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Conserved domains on  [gi|19921820|ref|NP_610380|]
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cytochrome P450 4ad1, isoform A [Drosophila melanogaster]

Protein Classification

cytochrome P450( domain architecture ID 15334963)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
73-511 6.10e-167

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: 478.94  E-value: 6.10e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  73 FRSLVFLQYHMMLSDPAEIQNILSSSSLLYKEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRT 152
Cdd:cd20628   4 FRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFNEN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 153 GGQFVQKLDVLSDTqEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLT 232
Cdd:cd20628  84 SKILVEKLKKKAGG-GEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEIILKRIFSPWLRFDFIFRLT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 233 SYYMKQRRALSLLRSELNRIISQRRHQLAAE-----NTCQQGQPINKPFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGH 307
Cdd:cd20628 163 SLGKEQRKALKVLHDFTNKVIKERREELKAEkrnseEDDEFGKKKRKAFLDLLLEAHEDGGPLTDEDIREEVDTFMFAGH 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 308 DPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAgEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDING 387
Cdd:cd20628 243 DTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDR-RPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDG 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 388 TKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFEnPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd20628 322 YTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFL-PENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFR 400
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 19921820 468 ILPAVdglppgindhSREDCVPQSEydpvlnirVTLKSENGIQI 511
Cdd:cd20628 401 VLPVP----------PGEDLKLIAE--------IVLRSKNGIRV 426
 
Name Accession Description Interval E-value
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
73-511 6.10e-167

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: 478.94  E-value: 6.10e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  73 FRSLVFLQYHMMLSDPAEIQNILSSSSLLYKEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRT 152
Cdd:cd20628   4 FRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFNEN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 153 GGQFVQKLDVLSDTqEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLT 232
Cdd:cd20628  84 SKILVEKLKKKAGG-GEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEIILKRIFSPWLRFDFIFRLT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 233 SYYMKQRRALSLLRSELNRIISQRRHQLAAE-----NTCQQGQPINKPFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGH 307
Cdd:cd20628 163 SLGKEQRKALKVLHDFTNKVIKERREELKAEkrnseEDDEFGKKKRKAFLDLLLEAHEDGGPLTDEDIREEVDTFMFAGH 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 308 DPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAgEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDING 387
Cdd:cd20628 243 DTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDR-RPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDG 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 388 TKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFEnPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd20628 322 YTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFL-PENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFR 400
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 19921820 468 ILPAVdglppgindhSREDCVPQSEydpvlnirVTLKSENGIQI 511
Cdd:cd20628 401 VLPVP----------PGEDLKLIAE--------IVLRSKNGIRV 426
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
36-477 2.07e-83

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: 266.07  E-value: 2.07e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820    36 PGPTPYPFVGNLFQFGLKpaEYPKKVLQYCRKYDFQGFRSLVFLQYHMMLSDPAEIQNIL-----SSSSLLYKEHLYSFL 110
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRK--GNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLikkgeEFSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   111 RPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATG 190
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   191 QDSSSLNGET-SDLHGAIKDLCDVVQERTFSIVKRFDALFR-LTSYYMKQRRALSLLRSELNRIISQRRHQLaaentcQQ 268
Cdd:pfam00067 160 ERFGSLEDPKfLELVKAVQELSSLLSSPSPQLLDLFPILKYfPGPHGRKLKRARKKIKDLLDKLIEERRETL------DS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   269 GQPINKPFLDVLLTAKL--DGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfaGE 346
Cdd:pfam00067 234 AKKSPRDFLDALLLAKEeeDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDK--RS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   347 ADLARLDQMHYLELIIRETLRLYPSVP-LIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPT 425
Cdd:pfam00067 312 PTYDDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDEN 391
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19921820   426 GNVGIEaFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF--EILPAVDGLPP 477
Cdd:pfam00067 392 GKFRKS-FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFevELPPGTDPPDI 444
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
73-477 1.40e-52

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: 183.17  E-value: 1.40e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  73 FRSLVFLQYHMMLSDPAEIQNILSSSSLLYKEH-LYSFLRP--WLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVV 149
Cdd:COG2124  35 FRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGgLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 150 HRTGGQFVQKLDvlsdTQEVFDAQELVAKCTLDIVCenatgqdsSSLNGETSDLHGAIKDLCDVVqertfsivkrFDALF 229
Cdd:COG2124 115 REIADELLDRLA----ARGPVDLVEEFARPLPVIVI--------CELLGVPEEDRDRLRRWSDAL----------LDALG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 230 RLTSYYMKQ-RRALSLLRSELNRIISQRRHQLAAEntcqqgqpinkpFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHD 308
Cdd:COG2124 173 PLPPERRRRaRRARAELDAYLRELIAERRAEPGDD------------LLSALLAARDDGERLSDEELRDELLLLLLAGHE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 309 PIAAAISFTLYTLSRHSEIQQKAAEEQRrifgenfageadlarldqmhYLELIIRETLRLYPSVPLIARTNRNPIDINGT 388
Cdd:COG2124 241 TTANALAWALYALLRHPEQLARLRAEPE--------------------LLPAAVEETLRLYPPVPLLPRTATEDVELGGV 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 389 KVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERfenptgnvgiEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI 468
Cdd:COG2124 301 TIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPD 370

                ....*....
gi 19921820 469 LPAVDGLPP 477
Cdd:COG2124 371 LRLAPPEEL 379
PLN02290 PLN02290
cytokinin trans-hydroxylase
83-514 7.03e-34

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 134.17  E-value: 7.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   83 MMLSDPAEIQNILSS------SSLLYKEHLYSFLrpwlGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQF 156
Cdd:PLN02290 107 LCLTETELIKELLTKyntvtgKSWLQQQGTKHFI----GRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQM 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  157 VQKL-DVLSDTQEVFDAQELVAKCTLDIVCEnaTGQDSSSLNGETsdlhgaIKDLCDVVQERTFSIVKRFdaLFRLTSYY 235
Cdd:PLN02290 183 LQSLqKAVESGQTEVEIGEYMTRLTADIISR--TEFDSSYEKGKQ------IFHLLTVLQRLCAQATRHL--CFPGSRFF 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  236 -MKQRRALSLLRSELNRI---ISQRRHQLAAEN-TCQQGQPINKPFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPI 310
Cdd:PLN02290 253 pSKYNREIKSLKGEVERLlmeIIQSRRDCVEIGrSSSYGDDLLGMLLNEMEKKRSNGFNLNLQLIMDECKTFFFAGHETT 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  311 AAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLARLDqmhYLELIIRETLRLYPSVPLIARTNRNPIDINGTKV 390
Cdd:PLN02290 333 ALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVDHLSKLT---LLNMVINESLRLYPPATLLPRMAFEDIKLGDLHI 409
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  391 AKCTTVIMCLIAMGYNEKYF-DDPCTFRPERFenpTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIl 469
Cdd:PLN02290 410 PKGLSIWIPVLAIHHSEELWgKDANEFNPDRF---AGRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSF- 485
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 19921820  470 pavdglppGINDHSRedcvpqseYDPVlnIRVTLKSENGIQIRLR 514
Cdd:PLN02290 486 --------TISDNYR--------HAPV--VVLTIKPKYGVQVCLK 512
 
Name Accession Description Interval E-value
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
73-511 6.10e-167

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: 478.94  E-value: 6.10e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  73 FRSLVFLQYHMMLSDPAEIQNILSSSSLLYKEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRT 152
Cdd:cd20628   4 FRLWIGPKPYVVVTNPEDIEVILSSSKLITKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFNEN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 153 GGQFVQKLDVLSDTqEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLT 232
Cdd:cd20628  84 SKILVEKLKKKAGG-GEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEIILKRIFSPWLRFDFIFRLT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 233 SYYMKQRRALSLLRSELNRIISQRRHQLAAE-----NTCQQGQPINKPFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGH 307
Cdd:cd20628 163 SLGKEQRKALKVLHDFTNKVIKERREELKAEkrnseEDDEFGKKKRKAFLDLLLEAHEDGGPLTDEDIREEVDTFMFAGH 242
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 308 DPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAgEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDING 387
Cdd:cd20628 243 DTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDDR-RPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKLDG 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 388 TKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFEnPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd20628 322 YTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFL-PENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFR 400
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 19921820 468 ILPAVdglppgindhSREDCVPQSEydpvlnirVTLKSENGIQI 511
Cdd:cd20628 401 VLPVP----------PGEDLKLIAE--------IVLRSKNGIRV 426
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
83-512 3.86e-100

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: 307.95  E-value: 3.86e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  83 MMLSDPAEIQNILSSSSLlYKEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDV 162
Cdd:cd20659  15 LVLNHPDTIKAVLKTSEP-KDRDSYRFLKPWLGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVYNECTDILLEKWSK 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 163 LSDTQEVFDAQELVAKCTLDIVCENATGQDSS-SLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSYYMKQRRA 241
Cdd:cd20659  94 LAETGESVEVFEDISLLTLDIILRCAFSYKSNcQQTGKNHPYVAAVHELSRLVMERFLNPLLHFDWIYYLTPEGRRFKKA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 242 LSLLRSELNRIISQRRHQLAAENTCQQGQPINKPFLDVLLTAK-LDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYT 320
Cdd:cd20659 174 CDYVHKFAEEIIKKRRKELEDNKDEALSKRKYLDFLDILLTARdEDGKGLTDEEIRDEVDTFLFAGHDTTASGISWTLYS 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 321 LSRHSEIQQKAAEEQRRIFGenfaGEADL--ARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIM 398
Cdd:cd20659 254 LAKHPEHQQKCREEVDEVLG----DRDDIewDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITIDGVTLPAGTLIAI 329
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 399 CLIAMGYNEKYFDDPCTFRPERFeNPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPavdglppg 478
Cdd:cd20659 330 NIYALHHNPTVWEDPEEFDPERF-LPENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELSV-------- 400
                       410       420       430
                ....*....|....*....|....*....|....
gi 19921820 479 indhsredcVPQSEYDPVlnIRVTLKSENGIQIR 512
Cdd:cd20659 401 ---------DPNHPVEPK--PGLVLRSKNGIKLK 423
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
84-511 1.55e-97

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: 301.49  E-value: 1.55e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  84 MLSDPAEIQNILSSSSLLYKEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVL 163
Cdd:cd20660  15 VLYSAETVEVILSSSKHIDKSFEYDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDFLDVFNEQSEILVKKLKKE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 164 SDTqEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSYYMKQRRALS 243
Cdd:cd20660  95 VGK-EEFDIFPYITLCALDIICETAMGKSVNAQQNSDSEYVKAVYRMSELVQKRQKNPWLWPDFIYSLTPDGREHKKCLK 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 244 LLRSELNRIISQRRHQLAA----ENTCQQGQPINK----PFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAIS 315
Cdd:cd20660 174 ILHGFTNKVIQERKAELQKsleeEEEDDEDADIGKrkrlAFLDLLLEASEEGTKLSDEDIREEVDTFMFEGHDTTAAAIN 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 316 FTLYTLSRHSEIQQKAAEEQRRIFGENfAGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTT 395
Cdd:cd20660 254 WALYLIGSHPEVQEKVHEELDRIFGDS-DRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIPKGTT 332
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 396 VIMCLIAMGYNEKYFDDPCTFRPERF--ENptgNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVd 473
Cdd:cd20660 333 VLVLTYALHRDPRQFPDPEKFDPDRFlpEN---SAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESVQ- 408
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 19921820 474 glppgindhSREDCVPQSEydpvlnirVTLKSENGIQI 511
Cdd:cd20660 409 ---------KREDLKPAGE--------LILRPVDGIRV 429
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
36-477 2.07e-83

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: 266.07  E-value: 2.07e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820    36 PGPTPYPFVGNLFQFGLKpaEYPKKVLQYCRKYDFQGFRSLVFLQYHMMLSDPAEIQNIL-----SSSSLLYKEHLYSFL 110
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRK--GNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLikkgeEFSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   111 RPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATG 190
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   191 QDSSSLNGET-SDLHGAIKDLCDVVQERTFSIVKRFDALFR-LTSYYMKQRRALSLLRSELNRIISQRRHQLaaentcQQ 268
Cdd:pfam00067 160 ERFGSLEDPKfLELVKAVQELSSLLSSPSPQLLDLFPILKYfPGPHGRKLKRARKKIKDLLDKLIEERRETL------DS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   269 GQPINKPFLDVLLTAKL--DGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfaGE 346
Cdd:pfam00067 234 AKKSPRDFLDALLLAKEeeDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDK--RS 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   347 ADLARLDQMHYLELIIRETLRLYPSVP-LIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPT 425
Cdd:pfam00067 312 PTYDDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDEN 391
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19921820   426 GNVGIEaFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF--EILPAVDGLPP 477
Cdd:pfam00067 392 GKFRKS-FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFevELPPGTDPPDI 444
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
91-511 9.41e-81

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: 258.54  E-value: 9.41e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  91 IQNILSSSSLLYKEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDtQEVF 170
Cdd:cd20680  33 VEVILSSSKHIDKSYLYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFHFTILSDFLEVMNEQSNILVEKLEKHVD-GEAF 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 171 DAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSYYMKQRRALSLLRSELN 250
Cdd:cd20680 112 NCFFDITLCALDIICETAMGKKIGAQSNKDSEYVQAVYRMSDIIQRRQKMPWLWLDLWYLMFKEGKEHNKNLKILHTFTD 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 251 RIISQRRHQLAAENTCQ-------QGQPINKPFLDVLLTAKLD-GKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLS 322
Cdd:cd20680 192 NVIAERAEEMKAEEDKTgdsdgesPSKKKRKAFLDMLLSVTDEeGNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLG 271
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 323 RHSEIQQKAAEEQRRIFG--ENFAGEADLARLdqmHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCL 400
Cdd:cd20680 272 SHPEVQRKVHKELDEVFGksDRPVTMEDLKKL---RYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIP 348
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 401 IAMGYNEKYFDDPCTFRPERF--ENPTGNvgiEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILpavdglppg 478
Cdd:cd20680 349 YALHRDPRYFPEPEEFRPERFfpENSSGR---HPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVE--------- 416
                       410       420       430
                ....*....|....*....|....*....|...
gi 19921820 479 iNDHSREDCVPQSEydpvlnirVTLKSENGIQI 511
Cdd:cd20680 417 -ANQKREELGLVGE--------LILRPQNGIWI 440
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
81-473 2.68e-80

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: 257.20  E-value: 2.68e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  81 YHMMLSDPAEIQNILSSSSLLYKEH--LYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQ 158
Cdd:cd11069  14 ERLLVTDPKALKHILVTNSYDFEKPpaFRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKELYPIFWSKAEELVD 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 159 KLDVL----SDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSY 234
Cdd:cd11069  94 KLEEEieesGDESISIDVLEWLSRATLDIIGLAGFGYDFDSLENPDNELAEAYRRLFEPTLLGSLLFILLLFLPRWLVRI 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 235 YM-----KQRRALSLLRSELNRIISQRRHQLAAENTCQqgqpiNKPFLDVLLTA--KLDGKVLKEREIIEEVSTFIFTGH 307
Cdd:cd11069 174 LPwkanrEIRRAKDVLRRLAREIIREKKAALLEGKDDS-----GKDILSILLRAndFADDERLSDEELIDQILTFLAAGH 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 308 DPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDING 387
Cdd:cd11069 249 ETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKDTVIKG 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 388 TKVAKCTTVIMCLIAMGYN-EKYFDDPCTFRPERFENPTGNVGIEAFKS----VPFSAGPRRCIAEKFAMYQMKALLSQL 462
Cdd:cd11069 329 VPIPKGTVVLIPPAAINRSpEIWGPDAEEFNPERWLEPDGAASPGGAGSnyalLTFLHGPRSCIGKKFALAEMKVLLAAL 408
                       410
                ....*....|.
gi 19921820 463 LRRFEILPAVD 473
Cdd:cd11069 409 VSRFEFELDPD 419
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
104-512 2.94e-75

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: 244.11  E-value: 2.94e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 104 EHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDI 183
Cdd:cd20678  46 QGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYDILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDT 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 184 VCENATG-QDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSYYMKQRRALSLLRSELNRIISQRRHQLAA 262
Cdd:cd20678 126 IMKCAFShQGSCQLDGRSNSYIQAVSDLSNLIFQRLRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQD 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 263 ENTCQQGQpiNK---PFLDVLLTAKL-DGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRI 338
Cdd:cd20678 206 EGELEKIK--KKrhlDFLDILLFAKDeNGKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREI 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 339 FGENFAGEADlaRLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDI-NGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFR 417
Cdd:cd20678 284 LGDGDSITWE--HLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFpDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFD 361
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 418 PERF--ENPtgnVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPavdglppginDHSREdcvpqseydP 495
Cdd:cd20678 362 PLRFspENS---SKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFELLP----------DPTRI---------P 419
                       410
                ....*....|....*..
gi 19921820 496 VLNIRVTLKSENGIQIR 512
Cdd:cd20678 420 IPIPQLVLKSKNGIHLY 436
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
82-468 1.90e-72

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: 236.34  E-value: 1.90e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  82 HMMLSDPAEIQNILSSSSLLYKEHLYSFLrpWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLD 161
Cdd:cd11057  13 FVITSDPEIVQVVLNSPHCLNKSFFYDFF--RLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIFNEEAQKLVQRLD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 162 VLSDTQEvFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSYYMKQRRA 241
Cdd:cd11057  91 TYVGGGE-FDILPDLSRCTLEMICQTTLGSDVNDESDGNEEYLESYERLFELIAKRVLNPWLHPEFIYRLTGDYKEEQKA 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 242 LSLLRSELNRIISQRRHQLAAENTCQQGQP---INKP--FLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISF 316
Cdd:cd11057 170 RKILRAFSEKIIEKKLQEVELESNLDSEEDeenGRKPqiFIDQLLELARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAY 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 317 TLYTLSRHSEIQQKAAEEQRRIFGENFAgEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDI-NGTKVAKCTT 395
Cdd:cd11057 250 TLLLLAMHPEVQEKVYEEIMEVFPDDGQ-FITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLsNGVVIPKGTT 328
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921820 396 VIMCLIAMGYNEKYF-DDPCTFRPERF--ENPTGNvgiEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI 468
Cdd:cd11057 329 IVIDIFNMHRRKDIWgPDADQFDPDNFlpERSAQR---HPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRL 401
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
84-474 1.65e-71

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: 232.79  E-value: 1.65e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  84 MLSDPAEIQNILSSSSLLYKEHLYSF--LRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLD 161
Cdd:cd00302  15 VVSDPELVREVLRDPRDFSSDAGPGLpaLGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVIREIARELLDRLA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 162 VLSDTQevFDAQELVAKCTLDIVCENATGQDsssLNGETSDLHGAIKDLCDVVQERTFSIVKRFDalfrltsyYMKQRRA 241
Cdd:cd00302  95 AGGEVG--DDVADLAQPLALDVIARLLGGPD---LGEDLEELAELLEALLKLLGPRLLRPLPSPR--------LRRLRRA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 242 LSLLRSELNRIISQRRhqlaaentcqqgQPINKPFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTL 321
Cdd:cd00302 162 RARLRDYLEELIARRR------------AEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLL 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 322 SRHSEIQQKAAEEQRRIFGENfageaDLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLI 401
Cdd:cd00302 230 ARHPEVQERLRAEIDAVLGDG-----TPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLY 304
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921820 402 AMGYNEKYFDDPCTFRPERFENPTGNvgiEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDG 474
Cdd:cd00302 305 AAHRDPEVFPDPDEFDPERFLPEREE---PRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDE 374
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
84-511 9.30e-71

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: 231.31  E-value: 9.30e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  84 MLSDPAEIQNILSSSSLLY-KEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDV 162
Cdd:cd20620  15 LVTHPDHIQHVLVTNARNYvKGGVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAMVEATAALLDRWEA 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 163 LSDTQEVFDAQELVAkCTLDIVCENATGQDssslngeTSDLHGAIKDLCDVVQERTFSIVKRFDALFR--LTSYYMKQRR 240
Cdd:cd20620  95 GARRGPVDVHAEMMR-LTLRIVAKTLFGTD-------VEGEADEIGDALDVALEYAARRMLSPFLLPLwlPTPANRRFRR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 241 ALSLLRSELNRIISQRRHQLAAENtcqqgqpinkPFLDVLLTAKL--DGKVLKEREIIEEVSTFIFTGHDPIAAAISFTL 318
Cdd:cd20620 167 ARRRLDEVIYRLIAERRAAPADGG----------DLLSMLLAARDeeTGEPMSDQQLRDEVMTLFLAGHETTANALSWTW 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 319 YTLSRHSEIQQKAAEEQRRIFGENFAGEADLARLDqmhYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIM 398
Cdd:cd20620 237 YLLAQHPEVAARLRAEVDRVLGGRPPTAEDLPQLP---YTEMVLQESLRLYPPAWIIGREAVEDDEIGGYRIPAGSTVLI 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 399 CLIAMGYNEKYFDDPCTFRPERFEnPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILpavdgLPPG 478
Cdd:cd20620 314 SPYVTHRDPRFWPDPEAFDPERFT-PEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLR-----LVPG 387
                       410       420       430
                ....*....|....*....|....*....|...
gi 19921820 479 indhsredcvpqseYDPVLNIRVTLKSENGIQI 511
Cdd:cd20620 388 --------------QPVEPEPLITLRPKNGVRM 406
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
58-468 2.61e-62

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: 209.68  E-value: 2.61e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  58 PKKVLQYCRKYdfqG--FRSLVFLQYHMMLSDPAEIQNILSSSSLLYKEHLYSFL-----RPWLGDGLLTSSG-ARWLKH 129
Cdd:cd20613   1 HDLLLEWAKEY---GpvFVFWILHRPIVVVSDPEAVKEVLITLNLPKPPRVYSRLaflfgERFLGNGLVTEVDhEKWKKR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 130 QKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKD 209
Cdd:cd20613  78 RAILNPAFHRKYLKNLMDEFNESADLLVEKLSKKADGKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDPDSPFPKAISL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 210 LCDVVQERTFSIVKRFDALFRltSYYMKQRRALSLLRSELNRIISQRRHQLAAENTCQQgqpinkpflDVL---LTAKLD 286
Cdd:cd20613 158 VLEGIQESFRNPLLKYNPSKR--KYRREVREAIKFLRETGRECIEERLEALKRGEEVPN---------DILthiLKASEE 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 287 GKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGE-NFAGEADLARLDqmhYLELIIRET 365
Cdd:cd20613 227 EPDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSkQYVEYEDLGKLE---YLSQVLKET 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 366 LRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFeNPTGNVGIEAFKSVPFSAGPRRC 445
Cdd:cd20613 304 LRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERF-SPEAPEKIPSYAYFPFSLGPRSC 382
                       410       420
                ....*....|....*....|...
gi 19921820 446 IAEKFAMYQMKALLSQLLRRFEI 468
Cdd:cd20613 383 IGQQFAQIEAKVILAKLLQNFKF 405
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
85-470 6.99e-62

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: 209.16  E-value: 6.99e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  85 LSDPAEIQNILSSSSLLY-KEHL-YSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVvhrtggqFVQKLDV 162
Cdd:cd20679  28 LFHPDYIRPVLLASAAVApKDELfYGFLKPWLGDGLLLSSGDKWSRHRRLLTPAFHFNILKPYVKI-------FNQSTNI 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 163 L--------SDTQEVFDAQELVAKCTLDIVCENATGQDSSSlNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSY 234
Cdd:cd20679 101 MhakwrrlaSEGSARLDMFEHISLMTLDSLQKCVFSFDSNC-QEKPSEYIAAILELSALVVKRQQQLLLHLDFLYYLTAD 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 235 YMKQRRALSLLRSELNRIISQRRHQL----AAENTCQQGQPINKPFLDVLLTAK-LDGKVLKEREIIEEVSTFIFTGHDP 309
Cdd:cd20679 180 GRRFRRACRLVHDFTDAVIQERRRTLpsqgVDDFLKAKAKSKTLDFIDVLLLSKdEDGKELSDEDIRAEADTFMFEGHDT 259
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 310 IAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLARLDQMHYLELIIRETLRLYPSVPLIARtnRNPIDI---N 386
Cdd:cd20679 260 TASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEIEWDDLAQLPFLTMCIKESLRLHPPVTAISR--CCTQDIvlpD 337
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 387 GTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERF--ENPTGNVGIeAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLR 464
Cdd:cd20679 338 GRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFdpENSQGRSPL-AF--IPFSAGPRNCIGQTFAMAEMKVVLALTLL 414

                ....*.
gi 19921820 465 RFEILP 470
Cdd:cd20679 415 RFRVLP 420
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
86-509 1.79e-55

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: 191.64  E-value: 1.79e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  86 SDPAEIQNIL-SSSSLLYKEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLS 164
Cdd:cd11055  19 SDPEMIKEILvKEFSNFTNRPLFILLDEPFDSSLLFLKGERWKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 165 DTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLT--SYYMKQRRAL 242
Cdd:cd11055  99 ETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKAAKKIFRNSIIRLFLLLLLFPLRLFLFllFPFVFGFKSF 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 243 SLLRSELNRIISQRRhqlaaentcQQGQPINKPFLDVLLTAKLDG-----KVLKEREIIEEVSTFIFTGHDPIAAAISFT 317
Cdd:cd11055 179 SFLEDVVKKIIEQRR---------KNKSSRRKDLLQLMLDAQDSDedvskKKLTDDEIVAQSFIFLLAGYETTSNTLSFA 249
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 318 LYTLSRHSEIQQKAAEEQRRIFGENfaGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVI 397
Cdd:cd11055 250 SYLLATNPDVQEKLIEEIDEVLPDD--GSPTYDTVSKLKYLDMVINETLRLYPPAFFISRECKEDCTINGVFIPKGVDVV 327
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 398 MCLIAMGYNEKYFDDPCTFRPERFENPTgNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPavdglpp 477
Cdd:cd11055 328 IPVYAIHHDPEFWPDPEKFDPERFSPEN-KAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVP------- 399
                       410       420       430
                ....*....|....*....|....*....|..
gi 19921820 478 gindhsredcVPQSEYDPVLNIRVTLKSENGI 509
Cdd:cd11055 400 ----------CKETEIPLKLVGGATLSPKNGI 421
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
83-479 8.88e-55

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: 190.27  E-value: 8.88e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  83 MMLSDPAEIQNILSSSSLLYKEH--LYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKL 160
Cdd:cd11046  24 LVISDPAIAKHVLRSNAFSYDKKglLAEILEPIMGKGLIPADGEIWKKRRRALVPALHKDYLEMMVRVFGRCSERLMEKL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 161 DVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETS---DLHGAIKDLCdvvQERTFSI-VKRFDALFRLTSYYM 236
Cdd:cd11046 104 DAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVTEESPvikAVYLPLVEAE---HRSVWEPpYWDIPAALFIVPRQR 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 237 KQRRALSLLRSELNRIISQR---RHQLAAENTCQQGQPINKP-FLDVLLTAKldGKVLKEREIIEEVSTFIFTGHDPIAA 312
Cdd:cd11046 181 KFLRDLKLLNDTLDDLIRKRkemRQEEDIELQQEDYLNEDDPsLLRFLVDMR--DEDVDSKQLRDDLMTMLIAGHETTAA 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 313 AISFTLYTLSRHSEIQQKAAEEQRRIFGENFAgeADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNP--IDINGTKV 390
Cdd:cd11046 259 VLTWTLYELSQNPELMAKVQAEVDAVLGDRLP--PTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDdkLPGGGVKV 336
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 391 AKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVG---IEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd11046 337 PAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPnevIDDFAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFD 416
                       410
                ....*....|..
gi 19921820 468 ILPAVDGLPPGI 479
Cdd:cd11046 417 FELDVGPRHVGM 428
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
85-478 2.40e-54

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: 188.68  E-value: 2.40e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  85 LSDPAEIQNILSSSSLLYK--EHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDV 162
Cdd:cd11083  16 ISDPELIREVLRRRPDEFRriSSLESVFREMGINGVFSAEGDAWRRQRRLVMPAFSPKHLRYFFPTLRQITERLRERWER 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 163 LSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETsdlHGAIKDLcdvvqERTF-SIVKRFDALFRLTSYYMKQR-- 239
Cdd:cd11083  96 AAAEGEAVDVHKDLMRYTVDVTTSLAFGYDLNTLERGG---DPLQEHL-----ERVFpMLNRRVNAPFPYWRYLRLPAdr 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 240 ---RALSLLRSELNRIISQRRHQLAAEntcQQGQPINKPFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISF 316
Cdd:cd11083 168 aldRALVEVRALVLDIIAAARARLAAN---PALAEAPETLLAMMLAEDDPDARLTDDEIYANVLTLLLAGEDTTANTLAW 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 317 TLYTLSRHSEIQQKAAEEQRRIFGeNFAGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTV 396
Cdd:cd11083 245 MLYYLASRPDVQARVREEVDAVLG-GARVPPLLEALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTPV 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 397 IMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFKS-VPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDGL 475
Cdd:cd11083 324 FLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEPHDPSSlLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPEPAP 403

                ...
gi 19921820 476 PPG 478
Cdd:cd11083 404 AVG 406
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
83-476 4.62e-53

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: 185.49  E-value: 4.62e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  83 MMLSDPAEIQNILSSSSLLYK--EHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFE----RSAIEgylRVVHRTGGQ- 155
Cdd:cd11064  14 IVTADPANVEHILKTNFDNYPkgPEFRDLFFDLLGDGIFNVDGELWKFQRKTASHEFSsralREFME---SVVREKVEKl 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 156 FVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLH--GAIkdlcDVVQErtfSIVKRF---DALFR 230
Cdd:cd11064  91 LVPLLDHAAESGKVVDLQDVLQRFTFDVICKIAFGVDPGSLSPSLPEVPfaKAF----DDASE---AVAKRFivpPWLWK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 231 LTSYYM-----KQRRALSLLRSELNRIISQRRHQLAAENTCQQGQPinkpflDvLLTAKLD-----GKVLKEREIIEEVS 300
Cdd:cd11064 164 LKRWLNigsekKLREAIRVIDDFVYEVISRRREELNSREEENNVRE------D-LLSRFLAseeeeGEPVSDKFLRDIVL 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 301 TFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEA---DLARLDQMHYLELIIRETLRLYPSVPLIAR 377
Cdd:cd11064 237 NFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTTDESrvpTYEELKKLVYLHAALSESLRLYPPVPFDSK 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 378 TNRNPiDI--NGTKVAKCTTVIMCLIAMGYNEKYF-DDPCTFRPERFENPTGN-VGIEAFKSVPFSAGPRRCIAEKFAMY 453
Cdd:cd11064 317 EAVND-DVlpDGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDGGlRPESPYKFPAFNAGPRICLGKDLAYL 395
                       410       420
                ....*....|....*....|...
gi 19921820 454 QMKALLSQLLRRFEILpAVDGLP 476
Cdd:cd11064 396 QMKIVAAAILRRFDFK-VVPGHK 417
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
73-477 1.40e-52

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: 183.17  E-value: 1.40e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  73 FRSLVFLQYHMMLSDPAEIQNILSSSSLLYKEH-LYSFLRP--WLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVV 149
Cdd:COG2124  35 FRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGgLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 150 HRTGGQFVQKLDvlsdTQEVFDAQELVAKCTLDIVCenatgqdsSSLNGETSDLHGAIKDLCDVVqertfsivkrFDALF 229
Cdd:COG2124 115 REIADELLDRLA----ARGPVDLVEEFARPLPVIVI--------CELLGVPEEDRDRLRRWSDAL----------LDALG 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 230 RLTSYYMKQ-RRALSLLRSELNRIISQRRHQLAAEntcqqgqpinkpFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHD 308
Cdd:COG2124 173 PLPPERRRRaRRARAELDAYLRELIAERRAEPGDD------------LLSALLAARDDGERLSDEELRDELLLLLLAGHE 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 309 PIAAAISFTLYTLSRHSEIQQKAAEEQRrifgenfageadlarldqmhYLELIIRETLRLYPSVPLIARTNRNPIDINGT 388
Cdd:COG2124 241 TTANALAWALYALLRHPEQLARLRAEPE--------------------LLPAAVEETLRLYPPVPLLPRTATEDVELGGV 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 389 KVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERfenptgnvgiEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI 468
Cdd:COG2124 301 TIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR----------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPD 370

                ....*....
gi 19921820 469 LPAVDGLPP 477
Cdd:COG2124 371 LRLAPPEEL 379
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
69-474 1.72e-52

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: 183.55  E-value: 1.72e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  69 DFQGFRSLVFLqyhmmlSDPAEIQNILSSSS-LLYKEHLYSFLRPWLGD-GLLTSSGARWLKHQKLYAPAFERSAIEGYl 146
Cdd:cd11053  18 RVPGLGPVVVL------SDPEAIKQIFTADPdVLHPGEGNSLLEPLLGPnSLLLLDGDRHRRRRKLLMPAFHGERLRAY- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 147 rvvhrtGGQFVQKLDVLSDTQ---EVFDAQELVAKCTLDIVCENATGQDSSSlngetsdlhgAIKDLCDVVQertfSIVK 223
Cdd:cd11053  91 ------GELIAEITEREIDRWppgQPFDLRELMQEITLEVILRVVFGVDDGE----------RLQELRRLLP----RLLD 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 224 RFDALFRLTSYYMKQRRALSL------LRSELNRI----ISQRRHQLAAENTcqqgqpinkpflDVL---LTAK-LDGKV 289
Cdd:cd11053 151 LLSSPLASFPALQRDLGPWSPwgrflrARRRIDALiyaeIAERRAEPDAERD------------DILsllLSARdEDGQP 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 290 LKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIfgenfAGEADLARLDQMHYLELIIRETLRLY 369
Cdd:cd11053 219 LSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDAL-----GGDPDPEDIAKLPYLDAVIKETLRLY 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 370 PSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFEnpTGNVGIEAFksVPFSAGPRRCIAEK 449
Cdd:cd11053 294 PVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFL--GRKPSPYEY--LPFGGGVRRCIGAA 369
                       410       420
                ....*....|....*....|....*
gi 19921820 450 FAMYQMKALLSQLLRRFEILPAVDG 474
Cdd:cd11053 370 FALLEMKVVLATLLRRFRLELTDPR 394
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
82-468 2.14e-52

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: 183.31  E-value: 2.14e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  82 HMMLSDPAEIQNILSSSSLLY-KEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKL 160
Cdd:cd11052  24 RLYVTEPELIKELLSKKEGYFgKSPLQPGLKKLLGRGLVMSNGEKWAKHRRIANPAFHGEKLKGMVPAMVESVSDMLERW 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 161 -DVLSDTQEVFDAQELVAKCTLDIVCENATGqdSSSLNGetsdlhGAIKDLCDVVQERTFSIVKR--FDALFRLTSYYMK 237
Cdd:cd11052 104 kKQMGEEGEEVDVFEEFKALTADIISRTAFG--SSYEEG------KEVFKLLRELQKICAQANRDvgIPGSRFLPTKGNK 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 238 QRRALSL-LRSELNRIISQRRHQLAAentcQQGQPINKPFLDVLLTAKLDGKVLKE---REIIEEVSTFIFTGHDPIAAA 313
Cdd:cd11052 176 KIKKLDKeIEDSLLEIIKKREDSLKM----GRGDDYGDDLLGLLLEANQSDDQNKNmtvQEIVDECKTFFFAGHETTALL 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 314 ISFTLYTLSRHSEIQQKAAEEQRRIFGENFAgEADlaRLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKC 393
Cdd:cd11052 252 LTWTTMLLAIHPEWQEKAREEVLEVCGKDKP-PSD--SLSKLKTVSMVINESLRLYPPAVFLTRKAKEDIKLGGLVIPKG 328
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921820 394 TTVIMCLIAMGYNEKYF-DDPCTFRPERFEN--PTGNVGIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI 468
Cdd:cd11052 329 TSIWIPVLALHHDEEIWgEDANEFNPERFADgvAKAAKHPMAF--LPFGLGPRNCIGQNFATMEAKIVLAMILQRFSF 404
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
81-476 2.71e-52

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: 182.80  E-value: 2.71e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  81 YHMMLSDPAEIQNILSSSSLLYKEHLYSFLRPWL--GDGLLTSSGARWLKHQKLYAPAF----------ERsaIEGYLRv 148
Cdd:cd20617  12 PTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIIsgGKGILFSNGDYWKELRRFALSSLtktklkkkmeEL--IEEEVN- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 149 vhrtggQFVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLN-GETSDLHGAIKDLCDVVQERTFSIVKRFDA 227
Cdd:cd20617  89 ------KLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDdGEFLKLVKPIEEIFKELGSGNPSDFIPILL 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 228 LFRLTsYYMKQRRALSLLRSELNRIISQRRHQLAAENtcqqgqPINKPFLDVLLTAKLDGKVLKEREIIEEVST-FIFTG 306
Cdd:cd20617 163 PFYFL-YLKKLKKSYDKIKDFIEKIIEEHLKTIDPNN------PRDLIDDELLLLLKEGDSGLFDDDSIISTCLdLFLAG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 307 HDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfaGEADLARLDQMHYLELIIRETLRLYPSVPLIA-RTNRNPIDI 385
Cdd:cd20617 236 TDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGND--RRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLpRVTTEDTEI 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 386 NGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRR 465
Cdd:cd20617 314 GGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGNKLSEQF--IPFGIGKRNCVGENLARDELFLFFANLLLN 391
                       410
                ....*....|.
gi 19921820 466 FEILPaVDGLP 476
Cdd:cd20617 392 FKFKS-SDGLP 401
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
84-468 5.11e-50

cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of vertebrate cytochrome P450 24A1 (CYP24A1) and similar proteins including several Drosophila proteins such as CYP315A1 (also called protein shadow) and CYP314A1 (also called ecdysone 20-monooxygenase), and vertebrate CYP11 and CYP27 subfamilies. Both CYP314A1 and CYP315A1, which has ecdysteroid C2-hydroxylase activity, are involved in the metabolism of insect hormones. CYP24A1 and CYP27B1 have roles in calcium homeostasis and metabolism, and the regulation of vitamin D. CYP24A1 catabolizes calcitriol (1,25(OH)2D), the physiologically active vitamin D hormone, by catalyzing its hydroxylation, while CYP27B1 is a calcidiol 1-monooxygenase that coverts 25-hydroxyvitamin D3 to calcitriol. The CYP24A1-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410677 [Multi-domain]  Cd Length: 426  Bit Score: 176.95  E-value: 5.11e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  84 MLSDPAEIQNILSS-----------SSLLYKEHlysflRPwLGDGLLTSSGARWLKHQKLYAPAFER-SAIEGYLRVVHR 151
Cdd:cd11054  19 HLFDPDDIEKVFRNegkypirpslePLEKYRKK-----RG-KPLGLLNSNGEEWHRLRSAVQKPLLRpKSVASYLPAINE 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 152 TGGQFVQKLDVLSD--TQEVFDAQELVAKCTLDIVCENATGQDSSSLNG----ETSDLHGAIKDLCDVVQERTFS--IVK 223
Cdd:cd11054  93 VADDFVERIRRLRDedGEEVPDLEDELYKWSLESIGTVLFGKRLGCLDDnpdsDAQKLIEAVKDIFESSAKLMFGppLWK 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 224 RFDalfrlTSYYMKQRRALSLLRSELNRIISQRRHQLAAENTCQQGQPinkPFLDVLLTAKldgkVLKEREIIEEVSTFI 303
Cdd:cd11054 173 YFP-----TPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEEDEEED---SLLEYLLSKP----GLSKKEIVTMALDLL 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 304 FTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfaGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPI 383
Cdd:cd11054 241 LAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDG--EPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKDI 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 384 DINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERF-ENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQL 462
Cdd:cd11054 319 VLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlRDDSENKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAKL 398

                ....*.
gi 19921820 463 LRRFEI 468
Cdd:cd11054 399 LQNFKV 404
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
77-471 5.36e-50

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: 176.96  E-value: 5.36e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  77 VFLQYHMMLSDPAEIQNILSS------SSLLYK-EHLYSflrpwLGDGLLTSSGARWLK-HQKLyAPAFERSAIEGYLRV 148
Cdd:cd11056  10 LFRRPALLVRDPELIKQILVKdfahfhDRGLYSdEKDDP-----LSANLFSLDGEKWKElRQKL-TPAFTSGKLKNMFPL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 149 VHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLcdVVQERTFSIVKRFDAL 228
Cdd:cd11056  84 MVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGLDANSLNDPENEFREMGRRL--FEPSRLRGLKFMLLFF 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 229 FRLTSYYMKqrraLSLLRSELNR--------IISQRrhqlaaentcqQGQPINKP-FLDVLLTAKLDGKV--------LK 291
Cdd:cd11056 162 FPKLARLLR----LKFFPKEVEDffrklvrdTIEYR-----------EKNNIVRNdFIDLLLELKKKGKIeddksekeLT 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 292 EREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFgENFAGEADLARLDQMHYLELIIRETLRLYPS 371
Cdd:cd11056 227 DEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVL-EKHGGELTYEALQEMKYLDQVVNETLRKYPP 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 372 VPLIARTNRNPIDINGTKV--AKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNvGIEAFKSVPFSAGPRRCIAEK 449
Cdd:cd11056 306 LPFLDRVCTKDYTLPGTDVviEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKK-KRHPYTYLPFGDGPRNCIGMR 384
                       410       420
                ....*....|....*....|..
gi 19921820 450 FAMYQMKALLSQLLRRFEILPA 471
Cdd:cd11056 385 FGLLQVKLGLVHLLSNFRVEPS 406
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
84-471 9.09e-47

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: 168.21  E-value: 9.09e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  84 MLSDPAEIQNILSSSSLLYKE-HLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFV----- 157
Cdd:cd11049  27 VVTSPELVRQVLVNDRVFDKGgPLFDRARPLLGNGLATCPGEDHRRQRRLMQPAFHRSRIPAYAEVMREEAEALAgswrp 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 158 -QKLDVLSDTQEVfdaqelvakcTLDIVCENATGQDsssLNGETSD-LHGAIKDLCDVVQERTFSivkrFDALFRL-TSY 234
Cdd:cd11049 107 gRVVDVDAEMHRL----------TLRVVARTLFSTD---LGPEAAAeLRQALPVVLAGMLRRAVP----PKFLERLpTPG 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 235 YMKQRRALSLLRSELNRIISQRRhqlaaentcQQGQPINKpFLDVLLTAKLD-GKVLKEREIIEEVSTFIFTGHDPIAAA 313
Cdd:cd11049 170 NRRFDRALARLRELVDEIIAEYR---------ASGTDRDD-LLSLLLAARDEeGRPLSDEELRDQVITLLTAGTETTAST 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 314 ISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLARLdqmHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKC 393
Cdd:cd11049 240 LAWAFHLLARHPEVERRLHAELDAVLGGRPATFEDLPRL---TYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAG 316
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921820 394 TTVIMCLIAMGYNEKYFDDPCTFRPERF-ENPTGNVGIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPA 471
Cdd:cd11049 317 TEVAFSPYALHRDPEVYPDPERFDPDRWlPGRAAAVPRGAF--IPFGAGARKCIGDTFALTELTLALATIASRWRLRPV 393
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
80-468 7.31e-46

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: 165.97  E-value: 7.31e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  80 QYHMMLSDPAEIQNILSSSSLLYKEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAF-ERSAIEGYLRVVHRTggqfvQ 158
Cdd:cd11070  12 RWNILVTKPEYLTQIFRRRDDFPKPGNQYKIPAFYGPNVISSEGEDWKRYRKIVAPAFnERNNALVWEESIRQA-----Q 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 159 KL------DVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRlt 232
Cdd:cd11070  87 RLirylleEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHDTLNAIKLAIFPPLFLNFPFLDRLPW-- 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 233 sYYMKQR-RALSLLRSELNRIISQRRHQLAAENTCQQGQPINKpfLDVLLTAkLDGKVLKEREIIEEVSTFIFTGHDPIA 311
Cdd:cd11070 165 -VLFPSRkRAFKDVDEFLSELLDEVEAELSADSKGKQGTESVV--ASRLKRA-RRSGGLTEKELLGNLFIFFIAGHETTA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 312 AAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLARLDQMHYLELIIRETLRLYPSVPLIAR---TNRNPIDINGT 388
Cdd:cd11070 241 NTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEEDFPKLPYLLAVIYETLRLYPPVQLLNRkttEPVVVITGLGQ 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 389 KVA--KCTTVIMCLIAMGYNEKY-FDDPCTFRPERFENPTGNVGIE--------AFksVPFSAGPRRCIAEKFAMYQMKA 457
Cdd:cd11070 321 EIVipKGTYVGYNAYATHRDPTIwGPDADEFDPERWGSTSGEIGAAtrftpargAF--IPFSAGPRACLGRKFALVEFVA 398
                       410
                ....*....|.
gi 19921820 458 LLSQLLRRFEI 468
Cdd:cd11070 399 ALAELFRQYEW 409
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
94-473 1.20e-45

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: 164.73  E-value: 1.20e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  94 ILSSSSLLYKEHLYSFLRPWLGDG-LLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDA 172
Cdd:cd11051  24 ITQVTNLPKPPPLRKFLTPLTGGSsLISMEGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVEIFAAILRELAESGEVFSL 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 173 QELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQErtFSIVKRFDALFRLtsyymKQRRALSLLRSELNRI 252
Cdd:cd11051 104 EELTTNLTFDVIGRVTLDIDLHAQTGDNSLLTALRLLLALYRSL--LNPFKRLNPLRPL-----RRWRNGRRLDRYLKPE 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 253 ISQRrhqLAAENTCQQgqpinkpfldvlltakldgkvlkereiieeVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAA 332
Cdd:cd11051 177 VRKR---FELERAIDQ------------------------------IKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVR 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 333 EEQRRIFGENFAGEADLAR-----LDQMHYLELIIRETLRLYPsvplIARTNRNPI------DINGTKVakCTT---VIM 398
Cdd:cd11051 224 AEHDEVFGPDPSAAAELLRegpelLNQLPYTTAVIKETLRLFP----PAGTARRGPpgvgltDRDGKEY--PTDgciVYV 297
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921820 399 CLIAMGYNEKYFDDPCTFRPERFENPTGN---VGIEAFKsvPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVD 473
Cdd:cd11051 298 CHHAIHRDPEYWPRPDEFIPERWLVDEGHelyPPKSAWR--PFERGPRNCIGQELAMLELKIILAMTVRRFDFEKAYD 373
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
108-516 4.76e-44

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: 160.81  E-value: 4.76e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 108 SFLRPWLGDGLLTSSG--ARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVfDAQELVAKCTLDIVC 185
Cdd:cd11068  52 EELRDFAGDGLFTAYThePNWGKAHRILMPAFGPLAMRGYFPMMLDIAEQLVLKWERLGPDEPI-DVPDDMTRLTLDTIA 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 186 ENATGQDSSSlnGETSDLHGAIKDLCDVVQErTFSIVKRFDALFRLTSYYMKQRRA-LSLLRSELNRIISQRRhqlaaen 264
Cdd:cd11068 131 LCGFGYRFNS--FYRDEPHPFVEAMVRALTE-AGRRANRPPILNKLRRRAKRQFREdIALMRDLVDEIIAERR------- 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 265 tcQQGQPINKPFLDVLLTAKlD---GKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGE 341
Cdd:cd11068 201 --ANPDGSPDDLLNLMLNGK-DpetGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGD 277
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 342 NFAGEADLARLDqmhYLELIIRETLRLYPSVPLIARTNRNPIDINGT-KVAKCTTVIMCLIAMGYNEK-YFDDPCTFRPE 419
Cdd:cd11068 278 DPPPYEQVAKLR---YIRRVLDETLRLWPTAPAFARKPKEDTVLGGKyPLKKGDPVLVLLPALHRDPSvWGEDAEEFRPE 354
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 420 RFENP-TGNVGIEAFKsvPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPavdglppginDHSREDCVPQseydpvln 498
Cdd:cd11068 355 RFLPEeFRKLPPNAWK--PFGNGQRACIGRQFALQEATLVLAMLLQRFDFED----------DPDYELDIKE-------- 414
                       410
                ....*....|....*...
gi 19921820 499 iRVTLKSEnGIQIRLRKR 516
Cdd:cd11068 415 -TLTLKPD-GFRLKARPR 430
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
84-468 3.94e-42

cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is composed of CYPs from unicellular ciliates similar to Tetrahymena thermophila CYP5011A1, whose function is still unknown. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410714 [Multi-domain]  Cd Length: 427  Bit Score: 155.88  E-value: 3.94e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  84 MLSDPAEIQNILSSSSLLYKE---HLYSFLrpwLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKL 160
Cdd:cd20621  17 SLVDPEYIKEFLQNHHYYKKKfgpLGIDRL---FGKGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINEITKEKIKKL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 161 DvlsdtQEVFDAQELVAKCTLDIV-----CENATGQdssSLNGEtsDLHGAIKDLC----DVVQERTFSIVKRF------ 225
Cdd:cd20621  94 D-----NQNVNIIQFLQKITGEVVirsffGEEAKDL---KINGK--EIQVELVEILiesfLYRFSSPYFQLKRLifgrks 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 226 DALFRLTSYYMKQRRaLSLLRSELNRIISQRRHQLAAENTcQQGQPINKPFLDVLLTAKLDGKVLKErEIIEEVSTFIFT 305
Cdd:cd20621 164 WKLFPTKKEKKLQKR-VKELRQFIEKIIQNRIKQIKKNKD-EIKDIIIDLDLYLLQKKKLEQEITKE-EIIQQFITFFFA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 306 GHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLarLDQMHYLELIIRETLRLYPSVP-LIARTNRNPID 384
Cdd:cd20621 241 GTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFED--LQKLNYLNAFIKEVLRLYNPAPfLFPRVATQDHQ 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 385 INGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTgNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLR 464
Cdd:cd20621 319 IGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQN-NIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILK 397

                ....
gi 19921820 465 RFEI 468
Cdd:cd20621 398 NFEI 401
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
85-470 4.26e-42

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: 155.52  E-value: 4.26e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  85 LSDPAEIQNILSSSSLLYKEHLYSFLRPWLGDG-LLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLdvl 163
Cdd:cd11044  37 VIGAEAVRFILSGEGKLVRYGWPRSVRRLLGENsLSLQDGEEHRRRRKLLAPAFSREALESYVPTIQAIVQSYLRKW--- 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 164 SDTQEVFDAQELvAKCTLDIVCENATGQDSsslNGETSDLHGAIKDLCDVVqertFSIVKRFDAlfrltSYYMKQRRALS 243
Cdd:cd11044 114 LKAGEVALYPEL-RRLTFDVAARLLLGLDP---EVEAEALSQDFETWTDGL----FSLPVPLPF-----TPFGRAIRARN 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 244 LLRSELNRIISQRRHQLAAENtcqqgqpinKPFLDVLLTAKL-DGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLS 322
Cdd:cd11044 181 KLLARLEQAIRERQEEENAEA---------KDALGLLLEAKDeDGEPLSMDELKDQALLLLFAGHETTASALTSLCFELA 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 323 RHSEIQQKAAEEQRRIFGENfagEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIA 402
Cdd:cd11044 252 QHPDVLEKLRQEQDALGLEE---PLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQIPKGWLVYYSIRD 328
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 403 MGYNEKYFDDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLR--RFEILP 470
Cdd:cd11044 329 THRDPELYPDPERFDPERFSPARSEDKKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRnyDWELLP 398
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
73-511 5.71e-41

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: 152.33  E-value: 5.71e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  73 FRSLVFLQYHMMLSDPAEIQNILSSSSL---LYKEHLYSFlRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEgYLRVV 149
Cdd:cd11063   5 FEVNLLGTRVIFTIEPENIKAVLATQFKdfgLGERRRDAF-KPLLGDGIFTSDGEEWKHSRALLRPQFSRDQIS-DLELF 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 150 HRTGGQFVQKLDVlsdTQEVFDAQELVAKCTLDIvcenAT----GQDSSSL--NGETSDLHGAIKDLcDVVQERtfsIVK 223
Cdd:cd11063  83 ERHVQNLIKLLPR---DGSTVDLQDLFFRLTLDS----ATeflfGESVDSLkpGGDSPPAARFAEAF-DYAQKY---LAK 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 224 RFdalfRLTSYYM-----KQRRALSLLRSELNRIISQRrhqLAAENTCQQGQPINK-PFLDVLLTAKLDgkvlkEREIIE 297
Cdd:cd11063 152 RL----RLGKLLWllrdkKFREACKVVHRFVDPYVDKA---LARKEESKDEESSDRyVFLDELAKETRD-----PKELRD 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 298 EVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGEnfAGEADLARLDQMHYLELIIRETLRLYPSVPLIAR 377
Cdd:cd11063 220 QLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGP--EPTPTYEDLKNMKYLRAVINETLRLYPPVPLNSR 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 378 T-NRNPI-----DINGTK---VAKCTTVIMCLIAMGYNEK-YFDDPCTFRPERFENPTGNvgieAFKSVPFSAGPRRCIA 447
Cdd:cd11063 298 VaVRDTTlprggGPDGKSpifVPKGTRVLYSVYAMHRRKDiWGPDAEEFRPERWEDLKRP----GWEYLPFNGGPRICLG 373
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921820 448 EKFAMYQMKALLSQLLRRFEILPAVDglppgindhsredcvpqsEYDPVLNIRVTLKSENGIQI 511
Cdd:cd11063 374 QQFALTEASYVLVRLLQTFDRIESRD------------------VRPPEERLTLTLSNANGVKV 419
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
85-473 9.96e-40

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: 148.99  E-value: 9.96e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  85 LSDPAEIQNILSSSSLLYKEHLYSFLRPWLGDGLLTSSGAR-WLKHQKLYAPAFERSAIEGYLR--VVHRTGGQFVQKLD 161
Cdd:cd11059  13 VNDLDAVREIYGGGFGKTKSYWYFTLRGGGGPNLFSTLDPKeHSARRRLLSGVYSKSSLLRAAMepIIRERVLPLIDRIA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 162 VLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDlhgaikdlcdvVQERTFSIVKRFDALFRLTSYYMKQRRA 241
Cdd:cd11059  93 KEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKD-----------SRERELLRRLLASLAPWLRWLPRYLPLA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 242 LSLLRSELNRIISQR-----RHQLA-AENTCQQGQPINKPFLDVLLTAKLDGKV-LKEREIIEEVSTFIFTGHDPIAAAI 314
Cdd:cd11059 162 TSRLIIGIYFRAFDEieewaLDLCArAESSLAESSDSESLTVLLLEKLKGLKKQgLDDLEIASEALDHIVAGHDTTAVTL 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 315 SFTLYTLSRHSEIQQKAAEEQRRIFGeNFAGEADLARLDQMHYLELIIRETLRLYPSVPLIA--RTNRNPIDINGTKVAK 392
Cdd:cd11059 242 TYLIWELSRPPNLQEKLREELAGLPG-PFRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLprVVPEGGATIGGYYIPG 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 393 CTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFKS-VPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPA 471
Cdd:cd11059 321 GTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETAREMKRAfWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTSTT 400

                ..
gi 19921820 472 VD 473
Cdd:cd11059 401 TD 402
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
87-487 3.37e-38

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: 144.67  E-value: 3.37e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  87 DPAEIQNILSSSSLLYKEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDT 166
Cdd:cd11061  15 DPDALKDIYGHGSNCLKGPFYDALSPSASLTFTTRDKAEHARRRRVWSHAFSDKALRGYEPRILSHVEQLCEQLDDRAGK 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 167 QEV--FDAQELVAKCTLDIVCENATGQDSSSLngETSDLHGAIKDLCDVVqeRTFSIVKRFDALFRLTSYyMKQRRALSL 244
Cdd:cd11061  95 PVSwpVDMSDWFNYLSFDVMGDLAFGKSFGML--ESGKDRYILDLLEKSM--VRLGVLGHAPWLRPLLLD-LPLFPGATK 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 245 LRSELNRIISQRrhqlaAENTCQQGQPINKPFLDVLLTAKL--DGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLS 322
Cdd:cd11061 170 ARKRFLDFVRAQ-----LKERLKAEEEKRPDIFSYLLEAKDpeTGEGLDLEELVGEARLLIVAGSDTTATALSAIFYYLA 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 323 RHSEIQQKAAEEQRRIFGENfAGEADLARLDQMHYLELIIRETLRLYPSVP--LIARTNRNPIDINGTKVAKCTTVIMCL 400
Cdd:cd11061 245 RNPEAYEKLRAELDSTFPSD-DEIRLGPKLKSLPYLRACIDEALRLSPPVPsgLPRETPPGGLTIDGEYIPGGTTVSVPI 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 401 IAMGYNEKYFDDPCTFRPERFENPTGNVGIE--AFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIlpavdGLPPG 478
Cdd:cd11061 324 YSIHRDERYFPDPFEFIPERWLSRPEELVRArsAF--IPFSIGPRGCIGKNLAYMELRLVLARLLHRYDF-----RLAPG 396

                ....*....
gi 19921820 479 INDHSREDC 487
Cdd:cd11061 397 EDGEAGEGG 405
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
116-469 7.27e-37

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


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 140.79  E-value: 7.27e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 116 DGLLTSSGARWLKHQKLYAPAF-ERSaiegyLR----VVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATG 190
Cdd:cd11058  48 PSISTADDEDHARLRRLLAHAFsEKA-----LReqepIIQRYVDLLVSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFG 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 191 QDSSSLngETSDLHGAIKDLCDVVQERTFS-IVKRFDALFRL----TSYYMKQRRA--LSLLRSELnriisQRRHQLAAE 263
Cdd:cd11058 123 ESFGCL--ENGEYHPWVALIFDSIKALTIIqALRRYPWLLRLlrllIPKSLRKKRKehFQYTREKV-----DRRLAKGTD 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 264 NtcqqgqpinKPFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRrifgENF 343
Cdd:cd11058 196 R---------PDFMSYILRNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIR----SAF 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 344 AGEAD--LARLDQMHYLELIIRETLRLYPSVPLIA--RTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPE 419
Cdd:cd11058 263 SSEDDitLDSLAQLPYLNAVIQEALRLYPPVPAGLprVVPAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPE 342
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 19921820 420 RF-ENPTGNVG---IEAFKsvPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIL 469
Cdd:cd11058 343 RWlGDPRFEFDndkKEAFQ--PFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLE 394
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
235-483 1.10e-36

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: 140.43  E-value: 1.10e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 235 YMKQRRALSLLRSELNRIISQRRhqlaaentcQQGQPINKPFLDVLLTAKL-DGKVLKEREIIEEVSTFIFTGHDPIAAA 313
Cdd:cd11042 161 FRRRDRARAKLKEIFSEIIQKRR---------KSPDKDEDDMLQTLMDAKYkDGRPLTDDEIAGLLIALLFAGQHTSSAT 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 314 ISFTLYTLSRHSEIQQKAAEEQRRIFGENfAGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTK--VA 391
Cdd:cd11042 232 SAWTGLELLRNPEHLEALREEQKEVLGDG-DDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVEGGGyvIP 310
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 392 KCTTVimcLIAMGYN---EKYFDDPCTFRPERFENPTGNVGI-EAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd11042 311 KGHIV---LASPAVShrdPEIFKNPDEFDPERFLKGRAEDSKgGKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFD 387
                       250
                ....*....|....*.
gi 19921820 468 iLPAVDGLPPGINDHS 483
Cdd:cd11042 388 -FELVDSPFPEPDYTT 402
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
86-466 1.15e-36

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: 140.66  E-value: 1.15e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  86 SDPAEIQNILSSSSLLYKEhlySFLRP----WLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQ--- 158
Cdd:cd20641  28 SDHELAKQVLSDKFGFFGK---SKARPeilkLSGKGLVFVNGDDWVRHRRVLNPAFSMDKLKSMTQVMADCTERMFQewr 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 159 KLDVLSDTQEVF-DAQELVAKCTLDIVCENATGqdSSSLNGetsdlhgaiKDLCDVVQERTFSIVKRFDALFRLTSYYMK 237
Cdd:cd20641 105 KQRNNSETERIEvEVSREFQDLTADIIATTAFG--SSYAEG---------IEVFLSQLELQKCAAASLTNLYIPGTQYLP 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 238 QRRALSL------LRSELNRIISQRrhqLAAEntcqqGQPINKPFLDVLLTA-------KLDGKVLKEREIIEEVSTFIF 304
Cdd:cd20641 174 TPRNLRVwklekkVRNSIKRIIDSR---LTSE-----GKGYGDDLLGLMLEAassneggRRTERKMSIDEIIDECKTFFF 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 305 TGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEAD-LARLDQMHyleLIIRETLRLYPSVPLIARTNRNPI 383
Cdd:cd20641 246 AGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADtLSKLKLMN---MVLMETLRLYGPVINIARRASEDM 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 384 DINGTKVAKCTTVIMCLIAMGYNEKYF-DDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQL 462
Cdd:cd20641 323 KLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHPNALLSFSLGPRACIGQNFAMIEAKTVLAMI 402

                ....
gi 19921820 463 LRRF 466
Cdd:cd20641 403 LQRF 406
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
84-476 2.08e-36

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: 139.38  E-value: 2.08e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  84 MLSDPAEIQNILSSssllyKEHLYSF-------LRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRtggqf 156
Cdd:cd11045  25 ALLGPDANQLVLRN-----RDKAFSSkqgwdpvIGPFFHRGLMLLDFDEHRAHRRIMQQAFTRSALAGYLDRMTP----- 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 157 vQKLDVLSD--TQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSdlhgaiKDLCDVVQERTfSIVkRFDALFrlTSY 234
Cdd:cd11045  95 -GIERALARwpTGAGFQFYPAIKELTLDLATRVFLGVDLGPEADKVN------KAFIDTVRAST-AII-RTPIPG--TRW 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 235 Y--MKQRRalsLLRSELNRIISQRRhqlaAENT-------CQQGQPinkpfldvlltaklDGKVLKEREIIEEVSTFIFT 305
Cdd:cd11045 164 WrgLRGRR---YLEEYFRRRIPERR----AGGGddlfsalCRAEDE--------------DGDRFSDDDIVNHMIFLMMA 222
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 306 GHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGenfaGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDI 385
Cdd:cd11045 223 AHDTTTSTLTSMAYFLARHPEWQERLREESLALGK----GTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEV 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 386 NGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRR 465
Cdd:cd11045 299 LGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRR 378
                       410       420
                ....*....|....*....|....*.
gi 19921820 466 FEI--------------LPA-VDGLP 476
Cdd:cd11045 379 FRWwsvpgyyppwwqspLPApKDGLP 404
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
134-467 1.38e-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: 137.38  E-value: 1.38e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 134 APAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLngetsDLHGAIKDLCDV 213
Cdd:cd11062  63 SPFFSKRSILRLEPLIQEKVDKLVSRLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGYL-----DEPDFGPEFLDA 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 214 VQE--------RTFSIVKRFDALFRLTSYYMKQRRALSL--LRSELNRIISQRRHQLAAENTcqqgQPINKPFLDVLLTA 283
Cdd:cd11062 138 LRAlaemihllRHFPWLLKLLRSLPESLLKRLNPGLAVFldFQESIAKQVDEVLRQVSAGDP----PSIVTSLFHALLNS 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 284 KLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfAGEADLARLDQMHYLELIIR 363
Cdd:cd11062 214 DLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDP-DSPPSLAELEKLPYLTAVIK 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 364 ETLRLYPSVPliARTNR----NPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFkSVPFS 439
Cdd:cd11062 293 EGLRLSYGVP--TRLPRvvpdEGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEKGKLDRY-LVPFS 369
                       330       340
                ....*....|....*....|....*...
gi 19921820 440 AGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd11062 370 KGSRSCLGINLAYAELYLALAALFRRFD 397
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
167-466 9.35e-35

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: 135.00  E-value: 9.35e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 167 QEVFDAQELVAKCTLDIVCENATGQDSsslnGETSDlhgAIKDLCDVVQERTFSI-VKrfdalFRLTSYY--MKQRRALs 243
Cdd:cd11043 101 GKSVVVLELAKKMTFELICKLLLGIDP----EEVVE---ELRKEFQAFLEGLLSFpLN-----LPGTTFHraLKARKRI- 167
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 244 llRSELNRIISQRRHQLAAENTCQQgqpinkpFLDVLLTAK-LDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLS 322
Cdd:cd11043 168 --RKELKKIIEERRAELEKASPKGD-------LLDVLLEEKdEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLA 238
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 323 RHSEIQQKAAEEQRRIFGENFAGEA-DLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLI 401
Cdd:cd11043 239 ENPKVLQELLEEHEEIAKRKEEGEGlTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSAR 318
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921820 402 AMGYNEKYFDDPCTFRPERFENPTGNVgieAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:cd11043 319 ATHLDPEYFPDPLKFNPWRWEGKGKGV---PYTFLPFGGGPRLCPGAELAKLEILVFLHHLVTRF 380
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
83-470 1.08e-34

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: 135.23  E-value: 1.08e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  83 MMLSDPAEIQNILssssllYKEhLYSFL---RPW-----LGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGG 154
Cdd:cd20650  16 LAITDPDMIKTVL------VKE-CYSVFtnrRPFgpvgfMKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMFPIIAQYGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 155 QFVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCdvvqerTFSIvkrFDALFRLTSY 234
Cdd:cd20650  89 VLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLL------KFDF---LDPLFLSITV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 235 Y-------------MKQRRALSLLRSELNRIISQRrhqlaaENTCQQGQpinKPFLDVLLTAKLDG-----KVLKEREII 296
Cdd:cd20650 160 FpfltpileklnisVFPKDVTNFFYKSVKKIKESR------LDSTQKHR---VDFLQLMIDSQNSKeteshKALSDLEIL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 297 EEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLarLDQMHYLELIIRETLRLYPSVPLIA 376
Cdd:cd20650 231 AQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDT--VMQMEYLDMVVNETLRLFPIAGRLE 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 377 RTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFeNPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMK 456
Cdd:cd20650 309 RVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERF-SKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMK 387
                       410
                ....*....|....
gi 19921820 457 ALLSQLLRRFEILP 470
Cdd:cd20650 388 LALVRVLQNFSFKP 401
PLN02290 PLN02290
cytokinin trans-hydroxylase
83-514 7.03e-34

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 134.17  E-value: 7.03e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   83 MMLSDPAEIQNILSS------SSLLYKEHLYSFLrpwlGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQF 156
Cdd:PLN02290 107 LCLTETELIKELLTKyntvtgKSWLQQQGTKHFI----GRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQM 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  157 VQKL-DVLSDTQEVFDAQELVAKCTLDIVCEnaTGQDSSSLNGETsdlhgaIKDLCDVVQERTFSIVKRFdaLFRLTSYY 235
Cdd:PLN02290 183 LQSLqKAVESGQTEVEIGEYMTRLTADIISR--TEFDSSYEKGKQ------IFHLLTVLQRLCAQATRHL--CFPGSRFF 252
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  236 -MKQRRALSLLRSELNRI---ISQRRHQLAAEN-TCQQGQPINKPFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPI 310
Cdd:PLN02290 253 pSKYNREIKSLKGEVERLlmeIIQSRRDCVEIGrSSSYGDDLLGMLLNEMEKKRSNGFNLNLQLIMDECKTFFFAGHETT 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  311 AAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLARLDqmhYLELIIRETLRLYPSVPLIARTNRNPIDINGTKV 390
Cdd:PLN02290 333 ALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVDHLSKLT---LLNMVINESLRLYPPATLLPRMAFEDIKLGDLHI 409
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  391 AKCTTVIMCLIAMGYNEKYF-DDPCTFRPERFenpTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIl 469
Cdd:PLN02290 410 PKGLSIWIPVLAIHHSEELWgKDANEFNPDRF---AGRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSF- 485
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 19921820  470 pavdglppGINDHSRedcvpqseYDPVlnIRVTLKSENGIQIRLR 514
Cdd:PLN02290 486 --------TISDNYR--------HAPV--VVLTIKPKYGVQVCLK 512
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
111-477 1.58e-33

cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily contains cytochrome P450 17A1 (CYP17A1 or Cyp17a1), cytochrome P450 21 (CYP21 or Cyp21) and similar proteins. CYP17A1, also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione; it catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. This subfamily also contains CYP21, also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2, catalyzes the 21-hydroxylation of steroids and is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. The CYP17A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410653 [Multi-domain]  Cd Length: 428  Bit Score: 131.95  E-value: 1.58e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 111 RPWL---------GDGL-LTSSGARWLKHQKLYApaferSAIEGYLRVVHRTG---GQFVQKL-DVLSDTQE-VFDAQEL 175
Cdd:cd11027  37 RPKLftfdlfsrgGKDIaFGDYSPTWKLHRKLAH-----SALRLYASGGPRLEekiAEEAEKLlKRLASQEGqPFDPKDE 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 176 VAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVqeRTFSIVkrfDALFRLTSYYMKQRRALSLLRSELNRIISQ 255
Cdd:cd11027 112 LFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKFFELL--GAGSLL---DIFPFLKYFPNKALRELKELMKERDEILRK 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 256 --RRHQLaaenTCQQGQPINkpFLDVLLTAKLDGK--------VLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHS 325
Cdd:cd11027 187 klEEHKE----TFDPGNIRD--LTDALIKAKKEAEdegdedsgLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYP 260
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 326 EIQQKAAEEQRRIFGENFAGE-ADLARLDqmhYLELIIRETLRLYPSVPLIA--RTNRnPIDINGTKVAKCTTVIMCLIA 402
Cdd:cd11027 261 EVQAKLHAELDDVIGRDRLPTlSDRKRLP---YLEATIAEVLRLSSVVPLALphKTTC-DTTLRGYTIPKGTTVLVNLWA 336
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921820 403 MGYNEKYFDDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDGLPP 477
Cdd:cd11027 337 LHHDPKEWDDPDEFRPERFLDENGKLVPKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEPPP 411
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
85-466 7.28e-32

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: 127.01  E-value: 7.28e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  85 LSDPAEIQNILSSSSLLYKEHLYSFLRpWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLS 164
Cdd:cd20642  27 IMDPELIKEVLNKVYDFQKPKTNPLTK-LLATGLASYEGDKWAKHRKIINPAFHLEKLKNMLPAFYLSCSEMISKWEKLV 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 165 DTQ---EVfDAQELVAKCTLDIVCENATGqdsSSLNgETSDLHGAIKDLCDVVQErtfSIVKRFDALFR-LTSYYMKQRR 240
Cdd:cd20642 106 SSKgscEL-DVWPELQNLTSDVISRTAFG---SSYE-EGKKIFELQKEQGELIIQ---ALRKVYIPGWRfLPTKRNRRMK 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 241 ALSL-LRSELNRIISQRrhqlaaENTCQQGQPINKPFLDVLL-----TAKLDGKV---LKEREIIEEVSTFIFTGHDPIA 311
Cdd:cd20642 178 EIEKeIRSSLRGIINKR------EKAMKAGEATNDDLLGILLesnhkEIKEQGNKnggMSTEDVIEECKLFYFAGQETTS 251
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 312 AAISFTLYTLSRHSEIQQKAAEEQRRIFGENfagEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVA 391
Cdd:cd20642 252 VLLVWTMVLLSQHPDWQERAREEVLQVFGNN---KPDFEGLNHLKVVTMILYEVLRLYPPVIQLTRAIHKDTKLGDLTLP 328
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 392 KCTTVIMCLIAMGYNEKYF-DDPCTFRPERFENptgnvGI-EAFKS----VPFSAGPRRCIAEKFAMYQMKALLSQLLRR 465
Cdd:cd20642 329 AGVQVSLPILLVHRDPELWgDDAKEFNPERFAE-----GIsKATKGqvsyFPFGWGPRICIGQNFALLEAKMALALILQR 403

                .
gi 19921820 466 F 466
Cdd:cd20642 404 F 404
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
116-474 1.14e-31

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: 126.51  E-value: 1.14e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 116 DGLLTSSGARWLKHQKLYA-PAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATGQ--- 191
Cdd:cd20618  51 DIVFAPYGPHWRHLRKICTlELFSAKRLESFQGVRKEELSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKryf 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 192 -DSSSLNGETSDLHGAIKDLCDVVQERT----FSIVKRFDalfrLTSYYMKQRRALSLLRSELNRIISQRRHQLAAENTC 266
Cdd:cd20618 131 gESEKESEEAREFKELIDEAFELAGAFNigdyIPWLRWLD----LQGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKG 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 267 qqgqPINKPFLDVLLTAKLDGKvLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGEN-FAG 345
Cdd:cd20618 207 ----GDDDDDLLLLLDLDGEGK-LSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRErLVE 281
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 346 EADLARLdqmHYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFEN- 423
Cdd:cd20618 282 ESDLPKL---PYLQAVVKETLRLHPPGPLlLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLEs 358
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 19921820 424 PTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE-ILPAVDG 474
Cdd:cd20618 359 DIDDVKGQDFELLPFGSGRRMCPGMPLGLRMVQLTLANLLHGFDwSLPGPKP 410
PLN02738 PLN02738
carotene beta-ring hydroxylase
83-477 2.44e-31

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 128.11  E-value: 2.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   83 MMLSDPAEIQNILSSSSLLY-KEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLD 161
Cdd:PLN02738 178 LIVSDPSIAKHILRDNSKAYsKGILAEILEFVMGKGLIPADGEIWRVRRRAIVPALHQKYVAAMISLFGQASDRLCQKLD 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  162 VLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETsdlhGAIKDLCDVVQE---RTFSIVKRFD-ALFRLTSyyMK 237
Cdd:PLN02738 258 AAASDGEDVEMESLFSRLTLDIIGKAVFNYDFDSLSNDT----GIVEAVYTVLREaedRSVSPIPVWEiPIWKDIS--PR 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  238 QRR---ALSLLRSELN-------RIISQRRHQLAAENTCQQGQPInkpfLDVLLTAkldGKVLKEREIIEEVSTFIFTGH 307
Cdd:PLN02738 332 QRKvaeALKLINDTLDdliaickRMVEEEELQFHEEYMNERDPSI----LHFLLAS---GDDVSSKQLRDDLMTMLIAGH 404
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  308 DPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLARLdqmHYLELIIRETLRLYPSVP-LIARTNRNPIdIN 386
Cdd:PLN02738 405 ETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKL---KYTTRVINESLRLYPQPPvLIRRSLENDM-LG 480
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  387 GTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERF--ENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLR 464
Cdd:PLN02738 481 GYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWplDGPNPNETNQNFSYLPFGGGPRKCVGDMFASFENVVATAMLVR 560
                        410
                 ....*....|...
gi 19921820  465 RFEILPAVdGLPP 477
Cdd:PLN02738 561 RFDFQLAP-GAPP 572
PTZ00404 PTZ00404
cytochrome P450; Provisional
35-476 6.74e-31

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 125.22  E-value: 6.74e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   35 IPGPTPYPFVGNLFQFGLKPAeypKKVLQYCRKYDfQGFRSLVFLQYHMMLSDPAEIQNIL--SSSSLLYKEHLYSFLRP 112
Cdd:PTZ00404  31 LKGPIPIPILGNLHQLGNLPH---RDLTKMSKKYG-GIFRIWFADLYTVVLSDPILIREMFvdNFDNFSDRPKIPSIKHG 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  113 WLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDI----VCENA 188
Cdd:PTZ00404 107 TFYHGIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQVDVLIESMKKIESSGETFEPRYYLTKFTMSAmfkyIFNED 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  189 TGQDSSSLNGETSDLHGAIKDLCdvvqeRTFSIVKRFDALFRLTSYYMKQrraLSLLRSELNRI---ISQRRHQlaAENT 265
Cdd:PTZ00404 187 ISFDEDIHNGKLAELMGPMEQVF-----KDLGSGSLFDVIEITQPLYYQY---LEHTDKNFKKIkkfIKEKYHE--HLKT 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  266 CQQGQPinKPFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfaG 345
Cdd:PTZ00404 257 IDPEVP--RDLLDLLIKEYGTNTDDDILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGR--N 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  346 EADLARLDQMHYLELIIRETLRLYPSVPL-IARTNRNPIDINGTK-VAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFEN 423
Cdd:PTZ00404 333 KVLLSDRQSTPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIGGGHfIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLN 412
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19921820  424 PTGNVgieAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIlPAVDGLP 476
Cdd:PTZ00404 413 PDSND---AF--MPFSIGPRNCVGQQFAQDELYLAFSNIILNFKL-KSIDGKK 459
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
156-466 9.29e-31

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: 124.11  E-value: 9.29e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 156 FVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGEtsDLHGAIKDLCDVVqeRTFSI------VKRFDALF 229
Cdd:cd11072  94 LVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQD--KFKELVKEALELL--GGFSVgdyfpsLGWIDLLT 169
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 230 RLTSYYMKQRRALSLLrseLNRIISQRRHQLAAENTCQqgqpinkpFLDVLLTAKLDGKVLKE----REIIEEVSTFIFT 305
Cdd:cd11072 170 GLDRKLEKVFKELDAF---LEKIIDEHLDKKRSKDEDD--------DDDDLLDLRLQKEGDLEfpltRDNIKAIILDMFL 238
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 306 -GHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfaGEADLARLDQMHYLELIIRETLRLYPSVP-LIARTNRNPI 383
Cdd:cd11072 239 aGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGK--GKVTEEDLEKLKYLKAVIKETLRLHPPAPlLLPRECREDC 316
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 384 DINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLL 463
Cdd:cd11072 317 KINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIDFKGQDFELIPFGAGRRICPGITFGLANVELALANLL 396

                ...
gi 19921820 464 RRF 466
Cdd:cd11072 397 YHF 399
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
86-468 1.80e-28

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: 117.55  E-value: 1.80e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  86 SDPAEIQNILSSSSLLYK--EHlYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLD-- 161
Cdd:cd20639  28 ADPELIREILLTRADHFDryEA-HPLVRQLEGDGLVSLRGEKWAHHRRVITPAFHMENLKRLVPHVVKSVADMLDKWEam 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 162 VLSDTQEVFDAQELVAKCTLDIVCENATGqdSSSLNGEtsdlhgAIKDLcdvvQERTFsivkRFDALFRLTSYY------ 235
Cdd:cd20639 107 AEAGGEGEVDVAEWFQNLTEDVISRTAFG--SSYEDGK------AVFRL----QAQQM----LLAAEAFRKVYIpgyrfl 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 236 --MKQRRALSL---LRSELNRIISQRrhQLAAENTCQQGQpiNKPFLDVLLTAKLD--GKVLKEREIIEEVSTFIFTGHD 308
Cdd:cd20639 171 ptKKNRKSWRLdkeIRKSLLKLIERR--QTAADDEKDDED--SKDLLGLMISAKNArnGEKMTVEEIIEECKTFFFAGKE 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 309 PIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADlaRLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGT 388
Cdd:cd20639 247 TTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKD--HLPKLKTLGMILNETLRLYPPAVATIRRAKKDVKLGGL 324
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 389 KVAKCTTVIMCLIAMGYNEKYF-DDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd20639 325 DIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARAAKHPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFE 404

                .
gi 19921820 468 I 468
Cdd:cd20639 405 F 405
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
82-467 5.73e-28

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: 115.97  E-value: 5.73e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  82 HMMLSDPAEIQNILSSSSLLYKE--HLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQK 159
Cdd:cd20640  24 FLYVSRPEMVKEINLCVSLDLGKpsYLKKTLKPLFGGGILTSNGPHWAHQRKIIAPEFFLDKVKGMVDLMVDSAQPLLSS 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 160 LDvlsdtQEVFDAQELVAKCTLDIVCENATGQ-------DSSSLNGEtsDLHGAIKDLCDVVQERtfSIVKRFDALFRLT 232
Cdd:cd20640 104 WE-----ERIDRAGGMAADIVVDEDLRAFSADvisracfGSSYSKGK--EIFSKLRELQKAVSKQ--SVLFSIPGLRHLP 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 233 SyymKQRRALSLLRSELNRIISQrrhqLAAENTCQQgqPINKPFLDVLLTAKLDGKVLK---EREIIEEVSTFIFTGHDP 309
Cdd:cd20640 175 T---KSNRKIWELEGEIRSLILE----IVKEREEEC--DHEKDLLQAILEGARSSCDKKaeaEDFIVDNCKNIYFAGHET 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 310 IAAAISFTLYTLSRHSEIQQKAAEEQRRIFGenfAGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTK 389
Cdd:cd20640 246 TAVTAAWCLMLLALHPEWQDRVRAEVLEVCK---GGPPDADSLSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLV 322
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 390 VAKcTTVIMCLIAMGYNEK--YFDDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd20640 323 VPK-GVNIWVPVSTLHLDPeiWGPDANEFNPERFSNGVAAACKPPHSYMPFGAGARTCLGQNFAMAELKVLVSLILSKFS 401
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
85-468 6.14e-28

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: 115.76  E-value: 6.14e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  85 LSDPAEIQNILSSSSLLYKEHLYSFLRPWLG--DGLLTSSGARWlkHQKLY---APAFERSAIEGYLRVVHRTGGQFVQK 159
Cdd:cd11060  13 ISDPEAIKTIYGTRSPYTKSDWYKAFRPKDPrkDNLFSERDEKR--HAALRrkvASGYSMSSLLSLEPFVDECIDLLVDL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 160 LDVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETsDLHGAIKDLcDVVQeRTFSIVKRFDALFRLTsyYMKQR 239
Cdd:cd11060  91 LDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFGFLEAGT-DVDGYIASI-DKLL-PYFAVVGQIPWLDRLL--LKNPL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 240 RALSLLRSELNRIISQRRHQLAAENTCQQGQPINKP-FLDVLLTAKL-DGKVLKEREIIEEVSTFIFTGHDPIAAAISFT 317
Cdd:cd11060 166 GPKRKDKTGFGPLMRFALEAVAERLAEDAESAKGRKdMLDSFLEAGLkDPEKVTDREVVAEALSNILAGSDTTAIALRAI 245
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 318 LYTLSRHSEIQQKAAEEQRRIFGENFAGEA---DLARldQMHYLELIIRETLRLYPSVPLI-ARTNrnP---IDINGTKV 390
Cdd:cd11060 246 LYYLLKNPRVYAKLRAEIDAAVAEGKLSSPitfAEAQ--KLPYLQAVIKEALRLHPPVGLPlERVV--PpggATICGRFI 321
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 391 AKCTTVIMCLIAMGYNEKYF-DDPCTFRPERF-ENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI 468
Cdd:cd11060 322 PGGTIVGVNPWVIHRDKEVFgEDADVFRPERWlEADEEQRRMMDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDF 401
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
85-476 1.03e-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: 115.24  E-value: 1.03e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  85 LSDPAEIQNILSSSSllyKEHLYSFLRPW--------LGDGLLTSSGARWLKHQKLYAPAFER-SAIEGYLRVVHRTGGQ 155
Cdd:cd20648  21 VADPALIEQVLRQEG---KHPVRSDLSSWkdyrqlrgHAYGLLTAEGEEWQRLRSLLAKHMLKpKAVEAYAGVLNAVVTD 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 156 FVQKLDVLSdtqevfdaqelvAKCTLDIVCENATGQDSSSLNGETSDLHGA-IKDLCDVVQERTFSIVKRFDALFRLTSY 234
Cdd:cd20648  98 LIRRLRRQR------------SRSSPGVVKDIAGEFYKFGLEGISSVLFESrIGCLEANVPEETETFIQSINTMFVMTLL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 235 YMKQRRAL-SLLRSELNRI--------------ISQRRHQLAAENTCqqGQPINKPFLdvllTAKLDGKVLKEREIIEEV 299
Cdd:cd20648 166 TMAMPKWLhRLFPKPWQRFcrswdqmfafakghIDRRMAEVAAKLPR--GEAIEGKYL----TYFLAREKLPMKSIYGNV 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 300 STFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEAdlARLDQMHYLELIIRETLRLYPSVPLIART- 378
Cdd:cd20648 240 TELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSA--ADVARMPLLKAVVKEVLRLYPVIPGNARVi 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 379 NRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERF--ENPTGNvgieAFKSVPFSAGPRRCIAEKFAMYQMK 456
Cdd:cd20648 318 PDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWlgKGDTHH----PYASLPFGFGKRSCIGRRIAELEVY 393
                       410       420
                ....*....|....*....|
gi 19921820 457 ALLSQLLRRFEILPAVDGLP 476
Cdd:cd20648 394 LALARILTHFEVRPEPGGSP 413
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
268-474 1.66e-27

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: 114.76  E-value: 1.66e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 268 QGQPINKPFLDVLLTAkldGKvLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIF-GENFAGE 346
Cdd:cd20646 211 RGEPVEGEYLTYLLSS---GK-LSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCpGDRIPTA 286
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 347 ADLARldqMHYLELIIRETLRLYPSVPLIAR-TNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERF---- 421
Cdd:cd20646 287 EDIAK---MPLLKAVIKETLRLYPVVPGNARvIVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWlrdg 363
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19921820 422 ---ENPtgnvgieaFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDG 474
Cdd:cd20646 364 glkHHP--------FGSIPFGYGVRACVGRRIAELEMYLALSRLIKRFEVRPDPSG 411
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
114-486 3.41e-27

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: 113.54  E-value: 3.41e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 114 LGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDT--QEVFDAQELVAKCTLDIVCEnatgq 191
Cdd:cd20615  48 LGQCVGLLSGTDWKRVRKVFDPAFSHSAAVYYIPQFSREARKWVQNLPTNSGDgrRFVIDPAQALKFLPFRVIAE----- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 192 dssSLNGE-TSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSY-YMKQRRALSLLRS---ELNRIISQRRHQLAAENTC 266
Cdd:cd20615 123 ---ILYGElSPEEKEELWDLAPLREELFKYVIKGGLYRFKISRYlPTAANRRLREFQTrwrAFNLKIYNRARQRGQSTPI 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 267 QQgqpinkpfldvLLTAKLDGKvLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEE--QRRifgENFA 344
Cdd:cd20615 200 VK-----------LYEAVEKGD-ITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEisAAR---EQSG 264
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 345 GEADLARLDQMHYLELIIRETLRLYP----SVPLIARTNRNpidINGTKVAKCTTVIMCLIAMGYN-EKYFDDPCTFRPE 419
Cdd:cd20615 265 YPMEDYILSTDTLLAYCVLESLRLRPllafSVPESSPTDKI---IGGYRIPANTPVVVDTYALNINnPFWGPDGEAYRPE 341
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921820 420 RFENPTGNVGIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILpavdglpPGINDHSRED 486
Cdd:cd20615 342 RFLGISPTDLRYNF--WRFGFGPRKCLGQHVADVILKALLAHLLEQYELK-------LPDQGENEED 399
PLN02936 PLN02936
epsilon-ring hydroxylase
83-468 1.84e-26

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 112.19  E-value: 1.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   83 MMLSDPAEIQNILSSSSLLYKEHLYSFLRPWL-GDGLLTSSGARWLKHQKLYAPAFERSAIEGYL-RVVHRTGGQFVQKL 160
Cdd:PLN02936  63 VVVSDPAIAKHVLRNYGSKYAKGLVAEVSEFLfGSGFAIAEGELWTARRRAVVPSLHRRYLSVMVdRVFCKCAERLVEKL 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  161 DVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLngeTSD------LHGAIKDlcdvVQERTFSIVK--RFDALFRLT 232
Cdd:PLN02936 143 EPVALSGEAVNMEAKFSQLTLDVIGLSVFNYNFDSL---TTDspviqaVYTALKE----AETRSTDLLPywKVDFLCKIS 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  233 SYYMKQRRALSLLRSELNRIISQRRHQLAAENTCQQGQPI----NKPFLDVLLTAKldgkvlkereiiEEVST------- 301
Cdd:PLN02936 216 PRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGEVIEGEEYvndsDPSVLRFLLASR------------EEVSSvqlrddl 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  302 --FIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLArldQMHYLELIIRETLRLYPSVP-LIART 378
Cdd:PLN02936 284 lsMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDIK---ELKYLTRCINESMRLYPHPPvLIRRA 360
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  379 NRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERF--ENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMK 456
Cdd:PLN02936 361 QVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFdlDGPVPNETNTDFRYIPFSGGPRKCVGDQFALLEAI 440
                        410
                 ....*....|..
gi 19921820  457 ALLSQLLRRFEI 468
Cdd:PLN02936 441 VALAVLLQRLDL 452
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
167-467 2.13e-26

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: 111.54  E-value: 2.13e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 167 QEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKDLCDVVQE--------------------RTFSIVKRFD 226
Cdd:cd20655 103 GESVDIGKELMKLTNNIICRMIMGRSCSEENGEAEEVRKLVKESAELAGKfnasdfiwplkkldlqgfgkRIMDVSNRFD 182
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 227 ALfrltsyymkqrralsllrseLNRIISQRRHQLAAENtcqqgQPINKPFLDVLLTAKLDgkvlKEREI---IEEVSTFI 303
Cdd:cd20655 183 EL--------------------LERIIKEHEEKRKKRK-----EGGSKDLLDILLDAYED----ENAEYkitRNHIKAFI 233
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 304 ---FT-GHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGEN-FAGEADLARLdqmHYLELIIRETLRLYPSVPLIART 378
Cdd:cd20655 234 ldlFIaGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTrLVQESDLPNL---PYLQAVVKETLRLHPPGPLLVRE 310
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 379 NRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERF---ENPTGNVGI--EAFKSVPFSAGPRRCIAEKFAMY 453
Cdd:cd20655 311 STEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFlasSRSGQELDVrgQHFKLLPFGSGRRGCPGASLAYQ 390
                       330
                ....*....|....
gi 19921820 454 QMKALLSQLLRRFE 467
Cdd:cd20655 391 VVGTAIAAMVQCFD 404
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
114-477 2.37e-25

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: 108.27  E-value: 2.37e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 114 LGDGLLTssgarWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQevFDAQELVAKCTLDIVCENATGqDS 193
Cdd:cd20674  55 LGDYSLL-----WKAHRKLTRSALQLGIRNSLEPVVEQLTQELCERMRAQAGTP--VDIQEEFSLLTCSIICCLTFG-DK 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 194 SSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSYYMKqrralSLLRSELNR---IISQ-RRHQlaaeNTCQQG 269
Cdd:cd20674 127 EDKDTLVQAFHDCVQELLKTWGHWSIQALDSIPFLRFFPNPGLR-----RLKQAVENRdhiVESQlRQHK----ESLVAG 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 270 QPinKPFLDVLLTAKLDGKVLKEREIIEE-------VSTFIfTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFG-E 341
Cdd:cd20674 198 QW--RDMTDYMLQGLGQPRGEKGMGQLLEghvhmavVDLFI-GGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGpG 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 342 NFAGEADLARLDqmhYLELIIRETLRLYPSVPLIA--RTNRnPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPE 419
Cdd:cd20674 275 ASPSYKDRARLP---LLNATIAEVLRLRPVVPLALphRTTR-DSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPE 350
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 19921820 420 RFENPtgnvGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDGLPP 477
Cdd:cd20674 351 RFLEP----GAANRALLPFGCGARVCLGEPLARLELFVFLARLLQAFTLLPPSDGALP 404
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
280-468 2.93e-25

cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3,4-desaturase; Cytochrome P450 27C1 (CYP27C1) is also called all-trans retinol 3,4-desaturase. It catalyzes the conversion of all-trans retinol (also called vitamin A1, the precursor of 11-cis retinal) to 3,4-didehydroretinol (also called vitamin A2, the precursor of 11-cis 3,4-didehydroretinal). CYP27C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410740 [Multi-domain]  Cd Length: 433  Bit Score: 108.08  E-value: 2.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 280 LLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGEN-FAGEADLARLDqmhYL 358
Cdd:cd20647 223 LLTYLLVSKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRvVPTAEDVPKLP---LI 299
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 359 ELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFKSVPF 438
Cdd:cd20647 300 RALLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRVDNFGSIPF 379
                       170       180       190
                ....*....|....*....|....*....|
gi 19921820 439 SAGPRRCIAEKFAMYQMKALLSQLLRRFEI 468
Cdd:cd20647 380 GYGIRSCIGRRIAELEIHLALIQLLQNFEI 409
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
105-467 3.28e-25

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: 108.10  E-value: 3.28e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 105 HLYSFLRPWLGDGLLTSSgarwlkHQKLYAPAFERsAIEGYLRVVH---RTGGQFVQKLDVLSDTqeVFdaqelvakCTL 181
Cdd:cd11075  62 PLWRTLRRNLVSEVLSPS------RLKQFRPARRR-ALDNLVERLReeaKENPGPVNVRDHFRHA--LF--------SLL 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 182 DIVCenatgqdssslNGETSDlHGAIKDLcDVVQERTFSIVKRFD--ALF-RLTSYYMKQR--RALSLLRSE---LNRII 253
Cdd:cd11075 125 LYMC-----------FGERLD-EETVREL-ERVQRELLLSFTDFDvrDFFpALTWLLNRRRwkKVLELRRRQeevLLPLI 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 254 SQRRHQLAAENTCQQgqPINKPFLDVLLTAKLDGK-VLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAA 332
Cdd:cd11075 192 RARRKRRASGEADKD--YTDFLLLDLLDLKEEGGErKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLY 269
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 333 EEQRRIFGEN-FAGEADLarlDQMHYLELIIRETLRLYPSVP-LIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYF 410
Cdd:cd11075 270 EEIKEVVGDEaVVTEEDL---PKMPYLKAVVLETLRRHPPGHfLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVW 346
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19921820 411 DDPCTFRPERF----ENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd11075 347 EDPEEFKPERFlaggEAADIDTGSKEIKMMPFGAGRRICPGLGLATLHLELFVARLVQEFE 407
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
302-478 1.01e-24

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: 106.53  E-value: 1.01e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 302 FIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfageadlaRL------DQMHYLELIIRETLRLYPSVPL- 374
Cdd:cd20651 233 LFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRD--------RLptlddrSKLPYTEAVILEVLRIFTLVPIg 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 375 IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAfKSVPFSAGPRRCIAEKFAMYQ 454
Cdd:cd20651 305 IPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDE-WFLPFGAGKRRCLGESLARNE 383
                       170       180
                ....*....|....*....|....
gi 19921820 455 MKALLSQLLRRFEILPAVDGLPPG 478
Cdd:cd20651 384 LFLFFTGLLQNFTFSPPNGSLPDL 407
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
32-478 2.19e-23

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 103.36  E-value: 2.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   32 MEMIPGPTPYPFVGNLFQFGLKPAeypKKVLQYCRKYDfqgfrSLVFLQY----HMMLSDPAEIQNIL--------SSSS 99
Cdd:PLN03112  31 LRLPPGPPRWPIVGNLLQLGPLPH---RDLASLCKKYG-----PLVYLRLgsvdAITTDDPELIREILlrqddvfaSRPR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  100 LLYKEHL-YSflrpwLGDGLLTSSGARWLK------HQKLYAPAFERSAIEGYLRVVHrtggqFVQKLDVLSDTQEVFDA 172
Cdd:PLN03112 103 TLAAVHLaYG-----CGDVALAPLGPHWKRmrricmEHLLTTKRLESFAKHRAEEARH-----LIQDVWEAAQTGKPVNL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  173 QELVAKCTLDIVCENATGQDSSslnGETSDLHGAIKDLCDVVQErtfsivkrfdaLFRLTSY-----YMKQRRALSL--- 244
Cdd:PLN03112 173 REVLGAFSMNNVTRMLLGKQYF---GAESAGPKEAMEFMHITHE-----------LFRLLGViylgdYLPAWRWLDPygc 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  245 ------LRSEL----NRIISQrrHQLAAENTCQQGQPINkpFLDVLLT-AKLDGKV-LKEREIIEEVSTFIFTGHDPIAA 312
Cdd:PLN03112 239 ekkmreVEKRVdefhDKIIDE--HRRARSGKLPGGKDMD--FVDVLLSlPGENGKEhMDDVEIKALMQDMIAAATDTSAV 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  313 AISFTLYTLSRHSEIQQKAAEEQRRIFGEN-FAGEADLArldQMHYLELIIRETLRLYPSVP-LIARTNRNPIDINGTKV 390
Cdd:PLN03112 315 TNEWAMAEVIKNPRVLRKIQEELDSVVGRNrMVQESDLV---HLNYLRCVVRETFRMHPAGPfLIPHESLRATTINGYYI 391
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  391 AKCTTVIMCLIAMGYNEKYFDDPCTFRPER-FENPTGNVGIE---AFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:PLN03112 392 PAKTRVFINTHGLGRNTKIWDDVEEFRPERhWPAEGSRVEIShgpDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCF 471
                        490
                 ....*....|..
gi 19921820  467 EILPAvDGLPPG 478
Cdd:PLN03112 472 DWSPP-DGLRPE 482
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
114-469 2.27e-23

cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; Cytochrome P450 5A1 (CYP5A1), also called thromboxane-A synthase (EC 5.3.99.5) or thromboxane synthetase, converts prostaglandin H2 into thromboxane A2, a biologically active metabolite of arachidonic acid that has been implicated in stroke, asthma, and various cardiovascular diseases, due to its acute and chronic effects in promoting platelet aggregation, vasoconstriction, bronchoconstriction, and proliferation. CYP5A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410742 [Multi-domain]  Cd Length: 457  Bit Score: 102.61  E-value: 2.27e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 114 LGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDIVCENATG-QD 192
Cdd:cd20649  48 MSDSLLCLRDERWKRVRSILTPAFSAAKMKEMVPLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGtQV 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 193 SSSLNGETSDLHGAikdlcdvvqERTFSIVKRFDALFRLTSYYMKQRRALSLL----RSELN--------RIISQRRHQL 260
Cdd:cd20649 128 DSQKNPDDPFVKNC---------KRFFEFSFFRPILILFLAFPFIMIPLARILpnksRDELNsfftqcirNMIAFRDQQS 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 261 AAE----------NTCQQGQPINKPFLDVLLTAKLDG-------------------KVLKEREIIEEVSTFIFTGHDPIA 311
Cdd:cd20649 199 PEErrrdflqlmlDARTSAKFLSVEHFDIVNDADESAydghpnspaneqtkpskqkRMLTEDEIVGQAFIFLIAGYETTT 278
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 312 AAISFTLYTLSRHSEIQQKAAEEQRRIFGENFagEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVA 391
Cdd:cd20649 279 NTLSFATYLLATHPECQKKLLREVDEFFSKHE--MVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIP 356
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19921820 392 KCTTVIMCLIAMGYNEKYFDDPCTFRPERFeNPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIL 469
Cdd:cd20649 357 AGAVLEIPVGFLHHDPEHWPEPEKFIPERF-TAEAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQ 433
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
226-470 3.02e-23

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: 102.05  E-value: 3.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 226 DALFRLTSYYMKQRRALSLLRSELNRIISQRRHQLAAENTCQQgqpiNKPFLDVLLTAKLDGKVLKE--REIIEEVstfI 303
Cdd:cd20616 161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLED----HMDFATELIFAQKRGELTAEnvNQCVLEM---L 233
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 304 FTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLArldQMHYLELIIRETLRLYPSVPLIARTNRNPI 383
Cdd:cd20616 234 IAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQ---KLKVLENFINESMRYQPVVDFVMRKALEDD 310
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 384 DINGTKVAKCTTVIMCLIAMGYNEkYFDDPCTFRPERFENptgNVGIEAFKsvPFSAGPRRCIAEKFAMYQMKALLSQLL 463
Cdd:cd20616 311 VIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFEK---NVPSRYFQ--PFGFGPRSCVGKYIAMVMMKAILVTLL 384

                ....*..
gi 19921820 464 RRFEILP 470
Cdd:cd20616 385 RRFQVCT 391
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
276-477 1.21e-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: 1.21e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 276 FLDVLLTAKlDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFG-ENFAGEADLARLDq 354
Cdd:cd20656 213 HFVALLTLK-EQYDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGsDRVMTEADFPQLP- 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 355 mhYLELIIRETLRLYPSVPLIA--RTNRNpIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEA 432
Cdd:cd20656 291 --YLQCVVKEALRLHPPTPLMLphKASEN-VKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKGHD 367
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 19921820 433 FKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAvDGLPP 477
Cdd:cd20656 368 FRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHFSWTPP-EGTPP 411
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
87-470 2.16e-22

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 100.24  E-value: 2.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   87 DPAEIQNILSSSSLLY-KEHLY-SFLRPWLGDGLLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRtggQFVQKL-DVL 163
Cdd:PLN03195  82 DPVNVEHVLKTNFANYpKGEVYhSYMEVLLGDGIFNVDGELWRKQRKTASFEFASKNLRDFSTVVFR---EYSLKLsSIL 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  164 SD---TQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIK-DLCDVVQERTFsivkrFDALFRLTSYYMKQR 239
Cdd:PLN03195 159 SQasfANQVVDMQDLFMRMTLDSICKVGFGVEIGTLSPSLPENPFAQAfDTANIIVTLRF-----IDPLWKLKKFLNIGS 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  240 RALsLLRSE------LNRIISQRRHQLaaENTCQQGQPINKPFLD--VLLTAKLDGKvLKEREIIEEVSTFIFTGHDPIA 311
Cdd:PLN03195 234 EAL-LSKSIkvvddfTYSVIRRRKAEM--DEARKSGKKVKHDILSrfIELGEDPDSN-FTDKSLRDIVLNFVIAGRDTTA 309
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  312 AAISFTLYTLSRHSEIQQK------AAEEQR---------RIFGENFAGEADLARLD---QMHYLELIIRETLRLYPSVP 373
Cdd:PLN03195 310 TTLSWFVYMIMMNPHVAEKlyselkALEKERakeedpedsQSFNQRVTQFAGLLTYDslgKLQYLHAVITETLRLYPAVP 389
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  374 LiartnrNPIDI-------NGTKVAKCTTVIMCLIAMGYNE-KYFDDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRC 445
Cdd:PLN03195 390 Q------DPKGIleddvlpDGTKVKAGGMVTYVPYSMGRMEyNWGPDAASFKPERWIKDGVFQNASPFKFTAFQAGPRIC 463
                        410       420
                 ....*....|....*....|....*..
gi 19921820  446 IAEKFAMYQMKALLSQLLR--RFEILP 470
Cdd:PLN03195 464 LGKDSAYLQMKMALALLCRffKFQLVP 490
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
214-467 6.48e-22

cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the biosynthesis of colored class of flavonoids, anthocyanins, which confer a diverse range of colors to flowers from orange to red to violet and blue. The number of hydroxyl groups on the B-ring of anthocyanidins, the chromophores and precursors of anthocyanins, impact the anthocyanin color - the more the bluer. The hydroxylation pattern is determined by CYP75 proteins: flavonoid 3'-hydroxylase (F3'H, EC 1.14.14.82) and and flavonoid 3',5'-hydroxylase (F3'5'H, EC 1.14.14.81), which belong to CYP75B and CYP75A subfamilies, respectively. Both enzymes have broad substrate specificity and catalyze the hydroxylation of flavanones, dihydroflavonols, flavonols and flavones. F3'H catalyzes the 3'-hydroxylation of the flavonoid B-ring to the 3',4'-hydroxylated state. F3'5'H catalysis leads to trihydroxylated delphinidin-based anthocyanins that tend to have violet/blue colours. CYP75 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 98.26  E-value: 6.48e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 214 VQERTFSIVKRFDALfrltsyymkqrralsllrseLNRIISQrrHQLAAentcqQGQPINKPFLDVLLTAKL---DGKVL 290
Cdd:cd20657 172 VEKKMKRLHKRFDAL--------------------LTKILEE--HKATA-----QERKGKPDFLDFVLLENDdngEGERL 224
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 291 KEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGEN-FAGEADLARLDqmhYLELIIRETLRLY 369
Cdd:cd20657 225 TDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDrRLLESDIPNLP---YLQAICKETFRLH 301
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 370 PSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFEnPTGNVGIEA----FKSVPFSAGPRR 444
Cdd:cd20657 302 PSTPLnLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFL-PGRNAKVDVrgndFELIPFGAGRRI 380
                       250       260
                ....*....|....*....|...
gi 19921820 445 CIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd20657 381 CAGTRMGIRMVEYILATLVHSFD 403
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
118-481 1.88e-21

cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus cytochrome P450 64 (CYP64), also called O-methylsterigmatocystin (OMST) oxidoreductase or aflatoxin B synthase or aflatoxin biosynthesis protein Q, and similar fungal cytochrome P450s. CYP64 converts OMST to aflatoxin B1 and converts dihydro-O-methylsterigmatocystin (DHOMST) to aflatoxin B2 in the aflatoxin biosynthesis pathway. The CYP64-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410688 [Multi-domain]  Cd Length: 425  Bit Score: 96.49  E-value: 1.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 118 LLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFVqkLDVLSDTQEVFDAqelVAKCTLDIVCENATGQDSSS-- 195
Cdd:cd11065  54 LLMPYGPRWRLHRRLFHQLLNPSAVRKYRPLQELESKQLL--RDLLESPDDFLDH---IRRYAASIILRLAYGYRVPSyd 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 196 ---------LNGETSDLHGAIKDLCDVvqertFSIVKR----FDALFRLTSYYMKqRRALSLLRSELNRIISQRRHQLAA 262
Cdd:cd11065 129 dpllrdaeeAMEGFSEAGSPGAYLVDF-----FPFLRYlpswLGAPWKRKARELR-ELTRRLYEGPFEAAKERMASGTAT 202
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 263 ENtcqqgqpinkpFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAI-SFTLYtLSRHSEIQQKAAEEQRRIFGE 341
Cdd:cd11065 203 PS-----------FVKDLLEELDKEGGLSEEEIKYLAGSLYEAGSDTTASTLqTFILA-MALHPEVQKKAQEELDRVVGP 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 342 N-FAGEADLARLdqmHYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPE 419
Cdd:cd11065 271 DrLPTFEDRPNL---PYVNAIVKEVLRWRPVAPLgIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPE 347
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921820 420 RF-ENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDGLPPGIND 481
Cdd:cd11065 348 RYlDDPKGTPDPPDPPHFAFGFGRRICPGRHLAENSLFIAIARLLWAFDIKKPKDEGGKEIPD 410
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
290-485 2.12e-21

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


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 96.41  E-value: 2.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 290 LKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADlaRLDQMHYLELIIRETLRLY 369
Cdd:cd20645 222 LSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAE--DLKNMPYLKACLKESMRLT 299
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 370 PSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNvgIEAFKSVPFSAGPRRCIAEK 449
Cdd:cd20645 300 PSVPFTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQEKHS--INPFAHVPFGIGKRMCIGRR 377
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 19921820 450 FAMYQMKALLSQLLRRFEILPA----VDGLPPGINDHSRE 485
Cdd:cd20645 378 LAELQLQLALCWIIQKYQIVATdnepVEMLHSGILVPSRE 417
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
277-476 3.35e-21

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: 95.85  E-value: 3.35e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 277 LDVLLTAKL-----------DGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGenFAG 345
Cdd:cd20673 204 LDALLQAKMnaennnagpdqDSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIG--FSR 281
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 346 EADLARLDQMHYLELIIRETLRLYPSVP-LIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENP 424
Cdd:cd20673 282 TPTLSDRNHLPLLEATIREVLRIRPVAPlLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDP 361
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 19921820 425 TGNVGIEAFKS-VPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI-LPAVDGLP 476
Cdd:cd20673 362 TGSQLISPSLSyLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLeVPDGGQLP 415
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
249-470 1.29e-20

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: 94.32  E-value: 1.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 249 LNRIISQRRhqlaaentcQQGQPINKPFL---DVLLTAKLDGKvLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHS 325
Cdd:cd11076 186 VGKIIEEHR---------AKRSNRARDDEddvDVLLSLQGEEK-LSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHP 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 326 EIQQKAAEEQRRIFGENFAG-EADLARLDqmhYLELIIRETLRLYPSVPLI--ARTNRNPIDINGTKVAKCTTVIMCLIA 402
Cdd:cd11076 256 DIQSKAQAEIDAAVGGSRRVaDSDVAKLP---YLQAVVKETLRLHPPGPLLswARLAIHDVTVGGHVVPAGTTAMVNMWA 332
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921820 403 MGYNEKYFDDPCTFRPERFENPTGNVGIEAFKS----VPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILP 470
Cdd:cd11076 333 ITHDPHVWEDPLEFKPERFVAAEGGADVSVLGSdlrlAPFGAGRRVCPGKALGLATVHLWVAQLLHEFEWLP 404
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
235-480 1.75e-20

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: 93.92  E-value: 1.75e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 235 YMKQRraLSLLRSELNRIISQRRHqlAAENTCQQGQpinkpfldvLLTAKLDGKVLKEREIIeeVSTFIFTGHDPIAAAI 314
Cdd:cd11066 184 YRNRR--DKYLKKLLAKLKEEIED--GTDKPCIVGN---------ILKDKESKLTDAELQSI--CLTMVSAGLDTVPLNL 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 315 SFTLYTLSRH--SEIQQKAAEEQRRIFGENFAGEADLARLDQMHYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVA 391
Cdd:cd11066 249 NHLIGHLSHPpgQEIQEKAYEEILEAYGNDEDAWEDCAAEEKCPYVVALVKETLRYFTVLPLgLPRKTTKDIVYNGAVIP 328
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 392 KCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFKsVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPA 471
Cdd:cd11066 329 AGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPH-FSFGAGSRMCAGSHLANRELYTAICRLILLFRIGPK 407

                ....*....
gi 19921820 472 VDGLPPGIN 480
Cdd:cd11066 408 DEEEPMELD 416
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
219-478 6.05e-20

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: 92.21  E-value: 6.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 219 FSIVKRFD--ALFRLTSYYMKqrRALSLLRselnRIISQRRhqlaaENTCQQGQPINKPFLDVLLTAKLDGKVLKEREII 296
Cdd:cd11073 164 FPFLKFLDlqGLRRRMAEHFG--KLFDIFD----GFIDERL-----AEREAGGDKKKDDDLLLLLDLELDSESELTRNHI 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 297 EEVSTFIFT-GHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGEN-FAGEADLARLdqmHYLELIIRETLRLYPSVP- 373
Cdd:cd11073 233 KALLLDLFVaGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDkIVEESDISKL---PYLQAVVKETLRLHPPAPl 309
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 374 LIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMY 453
Cdd:cd11073 310 LLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKGRDFELIPFGSGRRICPGLPLAER 389
                       250       260
                ....*....|....*....|....*.
gi 19921820 454 QMKALLSQLLRRFE-ILPavDGLPPG 478
Cdd:cd11073 390 MVHLVLASLLHSFDwKLP--DGMKPE 413
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
114-468 9.70e-20

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 92.06  E-value: 9.70e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  114 LGDGLLTSSGARWLKHQKLYAPAFERSAIEGY-LRVV-----HRTggqfvqkLDVLSD-----TQEVFDAQELVAKCTLD 182
Cdd:PLN02426 119 LGRGIFNVDGDSWRFQRKMASLELGSVSIRSYaFEIVaseieSRL-------LPLLSSaaddgEGAVLDLQDVFRRFSFD 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  183 IVCENATGQDSSSLNGE--TSDLHGAIKDLCDVVQERT---FSIVKRFDALFRLTSYyMKQRRALSLLRSELNRIISQRR 257
Cdd:PLN02426 192 NICKFSFGLDPGCLELSlpISEFADAFDTASKLSAERAmaaSPLLWKIKRLLNIGSE-RKLKEAIKLVDELAAEVIRQRR 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  258 hqlaaentcQQGQPINKPFLDVLLTAKLDGKVLkeREIieeVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRR 337
Cdd:PLN02426 271 ---------KLGFSASKDLLSRFMASINDDKYL--RDI---VVSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADR 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  338 IFGENFAgEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPiDI--NGTKVAKCTTVIMCLIAMGYNEKYFDDPC- 414
Cdd:PLN02426 337 VMGPNQE-AASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAED-DVlpDGTFVAKGTRVTYHPYAMGRMERIWGPDCl 414
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921820  415 TFRPERF--------ENPtgnvgieaFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI 468
Cdd:PLN02426 415 EFKPERWlkngvfvpENP--------FKYPVFQAGLRVCLGKEMALMEMKSVAVAVVRRFDI 468
PLN02302 PLN02302
ent-kaurenoic acid oxidase
232-471 1.75e-19

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 91.31  E-value: 1.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  232 TSYY--MKQRRALSLLrseLNRIISQRRHQLAaentcQQGQPINKPFLDVLLTAKLD-GKVLKEREIIEEVSTFIFTGHD 308
Cdd:PLN02302 230 FAYHraLKARKKLVAL---FQSIVDERRNSRK-----QNISPRKKDMLDLLLDAEDEnGRKLDDEEIIDLLLMYLNAGHE 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  309 PIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLARLD--QMHYLELIIRETLRLYPSVPLIARTNRNPIDIN 386
Cdd:PLN02302 302 SSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKKRPPGQKGLTLKDvrKMEYLSQVIDETLRLINISLTVFREAKTDVEVN 381
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  387 GTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTgnvgIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:PLN02302 382 GYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYT----PKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGY 457

                 ....*
gi 19921820  467 EILPA 471
Cdd:PLN02302 458 RLERL 462
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
239-480 2.03e-19

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: 90.50  E-value: 2.03e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 239 RRALSLLRSELNRIISQRRHQLAaentcQQGQPINKPFLDVLLTAK-LDGK-VLKEREIIEEVSTFIFTGHDPIAAAISF 316
Cdd:cd20658 185 REAMRIIRKYHDPIIDERIKQWR-----EGKKKEEEDWLDVFITLKdENGNpLLTPDEIKAQIKELMIAAIDNPSNAVEW 259
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 317 TLYTLSRHSEIQQKAAEEQRRIFG-ENFAGEADLARLDqmhYLELIIRETLRLYPSVP-LIARTNRNPIDINGTKVAKCT 394
Cdd:cd20658 260 ALAEMLNQPEILRKATEELDRVVGkERLVQESDIPNLN---YVKACAREAFRLHPVAPfNVPHVAMSDTTVGGYFIPKGS 336
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 395 TVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEA--FKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPav 472
Cdd:cd20658 337 HVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEVTLTEpdLRFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTL-- 414

                ....*...
gi 19921820 473 dglPPGIN 480
Cdd:cd20658 415 ---PPNVS 419
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
83-467 4.97e-19

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 90.07  E-value: 4.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   83 MMLSDPAEIQNILSSSSLLY-KEHLYSFLRPWLGDGLLTSSGARWLKHQKLYAPAFERsaiEGYLRVVHRTGGQ-----F 156
Cdd:PLN02169  83 LFTADPKNIHHILSSNFGNYpKGPEFKKIFDVLGEGILTVDFELWEDLRKSNHALFHN---QDFIELSLSSNKSklkegL 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  157 VQKLDVLSDTQEVFDAQELVAKCTLDIVCENATGQDSSSLNGETsdLHGAIKDLCDVVQERTFSIVKRFDALFRLTSYY- 235
Cdd:PLN02169 160 VPFLDNAAHENIIIDLQDVFMRFMFDTSSILMTGYDPMSLSIEM--LEVEFGEAADIGEEAIYYRHFKPVILWRLQNWIg 237
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  236 ----MKQRRALSLLRSELNRIISQRRHQlaaENTCQQGQPINKPFLDVLLTAKLDG-KVLKERE---IIEEVSTFIFTGH 307
Cdd:PLN02169 238 igleRKMRTALATVNRMFAKIISSRRKE---EISRAETEPYSKDALTYYMNVDTSKyKLLKPKKdkfIRDVIFSLVLAGR 314
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  308 DPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFgenfageaDLARLDQMHYLELIIRETLRLYPSVPLIARTNRNP-IDIN 386
Cdd:PLN02169 315 DTTSSALTWFFWLLSKHPQVMAKIRHEINTKF--------DNEDLEKLVYLHAALSESMRLYPPLPFNHKAPAKPdVLPS 386
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  387 GTKVAKCTTVIMCLIAMGYNEKYF-DDPCTFRPERFENPTGNVGIE-AFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLR 464
Cdd:PLN02169 387 GHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGLRHEpSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIK 466

                 ...
gi 19921820  465 RFE 467
Cdd:PLN02169 467 NYD 469
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
286-478 9.90e-19

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: 88.27  E-value: 9.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 286 DGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRifgenfAGEADL--ARLDQMHYLELIIR 363
Cdd:cd20614 200 NGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAA------AGDVPRtpAELRRFPLAEALFR 273
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 364 ETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGnvGIEAFKSVPFSAGPR 443
Cdd:cd20614 274 ETLRLHPPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDR--APNPVELLQFGGGPH 351
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19921820 444 RCIAEKFA---MYQMKALLSQLLRRFEILPAVDGLPPG 478
Cdd:cd20614 352 FCLGYHVAcveLVQFIVALARELGAAGIRPLLVGVLPG 389
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
242-468 2.85e-18

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: 86.97  E-value: 2.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 242 LSLLRSELNRIISQRRHQLAaenTCQQGQPinKPFLDVLLTAKLDGK-------VLKEREIIEEVSTFIFTGHDPIAAAI 314
Cdd:cd11028 177 KELLNRLNSFILKKVKEHLD---TYDKGHI--RDITDALIKASEEKPeeekpevGLTDEHIISTVQDLFGAGFDTISTTL 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 315 SFTLYTLSRHSEIQQKAAEEQRRIFGENfageaDLARLDQMH---YLELIIRETLRLYPSVPL-IAR-TNRNPIdINGTK 389
Cdd:cd11028 252 QWSLLYMIRYPEIQEKVQAELDRVIGRE-----RLPRLSDRPnlpYTEAFILETMRHSSFVPFtIPHaTTRDTT-LNGYF 325
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 390 VAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVG---IEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:cd11028 326 IPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDktkVDKF--LPFGAGRRRCLGEELARMELFLFFATLLQQC 403

                ..
gi 19921820 467 EI 468
Cdd:cd11028 404 EF 405
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
276-479 1.19e-17

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: 85.24  E-value: 1.19e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 276 FLDVLLTAKLDGK-----VLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfagEADLA 350
Cdd:cd20664 202 FIDAFLVKQQEEEessdsFFHDDNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSR---QPQVE 278
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 351 RLDQMHYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGN-V 428
Cdd:cd20664 279 HRKNMPYTDAVIHEIQRFANIVPMnLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKfV 358
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 19921820 429 GIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPavdglPPGI 479
Cdd:cd20664 359 KRDAF--MPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQP-----PPGV 402
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
237-479 1.46e-17

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: 85.04  E-value: 1.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 237 KQRRALSLLRSELNRIISQRRHQlaaentcQQGQPINKP--FLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAI 314
Cdd:cd11041 175 RLRRLLRRARPLIIPEIERRRKL-------KKGPKEDKPndLLQWLIEAAKGEGERTPYDLADRQLALSFAAIHTTSMTL 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 315 SFTLYTLSRHSEIQQKAAEEQRRIFGENfaGEADLARLDQMHYLELIIRETLRLYPSVPL-IARTNRNPIDI-NGTKVAK 392
Cdd:cd11041 248 THVLLDLAAHPEYIEPLREEIRSVLAEH--GGWTKAALNKLKKLDSFMKESQRLNPLSLVsLRRKVLKDVTLsDGLTLPK 325
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 393 CTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEA---FKSV-----PFSAGPRRCIAEKFAMYQMKALLSQLLR 464
Cdd:cd11041 326 GTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQEKkhqFVSTspdflGFGHGRHACPGRFFASNEIKLILAHLLL 405
                       250
                ....*....|....*.
gi 19921820 465 RFEI-LPAVDGLPPGI 479
Cdd:cd11041 406 NYDFkLPEGGERPKNI 421
PLN02687 PLN02687
flavonoid 3'-monooxygenase
249-445 2.13e-17

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 84.86  E-value: 2.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  249 LNRIIsqRRHQLAAENTCQQGqpinKPFLDVLLT------AKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLS 322
Cdd:PLN02687 252 MNGII--EEHKAAGQTGSEEH----KDLLSTLLAlkreqqADGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELI 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  323 RHSEIQQKAAEEQRRIFGEN-FAGEADLARLDqmhYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCL 400
Cdd:PLN02687 326 RHPDILKKAQEELDAVVGRDrLVSESDLPQLT---YLQAVIKETFRLHPSTPLsLPRMAAEECEINGYHIPKGATLLVNV 402
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 19921820  401 IAMGYNEKYFDDPCTFRPERF----ENPTGNVGIEAFKSVPFSAGPRRC 445
Cdd:PLN02687 403 WAIARDPEQWPDPLEFRPDRFlpggEHAGVDVKGSDFELIPFGAGRRIC 451
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
249-467 2.81e-17

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 84.52  E-value: 2.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  249 LNRIISQrrHQLAAENtcQQGQPinkPFLDVLLTAK--LDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSE 326
Cdd:PLN00110 249 LTRMIEE--HTASAHE--RKGNP---DFLDVVMANQenSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPS 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  327 IQQKAAEEQRRIFGEN-FAGEADLARLDqmhYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAMG 404
Cdd:PLN00110 322 ILKRAHEEMDQVIGRNrRLVESDLPKLP---YLQAICKESFRKHPSTPLnLPRVSTQACEVNGYYIPKNTRLSVNIWAIG 398
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  405 YNEKYFDDPCTFRPERFE-------NPTGNvgieAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:PLN00110 399 RDPDVWENPEEFRPERFLseknakiDPRGN----DFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFD 464
PLN02966 PLN02966
cytochrome P450 83A1
36-477 2.97e-17

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 84.41  E-value: 2.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   36 PGPTPYPFVGNLFQF-GLKPAEYpkkVLQYCRKY----DFQ-GFRSLVFLQYHMMLSDPAEIQNILSSSSLLYKEHLY-S 108
Cdd:PLN02966  32 PGPSPLPVIGNLLQLqKLNPQRF---FAGWAKKYgpilSYRiGSRTMVVISSAELAKELLKTQDVNFADRPPHRGHEFiS 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  109 FLRPWLGDGLLTS--SGARWLKHQKLYAPaferSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDIVCE 186
Cdd:PLN02966 109 YGRRDMALNHYTPyyREIRKMGMNHLFSP----TRVATFKHVREEEARRMMDKINKAADKSEVVDISELMLTFTNSVVCR 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  187 NATG----QDSSSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSYyMKQ--RRALSLLRSELNRIISQRRHQl 260
Cdd:PLN02966 185 QAFGkkynEDGEEMKRFIKILYGTQSVLGKIFFSDFFPYCGFLDDLSGLTAY-MKEcfERQDTYIQEVVNETLDPKRVK- 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  261 aaentcqqgqPINKPFLDVLLtakldgKVLKEREIIEEVST---------FIFTGHDPIAAAISFTLYTLSRHSEIQQKA 331
Cdd:PLN02966 263 ----------PETESMIDLLM------EIYKEQPFASEFTVdnvkavildIVVAGTDTAAAAVVWGMTYLMKYPQVLKKA 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  332 AEEQRRIF---GENFAGEADLARLDqmhYLELIIRETLRLYPSVP-LIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNE 407
Cdd:PLN02966 327 QAEVREYMkekGSTFVTEDDVKNLP---YFRALVKETLRIEPVIPlLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDE 403
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921820  408 KYFD-DPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI-LPavDGLPP 477
Cdd:PLN02966 404 KEWGpNPDEFRPERFLEKEVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFkLP--NGMKP 473
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
236-478 3.77e-17

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 84.01  E-value: 3.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  236 MKQRRaLSLLRselNRIISQRRHQLAAENTCQQGQpinKPFLDVLLTAKLDGkvlkerEIIEEVSTFIFTGHDpiAAAIS 315
Cdd:PLN02394 243 VKERR-LALFK---DYFVDERKKLMSAKGMDKEGL---KCAIDHILEAQKKG------EINEDNVLYIVENIN--VAAIE 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  316 FTLYT-------LSRHSEIQQKAAEEQRRIFGE-NFAGEADLARLDqmhYLELIIRETLRLYPSVPL-IARTNRNPIDIN 386
Cdd:PLN02394 308 TTLWSiewgiaeLVNHPEIQKKLRDELDTVLGPgNQVTEPDTHKLP---YLQAVVKETLRLHMAIPLlVPHMNLEDAKLG 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  387 GTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGnvGIEA----FKSVPFSAGPRRCIAEKFAMYQMKALLSQL 462
Cdd:PLN02394 385 GYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEA--KVEAngndFRFLPFGVGRRSCPGIILALPILGIVLGRL 462
                        250
                 ....*....|....*.
gi 19921820  463 LRRFEILPavdglPPG 478
Cdd:PLN02394 463 VQNFELLP-----PPG 473
PLN02655 PLN02655
ent-kaurene oxidase
249-488 6.92e-17

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 83.25  E-value: 6.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  249 LNRIISQRRHQLA--AENTCqqgqpinkpFLDVLLTAKldgKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSE 326
Cdd:PLN02655 227 MKALIKQQKKRIArgEERDC---------YLDFLLSEA---THLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPD 294
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  327 IQQKAAEEQRRIFGENFAGEADLARLDqmhYLELIIRETLRLYPSVPLI-ARTNRNPIDINGTKVAKCTTVIMCLIAMGY 405
Cdd:PLN02655 295 KQERLYREIREVCGDERVTEEDLPNLP---YLNAVFHETLRKYSPVPLLpPRFVHEDTTLGGYDIPAGTQIAINIYGCNM 371
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  406 NEKYFDDPCTFRPERFENPTGNVGiEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIlpavdGLPPGinDHSRE 485
Cdd:PLN02655 372 DKKRWENPEEWDPERFLGEKYESA-DMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEW-----RLREG--DEEKE 443

                 ...
gi 19921820  486 DCV 488
Cdd:PLN02655 444 DTV 446
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
85-482 1.33e-16

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


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 82.35  E-value: 1.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  85 LSDPAEIQNILSSSSLLYkeHLYSFLRPWLGD-----GLLTSSGARWLKH----QKLYAPAFERSAIEGYLrvvHRTGGQ 155
Cdd:cd20622  18 VADFREAQDILMRRTKEF--DRSDFTIDVFGGigphhHLVKSTGPAFRKHrslvQDLMTPSFLHNVAAPAI---HSKFLD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 156 FVQKLDV---LSDTQEvFDAQELVAKCTLDIVCENATGQ-----------------DSSSLNG-----------ETSDLH 204
Cdd:cd20622  93 LIDLWEAkarLAKGRP-FSAKEDIHHAALDAIWAFAFGInfdasqtrpqlelleaeDSTILPAgldepvefpeaPLPDEL 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 205 GAIKDLCDVVQERTFSIVKRFDALF-RLTSYYMKQRRALSllrselNRIISQRRHQLAAENTCQQGQPInKPFLDVLLTA 283
Cdd:cd20622 172 EAVLDLADSVEKSIKSPFPKLSHWFyRNQPSYRRAAKIKD------DFLQREIQAIARSLERKGDEGEV-RSAVDHMVRR 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 284 KldgKVLKERE----------IIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAgEADLARLD 353
Cdd:cd20622 245 E---LAAAEKEgrkpdyysqvIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPEAVA-EGRLPTAQ 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 354 QM-----HYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGY----------------NEK---- 408
Cdd:cd20622 321 EIaqariPYLDAVIEEILRCANTAPILSREATVDTQVLGYSIPKGTNVFLLNNGPSYlsppieidesrrssssAAKgkka 400
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 409 -YFD--DPCTFRPERF---ENPTGNV--GIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPavdgLPPGIN 480
Cdd:cd20622 401 gVWDskDIADFDPERWlvtDEETGETvfDPSAGPTLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLP----LPEALS 476

                ..
gi 19921820 481 DH 482
Cdd:cd20622 477 GY 478
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
295-466 3.41e-16

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: 80.63  E-value: 3.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 295 IIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfaGEADLARLDQMHYLELIIRETLRLYPSVPL 374
Cdd:cd20661 239 LIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPN--GMPSFEDKCKMPYTEAVLHEVLRFCNIVPL 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 375 -IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGN-VGIEAFksVPFSAGPRRCIAEKFAM 452
Cdd:cd20661 317 gIFHATSKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQfAKKEAF--VPFSLGRRHCLGEQLAR 394
                       170
                ....*....|....
gi 19921820 453 YQMKALLSQLLRRF 466
Cdd:cd20661 395 MEMFLFFTALLQRF 408
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
240-464 3.55e-16

cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It effectively metabolizes all-trans retinoic acid (atRA), 9-cis-retinoic acid (9-cis-RA), 13-cis-retinoic acid, and 4-oxo-atRA with the highest intrinsic clearance toward 9-cis-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. Loss of function mutations in the CYP26C1 gene cause type IV focal facial dermal dysplasia (FFDD), a rare syndrome characterized by facial lesions resembling aplasia cutis. CYP26C1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 80.65  E-value: 3.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 240 RALSLLRSELNRIISQRRHQLAAENTCQQgqpinkpfLDVLL-TAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTL 318
Cdd:cd20636 180 KARDILHEYMEKAIEEKLQRQQAAEYCDA--------LDYMIhSARENGKELTMQELKESAVELIFAAFSTTASASTSLV 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 319 YTLSRHSEIQQKAAEE--QRRIFGE--NFAGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCT 394
Cdd:cd20636 252 LLLLQHPSAIEKIRQElvSHGLIDQcqCCPGALSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFELDGYQIPKGW 331
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 395 TVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLR 464
Cdd:cd20636 332 SVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGRFNYIPFGGGVRSCIGKELAQVILKTLAVELVT 401
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
303-467 6.14e-16

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: 79.96  E-value: 6.14e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 303 IFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGEN-FAGEADLARLdqmHYLELIIRETLRLYPSVP-LIARTNR 380
Cdd:cd20653 236 LLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDrLIEESDLPKL---PYLQNIISETLRLYPAAPlLVPHESS 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 381 NPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFEnptgNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLS 460
Cdd:cd20653 313 EDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFE----GEEREGYKLIPFGLGRRACPGAGLAQRVVGLALG 388

                ....*..
gi 19921820 461 QLLRRFE 467
Cdd:cd20653 389 SLIQCFE 395
PLN02971 PLN02971
tryptophan N-hydroxylase
276-466 1.42e-15

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 79.31  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  276 FLDVLLTAKLDG--KVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFG-ENFAGEADLARL 352
Cdd:PLN02971 307 FLDIFISIKDEAgqPLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGkERFVQESDIPKL 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  353 DqmhYLELIIRETLRLYP----SVPLIARTNRNpidINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNV 428
Cdd:PLN02971 387 N---YVKAIIREAFRLHPvaafNLPHVALSDTT---VAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEV 460
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 19921820  429 GIEA--FKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:PLN02971 461 TLTEndLRFISFSTGKRGCAAPALGTAITTMMLARLLQGF 500
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
303-469 2.37e-15

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: 78.04  E-value: 2.37e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 303 IFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFG-ENFAGEADLARLDqmhYLELIIRETLRLYPSVPLIA-RTNR 380
Cdd:cd20654 250 ILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGkDRWVEESDIKNLV---YLQAIVKETLRLYPPGPLLGpREAT 326
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 381 NPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERF--ENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKAL 458
Cdd:cd20654 327 EDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFltTHKDIDVRGQNFELIPFGSGRRSCPGVSFGLQVMHLT 406
                       170
                ....*....|.
gi 19921820 459 LSQLLRRFEIL 469
Cdd:cd20654 407 LARLLHGFDIK 417
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
203-478 2.56e-15

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: 77.90  E-value: 2.56e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 203 LHGAIKdLCDVVQERTFsivkrfdALFRltSYYMKQRRALSLLRSELNRIIsqrrhqlaaentcqqgqpinKPFLDVLLT 282
Cdd:cd11074 173 LRGYLK-ICKEVKERRL-------QLFK--DYFVDERKKLGSTKSTKNEGL--------------------KCAIDHILD 222
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 283 AKLDGkvlkerEIIEEVSTFIFTGHDpiAAAISFTLYT-------LSRHSEIQQKAAEEQRRIFGENFA-GEADLARLDq 354
Cdd:cd11074 223 AQKKG------EINEDNVLYIVENIN--VAAIETTLWSiewgiaeLVNHPEIQKKLRDELDTVLGPGVQiTEPDLHKLP- 293
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 355 mhYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEA- 432
Cdd:cd11074 294 --YLQAVVKETLRLRMAIPLlVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKVEANGn 371
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 19921820 433 -FKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPavdglPPG 478
Cdd:cd11074 372 dFRYLPFGVGRRSCPGIILALPILGITIGRLVQNFELLP-----PPG 413
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
291-463 2.66e-15

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: 77.67  E-value: 2.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 291 KEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGeNFAGEADLARLDQMHYLELIIRETLRLYP 370
Cdd:cd11082 217 SDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRP-NDEPPLTLDLLEEMKYTRQVVKEVLRYRP 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 371 SVPLIARTNRNPIDIN-GTKVAKCTTVIMCLIAMGYNEkyFDDPCTFRPERFeNPTGNVGIEAFK-SVPFSAGPRRCIAE 448
Cdd:cd11082 296 PAPMVPHIAKKDFPLTeDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRF-SPERQEDRKYKKnFLVFGAGPHQCVGQ 372
                       170
                ....*....|....*...
gi 19921820 449 KFAMYQMK---ALLSQLL 463
Cdd:cd11082 373 EYAINHLMlflALFSTLV 390
PLN02183 PLN02183
ferulate 5-hydroxylase
293-477 2.99e-15

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 78.35  E-value: 2.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  293 REIIEEVstfIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFG-ENFAGEADLARLDqmhYLELIIRETLRLYPS 371
Cdd:PLN02183 306 KAIIMDV---MFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGlNRRVEESDLEKLT---YLKCTLKETLRLHPP 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  372 VPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPtgnvGIEAFKS-----VPFSAGPRRCI 446
Cdd:PLN02183 380 IPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKP----GVPDFKGshfefIPFGSGRRSCP 455
                        170       180       190
                 ....*....|....*....|....*....|..
gi 19921820  447 AEKFAMYQMKALLSQLLRRFEI-LPavDGLPP 477
Cdd:PLN02183 456 GMQLGLYALDLAVAHLLHCFTWeLP--DGMKP 485
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
306-468 5.19e-15

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: 77.19  E-value: 5.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 306 GHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRifGENFAGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDI 385
Cdd:cd20644 244 GVDTTAFPLLFTLFELARNPDVQQILRQESLA--AAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQRVPSSDLVL 321
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 386 NGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGieAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRR 465
Cdd:cd20644 322 QNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGR--NFKHLAFGFGMRQCLGRRLAEAEMLLLLMHVLKN 399

                ...
gi 19921820 466 FEI 468
Cdd:cd20644 400 FLV 402
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
32-479 7.19e-15

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 77.04  E-value: 7.19e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820   32 MEMIPGPTPYPFVGNLFQF-GLKPAEYPKKVLQ-YCRKYDFQ-GFRSLVFLQYHMMLSDPAEIQNI-LSSSSLLYKEHLY 107
Cdd:PLN03234  27 LRLPPGPKGLPIIGNLHQMeKFNPQHFLFRLSKlYGPIFTMKiGGRRLAVISSAELAKELLKTQDLnFTARPLLKGQQTM 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  108 SFLRPWLGDGLLTS--SGARWLKHQKLYAPaferSAIEGYLRVVHRTGGQFVQKLDVLSDTQEVFDAQELVAKCTLDIVC 185
Cdd:PLN03234 107 SYQGRELGFGQYTAyyREMRKMCMVNLFSP----NRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVC 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  186 ENATGQDSSSLNGETSDLHGAIKDLCDVVQERTFS-IVKRFDALFRLTSYYMKQRRALSLLRSELNRIISQrrhqlaaen 264
Cdd:PLN03234 183 RQAFGKRYNEYGTEMKRFIDILYETQALLGTLFFSdLFPYFGFLDNLTGLSARLKKAFKELDTYLQELLDE--------- 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  265 TCQQGQPINK--PFLDVLLTAKLDGKV---LKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIF 339
Cdd:PLN03234 254 TLDPNRPKQEteSFIDLLMQIYKDQPFsikFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVI 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  340 GEN-FAGEADLARLDqmhYLELIIRETLRLYPSVP-LIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYF-DDPCTF 416
Cdd:PLN03234 334 GDKgYVSEEDIPNLP---YLKAVIKESLRLEPVIPiLLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEF 410
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921820  417 RPERFENPTGNVGIEA--FKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIlpavdGLPPGI 479
Cdd:PLN03234 411 IPERFMKEHKGVDFKGqdFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDW-----SLPKGI 470
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
267-468 7.50e-15

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: 76.68  E-value: 7.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 267 QQGQPINKPFLDVLLTAKLDGKVLKErEIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEqrrIFGENFAGE 346
Cdd:cd20643 208 RQKGKNEHEYPGILANLLLQDKLPIE-DIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAE---VLAARQEAQ 283
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 347 ADLARLDQM-HYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENpt 425
Cdd:cd20643 284 GDMVKMLKSvPLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLS-- 361
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19921820 426 gnVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI 468
Cdd:cd20643 362 --KDITHFRNLGFGFGPRQCLGRRIAETEMQLFLIHMLENFKI 402
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
277-466 1.35e-14

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: 75.29  E-value: 1.35e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 277 LDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHseiqqkaaEEQRrifgenfageaDLARLDQmh 356
Cdd:cd11031 189 LSALVAARDDDDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRH--------PEQL-----------ARLRADP-- 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 357 ylELI---IRETLRLYP--SVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPtgnvgie 431
Cdd:cd11031 248 --ELVpaaVEELLRYIPlgAGGGFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDREPNP------- 318
                       170       180       190
                ....*....|....*....|....*....|....*
gi 19921820 432 afkSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:cd11031 319 ---HLAFGHGPHHCLGAPLARLELQVALGALLRRL 350
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
239-479 1.56e-14

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: 75.58  E-value: 1.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 239 RRALSLLRSELNRIISQRRHQLAAENTcqqgqpinKPFLDV-LLTAKLDGKVLKEREIIEEVSTFI-----FTGHDPIAA 312
Cdd:cd20666 175 RQIEKDITAFLKKIIADHRETLDPANP--------RDFIDMyLLHIEEEQKNNAESSFNEDYLFYIigdlfIAGTDTTTN 246
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 313 AISFTLYTLSRHSEIQQKAAEEQRRIFGENFAgeADLARLDQMHYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVA 391
Cdd:cd20666 247 TLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRA--PSLTDKAQMPFTEATIMEVQRMTVVVPLsIPHMASENTVLQGYTIP 324
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 392 KCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNV-GIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILP 470
Cdd:cd20666 325 KGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLiKKEAF--IPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLL 402

                ....*....
gi 19921820 471 AVDGLPPGI 479
Cdd:cd20666 403 PPNAPKPSM 411
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
90-477 1.98e-14

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: 74.82  E-value: 1.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  90 EIQNILSSSSLLYKEHLYSFLRPWLGDG-LLTSSGARWLKHQKLYAPAFERSAIEGYLRVVHRTGGQFvqkLDVLSDTQE 168
Cdd:cd11080  19 DVRRILKDPDGFTTKSLAERAEPVMRGPvLAQMTGKEHAAKRAIVVRAFRGDALDHLLPLIKENAEEL---IAPFLERGR 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 169 VFDAQELVAKCTLDIVCenatgqdssslngetsDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSYYMKQRRALSLLRSE 248
Cdd:cd11080  96 VDLVNDFGKPFAVNVTM----------------DMLGLDKRDHEKIHEWHSSVAAFITSLSQDPEARAHGLRCAEQLSQY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 249 LNRIISQRRHQLAAEntcqqgqpinkpFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEiq 328
Cdd:cd11080 160 LLPVIEERRVNPGSD------------LISILCTAEYEGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPE-- 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 329 QKAAEEQRRIFgenfageadlarldqmhyLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTViMCLI-AMGYNE 407
Cdd:cd11080 226 QLAAVRADRSL------------------VPRAIAETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTV-FCLIgAANRDP 286
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 408 KYFDDPCTFRPERFENPTGNVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDGLPP 477
Cdd:cd11080 287 AAFEDPDTFNIHREDLGIRSAFSGAADHLAFGSGRHFCVGAALAKREIEIVANQVLDALPNIRLEPGFEY 356
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
91-464 2.82e-14

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: 74.85  E-value: 2.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  91 IQNILSSSSLLYKEHLYSFLRPWLGDGLLTSSGARWLKH-QKLYAPAFERSAIEGYLRVVHRTGGQFVQKLdvLSDTQEV 169
Cdd:cd20638  43 VRQILLGEHKLVSVQWPASVRTILGSGCLSNLHDSQHKHrKKVIMRAFSREALENYVPVIQEEVRSSVNQW--LQSGPCV 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 170 FDAQElVAKCTLDIVCENATGQDSSSLNGETSdlhgaiKDLCDVVQERT---FS--IVKRFDALFRltsyymkQRRALSL 244
Cdd:cd20638 121 LVYPE-VKRLMFRIAMRILLGFEPQQTDREQE------QQLVEAFEEMIrnlFSlpIDVPFSGLYR-------GLRARNL 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 245 LRSELNRIIsqrRHQLAAENTCQQgqpiNKPFLDVLLT-AKLDGKVLKEREIIEEVSTFIFTGHDPIA-AAISFTLYtLS 322
Cdd:cd20638 187 IHAKIEENI---RAKIQREDTEQQ----CKDALQLLIEhSRRNGEPLNLQALKESATELLFGGHETTAsAATSLIMF-LG 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 323 RHSEIQQKAAEE--QRRIFGE--NFAGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIM 398
Cdd:cd20638 259 LHPEVLQKVRKElqEKGLLSTkpNENKELSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIY 338
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921820 399 CLIAMGYNEKYFDDPCTFRPERFENPTGNVGiEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLR 464
Cdd:cd20638 339 SICDTHDVADIFPNKDEFNPDRFMSPLPEDS-SRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELAR 403
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
303-479 3.56e-14

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: 74.52  E-value: 3.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 303 IFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfageaDLARLD---QMHYLELIIRETLRLYPSVPL-IART 378
Cdd:cd11026 235 FFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRN-----RTPSLEdraKMPYTDAVIHEVQRFGDIVPLgVPHA 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 379 NRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGN-VGIEAFksVPFSAGPRRCIAEKFAMYQMKA 457
Cdd:cd11026 310 VTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKfKKNEAF--MPFSAGKRVCLGEGLARMELFL 387
                       170       180
                ....*....|....*....|..
gi 19921820 458 LLSQLLRRFEILPAVDGLPPGI 479
Cdd:cd11026 388 FFTSLLQRFSLSSPVGPKDPDL 409
PLN03018 PLN03018
homomethionine N-hydroxylase
242-466 3.72e-14

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 75.05  E-value: 3.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  242 LSLLRSELNRIISQRRhQLAAEntcQQGQPINKPFLDVLLTAK-LDGKVL-KEREIIEEVSTFIFTGHDPIAAAISFTLY 319
Cdd:PLN03018 264 VNLVRSYNNPIIDERV-ELWRE---KGGKAAVEDWLDTFITLKdQNGKYLvTPDEIKAQCVEFCIAAIDNPANNMEWTLG 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  320 TLSRHSEIQQKAAEEQRRIFG-ENFAGEADLARLDqmhYLELIIRETLRLYPSV----PLIARTNRNpidINGTKVAKCT 394
Cdd:PLN03018 340 EMLKNPEILRKALKELDEVVGkDRLVQESDIPNLN---YLKACCRETFRIHPSAhyvpPHVARQDTT---LGGYFIPKGS 413
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921820  395 TVIMCLIAMGYNEKYFDDPCTFRPERF---ENPTGNVGI--EAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:PLN03018 414 HIHVCRPGLGRNPKIWKDPLVYEPERHlqgDGITKEVTLveTEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGF 490
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
94-485 6.28e-14

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: 73.72  E-value: 6.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  94 ILSSSSLLYKEHLYSFLRPWLGD-GLLTSSGARWlKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQ-EVFD 171
Cdd:cd20667  27 LVSHSEEFSGRPLTPFFRDLFGEkGIICTNGLTW-KQQRRFCMTTLRELGLGKQALESQIQHEAAELVKVFAQENgRPFD 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 172 AQELVAKCTLDIVCENATGQDSSSLNGETSDLHGAIKdlCDVVQERTfsIVKR-FDALFRLTSY----YMKQRRALSLLR 246
Cdd:cd20667 106 PQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAIN--LGLAFAST--IWGRlYDAFPWLMRYlpgpHQKIFAYHDAVR 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 247 SELNRIIsqRRHQLaaeNTCQQGQPINKPFLDVLLTAKLD-GKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHS 325
Cdd:cd20667 182 SFIKKEV--IRHEL---RTNEAPQDFIDCYLAQITKTKDDpVSTFSEENMIQVVIDLFLGGTETTATTLHWALLYMVHHP 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 326 EIQQKAAEEQRRIFG-ENFAGEADLARLDqmhYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAM 403
Cdd:cd20667 257 EIQEKVQQELDEVLGaSQLICYEDRKRLP---YTNAVIHEVQRLSNVVSVgAVRQCVTSTTMHGYYVEKGTIILPNLASV 333
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 404 GYNEKYFDDPCTFRPERFENPTGN-VGIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIlpavdGLPPGINDH 482
Cdd:cd20667 334 LYDPECWETPHKFNPGHFLDKDGNfVMNEAF--LPFSAGHRVCLGEQLARMELFIFFTTLLRTFNF-----QLPEGVQEL 406

                ...
gi 19921820 483 SRE 485
Cdd:cd20667 407 NLE 409
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
248-476 8.06e-14

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: 73.21  E-value: 8.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 248 ELNRIISQRRHQLAAENtcqqgqpinkPFLDVLLTAKLDGKVLKEREIIEEVSTF------IFTGHDPIAAAISFTLYTL 321
Cdd:cd20652 185 IYQKIIDEHKRRLKPEN----------PRDAEDFELCELEKAKKEGEDRDLFDGFytdeqlHHLLADLFGAGVDTTITTL 254
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 322 SRHSEIQQKAAEEQRRIFGE--NFAGEADLARLDQMHYLELI---IRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTT 395
Cdd:cd20652 255 RWFLLYMALFPKEQRRIQREldEVVGRPDLVTLEDLSSLPYLqacISESQRIRSVVPLgIPHGCTEDAVLAGYRIPKGSM 334
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 396 VIMCLIAMGYNEKYFDDPCTFRPERFENPTGNV-GIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI-LPavD 473
Cdd:cd20652 335 IIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYlKPEAF--IPFQTGKRMCLGDELARMILFLFTARILRKFRIaLP--D 410

                ...
gi 19921820 474 GLP 476
Cdd:cd20652 411 GQP 413
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
278-467 9.21e-14

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


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 72.64  E-value: 9.21e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 278 DVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIfgENFageadlarldqmhy 357
Cdd:cd11078 193 DLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRADPSLI--PNA-------------- 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 358 leliIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERfENptgnvgieAFKSVP 437
Cdd:cd11078 257 ----VEETLRYDSPVQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR-PN--------ARKHLT 323
                       170       180       190
                ....*....|....*....|....*....|
gi 19921820 438 FSAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd11078 324 FGHGIHFCLGAALARMEARIALEELLRRLP 353
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
280-477 1.13e-13

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: 72.58  E-value: 1.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 280 LLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEiqqkaaeeqrrifgenfageaDLARLdQMHyLE 359
Cdd:cd20625 187 LVAAEEDGDRLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPE---------------------QLALL-RAD-PE 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 360 LI---IRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPtgnvgieafkSV 436
Cdd:cd20625 244 LIpaaVEELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITRAPNR----------HL 313
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19921820 437 PFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDGLPP 477
Cdd:cd20625 314 AFGAGIHFCLGAPLARLEAEIALRALLRRFPDLRLLAGEPE 354
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
279-467 1.22e-13

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: 72.56  E-value: 1.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 279 VLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHseiqqkaaEEQRRIFgenfagEADLARLDQMhyl 358
Cdd:cd11033 194 VLANAEVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEH--------PDQWERL------RADPSLLPTA--- 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 359 eliIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPtgnvgieafkSVPF 438
Cdd:cd11033 257 ---VEEILRWASPVIHFRRTATRDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITRSPNP----------HLAF 323
                       170       180
                ....*....|....*....|....*....
gi 19921820 439 SAGPRRCIAEKFAMYQMKALLSQLLRRFE 467
Cdd:cd11033 324 GGGPHFCLGAHLARLELRVLFEELLDRVP 352
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
241-474 1.25e-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: 72.54  E-value: 1.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 241 ALSLLRSELNRIISQRRHQLAAENTcqqgqpinkpFLDVLLTAKLDgkvlkEREIIEEVSTFIFTGHDPIAAAISFTLYT 320
Cdd:cd20627 164 ALMEMESVLKKVIKERKGKNFSQHV----------FIDSLLQGNLS-----EQQVLEDSMIFSLAGCVITANLCTWAIYF 228
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 321 LSRHSEIQQKAAEEQRRIFGEnfaGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCL 400
Cdd:cd20627 229 LTTSEEVQKKLYKEVDQVLGK---GPITLEKIEQLRYCQQVLCETVRTAKLTPVSARLQELEGKVDQHIIPKETLVLYAL 305
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921820 401 IAMGYNEKYFDDPCTFRPERFENPTgnvGIEAFKSVPFSaGPRRCIAEKFAMYQMKALLSQLLRRFEILPaVDG 474
Cdd:cd20627 306 GVVLQDNTTWPLPYRFDPDRFDDES---VMKSFSLLGFS-GSQECPELRFAYMVATVLLSVLVRKLRLLP-VDG 374
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
284-468 1.78e-13

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: 72.44  E-value: 1.78e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 284 KLDGK--VLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQrrifgENFAGEADLARLD---QMHYL 358
Cdd:cd20677 224 KAEDKsaVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEI-----DEKIGLSRLPRFEdrkSLHYT 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 359 ELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAF-KSV 436
Cdd:cd20677 299 EAFINEVFRHSSFVPFtIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLVeKVL 378
                       170       180       190
                ....*....|....*....|....*....|..
gi 19921820 437 PFSAGPRRCIAEKFAMYQMKALLSQLLRRFEI 468
Cdd:cd20677 379 IFGMGVRKCLGEDVARNEIFVFLTTILQQLKL 410
PLN00168 PLN00168
Cytochrome P450; Provisional
230-467 2.39e-13

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 72.29  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  230 RLTSYYMKQRRALSLLRSELNRIISQRRHQLAAENTCQQGQPINKPFLDVLLTAKL---DGKVLKEREIIEEVSTFIFTG 306
Cdd:PLN00168 239 RLQKALALRRRQKELFVPLIDARREYKNHLGQGGEPPKKETTFEHSYVDTLLDIRLpedGDRALTDDEIVNLCSEFLNAG 318
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  307 HDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAG--EADLARldqMHYLELIIRETLRLYPsvP---LIARTNRN 381
Cdd:PLN00168 319 TDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQEEvsEEDVHK---MPYLKAVVLEGLRKHP--PahfVLPHKAAE 393
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  382 PIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFEnPTGN------VGIEAFKSVPFSAGPRRCIAEKFAMYQM 455
Cdd:PLN00168 394 DMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFL-AGGDgegvdvTGSREIRMMPFGVGRRICAGLGIAMLHL 472
                        250
                 ....*....|..
gi 19921820  456 KALLSQLLRRFE 467
Cdd:PLN00168 473 EYFVANMVREFE 484
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
348-499 3.00e-13

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: 71.63  E-value: 3.00e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 348 DLARLDQMHYLELIIRETLRLYpSVPLIARTNRNPIDINGTKV-AKCTTVIMCLIAMGYNEKYF-DDPCTFRPERFENPT 425
Cdd:cd11040 280 LTDLLTSCPLLDSTYLETLRLH-SSSTSVRLVTEDTVLGGGYLlRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKD 358
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921820 426 GNVGIEAFKS--VPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDGLPPgindhsredcVPQSEYDPVLNI 499
Cdd:cd11040 359 GDKKGRGLPGafRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWK----------VPGMDESPGLGI 424
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
92-473 3.53e-13

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: 71.37  E-value: 3.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  92 QNILSSSSLLYKEHLYSflrpwlGDGLLTSSGARWlKHQKLYAPAFERSAIEGYLRVVHRTGGQFVQKLDVLSDTQE-VF 170
Cdd:cd20662  32 QNFMNRPETPLRERIFN------KNGLIFSSGQTW-KEQRRFALMTLRNFGLGKKSLEERIQEECRHLVEAIREEKGnPF 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 171 DAQELVAKCTLDIVCENATGQdssSLNGETSDLHGAIKDLCDVVQERTFSIVKRFDALFRLTSY----YMKQRRALSLLR 246
Cdd:cd20662 105 NPHFKINNAVSNIICSVTFGE---RFEYHDEWFQELLRLLDETVYLEGSPMSQLYNAFPWIMKYlpgsHQTVFSNWKKLK 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 247 SELNRIISQRRHQLAAENTcqqgqpinKPFLDVLLTA----KLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLS 322
Cdd:cd20662 182 LFVSDMIDKHREDWNPDEP--------RDFIDAYLKEmakyPDPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMA 253
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 323 RHSEIQQKAAEEQRRIFGEnfAGEADLARLDQMHYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLI 401
Cdd:cd20662 254 LYPEIQEKVQAEIDRVIGQ--KRQPSLADRESMPYTNAVIHEVQRMGNIIPLnVPREVAVDTKLAGFHLPKGTMILTNLT 331
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921820 402 AMGYNEKYFDDPCTFRPERFENPTGNVGIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVD 473
Cdd:cd20662 332 ALHRDPKEWATPDTFNPGHFLENGQFKKREAF--LPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKPPPN 401
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
303-479 3.61e-13

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: 71.37  E-value: 3.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 303 IFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADLARldQMHYLELIIRETLRLYPSVPLIARTNRNP 382
Cdd:cd20671 232 VMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRK--ALPYTSAVIHEVQRFITLLPHVPRCTAAD 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 383 IDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGN-VGIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQ 461
Cdd:cd20671 310 TQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKfVKKEAF--LPFSAGRRVCVGESLARTELFIFFTG 387
                       170
                ....*....|....*...
gi 19921820 462 LLRRFEILPavdglPPGI 479
Cdd:cd20671 388 LLQKFTFLP-----PPGV 400
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
253-470 5.09e-13

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: 70.44  E-value: 5.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 253 ISQRRHQLAAENTCQQGQPInkpfLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKaa 332
Cdd:cd11034 153 LFGHLRDLIAERRANPRDDL----ISRLIEGEIDGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRR-- 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 333 eeqrrifgenFAGEADLarldqmhyLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDD 412
Cdd:cd11034 227 ----------LIADPSL--------IPNAVEEFLRFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFED 288
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19921820 413 PCTFRPERFENPtgnvgieafkSVPFSAGPRRCIAEKFAMYQMKALLSQLLRR---FEILP 470
Cdd:cd11034 289 PDRIDIDRTPNR----------HLAFGSGVHRCLGSHLARVEARVALTEVLKRipdFELDP 339
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
131-466 1.74e-12

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 68.99  E-value: 1.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 131 KLYAPAFERSAIEGYLRVVHRTggqfvqkldvlsdTQEVFDaqELVAKCTLDIVCENATGQDSSslngetsdlhgAIKDL 210
Cdd:cd20630  71 KLVAPAFTPRAIDRLRAEIQAI-------------VDQLLD--ELGEPEEFDVIREIAEHIPFR-----------VISAM 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 211 CDVVQERTfSIVKRF-DALFRLTSYYMKQRRaLSLLRSELNRIISqRRHQLAAENTCQQGQPInkpFLDVLLTAKLDGKV 289
Cdd:cd20630 125 LGVPAEWD-EQFRRFgTATIRLLPPGLDPEE-LETAAPDVTEGLA-LIEEVIAERRQAPVEDD---LLTTLLRAEEDGER 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 290 LKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEiQQKAAEEQRRIFGEnfageadlarldqmhylelIIRETLRLY 369
Cdd:cd20630 199 LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPE-ALRKVKAEPELLRN-------------------ALEEVLRWD 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 370 PSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPtgnvgieafkSVPFSAGPRRCIAE 448
Cdd:cd20630 259 NFGKMgTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRRDPNA----------NIAFGYGPHFCIGA 328
                       330
                ....*....|....*...
gi 19921820 449 KFAMYQMKALLSQLLRRF 466
Cdd:cd20630 329 ALARLELELAVSTLLRRF 346
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
290-472 4.91e-12

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: 67.73  E-value: 4.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 290 LKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfaGEADLARLDQMHYLELIIRETLRLY 369
Cdd:cd20676 233 LSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRE--RRPRLSDRPQLPYLEAFILETFRHS 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 370 PSVPL-IAR-TNRNPIdINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNV--GIEAFKSVPFSAGPRRC 445
Cdd:cd20676 311 SFVPFtIPHcTTRDTS-LNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEinKTESEKVMLFGLGKRRC 389
                       170       180
                ....*....|....*....|....*....
gi 19921820 446 IAEKFAMYQMKALLSQLLRR--FEILPAV 472
Cdd:cd20676 390 IGESIARWEVFLFLAILLQQleFSVPPGV 418
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
297-483 7.61e-12

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: 66.72  E-value: 7.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 297 EEVSTFIFtGHDPIAAAISFTLYTLSRHSEIQQKAAEEqrrifgenfAGEADLARLdqMHYLELIIRETLRLYPSVPLIA 376
Cdd:cd20624 195 GQVPQWLF-AFDAAGMALLRALALLAAHPEQAARAREE---------AAVPPGPLA--RPYLRACVLDAVRLWPTTPAVL 262
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 377 RTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENpTGNVGIEAFksVPFSAGPRRCIAEKFAMYQMK 456
Cdd:cd20624 263 RESTEDTVWGGRTVPAGTGFLIFAPFFHRDDEALPFADRFVPEIWLD-GRAQPDEGL--VPFSAGPARCPGENLVLLVAS 339
                       170       180       190
                ....*....|....*....|....*....|...
gi 19921820 457 ALLSQLLRRFEILP-----AVDGLP-PGINDHS 483
Cdd:cd20624 340 TALAALLRRAEIDPlesprSGPGEPlPGTLDHF 372
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
304-477 7.80e-12

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: 67.26  E-value: 7.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 304 FTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENFAGEADlARLdQMHYLELIIRETLRLYPSVPL-IARTNRNP 382
Cdd:cd20670 236 FAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVD-DRV-KMPYTDAVIHEIQRLTDIVPLgVPHNVIRD 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 383 IDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGI-EAFksVPFSAGPRRCIAEKFAMYQMKALLSQ 461
Cdd:cd20670 314 TQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKnEAF--VPFSSGKRVCLGEAMARMELFLYFTS 391
                       170
                ....*....|....*.
gi 19921820 462 LLRRFEILPAVdglPP 477
Cdd:cd20670 392 ILQNFSLRSLV---PP 404
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
231-471 1.28e-11

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 66.54  E-value: 1.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  231 LTSYYMKQRRALSLLRSELNRIISQRRHQlaaentCQQGQPINKPFLDVLLTAKlDGkvLKEREIIEEVSTFIFTGHDPI 310
Cdd:PLN02987 213 FSTTYRRAIQARTKVAEALTLVVMKRRKE------EEEGAEKKKDMLAALLASD-DG--FSDEEIVDFLVALLVAGYETT 283
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  311 AAAISFTLYTLSRHSEIQQKAAEEQRRIFG-ENFAGEADLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTK 389
Cdd:PLN02987 284 STIMTLAVKFLTETPLALAQLKEEHEKIRAmKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYT 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  390 VAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGiEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIL 469
Cdd:PLN02987 364 IPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTV-PSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSWV 442

                 ..
gi 19921820  470 PA 471
Cdd:PLN02987 443 PA 444
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
277-455 1.65e-11

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: 66.18  E-value: 1.65e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 277 LDVLLTAKLDGK-----VLKEREIIEEVSTFIF-TGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfageadla 350
Cdd:cd20675 212 MDAFILALEKGKsgdsgVGLDKEYVPSTVTDIFgASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRD-------- 283
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 351 RL----DQMH--YLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFEN 423
Cdd:cd20675 284 RLpcieDQPNlpYVMAFLYEAMRFSSFVPVtIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLD 363
                       170       180       190
                ....*....|....*....|....*....|...
gi 19921820 424 PTGNVGIEAFKSVP-FSAGPRRCIAEKFAMYQM 455
Cdd:cd20675 364 ENGFLNKDLASSVMiFSVGKRRCIGEELSKMQL 396
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
219-468 2.05e-11

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: 66.03  E-value: 2.05e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 219 FSIVKRF-DALFRLT-----SYYMKQRRALSLLRSELNRIISQRRHqlaaentCQQGQPINKPfLDVLL-TAKLDGKVLK 291
Cdd:cd20637 152 FSVFQQFvENVFSLPldlpfSGYRRGIRARDSLQKSLEKAIREKLQ-------GTQGKDYADA-LDILIeSAKEHGKELT 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 292 EREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRR--IFGENFAGEADLaRLD---QMHYLELIIRETL 366
Cdd:cd20637 224 MQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELRSngILHNGCLCEGTL-RLDtisSLKYLDCVIKEVL 302
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 367 RLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERF-----ENPTGNvgieaFKSVPFSAG 441
Cdd:cd20637 303 RLFTPVSGGYRTALQTFELDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFgqersEDKDGR-----FHYLPFGGG 377
                       250       260
                ....*....|....*....|....*....
gi 19921820 442 PRRCIAEKFAMYQMKALLSQL--LRRFEI 468
Cdd:cd20637 378 VRTCLGKQLAKLFLKVLAVELasTSRFEL 406
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
280-477 2.28e-11

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: 65.31  E-value: 2.28e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 280 LLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGenfageadlarldqmhyle 359
Cdd:cd11032 184 LVEAEVDGERLTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRADPSLIPG------------------- 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 360 lIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPtgnvgieafkSVPFS 439
Cdd:cd11032 245 -AIEEVLRYRPPVQRTARVTTEDVELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDRNPNP----------HLSFG 313
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19921820 440 AGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDGLPP 477
Cdd:cd11032 314 HGIHFCLGAPLARLEARIALEALLDRFPRIRVDPDVPL 351
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
318-467 2.81e-11

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: 65.36  E-value: 2.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 318 LYTLSRHS-EIQQKAAEEQRRIFGENfaGEADLARLDQMHYLELIIRETLRLYPSVPLI-ARTNRN-PIDINGT--KVAK 392
Cdd:cd11071 249 LARLGLAGeELHARLAEEIRSALGSE--GGLTLAALEKMPLLKSVVYETLRLHPPVPLQyGRARKDfVIESHDAsyKIKK 326
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 393 CTTVimcliaMGYN------EKYFDDPCTFRPERFENPTGnvgiEAFKSVPFSAGP---------RRCIAEKFAMYQMKA 457
Cdd:cd11071 327 GELL------VGYQplatrdPKVFDNPDEFVPDRFMGEEG----KLLKHLIWSNGPeteeptpdnKQCPGKDLVVLLARL 396
                       170
                ....*....|
gi 19921820 458 LLSQLLRRFE 467
Cdd:cd11071 397 FVAELFLRYD 406
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
324-466 3.08e-11

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: 65.49  E-value: 3.08e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 324 HSEIQQKAAEEQRRIFGENFAGE-ADLARldqMHYLELIIRETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLI 401
Cdd:cd20663 260 HPDVQRRVQQEIDEVIGQVRRPEmADQAR---MPYTNAVIHEVQRFGDIVPLgVPHMTSRDIEVQGFLIPKGTTLITNLS 336
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19921820 402 AMGYNEKYFDDPCTFRPERFENPTGN-VGIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:cd20663 337 SVLKDETVWEKPLRFHPEHFLDAQGHfVKPEAF--MPFSAGRRACLGEPLARMELFLFFTCLLQRF 400
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
309-473 7.88e-11

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


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 63.70  E-value: 7.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 309 PIAAA---ISFTLYTLSRHSEIQQKAAEEQRRifgenfageadlarldqmhYLELIIRETLRLYPSVPLIARTNRNPIDI 385
Cdd:cd11067 232 PTVAVarfVTFAALALHEHPEWRERLRSGDED-------------------YAEAFVQEVRRFYPFFPFVGARARRDFEW 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 386 NGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNvgieAFKSVPFSAGPR----RCIAEKFAMYQMKALLSQ 461
Cdd:cd11067 293 QGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGD----PFDFIPQGGGDHatghRCPGEWITIALMKEALRL 368
                       170
                ....*....|...
gi 19921820 462 LLRRFE-ILPAVD 473
Cdd:cd11067 369 LARRDYyDVPPQD 381
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
254-480 2.23e-10

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: 62.47  E-value: 2.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 254 SQRRHQlaaeNTCQQGQPinKPFLDVLLT--AKLDGKVLK---EREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQ 328
Cdd:cd20669 187 SVREHQ----ESLDPNSP--RDFIDCFLTkmAEEKQDPLShfnMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVA 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 329 QKAAEEQRRIFGEN-FAGEADLARldqMHYLELIIRETLRLYPSVP--LIARTNRNpIDINGTKVAKCTTVIMCLIAMGY 405
Cdd:cd20669 261 ARVQEEIDRVVGRNrLPTLEDRAR---MPYTDAVIHEIQRFADIIPmsLPHAVTRD-TNFRGFLIPKGTDVIPLLNSVHY 336
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921820 406 NEKYFDDPCTFRPERFENPTGnvgieAFKS----VPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPAVDglPPGIN 480
Cdd:cd20669 337 DPTQFKDPQEFNPEHFLDDNG-----SFKKndafMPFSAGKRICLGESLARMELFLYLTAILQNFSLQPLGA--PEDID 408
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
240-474 2.57e-10

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: 62.38  E-value: 2.57e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 240 RALSLLRSELNRIISQRRHQLAAEntcqqgqpinkpFLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLY 319
Cdd:cd11038 172 AAVEELYDYADALIEARRAEPGDD------------LISTLVAAEQDGDRLSDEELRNLIVALLFAGVDTTRNQLGLAML 239
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 320 TLSRHSEiqqkaaeeQRRIFGENfageADLArldqmhylELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMC 399
Cdd:cd11038 240 TFAEHPD--------QWRALRED----PELA--------PAAVEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLC 299
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921820 400 LIAMGynekyfDDPCTFRPERFEnptgnVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEIlPAVDG 474
Cdd:cd11038 300 SHAAN------RDPRVFDADRFD-----ITAKRAPHLGFGGGVHHCLGAFLARAELAEALTVLARRLPT-PAIAG 362
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
276-477 3.26e-10

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: 61.55  E-value: 3.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 276 FLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIqqkaaeeqrrifgenfageadLARLDQM 355
Cdd:cd20629 174 LISRLLRAEVEGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQ---------------------LERVRRD 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 356 H-YLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERfeNPTGNVGieafk 434
Cdd:cd20629 233 RsLIPAAIEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR--KPKPHLV----- 305
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 19921820 435 svpFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILpAVDGLPP 477
Cdd:cd20629 306 ---FGGGAHRCLGEHLARVELREALNALLDRLPNL-RLDPDAP 344
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
280-477 7.64e-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: 60.45  E-value: 7.64e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 280 LLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAeeqrrifgenfAGEADLArldqmhyle 359
Cdd:cd11079 169 LLRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYLARHPELQARLR-----------ANPALLP--------- 228
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 360 LIIRETLRLYpsVPLIA--RTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERfeNPTGNVGieafksvp 437
Cdd:cd11079 229 AAIDEILRLD--DPFVAnrRITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR--HAADNLV-------- 296
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 19921820 438 FSAGPRRCIAEKFAMYQMKALLSQLLRRFE-ILPAVDGLPP 477
Cdd:cd11079 297 YGRGIHVCPGAPLARLELRILLEELLAQTEaITLAAGGPPE 337
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
316-473 9.44e-10

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: 60.74  E-value: 9.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 316 FTLYTLSRHSEIQQKAAEEQRRIFGENfageadlaRL------DQMHYLELIIRETLRLYPSVP--LIARTNRNpIDING 387
Cdd:cd20665 248 YGLLLLLKHPEVTAKVQEEIDRVIGRH--------RSpcmqdrSHMPYTDAVIHEIQRYIDLVPnnLPHAVTCD-TKFRN 318
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 388 TKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNvgieaFKS----VPFSAGPRRCIAEKFAMYQMKALLSQLL 463
Cdd:cd20665 319 YLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGN-----FKKsdyfMPFSAGKRICAGEGLARMELFLFLTTIL 393
                       170
                ....*....|
gi 19921820 464 RRFEILPAVD 473
Cdd:cd20665 394 QNFNLKSLVD 403
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
276-470 9.86e-10

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


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 60.30  E-value: 9.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 276 FLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIfgenfageadlarldqm 355
Cdd:cd11035 172 LISAILNAEIDGRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLREDPELI----------------- 234
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 356 hylELIIRETLRLYPsVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERfenptgnvgiEAFKS 435
Cdd:cd11035 235 ---PAAVEELLRRYP-LVNVARIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR----------KPNRH 300
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 19921820 436 VPFSAGPRRCIAEKFAMYQMKALLSQLLRR---FEILP 470
Cdd:cd11035 301 LAFGAGPHRCLGSHLARLELRIALEEWLKRipdFRLAP 338
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
236-478 1.12e-09

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 60.72  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  236 MKQRRALSLLrseLNRIISQRRHQLAAENtcqqgqpinkpflDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAIS 315
Cdd:PLN02196 222 MKARKELAQI---LAKILSKRRQNGSSHN-------------DLLGSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLT 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  316 FTLYTLSRHSEIQQKAAEEQRRIFGENFAGEA-DLARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCT 394
Cdd:PLN02196 286 WILKYLAENPSVLEAVTEEQMAIRKDKEEGESlTWEDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEYEGYLIPKGW 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  395 TVIMCLIAMGYNEKYFDDPCTFRPERFEnptgnVGIEAFKSVPFSAGPRRCIAEKFAMYQMKALLSQLLR--RFEILPAV 472
Cdd:PLN02196 366 KVLPLFRNIHHSADIFSDPGKFDPSRFE-----VAPKPNTFMPFGNGTHSCPGNELAKLEISVLIHHLTTkyRWSIVGTS 440

                 ....*.
gi 19921820  473 DGLPPG 478
Cdd:PLN02196 441 NGIQYG 446
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
304-466 1.33e-09

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: 60.20  E-value: 1.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 304 FTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfaGEADLARLDQMHYLELIIRETLRLYPSVPL-IARTNRNP 382
Cdd:cd20668 236 FAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRN--RQPKFEDRAKMPYTEAVIHEIQRFGDVIPMgLARRVTKD 313
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 383 IDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVG-IEAFksVPFSAGPRRCIAEKFAMYQMKALLSQ 461
Cdd:cd20668 314 TKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKkSDAF--VPFSIGKRYCFGEGLARMELFLFFTT 391

                ....*
gi 19921820 462 LLRRF 466
Cdd:cd20668 392 IMQNF 396
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
311-476 1.43e-09

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: 60.02  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 311 AAAISFTLYTLS---RHSEIQQKAAEEQRRIFGENFAGEA--DLARLDQMHYLELIIRETLRLYpSVPLIARTNRNPIDI 385
Cdd:cd20635 224 ANAIPITFWTLAfilSHPSVYKKVMEEISSVLGKAGKDKIkiSEDDLKKMPYIKRCVLEAIRLR-SPGAITRKVVKPIKI 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 386 NGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFE--NPTGNVGIEAFksVPFSAGPRRCIAEKFAMYQMKALLSQLL 463
Cdd:cd20635 303 KNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERWKkaDLEKNVFLEGF--VAFGGGRYQCPGRWFALMEIQMFVAMFL 380
                       170
                ....*....|...
gi 19921820 464 RRFEIlPAVDGLP 476
Cdd:cd20635 381 YKYDF-TLLDPVP 392
PLN02500 PLN02500
cytochrome P450 90B1
278-476 1.71e-09

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 59.88  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  278 DVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIF-GENFAGEADLARLD--Q 354
Cdd:PLN02500 263 DDLLGWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIArAKKQSGESELNWEDykK 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  355 MHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFK 434
Cdd:PLN02500 343 MEFTQCVINETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRGGSSGSS 422
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19921820  435 S------VPFSAGPRRCIAEKFAMYQMKALLSQLLRRFE----------ILPAVD---GLP 476
Cdd:PLN02500 423 SattnnfMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNwelaeadqafAFPFVDfpkGLP 483
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
343-471 1.42e-08

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 56.58  E-value: 1.42e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 343 FAGEADLARLDQMHYLeliiRETLRLYPSVPLIARTNRNPIDI-----NGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFR 417
Cdd:cd20612 229 LARENDEADATLRGYV----LEALRLNPIAPGLYRRATTDTTVadgggRTVSIKAGDRVFVSLASAMRDPRAFPDPERFR 304
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 19921820 418 PERfenPTGnvgieafKSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRFEILPA 471
Cdd:cd20612 305 LDR---PLE-------SYIHFGHGPHQCLGEEIARAALTEMLRVVLRLPNLRRA 348
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
292-465 1.62e-07

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: 53.36  E-value: 1.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 292 EREIIEE-----VSTFIFTGHDPIAAAISFTLYTLSRHSEiqqkaaeeqrrifgenfagEADLARLDQmhylELI---IR 363
Cdd:cd11037 195 RGEITEDeapllMRDYLSAGLDTTISAIGNALWLLARHPD-------------------QWERLRADP----SLApnaFE 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 364 ETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERfeNPTGNVGieafksvpFSAGPR 443
Cdd:cd11037 252 EAVRLESPVQTFSRTTTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR--NPSGHVG--------FGHGVH 321
                       170       180
                ....*....|....*....|..
gi 19921820 444 RCIAEKFAMYQMKALLSQLLRR 465
Cdd:cd11037 322 ACVGQHLARLEGEALLTALARR 343
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
277-473 2.70e-07

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: 52.92  E-value: 2.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 277 LDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHseiqqkaaEEQRRIFgenfagEADLARLDQMh 356
Cdd:cd11029 194 LSALVAARDEGDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTH--------PDQLALL------RADPELWPAA- 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 357 yleliIRETLRLYPSVP-LIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERfeNPTGNVGieafks 435
Cdd:cd11029 259 -----VEELLRYDGPVAlATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR--DANGHLA------ 325
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 19921820 436 vpFSAGPRRCIAEKFAMYQMKALLSQLLRRF-EILPAVD 473
Cdd:cd11029 326 --FGHGIHYCLGAPLARLEAEIALGALLTRFpDLRLAVP 362
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
362-472 1.96e-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: 49.80  E-value: 1.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 362 IRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERfenPTGnvgieafKSVPFSAG 441
Cdd:cd11036 225 VAETLRYDPPVRLERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR---PTA-------RSAHFGLG 294
                        90       100       110
                ....*....|....*....|....*....|.
gi 19921820 442 PRRCIAEKFAMYQMKALLSQLLRRFEILPAV 472
Cdd:cd11036 295 RHACLGAALARAAAAAALRALAARFPGLRAA 325
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
317-484 6.47e-06

cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also called cholesterol 7-alpha-monooxygenase (EC 1.14.14.23) or cholesterol 7-alpha-hydroxylase. It catalyzes the hydroxylation at position 7 of cholesterol, a rate-limiting step in the classic (or neutral) pathway of cholesterol catabolism and bile acid biosynthesis. It is important for cholesterol homeostasis. CYP7A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 48.53  E-value: 6.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 317 TLYTLSRHSEIQQKAAEEQRRIFGE-----NFAGEA-DLAR--LDQMHYLELIIRETLRLyPSVPLIARTNRNPIDI--- 385
Cdd:cd20631 250 SLFYLLRCPEAMKAATKEVKRTLEKtgqkvSDGGNPiVLTReqLDDMPVLGSIIKEALRL-SSASLNIRVAKEDFTLhld 328
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 386 NGTKVA--KCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFKS--------VPFSAGPRRCIAEKFAMYQM 455
Cdd:cd20631 329 SGESYAirKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTFYKNgrklkyyyMPFGSGTSKCPGRFFAINEI 408
                       170       180       190
                ....*....|....*....|....*....|
gi 19921820 456 KALLSQLLRRFEI-LPAVDGLPPGInDHSR 484
Cdd:cd20631 409 KQFLSLMLCYFDMeLLDGNAKCPPL-DQSR 437
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
217-473 1.59e-05

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: 47.47  E-value: 1.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 217 RTFSIVKRFDA-LFRLTSYYMK----QRRALSLLRSELNRIISQRRHQLAAenTCQQGQPinKPFLDVLLTAKLDGKV-- 289
Cdd:cd20672 143 QTFSLISSFSSqVFELFSGFLKyfpgAHRQIYKNLQEILDYIGHSVEKHRA--TLDPSAP--RDFIDTYLLRMEKEKSnh 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 290 ---LKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQKAAEEQRRIFGENfageaDLARLD---QMHYLELIIR 363
Cdd:cd20672 219 hteFHHQNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSH-----RLPTLDdraKMPYTDAVIH 293
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 364 ETLRLYPSVPL-IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPTGNVG-IEAFksVPFSAG 441
Cdd:cd20672 294 EIQRFSDLIPIgVPHRVTKDTLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKkSEAF--MPFSTG 371
                       250       260       270
                ....*....|....*....|....*....|..
gi 19921820 442 PRRCIAEKFAMYQMKALLSQLLRRFEILPAVD 473
Cdd:cd20672 372 KRICLGEGIARNELFLFFTTILQNFSVASPVA 403
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
251-466 4.67e-05

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 45.89  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  251 RIISQRRHQLAAENTCQQGQPinKPFLDVLLTaklDGKVLKEREII-EEVSTFIFTGHDPIAAAISFTLYTLSRHSEIQQ 329
Cdd:PLN03141 212 KIIEEKRRAMKNKEEDETGIP--KDVVDVLLR---DGSDELTDDLIsDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVALQ 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  330 KAAEEQRRI-FGENFAGEaDLARLDQMH--YLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYN 406
Cdd:PLN03141 287 QLTEENMKLkRLKADTGE-PLYWTDYMSlpFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLD 365
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  407 EKYFDDPCTFRPERFENPTGNVGieAFksVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:PLN03141 366 EENYDNPYQFNPWRWQEKDMNNS--SF--TPFGGGQRLCPGLDLARLEASIFLHHLVTRF 421
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
318-474 1.12e-04

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: 44.67  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 318 LYTLsRHSEIQQKAAEEQRRIFGEN------FAGEADLAR--LDQMHYLELIIRETLRLYPSvPLIARTNRNPIDI---N 386
Cdd:cd20633 249 LYLL-KHPEAMKAVREEVEQVLKETgqevkpGGPLINLTRdmLLKTPVLDSAVEETLRLTAA-PVLIRAVVQDMTLkmaN 326
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 387 GTKVAKCTTVIMCL---IAMGYNEKYFDDPCTFRPERFENPTGNVGIEAFKS--------VPFSAGPRRCIAEKFAMYQM 455
Cdd:cd20633 327 GREYALRKGDRLALfpyLAVQMDPEIHPEPHTFKYDRFLNPDGGKKKDFYKNgkklkyynMPWGAGVSICPGRFFAVNEM 406
                       170       180
                ....*....|....*....|....*..
gi 19921820 456 KALLSQLLRRFEI--------LPAVDG 474
Cdd:cd20633 407 KQFVFLMLTYFDLelvnpdeeIPSIDP 433
PLN02774 PLN02774
brassinosteroid-6-oxidase
277-466 1.15e-04

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 44.77  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  277 LDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSeiqqKAAEEQRRifgENFAGEA--------D 348
Cdd:PLN02774 247 LGYLMRKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHP----KALQELRK---EHLAIRErkrpedpiD 319
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820  349 LARLDQMHYLELIIRETLRLYPSVPLIARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERFENPtgnv 428
Cdd:PLN02774 320 WNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDK---- 395
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 19921820  429 GIEAFKS-VPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:PLN02774 396 SLESHNYfFLFGGGTRLCPGKELGIVEISTFLHYFVTRY 434
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
276-466 4.40e-04

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: 42.51  E-value: 4.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 276 FLDVLLTAKLDGKVLKEREIIEEVSTFIFTGHDPIAAAISFTLYTLSRHSEiqqkAAEEQRrifgenfageADLARLDQM 355
Cdd:cd11030 190 LLSRLVAEHGAPGELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPE----QLAALR----------ADPSLVPGA 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921820 356 hyleliIRETLRlYPSVPL--IARTNRNPIDINGTKVAKCTTVIMCLIAMGYNEKYFDDPCTFRPERfenptgnvgiEAF 433
Cdd:cd11030 256 ------VEELLR-YLSIVQdgLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR----------PAR 318
                       170       180       190
                ....*....|....*....|....*....|...
gi 19921820 434 KSVPFSAGPRRCIAEKFAMYQMKALLSQLLRRF 466
Cdd:cd11030 319 RHLAFGHGVHQCLGQNLARLELEIALPTLFRRF 351
 
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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