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Conserved domains on  [gi|1034678150|ref|XP_016885820|]
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cytochrome P450 2D6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
65-492 0e+00

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: 934.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20663     1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGPKSQGVVLARYGPAWREQRRFSVSTLRNFGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20663    81 GKKSLEQWVTEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFS 304
Cdd:cd20663   161 NAFPVLLRIPGLAGKVFPGQKAFLALLDELLTEHRTTWDPAQPPRDLTDAFLAEMEKAKGNPESSFNDENLRLVVADLFS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEV 384
Cdd:cd20663   241 AGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIEV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 385 QGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHF 464
Cdd:cd20663   321 QGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRF 400
                         410       420
                  ....*....|....*....|....*...
gi 1034678150 465 SFSVAAGQPRPSHSRVVSFLVTPSPYEL 492
Cdd:cd20663   401 SFSVPAGQPRPSDHGVFAFLVSPSPYQL 428
 
Name Accession Description Interval E-value
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
65-492 0e+00

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: 934.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20663     1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGPKSQGVVLARYGPAWREQRRFSVSTLRNFGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20663    81 GKKSLEQWVTEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFS 304
Cdd:cd20663   161 NAFPVLLRIPGLAGKVFPGQKAFLALLDELLTEHRTTWDPAQPPRDLTDAFLAEMEKAKGNPESSFNDENLRLVVADLFS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEV 384
Cdd:cd20663   241 AGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIEV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 385 QGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHF 464
Cdd:cd20663   321 QGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRF 400
                         410       420
                  ....*....|....*....|....*...
gi 1034678150 465 SFSVAAGQPRPSHSRVVSFLVTPSPYEL 492
Cdd:cd20663   401 SFSVPAGQPRPSDHGVFAFLVSPSPYQL 428
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
58-493 1.22e-152

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: 443.26  E-value: 1.22e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  58 FDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARyGPAWREQRRFSVS 137
Cdd:pfam00067  26 FTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRGPFLGKGIVFAN-GPRWRQLRRFLTP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 138 TLRNLGlgKKSLEQWVTEEAACLCAAFANHSGRP--FRPNGLLDKAVSNVIASLTCGRRFE-YDDPRFLRLLDLAQEGLK 214
Cdd:pfam00067 105 TFTSFG--KLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILFGERFGsLEDPKFLELVKAVQELSS 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 215 EESGFLREVLNAVPVLLHIPALAGKVL-RFQKAFLTQLDELLTEHRMTWDPAQ-PPRDLTEAFLAEMEKAKGnpeSSFND 292
Cdd:pfam00067 183 LLSSPSPQLLDLFPILKYFPGPHGRKLkRARKKIKDLLDKLIEERRETLDSAKkSPRDFLDALLLAKEEEDG---SKLTD 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 293 ENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPL 372
Cdd:pfam00067 260 EELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPL 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 373 GVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARME 452
Cdd:pfam00067 340 LLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARME 419
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1034678150 453 LFLFFTSLLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYELC 493
Cdd:pfam00067 420 MKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLK 460
PLN02687 PLN02687
flavonoid 3'-monooxygenase
61-472 1.08e-51

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 183.47  E-value: 1.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  61 LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprSQGVFLARYGPAWREQRR------F 134
Cdd:PLN02687   62 LAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSGAEHMAYN--YQDLVFAPYGPRWRALRKicavhlF 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 135 SVSTLRNLglgkKSLEQwvtEEAACLCAAFANHSGRPFRPNG-LLDKAVSNVIASLTCGRR-FEYD-DPRFLRLLDLAQE 211
Cdd:PLN02687  140 SAKALDDF----RHVRE---EEVALLVRELARQHGTAPVNLGqLVNVCTTNALGRAMVGRRvFAGDgDEKAREFKEMVVE 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 212 gLKEESGFLrEVLNAVPVL--LHIPALAGKVLRFQKAFLTQLDELLTEHRM-TWDPAQPPRDLTEAFLAEMEKAKGNPE- 287
Cdd:PLN02687  213 -LMQLAGVF-NVGDFVPALrwLDLQGVVGKMKRLHRRFDAMMNGIIEEHKAaGQTGSEEHKDLLSTLLALKREQQADGEg 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 288 SSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFG 367
Cdd:PLN02687  291 GRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLH 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 368 DIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHF---VKPEAF--LPFSAGRRA 442
Cdd:PLN02687  371 PSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPGGEHAgvdVKGSDFelIPFGAGRRI 450
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1034678150 443 CLGEPLA-RMELFLFFTsLLQHFSFSVAAGQ 472
Cdd:PLN02687  451 CAGLSWGlRMVTLLTAT-LVHAFDWELADGQ 480
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
50-481 1.17e-42

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: 156.21  E-value: 1.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  50 DFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSqgvFLARYGPAWR 129
Cdd:COG2124    16 AFLRDPYPFYARLREYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDS---LLTLDGPEHT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 130 EQRR-----FSVSTLRnlglgkkSLEQWVTEEAACLCAAFANHSGRPFRPnglldkAVSNVIASLTCGRRFEYDDPRFLR 204
Cdd:COG2124    93 RLRRlvqpaFTPRRVA-------ALRPRIREIADELLDRLAARGPVDLVE------EFARPLPVIVICELLGVPEEDRDR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 205 LLDLAQEGLKEESGFLREVLnavpvllhipalaGKVLRFQKAFLTQLDELLTEHRmtwdpAQPPRDLTEAFLAEmeKAKG 284
Cdd:COG2124   160 LRRWSDALLDALGPLPPERR-------------RRARRARAELDAYLRELIAERR-----AEPGDDLLSALLAA--RDDG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 285 NPessFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIddvigqvrrpemgdqahmPYTTAVIHEVQ 364
Cdd:COG2124   220 ER---LSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETL 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 365 RFGDIVPlGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHfldaqghfvKPEAFLPFSAGRRACL 444
Cdd:COG2124   279 RLYPPVP-LLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCL 348
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1034678150 445 GEPLARMELFLFFTSLLQHF-SFSVAAGQ-PRPSHSRVV 481
Cdd:COG2124   349 GAALARLEARIALATLLRRFpDLRLAPPEeLRWRPSLTL 387
 
Name Accession Description Interval E-value
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
65-492 0e+00

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: 934.11  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20663     1 FGDVFSLQMAWKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGPKSQGVVLARYGPAWREQRRFSVSTLRNFGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20663    81 GKKSLEQWVTEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFS 304
Cdd:cd20663   161 NAFPVLLRIPGLAGKVFPGQKAFLALLDELLTEHRTTWDPAQPPRDLTDAFLAEMEKAKGNPESSFNDENLRLVVADLFS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEV 384
Cdd:cd20663   241 AGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIEV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 385 QGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHF 464
Cdd:cd20663   321 QGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRF 400
                         410       420
                  ....*....|....*....|....*...
gi 1034678150 465 SFSVAAGQPRPSHSRVVSFLVTPSPYEL 492
Cdd:cd20663   401 SFSVPAGQPRPSDHGVFAFLVSPSPYQL 428
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
65-492 0e+00

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: 652.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILgfgPRSQGVFLARyGPAWREQRRFSVSTLRNLGL 144
Cdd:cd11026     1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRV---TKGYGVVFSN-GERWKQLRRFSLTTLRNFGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd11026    77 GKRSIEERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVP-VLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPaQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLF 303
Cdd:cd11026   157 NMFPpLLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDP-SSPRDFIDCFLLKMEKEKDNPNSEFHEENLVMTVLDLF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 304 SAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIE 383
Cdd:cd11026   236 FAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTK 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 384 VQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQH 463
Cdd:cd11026   316 FRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQR 395
                         410       420       430
                  ....*....|....*....|....*....|
gi 1034678150 464 FSFSVAAGQPRPSHS-RVVSFLVTPSPYEL 492
Cdd:cd11026   396 FSLSSPVGPKDPDLTpRFSGFTNSPRPYQL 425
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
65-492 4.93e-154

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: 445.40  E-value: 4.93e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprsQGVFLARyGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20664     1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKG---YGILFSN-GENWKEMRRFTLTTLRDFGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20664    77 GKKTSEDKILEEIPYLIEVFEKHKGKPFETTLSMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGSPSVQLY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPpRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFS 304
Cdd:cd20664   157 NMFPWLGPFPGDINKLLRNTKELNDFLMETFMKHLDVLEPNDQ-RGFIDAFLVKQQEEEESSDSFFHDDNLTCSVGNLFG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQvRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEV 384
Cdd:cd20664   236 AGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGS-RQPQVEHRKNMPYTDAVIHEIQRFANIVPMNLPHATTRDVTF 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 385 QGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHF 464
Cdd:cd20664   315 RGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRF 394
                         410       420       430
                  ....*....|....*....|....*....|
gi 1034678150 465 SFSVAAG--QPRPSHSRVVSFLVTPSPYEL 492
Cdd:cd20664   395 RFQPPPGvsEDDLDLTPGLGFTLNPLPHQL 424
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
65-465 1.71e-153

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: 444.01  E-value: 1.71e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprsQGVFLARyGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20665     1 YGPVFTLYLGMKPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKG---LGIVFSN-GERWKETRRFSLMTLRNFGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20665    77 GKRSIEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVC 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLLH-IPALAGKVLR---FQKAFLTqldELLTEHRMTWDPAQPpRDLTEAFLAEMEKAKGNPESSFNDENLRIVVA 300
Cdd:cd20665   157 NNFPALLDyLPGSHNKLLKnvaYIKSYIL---EKVKEHQESLDVNNP-RDFIDCFLIKMEQEKHNQQSEFTLENLAVTVT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 301 DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSR 380
Cdd:cd20665   233 DLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLPHAVTC 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 381 DIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSL 460
Cdd:cd20665   313 DTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTI 392

                  ....*
gi 1034678150 461 LQHFS 465
Cdd:cd20665   393 LQNFN 397
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
65-492 3.51e-153

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: 443.08  E-value: 3.51e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPI-TQILGfgprSQGVFLARyGPAWREQRRFSVSTLRNLG 143
Cdd:cd20662     1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLrERIFN----KNGLIFSS-GQTWKEQRRFALMTLRNFG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 144 LGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREV 223
Cdd:cd20662    76 LGKKSLEERIQEECRHLVEAIREEKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSPMSQL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 224 LNAVPVLL-HIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPpRDLTEAFLAEMEKAKGnPESSFNDENLRIVVADL 302
Cdd:cd20662   156 YNAFPWIMkYLPGSHQTVFSNWKKLKLFVSDMIDKHREDWNPDEP-RDFIDAYLKEMAKYPD-PTTSFNEENLICSTLDL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 303 FSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDI 382
Cdd:cd20662   234 FFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAVDT 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 383 EVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDaQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQ 462
Cdd:cd20662   314 KLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLE-NGQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQ 392
                         410       420       430
                  ....*....|....*....|....*....|
gi 1034678150 463 HFSFSVAAGQpRPSHSRVVSFLVTPSPYEL 492
Cdd:cd20662   393 KFTFKPPPNE-KLSLKFRMGITLSPVPHRI 421
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
58-493 1.22e-152

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: 443.26  E-value: 1.22e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  58 FDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVFLARyGPAWREQRRFSVS 137
Cdd:pfam00067  26 FTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSRGPFLGKGIVFAN-GPRWRQLRRFLTP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 138 TLRNLGlgKKSLEQWVTEEAACLCAAFANHSGRP--FRPNGLLDKAVSNVIASLTCGRRFE-YDDPRFLRLLDLAQEGLK 214
Cdd:pfam00067 105 TFTSFG--KLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILFGERFGsLEDPKFLELVKAVQELSS 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 215 EESGFLREVLNAVPVLLHIPALAGKVL-RFQKAFLTQLDELLTEHRMTWDPAQ-PPRDLTEAFLAEMEKAKGnpeSSFND 292
Cdd:pfam00067 183 LLSSPSPQLLDLFPILKYFPGPHGRKLkRARKKIKDLLDKLIEERRETLDSAKkSPRDFLDALLLAKEEEDG---SKLTD 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 293 ENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPL 372
Cdd:pfam00067 260 EELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPL 339
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 373 GVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARME 452
Cdd:pfam00067 340 LLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNCLGERLARME 419
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1034678150 453 LFLFFTSLLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYELC 493
Cdd:pfam00067 420 MKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLK 460
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
65-491 1.56e-149

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: 433.94  E-value: 1.56e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQIlgFGPRSQGVFLARYGPAWREQRRFSVSTLRNLGL 144
Cdd:cd11027     1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDL--FSRGGKDIAFGDYSPTWKLHRKLAHSALRLYAS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLreVL 224
Cdd:cd11027    79 GGPRLEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKFFELLGAGS--LL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLLHIPALAGKVLR-FQKAFLTQLDELLTEHRMTWDPAQPpRDLTEAFLAEMEKAK---GNPESSFNDENLRIVVA 300
Cdd:cd11027   157 DIFPFLKYFPNKALRELKeLMKERDEILRKKLEEHKETFDPGNI-RDLTDALIKAKKEAEdegDEDSGLLTDDHLVMTIS 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 301 DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSR 380
Cdd:cd11027   236 DIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALPHKTTC 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 381 DIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFV-KPEAFLPFSAGRRACLGEPLARMELFLFFTS 459
Cdd:cd11027   316 DTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVpKPESFLPFSAGRRVCLGESLAKAELFLFLAR 395
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1034678150 460 LLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYE 491
Cdd:cd11027   396 LLQKFRFSPPEGEPPPELEGIPGLVLYPLPYK 427
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
65-492 9.04e-146

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: 424.19  E-value: 9.04e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILgfgPRSQGVFLARYGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20666     1 YGNIFSLFIGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTIL---TKGKGIVFAPYGPVWRQQRKFSHSTLRHFGL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20666    78 GKLSLEPKIIEEFRYVKAEMLKHGGDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLMSRGLEISVNSAAILV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLLHIPALAGKVLR-FQKAFLTQLDELLTEHRMTWDPAQPpRDLTEAFLAEM-EKAKGNPESSFNDENLRIVVADL 302
Cdd:cd20666   158 NICPWLYYLPFGPFRELRqIEKDITAFLKKIIADHRETLDPANP-RDFIDMYLLHIeEEQKNNAESSFNEDYLFYIIGDL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 303 FSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDI 382
Cdd:cd20666   237 FIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENT 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 383 EVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQ 462
Cdd:cd20666   317 VLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQ 396
                         410       420       430
                  ....*....|....*....|....*....|
gi 1034678150 463 HFSFSVAAGQPRPSHSRVVSFLVTPSPYEL 492
Cdd:cd20666   397 SFTFLLPPNAPKPSMEGRFGLTLAPCPFNI 426
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
66-492 5.47e-134

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: 394.28  E-value: 5.47e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALvtHGEDTADRPPVPITQILGFGPRsQGVFLARyGPAWREQRRFSVSTLRNLGLG 145
Cdd:cd20651     1 GDVVGLKLGKDKVVVVSGYEAVREVL--SREEFDGRPDGFFFRLRTFGKR-LGITFTD-GPFWKEQRRFVLRHLRDFGFG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 146 KKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLK--EESGFLrev 223
Cdd:cd20651    77 RRSMEEVIQEEAEELIDLLKKGEKGPIQMPDLFNVSVLNVLWAMVAGERYSLEDQKLRKLLELVHLLFRnfDMSGGL--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 224 LNAVPVLLHI-PALAG--KVLRFQKAFLTQLDELLTEHRMTWDPAQPpRDLTEAFLAEMEKAKgNPESSFNDENLRIVVA 300
Cdd:cd20651   154 LNQFPWLRFIaPEFSGynLLVELNQKLIEFLKEEIKEHKKTYDEDNP-RDLIDAYLREMKKKE-PPSSSFTDDQLVMICL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 301 DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSR 380
Cdd:cd20651   232 DLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALK 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 381 DIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSL 460
Cdd:cd20651   312 DTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGL 391
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1034678150 461 LQHFSFSVAAGQPRPSHSRVVSFLVTPSPYEL 492
Cdd:cd20651   392 LQNFTFSPPNGSLPDLEGIPGGITLSPKPFRV 423
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
65-466 8.53e-132

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: 388.74  E-value: 8.53e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPItqILGFgPRSQGVFLARyGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20669     1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQAEEFSGRGDYPV--FFNF-TKGNGIAFSN-GERWKILRRFALQTLRNFGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20669    77 GKRSIEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVP-VLLHIPALAGKVLR-FQKAFLTQLDELlTEHRMTWDPaQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADL 302
Cdd:cd20669   157 NIFPsVMDWLPGPHQRIFQnFEKLRDFIAESV-REHQESLDP-NSPRDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 303 FSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDI 382
Cdd:cd20669   235 LFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 383 EVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQ 462
Cdd:cd20669   315 NFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQ 394

                  ....
gi 1034678150 463 HFSF 466
Cdd:cd20669   395 NFSL 398
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
66-492 1.55e-130

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: 385.03  E-value: 1.55e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprsQGVFLArYGPAWREQRRFSVSTLRNLGLg 145
Cdd:cd20617     1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGG---KGILFS-NGDYWKELRRFALSSLTKTKL- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 146 KKSLEQWVTEEAACLCAAFANH--SGRPFRPNGLLDKAVSNVIASLTCGRRFE-YDDPRFLRLLDLAQEGLKEesgflre 222
Cdd:cd20617    76 KKKMEELIEEEVNKLIESLKKHskSGEPFDPRPYFKKFVLNIINQFLFGKRFPdEDDGEFLKLVKPIEEIFKE------- 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 223 vLNAVPVLLHIPALAGKVLRFQKAFLTQLDEL-------LTEHRMTWDPaQPPRDLTEAFLAEMEKakGNPESSFNDENL 295
Cdd:cd20617   149 -LGSGNPSDFIPILLPFYFLYLKKLKKSYDKIkdfiekiIEEHLKTIDP-NNPRDLIDDELLLLLK--EGDSGLFDDDSI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 296 RIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVT 375
Cdd:cd20617   225 ISTCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLP 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 376 HMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDaQGHFVKPEAFLPFSAGRRACLGEPLARMELFL 455
Cdd:cd20617   305 RVTTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLE-NDGNKLSEQFIPFGIGKRNCVGENLARDELFL 383
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1034678150 456 FFTSLLQHFSFSVaaGQPRPSHSRVV-SFLVTPSPYEL 492
Cdd:cd20617   384 FFANLLLNFKFKS--SDGLPIDEKEVfGLTLKPKPFKV 419
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
65-467 6.77e-126

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: 373.73  E-value: 6.77e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILgfgPRSQGVFLARyGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20672     1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPI---FQGYGVIFAN-GERWKTLRRFSLATMRDFGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20672    77 GKRSVEERIQEEAQCLVEELRKSKGALLDPTFLFQSITANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISSFSSQVF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLL-HIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPpRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLF 303
Cdd:cd20672   157 ELFSGFLkYFPGAHRQIYKNLQEILDYIGHSVEKHRATLDPSAP-RDFIDTYLLRMEKEKSNHHTEFHHQNLMISVLSLF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 304 SAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIE 383
Cdd:cd20672   236 FAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTL 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 384 VQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQH 463
Cdd:cd20672   316 FRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQN 395

                  ....
gi 1034678150 464 FSFS 467
Cdd:cd20672   396 FSVA 399
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
65-492 4.68e-123

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: 366.09  E-value: 4.68e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILgFGPRsqGVFLARyGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20667     1 YGNIYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDL-FGEK--GIICTN-GLTWKQQRRFCMTTLRELGL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20667    77 GKQALESQIQHEAAELVKVFAQENGRPFDPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINLGLAFASTIWGRLY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLL-HIPALAGKVLRFQKAFLTQLDELLTEHRMtwDPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLF 303
Cdd:cd20667   157 DAFPWLMrYLPGPHQKIFAYHDAVRSFIKKEVIRHEL--RTNEAPQDFIDCYLAQITKTKDDPVSTFSEENMIQVVIDLF 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 304 SAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIE 383
Cdd:cd20667   235 LGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAVRQCVTSTT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 384 VQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQH 463
Cdd:cd20667   315 MHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRT 394
                         410       420
                  ....*....|....*....|....*....
gi 1034678150 464 FSFSVAAGQPRPSHSRVVSFLVTPSPYEL 492
Cdd:cd20667   395 FNFQLPEGVQELNLEYVFGGTLQPQPYKI 423
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
65-465 7.21e-118

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: 353.07  E-value: 7.21e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQ--ILGFGprsqgVFLARyGPAWREQRRFSVSTLRNL 142
Cdd:cd20670     1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQADEFSGRGELATIErnFQGHG-----VALAN-GERWRILRRFSLTILRNF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 143 GLGKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLRE 222
Cdd:cd20670    75 GMGKRSIEERIQEEAGYLLEEFRKTKGAPIDPTFFLSRTVSNVISSVVFGSRFDYEDKQFLSLLRMINESFIEMSTPWAQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 223 VLNAVP-VLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPaQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVAD 301
Cdd:cd20670   155 LYDMYSgIMQYLPGRHNRIYYLIEELKDFIASRVKINEASLDP-QNPRDFIDCFLIKMHQDKNNPHTEFNLKNLVLTTLN 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 302 LFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRD 381
Cdd:cd20670   234 LFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGVPHNVIRD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 382 IEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLL 461
Cdd:cd20670   314 TQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSIL 393

                  ....
gi 1034678150 462 QHFS 465
Cdd:cd20670   394 QNFS 397
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
65-473 3.79e-117

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: 351.21  E-value: 3.79e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPP------VPITQILGFGPrsqgvflarYGPAWREQRRFSVST 138
Cdd:cd11028     1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDfysfqfISNGKSMAFSD---------YGPRWKLHRKLAQNA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 139 LRNLGLGKKS--LEQWVTEEAACLCAAFANHSGR--PFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLK 214
Cdd:cd11028    72 LRTFSNARTHnpLEEHVTEEAEELVTELTENNGKpgPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFLELVKSNDDFGA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 215 -EESGFLREVLnavPVLLHIPAlaGKVLRFqKAFLTQLDELLT----EHRMTWDPAQPpRDLTEAFLAEMEK--AKGNPE 287
Cdd:cd11028   152 fVGAGNPVDVM---PWLRYLTR--RKLQKF-KELLNRLNSFILkkvkEHLDTYDKGHI-RDITDALIKASEEkpEEEKPE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 288 SSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFG 367
Cdd:cd11028   225 VGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHS 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 368 DIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKP--EAFLPFSAGRRACLG 445
Cdd:cd11028   305 SFVPFTIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDKTkvDKFLPFGAGRRRCLG 384
                         410       420
                  ....*....|....*....|....*...
gi 1034678150 446 EPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:cd11028   385 EELARMELFLFFATLLQQCEFSVKPGEK 412
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
65-493 1.09e-116

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: 350.27  E-value: 1.09e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILgfgPRSQGVFLARYGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20661    12 HGQIFSLDLGGISTVVLNGYDAVKECLVHQSEIFADRPSLPLFMKL---TNMGGLLNSKYGRGWTEHRKLAVNCFRYFGY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20661    89 GQKSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAWVFLY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLLHIPAlaGKVLR-FQKA-----FLTQLDELLTEHRMtwdpAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIV 298
Cdd:cd20661   169 NAFPWIGILPF--GKHQQlFRNAaevydFLLRLIERFSENRK----PQSPRHFIDAYLDEMDQNKNDPESTFSMENLIFS 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 299 VADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMT 378
Cdd:cd20661   243 VGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFHAT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 379 SRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFT 458
Cdd:cd20661   323 SKDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFT 402
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1034678150 459 SLLQHFSFSVAAGQPrPSHSRVVSFLVTPSPYELC 493
Cdd:cd20661   403 ALLQRFHLHFPHGLI-PDLKPKLGMTLQPQPYLIC 436
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
65-471 1.25e-115

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: 347.17  E-value: 1.25e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILgfgPRSQGVFLARyGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20671     1 YGPVFTIHLGMQKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAI---QHGNGVFFSS-GERWRTTRRFTVRSMKSLGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFrPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20671    77 GKRTIEDKILEELQFLNGQIDSFNGKPF-PLRLLGWAPTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLlhipalaGKVLRFQKAFLTQLDEL------LTEHRMTWDPAQPPRDLTEAFLAEMEKAKgNPESSFNDENLRIV 298
Cdd:cd20671   156 NLYPVL-------GAFLKLHKPILDKVEEVcmilrtLIEARRPTIDGNPLHSYIEALIQKQEEDD-PKETLFHDANVLAC 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 299 VADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPlGVTHMT 378
Cdd:cd20671   228 TLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLP-HVPRCT 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 379 SRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFT 458
Cdd:cd20671   307 AADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFT 386
                         410
                  ....*....|...
gi 1034678150 459 SLLQHFSFSVAAG 471
Cdd:cd20671   387 GLLQKFTFLPPPG 399
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
65-497 2.30e-113

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: 341.39  E-value: 2.30e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILgFgpRSQGVFLARyGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20668     1 YGPVFTIHLGPRRVVVLCGYDAVKEALVDQAEEFSGRGEQATFDWL-F--KGYGVAFSN-GERAKQLRRFSIATLRDFGV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLK---EESGFLR 221
Cdd:cd20668    77 GKRGIEERIQEEAGFLIDALRGTGGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQftaTSTGQLY 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 222 EVLNAVpvLLHIPA---LAGKVLRFQKAFLTQLDElltEHRMTWDPaQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIV 298
Cdd:cd20668   157 EMFSSV--MKHLPGpqqQAFKELQGLEDFIAKKVE---HNQRTLDP-NSPRDFIDSFLIRMQEEKKNPNTEFYMKNLVMT 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 299 VADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMT 378
Cdd:cd20668   231 TLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 379 SRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFT 458
Cdd:cd20668   311 TKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFT 390
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1034678150 459 SLLQHFSFSvaagQPRPSHsrvvSFLVTPSPYELCAVPR 497
Cdd:cd20668   391 TIMQNFRFK----SPQSPE----DIDVSPKHVGFATIPR 421
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
66-492 1.55e-105

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: 321.67  E-value: 1.55e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALvtHGEDTADRPPVPITQILGFGprsQGVFLARyGPAWREQRRFSVSTLRNLGL- 144
Cdd:cd20652     1 GSIFSLKMGSVYTVVLSDPKLIRDTF--RRDEFTGRAPLYLTHGIMGG---NGIICAE-GDLWRDQRRFVHDWLRQFGMt 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 ----GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKE--ESG 218
Cdd:cd20652    75 kfgnGRAKMEKRIATGVHELIKHLKAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFLQEEGTKLigVAG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 219 flreVLNAVPVLLHIPALAG---KVLRFQKAFLTQLDELLTEHRMTWDPAQPpRDLTEAFLAEMEKAK------GNPESS 289
Cdd:cd20652   155 ----PVNFLPFLRHLPSYKKaieFLVQGQAKTHAIYQKIIDEHKRRLKPENP-RDAEDFELCELEKAKkegedrDLFDGF 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 290 FNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDI 369
Cdd:cd20652   230 YTDEQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSV 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 370 VPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLA 449
Cdd:cd20652   310 VPLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELA 389
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1034678150 450 RMELFLFFTSLLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYEL 492
Cdd:cd20652   390 RMILFLFTARILRKFRIALPDGQPVDSEGGNVGITLTPPPFKI 432
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
65-463 3.03e-92

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: 287.29  E-value: 3.03e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPitqilGFGPRSQGVFLA--RYGPAWREQRRFSVSTLRNL 142
Cdd:cd20675     1 YGDVFQIRLGSRPVVVLNGERAIRQALVQQGTDFAGRPDFA-----SFRVVSGGRSLAfgGYSERWKAHRRVAHSTVRAF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 143 GLG----KKSLEQWVTEEAACLCAAFANHS--GRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLdlaqeGLKEE 216
Cdd:cd20675    76 STRnprtRKAFERHVLGEARELVALFLRKSagGAYFDPAPPLVVAVANVMSAVCFGKRYSHDDAEFRSLL-----GRNDQ 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 217 sgFLREV-----LNAVPVLLHIP----ALAGKVLRFQKAFLTQLDELLTEHRMTWDPAqPPRDLTEAFLAEMEKAKGNPE 287
Cdd:cd20675   151 --FGRTVgagslVDVMPWLQYFPnpvrTVFRNFKQLNREFYNFVLDKVLQHRETLRGG-APRDMMDAFILALEKGKSGDS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 288 SSFND-ENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRF 366
Cdd:cd20675   228 GVGLDkEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRF 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 367 GDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAF--LPFSAGRRACL 444
Cdd:cd20675   308 SSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFLNKDLASsvMIFSVGKRRCI 387
                         410
                  ....*....|....*....
gi 1034678150 445 GEPLARMELFLfFTSLLQH 463
Cdd:cd20675   388 GEELSKMQLFL-FTSILAH 405
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
65-487 8.48e-90

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: 281.13  E-value: 8.48e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprSQGVFLARYGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20673     1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRN--GKDIAFADYSATWQLHRKLVHSAFALFGE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQeglkeesGFLREV- 223
Cdd:cd20673    79 GSQKLEKIICQEASSLCDTLATHNGESIDLSPPLFRAVTNVICLLCFNSSYKNGDPELETILNYNE-------GIVDTVa 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 224 ----LNAVPVLLHIPalaGKVLRFQKAFLTQLDELLT----EHRMTWDPaQPPRDLTEAFLaemeKAKGNPE-------- 287
Cdd:cd20673   152 kdslVDIFPWLQIFP---NKDLEKLKQCVKIRDKLLQkkleEHKEKFSS-DSIRDLLDALL----QAKMNAEnnnagpdq 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 288 --SSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQR 365
Cdd:cd20673   224 dsVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLR 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 366 FGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQG-HFVKP-EAFLPFSAGRRAC 443
Cdd:cd20673   304 IRPVAPLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGsQLISPsLSYLPFGAGPRVC 383
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1034678150 444 LGEPLARMELFLFFTSLLQHFSFSVAAGQPRPS---HSRVVsFLVTP 487
Cdd:cd20673   384 LGEALARQELFLFMAWLLQRFDLEVPDGGQLPSlegKFGVV-LQIDP 429
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
65-462 4.52e-87

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: 274.28  E-value: 4.52e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprSQGVFLARYGPAWREQRRFSVSTLRNLGL 144
Cdd:cd20677     1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPDFYTFSLIANG--KSMTFSEKYGESWKLHKKIAKNALRTFSK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 GKKS-------LEQWVTEEAACLCAAFANHSGR--PFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKE 215
Cdd:cd20677    79 EEAKsstcsclLEEHVCAEASELVKTLVELSKEkgSFDPVSLITCAVANVVCALCFGKRYDHSDKEFLTIVEINNDLLKA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 216 ESGFLreVLNAVPVLLHIPALAGKVLR-FQKAFLTQLDELLTEHRMTWDpAQPPRDLTEAFLAEMEKAKGNPESS-FNDE 293
Cdd:cd20677   159 SGAGN--LADFIPILRYLPSPSLKALRkFISRLNNFIAKSVQDHYATYD-KNHIRDITDALIALCQERKAEDKSAvLSDE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 294 NLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLG 373
Cdd:cd20677   236 QIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSFVPFT 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 374 VTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKP--EAFLPFSAGRRACLGEPLARM 451
Cdd:cd20677   316 IPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSlvEKVLIFGMGVRKCLGEDVARN 395
                         410
                  ....*....|.
gi 1034678150 452 ELFLFFTSLLQ 462
Cdd:cd20677   396 EIFVFLTTILQ 406
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
65-473 1.50e-86

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: 273.04  E-value: 1.50e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVP----IT--QILGFGPRSqgvflaryGPAWREQRRFSVST 138
Cdd:cd20676     1 YGDVLQIQIGSRPVVVLSGLDTIRQALVKQGDDFKGRPDLYsfrfISdgQSLTFSTDS--------GPVWRARRKLAQNA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 139 LRNLGL--GKKS-----LEQWVTEEAACLCAAF---ANHSGRpFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDL 208
Cdd:cd20676    73 LKTFSIasSPTSsssclLEEHVSKEAEYLVSKLqelMAEKGS-FDPYRYIVVSVANVICAMCFGKRYSHDDQELLSLVNL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 209 AQE-GLKEESGFLrevLNAVPVLLHIPALAGKV-LRFQKAFLTQLDELLTEHRMTWDPAQPpRDLTEAFLAEMEKAKGNP 286
Cdd:cd20676   152 SDEfGEVAGSGNP---ADFIPILRYLPNPAMKRfKDINKRFNSFLQKIVKEHYQTFDKDNI-RDITDSLIEHCQDKKLDE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 287 ESSFNDENLRIV--VADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQ 364
Cdd:cd20676   228 NANIQLSDEKIVniVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETF 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 365 RFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFV-KPEA--FLPFSAGRR 441
Cdd:cd20676   308 RHSSFVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEInKTESekVMLFGLGKR 387
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1034678150 442 ACLGEPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:cd20676   388 RCIGESIARWEVFLFLAILLQQLEFSVPPGVK 419
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
65-493 2.95e-82

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: 261.19  E-value: 2.95e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSqgVFLARYGPAWREQRRFSVSTLRNLGl 144
Cdd:cd20674     1 YGPIYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTGKLVSQGGQD--LSLGDYSLLWKAHRKLTRSALQLGI- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 gKKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEyDDPRFLRLLDLAQEGLKEESGFLREVL 224
Cdd:cd20674    78 -RNSLEPVVEQLTQELCERMRAQAGTPVDIQEEFSLLTCSIICCLTFGDKED-KDTLVQAFHDCVQELLKTWGHWSIQAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 225 NAVPVLLHIPALAgkvLRFQKAFLTQLDEL----LTEHRMTWDpAQPPRDLTEAFLAEMEKAKGN-PESSFNDENLRIVV 299
Cdd:cd20674   156 DSIPFLRFFPNPG---LRRLKQAVENRDHIvesqLRQHKESLV-AGQWRDMTDYMLQGLGQPRGEkGMGQLLEGHVHMAV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 300 ADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTS 379
Cdd:cd20674   232 VDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTT 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 380 RDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGhfvKPEAFLPFSAGRRACLGEPLARMELFLFFTS 459
Cdd:cd20674   312 RDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGA---ANRALLPFGCGARVCLGEPLARLELFVFLAR 388
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1034678150 460 LLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYELC 493
Cdd:cd20674   389 LLQAFTLLPPSDGALPSLQPVAGINLKVQPFQVR 422
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
65-467 1.93e-78

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: 251.34  E-value: 1.93e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQ-ILGFGPRsqgVFLARYGPAWREQRRFSVSTLRNLG 143
Cdd:cd11065     1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGeLMGWGMR---LLLMPYGPRWRLHRRLFHQLLNPSA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 144 LgkKSLEQWVTEEAACLCAAFANHsgrPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESGFLREV 223
Cdd:cd11065    78 V--RKYRPLQELESKQLLRDLLES---PDDFLDHIRRYAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGSPGAYL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 224 LNAVPVLLHIPA-LAGKVLRFQKAFLTQLDELLTEH------RMTWDPAQPPrdLTEAFLAEMEKakgnpESSFNDENLR 296
Cdd:cd11065   153 VDFFPFLRYLPSwLGAPWKRKARELRELTRRLYEGPfeaakeRMASGTATPS--FVKDLLEELDK-----EGGLSEEEIK 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 297 IVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTH 376
Cdd:cd11065   226 YLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIPH 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 377 MTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLD--AQGHFVKPEAFLPFSAGRRACLGEPLARMELF 454
Cdd:cd11065   306 ALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDdpKGTPDPPDPPHFAFGFGRRICPGRHLAENSLF 385
                         410
                  ....*....|...
gi 1034678150 455 LFFTSLLQHFSFS 467
Cdd:cd11065   386 IAIARLLWAFDIK 398
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
66-474 3.76e-70

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: 229.75  E-value: 3.76e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPrsQGVFLARYGPAWREQRRFSVSTLrnlgLG 145
Cdd:cd20618     1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNG--QDIVFAPYGPHWRHLRKICTLEL----FS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 146 KKSLE--QWV-TEEAACLCAAFANHS--GRPFRPNGLLDKAVSNVIASLTCGRRF----EYDDPRFLRLLDLAQEglkee 216
Cdd:cd20618    75 AKRLEsfQGVrKEELSHLVKSLLEESesGKPVNLREHLSDLTLNNITRMLFGKRYfgesEKESEEAREFKELIDE----- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 217 sgfLREVLNAVPVLLHIPALA----GKVLRFQKAFLTQLDELLT----EHRMTWDPAQPPRDLTEAFLAEMEKakgNPES 288
Cdd:cd20618   150 ---AFELAGAFNIGDYIPWLRwldlQGYEKRMKKLHAKLDRFLQkiieEHREKRGESKKGGDDDDDLLLLLDL---DGEG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 289 SFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGD 368
Cdd:cd20618   224 KLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHP 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 369 IVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAF--LPFSAGRRACLGE 446
Cdd:cd20618   304 PGPLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVKGQDFelLPFGSGRRMCPGM 383
                         410       420
                  ....*....|....*....|....*....
gi 1034678150 447 PLA-RMeLFLFFTSLLQHFSFSVAAGQPR 474
Cdd:cd20618   384 PLGlRM-VQLTLANLLHGFDWSLPGPKPE 411
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
66-473 2.18e-57

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: 195.43  E-value: 2.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALVTHgEDTADRPPVPITQILGFGPRSqgvFLARYGPAWREQRRFSVSTLRNLGLg 145
Cdd:cd00302     1 GPVFRVRLGGGPVVVVSDPELVREVLRDP-RDFSSDAGPGLPALGDFLGDG---LLTLDGPEHRRLRRLLAPAFTPRAL- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 146 kKSLEQWVTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLDLAQEGLKEESgflrevln 225
Cdd:cd00302    76 -AALRPVIREIARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLKLLGPRL-------- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 226 avpvllhIPALAGKVLRFQKAFLTQLDELLTEHRMTwDPAQPPRDLTEAFLAEMEKAKGnpessFNDENLRIVVADLFSA 305
Cdd:cd00302   147 -------LRPLPSPRLRRLRRARARLRDYLEELIAR-RRAEPADDLDLLLLADADDGGG-----LSDEEIVAELLTLLLA 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 306 GMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGqvrRPEMGDQAHMPYTTAVIHEVQRFgDIVPLGVTHMTSRDIEVQ 385
Cdd:cd00302   214 GHETTASLLAWALYLLARHPEVQERLRAEIDAVLG---DGTPEDLSKLPYLEAVVEETLRL-YPPVPLLPRVATEDVELG 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 386 GFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDaqGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFS 465
Cdd:cd00302   290 GYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLP--EREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFD 367

                  ....*...
gi 1034678150 466 FSVAAGQP 473
Cdd:cd00302   368 FELVPDEE 375
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
66-472 7.03e-53

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: 184.55  E-value: 7.03e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprSQGVFLARYGPAWREQRRFSVSTLrnlgLG 145
Cdd:cd20657     1 GPIMYLKVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMAYN--AQDMVFAPYGPRWRLLRKLCNLHL----FG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 146 KKSLEQWV---TEEAACLCAAFANHS--GRPFRPNGLLDKAVSNVIASLTCGRR-FEYD-DPRFLRLLDLAQEgLKEESG 218
Cdd:cd20657    75 GKALEDWAhvrENEVGHMLKSMAEASrkGEPVVLGEMLNVCMANMLGRVMLSKRvFAAKaGAKANEFKEMVVE-LMTVAG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 219 FLrEVLNAVPVL--LHIPALAGKVLRFQKAFLTQLDELLTEHRMT-WDPAQPPRDLTEAFLAEMEKAKGNpesSFNDENL 295
Cdd:cd20657   154 VF-NIGDFIPSLawMDLQGVEKKMKRLHKRFDALLTKILEEHKATaQERKGKPDFLDFVLLENDDNGEGE---RLTDTNI 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 296 RIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVT 375
Cdd:cd20657   230 KALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLP 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 376 HMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEA----FLPFSAGRRACLGEPL-AR 450
Cdd:cd20657   310 RIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGRNAKVDVRGndfeLIPFGAGRRICAGTRMgIR 389
                         410       420
                  ....*....|....*....|..
gi 1034678150 451 MELFLFFTsLLQHFSFSVAAGQ 472
Cdd:cd20657   390 MVEYILAT-LVHSFDWKLPAGQ 410
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
62-464 2.91e-52

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: 182.73  E-value: 2.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  62 RRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSqgVFLARYGPAWREQRRFSVSTL-- 139
Cdd:cd11073     1 AKKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSS--IVWPPYGPRWRMLRKICTTELfs 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 140 -RNL----GLGKKSLEQ---WVTEEAAclcaafanhSGRPFRPNGLLDKAVSNVIASLTCGRrfeyddprflrllDLAQE 211
Cdd:cd11073    79 pKRLdatqPLRRRKVRElvrYVREKAG---------SGEAVDIGRAAFLTSLNLISNTLFSV-------------DLVDP 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 212 GLKEESGFlREVLNAVPVLLHIPALAG--KVLRF---------QKAFLTQLDEL---LTEHRMTWDPAQPPRDLTEAFLA 277
Cdd:cd11073   137 DSESGSEF-KELVREIMELAGKPNVADffPFLKFldlqglrrrMAEHFGKLFDIfdgFIDERLAEREAGGDKKKDDDLLL 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 278 EMEKAKGNpESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTT 357
Cdd:cd11073   216 LLDLELDS-ESELTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQ 294
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 358 AVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFL----DAQGHfvKPEaF 433
Cdd:cd11073   295 AVVKETLRLHPPAPLLLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLgseiDFKGR--DFE-L 371
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1034678150 434 LPFSAGRRACLGEPLA-RMeLFLFFTSLLQHF 464
Cdd:cd11073   372 IPFGSGRRICPGLPLAeRM-VHLVLASLLHSF 402
PLN02687 PLN02687
flavonoid 3'-monooxygenase
61-472 1.08e-51

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 183.47  E-value: 1.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  61 LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprSQGVFLARYGPAWREQRR------F 134
Cdd:PLN02687   62 LAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHDANFSNRPPNSGAEHMAYN--YQDLVFAPYGPRWRALRKicavhlF 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 135 SVSTLRNLglgkKSLEQwvtEEAACLCAAFANHSGRPFRPNG-LLDKAVSNVIASLTCGRR-FEYD-DPRFLRLLDLAQE 211
Cdd:PLN02687  140 SAKALDDF----RHVRE---EEVALLVRELARQHGTAPVNLGqLVNVCTTNALGRAMVGRRvFAGDgDEKAREFKEMVVE 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 212 gLKEESGFLrEVLNAVPVL--LHIPALAGKVLRFQKAFLTQLDELLTEHRM-TWDPAQPPRDLTEAFLAEMEKAKGNPE- 287
Cdd:PLN02687  213 -LMQLAGVF-NVGDFVPALrwLDLQGVVGKMKRLHRRFDAMMNGIIEEHKAaGQTGSEEHKDLLSTLLALKREQQADGEg 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 288 SSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFG 367
Cdd:PLN02687  291 GRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLH 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 368 DIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHF---VKPEAF--LPFSAGRRA 442
Cdd:PLN02687  371 PSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPGGEHAgvdVKGSDFelIPFGAGRRI 450
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1034678150 443 CLGEPLA-RMELFLFFTsLLQHFSFSVAAGQ 472
Cdd:PLN02687  451 CAGLSWGlRMVTLLTAT-LVHAFDWELADGQ 480
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
64-471 2.36e-50

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: 177.65  E-value: 2.36e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  64 RFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRsqGVFLARYGPAWREQRRFSVSTLrnlg 143
Cdd:cd11072     1 KYGPLMLLRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGK--DIAFAPYGEYWRQMRKICVLEL---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 144 LGKK---SLEQWVTEEAACLCAAFANHSGRPFRPNglLDKAVSNVIASLTC----GRRFEYDDPRflRLLDLAQEGLKEE 216
Cdd:cd11072    75 LSAKrvqSFRSIREEEVSLLVKKIRESASSSSPVN--LSELLFSLTNDIVCraafGRKYEGKDQD--KFKELVKEALELL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 217 SGFlrEVLNAVPVLLHIPALAGKVLRFQKAFLTQ---LDELLTEHRMTWDPAQPPRDLTEAFLAEMEKaKGNPESSFNDE 293
Cdd:cd11072   151 GGF--SVGDYFPSLGWIDLLTGLDRKLEKVFKELdafLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQK-EGDLEFPLTRD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 294 NLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLG 373
Cdd:cd11072   228 NIKAIILDMFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 374 VTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFL----DAQG-HFvkpeAFLPFSAGRRAC----L 444
Cdd:cd11072   308 LPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLdssiDFKGqDF----ELIPFGAGRRICpgitF 383
                         410       420
                  ....*....|....*....|....*..
gi 1034678150 445 GepLARMELFLffTSLLQHFSFSVAAG 471
Cdd:cd11072   384 G--LANVELAL--ANLLYHFDWKLPDG 406
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
66-473 3.52e-48

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: 172.03  E-value: 3.52e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVflARYGPAWREQRRFSVSTLrnlgLG 145
Cdd:cd20654     1 GPIFTLRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMGYNYAMFGF--APYGPYWRELRKIATLEL----LS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 146 KKSLEQW----VTEEAACLCAAF-------ANHSGRPFRPNGLLDKAVSNVIASLTCGRRF-----EYDDPRFLRLldla 209
Cdd:cd20654    75 NRRLEKLkhvrVSEVDTSIKELYslwsnnkKGGGGVLVEMKQWFADLTFNVILRMVVGKRYfggtaVEDDEEAERY---- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 210 QEGLKEesgFLRevLNAVPVLL-HIPALA----GKVLRFQKAFLTQLDELLT----EHRMTWDPAQPPRDLTEAFLAEME 280
Cdd:cd20654   151 KKAIRE---FMR--LAGTFVVSdAIPFLGwldfGGHEKAMKRTAKELDSILEewleEHRQKRSSSGKSKNDEDDDDVMML 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 281 KAKGNPESSFNDENLRI--VVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTA 358
Cdd:cd20654   226 SILEDSQISGYDADTVIkaTCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 359 VIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFL------DAQG-HFvkpe 431
Cdd:cd20654   306 IVKETLRLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLtthkdiDVRGqNF---- 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1034678150 432 AFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:cd20654   382 ELIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIKTPSNEP 423
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
58-488 2.20e-46

cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins, including Nostoc sp. probable cytochrome P450 110 (CYP110) and putative cytochrome P450s 139 (CYP139), 138 (CYP138), and 135B1 (CYP135B1) from Mycobacterium bovis. CYP110 genes, unique to cyanobacteria, are widely distributed in heterocyst-forming cyanobacteria including nitrogen-fixing genera Nostoc and Anabaena. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410676 [Multi-domain]  Cd Length: 415  Bit Score: 166.60  E-value: 2.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  58 FDQLRRRFGDVFSLQLAWT-PVVVLNGLAAVREALVTHGEDTADRP-PVPITQIlgFGPRSqgVFLARyGPAWREQRR-- 133
Cdd:cd11053     4 LERLRARYGDVFTLRVPGLgPVVVLSDPEAIKQIFTADPDVLHPGEgNSLLEPL--LGPNS--LLLLD-GDRHRRRRKll 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 134 ---FSVSTLRNLG-----LGKKSLEQWVteeaaclcaafanhSGRPFRPNGLLDKAVSNVIASLTCGrrfEYDDPRFLRL 205
Cdd:cd11053    79 mpaFHGERLRAYGeliaeITEREIDRWP--------------PGQPFDLRELMQEITLEVILRVVFG---VDDGERLQEL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 206 LDLAQEGLKeesgFLREVLNAVPVLLHIPALAGKVLRFQKAfLTQLDELL----TEHRmtWDPAQPPRDLteafLAEMEK 281
Cdd:cd11053   142 RRLLPRLLD----LLSSPLASFPALQRDLGPWSPWGRFLRA-RRRIDALIyaeiAERR--AEPDAERDDI----LSLLLS 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 282 AKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQvrrPEMGDQAHMPYTTAVIH 361
Cdd:cd11053   211 ARDEDGQPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGD---PDPEDIAKLPYLDAVIK 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 362 EVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQghfVKPEAFLPFSAGRR 441
Cdd:cd11053   288 ETLRLYPVAPL-VPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRK---PSPYEYLPFGGGVR 363
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1034678150 442 ACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRPSHSRvvSFLVTPS 488
Cdd:cd11053   364 RCIGAAFALLEMKVVLATLLRRFRLELTDPRPERPVRR--GVTLAPS 408
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
66-473 2.14e-44

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: 161.61  E-value: 2.14e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprSQGVFLARYGPAWREQRRFSVSTLrnlgLG 145
Cdd:cd20655     1 GPLLHLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYG--SSGFAFAPYGDYWKFMKKLCMTEL----LG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 146 KKSLEQWvteeaaclcaafanhsgRPFRPNG-------LLDKA---------------VSNVIASLTCGRRFEYDDPRFL 203
Cdd:cd20655    75 PRALERF-----------------RPIRAQElerflrrLLDKAekgesvdigkelmklTNNIICRMIMGRSCSEENGEAE 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 204 RLLDLAQEglkeeSGFLREVLNAVPVL-----LHIPALAGKVLRFQKAFLTQLDELLTEH--RMTWDPAQPPRDLTEAFL 276
Cdd:cd20655   138 EVRKLVKE-----SAELAGKFNASDFIwplkkLDLQGFGKRIMDVSNRFDELLERIIKEHeeKRKKRKEGGSKDLLDILL 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 277 A--EMEKAkgnpESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMP 354
Cdd:cd20655   213 DayEDENA----EYKITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLP 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 355 YTTAVIHEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEA-- 432
Cdd:cd20655   289 YLQAVVKETLRLHPPGPL-LVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRSGQELDVrg 367
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1034678150 433 ----FLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:cd20655   368 qhfkLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCFDWKVGDGEK 412
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
66-464 6.32e-43

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: 157.38  E-value: 6.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprSQGVFLARYGPAWREQRRFSV----STLR- 140
Cdd:cd20653     1 GPIFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLTGKHIGYN--YTTVGSAPYGDHWRNLRRITTleifSSHRl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 141 --NLGLGKksleqwvtEEAACLCAAFANHSGRPFRPNGL---LDKAVSNVIASLTCGRRFEYDDprflrlldlaqEGLKE 215
Cdd:cd20653    79 nsFSSIRR--------DEIRRLLKRLARDSKGGFAKVELkplFSELTFNNIMRMVAGKRYYGED-----------VSDAE 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 216 ESGFLREVLNAV-------------PVL--LHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQppRDLTEAFLAEME 280
Cdd:cd20653   140 EAKLFRELVSEIfelsgagnpadflPILrwFDFQGLEKRVKKLAKRRDAFLQGLIDEHRKNKESGK--NTMIDHLLSLQE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 281 KakgNPESsFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI 360
Cdd:cd20653   218 S---QPEY-YTDEIIKGLILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNII 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 361 HEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFldaQGHFVKPEAFLPFSAGR 440
Cdd:cd20653   294 SETLRLYPAAPLLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF---EGEEREGYKLIPFGLGR 370
                         410       420
                  ....*....|....*....|....
gi 1034678150 441 RACLGEPLARMELFLFFTSLLQHF 464
Cdd:cd20653   371 RACPGAGLAQRVVGLALGSLIQCF 394
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
50-481 1.17e-42

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: 156.21  E-value: 1.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  50 DFQNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSqgvFLARYGPAWR 129
Cdd:COG2124    16 AFLRDPYPFYARLREYGPVFRVRLPGGGAWLVTRYEDVREVLRDPRTFSSDGGLPEVLRPLPLLGDS---LLTLDGPEHT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 130 EQRR-----FSVSTLRnlglgkkSLEQWVTEEAACLCAAFANHSGRPFRPnglldkAVSNVIASLTCGRRFEYDDPRFLR 204
Cdd:COG2124    93 RLRRlvqpaFTPRRVA-------ALRPRIREIADELLDRLAARGPVDLVE------EFARPLPVIVICELLGVPEEDRDR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 205 LLDLAQEGLKEESGFLREVLnavpvllhipalaGKVLRFQKAFLTQLDELLTEHRmtwdpAQPPRDLTEAFLAEmeKAKG 284
Cdd:COG2124   160 LRRWSDALLDALGPLPPERR-------------RRARRARAELDAYLRELIAERR-----AEPGDDLLSALLAA--RDDG 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 285 NPessFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIddvigqvrrpemgdqahmPYTTAVIHEVQ 364
Cdd:COG2124   220 ER---LSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETL 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 365 RFGDIVPlGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHfldaqghfvKPEAFLPFSAGRRACL 444
Cdd:COG2124   279 RLYPPVP-LLPRTATEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCL 348
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1034678150 445 GEPLARMELFLFFTSLLQHF-SFSVAAGQ-PRPSHSRVV 481
Cdd:COG2124   349 GAALARLEARIALATLLRRFpDLRLAPPEeLRWRPSLTL 387
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
60-455 2.57e-41

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 154.62  E-value: 2.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  60 QLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprSQGVFLARYGPAWREQRRFSVSTL 139
Cdd:PLN00110   58 KMAKRYGPVMFLKMGTNSMVVASTPEAARAFLKTLDINFSNRPPNAGATHLAYG--AQDMVFADYGPRWKLLRKLSNLHM 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 140 rnlgLGKKSLEQW----VTEEAACLCAAF-ANHSGRPFRPNGLLDKAVSNVIASLTCGRR-FEYDDPRFLRLLDLAQEgL 213
Cdd:PLN00110  136 ----LGGKALEDWsqvrTVELGHMLRAMLeLSQRGEPVVVPEMLTFSMANMIGQVILSRRvFETKGSESNEFKDMVVE-L 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 214 KEESGFLrEVLNAVPVL--LHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAkgnPESSFN 291
Cdd:PLN00110  211 MTTAGYF-NIGDFIPSIawMDIQGIERGMKHLHKKFDKLLTRMIEEHTASAHERKGNPDFLDVVMANQENS---TGEKLT 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 292 DENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVP 371
Cdd:PLN00110  287 LTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTP 366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 372 LGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEA----FLPFSAGRRACLGep 447
Cdd:PLN00110  367 LNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKIDPRGndfeLIPFGAGRRICAG-- 444

                  ....*...
gi 1034678150 448 lARMELFL 455
Cdd:PLN00110  445 -TRMGIVL 451
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
64-473 4.13e-41

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: 152.78  E-value: 4.13e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  64 RFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILgFGPRSQGVFLARYGPAWREQRRFSVSTLrnlg 143
Cdd:cd11075     1 KYGPIFTLRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPLRVL-FSSNKHMVNSSPYGPLWRTLRRNLVSEV---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 144 LGKKSLEQWvteeaaclcaafanhsgRPFRpngllDKAVSNVIASLtcgRRFEYDDPRFLRLLDLAQ------------- 210
Cdd:cd11075    76 LSPSRLKQF-----------------RPAR-----RRALDNLVERL---REEAKENPGPVNVRDHFRhalfslllymcfg 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 211 EGLKEES-----GFLREVL---NAVPVLLHIPALAgKVLRFQ--KAFLT----QLD---ELLTEHRMTWDPAQPPRDLTE 273
Cdd:cd11075   131 ERLDEETvreleRVQRELLlsfTDFDVRDFFPALT-WLLNRRrwKKVLElrrrQEEvllPLIRARRKRRASGEADKDYTD 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 274 AFLAEMEKAKGNPESS-FNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAH 352
Cdd:cd11075   210 FLLLDLLDLKEEGGERkLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPK 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 353 MPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLD-----AQGHF 427
Cdd:cd11075   290 MPYLKAVVLETLRRHPPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAggeaaDIDTG 369
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1034678150 428 VKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:cd11075   370 SKEIKMMPFGAGRRICPGLGLATLHLELFVARLVQEFEWKLVEGEE 415
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
66-473 6.89e-41

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: 151.58  E-value: 6.89e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILgFGprsQGVFLARyGPAWREQRR-----FSVSTLR 140
Cdd:cd20620     1 GDVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVKGGVYERLKLL-LG---NGLLTSE-GDLWRRQRRlaqpaFHRRRIA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 141 NLGlgkksleQWVTEEAACLCAAFanHSGRPFRPNGLLDK--AVSNVIASLTC-GRRFEYDDPRFLRLLDLAQEGlkees 217
Cdd:cd20620    76 AYA-------DAMVEATAALLDRW--EAGARRGPVDVHAEmmRLTLRIVAKTLfGTDVEGEADEIGDALDVALEY----- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 218 gFLREVLNAVPVLLHIPAlaGKVLRFQKAFLTqLDE----LLTEHRmtwdpAQPPR--DLTEAFLAEMEKAKGNPESsfn 291
Cdd:cd20620   142 -AARRMLSPFLLPLWLPT--PANRRFRRARRR-LDEviyrLIAERR-----AAPADggDLLSMLLAARDEETGEPMS--- 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 292 DENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQvRRPEMGDQAHMPYTTAVIHEVQRFGDIVP 371
Cdd:cd20620   210 DQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGG-RPPTAEDLPQLPYTEMVLQESLRLYPPAW 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 372 LgVTHMTSRDIEVQGFRIPKGTTLItnLSSVL--KDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLA 449
Cdd:cd20620   289 I-IGREAVEDDEIGGYRIPAGSTVL--ISPYVthRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFA 365
                         410       420
                  ....*....|....*....|....
gi 1034678150 450 RMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:cd20620   366 MMEAVLLLATIAQRFRLRLVPGQP 389
PTZ00404 PTZ00404
cytochrome P450; Provisional
59-473 2.19e-39

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 149.10  E-value: 2.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  59 DQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQilgFGPRSQGVfLARYGPAWREQRRFSVST 138
Cdd:PTZ00404   55 TKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNFSDRPKIPSIK---HGTFYHGI-VTSSGEYWKRNREIVGKA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 139 LR--NLGLGKKSLEQWVTEeaacLCAAFANH--SGRPFRPNGLLDKAVSNVIASLTCGRRFEYDD----PRFLRLLDLAQ 210
Cdd:PTZ00404  131 MRktNLKHIYDLLDDQVDV----LIESMKKIesSGETFEPRYYLTKFTMSAMFKYIFNEDISFDEdihnGKLAELMGPME 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 211 EGLKE-ESGFLREVLN-AVPVLLHIPALAGKVLRFQKAFLTqldELLTEHRMTWDPaQPPRDLTEAFLAEMekakgnpeS 288
Cdd:PTZ00404  207 QVFKDlGSGSLFDVIEiTQPLYYQYLEHTDKNFKKIKKFIK---EKYHEHLKTIDP-EVPRDLLDLLIKEY--------G 274
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 289 SFNDEN-LRI--VVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQR 365
Cdd:PTZ00404  275 TNTDDDiLSIlaTILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLR 354
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 366 FGDIVPLGVTHMTSRDIEV-QGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQghfvKPEAFLPFSAGRRACL 444
Cdd:PTZ00404  355 YKPVSPFGLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPD----SNDAFMPFSIGPRNCV 430
                         410       420
                  ....*....|....*....|....*....
gi 1034678150 445 GEPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:PTZ00404  431 GQQFAQDELYLAFSNIILNFKLKSIDGKK 459
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
65-487 5.97e-39

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: 146.86  E-value: 5.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQilGFGPRSQGVFLARYGPAWREQRRfsVSTLRNLGL 144
Cdd:cd20656     1 YGPIISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAA--RFSRNGQDLIWADYGPHYVKVRK--LCTLELFTP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 145 gkKSLE--QWVTE-EAACLCAAFANH------SGRPFRPNGLLDKAVSNVIASLTCGRRFEYD----DPRFLRLLDLAQE 211
Cdd:cd20656    77 --KRLEslRPIREdEVTAMVESIFNDcmspenEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAegvmDEQGVEFKAIVSN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 212 GLKeesgflreVLNAVPVLLHIPALAGKVLRFQKAFLTQLD-------ELLTEHRMTWDPAQPPRDLTEAFLAEMEKakg 284
Cdd:cd20656   155 GLK--------LGASLTMAEHIPWLRWMFPLSEKAFAKHGArrdrltkAIMEEHTLARQKSGGGQQHFVALLTLKEQ--- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 285 npeSSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQ 364
Cdd:cd20656   224 ---YDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEAL 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 365 RFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFL----DAQGHFVKpeaFLPFSAGR 440
Cdd:cd20656   301 RLHPPTPLMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLeedvDIKGHDFR---LLPFGAGR 377
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034678150 441 RACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRP-----SHSRVVSFLVTP 487
Cdd:cd20656   378 RVCPGAQLGINLVTLMLGHLLHHFSWTPPEGTPPEeidmtENPGLVTFMRTP 429
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
289-467 1.71e-37

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: 142.66  E-value: 1.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 289 SFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQV-RRPEMGDQAHMPYTTAVIHEVQRFG 367
Cdd:cd20628   224 PLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDDdRRPTLEDLNKMKYLERVIKETLRLY 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 368 DIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEP 447
Cdd:cd20628   304 PSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIPFSAGPRNCIGQK 382
                         170       180
                  ....*....|....*....|
gi 1034678150 448 LARMELFLFFTSLLQHFSFS 467
Cdd:cd20628   383 FAMLEMKTLLAKILRNFRVL 402
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
297-464 3.34e-37

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: 141.90  E-value: 3.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 297 IVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPlGVTH 376
Cdd:cd11054   234 TMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPVAP-GNGR 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 377 MTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAF--LPFSAGRRACLGEPLARMELF 454
Cdd:cd11054   313 ILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENKNIHPFasLPFGFGPRMCIGRRFAELEMY 392
                         170
                  ....*....|
gi 1034678150 455 LFFTSLLQHF 464
Cdd:cd11054   393 LLLAKLLQNF 402
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
141-492 1.83e-36

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: 139.67  E-value: 1.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 141 NLGLGKKSLEQW---VTEEAACLCAAFANHSGRPfrPNGLLDKA------VSNVIASLTCGRRFEY-DDPRFLRLLDLAQ 210
Cdd:cd11061    62 SHAFSDKALRGYeprILSHVEQLCEQLDDRAGKP--VSWPVDMSdwfnylSFDVMGDLAFGKSFGMlESGKDRYILDLLE 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 211 EGLKEESGFLRevLNAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRMTWDPaqPPRDLTEAFLAEMEKAKGNPESsf 290
Cdd:cd11061   140 KSMVRLGVLGH--APWLRPLLLDLPLFPGATKARKRFLDFVRAQLKERLKAEEE--KRPDIFSYLLEAKDPETGEGLD-- 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 291 ndenLRIVVAD---LFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQ-AHMPYTTAVIHEVQRF 366
Cdd:cd11061   214 ----LEELVGEarlLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLGPKlKSLPYLRACIDEALRL 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 367 GDIVPLGVTHMTSRD-IEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPE-AFLPFSAGRRACL 444
Cdd:cd11061   290 SPPVPSGLPRETPPGgLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVRARsAFIPFSIGPRGCI 369
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1034678150 445 GEPLARMELFLFFTSLLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYEL 492
Cdd:cd11061   370 GKNLAYMELRLVLARLLHRYDFRLAPGEDGEAGEGGFKDAFGRGPGDL 417
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
268-473 1.33e-35

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: 137.27  E-value: 1.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 268 PRDLteafLAEMEKAKGNpESSFNDENLrivVAD---LFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRR 344
Cdd:cd20613   213 PNDI----LTHILKASEE-EPDFDMEEL---LDDfvtFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQY 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 345 PEMGDQAHMPYTTAVIHEVQRFGDIVPlGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQ 424
Cdd:cd20613   285 VEYEDLGKLEYLSQVLKETLRLYPPVP-GTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEA 363
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034678150 425 GHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:cd20613   364 PEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKFELVPGQS 412
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
58-471 1.45e-34

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 135.72  E-value: 1.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  58 FDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGprSQGVFLARYGPAWREQRRFSVS 137
Cdd:PLN03112   57 LASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQDDVFASRPRTLAAVHLAYG--CGDVALAPLGPHWKRMRRICME 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 138 TLrnlgLGKKSLEQWVT---EEAACLCAAF--ANHSGRPFRPNGLLDKAVSNVIASLTCGRRFeyddprflrlLDLAQEG 212
Cdd:PLN03112  135 HL----LTTKRLESFAKhraEEARHLIQDVweAAQTGKPVNLREVLGAFSMNNVTRMLLGKQY----------FGAESAG 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 213 LKEESGF------LREVLNAVPVLLHIPALA--------GKVLRFQKAFLTQLDELLTEHRMTWD---PAQPPRDLTEAF 275
Cdd:PLN03112  201 PKEAMEFmhitheLFRLLGVIYLGDYLPAWRwldpygceKKMREVEKRVDEFHDKIIDEHRRARSgklPGGKDMDFVDVL 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 276 LAEMEKakgNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPY 355
Cdd:PLN03112  281 LSLPGE---NGKEHMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNY 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 356 TTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVK----PE 431
Cdd:PLN03112  358 LRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAEGSRVEishgPD 437
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1034678150 432 -AFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAG 471
Cdd:PLN03112  438 fKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPPDG 478
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
62-490 4.39e-34

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: 132.79  E-value: 4.39e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  62 RRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGfgprSQGVFLaRYGPAWREQRR-----FSV 136
Cdd:cd11044    18 YQKYGPVFKTHLLGRPTVFVIGAEAVRFILSGEGKLVRYGWPRSVRRLLG----ENSLSL-QDGEEHRRRRKllapaFSR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 137 STLRNL-----GLGKKSLEQWVTEEAACLCAAFANHSgrpFRpnglldkavsnVIASLTCGRRFEYDDPRFLRLLDLAQE 211
Cdd:cd11044    93 EALESYvptiqAIVQSYLRKWLKAGEVALYPELRRLT---FD-----------VAARLLLGLDPEVEAEALSQDFETWTD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 212 GLkeesgflrevlNAVPVllHIPA-LAGKVLRFQKAFLTQLDELLTEHRmtwdpAQPPRDLTEAF--LAEMEKAKGNPES 288
Cdd:cd11044   159 GL-----------FSLPV--PLPFtPFGRAIRARNKLLARLEQAIRERQ-----EEENAEAKDALglLLEAKDEDGEPLS 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 289 sfnDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQvRRPEMGDQAHMPYTTAVIHEVQRFGD 368
Cdd:cd11044   221 ---MDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLE-EPLTLESLKKMPYLDQVIKEVLRLVP 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 369 IVPLGVTHMTsRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDA-QGHFVKPEAFLPFSAGRRACLGEP 447
Cdd:cd11044   297 PVGGGFRKVL-EDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPArSEDKKKPFSLIPFGGGPRECLGKE 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1034678150 448 LARMELFLFFTSLLQHFSFSVAAGQPRPSHsrvvsflVTPSPY 490
Cdd:cd11044   376 FAQLEMKILASELLRNYDWELLPNQDLEPV-------VVPTPR 411
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
63-472 4.70e-34

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: 132.98  E-value: 4.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  63 RRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQIlgFGPRSQGVFLARYGPAWREQRR-FSVSTLRN 141
Cdd:cd11074     1 KKFGDIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDI--FTGKGQDMVFTVYGEHWRKMRRiMTVPFFTN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 142 lglgkKSLEQ----WVTEEAACLCAAFANHSGRPfrpNGL-----LDKAVSNVIASLTCGRRFEY-DDPRFLRLLDLAQE 211
Cdd:cd11074    79 -----KVVQQyrygWEEEAARVVEDVKKNPEAAT---EGIvirrrLQLMMYNNMYRIMFDRRFESeDDPLFVKLKALNGE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 212 GLKEESGFLREVLNAVPVLLhiPALAG-----------KVLRFQKAFLTQLDELLTEHRMTWDPAQPPRD-LTEAflaem 279
Cdd:cd11074   151 RSRLAQSFEYNYGDFIPILR--PFLRGylkickevkerRLQLFKDYFVDERKKLGSTKSTKNEGLKCAIDhILDA----- 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 280 eKAKGnpesSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIG---QVRRPemgDQAHMPYT 356
Cdd:cd11074   224 -QKKG----EINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGpgvQITEP---DLHKLPYL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 357 TAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFvkpEA---- 432
Cdd:cd11074   296 QAVVKETLRLRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKV---EAngnd 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1034678150 433 --FLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQ 472
Cdd:cd11074   373 frYLPFGVGRRSCPGIILALPILGITIGRLVQNFELLPPPGQ 414
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
302-481 4.98e-34

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: 132.68  E-value: 4.98e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 302 LFsAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLgVTHMTSRD 381
Cdd:cd20659   236 LF-AGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPF-IARTLTKP 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 382 IEVQGFRIPKGTTLITNLSSVLKDEAVWE-----KPFRFHPEHFLDaqghfVKPEAFLPFSAGRRACLGEPLARMELFLF 456
Cdd:cd20659   314 ITIDGVTLPAGTLIAINIYALHHNPTVWEdpeefDPERFLPENIKK-----RDPFAFIPFSAGPRNCIGQNFAMNEMKVV 388
                         170       180
                  ....*....|....*....|....*
gi 1034678150 457 FTSLLQHFSFSVAAGQPRPSHSRVV 481
Cdd:cd20659   389 LARILRRFELSVDPNHPVEPKPGLV 413
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
70-473 1.50e-33

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: 131.68  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  70 SLQLAWTPVVVLNGLAAVREALvtHGEDTADRPPVPITQILGFGpRSQGvfLARYGPAWREQRRFSVSTL---RNLglgk 146
Cdd:cd11076     7 AFSLGETRVVITSHPETAREIL--NSPAFADRPVKESAYELMFN-RAIG--FAPYGEYWRNLRRIASNHLfspRRI---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 147 KSLEQWVTEEAACLCAAFAN--HSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPrflrllDLAQEGLKE--ESGFlrE 222
Cdd:cd11076    78 AASEPQRQAIAAQMVKAIAKemERSGEVAVRKHLQRASLNNIMGSVFGRRYDFEAG------NEEAEELGEmvREGY--E 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 223 VLNA------VPVLLHIP---------ALAGKVLRFqkafltqLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKakgnpE 287
Cdd:cd11076   150 LLGAfnwsdhLPWLRWLDlqgirrrcsALVPRVNTF-------VGKIIEEHRAKRSNRARDDEDDVDVLLSLQG-----E 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 288 SSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFG 367
Cdd:cd11076   218 EKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLH 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 368 DIVP-LGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGhfvkPEAF---------LPFS 437
Cdd:cd11076   298 PPGPlLSWARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEG----GADVsvlgsdlrlAPFG 373
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1034678150 438 AGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:cd11076   374 AGRRVCPGKALGLATVHLWVAQLLHEFEWLPDDAKP 409
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
305-484 2.79e-33

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: 130.78  E-value: 2.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMgDQAH-MPYTTAVIHEVQRfgdIVPLG--VTHMTSRD 381
Cdd:cd11055   237 AGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTY-DTVSkLKYLDMVINETLR---LYPPAffISRECKED 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 382 IEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLL 461
Cdd:cd11055   313 CTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKIL 392
                         170       180
                  ....*....|....*....|...
gi 1034678150 462 QHFSFSVAAGQPRPSHSRVVSFL 484
Cdd:cd11055   393 QKFRFVPCKETEIPLKLVGGATL 415
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
65-464 2.97e-33

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: 130.90  E-value: 2.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  65 FGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPP-------VPITQILGFG--PrsqgvflarYGPAWREQRRfS 135
Cdd:cd11066     1 NGPVFQIRLGNKRIVVVNSFASVRDLWIKNSSALNSRPTfytfhkvVSSTQGFTIGtsP---------WDESCKRRRK-A 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 136 VSTlrnlGLGKKSLEQWVT----EEAACLCAAFA-NHSGR-PFRPNGLLDKAVSNVIASLTCGRRFE--YDDPrflrlld 207
Cdd:cd11066    71 AAS----ALNRPAVQSYAPiidlESKSFIRELLRdSAEGKgDIDPLIYFQRFSLNLSLTLNYGIRLDcvDDDS------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 208 LAQEGLKEESGFLR------EVLNAVPVLLHIPALAGKVLRFQKaFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEK 281
Cdd:cd11066   140 LLLEIIEVESAISKfrstssNLQDYIPILRYFPKMSKFRERADE-YRNRRDKYLKKLLAKLKEEIEDGTDKPCIVGNILK 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 282 akgNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHP--DVQRRVQQEIDDV--IGQVRRPEMGDQAHMPYTT 357
Cdd:cd11066   219 ---DKESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAygNDEDAWEDCAAEEKCPYVV 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 358 AVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFS 437
Cdd:cd11066   296 ALVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHFSFG 375
                         410       420
                  ....*....|....*....|....*..
gi 1034678150 438 AGRRACLGEPLARMELFLFFTSLLQHF 464
Cdd:cd11066   376 AGSRMCAGSHLANRELYTAICRLILLF 402
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
62-471 5.45e-33

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: 129.61  E-value: 5.45e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  62 RRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQIlgFGPRSQgvfLARYGPAWREQRRFSVSTLRN 141
Cdd:cd11043     2 IKRYGPVFKTSLFGRPTVVSADPEANRFILQNEGKLFVSWYPKSVRKL--LGKSSL---LTVSGEEHKRLRGLLLSFLGP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 142 LGLGKKSLEQwvTEEAACLcaAFANHSGRPfrpNGLLDKAVSNVIASLTCGRRFEYDDPRflrlldlAQEGLKEESGFLR 221
Cdd:cd11043    77 EALKDRLLGD--IDELVRQ--HLDSWWRGK---SVVVLELAKKMTFELICKLLLGIDPEE-------VVEELRKEFQAFL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 222 EVLNAVPvlLHIPALA-GKVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKakgnPESSFNDENLRIVVA 300
Cdd:cd11043   143 EGLLSFP--LNLPGTTfHRALKARKRIRKELKKIIEERRAELEKASPKGDLLDVLLEEKDE----DGDSLTDEEILDNIL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 301 DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGqvRRPEMG-----DQAHMPYTTAVIHEVQRFGDIVPlGVT 375
Cdd:cd11043   217 TLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAK--RKEEGEgltweDYKSMKYTWQVINETLRLAPIVP-GVF 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 376 HMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHfvKPEAFLPFSAGRRACLGEPLARMELFL 455
Cdd:cd11043   294 RKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKG--VPYTFLPFGGGPRLCPGAELAKLEILV 371
                         410
                  ....*....|....*.
gi 1034678150 456 FFTSLLQHFSFSVAAG 471
Cdd:cd11043   372 FLHHLVTRFRWEVVPD 387
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
61-464 5.51e-33

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 131.39  E-value: 5.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  61 LRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQIlgFGPRSQGVFLARYGPAWREQRRFSVSTLR 140
Cdd:PLN02394   59 MAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDI--FTGKGQDMVFTVYGDHWRKMRRIMTVPFF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 141 NLGLGKKSLEQWVTEEAACLCAAFANHSGRPfrpNGL-----LDKAVSNVIASLTCGRRFE-YDDPRFLRLLDLAQEGLK 214
Cdd:PLN02394  137 TNKVVQQYRYGWEEEADLVVEDVRANPEAAT---EGVvirrrLQLMMYNIMYRMMFDRRFEsEDDPLFLKLKALNGERSR 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 215 EESGFLREVLNAVPVLLhiPALAGKVLRFQKAFLTQL----DELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPEssF 290
Cdd:PLN02394  214 LAQSFEYNYGDFIPILR--PFLRGYLKICQDVKERRLalfkDYFVDERKKLMSAKGMDKEGLKCAIDHILEAQKKGE--I 289
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 291 NDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIG---QVRRPemgDQAHMPYTTAVIHEVQRFG 367
Cdd:PLN02394  290 NEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGpgnQVTEP---DTHKLPYLQAVVKETLRLH 366
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 368 DIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFvkpEA------FLPFSAGRR 441
Cdd:PLN02394  367 MAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAKV---EAngndfrFLPFGVGRR 443
                         410       420
                  ....*....|....*....|...
gi 1034678150 442 ACLGEPLARMELFLFFTSLLQHF 464
Cdd:PLN02394  444 SCPGIILALPILGIVLGRLVQNF 466
PLN02183 PLN02183
ferulate 5-hydroxylase
60-497 5.72e-32

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 128.43  E-value: 5.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  60 QLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGpRSQGVFlARYGPAWREQRRFSVSTL 139
Cdd:PLN02183   63 NLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLQVQDSVFSNRPANIAISYLTYD-RADMAF-AHYGPFWRQMRKLCVMKL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 140 rnlgLGKKSLEQW--VTEEAACLCAAFANHSGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRLLdlaQEGLKEES 217
Cdd:PLN02183  141 ----FSRKRAESWasVRDEVDSMVRSVSSNIGKPVNIGELIFTLTRNITYRAAFGSSSNEGQDEFIKIL---QEFSKLFG 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 218 GFlrEVLNAVPVLLHIPA--LAGKVLRFQKAFLTQLDELLTEHrMTWDPAQPPRDLTEAFLAEM---------EKAKGNP 286
Cdd:PLN02183  214 AF--NVADFIPWLGWIDPqgLNKRLVKARKSLDGFIDDIIDDH-IQKRKNQNADNDSEEAETDMvddllafysEEAKVNE 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 287 ES------SFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVI 360
Cdd:PLN02183  291 SDdlqnsiKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTL 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 361 HEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQ------GHFvkpeAFL 434
Cdd:PLN02183  371 KETLRLHPPIPL-LLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGvpdfkgSHF----EFI 445
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034678150 435 PFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQpRPSHSRV--VSFLVTPSPYELCAVPR 497
Cdd:PLN02183  446 PFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWELPDGM-KPSELDMndVFGLTAPRATRLVAVPT 509
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
66-493 7.20e-32

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: 126.67  E-value: 7.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  66 GDVFSLQLAWTPVVVLNGLAAVREALvthgedtADRPPV--------PITQILGFgprsQGVFLARyGPAWREQRR---- 133
Cdd:cd11083     1 GSAYRFRLGRQPVLVISDPELIREVL-------RRRPDEfrrissleSVFREMGI----NGVFSAE-GDAWRRQRRlvmp 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 134 -FSVSTLRNLglgKKSLEQwVTEEaacLCAAFANHS--GRPFRPNGLLDKAVSNVIASLTcgrrFEYDdprfLRLLDLAQ 210
Cdd:cd11083    69 aFSPKHLRYF---FPTLRQ-ITER---LRERWERAAaeGEAVDVHKDLMRYTVDVTTSLA----FGYD----LNTLERGG 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 211 EGLKEE-----SGFLREVLNAVPVLLHIPALAGK----VLRFQKAFLTQLDELlTEHRMTWDPAQPPRDLTeafLAEMEK 281
Cdd:cd11083   134 DPLQEHlervfPMLNRRVNAPFPYWRYLRLPADRaldrALVEVRALVLDIIAA-ARARLAANPALAEAPET---LLAMML 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 282 AKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQA-HMPYTTAVI 360
Cdd:cd11083   210 AEDDPDARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPLLEALdRLPYLEAVA 289
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 361 HEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLD----AQGHFvkPEAFLPF 436
Cdd:cd11083   290 RETLRLKPVAPL-LFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDgaraAEPHD--PSSLLPF 366
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034678150 437 SAGRRACLGEPLARMELFLFFTSLLQhfSFSVAAGQPRPSHSRVVSFLVTPSPYELC 493
Cdd:cd11083   367 GAGPRLCPGRSLALMEMKLVFAMLCR--NFDIELPEPAPAVGEEFAFTMSPEGLRVR 421
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
287-474 1.70e-31

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: 125.84  E-value: 1.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 287 ESSFNDENLRIVVaDLFS-AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIG-QVRRPEMGDQAHMPYTTAVIHEVQ 364
Cdd:cd20660   225 GTKLSDEDIREEV-DTFMfEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGdSDRPATMDDLKEMKYLECVIKEAL 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 365 RFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFL--DAQGHfvKPEAFLPFSAGRRA 442
Cdd:cd20660   304 RLFPSVPM-FGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLpeNSAGR--HPYAYIPFSAGPRN 380
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034678150 443 CLGEPLARMELFLFFTSLLQHfsFSVAAGQPR 474
Cdd:cd20660   381 CIGQKFALMEEKVVLSSILRN--FRIESVQKR 410
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
305-467 2.26e-30

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: 122.71  E-value: 2.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQ-AHMPYTTAVIHEVQRFGDIVPLgVTHMTSRDIE 383
Cdd:cd11057   238 AGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGQFITYEDlQQLVYLEMVLKETMRLFPVGPL-VGRETTADIQ 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 384 V-QGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLD---AQGHfvkPEAFLPFSAGRRACLGEPLARMELFLFFT 458
Cdd:cd11057   317 LsNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPersAQRH---PYAFIPFSAGPRNCIGWRYAMISMKIMLA 393

                  ....*....
gi 1034678150 459 SLLQHFSFS 467
Cdd:cd11057   394 KILRNYRLK 402
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
60-471 1.09e-29

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 121.72  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  60 QLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGvfLARYGPAWREQRRFSVSTL 139
Cdd:PLN03234   56 RLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELG--FGQYTAYYREMRKMCMVNL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 140 rnLGLGKKSLEQWVTEEAaclCAAFANHSGRPFRPNGLLDkaVSNVIASLT----C----GRRFEYDDPRFLRLLDLaqe 211
Cdd:PLN03234  134 --FSPNRVASFRPVREEE---CQRMMDKIYKAADQSGTVD--LSELLLSFTncvvCrqafGKRYNEYGTEMKRFIDI--- 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 212 gLKEESGFLREVL--NAVPVLLHIPALAGKVLRFQKAFL---TQLDELLTEhrmTWDPAQPPRDlTEAFL-AEMEKAKGN 285
Cdd:PLN03234  204 -LYETQALLGTLFfsDLFPYFGFLDNLTGLSARLKKAFKeldTYLQELLDE---TLDPNRPKQE-TESFIdLLMQIYKDQ 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 286 PES-SFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQ 364
Cdd:PLN03234  279 PFSiKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVIKESL 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 365 RFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLDA-QGHFVKPEAF--LPFSAGR 440
Cdd:PLN03234  359 RLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPERFMKEhKGVDFKGQDFelLPFGSGR 438
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1034678150 441 RACLGEPLARMELFLFFTSLLQHFSFSVAAG 471
Cdd:PLN03234  439 RMCPAMHLGIAMVEIPFANLLYKFDWSLPKG 469
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
291-487 1.74e-29

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: 120.14  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 291 NDENLRIVVADL-------FSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQvRRPEMGDQAHMPYTTAVIHEV 363
Cdd:cd11052   222 DDQNKNMTVQEIvdecktfFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGK-DKPPSDSLSKLKTVSMVINES 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 364 QRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLD----AQGHfvkPEAFLPFSA 438
Cdd:cd11052   301 LRLYPPAVF-LTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADgvakAAKH---PMAFLPFGL 376
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034678150 439 GRRACLGEPLARMELFLFFTSLLQHFSFSVAagqPRPSHSRVVSFLVTP 487
Cdd:cd11052   377 GPRNCIGQNFATMEAKIVLAMILQRFSFTLS---PTYRHAPTVVLTLRP 422
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
305-476 4.17e-28

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: 116.31  E-value: 4.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEV 384
Cdd:cd11046   251 AGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLP 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 385 QG-FRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQG----HFVKPEAFLPFSAGRRACLGEPLARMELFLFFTS 459
Cdd:cd11046   331 GGgVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFInppnEVIDDFAFLPFGGGPRKCLGDQFALLEATVALAM 410
                         170
                  ....*....|....*..
gi 1034678150 460 LLQHFSFSVAAGQPRPS 476
Cdd:cd11046   411 LLRRFDFELDVGPRHVG 427
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
280-487 5.47e-28

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: 115.71  E-value: 5.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 280 EKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVI----GQVRRPEMGDqahMPY 355
Cdd:cd11056   215 KIEDDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLekhgGELTYEALQE---MKY 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 356 TTAVIHEVQRFGDIVPLgVTHMTSRDIEV--QGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAF 433
Cdd:cd11056   292 LDQVVNETLRKYPPLPF-LDRVCTKDYTLpgTDVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRHPYTY 370
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034678150 434 LPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRPSHSRVVSFLVTP 487
Cdd:cd11056   371 LPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSKTKIPLKLSPKSFVLSP 424
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
219-466 6.06e-28

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: 115.43  E-value: 6.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 219 FLREVLNAVP--VLLHIPALAGKVLRFQKAFLTQLDELLTEHR---MTWDPAQPPRDLTEAFLAEMEKAkgnpessfnDE 293
Cdd:cd11062   153 WLLKLLRSLPesLLKRLNPGLAVFLDFQESIAKQVDEVLRQVSagdPPSIVTSLFHALLNSDLPPSEKT---------LE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 294 NLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVR-RPEMGDQAHMPYTTAVIHEVQRFGdivpL 372
Cdd:cd11062   224 RLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDPDsPPSLAELEKLPYLTAVIKEGLRLS----Y 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 373 GVTHMTSR-----DIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHfVKPEAFL-PFSAGRRACLGE 446
Cdd:cd11062   300 GVPTRLPRvvpdeGLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEK-GKLDRYLvPFSKGSRSCLGI 378
                         250       260
                  ....*....|....*....|
gi 1034678150 447 PLARMELFLFFTSLLQHFSF 466
Cdd:cd11062   379 NLAYAELYLALAALFRRFDL 398
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
242-481 7.38e-28

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: 115.05  E-value: 7.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 242 RFQKAfLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPessFNDENLRIVVADLFSAGMVTTSTTLAWGLLLM 321
Cdd:cd11049   172 RFDRA-LARLRELVDEIIAEYRASGTDRDDLLSLLLAARDEEGRP---LSDEELRDQVITLLTAGTETTASTLAWAFHLL 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 322 ILHPDVQRRVQQEIDDVIGQvRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSS 401
Cdd:cd11049   248 ARHPEVERRLHAELDAVLGG-RPATFEDLPRLTYTRRVVTEALRLYPPVWL-LTRRTTADVELGGHRLPAGTEVAFSPYA 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 402 VLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAG-QPRPSHSRV 480
Cdd:cd11049   326 LHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPVPGrPVRPRPLAT 405

                  .
gi 1034678150 481 V 481
Cdd:cd11049   406 L 406
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
251-468 8.46e-28

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: 115.50  E-value: 8.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 251 LDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKGNPESSFNDE---NLRIvvadLFSAGMVTTSTTLAWGLLLMILHPDV 327
Cdd:cd11070   181 LSELLDEVEAELSADSKGKQGTESVVASRLKRARRSGGLTEKEllgNLFI----FFIAGHETTANTLSFALYLLAKHPEV 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 328 QRRVQQEIDDVIGqvRRPEMGDQA----HMPYTTAVIHEVQRFGDIVPLgVTHMTSRDIEV-----QGFRIPKGTTLITN 398
Cdd:cd11070   257 QDWLREEIDSVLG--DEPDDWDYEedfpKLPYLLAVIYETLRLYPPVQL-LNRKTTEPVVVitglgQEIVIPKGTYVGYN 333
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034678150 399 LSSVLKDEAVWEKPFR-FHPEHFLD-------AQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSV 468
Cdd:cd11070   334 AYATHRDPTIWGPDADeFDPERWGStsgeigaATRFTPARGAFIPFSAGPRACLGRKFALVEFVAALAELFRQYEWRV 411
PLN02966 PLN02966
cytochrome P450 83A1
63-496 1.12e-27

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 116.00  E-value: 1.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  63 RRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGvfLARYGPAWREQRRFSVSTLrnL 142
Cdd:PLN02966   60 KKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRPPHRGHEFISYGRRDMA--LNHYTPYYREIRKMGMNHL--F 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 143 GLGKKSLEQWVTEEAACLCAAFANHSGRPFRP---NGLLDKAVSNVIASLTCGRRFEYDD---PRFLRLLDLAQEGLKEE 216
Cdd:PLN02966  136 SPTRVATFKHVREEEARRMMDKINKAADKSEVvdiSELMLTFTNSVVCRQAFGKKYNEDGeemKRFIKILYGTQSVLGKI 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 217 sgFLREVLnavPVLLHIPALAGKVLRFQKAFLTQ---LDELLTEhrmTWDPAQPPRDLTEAFLAEMEKAKGNP-ESSFND 292
Cdd:PLN02966  216 --FFSDFF---PYCGFLDDLSGLTAYMKECFERQdtyIQEVVNE---TLDPKRVKPETESMIDLLMEIYKEQPfASEFTV 287
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 293 ENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQ--VRRPEMGDQAHMPYTTAVIHEVQRFGDIV 370
Cdd:PLN02966  288 DNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEkgSTFVTEDDVKNLPYFRALVKETLRIEPVI 367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 371 PLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLDAQGHFVKPE-AFLPFSAGRRACLGEPL 448
Cdd:PLN02966  368 PLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKGTDyEFIPFGSGRRMCPGMRL 447
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1034678150 449 ARMELFLFFTSLLQHFSFSVAAG-QPRPSHSRVVSFLVTPSPYELCAVP 496
Cdd:PLN02966  448 GAAMLEVPYANLLLNFNFKLPNGmKPDDINMDVMTGLAMHKSQHLKLVP 496
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
297-489 3.42e-26

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: 110.38  E-value: 3.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 297 IVVADLFsAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAH-MPYTTAVIHEVQRfgdIVPLGVT 375
Cdd:cd11042   216 LLIALLF-AGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDPLTYDVLKeMPLLHACIKETLR---LHPPIHS 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 376 HM--TSRDIEV--QGFRIPKGTTLitnLSSVL---KDEAVWEKPFRFHPEHFLDAQGHFVK--PEAFLPFSAGRRACLGE 446
Cdd:cd11042   292 LMrkARKPFEVegGGYVIPKGHIV---LASPAvshRDPEIFKNPDEFDPERFLKGRAEDSKggKFAYLPFGAGRHRCIGE 368
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034678150 447 PLARMELFLFFTSLLQHFSFS-VAAGQPRPSHSRVVSflVTPSP 489
Cdd:cd11042   369 NFAYLQIKTILSTLLRNFDFElVDSPFPEPDYTTMVV--WPKGP 410
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
304-492 3.48e-26

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: 110.82  E-value: 3.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 304 SAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPE--MGDQAHMPYTTAVIHEVQRFGDIVPLgVTHMTSRD 381
Cdd:cd11069   245 AAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDGDlsYDDLDRLPYLNAVCRETLRLYPPVPL-TSREATKD 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 382 IEVQGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLD-----AQGHFVKPEAFLPFSAGRRACLGEPLARMELFL 455
Cdd:cd11069   324 TVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEpdgaaSPGGAGSNYALLTFLHGPRSCIGKKFALAEMKV 403
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034678150 456 FFTSLLQHFSFSVAAGQPRPSHSRVvsfLVTPSPYEL 492
Cdd:cd11069   404 LLAALVSRFEFELDPDAEVERPIGI---ITRPPVDGL 437
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
125-478 6.21e-26

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: 109.99  E-value: 6.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 125 GPAWREQRR-----FSVSTLRNLglgkksLEQWVTEEAACLC---AAFANHSGRPFRPNGLLDKAVSNVIASL-----TC 191
Cdd:cd11064    56 GELWKFQRKtasheFSSRALREF------MESVVREKVEKLLvplLDHAAESGKVVDLQDVLQRFTFDVICKIafgvdPG 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 192 GRRFEYDDPRFLRLLDLAQEGLkeesgFLRevlnavpvlLHIPALAGKVLRF---------QKAfLTQLDELLTEH---- 258
Cdd:cd11064   130 SLSPSLPEVPFAKAFDDASEAV-----AKR---------FIVPPWLWKLKRWlnigsekklREA-IRVIDDFVYEVisrr 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 259 ----RMTWDPAQPPRDLTEAFLAEMEKakgnPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQE 334
Cdd:cd11064   195 reelNSREEENNVREDLLSRFLASEEE----EGEPVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREE 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 335 IDDVI-----GQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVW 409
Cdd:cd11064   271 LKSKLpklttDESRVPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIW 350
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034678150 410 -EKPFRFHPEHFLDAQGHFVKPEA--FLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP-RPSHS 478
Cdd:cd11064   351 gEDALEFKPERWLDEDGGLRPESPykFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKvEPKMS 423
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
299-480 6.27e-26

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: 109.75  E-value: 6.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 299 VADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMT 378
Cdd:cd20646   238 LTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIV 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 379 SRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFT 458
Cdd:cd20646   318 EKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALS 397
                         170       180
                  ....*....|....*....|..
gi 1034678150 459 SLLQHFSFsvaagQPRPSHSRV 480
Cdd:cd20646   398 RLIKRFEV-----RPDPSGGEV 414
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
263-474 6.56e-26

cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 (CYP4V2) is the most characterized member of the CYP4V subfamily. It is a selective omega-hydroxylase of saturated, medium-chain fatty acids, such as laurate, myristate and palmitate, with high catalytic efficiency toward myristate. Polymorphisms in the CYP4V2 gene cause Bietti's crystalline corneoretinal dystrophy (BCD), a recessive degenerative retinopathy that is characterized clinically by a progressive decline in central vision, night blindness, and constriction of the visual field. The CYP4V subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410773 [Multi-domain]  Cd Length: 440  Bit Score: 109.85  E-value: 6.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 263 DPAQPPRDLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQV 342
Cdd:cd20680   212 DGESPSKKKRKAFLDMLLSVTDEEGNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKS 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 343 RRP-EMGDQAHMPYTTAVIHEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFL 421
Cdd:cd20680   292 DRPvTMEDLKKLRYLECVIKESLRLFPSVPL-FARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFF 370
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034678150 422 DAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHfsFSVAAGQPR 474
Cdd:cd20680   371 PENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRH--FWVEANQKR 421
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
270-493 2.01e-25

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: 108.11  E-value: 2.01e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 270 DLTEAFLAEMEKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGD 349
Cdd:cd20621   205 KDIIIDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFED 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 350 QAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVK 429
Cdd:cd20621   285 LQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDN 364
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034678150 430 PEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFsvaAGQPRPSHSRVVSFLVTPSPYELC 493
Cdd:cd20621   365 PFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEI---EIIPNPKLKLIFKLLYEPVNDLLL 425
PLN00168 PLN00168
Cytochrome P450; Provisional
6-471 3.81e-25

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 108.50  E-value: 3.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150   6 LVPLAVIVAIFLLLVDLMHRRQRWAARYSPGPLPLPGLGNLLHVDFQNTPYCFDQLRRRF----GDVFSLQLAWTPVVVL 81
Cdd:PLN00168    7 LLLAALLLLPLLLLLLGKHGGRGGKKGRRLPPGPPAVPLLGSLVWLTNSSADVEPLLRRLiaryGPVVSLRVGSRLSVFV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  82 NGLAAVREALVTHGEDTADRPPVPITQILGfgPRSQGVFLARYGPAWREQRRFSVSTLRNLGLGK--KSLEQWVTEEAAC 159
Cdd:PLN00168   87 ADRRLAHAALVERGAALADRPAVASSRLLG--ESDNTITRSSYGPVWRLLRRNLVAETLHPSRVRlfAPARAWVRRVLVD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 160 LCAAFANHSGRPfRPNGLLDKAVSNVIASLTCGRRFeydDPRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHI------ 233
Cdd:PLN00168  165 KLRREAEDAAAP-RVVETFQYAMFCLLVLMCFGERL---DEPAVRAIAAAQRDWLLYVSKKMSVFAFFPAVTKHlfrgrl 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 234 -PALAGKvlRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAF-------LAEMeKAKGNPESSFNDENLRIVVADLFSA 305
Cdd:PLN00168  241 qKALALR--RRQKELFVPLIDARREYKNHLGQGGEPPKKETTFehsyvdtLLDI-RLPEDGDRALTDDEIVNLCSEFLNA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 306 GMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAH-MPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEV 384
Cdd:PLN00168  318 GTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQEEVSEEDVHkMPYLKAVVLEGLRKHPPAHFVLPHKAAEDMEV 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 385 QGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFL---DAQGHFV---KPEAFLPFSAGRRACLGEPLARMELFLFFT 458
Cdd:PLN00168  398 GGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLaggDGEGVDVtgsREIRMMPFGVGRRICAGLGIAMLHLEYFVA 477
                         490
                  ....*....|...
gi 1034678150 459 SLLQHFSFSVAAG 471
Cdd:PLN00168  478 NMVREFEWKEVPG 490
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
218-467 4.50e-25

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: 107.27  E-value: 4.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 218 GFLREV---LNAVPVLLHIPALAGKVLRFQKAFLTQL-DELLTEHRMtwDPAQPPRDLTEAFLAEMEKAKGNPESsfnDE 293
Cdd:cd11068   155 RALTEAgrrANRPPILNKLRRRAKRQFREDIALMRDLvDEIIAERRA--NPDGSPDDLLNLMLNGKDPETGEKLS---DE 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 294 NLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGqVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPlG 373
Cdd:cd11068   230 NIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLG-DDPPPYEQVAKLRYIRRVLDETLRLWPTAP-A 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 374 VTHMTSRDIEVQG-FRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLDaqGHFVK--PEAFLPFSAGRRACLGEPLA 449
Cdd:cd11068   308 FARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLP--EEFRKlpPNAWKPFGNGQRACIGRQFA 385
                         250
                  ....*....|....*...
gi 1034678150 450 RMELFLFFTSLLQHFSFS 467
Cdd:cd11068   386 LQEATLVLAMLLQRFDFE 403
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
67-497 8.33e-25

cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first committed step in the biosynthesis of the core structure of glucosinolates, the conversion of amino acids to the corresponding aldoximes. Glucosinolates are amino acid-derived natural plant products that function in the defense against herbivores and microorganisms. Arabidopsis thaliana contains seven family members: CYP79B2 and CYP79B3, which metabolize trytophan; CYP79F1 and CYP79F2, which metabolize chain-elongated methionine derivatives with respectively 1-6 or 5-6 additional methylene groups in the side chain; CYP79A2 that metabolizes phenylalanine; and CYP79C1 and CYP79C2, with unknown function. CYP79 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 106.68  E-value: 8.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  67 DVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGFGPRSQGVflARYGPAWREQRR------FSVSTLR 140
Cdd:cd20658     2 DIACIRLGNTHVIPVTCPKIAREILRKQDAVFASRPLTYATEIISGGYKTTVI--SPYGEQWKKMRKvlttelMSPKRHQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 141 NLgLGKKsleqwvTEEAACLCAAFANHSgrpfrPNGLLDKAVS----------NVIASLTCGRRFeyddprFLRLLDLAQ 210
Cdd:cd20658    80 WL-HGKR------TEEADNLVAYVYNMC-----KKSNGGGLVNvrdaarhycgNVIRKLMFGTRY------FGKGMEDGG 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 211 EGLKE----ESGFlrEVLNAVP---VLLHIPALAGKVLRFQKAFLTQL--------DELLTEHRMTWDPA--QPPRDLTE 273
Cdd:cd20658   142 PGLEEvehmDAIF--TALKCLYafsISDYLPFLRGLDLDGHEKIVREAmriirkyhDPIIDERIKQWREGkkKEEEDWLD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 274 AFLAeMEKAKGNPesSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHM 353
Cdd:cd20658   220 VFIT-LKDENGNP--LLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNL 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 354 PYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEA- 432
Cdd:cd20658   297 NYVKACAREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEVTLTEPd 376
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034678150 433 --FLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYELCAVPR 497
Cdd:cd20658   377 lrFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTLPPNVSSVDLSESKDDLFMAKPLVLVAKPR 443
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
185-469 1.19e-24

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: 106.13  E-value: 1.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 185 VIASLTCGRRFEY-----DDPRFLRLLDLAQEGLK--EESGFLREVL--NAVPVLLHIPALAGKVLRFQKAFLTQLDELL 255
Cdd:cd11060   114 VIGEITFGKPFGFleagtDVDGYIASIDKLLPYFAvvGQIPWLDRLLlkNPLGPKRKDKTGFGPLMRFALEAVAERLAED 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 256 TEHrmtwdpAQPPRDLTEAFLaEMEKAKGNPessFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEI 335
Cdd:cd11060   194 AES------AKGRKDMLDSFL-EAGLKDPEK---VTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEI 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 336 DDVIGQVRRPE---MGDQAHMPYTTAVIHEVQR--------FGDIVPLGvthmtsrDIEVQGFRIPKGTTLITNLSSVLK 404
Cdd:cd11060   264 DAAVAEGKLSSpitFAEAQKLPYLQAVIKEALRlhppvglpLERVVPPG-------GATICGRFIPGGTIVGVNPWVIHR 336
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034678150 405 DEAVW-EKPFRFHPEHFLDAQGHFVKPE--AFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVA 469
Cdd:cd11060   337 DKEVFgEDADVFRPERWLEADEEQRRMMdrADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELV 404
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
55-487 1.40e-24

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: 105.96  E-value: 1.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  55 PYcFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTAdrPPVPITQILG--FGprsQGVFLARyGPAWREQR 132
Cdd:cd20640     2 PY-FDKWRKQYGPIFTYSTGNKQFLYVSRPEMVKEINLCVSLDLG--KPSYLKKTLKplFG---GGILTSN-GPHWAHQR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 133 RFSVSTLRnlgLGK-KSLEQWVTEEAACLCAAFANH------SGRPFRPNGLLDKAVSNVIASLTCGRRFEYDDPRFLRL 205
Cdd:cd20640    75 KIIAPEFF---LDKvKGMVDLMVDSAQPLLSSWEERidraggMAADIVVDEDLRAFSADVISRACFGSSYSKGKEIFSKL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 206 LDLaQEGLKEESgflreVLNAVPVLLHIPALAG-KVLRFQKAFLTQLDELLTEHRMTWDPAqppRDLTEAFLaemEKAKG 284
Cdd:cd20640   152 REL-QKAVSKQS-----VLFSIPGLRHLPTKSNrKIWELEGEIRSLILEIVKEREEECDHE---KDLLQAIL---EGARS 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 285 NPESSFNDENLrIV--VADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVI-GQVRRPEMgdQAHMPYTTAVIH 361
Cdd:cd20640   220 SCDKKAEAEDF-IVdnCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCkGGPPDADS--LSRMKTVTMVIQ 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 362 EVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFR-FHPEHFLDAQGHFVK-PEAFLPFSAG 439
Cdd:cd20640   297 ETLRLYPPAAF-VSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWGPDANeFNPERFSNGVAAACKpPHSYMPFGAG 375
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1034678150 440 RRACLGEPLARMELFLFFTSLLQHFSFSVAagqPRPSHSRVVSFLVTP 487
Cdd:cd20640   376 ARTCLGQNFAMAELKVLVSLILSKFSFTLS---PEYQHSPAFRLIVEP 420
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
299-487 2.01e-24

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: 105.39  E-value: 2.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 299 VADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPlGVTHMT 378
Cdd:cd20647   242 MTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLP-GNGRVT 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 379 SRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLdAQGHFVKPEAF--LPFSAGRRACLGEPLARMELFLF 456
Cdd:cd20647   321 QDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWL-RKDALDRVDNFgsIPFGYGIRSCIGRRIAELEIHLA 399
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034678150 457 FTSLLQHFSFSVAAgQPRPSHSRVVSfLVTP 487
Cdd:cd20647   400 LIQLLQNFEIKVSP-QTTEVHAKTHG-LLCP 428
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
305-468 4.92e-24

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: 104.03  E-value: 4.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRfgdIVPLG--VTHMTSRDI 382
Cdd:cd20650   239 AGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLR---LFPIAgrLERVCKKDV 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 383 EVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQ 462
Cdd:cd20650   316 EINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQ 395

                  ....*.
gi 1034678150 463 HFSFSV 468
Cdd:cd20650   396 NFSFKP 401
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
299-480 2.80e-23

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


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 102.14  E-value: 2.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 299 VADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMT 378
Cdd:cd20648   239 VTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIP 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 379 SRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLD--AQGHfvkPEAFLPFSAGRRACLGEPLARMELFLF 456
Cdd:cd20648   319 DRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGkgDTHH---PYASLPFGFGKRSCIGRRIAELEVYLA 395
                         170       180
                  ....*....|....*....|....
gi 1034678150 457 FTSLLQHFSFsvaagQPRPSHSRV 480
Cdd:cd20648   396 LARILTHFEV-----RPEPGGSPV 414
PLN02655 PLN02655
ent-kaurene oxidase
287-472 8.20e-23

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 100.97  E-value: 8.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 287 ESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEmGDQAHMPYTTAVIHEVQRF 366
Cdd:PLN02655  255 ATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDERVTE-EDLPNLPYLNAVFHETLRK 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 367 GDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGE 446
Cdd:PLN02655  334 YSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCAGS 413
                         170       180
                  ....*....|....*....|....*.
gi 1034678150 447 PLARMELFLFFTSLLQHFSFSVAAGQ 472
Cdd:PLN02655  414 LQAMLIACMAIARLVQEFEWRLREGD 439
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
185-467 1.97e-22

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: 99.30  E-value: 1.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 185 VIASLTCGRRFeyddpRFLRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLRFQKAFLTQ--LDELLTE--HRM 260
Cdd:cd11059   114 VVSHLLFGESF-----GTLLLGDKDSRERELLRRLLASLAPWLRWLPRYLPLATSRLIIGIYFRAFdeIEEWALDlcARA 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 261 TWDPAQPPRDlTEAFLAEMEKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLA---WGLLLmilHPDVQRRVQQEIDD 337
Cdd:cd11059   189 ESSLAESSDS-ESLTVLLLEKLKGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTyliWELSR---PPNLQEKLREELAG 264
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 338 VIGQVR-RPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRD-IEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRF 415
Cdd:cd11059   265 LPGPFRgPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLPRVVPEGgATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEF 344
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034678150 416 HPEHFLDAQGHFVKP--EAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFS 467
Cdd:cd11059   345 DPERWLDPSGETAREmkRAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTS 398
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
77-466 3.33e-22

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: 99.30  E-value: 3.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  77 PVVVLnglAAVREA--LVTHGEDTADRPPVPITQILGFGPRSQGVFlaRYGPAWREQRRF-----SVSTLRN-------- 141
Cdd:cd20622    14 PWVIV---ADFREAqdILMRRTKEFDRSDFTIDVFGGIGPHHHLVK--STGPAFRKHRSLvqdlmTPSFLHNvaapaihs 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 142 --LGLgkksLEQWVTEeaaclcAAFANhsGRPFRPNGLLDKAVSNVIASLTCGRRFEYDD--PRFLRLLDLAQE----GL 213
Cdd:cd20622    89 kfLDL----IDLWEAK------ARLAK--GRPFSAKEDIHHAALDAIWAFAFGINFDASQtrPQLELLEAEDSTilpaGL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 214 KEESGF----LREVLNAVPVLLH---------IPALAGKVLR----FQKAFLTQLDELLTEHRMTWDPAQPPRDLT---- 272
Cdd:cd20622   157 DEPVEFpeapLPDELEAVLDLADsveksikspFPKLSHWFYRnqpsYRRAAKIKDDFLQREIQAIARSLERKGDEGevrs 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 273 --------EAFLAEMEKAKGNPESSfndenlrIVVADLFS---AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQ 341
Cdd:cd20622   237 avdhmvrrELAAAEKEGRKPDYYSQ-------VIHDELFGyliAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHPE 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 342 V----RRP---EMGdQAHMPYTTAVIHEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTT--LITNLSSVLK-----DEA 407
Cdd:cd20622   310 AvaegRLPtaqEIA-QARIPYLDAVIEEILRCANTAPI-LSREATVDTQVLGYSIPKGTNvfLLNNGPSYLSppieiDES 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 408 --------------VWE-KPFR-FHPEHFLDAQGHFVK----PEAF--LPFSAGRRACLGEPLARMELFLFFTSLLQHFS 465
Cdd:cd20622   388 rrssssaakgkkagVWDsKDIAdFDPERWLVTDEETGEtvfdPSAGptLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFE 467

                  .
gi 1034678150 466 F 466
Cdd:cd20622   468 L 468
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
282-477 2.71e-21

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: 96.19  E-value: 2.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 282 AKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIH 361
Cdd:cd20678   227 AKDENGKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIK 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 362 EVQRFGDIVPlGVTHMTSRDIE-VQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFldAQGHFVK--PEAFLPFSA 438
Cdd:cd20678   307 EALRLYPPVP-GISRELSKPVTfPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRF--SPENSSKrhSHAFLPFSA 383
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034678150 439 GRRACLGEPLARMELFLFFTSLLQHFSFSvaagqPRPSH 477
Cdd:cd20678   384 GPRNCIGQQFAMNEMKVAVALTLLRFELL-----PDPTR 417
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
272-475 4.19e-21

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: 95.08  E-value: 4.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 272 TEAFLAEMEKAKGNPESSFNDE---NLRIVVadLFSAGMVTTSTTLAWGLLLMIlHPDVQRRVQQEIDDVIGQvrRPEMG 348
Cdd:cd11045   189 GDDLFSALCRAEDEDGDRFSDDdivNHMIFL--MMAAHDTTTSTLTSMAYFLAR-HPEWQERLREESLALGKG--TLDYE 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 349 DQAHMPYTTAVIHEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQG-HF 427
Cdd:cd11045   264 DLGQLEVTDWVFKEALRLVPPVPT-LPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAeDK 342
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034678150 428 VKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVA-AGQPRP 475
Cdd:cd11045   343 VHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWSVpGYYPPW 391
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
303-488 6.25e-21

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: 94.82  E-value: 6.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 303 FSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLgVTHMTSRDI 382
Cdd:cd20641   244 FFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVIN-IARRASEDM 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 383 EVQGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLDAQGHFVK-PEAFLPFSAGRRACLGEPLARMELFLFFTSL 460
Cdd:cd20641   323 KLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAAThPNALLSFSLGPRACIGQNFAMIEAKTVLAMI 402
                         170       180
                  ....*....|....*....|....*...
gi 1034678150 461 LQHFSFSVAagqPRPSHSRVVSFLVTPS 488
Cdd:cd20641   403 LQRFSFSLS---PEYVHAPADHLTLQPQ 427
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
303-487 7.01e-21

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: 94.82  E-value: 7.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 303 FSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRfgdIVPLGVT--HMTSR 380
Cdd:cd20639   241 FFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLR---LYPPAVAtiRRAKK 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 381 DIEVQGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLDAQGHFVK-PEAFLPFSAGRRACLGEPLARMELFLFFT 458
Cdd:cd20639   318 DVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARAAKhPLAFIPFGLGPRTCVGQNLAILEAKLTLA 397
                         170       180
                  ....*....|....*....|....*....
gi 1034678150 459 SLLQHFSFSVAagqPRPSHSRVVSFLVTP 487
Cdd:cd20639   398 VILQRFEFRLS---PSYAHAPTVLMLLQP 423
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
295-464 8.54e-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: 94.49  E-value: 8.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 295 LRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLgV 374
Cdd:cd20645   227 LYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPF-T 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 375 THMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDaQGHFVKPEAFLPFSAGRRACLGEPLARMELF 454
Cdd:cd20645   306 SRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQ-EKHSINPFAHVPFGIGKRMCIGRRLAELQLQ 384
                         170
                  ....*....|
gi 1034678150 455 LFFTSLLQHF 464
Cdd:cd20645   385 LALCWIIQKY 394
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
239-464 2.37e-20

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: 93.03  E-value: 2.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 239 KVLRFQKAFLTQLDELLTEhRMTWDPAQPprDLTEAFLAEMEKAKGnpessFNDENLRIVVADLFSAGMVTTSTTLAwGL 318
Cdd:cd11058   170 SLRKKRKEHFQYTREKVDR-RLAKGTDRP--DFMSYILRNKDEKKG-----LTREELEANASLLIIAGSETTATALS-GL 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 319 LLMIL-HPDVQRRVQQEI-------DDVIGQVrrpemgdQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRD-IEVQGFRI 389
Cdd:cd11058   241 TYYLLkNPEVLRKLVDEIrsafsseDDITLDS-------LAQLPYLNAVIQEALRLYPPVPAGLPRVVPAGgATIDGQFV 313
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034678150 390 PKGTTLITNLSSVLKDEAVWEKPFRFHPEHFL-DAQGHFV--KPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHF 464
Cdd:cd11058   314 PGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLgDPRFEFDndKKEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNF 391
PLN02290 PLN02290
cytokinin trans-hydroxylase
269-469 3.25e-20

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 93.34  E-value: 3.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 269 RDLTEAFLAEMEKAKGNPessfNDENLRIVVAD---LFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQvRRP 345
Cdd:PLN02290  292 DDLLGMLLNEMEKKRSNG----FNLNLQLIMDEcktFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGG-ETP 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 346 EMGDQAHMPYTTAVIHEVQRF---GDIVPlgvtHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEK-PFRFHPEHFl 421
Cdd:PLN02290  367 SVDHLSKLTLLNMVINESLRLyppATLLP----RMAFEDIKLGDLHIPKGLSIWIPVLAIHHSEELWGKdANEFNPDRF- 441
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034678150 422 dAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVA 469
Cdd:PLN02290  442 -AGRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTIS 488
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
305-466 5.55e-20

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: 92.21  E-value: 5.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRfgdIVP--LGVTHMTSRDI 382
Cdd:cd20649   272 AGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLR---MYPpaFRFAREAAEDC 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 383 EVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQ 462
Cdd:cd20649   349 VVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILR 428

                  ....
gi 1034678150 463 HFSF 466
Cdd:cd20649   429 RFRF 432
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
302-469 9.06e-20

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: 91.16  E-value: 9.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 302 LFsAGMVTTSTTLAWglLLMIL--HPDVQRRVQQEIDDVIGQ---------VRRPEMGDQahMPYTTAVIHEVQRfgdIV 370
Cdd:cd11051   194 LF-AGHDTTSSTLCW--AFYLLskHPEVLAKVRAEHDEVFGPdpsaaaellREGPELLNQ--LPYTTAVIKETLR---LF 265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 371 PLGvthMTSRD-IEVQGFRIPKGTTLITNLSSVL-------KDEAVWEKPFRFHPEHFLDAQGH--FVKPEAFLPFSAGR 440
Cdd:cd11051   266 PPA---GTARRgPPGVGLTDRDGKEYPTDGCIVYvchhaihRDPEYWPRPDEFIPERWLVDEGHelYPPKSAWRPFERGP 342
                         170       180
                  ....*....|....*....|....*....
gi 1034678150 441 RACLGEPLARMELFLFFTSLLQHFSFSVA 469
Cdd:cd11051   343 RNCIGQELAMLELKIILAMTVRRFDFEKA 371
PLN02936 PLN02936
epsilon-ring hydroxylase
276-472 1.37e-19

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 91.39  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 276 LAEMEKAKGNPESSFNDEN---LRIVVA------------DLFS---AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDD 337
Cdd:PLN02936  242 IVEAEGEVIEGEEYVNDSDpsvLRFLLAsreevssvqlrdDLLSmlvAGHETTGSVLTWTLYLLSKNPEALRKAQEELDR 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 338 VIGQvRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHP 417
Cdd:PLN02936  322 VLQG-RPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVP 400
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 418 EHFlDAQGHfVKPEA-----FLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQ 472
Cdd:PLN02936  401 ERF-DLDGP-VPNETntdfrYIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVPDQ 458
PLN02971 PLN02971
tryptophan N-hydroxylase
232-474 1.39e-19

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 91.64  E-value: 1.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 232 HIPALAG-------KVLRFQKAFLTQL-DELLTEHRMTWDPAQppRDLTEAFL---AEMEKAKGNPesSFNDENLRIVVA 300
Cdd:PLN02971  258 YLPMLTGldlngheKIMRESSAIMDKYhDPIIDERIKMWREGK--RTQIEDFLdifISIKDEAGQP--LLTADEIKPTIK 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 301 DLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSR 380
Cdd:PLN02971  334 ELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALS 413
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 381 DIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPE---AFLPFSAGRRACLGEPLARMELFLFF 457
Cdd:PLN02971  414 DTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTEndlRFISFSTGKRGCAAPALGTAITTMML 493
                         250
                  ....*....|....*..
gi 1034678150 458 TSLLQHFSFSVAAGQPR 474
Cdd:PLN02971  494 ARLLQGFKWKLAGSETR 510
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
265-469 3.79e-19

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 90.04  E-value: 3.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 265 AQPPRDLTEAFLAEmekakgnpESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRR 344
Cdd:PLN02987  246 AEKKKDMLAALLAS--------DDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKSD 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 345 P---EMGDQAHMPYTTAVIHEVQRFGDIVPlGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFL 421
Cdd:PLN02987  318 SyslEWSDYKSMPFTQCVVNETLRVANIIG-GIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQ 396
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034678150 422 DAQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVA 469
Cdd:PLN02987  397 SNSGTTVPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSWVPA 444
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
293-472 1.72e-18

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: 87.41  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 293 ENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQvRRPEMGDQAHMPYTTAVIHEVQRFGDIVPL 372
Cdd:cd20616   223 ENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGE-RDIQNDDLQKLKVLENFINESMRYQPVVDF 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 373 GVTHMTSRDIeVQGFRIPKGTTLITNLSSVLKDEaVWEKPFRFHPEHFLDAqghfVKPEAFLPFSAGRRACLGEPLARME 452
Cdd:cd20616   302 VMRKALEDDV-IDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFEKN----VPSRYFQPFGFGPRSCVGKYIAMVM 375
                         170       180
                  ....*....|....*....|
gi 1034678150 453 LFLFFTSLLQHFSFSVAAGQ 472
Cdd:cd20616   376 MKAILVTLLRRFQVCTLQGR 395
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
252-465 4.44e-18

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: 86.07  E-value: 4.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 252 DELLTEHRMTWDPAQPPRDLteaFLAEMEKAKGNPESsfndenLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRV 331
Cdd:cd11063   183 DKALARKEESKDEESSDRYV---FLDELAKETRDPKE------LRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 332 QQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGvTHMTSRD--IEVQG--------FrIPKGTTLITNLSS 401
Cdd:cd11063   254 REEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLN-SRVAVRDttLPRGGgpdgkspiF-VPKGTRVLYSVYA 331
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034678150 402 VLKDEAVW-EKPFRFHPEHFLDAQGhfvKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFS 465
Cdd:cd11063   332 MHRRKDIWgPDAEEFRPERWEDLKR---PGWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFD 393
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
208-482 6.37e-18

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: 85.17  E-value: 6.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 208 LAQEGLKEESGFLREVLNAVPV-----LLHIPA-LAGKVLRFQKAFLTQLDELLT-EHRMTWDPAQPPR-DLTEAFLAEM 279
Cdd:cd20630    97 LDELGEPEEFDVIREIAEHIPFrvisaMLGVPAeWDEQFRRFGTATIRLLPPGLDpEELETAAPDVTEGlALIEEVIAER 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 280 EKAKGNPE------------SSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEiddvigqvrrPEM 347
Cdd:cd20630   177 RQAPVEDDllttllraeedgERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE----------PEL 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 348 GDQAhmpyttavIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHfldaqghf 427
Cdd:cd20630   247 LRNA--------LEEVLRWDNFGKMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR-------- 310
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034678150 428 vKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP----RPSHSRVVS 482
Cdd:cd20630   311 -DPNANIAFGYGPHFCIGAALARLELELAVSTLLRRFPEMELAEPPvfdpHPVLRAIVS 368
PLN02302 PLN02302
ent-kaurenoic acid oxidase
231-495 1.08e-17

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 85.54  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 231 LHIPALA-GKVLRFQKAFLTQLDELLTEHRMTWDPAQPPR--DLTEAFLaEMEKAKGNPessFNDENLRIVVADLFSAGM 307
Cdd:PLN02302  225 INLPGFAyHRALKARKKLVALFQSIVDERRNSRKQNISPRkkDMLDLLL-DAEDENGRK---LDDEEIIDLLLMYLNAGH 300
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 308 VTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMG----DQAHMPYTTAVIHEVQRFGDIVPLgVTHMTSRDIE 383
Cdd:PLN02302  301 ESSGHLTMWATIFLQEHPEVLQKAKAEQEEIAKKRPPGQKGltlkDVRKMEYLSQVIDETLRLINISLT-VFREAKTDVE 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 384 VQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFldaQGHFVKPEAFLPFSAGRRACLGEPLARMELFLFftslLQH 463
Cdd:PLN02302  380 VNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRW---DNYTPKAGTFLPFGLGSRLCPGNDLAKLEISIF----LHH 452
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034678150 464 F--SFSVAAGQPRPShsrvVSFLVTPSPYELCAV 495
Cdd:PLN02302  453 FllGYRLERLNPGCK----VMYLPHPRPKDNCLA 482
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
305-489 1.32e-17

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: 85.02  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQvRRPEMGDQAHMPYTTAVIHEVQRFGDIVpLGVTHMTSRDIEV 384
Cdd:cd20642   245 AGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGN-NKPDFEGLNHLKVVTMILYEVLRLYPPV-IQLTRAIHKDTKL 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 385 QGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLD-----AQGHFvkpeAFLPFSAGRRACLGEPLARMELFLFFT 458
Cdd:cd20642   323 GDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFAEgiskaTKGQV----SYFPFGWGPRICIGQNFALLEAKMALA 398
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034678150 459 SLLQHFSFSVAagqprPSHSRVVSFLVTPSP 489
Cdd:cd20642   399 LILQRFSFELS-----PSYVHAPYTVLTLQP 424
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
293-464 1.45e-17

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: 84.77  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 293 ENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEiddvIGQVRRPEMGDQAHM----PYTTAVIHEVQRfgd 368
Cdd:cd20643   233 EDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAE----VLAARQEAQGDMVKMlksvPLLKAAIKETLR--- 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 369 IVPLGVT--HMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPeafLPFSAGRRACLGE 446
Cdd:cd20643   306 LHPVAVSlqRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRN---LGFGFGPRQCLGR 382
                         170
                  ....*....|....*...
gi 1034678150 447 PLARMELFLFFTSLLQHF 464
Cdd:cd20643   383 RIAETEMQLFLIHMLENF 400
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
260-464 2.40e-17

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: 83.50  E-value: 2.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 260 MTWDPAQP-----PRDLTEAFLAEMEKAKGNPESSF--------------NDENLRIVVADLFSAGMVTTSTTLAWGLLL 320
Cdd:cd20629   139 DPPDPDVPaaeaaAAELYDYVLPLIAERRRAPGDDLisrllraevegeklDDEEIISFLRLLLPAGSDTTYRALANLLTL 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 321 MILHPDVQRRVQQeiddvigqvrrpemgDQAHMPyttAVIHEVQRFgDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLS 400
Cdd:cd20629   219 LLQHPEQLERVRR---------------DRSLIP---AAIEEGLRW-EPPVASVPRMALRDVELDGVTIPAGSLLDLSVG 279
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034678150 401 SVLKDEAVWEKPFRFhpEHFLDAQGHFVkpeaflpFSAGRRACLGEPLARMELFLFFTSLLQHF 464
Cdd:cd20629   280 SANRDEDVYPDPDVF--DIDRKPKPHLV-------FGGGAHRCLGEHLARVELREALNALLDRL 334
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
276-453 2.49e-17

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: 83.97  E-value: 2.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 276 LAEMEKAKGnpessFNDENLRiVVADLFS-AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIgQVRRP---EMGDQA 351
Cdd:cd20679   231 LSKDEDGKE-----LSDEDIR-AEADTFMfEGHDTTASGLSWILYNLARHPEYQERCRQEVQELL-KDREPeeiEWDDLA 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 352 HMPYTTAVIHEVQRFGDIVPLgVTHMTSRDIEVQGFR-IPKGTTLITNLSSVLKDEAVWEK-----PFRFHPEhflDAQG 425
Cdd:cd20679   304 QLPFLTMCIKESLRLHPPVTA-ISRCCTQDIVLPDGRvIPKGIICLISIYGTHHNPTVWPDpevydPFRFDPE---NSQG 379
                         170       180
                  ....*....|....*....|....*...
gi 1034678150 426 HfvKPEAFLPFSAGRRACLGEPLARMEL 453
Cdd:cd20679   380 R--SPLAFIPFSAGPRNCIGQTFAMAEM 405
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
287-475 2.52e-17

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: 83.95  E-value: 2.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 287 ESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPE-----MGDQAHMPYTTAVIH 361
Cdd:cd11040   216 EAGLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNaildlTDLLTSCPLLDSTYL 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 362 EVQRFgDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFR-FHPEHFLDAQGH---FVKPEAFLPFS 437
Cdd:cd11040   296 ETLRL-HSSSTSVRLVTEDTVLGGGYLLRKGSLVMIPPRLLHMDPEIWGPDPEeFDPERFLKKDGDkkgRGLPGAFRPFG 374
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034678150 438 AGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRP 475
Cdd:cd11040   375 GGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWK 412
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
272-466 3.02e-17

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: 83.84  E-value: 3.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 272 TEAFLAEMEKAKGNPE---SSFNDENLRIVVAD-LFSAGMVTTSTtLAWGLLLMILHPDVQRRVQQEIDdvigQVRRPEM 347
Cdd:cd11082   195 THEILEEIKEAEEEGEpppPHSSDEEIAGTLLDfLFASQDASTSS-LVWALQLLADHPDVLAKVREEQA----RLRPNDE 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 348 ----GDQ-AHMPYTTAVIHEVQRFGDIVPLgVTHMTSRDIEV-QGFRIPKGTTLITNLSSVLKDEavWEKPFRFHPEHFL 421
Cdd:cd11082   270 ppltLDLlEEMKYTRQVVKEVLRYRPPAPM-VPHIAKKDFPLtEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFS 346
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034678150 422 DAQGHFVK-PEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSF 466
Cdd:cd11082   347 PERQEDRKyKKNFLVFGAGPHQCVGQEYAINHLMLFLALFSTLVDW 392
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
180-489 1.81e-16

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: 81.57  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 180 KAVSNVIASLTCGRRFEYDDprflRLLDLAQEGLkEESGFLREVLNAVPVLLHiPaLAGKVL---RFQKAFLTQLDELLT 256
Cdd:cd11041   116 RIVARVSARVFVGPPLCRNE----EWLDLTINYT-IDVFAAAAALRLFPPFLR-P-LVAPFLpepRRLRRLLRRARPLII 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 257 EHRM------TWDPAQPPRDLTEAFlaeMEKAKGNPESSFNDENLRIVVadLFSAGMVTTSTTLAWGLLLMILHPDVQRR 330
Cdd:cd11041   189 PEIErrrklkKGPKEDKPNDLLQWL---IEAAKGEGERTPYDLADRQLA--LSFAAIHTTSMTLTHVLLDLAAHPEYIEP 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 331 VQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQ-GFRIPKGTTLITNLSSVLKDEAVW 409
Cdd:cd11041   264 LREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVTLSdGLTLPKGTRIAVPAHAIHRDPDIY 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 410 E-----KPFRFHPEHFLDAQGH---FVKP-EAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRPsHSRV 480
Cdd:cd11041   344 PdpetfDGFRFYRLREQPGQEKkhqFVSTsPDFLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGERP-KNIW 422

                  ....*....
gi 1034678150 481 VSFLVTPSP 489
Cdd:cd11041   423 FGEFIMPDP 431
PLN02738 PLN02738
carotene beta-ring hydroxylase
282-473 8.01e-16

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 80.34  E-value: 8.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 282 AKGNPESSfndENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQvRRPEMGDQAHMPYTTAVIH 361
Cdd:PLN02738  382 ASGDDVSS---KQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGD-RFPTIEDMKKLKYTTRVIN 457
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 362 EVQRFGDIVPLGVTHMTSRDIeVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF-LDAQGHFVKPEAF--LPFSA 438
Cdd:PLN02738  458 ESLRLYPQPPVLIRRSLENDM-LGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpLDGPNPNETNQNFsyLPFGG 536
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034678150 439 GRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:PLN02738  537 GPRKCVGDMFASFENVVATAMLVRRFDFQLAPGAP 571
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
52-468 1.43e-15

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 78.82  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  52 QNTPYCFDQLRRRFGDVFSLQLAWTPVVVLNGLAAVREALVTHGEDTADRPPVPITQILGfgprSQGVFLAR--YGPAWR 129
Cdd:PLN02196   55 QDPNVFFASKQKRYGSVFKTHVLGCPCVMISSPEAAKFVLVTKSHLFKPTFPASKERMLG----KQAIFFHQgdYHAKLR 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 130 EQ--RRFSVSTLRNL-----GLGKKSLEQWvteeaaclcaafanhSGRPFRPNGLLDKAVSNViASLTCGRRFEYddprf 202
Cdd:PLN02196  131 KLvlRAFMPDAIRNMvpdieSIAQESLNSW---------------EGTQINTYQEMKTYTFNV-ALLSIFGKDEV----- 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 203 lrlldLAQEGLKEESGFLREVLNAVPVllHIPA-LAGKVLRFQKAFLTQLDELLTEHRmtwdpaQPPRDLTEAFLAEMEK 281
Cdd:PLN02196  190 -----LYREDLKRCYYILEKGYNSMPI--NLPGtLFHKSMKARKELAQILAKILSKRR------QNGSSHNDLLGSFMGD 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 282 AKGnpessFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEM---GDQAHMPYTTA 358
Cdd:PLN02196  257 KEG-----LTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGESltwEDTKKMPLTSR 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 359 VIHEVQRFGDIVPLGVTHMTsRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQghfvKPEAFLPFSA 438
Cdd:PLN02196  332 VIQETLRVASILSFTFREAV-EDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAP----KPNTFMPFGN 406
                         410       420       430
                  ....*....|....*....|....*....|
gi 1034678150 439 GRRACLGEPLARMELFLFFTSLLQHFSFSV 468
Cdd:PLN02196  407 GTHSCPGNELAKLEISVLIHHLTTKYRWSI 436
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
254-488 5.88e-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: 76.80  E-value: 5.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 254 LLTEHRMTWD-----------------PAQPPRDLTEAFLAEMEKAKGNPESsfndenLRIVVADLFSAGMVTTSTTLAW 316
Cdd:cd20644   181 LWKEHFEAWDcifqyadnciqkiyqelAFGRPQHYTGIVAELLLQAELSLEA------IKANITELTAGGVDTTAFPLLF 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 317 GLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRfgdIVPLGVT--HMTSRDIEVQGFRIPKGTT 394
Cdd:cd20644   255 TLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLR---LYPVGITvqRVPSSDLVLQNYHIPAGTL 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 395 LITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEAfLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAgqpR 474
Cdd:cd20644   332 VQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKH-LAFGFGMRQCLGRRLAEAEMLLLLMHVLKNFLVETLS---Q 407
                         250
                  ....*....|....
gi 1034678150 475 PSHSRVVSFLVTPS 488
Cdd:cd20644   408 EDIKTVYSFILRPE 421
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
349-466 1.06e-14

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 75.93  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 349 DQAHMPYTTAVIHEVQRFGDIVpLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQghfV 428
Cdd:PLN03141  310 DYMSLPFTQNVITETLRMGNII-NGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEKD---M 385
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034678150 429 KPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSF 466
Cdd:PLN03141  386 NNSSFTPFGGGQRLCPGLDLARLEASIFLHHLVTRFRW 423
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
251-481 1.45e-14

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: 74.90  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 251 LDELLTEHRmtwdpAQPPRDLTEAFLAEMEkakgnPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRR 330
Cdd:cd20625   168 FRDLIARRR-----ADPGDDLISALVAAEE-----DGDRLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQLAL 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 331 VQQeiddvigqvrRPEMgdqahmpyTTAVIHEVQRFgDivplGVTHMTSR----DIEVQGFRIPKGTTLITNLSSVLKDE 406
Cdd:cd20625   238 LRA----------DPEL--------IPAAVEELLRY-D----SPVQLTARvaleDVEIGGQTIPAGDRVLLLLGAANRDP 294
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034678150 407 AVWEKPFRFHPEHflDAQGHfvkpeafLPFSAGRRACLGEPLARMELFLFFTSLLQHF-SFSVAAGQPRPSHSRVV 481
Cdd:cd20625   295 AVFPDPDRFDITR--APNRH-------LAFGAGIHFCLGAPLARLEAEIALRALLRRFpDLRLLAGEPEWRPSLVL 361
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
252-478 1.54e-14

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


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 75.26  E-value: 1.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 252 DELLTEHRmtwdpAQPPRDLTEAfLAEMEkAKGNPessFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRV 331
Cdd:cd11033   177 RELAEERR-----ANPGDDLISV-LANAE-VDGEP---LTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERL 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 332 QqeiddvigqvrrpemGDQAHMPytTAViHEVQRFgdIVPlgVTHM---TSRDIEVQGFRIPKGTTLITNLSSVLKDEAV 408
Cdd:cd11033   247 R---------------ADPSLLP--TAV-EEILRW--ASP--VIHFrrtATRDTELGGQRIRAGDKVVLWYASANRDEEV 304
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 409 WEKPFRFHPEHfldaqghfvKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRPSHS 478
Cdd:cd11033   305 FDDPDRFDITR---------SPNPHLAFGGGPHFCLGAHLARLELRVLFEELLDRVPDIELAGEPERLRS 365
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
285-473 1.66e-14

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 75.59  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 285 NPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEI---DDVIGQVRRPEmGDQA---------- 351
Cdd:PLN03195  283 DPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELkalEKERAKEEDPE-DSQSfnqrvtqfag 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 352 --------HMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLD 422
Cdd:PLN03195  362 lltydslgKLQYLHAVITETLRLYPAVPQDPKGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIK 441
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034678150 423 aQGHF--VKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:PLN03195  442 -DGVFqnASPFKFTAFQAGPRICLGKDSAYLQMKMALALLCRFFKFQLVPGHP 493
PLN03018 PLN03018
homomethionine N-hydroxylase
305-497 2.25e-14

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 75.43  E-value: 2.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 305 AGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTSRDIEV 384
Cdd:PLN03018  325 AAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTL 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 385 QGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQG-----HFVKPEA-FLPFSAGRRACLGEPLARMELFLFFT 458
Cdd:PLN03018  405 GGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDGitkevTLVETEMrFVSFSTGRRGCVGVKVGTIMMVMMLA 484
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034678150 459 SLLQHFSFSVAAGQPRPSHSRVVSFLVTPSPYELCAVPR 497
Cdd:PLN03018  485 RFLQGFNWKLHQDFGPLSLEEDDASLLMAKPLLLSVEPR 523
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
251-474 7.41e-14

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: 73.17  E-value: 7.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 251 LDELLTEHRmtwdpAQPPRDLTEAFLAEMEkakgnPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDvQRR 330
Cdd:cd11038   181 ADALIEARR-----AEPGDDLISTLVAAEQ-----DGDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPD-QWR 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 331 VQQEiddvigqvrRPEMGDQAhmpyttavIHEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDeavwe 410
Cdd:cd11038   250 ALRE---------DPELAPAA--------VEEVLRWCPTTTW-ATREAVEDVEYNGVTIPAGTVVHLCSHAANRD----- 306
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034678150 411 kPFRFHPEHF-LDAQGhfvkpEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPR 474
Cdd:cd11038   307 -PRVFDADRFdITAKR-----APHLGFGGGVHHCLGAFLARAELAEALTVLARRLPTPAIAGEPT 365
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
276-460 2.89e-13

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: 71.32  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 276 LAEMEKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQahMPY 355
Cdd:cd20614   190 VAALIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAAGDVPRTPAELRR--FPL 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 356 TTAVIHEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHfVKPEAFLP 435
Cdd:cd20614   268 AEALFRETLRLHPPVPF-VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDRA-PNPVELLQ 345
                         170       180
                  ....*....|....*....|....*
gi 1034678150 436 FSAGRRACLGEPLARMELFLFFTSL 460
Cdd:cd20614   346 FGGGPHFCLGYHVACVELVQFIVAL 370
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
279-473 2.35e-12

cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is the main all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA and 18-OH-RA. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. CYP26A1 has been shown to upregulate fascin and promote the malignant behavior of breast carcinoma cells. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 68.69  E-value: 2.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 279 MEKAKGNPESsFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQAHM----- 353
Cdd:cd20638   216 IEHSRRNGEP-LNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKGLLSTKPNENKELSMevleq 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 354 -PYTTAVIHEVQRFGDIVPLGVtHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHFVKPEA 432
Cdd:cd20638   295 lKYTGCVIKETLRLSPPVPGGF-RVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFS 373
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034678150 433 FLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP 473
Cdd:cd20638   374 FIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQLLNGPP 414
PLN02774 PLN02774
brassinosteroid-6-oxidase
276-456 2.53e-12

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 68.65  E-value: 2.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 276 LAEMEKAKGNPESSFNDENLRIVVADLFSaGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDvIGQVRRPE----MGDQA 351
Cdd:PLN02774  247 LGYLMRKEGNRYKLTDEEIIDQIITILYS-GYETVSTTSMMAVKYLHDHPKALQELRKEHLA-IRERKRPEdpidWNDYK 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 352 HMPYTTAVIHEVQRFGDIVPlGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLD----AQGHf 427
Cdd:PLN02774  325 SMRFTRAVIFETSRLATIVN-GVLRKTTQDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDksleSHNY- 402
                         170       180
                  ....*....|....*....|....*....
gi 1034678150 428 vkpeaFLPFSAGRRACLGEPLARMELFLF 456
Cdd:PLN02774  403 -----FFLFGGGTRLCPGKELGIVEISTF 426
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
292-475 2.95e-12

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: 67.99  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 292 DENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEiddvigqvrrPEMgdqahmpyTTAVIHEVQRFGDIVP 371
Cdd:cd11037   200 EDEAPLLMRDYLSAGLDTTISAIGNALWLLARHPDQWERLRAD----------PSL--------APNAFEEAVRLESPVQ 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 372 lGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHflDAQGHfvkpeafLPFSAGRRACLGEPLARM 451
Cdd:cd11037   262 -TFSRTTTRDTELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR--NPSGH-------VGFGHGVHACVGQHLARL 331
                         170       180
                  ....*....|....*....|....
gi 1034678150 452 ELFLFFTSLLQHFSFSVAAGQPRP 475
Cdd:cd11037   332 EGEALLTALARRVDRIELAGPPVR 355
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
253-464 3.17e-12

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: 67.98  E-value: 3.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 253 ELLTEHRmtwdpAQPPRDLTEAFLAEMEKakgnpESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVq 332
Cdd:cd11031   175 ELVAARR-----AEPGDDLLSALVAARDD-----DDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARL- 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 333 qeiddvigqVRRPEMgdqahMPytTAViHEVQRFgdiVPLGVTHMTSR----DIEVQGFRIPKGTTLITNLSSVLKDEAV 408
Cdd:cd11031   244 ---------RADPEL-----VP--AAV-EELLRY---IPLGAGGGFPRyateDVELGGVTIRAGEAVLVSLNAANRDPEV 303
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034678150 409 WEKPFRFHPEHfldaqghfvKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHF 464
Cdd:cd11031   304 FPDPDRLDLDR---------EPNPHLAFGHGPHHCLGAPLARLELQVALGALLRRL 350
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
246-464 7.22e-12

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: 66.78  E-value: 7.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 246 AFLTQLDELLTEHRmtwdpAQPPRDLTEAFLAEmEKAKGNpessFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHP 325
Cdd:cd11030   170 ELRAYLDELVARKR-----REPGDDLLSRLVAE-HGAPGE----LTDEELVGIAVLLLVAGHETTANMIALGTLALLEHP 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 326 DvQRRVQQEiddvigqvrRPEMGDQAhmpyttavIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKD 405
Cdd:cd11030   240 E-QLAALRA---------DPSLVPGA--------VEELLRYLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRD 301
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034678150 406 EAVWEKPFRFHPEHflDAQGHfvkpeafLPFSAGRRACLGEPLARMELFLFFTSLLQHF 464
Cdd:cd11030   302 PAVFPDPDRLDITR--PARRH-------LAFGHGVHQCLGQNLARLELEIALPTLFRRF 351
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
290-465 1.40e-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: 66.08  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 290 FNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGqvrrpemgdqahmpyttaVIHEVQRFGDI 369
Cdd:cd11032   194 LTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRADPSLIPG------------------AIEEVLRYRPP 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 370 VPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHfldaqghfvKPEAFLPFSAGRRACLGEPLA 449
Cdd:cd11032   256 VQR-TARVTTEDVELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR---------NPNPHLSFGHGIHFCLGAPLA 325
                         170
                  ....*....|....*.
gi 1034678150 450 RMELFLFFTSLLQHFS 465
Cdd:cd11032   326 RLEARIALEALLDRFP 341
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
223-481 3.53e-11

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: 64.93  E-value: 3.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 223 VLNAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEhrmtwdpaqPPRDLTEAFLaemEKAKGNPESSFNDENLRIVVADL 302
Cdd:cd11078   151 VTWGRPSEEEQVEAAAAVGELWAYFADLVAERRRE---------PRDDLISDLL---AAADGDGERLTDEELVAFLFLLL 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 303 FsAGMVTTSTTLAWGLLLMILHPDVQRRVQqeiDDvigqvrrPEMGDQAhmpyttavIHEVQRFgDIVPLGVTHMTSRDI 382
Cdd:cd11078   219 V-AGHETTTNLLGNAVKLLLEHPDQWRRLR---AD-------PSLIPNA--------VEETLRY-DSPVQGLRRTATRDV 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 383 EVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPeHFLDAQGHfvkpeafLPFSAGRRACLGEPLARMELFLFFTSLLQ 462
Cdd:cd11078   279 EIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDI-DRPNARKH-------LTFGHGIHFCLGAALARMEARIALEELLR 350
                         250       260
                  ....*....|....*....|
gi 1034678150 463 HF-SFSVAAGQPRPSHSRVV 481
Cdd:cd11078   351 RLpGMRVPGQEVVYSPSLSF 370
PLN02500 PLN02500
cytochrome P450 90B1
287-469 5.82e-11

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 64.50  E-value: 5.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 287 ESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPD-VQRRVQQEIDDVIGQVRRPEM----GDQAHMPYTTAVIH 361
Cdd:PLN02500  272 HSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKaVQELREEHLEIARAKKQSGESelnwEDYKKMEFTQCVIN 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 362 EVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHFLD-------AQGHFVKPEAFL 434
Cdd:PLN02500  352 ETLRLGNVVRF-LHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQnnnrggsSGSSSATTNNFM 430
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034678150 435 PFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVA 469
Cdd:PLN02500  431 PFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELA 465
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
314-480 9.62e-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: 9.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 314 LAWGLLLMILHPDVQRRVQQEIDDvigqvrrpemgdqahmpYTTAVIHEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKGT 393
Cdd:cd11067   240 VTFAALALHEHPEWRERLRSGDED-----------------YAEAFVQEVRRFYPFFPF-VGARARRDFEWQGYRFPKGQ 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 394 TLITNLSSVLKDEAVWEKPFRFHPEHFLDAQGHfvkPEAFLP-----FSAGRRaCLGEPL--ARMELFLFFtsLLQHFSF 466
Cdd:cd11067   302 RVLLDLYGTNHDPRLWEDPDRFRPERFLGWEGD---PFDFIPqgggdHATGHR-CPGEWItiALMKEALRL--LARRDYY 375
                         170
                  ....*....|....
gi 1034678150 467 SVAAGQPRPSHSRV 480
Cdd:cd11067   376 DVPPQDLSIDLNRM 389
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
251-481 9.84e-11

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: 63.32  E-value: 9.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 251 LDELLTEHRmtwdpAQPPRDLTEAFLAEMEKakgnpESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRR 330
Cdd:cd11029   178 LAELVARKR-----AEPGDDLLSALVAARDE-----GDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLAL 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 331 VQQEiddvigqvrrPEMGDQAhmpyttavIHEVQRFGDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWE 410
Cdd:cd11029   248 LRAD----------PELWPAA--------VEELLRYDGPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFP 309
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034678150 411 KPFRFHPEhfLDAQGHfvkpeafLPFSAGRRACLGEPLARMELFLFFTSLLQHF---SFSVAAGQPRPSHSRVV 481
Cdd:cd11029   310 DPDRLDIT--RDANGH-------LAFGHGIHYCLGAPLARLEAEIALGALLTRFpdlRLAVPPDELRWRPSFLL 374
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
310-468 2.43e-10

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: 62.30  E-value: 2.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 310 TSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQvRRPEMGDqaHMPYTTAVIH----EVQRFGDIVPLGVTHMTSRDIEVQ 385
Cdd:cd20615   231 TTGVLSWNLVFLAANPAVQEKLREEISAAREQ-SGYPMED--YILSTDTLLAycvlESLRLRPLLAFSVPESSPTDKIIG 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 386 GFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLDaqghfVKPEA----FLPFSAGRRACLGEPLARMELFLFFTSL 460
Cdd:cd20615   308 GYRIPANTPVVVDTYALNINNPFWgPDGEAYRPERFLG-----ISPTDlrynFWRFGFGPRKCLGQHVADVILKALLAHL 382

                  ....*...
gi 1034678150 461 LQHFSFSV 468
Cdd:cd20615   383 LEQYELKL 390
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
250-479 2.71e-10

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: 61.97  E-value: 2.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 250 QLDELLTEHRmtwdpAQPPRDLTEAFLaeMEKAKGNPessFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQR 329
Cdd:cd11034   156 HLRDLIAERR-----ANPRDDLISRLI--EGEIDGKP---LSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRR 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 330 RVqqeIDDvigqvrrPEMGDQAhmpyttavIHEVQRFGDIVpLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVW 409
Cdd:cd11034   226 RL---IAD-------PSLIPNA--------VEEFLRFYSPV-AGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKF 286
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034678150 410 EKPFRFHPEHFldaqghfvkPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHF-SFSVAAGQPRPSHSR 479
Cdd:cd11034   287 EDPDRIDIDRT---------PNRHLAFGSGVHRCLGSHLARVEARVALTEVLKRIpDFELDPGATCEFLDS 348
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
291-476 3.40e-10

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 62.33  E-value: 3.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 291 NDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDvigqvrRPEMGDQAHMPYTTAVIHEVQRFGDIV 370
Cdd:PLN02169  298 KDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINT------KFDNEDLEKLVYLHAALSESMRLYPPL 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 371 PLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLDAQGHFVKPEA--FLPFSAGRRACLGEP 447
Cdd:PLN02169  372 PFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGLRHEPSykFMAFNSGPRTCLGKH 451
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034678150 448 LARMELFLFFTSLLQHFSFSVAAG---QPRPS 476
Cdd:PLN02169  452 LALLQMKIVALEIIKNYDFKVIEGhkiEAIPS 483
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
316-476 5.15e-10

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


Pssm-ID: 410728  Cd Length: 410  Bit Score: 61.17  E-value: 5.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 316 WGLLLMILHPDVQRRVQQEIDDVIGQVRRP----EMGDQAHMPYTTAVIHEVQRfgdIVPLGV-THMTSRDIEVQGFRIP 390
Cdd:cd20635   232 WTLAFILSHPSVYKKVMEEISSVLGKAGKDkikiSEDDLKKMPYIKRCVLEAIR---LRSPGAiTRKVVKPIKIKNYTIP 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 391 KGTTLITNLSSVLKDEAVWEKPFRFHPEHFLDAQ-GHFVKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVA 469
Cdd:cd20635   309 AGDMLMLSPYWAHRNPKYFPDPELFKPERWKKADlEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFTLL 388

                  ....*..
gi 1034678150 470 AGQPRPS 476
Cdd:cd20635   389 DPVPKPS 395
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
62-469 1.15e-09

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: 60.23  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150  62 RRRFGDVFSLQLAWTPVVVLNGLAAVREALVthGEDTADRPPVP-ITQILgFGPRSqgvFLARYGPAWREQRRFSVSTLR 140
Cdd:cd20636    19 REKYGNVFKTHLLGRPVIRVTGAENIRKILL--GEHTLVSTQWPqSTRIL-LGSNT---LLNSVGELHRQRRKVLARVFS 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 141 NLGLGK--KSLEQWVTEEAACLCAAFANHSGRPfrpnglLDKAVSNVIASltcgrrfeyddpRFLRLLDLAQEGLKEESG 218
Cdd:cd20636    93 RAALESylPRIQDVVRSEVRGWCRGPGPVAVYT------AAKSLTFRIAV------------RILLGLRLEEQQFTYLAK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 219 -FLREVLNAVPVLLHIPaLAG--KVLRFQKAFLTQLDELLTEHRMTWDPAQPPRDLTEAFLAEMEKAKgnpesSFNDENL 295
Cdd:cd20636   155 tFEQLVENLFSLPLDVP-FSGlrKGIKARDILHEYMEKAIEEKLQRQQAAEYCDALDYMIHSARENGK-----ELTMQEL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 296 RIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDdvigqvrRPEMGDQ-AHMP------------YTTAVIHE 362
Cdd:cd20636   229 KESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELV-------SHGLIDQcQCCPgalsleklsrlrYLDCVVKE 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 363 VQRFgdIVPLGVTHMTS-RDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF-----LDAQGHFvkpeAFLPF 436
Cdd:cd20636   302 VLRL--LPPVSGGYRTAlQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFgvereESKSGRF----NYIPF 375
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1034678150 437 SAGRRACLGEPLARMELFLFFTSLLQHFSFSVA 469
Cdd:cd20636   376 GGGVRSCIGKELAQVILKTLAVELVTTARWELA 408
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
202-481 1.43e-09

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: 59.53  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 202 FLRLLDLAQEGLKEESGFLREVLNAVPvllhipalAGKVLRFQKAFLTQLDELLTEHRmtwdpAQPPRDLTEAFL-AEME 280
Cdd:cd11035   116 FLELMGLPLEDLDRFLEWEDAMLRPDD--------AEERAAAAQAVLDYLTPLIAERR-----ANPGDDLISAILnAEID 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 281 kakGNPESSfnDENLRIVVAdLFSAGMVTTSTTLAWGLLLMILHPDVQRRVqqeiddvigqVRRPEMgdqahmpyTTAVI 360
Cdd:cd11035   183 ---GRPLTD--DELLGLCFL-LFLAGLDTVASALGFIFRHLARHPEDRRRL----------REDPEL--------IPAAV 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 361 HEVQRFGDIVPLGvtHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHfldaqghfvKPEAFLPFSAGR 440
Cdd:cd11035   239 EELLRRYPLVNVA--RIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR---------KPNRHLAFGAGP 307
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1034678150 441 RACLGEPLARMELFLFftslLQHF-----SFSVAAGQPRPSHSRVV 481
Cdd:cd11035   308 HRCLGSHLARLELRIA----LEEWlkripDFRLAPGAQPTYHGGSV 349
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
273-497 1.71e-09

cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, polypeptide 1 (cytochrome P450 20A1 or CYP20A1) is expressed in human hippocampus and substantia nigra. In zebrafish, maternal transcript of CYP20A1 occurs in eggs, suggesting involvement in brain and early development. CYP20A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 59.45  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 273 EAFLAEME----------KAKGNPESSFNDE------NLRIVVAD--LFS-AGMVTTSTTLAWGLLLMILHPDVQRRVQQ 333
Cdd:cd20627   162 EDALMEMEsvlkkvikerKGKNFSQHVFIDSllqgnlSEQQVLEDsmIFSlAGCVITANLCTWAIYFLTTSEEVQKKLYK 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 334 EIDDVIGqvRRPEMGDQ-AHMPYTTAVIHEVQRFGDIVPLGVThmtSRDIE--VQGFRIPKGTTLITNLSSVLKDEAVWE 410
Cdd:cd20627   242 EVDQVLG--KGPITLEKiEQLRYCQQVLCETVRTAKLTPVSAR---LQELEgkVDQHIIPKETLVLYALGVVLQDNTTWP 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 411 KPFRFHPEHFLDAQghFVKPEAFLPFSaGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQprpshsrvvsflVTPSPY 490
Cdd:cd20627   317 LPYRFDPDRFDDES--VMKSFSLLGFS-GSQECPELRFAYMVATVLLSVLVRKLRLLPVDGQ------------VMETKY 381

                  ....*..
gi 1034678150 491 ELCAVPR 497
Cdd:cd20627   382 ELVTSPR 388
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
253-463 1.49e-08

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: 56.59  E-value: 1.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 253 ELLTEHRMtwDPAQPPRDLTEAFLAEMEKakGNPESsfnDENLRIVVADLFSAGMVTTSTTLawGLLLMIL--HPDVQRR 330
Cdd:cd11079   149 DLLADRRA--APRDADDDVTARLLRERVD--GRPLT---DEEIVSILRNWTVGELGTIAACV--GVLVHYLarHPELQAR 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 331 VQQEIDDVigqvrrpemgdqahmpytTAVIHEVQRFGDivPL-GVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVW 409
Cdd:cd11079   220 LRANPALL------------------PAAIDEILRLDD--PFvANRRITTRDVELGGRTIPAGSRVTLNWASANRDERVF 279
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034678150 410 EKPFRFHPEHfldaqghfvKPEAFLPFSAGRRACLGEPLARMELFLFFTSLLQH 463
Cdd:cd11079   280 GDPDEFDPDR---------HAADNLVYGRGIHVCPGAPLARLELRILLEELLAQ 324
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
288-471 1.92e-08

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 56.62  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 288 SSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDDVIGQVRRPEMGDQ-AHMPYTTAVIHEVQRF 366
Cdd:PLN02426  287 SINDDKYLRDIVVSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNQEAASFEEmKEMHYLHAALYESMRL 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 367 GDIVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVW-EKPFRFHPEHFLDaQGHFV--KPEAFLPFSAGRRAC 443
Cdd:PLN02426  367 FPPVQFDSKFAAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLK-NGVFVpeNPFKYPVFQAGLRVC 445
                         170       180
                  ....*....|....*....|....*...
gi 1034678150 444 LGEPLARMELFLFFTSLLQHFSFSVAAG 471
Cdd:PLN02426  446 LGKEMALMEMKSVAVAVVRRFDIEVVGR 473
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
236-473 2.45e-08

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


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 55.93  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 236 LAGKVLRFQKAFLTQLDELLTEHRmtwdpaqpPRDLTEAFLAEMEKAKGNPESSfndenlriVVADLF---SAGMVTTST 312
Cdd:cd20624   151 LRPRISRARERFRARLREYVERAE--------PGSLVGELSRLPEGDEVDPEGQ--------VPQWLFafdAAGMALLRA 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 313 tlawgLLLMILHPDVQRRVQQEIDDVIGQVRRPemgdqahmpYTTAVIHEVQRFGDIVPLgVTHMTSRDIEVQGFRIPKG 392
Cdd:cd20624   215 -----LALLAAHPEQAARAREEAAVPPGPLARP---------YLRACVLDAVRLWPTTPA-VLRESTEDTVWGGRTVPAG 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 393 TTLITNLSSVLKDEAVWEKPFRFHPEHFLD--AQGHfvkpEAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAA 470
Cdd:cd20624   280 TGFLIFAPFFHRDDEALPFADRFVPEIWLDgrAQPD----EGLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLE 355

                  ...
gi 1034678150 471 GQP 473
Cdd:cd20624   356 SPR 358
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
203-461 4.20e-08

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: 55.17  E-value: 4.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 203 LRLLDLAQEGLKEESGFLREVLNAVPVLLHIPALAGKVLRFQKAFLTQLDELLTEHRmtwdpAQPPRDLTeAFLAemekA 282
Cdd:cd11080   112 MDMLGLDKRDHEKIHEWHSSVAAFITSLSQDPEARAHGLRCAEQLSQYLLPVIEERR-----VNPGSDLI-SILC----T 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 283 KGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQeiddvigqvrrpemgDQAhmpYTTAVIHE 362
Cdd:cd11080   182 AEYEGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRA---------------DRS---LVPRAIAE 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 363 VQRFGDIVPLgVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEHF-LDAQGHFVKPEAFLPFSAGRR 441
Cdd:cd11080   244 TLRYHPPVQL-IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHREdLGIRSAFSGAADHLAFGSGRH 322
                         250       260
                  ....*....|....*....|
gi 1034678150 442 ACLGEPLARMELFLFFTSLL 461
Cdd:cd11080   323 FCVGAALAKREIEIVANQVL 342
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
269-469 1.78e-07

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: 53.31  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 269 RDLTEAFLAEMEKAKGNpESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQQEIDD---------VI 339
Cdd:cd20637   202 KDYADALDILIESAKEH-GKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELRSngilhngclCE 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 340 GQVRrpeMGDQAHMPYTTAVIHEVQRFGDIVPLGVTHMTsRDIEVQGFRIPKGTTLITNL------SSVLKDEAVWEkPF 413
Cdd:cd20637   281 GTLR---LDTISSLKYLDCVIKEVLRLFTPVSGGYRTAL-QTFELDGFQIPKGWSVLYSIrdthdtAPVFKDVDAFD-PD 355
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034678150 414 RFHPEHFLDAQGHFvkpeAFLPFSAGRRACLGEPLARMELFLFFTSLLQHFSFSVA 469
Cdd:cd20637   356 RFGQERSEDKDGRF----HYLPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFELA 407
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
325-460 2.77e-07

cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic conversions of fatty acid hydroperoxides to bioactive oxylipins in plants, some invertebrates, and bacteria. It includes two dehydrases, namely allene oxide synthase (AOS) and divinyl ether synthase (DES), and two isomerases, hydroperoxide lyase (HPL) and epoxyalcohol synthase (EAS). AOS (EC 4.2.1.92, also called hydroperoxide dehydratase), such as Arabidopsis thaliana CYP74A acts on a number of unsaturated fatty-acid hydroperoxides, forming the corresponding allene oxides. DES (EC 4.2.1.121), also called colneleate synthase or CYP74D, catalyzes the selective removal of pro-R hydrogen at C-8 in the biosynthesis of colneleic acid. The linolenate HPL, Arabidopsis thaliana CYP74B2, is required for the synthesis of the green leaf volatiles (GLVs) hexanal and trans-2-hexenal. The fatty acid HPL, Solanum lycopersicum CYP74B, is involved in the biosynthesis of traumatin and C6 aldehydes. The epoxyalcohol synthase Ranunculus japonicus CYP74A88 (also known as RjEAS) specifically converts linoleic acid 9- and 13-hydroperoxides to oxiranyl carbinols 9,10-epoxy-11-hydroxy-12-octadecenoic acid and 11-hydroxy-12,13-epoxy-9-octadecenoic acid, respectively. The CYP74 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 52.65  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 325 PDVQRRVQQEIDDVIGQVRRPEMGDQAHMPYTTAVIHEVQRFGDIVPLgVTHMTSRDIEVQ----GFRIPKGTTLITNLS 400
Cdd:cd11071   257 EELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPL-QYGRARKDFVIEshdaSYKIKKGELLVGYQP 335
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034678150 401 SVLKDEAVWEKPFRFHPEHFLDAQGHFVKpeaFLPFSAGR---------RAC----LGEPLAR---MELFLFFTSL 460
Cdd:cd11071   336 LATRDPKVFDNPDEFVPDRFMGEEGKLLK---HLIWSNGPeteeptpdnKQCpgkdLVVLLARlfvAELFLRYDTF 408
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
313-450 9.61e-04

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 41.33  E-value: 9.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 313 TLAWGLLLmilHPDVQRRVQqeiddvigqvRRPEMGDQAhmpyttavIHEVQRFgdIVPLGVT-HMTSRDIEVQGFRIPK 391
Cdd:cd11039   224 GTCWGLLS---NPEQLAEVM----------AGDVHWLRA--------FEEGLRW--ISPIGMSpRRVAEDFEIRGVTLPA 280
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034678150 392 GTTLITNLSSVLKDEAVWEKPFRFhpEHFLDAQGHfvkpeafLPFSAGRRACLGEPLAR 450
Cdd:cd11039   281 GDRVFLMFGSANRDEARFENPDRF--DVFRPKSPH-------VSFGAGPHFCAGAWASR 330
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
358-487 2.81e-03

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 40.11  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 358 AVIHEVQRFGDiVPLGVTHMTSRDIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHpehfldaqgHFVKPEAF--LP 435
Cdd:cd20619   236 AIINEMVRMDP-PQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFD---------HTRPPAASrnLS 305
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034678150 436 FSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQPRPSHS-RVVSFLVTP 487
Cdd:cd20619   306 FGLGPHSCAGQIISRAEATTVFAVLAERYERIELAEEPTVAHNdFARRYRKLP 358
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
204-483 3.98e-03

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: 39.40  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 204 RLLDLAQEGLKEESGFLRE-VLNAVPVLLHIPAlaGKVLRFQKAF---LTQLDELLTEHRMTWDPAQPpRDLTEAFLAEM 279
Cdd:cd11036    86 RALDAAPPGFDLVADFLRPlPVRVAAALLGLPA--DDRARFARLFaalAPALDSLLCARALLAARALL-RAALAELLALT 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 280 EKAKGNPESSFNDENLRIVVADLFSAGMVTTSTTLAWGLLLMILHPDVQRRVQqeiddvigqvRRPEMGDqahmpyttAV 359
Cdd:cd11036   163 RSAAADALALSAPGDLVANAILLAVQGAEAAAGLVGNAVLALLRRPAQWARLR----------PDPELAA--------AA 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034678150 360 IHEVQRFGDIVplgvtHMTSR----DIEVQGFRIPKGTTLITNLSSVLKDEAVWEKPFRFHPEhfldaqghfvKPEAFLP 435
Cdd:cd11036   225 VAETLRYDPPV-----RLERRfaaeDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLG----------RPTARSA 289
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034678150 436 -FSAGRRACLGEPLARMELFLFFTSLLQHFSFSVAAGQP-RPSHSRVVSF 483
Cdd:cd11036   290 hFGLGRHACLGAALARAAAAAALRALAARFPGLRAAGPVvRRLNARIPVF 339
 
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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