--KFPRV--EAPNGLHIRVSP 462
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 320-480 4.78e-14

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: 73.89  E-value: 4.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 320 GHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVP-----SVSRElssp 394
Cdd:cd20676 249 GFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPftiphCTTRD---- 324

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 395 vTFPDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGSS---RHSHSFLPFSGGARNCIGKQFAMNE--LKV 467
Cdd:cd20676 325 -TSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFltADGTEinkTESEKVMLFGLGKRRCIGESIARWEvfLFL 403

                       170
                ....*....|...
gi 86198312 468 AVALTLLRFELLP 480
Cdd:cd20676 404 AILLQQLEFSVPP 416
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 320-486 6.70e-14

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 73.00  E-value: 6.70e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 320 GHDTTASGISWIFYALATNPEHQQRCRkeiqsllgdgtsitwNDLDKMPYttmCIKEALRIYPPVPSVSRELSSPVTFpD 399
Cdd:cd11037 214 GLDTTISAIGNALWLLARHPDQWERLR---------------ADPSLAPN---AFEEAVRLESPVQTFSRTTTRDTEL-A 274

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 400 GRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFApgsSRHshsfLPFSGGARNCIGKQFAMNELKvAVALTLL----R 475
Cdd:cd11037 275 GVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITRNP---SGH----VGFGHGVHACVGQHLARLEGE-ALLTALArrvdR 346

                       170
                ....*....|.
gi 86198312 476 FELLPDPTRVP 486
Cdd:cd11037 347 IELAGPPVRAL 357
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 101-477 1.06e-13

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: 72.50  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 101 DYMKLILGRSDPKANGSYRFLA--PWIGRGLLMLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVRVMLDKweqivgqd 178
Cdd:cd11080  18 EDVRRILKDPDGFTTKSLAERAepVMRGPVLAQMTGKEHAAKRAIVVRAFRGDALDHLLPLIKENAEELIAP-------- 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 179 stleiFRHITLMTLDTIMKCAFSHEGSVQ---LDRKYKSYIQAvedLNDLVFSRVRNIfhQNDIIYRVSSNGCkansACK 255
Cdd:cd11080  90 -----FLERGRVDLVNDFGKPFAVNVTMDmlgLDKRDHEKIHE---WHSSVAAFITSL--SQDPEARAHGLRC----AEQ 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 256 LAHdHTDQVIKSRRIQLQDeeeleklkkkrrlDFLDILLFARMeNGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYAL 335
Cdd:cd11080 156 LSQ-YLLPVIEERRVNPGS-------------DLISILCTAEY-EGEALSDEDIKALILNVLLAATEPADKTLALMIYHL 220

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 336 ATNPEHQQRCRKEiQSLLgdgtsitwndldkmpytTMCIKEALRIYPPVPSVSRELSSPVTFPDGRsLPKGIHVMLSFYG 415
Cdd:cd11080 221 LNNPEQLAAVRAD-RSLV-----------------PRAIAETLRYHPPVQLIPRQASQDVVVSGME-IKKGTTVFCLIGA 281

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86198312 416 LHHNPTVWPNPEVFDPSR--------FAPgSSRHshsfLPFSGGARNCIGKQFAMNELKVAVALTL-----LRFE 477
Cdd:cd11080 282 ANRDPAAFEDPDTFNIHRedlgirsaFSG-AADH----LAFGSGRHFCVGAALAKREIEIVANQVLdalpnIRLE 351
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 335-488 1.48e-13

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: 72.11  E-value: 1.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 335 LATNPEHQQRCRKEIQSLLGDGTsitwndldkMPYTTMCIKEALRIYPPVPSVSRELSSPvTFPDGRSLPKGIHVMLSFY 414
Cdd:cd20624 218 LAAHPEQAARAREEAAVPPGPLA---------RPYLRACVLDAVRLWPTTPAVLRESTED-TVWGGRTVPAGTGFLIFAP 287

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86198312 415 GLHHNPTVWPNPEVFDPSRFAPGSSRHSHSFLPFSGGARNCIGKQFAMNELKVAVALTLLRFELLPDPTRVPIP 488
Cdd:cd20624 288 FFHRDDEALPFADRFVPEIWLDGRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLESPRSGP 361
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 328-495 2.16e-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: 71.79  E-value: 2.16e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 328 ISWIFYALATNPEHQQRCRKeiqsllgdgtsitwndlDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGI 407
Cdd:cd11067 240 VTFAALALHEHPEWRERLRS-----------------GDEDYAEAFVQEVRRFYPFFPFVGARARRDFEW-QGYRFPKGQ 301

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 408 HVMLSFYGLHHNPTVWPNPEVFDPSRFApGSSRHSHSFLPFSGG--ARN--CIGKQFAMNELKVAVA-LTLLRFELLPDP 482
Cdd:cd11067 302 RVLLDLYGTNHDPRLWEDPDRFRPERFL-GWEGDPFDFIPQGGGdhATGhrCPGEWITIALMKEALRlLARRDYYDVPPQ 380

                       170       180
                ....*....|....*....|
gi 86198312 483 ------TRVP-IPIPRIVLK 495
Cdd:cd11067 381 dlsidlNRMPaLPRSGFVIR 400
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
 289-480 3.72e-13

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: 71.00  E-value: 3.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 289 FLDILLFArmengkSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGtSITWNDLDKMP 368
Cdd:cd20627 189 FIDSLLQG------NLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQVLGKG-PITLEKIEQLR 261

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 369 YTTMCIKEALRI--YPPVPSVSRELSSPVtfpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHSHSFL 446
Cdd:cd20627 262 YCQQVLCETVRTakLTPVSARLQELEGKV---DQHIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRFDDESVMKSFSLL 338

                       170       180       190
                ....*....|....*....|....*....|....
gi 86198312 447 PFSgGARNCIGKQFAMNELKVAVALTLLRFELLP 480
Cdd:cd20627 339 GFS-GSQECPELRFAYMVATVLLSVLVRKLRLLP 371
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 330-489 4.03e-13

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: 71.25  E-value: 4.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 330 WIFYALATNPEHQQRCRKEIQSLL-------GDGTS---ITWNDLDKMPYTTMCIKEALRiyppVPSVS---RELSSPVT 396
Cdd:cd20631 249 WSLFYLLRCPEAMKAATKEVKRTLektgqkvSDGGNpivLTREQLDDMPVLGSIIKEALR----LSSASlniRVAKEDFT 324

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 397 F--PDGRSLP--KGIHVMLSFYGLHHNPTVWPNPEVFDPSR-----------FAPGSSRHSHSFLPFSGGARNCIGKQFA 461
Cdd:cd20631 325 LhlDSGESYAirKDDIIALYPQLLHLDPEIYEDPLTFKYDRyldengkekttFYKNGRKLKYYYMPFGSGTSKCPGRFFA 404

                       170       180
                ....*....|....*....|....*....
gi 86198312 462 MNELKVAVALTLLRFEL-LPDPTRVPIPI 489
Cdd:cd20631 405 INEIKQFLSLMLCYFDMeLLDGNAKCPPL 433
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 289-477 4.17e-13

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 71.26  E-value: 4.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  289 FLDILLFARMENGKSL--SDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGDGTSITWNDLDK 366
Cdd:PLN03234 267 FIDLLMQIYKDQPFSIkfTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPN 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  367 MPYTTMCIKEALRIYPPVPSVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFA---PGSSRHS 442
Cdd:PLN03234 347 LPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPERFMkehKGVDFKG 426

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 86198312  443 HSF--LPFSGGARNCIGKQFAMNELKVAVALTLLRFE 477
Cdd:PLN03234 427 QDFelLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFD 463
PLN02966 PLN02966
cytochrome P450 83A1
 308-481 7.11e-13

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 70.55  E-value: 7.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  308 DLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLGD--GTSITWNDLDKMPYTTMCIKEALRIYPPVP 385
Cdd:PLN02966 289 NVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEkgSTFVTEDDVKNLPYFRALVKETLRIEPVIP 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  386 SVSRELSSPVTFPDGRSLPKGIHVMLSFYGLHHNPTVW-PNPEVFDPSRFAPGS---SRHSHSFLPFSGGARNCIGKQFA 461
Cdd:PLN02966 369 LLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEvdfKGTDYEFIPFGSGRRMCPGMRLG 448

                        170       180
                 ....*....|....*....|.
gi 86198312  462 MNELKVAVALTLLRFEL-LPD 481
Cdd:PLN02966 449 AAMLEVPYANLLLNFNFkLPN 469
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 258-481 8.20e-13

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: 69.87  E-value: 8.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 258 HDHTDQVIKSRRIQLQDeeeleklkkkrrlDFLDILLFARmENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALAT 337
Cdd:cd11029 175 VDYLAELVARKRAEPGD-------------DLLSALVAAR-DEGDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLT 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 338 NPEhqQRcrkeiqSLLGDGTSiTWNDLdkmpyttmcIKEALRIYPPVPSVS-RELSSPVTFpDGRSLPKGIHVMLSFYGL 416
Cdd:cd11029 241 HPD--QL------ALLRADPE-LWPAA---------VEELLRYDGPVALATlRFATEDVEV-GGVTIPAGEPVLVSLAAA 301

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86198312 417 HHNPTVWPNPEVFDPSRfapGSSRHshsfLPFSGGARNCIGKQFAMNELKVAVAlTLL-RFellPD 481
Cdd:cd11029 302 NRDPARFPDPDRLDITR---DANGH----LAFGHGIHYCLGAPLARLEAEIALG-ALLtRF---PD 356
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 330-487 1.16e-12

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: 69.64  E-value: 1.16e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 330 WIFYALATNPEHQQRCRKEIQSLLGDG---------TSITWNDLDKMPYTTMCIKEALRiyppVPSVS---RELSSPVT- 396
Cdd:cd20632 237 WAMYYLLRHPEALAAVRDEIDHVLQSTgqelgpdfdIHLTREQLDSLVYLESAINESLR----LSSASmniRVVQEDFTl 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 397 -FPDGRS--LPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRFAPGSSRHS----------HSFLPFSGGARNCIGKQFAMN 463
Cdd:cd20632 313 kLESDGSvnLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKKTtfykrgqklkYYLMPFGSGSSKCPGRFFAVN 392

                       170       180
                ....*....|....*....|....
gi 86198312 464 ELKVAVALTLLRFELLPDPTRVPI 487
Cdd:cd20632 393 EIKQFLSLLLLYFDLELLEEQKPP 416
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 265-490 2.63e-12

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 68.39  E-value: 2.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 265 IKSRRIQLQDeeeleklkkkrrlDFLDILLFARMENGKsLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQR 344
Cdd:cd11032 169 LEERRRNPRD-------------DLISRLVEAEVDGER-LTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAAR 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 345 CRKEIQSLLGdgtsitwndldkmpyttmCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWP 424
Cdd:cd11032 235 LRADPSLIPG------------------AIEEVLRYRPPVQRTARVTTEDVEL-GGVTIPAGQLVIAWLASANRDERQFE 295

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86198312 425 NPEVFDPSRfapGSSRHshsfLPFSGGARNCIGKQFAMNELKVAVALTLLRFE-LLPDPTRVPIPIP 490
Cdd:cd11032 296 DPDTFDIDR---NPNPH----LSFGHGIHFCLGAPLARLEARIALEALLDRFPrIRVDPDVPLELID 355
PLN02500 PLN02500
cytochrome P450 90B1
 315-476 2.99e-12

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 68.74  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  315 TFMFEGHDTTASGISWIFYALATNPEHQQRCRKE------IQSLLGDgTSITWNDLDKMPYTTMCIKEALRIYPPVPSVS 388
Cdd:PLN02500 286 SLLFAGHETSSVAIALAIFFLQGCPKAVQELREEhleiarAKKQSGE-SELNWEDYKKMEFTQCVINETLRLGNVVRFLH 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  389 RELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRF---------APGSSRHSHSFLPFSGGARNCIGKQ 459
Cdd:PLN02500 365 RKALKDVRY-KGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWqqnnnrggsSGSSSATTNNFMPFGGGPRLCAGSE 443

                        170
                 ....*....|....*..
gi 86198312  460 FAMNELKVAVALTLLRF 476
Cdd:PLN02500 444 LAKLEMAVFIHHLVLNF 460
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 330-488 4.07e-10

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: 62.00  E-value: 4.07e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 330 WIFYALATNPEHQQRCRKEIQSLL----------GDGTSITWNDLDKMPYTTMCIKEALRIyPPVPSVSRELSSPVTF-- 397
Cdd:cd20633 246 WLLLYLLKHPEAMKAVREEVEQVLketgqevkpgGPLINLTRDMLLKTPVLDSAVEETLRL-TAAPVLIRAVVQDMTLkm 324

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 398 PDGR--SLPKGIHVMLS-FYGLHHNPTVWPNPEVFDPSRF-APGSSRHS----------HSFLPFSGGARNCIGKQFAMN 463
Cdd:cd20633 325 ANGReyALRKGDRLALFpYLAVQMDPEIHPEPHTFKYDRFlNPDGGKKKdfykngkklkYYNMPWGAGVSICPGRFFAVN 404

                       170       180
                ....*....|....*....|....*.
gi 86198312 464 ELKVAVALTLLRFEL-LPDPtRVPIP 488
Cdd:cd20633 405 EMKQFVFLMLTYFDLeLVNP-DEEIP 429
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 293-469 5.95e-10

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: 60.83  E-value: 5.95e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 293 LLFARMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRkeiqsllgdgtsitwNDLDKMPyttM 372
Cdd:cd11079 168 RLLRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYLARHPELQARLR---------------ANPALLP---A 229

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 373 CIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPsrfapgsSRHSHSFLPFSGGA 452
Cdd:cd11079 230 AIDEILRLDDPFVANRRITTRDVEL-GGRTIPAGSRVTLNWASANRDERVFGDPDEFDP-------DRHAADNLVYGRGI 301

                       170
                ....*....|....*..
gi 86198312 453 RNCIGKQFAMNELKVAV 469
Cdd:cd11079 302 HVCPGAPLARLELRILL 318
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 331-479 9.33e-10

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: 60.74  E-value: 9.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 331 IFYALAT-NPEHQQRCRKEIQSLLGDGTSITWNDLDKMPYTTMCIKEALRIYPPVPSVS------RELSSpvtfpDGRSL 403
Cdd:cd11071 248 LLARLGLaGEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPLQYgrarkdFVIES-----HDASY 322

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 404 P--KGIHVMLSFYGLHHNPTVWPNPEVFDPSRF--APGS-------SRHSHSFLPfSGGARNCIGKQFAMNELKVAVALT 472
Cdd:cd11071 323 KikKGELLVGYQPLATRDPKVFDNPDEFVPDRFmgEEGKllkhliwSNGPETEEP-TPDNKQCPGKDLVVLLARLFVAEL 401


                ....*..
gi 86198312 473 LLRFELL 479
Cdd:cd11071 402 FLRYDTF 408
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 263-461 1.12e-09

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 60.52  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  263 QVIKSRRIQLQDEEELEKLKKKrrlDFLDILLfarMENGKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQ 342
Cdd:PLN03141 212 KIIEEKRRAMKNKEEDETGIPK---DVVDVLL---RDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVAL 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  343 QRCRKE---IQSLLGD-GTSITWNDLDKMPYTTMCIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHH 418
Cdd:PLN03141 286 QQLTEEnmkLKRLKADtGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEI-KGYLIPKGWCVLAYFRSVHL 364

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 86198312  419 NPTVWPNPEVFDPSRFAPGSSRHShSFLPFSGGARNCIGKQFA 461
Cdd:PLN03141 365 DEENYDNPYQFNPWRWQEKDMNNS-SFTPFGGGQRLCPGLDLA 406
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 376-504 1.33e-09

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 60.05  E-value: 1.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 376 EALRIYPPVPSVSRELSSPVTFPDG----RSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRfaPgssrhSHSFLPFSGG 451
Cdd:cd20612 246 EALRLNPIAPGLYRRATTDTTVADGggrtVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR--P-----LESYIHFGHG 318

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 86198312 452 ARNCIGKQFAMnelkVAVALTLLRFELLPDPTRVPIPIPRIVLKSKNGIHLHL 504
Cdd:cd20612 319 PHQCLGEEIAR----AALTEMLRVVLRLPNLRRAPGPQGELKKIPRGGFKAYL 367
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
 374-458 8.55e-09

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: 57.42  E-value: 8.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 374 IKEALRIYPPVPSVSRelsspVTFPDGRSLPKGIHVMLSfyGLHHNPTVW-PNPEVFDPSRFAPGSSRHSHSFLPFSGGA 452
Cdd:cd20626 262 VKEALRLYPPTRRIYR-----AFQRPGSSKPEIIAADIE--ACHRSESIWgPDALEFNPSRWSKLTPTQKEAFLPFGSGP 334


                ....*.
gi 86198312 453 RNCIGK 458
Cdd:cd20626 335 FRCPAK 340
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
 330-486 2.51e-08

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: 56.31  E-value: 2.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 330 WIFYALATNPEHQQRCRKEIQSLL-------GDGTSITWNDLDKMPYTTMCIKEALRIyPPVPSVSRELSSPVTFP--DG 400
Cdd:cd20634 243 WLLLFLLKHPEAMAAVRGEIQRIKhqrgqpvSQTLTINQELLDNTPVFDSVLSETLRL-TAAPFITREVLQDMKLRlaDG 321

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 401 R--SLPKGIHVML-SFYGLHHNPTVWPNPEVFDPSRF--APGS---------SRHSHSFLPFSGGARNCIGKQFAMNELK 466
Cdd:cd20634 322 QeyNLRRGDRLCLfPFLSPQMDPEIHQEPEVFKYDRFlnADGTekkdfykngKRLKYYNMPWGAGDNVCIGRHFAVNSIK 401

                       170       180
                ....*....|....*....|..
gi 86198312 467 VAVALTLLRFEL-LPDP-TRVP 486
Cdd:cd20634 402 QFVFLILTHFDVeLKDPeAEIP 423
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 288-501 7.57e-07

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 51.37  E-value: 7.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 288 DFLDILLFARMENGKsLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRkeiqsllgdgtsitwNDLDKM 367
Cdd:cd11030 189 DLLSRLVAEHGAPGE-LTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPEQLAALR---------------ADPSLV 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 368 PyttMCIKEALRIYPPVP-SVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRfapGSSRHshsfL 446
Cdd:cd11030 253 P---GAVEELLRYLSIVQdGLPRVATEDVEI-GGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR---PARRH----L 321

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 447 PFSGGARNCIGKQFAMNELKVAVAlTLLRfellpdptRVP-----IPIPRIVLKSKNGIH 501
Cdd:cd11030 322 AFGHGVHQCLGQNLARLELEIALP-TLFR--------RFPglrlaVPAEELPFRPDSLVY 372
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
 374-485 1.03e-06

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: 50.57  E-value: 1.03e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 374 IKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRfAPGSSRHshsflpFSGGAR 453
Cdd:cd11036 225 VAETLRYDPPVRLERRFAAEDLEL-AGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR-PTARSAH------FGLGRH 296

                        90       100       110
                ....*....|....*....|....*....|..
gi 86198312 454 NCIGKQFAMneLKVAVALTLLRfELLPDPTRV 485
Cdd:cd11036 297 ACLGAALAR--AAAAAALRALA-ARFPGLRAA 325
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
 294-481 1.30e-04

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 44.42  E-value: 1.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 294 LFARMEN-GKSLSDKDLRAEVDTFMFEGHDTTASGISWIFYALATNPEHQQRCRKEIQSLLgdgtsitwndldkmpyttM 372
Cdd:cd11039 187 LLSVMLNaGMPMSLEQIRANIKVAIGGGLNEPRDAIAGTCWGLLSNPEQLAEVMAGDVHWL------------------R 248

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312 373 CIKEALRIYPPVPSVSRELSSPVTFpDGRSLPKGIHVMLSFYGLHHNPTVWPNPEVFDPSRfapGSSRHshsfLPFSGGA 452
Cdd:cd11039 249 AFEEGLRWISPIGMSPRRVAEDFEI-RGVTLPAGDRVFLMFGSANRDEARFENPDRFDVFR---PKSPH----VSFGAGP 320

                       170       180
                ....*....|....*....|....*....
gi 86198312 453 RNCIGKQFAmNELKVAVALTLLrFELLPD 481
Cdd:cd11039 321 HFCAGAWAS-RQMVGEIALPEL-FRRLPN 347
PLN02648 PLN02648
allene oxide synthase
 331-436 3.91e-04

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 43.00  E-value: 3.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86198312  331 IFYALAT-NPEHQQRCRKEIQSLLGD-GTSITWNDLDKMPYTTMCIKEALRIYPPVPSV---SRE---LSSpvtfPDGR- 401
Cdd:PLN02648 295 LLKWVGRaGEELQARLAEEVRSAVKAgGGGVTFAALEKMPLVKSVVYEALRIEPPVPFQygrAREdfvIES----HDAAf 370

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 86198312  402 SLPKGihVMLsfYGlhHNPTVWPNPEVFD-PSRFAP 436
Cdd:PLN02648 371 EIKKG--EML--FG--YQPLVTRDPKVFDrPEEFVP 400
 
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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