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Conserved domains on  [gi|7549754|ref|NP_037074|]
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cytochrome P450 7A1 [Rattus norvegicus]

Protein Classification

cytochrome P450( domain architecture ID 15334980)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
55-497 0e+00

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


:

Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 797.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   55 FLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLCHGKYFDWKKFHYTTSAKAFGHRSIDPNDGNTTENINNTFTKTLQ 134
Cdd:cd20631   1 FLRSRQKKYGHIFTCKIAGKYVHFITDPFSYHSVIRHGKHLDWKKFHFATSAKAFGHVSFDPSDGNTTENIHDTFIKTLQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  135 GDALCSLSEAMMQNLQSVMRPPGLPKSKSNAWVTEGMYAFCYRVMFEAGYLTLFGRDI-------SKTDTQKALILNNLD 207
Cdd:cd20631  81 GSALDSLTESMMENLQYVMLQDKSSSSSTKAWVTEGLYSFCYRVMFEAGYLTLFGKELtaredknARLEAQRALILNALE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  208 NFKQFDQVFPALVAGLPIHLFKTAHKAREKLAEGLKHKNLCVRDQVSELIRLRMFLNDTLSTFDDMEKAKTHLAILWASQ 287
Cdd:cd20631 161 NFKEFDKVFPALVAGLPIHMFKTAKSAREALAERLLHENLQKRENISELISLRMLLNDTLSTLDEMEKARTHVAMLWASQ 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  288 ANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGQELSSGGSAIYLDQVQLNDLPVLDSIIKEALRLSSASLNIRTAK 367
Cdd:cd20631 241 ANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEKTGQKVSDGGNPIVLTREQLDDMPVLGSIIKEALRLSSASLNIRVAK 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  368 EDFTLHLEDG-SYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSNGNKLKCFYMPFGSGATICPG 446
Cdd:cd20631 321 EDFTLHLDSGeSYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTFYKNGRKLKYYYMPFGSGTSKCPG 400
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 7549754  447 RLFAVQEIKQFLILMLSCFELEFVESQVKCPPLDQSRAGLGILPPLHDIEF 497
Cdd:cd20631 401 RFFAINEIKQFLSLMLCYFDMELLDGNAKCPPLDQSRAGLGILPPTHDVDF 451
 
Name Accession Description Interval E-value
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
55-497 0e+00

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 797.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   55 FLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLCHGKYFDWKKFHYTTSAKAFGHRSIDPNDGNTTENINNTFTKTLQ 134
Cdd:cd20631   1 FLRSRQKKYGHIFTCKIAGKYVHFITDPFSYHSVIRHGKHLDWKKFHFATSAKAFGHVSFDPSDGNTTENIHDTFIKTLQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  135 GDALCSLSEAMMQNLQSVMRPPGLPKSKSNAWVTEGMYAFCYRVMFEAGYLTLFGRDI-------SKTDTQKALILNNLD 207
Cdd:cd20631  81 GSALDSLTESMMENLQYVMLQDKSSSSSTKAWVTEGLYSFCYRVMFEAGYLTLFGKELtaredknARLEAQRALILNALE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  208 NFKQFDQVFPALVAGLPIHLFKTAHKAREKLAEGLKHKNLCVRDQVSELIRLRMFLNDTLSTFDDMEKAKTHLAILWASQ 287
Cdd:cd20631 161 NFKEFDKVFPALVAGLPIHMFKTAKSAREALAERLLHENLQKRENISELISLRMLLNDTLSTLDEMEKARTHVAMLWASQ 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  288 ANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGQELSSGGSAIYLDQVQLNDLPVLDSIIKEALRLSSASLNIRTAK 367
Cdd:cd20631 241 ANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEKTGQKVSDGGNPIVLTREQLDDMPVLGSIIKEALRLSSASLNIRVAK 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  368 EDFTLHLEDG-SYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSNGNKLKCFYMPFGSGATICPG 446
Cdd:cd20631 321 EDFTLHLDSGeSYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTFYKNGRKLKYYYMPFGSGTSKCPG 400
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 7549754  447 RLFAVQEIKQFLILMLSCFELEFVESQVKCPPLDQSRAGLGILPPLHDIEF 497
Cdd:cd20631 401 RFFAINEIKQFLSLMLCYFDMELLDGNAKCPPLDQSRAGLGILPPTHDVDF 451
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
32-497 4.10e-78

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: 251.81  E-value: 4.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754     32 PPLENGLiPYLGCALKFGS--NPLEFLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLCHGKY---FDWKKFHYTTSA 106
Cdd:pfam00067   1 PPGPPPL-PLFGNLLQLGRkgNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEefsGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    107 KAFGHRSIDPNDGNTTENINNTFTKTLQGD---ALCSLSEAMMQNLQSVMRPPGLPKSKSN--AWVTEGMYAFCYRVMFE 181
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFgklSFEPRVEEEARDLVEKLRKTAGEPGVIDitDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    182 AGYLTLFGRDISKTDTQKALILNNLDNF-KQFDQVFPALvAGLPIHLFKTAHKAREKLAEGLKHKNLCVRDQVS-ELIRL 259
Cdd:pfam00067 160 ERFGSLEDPKFLELVKAVQELSSLLSSPsPQLLDLFPIL-KYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDsAKKSP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    260 RMFLNDTL--------STFDDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGQelssggs 331
Cdd:pfam00067 239 RDFLDALLlakeeedgSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRS------- 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    332 aiyLDQVQLNDLPVLDSIIKEALRLSSAS-LNI-RTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKY 409
Cdd:pfam00067 312 ---PTYDDLQNMPYLDAVIKETLRLHPVVpLLLpREVTKDTVI----PGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDP 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    410 DRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQVKCPPLDQSraGLGIL 489
Cdd:pfam00067 385 ERFLDENGKFRKSFA---------FLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETP--GLLLP 453

                  ....*...
gi 7549754    490 PPLHDIEF 497
Cdd:pfam00067 454 PKPYKLKF 461
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
11-473 3.31e-19

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 89.99  E-value: 3.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    11 AVLVSCCIWFIVGIRRRKAGEPPLENGLI--PYLGCALK-FGSNPLEFLRANQRKHGHVFTCKLMGKYVHFITNSLSYHK 87
Cdd:PLN02196  13 GALFLCLLRFLAGFRRSSSTKLPLPPGTMgwPYVGETFQlYSQDPNVFFASKQKRYGSVFKTHVLGCPCVMISSPEAAKF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    88 VLCHGKYFdWKKFHYTTSAKAFGHRSIDPNDGNTTENINNTFTKTLQGDALcslsEAMMQNLQSVmrppglPKSKSNAWv 167
Cdd:PLN02196  93 VLVTKSHL-FKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLRAFMPDAI----RNMVPDIESI------AQESLNSW- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   168 tEGMYAFCYRVM----FEAGYLTLFGRD--ISKTDTQKALILnnldnfkqFDQVFPALVAGLPIHLFKTAHKAREKLAEG 241
Cdd:PLN02196 161 -EGTQINTYQEMktytFNVALLSIFGKDevLYREDLKRCYYI--------LEKGYNSMPINLPGTLFHKSMKARKELAQI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   242 LKhKNLCVRDQvselirLRMFLNDTLSTF-------DDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEE 314
Cdd:PLN02196 232 LA-KILSKRRQ------NGSSHNDLLGSFmgdkeglTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEE 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   315 VSGALQSAGQELSsggsaiyLDQVQLNDLPVLDSIIKEALRLSSA-SLNIRTAKEDftlhLEDGSYNIRKD-DMIALYPQ 392
Cdd:PLN02196 305 QMAIRKDKEEGES-------LTWEDTKKMPLTSRVIQETLRVASIlSFTFREAVED----VEYEGYLIPKGwKVLPLFRN 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   393 LMHlDPEIYPDPLTFKYDRYldESGKAKTTFysngnklkcfyMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVES 472
Cdd:PLN02196 374 IHH-SADIFSDPGKFDPSRF--EVAPKPNTF-----------MPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIVGT 439

                 .
gi 7549754   473 Q 473
Cdd:PLN02196 440 S 440
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
322-473 2.08e-15

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: 78.01  E-value: 2.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  322 AGQELSSG--GSAIYL-----DQVQL--NDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLHledGsYNIRKDDMIALYP 391
Cdd:COG2124 237 AGHETTANalAWALYAllrhpEQLARlrAEPELLPAAVEETLRLyPPVPLLPRTATEDVELG---G-VTIPAGDRVLLSL 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  392 QLMHLDPEIYPDPLTFKYDRyldesgkakttfysNGNKlkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFE-LEFV 470
Cdd:COG2124 313 AAANRDPRVFPDPDRFDPDR--------------PPNA----HLPFGGGPHRCLGAALARLEARIALATLLRRFPdLRLA 374

                ...
gi 7549754  471 ESQ 473
Cdd:COG2124 375 PPE 377
 
Name Accession Description Interval E-value
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
55-497 0e+00

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 797.36  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   55 FLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLCHGKYFDWKKFHYTTSAKAFGHRSIDPNDGNTTENINNTFTKTLQ 134
Cdd:cd20631   1 FLRSRQKKYGHIFTCKIAGKYVHFITDPFSYHSVIRHGKHLDWKKFHFATSAKAFGHVSFDPSDGNTTENIHDTFIKTLQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  135 GDALCSLSEAMMQNLQSVMRPPGLPKSKSNAWVTEGMYAFCYRVMFEAGYLTLFGRDI-------SKTDTQKALILNNLD 207
Cdd:cd20631  81 GSALDSLTESMMENLQYVMLQDKSSSSSTKAWVTEGLYSFCYRVMFEAGYLTLFGKELtaredknARLEAQRALILNALE 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  208 NFKQFDQVFPALVAGLPIHLFKTAHKAREKLAEGLKHKNLCVRDQVSELIRLRMFLNDTLSTFDDMEKAKTHLAILWASQ 287
Cdd:cd20631 161 NFKEFDKVFPALVAGLPIHMFKTAKSAREALAERLLHENLQKRENISELISLRMLLNDTLSTLDEMEKARTHVAMLWASQ 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  288 ANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGQELSSGGSAIYLDQVQLNDLPVLDSIIKEALRLSSASLNIRTAK 367
Cdd:cd20631 241 ANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEKTGQKVSDGGNPIVLTREQLDDMPVLGSIIKEALRLSSASLNIRVAK 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  368 EDFTLHLEDG-SYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSNGNKLKCFYMPFGSGATICPG 446
Cdd:cd20631 321 EDFTLHLDSGeSYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKTTFYKNGRKLKYYYMPFGSGTSKCPG 400
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 7549754  447 RLFAVQEIKQFLILMLSCFELEFVESQVKCPPLDQSRAGLGILPPLHDIEF 497
Cdd:cd20631 401 RFFAINEIKQFLSLMLCYFDMELLDGNAKCPPLDQSRAGLGILPPTHDVDF 451
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
55-499 1.34e-170

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


Pssm-ID: 410725  Cd Length: 438  Bit Score: 487.96  E-value: 1.34e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   55 FLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLCHGKYFDWKKFHYTTSAKAFGHRSI-DPNDGNTTENINNTFtKTL 133
Cdd:cd20632   1 FLLALQKKHGDVFTVLIAGKYITFIMDPFLYPYVIKHGKQLDFHEFSDRLASKTFGYPPLrSPKFPGLNEQIHRSY-QYL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  134 QGDALCSLSEAMMQNLQSVMRPPGLpksKSNAWVTEGMYAFCYRVMFEAGYLTLFGRDiSKTDTQKALilNNL-DNFKQF 212
Cdd:cd20632  80 QGENLDILTESMMGNLQLVLRQQFL---GETDWETEELYEFCSRIMFEATFLTLYGKP-PDDDRHKVI--SELrKKFRKF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  213 DQVFPALVAGLPIHLFKTAHKAREKLAEGLKHKNLCVRDQVSELIRLRMFLNDTLSTFDDMEKAKTHLAILWASQANTIP 292
Cdd:cd20632 154 DAMFPYLVANIPIELLGATKSIREKLIKYFLPQKMAKWSNPSEVIQARQELLEQYDVLQDYDKAAHHFAFLWASVGNTIP 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  293 ATFWSLFQMIRSPEAMKAASEEVSGALQSAGQELSSgGSAIYLDQVQLNDLPVLDSIIKEALRLSSASLNIRTAKEDFTL 372
Cdd:cd20632 234 ATFWAMYYLLRHPEALAAVRDEIDHVLQSTGQELGP-DFDIHLTREQLDSLVYLESAINESLRLSSASMNIRVVQEDFTL 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  373 HLE-DGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLdESGKAKTTFYSNGNKLKCFYMPFGSGATICPGRLFAV 451
Cdd:cd20632 313 KLEsDGSVNLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFV-EDGKKKTTFYKRGQKLKYYLMPFGSGSSKCPGRFFAV 391
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 7549754  452 QEIKQFLILMLSCFELEFVESQvKCPPLDQSRAGLGILPPLHDIEFKY 499
Cdd:cd20632 392 NEIKQFLSLLLLYFDLELLEEQ-KPPGLDNSRAGLGILPPNSDVRFRY 438
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
56-497 1.72e-119

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 358.22  E-value: 1.72e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   56 LRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLCHGKY-FDWKKFHYTTSAKAFGHRSIdpndGNTTENINNTFTKTLQ 134
Cdd:cd20633   1 LQKMQKKHGDIFTVQIGGHYFTFVMDPLSFGAIVKESKSkLDFGKFASELVLRVFGYQPT----ENDHKMLQTLSTKHLM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  135 GDALCSLSEAMMQNLQSVMRPPGLPKSKSNAWVTEGMYAFCYRVMFEAGYLTLFGRD-------ISKTDTQKALILNNL- 206
Cdd:cd20633  77 GDGLVVLNQAMMENLQNLMLHSKGSGDGGREWQQDGLFHYSYNIVFRAGYLALFGNEpdkeagnKEKAKEQDLLHSEELf 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  207 DNFKQFDQVFPALVAG-LPihlfktahkAREKL-AEGLK---HKNLCV-----RDQVSELI--RLRMfLNDtlSTFDDME 274
Cdd:cd20633 157 EEFRKFDQLFPRLAYSvLP---------PKDKLeAERLKrlfWDMLSVskmsqKENISGWIseQQRQ-LAE--HGMPEYM 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  275 KAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGQELSSGGSAIYLDQVQLNDLPVLDSIIKEAL 354
Cdd:cd20633 225 QDRFMFLLLWASQGNTGPASFWLLLYLLKHPEAMKAVREEVEQVLKETGQEVKPGGPLINLTRDMLLKTPVLDSAVEETL 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  355 RLSSASLNIRTAKEDFTLHLEDG-SYNIRKDDMIALYPQL-MHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSNGNKLKC 432
Cdd:cd20633 305 RLTAAPVLIRAVVQDMTLKMANGrEYALRKGDRLALFPYLaVQMDPEIHPEPHTFKYDRFLNPDGGKKKDFYKNGKKLKY 384
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7549754  433 FYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQVKCPPLDQSRAGLGILPPLHDIEF 497
Cdd:cd20633 385 YNMPWGAGVSICPGRFFAVNEMKQFVFLMLTYFDLELVNPDEEIPSIDPSRWGFGTMQPTHDIQF 449
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
56-496 1.70e-115

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: 347.43  E-value: 1.70e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   56 LRANQRKH---GHVFTCKLMGKYVHFITNSLSYHKVLCHGKYFDWKKFHYTTSAKAFGHRSID------PNDGNTTENIN 126
Cdd:cd11040   1 LLRNGKKYfsgGPIFTIRLGGQKIYVITDPELISAVFRNPKTLSFDPIVIVVVGRVFGSPESAkkkegePGGKGLIRLLH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  127 NTFTKTLQG-DALCSLSEAMMQNLQSVMRppGLPKSKSNAWVTEGMYAFCYRVMFEAGYLTLFGRDISKTDTqkalilNN 205
Cdd:cd11040  81 DLHKKALSGgEGLDRLNEAMLENLSKLLD--ELSLSGGTSTVEVDLYEWLRDVLTRATTEALFGPKLPELDP------DL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  206 LDNFKQFDQVFPALVAGLPIHLFKTAHKAREKLAEGLK--HKNLCV-RDQVSELIRLRMFLNDTLStFDDMEKAKTHLAI 282
Cdd:cd11040 153 VEDFWTFDRGLPKLLLGLPRLLARKAYAARDRLLKALEkyYQAAREeRDDGSELIRARAKVLREAG-LSEEDIARAELAL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  283 LWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGQElssgGSAIYLDQVqLNDLPVLDSIIKEALRLSSASLN 362
Cdd:cd11040 232 LWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGT----NAILDLTDL-LTSCPLLDSTYLETLRLHSSSTS 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  363 IRTAKEDFTLhleDGSYNIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYLDESGKAKttfysnGNKLKCFYMPFGSGA 441
Cdd:cd11040 307 VRLVTEDTVL---GGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKK------GRGLPGAFRPFGGGA 377
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7549754  442 TICPGRLFAVQEIKQFLILMLSCFELEFVESQV-KCPPLDQSrAGLGILPPLHDIE 496
Cdd:cd11040 378 SLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDwKVPGMDES-PGLGILPPKRDVR 432
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
55-496 5.97e-88

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 277.03  E-value: 5.97e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   55 FLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLchgkyfdWK---KFHYTTSAKAFGHRSID---PNDGNTTENinNT 128
Cdd:cd20634   2 FLTRMKEKHGDIFTVQVAGRYVTVLLDPHSYDAVV-------WEpstSLDFTSYARLLMDRIFDvqlPSYDPTEEK--KR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  129 FTKTLQGDALCSLSEAMMQNLQSVMRPPglPKSKSNAWVTEGMYAFCYRVMFEAGYLTLFGRD-ISKTDTQKALILNNL- 206
Cdd:cd20634  73 MESHFQGANLTQLTQAMFNNLQLLLLGD--AMGLSTEWKKDGLFNFCYSLLFRAGYLTLFGNEnENSTHESQNKDRAHSa 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  207 ---DNFKQFDQVFPALVAG-LPIHLFKTAHKAREKLAEGLKHKNLCVR-DQVSELIRLRMFLNDtLSTFDDMEkAKTHLA 281
Cdd:cd20634 151 evyHEFRKLDQLLPKLARGtLSKEEKQEAASVKERLWKLLSPKRLNRKaNRSSWLESYLLHLEE-EGVDEEMQ-ARAMLL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  282 ILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGQELSSggsAIYLDQVQLNDLPVLDSIIKEALRLSSASL 361
Cdd:cd20634 229 QLWATQGNAGPAAFWLLLFLLKHPEAMAAVRGEIQRIKHQRGQPVSQ---TLTINQELLDNTPVFDSVLSETLRLTAAPF 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  362 NIRTAKEDFTLHLEDG-SYNIRKDDMIALYPQLM-HLDPEIYPDPLTFKYDRYLDESGKAKTTFYSNGNKLKCFYMPFGS 439
Cdd:cd20634 306 ITREVLQDMKLRLADGqEYNLRRGDRLCLFPFLSpQMDPEIHQEPEVFKYDRFLNADGTEKKDFYKNGKRLKYYNMPWGA 385
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7549754  440 GATICPGRLFAVQEIKQFLILMLSCFELEFVESQVKCPPLDQSRAGLGILPPLHDIE 496
Cdd:cd20634 386 GDNVCIGRHFAVNSIKQFVFLILTHFDVELKDPEAEIPEFDPSRYGFGLLQPEGDII 442
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
32-497 4.10e-78

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: 251.81  E-value: 4.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754     32 PPLENGLiPYLGCALKFGS--NPLEFLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLCHGKY---FDWKKFHYTTSA 106
Cdd:pfam00067   1 PPGPPPL-PLFGNLLQLGRkgNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEefsGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    107 KAFGHRSIDPNDGNTTENINNTFTKTLQGD---ALCSLSEAMMQNLQSVMRPPGLPKSKSN--AWVTEGMYAFCYRVMFE 181
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFgklSFEPRVEEEARDLVEKLRKTAGEPGVIDitDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    182 AGYLTLFGRDISKTDTQKALILNNLDNF-KQFDQVFPALvAGLPIHLFKTAHKAREKLAEGLKHKNLCVRDQVS-ELIRL 259
Cdd:pfam00067 160 ERFGSLEDPKFLELVKAVQELSSLLSSPsPQLLDLFPIL-KYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDsAKKSP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    260 RMFLNDTL--------STFDDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGQelssggs 331
Cdd:pfam00067 239 RDFLDALLlakeeedgSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRS------- 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    332 aiyLDQVQLNDLPVLDSIIKEALRLSSAS-LNI-RTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKY 409
Cdd:pfam00067 312 ---PTYDDLQNMPYLDAVIKETLRLHPVVpLLLpREVTKDTVI----PGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDP 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    410 DRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQVKCPPLDQSraGLGIL 489
Cdd:pfam00067 385 ERFLDENGKFRKSFA---------FLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETP--GLLLP 453

                  ....*...
gi 7549754    490 PPLHDIEF 497
Cdd:pfam00067 454 PKPYKLKF 461
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
52-479 1.95e-39

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: 147.84  E-value: 1.95e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   52 PLEFLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKvlchgkYFDWKKFHYTTSAKAFGHR--SIDPNDGNTT-ENINNT 128
Cdd:cd20635   1 PLEFIEKARQKLGPVFTVKAAGERMTFVTDEEDFHV------FFKSKDVDFQKAVQDPVQNtaSISKESFFEYhTKIHDM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  129 FTKTLQGDALCSLSEAMMQNLqsvmrppglpKSKSNAWVTEG---MYAFCYRVMFEAGYLTLFGRDISKTDTQKalILNN 205
Cdd:cd20635  75 MKGKLASSNLAPLSDKLCEEF----------KEQLELLGSEGtgdLNDLVRHVMYPAVVNNLFGKGLLPTSEEE--IKEF 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  206 LDNFKQFDQVFpALVAGLPIHLFKTAHKAREKLAEGLKHK-NLCVRDQVSELIRLRMFLNdTLSTFDDMEKAKTHLAILW 284
Cdd:cd20635 143 EEHFVKFDEQF-EYGSQLPEFFLRDWSSSKQWLLSLFEKVvPDAEKTKPLENNSKTLLQH-LLDTVDKENAPNYSLLLLW 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  285 ASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGQElssggsAIYLDQVQLNDLPVLDSIIKEALRLSSASLNIR 364
Cdd:cd20635 221 ASLANAIPITFWTLAFILSHPSVYKKVMEEISSVLGKAGKD------KIKISEDDLKKMPYIKRCVLEAIRLRSPGAITR 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  365 TAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKaKTTFysngnkLKCFyMPFGSGATIC 444
Cdd:cd20635 295 KVVKPIKI----KNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKADLE-KNVF------LEGF-VAFGGGRYQC 362
                       410       420       430
                ....*....|....*....|....*....|....*
gi 7549754  445 PGRLFAVQEIKQFLILMLSCFELEFVESQVKCPPL 479
Cdd:cd20635 363 PGRWFALMEIQMFVAMFLYKYDFTLLDPVPKPSPL 397
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
64-490 1.30e-37

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: 142.27  E-value: 1.30e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   64 GHVFTCKLMGKYVHFITNSLSYHKVLCHGKYFDWKKFHYTTSAKAFGHRSIDPNDGNTTENINNTFTKTLQGDALCSLSE 143
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  144 AMMQNLQSVMRPpgLPKSKSNAWVtegMYAFCYRVMFEAGYLTLFGRDIsktDTQKALILNNLDNFkqFDQVFPALVAGL 223
Cdd:cd00302  81 VIREIARELLDR--LAAGGEVGDD---VADLAQPLALDVIARLLGGPDL---GEDLEELAELLEAL--LKLLGPRLLRPL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  224 PIHLFKTAHKAREKLAEGLKHK-NLCVRDQVSELIRLRMFLNDTLSTFDDMEKAKTHLAILWASQANTIPATFWSLFQMI 302
Cdd:cd00302 151 PSPRLRRLRRARARLRDYLEELiARRRAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLA 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  303 RSPEAMKAASEEVSGALQSAGQElssggsaiyldqvQLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhledGSYNI 381
Cdd:cd00302 231 RHPEVQERLRAEIDAVLGDGTPE-------------DLSKLPYLEAVVEETLRLyPPVPLLPRVATEDVEL----GGYTI 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  382 RKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTfysngnklkcfYMPFGSGATICPGRLFAVQEIKQFLILM 461
Cdd:cd00302 294 PAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEPRYA-----------HLPFGAGPHRCLGARLARLELKLALATL 362
                       410       420
                ....*....|....*....|....*....
gi 7549754  462 LSCFELEFVESqvkcPPLDQSRAGLGILP 490
Cdd:cd00302 363 LRRFDFELVPD----EELEWRPSLGTLGP 387
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
60-500 3.05e-36

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


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 138.89  E-value: 3.05e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   60 QRKHGHVFTCKLMGKYVHFITNSLsyhkvlCHGKYFDWKkfhyttsakafgHRSIDPNDGNTteninntFTKTLQGDALC 139
Cdd:cd11042   2 RKKYGDVFTFNLLGKKVTVLLGPE------ANEFFFNGK------------DEDLSAEEVYG-------FLTPPFGGGVV 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  140 SLSEAMMQNLQSVMRPPGLPKSKS---------------NAWVTEG----MYAFCYRVMFEAGYlTLFGRDI-SKTDTQK 199
Cdd:cd11042  57 YYAPFAEQKEQLKFGLNILRRGKLrgyvpliveevekyfAKWGESGevdlFEEMSELTILTASR-CLLGKEVrELLDDEF 135
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  200 ALILNNLDN-FKQFDQVFPalvaGLPIHLFKTAHKAREKLAEGLkhknlcvrdqvSELIRLRMFLN-----DTLSTF--- 270
Cdd:cd11042 136 AQLYHDLDGgFTPIAFFFP----PLPLPSFRRRDRARAKLKEIF-----------SEIIQKRRKSPdkdedDMLQTLmda 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  271 --------DDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGQELssggsaiYLDQvqLND 342
Cdd:cd11042 201 kykdgrplTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDDPL-------TYDV--LKE 271
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  343 LPVLDSIIKEALRLSSASLNI-RTAKEDFTLhlEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAkt 421
Cdd:cd11042 272 MPLLHACIKETLRLHPPIHSLmRKARKPFEV--EGGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAED-- 347
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7549754  422 tfySNGNKLKcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQVkcPPLDQSRAGlgiLPPLHDIEFKYK 500
Cdd:cd11042 348 ---SKGGKFA--YLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSPF--PEPDYTTMV---VWPKGPARVRYK 416
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
46-473 8.29e-28

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: 115.07  E-value: 8.29e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   46 LKFGSNPLEFLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLCHG-KYFdwkKFHYTTSAKA-FGHRSIDPNDGNTTE 123
Cdd:cd11044   4 LEFLRDPEDFIQSRYQKYGPVFKTHLLGRPTVFVIGAEAVRFILSGEgKLV---RYGWPRSVRRlLGENSLSLQDGEEHR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  124 NINNTFTKTLQGDALCSLSEAMMQNLQSVMRppGLPKSKSNAWVTEgmyafCYRVMFEAGYLTLFGRDISKTDTQKALIl 203
Cdd:cd11044  81 RRRKLLAPAFSREALESYVPTIQAIVQSYLR--KWLKAGEVALYPE-----LRRLTFDVAARLLLGLDPEVEAEALSQD- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  204 nnldnFKQFDQVFPALVAGLPIHLFKTAHKAREKLAEGL--------KHKNLCVRDQVSELIRLRMFLNDTLSTFDDMEK 275
Cdd:cd11044 153 -----FETWTDGLFSLPVPLPFTPFGRAIRARNKLLARLeqairerqEEENAEAKDALGLLLEAKDEDGEPLSMDELKDQ 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  276 AkthLAILWASQANTIPATFWSLFQMIRSPEAmkaaseevsgaLQSAGQELSSGGSAIYLDQVQLNDLPVLDSIIKEALR 355
Cdd:cd11044 228 A---LLLLFAGHETTASALTSLCFELAQHPDV-----------LEKLRQEQDALGLEEPLTLESLKKMPYLDQVIKEVLR 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  356 LS-SASLNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESgkakttfySNGNKLKCFY 434
Cdd:cd11044 294 LVpPVGGGFRKVLEDFEL----GGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPAR--------SEDKKKPFSL 361
                       410       420       430
                ....*....|....*....|....*....|....*....
gi 7549754  435 MPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQ 473
Cdd:cd11044 362 IPFGGGPRECLGKEFAQLEMKILASELLRNYDWELLPNQ 400
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
235-493 1.48e-27

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: 114.67  E-value: 1.48e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  235 REKLAEGLKHKNLCVRDQVSELIRLRMFLNDTLSTFDDMekaKTHLA-ILWASQANTIPATFWSLFQMIRSPEAMKAASE 313
Cdd:cd11069 198 REKKAALLEGKDDSGKDILSILLRANDFADDERLSDEEL---IDQILtFLAAGHETTSTALTWALYLLAKHPDVQERLRE 274
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  314 EVSGALQSagqelSSGGSAIYLDqvqLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhledGSYNIRKDDMIALYPQ 392
Cdd:cd11069 275 EIRAALPD-----PPDGDLSYDD---LDRLPYLNAVCRETLRLyPPVPLTSREATKDTVI----KGVPIPKGTVVLIPPA 342
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  393 LMHLDPEIY-PDPLTFKYDRYLDESGKAKTT-FYSNGNklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFV 470
Cdd:cd11069 343 AINRSPEIWgPDAEEFNPERWLEPDGAASPGgAGSNYA-----LLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELD 417
                       250       260
                ....*....|....*....|...
gi 7549754  471 ESQvKCPPldqsRAGLGILPPLH 493
Cdd:cd11069 418 PDA-EVER----PIGIITRPPVD 435
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
298-475 1.56e-24

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: 105.84  E-value: 1.56e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  298 LFQMIRSPEAMKAASEEVSGALQSAGQelssggsaiyLDQVQLNDLPVLDSIIKEALRLSSASL--NIRTAKEDFTLHle 375
Cdd:cd11041 251 LLDLAAHPEYIEPLREEIRSVLAEHGG----------WTKAALNKLKKLDSFMKESQRLNPLSLvsLRRKVLKDVTLS-- 318
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  376 DGsYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKA----KTTFYSNGNKlkcfYMPFGSGATICPGRLFAV 451
Cdd:cd11041 319 DG-LTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPgqekKHQFVSTSPD----FLGFGHGRHACPGRFFAS 393
                       170       180
                ....*....|....*....|....
gi 7549754  452 QEIKQFLILMLSCFELEFVESQVK 475
Cdd:cd11041 394 NEIKLILAHLLLNYDFKLPEGGER 417
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
296-468 1.23e-23

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: 103.05  E-value: 1.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALQSAgqelssggsaiylDQVQLNDLPVLDSIIKEALRLSSASLNI-RTAKEDFTLhl 374
Cdd:cd11053 245 WAFYWLHRHPEVLARLLAELDALGGDP-------------DPEDIAKLPYLDAVIKETLRLYPVAPLVpRRVKEPVEL-- 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 edGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDEsgkaKTTFYSngnklkcfYMPFGSGATICPGRLFAVQEI 454
Cdd:cd11053 310 --GGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGR----KPSPYE--------YLPFGGGVRRCIGAAFALLEM 375
                       170
                ....*....|....
gi 7549754  455 KQFLILMLSCFELE 468
Cdd:cd11053 376 KVVLATLLRRFRLE 389
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
296-476 7.79e-21

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: 94.52  E-value: 7.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALQSAGQelssggsaiyLDQVQLNDLPVLDSIIKEALRLSS-ASLNIRTAKEDFTLhl 374
Cdd:cd11054 253 FLLYHLAKNPEVQEKLYEEIRSVLPDGEP----------ITAEDLKKMPYLKACIKESLRLYPvAPGNGRILPKDIVL-- 320
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 edGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTT--FYSngnklkcfyMPFGSGATICPGRLFAVQ 452
Cdd:cd11054 321 --SGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENKNIhpFAS---------LPFGFGPRMCIGRRFAEL 389
                       170       180
                ....*....|....*....|....
gi 7549754  453 EIKQFLILMLSCFELEFVESQVKC 476
Cdd:cd11054 390 EMYLLLAKLLQNFKVEYHHEELKV 413
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
298-469 9.56e-21

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: 94.56  E-value: 9.56e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  298 LFQMIRSPEAMKAASEEVSGALqsagqelssGGSAIYLDQVqlNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLHled 376
Cdd:cd11068 254 LYYLLKNPEVLAKARAEVDEVL---------GDDPPPYEQV--AKLRYIRRVLDETLRLwPTAPAFARKPKEDTVLG--- 319
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  377 GSYNIRKDDMI-ALYPQLmHLDPEIY-PDPLTFKYDRYLDEsgkakttfysNGNKL-KCFYMPFGSGATICPGRLFAVQE 453
Cdd:cd11068 320 GKYPLKKGDPVlVLLPAL-HRDPSVWgEDAEEFRPERFLPE----------EFRKLpPNAWKPFGNGQRACIGRQFALQE 388
                       170
                ....*....|....*.
gi 7549754  454 IKQFLILMLSCFELEF 469
Cdd:cd11068 389 ATLVLAMLLQRFDFED 404
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
328-495 2.54e-20

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: 93.03  E-value: 2.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  328 SGGSAIYLDQVQlnDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLT 406
Cdd:cd11055 272 PDDGSPTYDTVS--KLKYLDMVINETLRLyPPAFFISRECKEDCTI----NGVFIPKGVDVVIPVYAIHHDPEFWPDPEK 345
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  407 FKYDRYLDESgKAKTTFYSngnklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQVKCPPLDQSragl 486
Cdd:cd11055 346 FDPERFSPEN-KAKRHPYA--------YLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKETEIPLKLVGG---- 412

                ....*....
gi 7549754  487 GILPPLHDI 495
Cdd:cd11055 413 ATLSPKNGI 421
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
186-490 3.09e-20

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: 92.99  E-value: 3.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  186 TLFGRDI-SKTD--------TQKALILNNLDNFKQ-FDQVFPALVAGLPI------------HLFKTAHKAREKlaeglk 243
Cdd:cd11056 122 CAFGLDAnSLNDpenefremGRRLFEPSRLRGLKFmLLFFFPKLARLLRLkffpkevedffrKLVRDTIEYREK------ 195
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  244 hKNLcVR-DQVSELIRLRmflNDTLSTFDDMEKAKTHLAIlwASQA--------NTIPAT-FWSLFQMIRSPEAMKAASE 313
Cdd:cd11056 196 -NNI-VRnDFIDLLLELK---KKGKIEDDKSEKELTDEEL--AAQAfvfflagfETSSSTlSFALYELAKNPEIQEKLRE 268
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  314 EVSGALQSAGQELSsggsaiYldqVQLNDLPVLDSIIKEALRLSSASLNI-RTAKEDFTLhlEDGSYNIRKDDMIALYPQ 392
Cdd:cd11056 269 EIDEVLEKHGGELT------Y---EALQEMKYLDQVVNETLRKYPPLPFLdRVCTKDYTL--PGTDVVIEKGTPVIIPVY 337
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  393 LMHLDPEIYPDPLTFKYDRYLDESGKakttfysngNKLKCFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVES 472
Cdd:cd11056 338 ALHHDPKYYPEPEKFDPERFSPENKK---------KRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSK 408
                       330
                ....*....|....*...
gi 7549754  473 QVKcpPLDQSRAGLGILP 490
Cdd:cd11056 409 TKI--PLKLSPKSFVLSP 424
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
46-460 1.46e-19

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: 90.73  E-value: 1.46e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   46 LKFGSNP------LEFLRANQRKHGHVFTcklmGKYVHFITNSLSYHKVLCHGKYFDWKKfhyttsakafgHRSIdpndg 119
Cdd:cd20617   6 LWLGDVPtvvlsdPEIIKEAFVKNGDNFS----DRPLLPSFEIISGGKGILFSNGDYWKE-----------LRRF----- 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  120 nttenINNTFTKT----LQGDALCSLSEAMMQNLQSVMrppglpKSKSNAWVTEGMYAFCYRVMFEagylTLFGRDISKT 195
Cdd:cd20617  66 -----ALSSLTKTklkkKMEELIEEEVNKLIESLKKHS------KSGEPFDPRPYFKKFVLNIINQ----FLFGKRFPDE 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  196 DTQKAL-ILNNLDN-FKQFDQVFPALVAGLPIHLFKTAHKAREKLAEGLK---------HKNL----CVRDQVSELIRLR 260
Cdd:cd20617 131 DDGEFLkLVKPIEEiFKELGSGNPSDFIPILLPFYFLYLKKLKKSYDKIKdfiekiieeHLKTidpnNPRDLIDDELLLL 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  261 MFLNDTlSTFDDMEKAKTHLAILWASQ---ANTIpatFWSLFQMIRSPEAMKAASEEVSGALqsaGQElssggsaiylDQ 337
Cdd:cd20617 211 LKEGDS-GLFDDDSIISTCLDLFLAGTdttSTTL---EWFLLYLANNPEIQEKIYEEIDNVV---GND----------RR 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  338 VQLND---LPVLDSIIKEALRL-SSASLNI-RTAKEDFTLhledGSYNIRKDDMIalYPQL--MHLDPEIYPDPLTFKYD 410
Cdd:cd20617 274 VTLSDrskLPYLNAVIKEVLRLrPILPLGLpRVTTEDTEI----GGYFIPKGTQI--IINIysLHRDEKYFEDPEEFNPE 347
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 7549754  411 RYLDESGKAKTTfysngnklkcFYMPFGSGATICPGRLFAVQEIkqFLIL 460
Cdd:cd20617 348 RFLENDGNKLSE----------QFIPFGIGKRNCVGENLARDEL--FLFF 385
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
11-473 3.31e-19

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 89.99  E-value: 3.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    11 AVLVSCCIWFIVGIRRRKAGEPPLENGLI--PYLGCALK-FGSNPLEFLRANQRKHGHVFTCKLMGKYVHFITNSLSYHK 87
Cdd:PLN02196  13 GALFLCLLRFLAGFRRSSSTKLPLPPGTMgwPYVGETFQlYSQDPNVFFASKQKRYGSVFKTHVLGCPCVMISSPEAAKF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754    88 VLCHGKYFdWKKFHYTTSAKAFGHRSIDPNDGNTTENINNTFTKTLQGDALcslsEAMMQNLQSVmrppglPKSKSNAWv 167
Cdd:PLN02196  93 VLVTKSHL-FKPTFPASKERMLGKQAIFFHQGDYHAKLRKLVLRAFMPDAI----RNMVPDIESI------AQESLNSW- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   168 tEGMYAFCYRVM----FEAGYLTLFGRD--ISKTDTQKALILnnldnfkqFDQVFPALVAGLPIHLFKTAHKAREKLAEG 241
Cdd:PLN02196 161 -EGTQINTYQEMktytFNVALLSIFGKDevLYREDLKRCYYI--------LEKGYNSMPINLPGTLFHKSMKARKELAQI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   242 LKhKNLCVRDQvselirLRMFLNDTLSTF-------DDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEE 314
Cdd:PLN02196 232 LA-KILSKRRQ------NGSSHNDLLGSFmgdkeglTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEE 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   315 VSGALQSAGQELSsggsaiyLDQVQLNDLPVLDSIIKEALRLSSA-SLNIRTAKEDftlhLEDGSYNIRKD-DMIALYPQ 392
Cdd:PLN02196 305 QMAIRKDKEEGES-------LTWEDTKKMPLTSRVIQETLRVASIlSFTFREAVED----VEYEGYLIPKGwKVLPLFRN 373
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   393 LMHlDPEIYPDPLTFKYDRYldESGKAKTTFysngnklkcfyMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVES 472
Cdd:PLN02196 374 IHH-SADIFSDPGKFDPSRF--EVAPKPNTF-----------MPFGNGTHSCPGNELAKLEISVLIHHLTTKYRWSIVGT 439

                 .
gi 7549754   473 Q 473
Cdd:PLN02196 440 S 440
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
296-479 1.62e-18

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: 87.63  E-value: 1.62e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALqsagqelssGGSAIYLDQVQlnDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhl 374
Cdd:cd20620 234 WTWYLLAQHPEVAARLRAEVDRVL---------GGRPPTAEDLP--QLPYTEMVLQESLRLyPPAWIIGREAVEDDEI-- 300
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 edGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAkttfysngnKLKCFYMPFGSGATICPGRLFAVQEI 454
Cdd:cd20620 301 --GGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAA---------RPRYAYFPFGGGPRICIGNHFAMMEA 369
                       170       180
                ....*....|....*....|....*.
gi 7549754  455 KQFLILMLSCFELEFVESQ-VKCPPL 479
Cdd:cd20620 370 VLLLATIAQRFRLRLVPGQpVEPEPL 395
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
296-468 2.44e-18

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: 87.31  E-value: 2.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALQSAGQelssggsaiyLDQVQLNDLPVLDSIIKEALRL--SSASLNIRTAKEDFTLh 373
Cdd:cd20621 251 MCLYYLAKYPEIQEKLRQEIKSVVGNDDD----------ITFEDLQKLNYLNAFIKEVLRLynPAPFLFPRVATQDHQI- 319
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  374 ledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQE 453
Cdd:cd20621 320 ---GDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFV---------FIPFSAGPRNCIGQHLALME 387
                       170
                ....*....|....*
gi 7549754  454 IKQFLILMLSCFELE 468
Cdd:cd20621 388 AKIILIYILKNFEIE 402
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
231-495 2.45e-18

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: 87.08  E-value: 2.45e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  231 AHKAREKLaeglKHKNLCVRDQVSELIRLRMFLNDTLSTFDDMEKAKTH--LAILWASQANTIPATF-WSLFQMIRSPEA 307
Cdd:cd20652 192 EHKRRLKP----ENPRDAEDFELCELEKAKKEGEDRDLFDGFYTDEQLHhlLADLFGAGVDTTITTLrWFLLYMALFPKE 267
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  308 MKAASEEVsgalqsagqeLSSGGSAIYLDQVQLNDLPVLDSIIKEALRLSS-ASLNI-RTAKEDFTLhledGSYNIRKDD 385
Cdd:cd20652 268 QRRIQREL----------DEVVGRPDLVTLEDLSSLPYLQACISESQRIRSvVPLGIpHGCTEDAVL----AGYRIPKGS 333
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  386 MIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCF 465
Cdd:cd20652 334 MIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEA---------FIPFQTGKRMCLGDELARMILFLFTARILRKF 404
                       250       260       270
                ....*....|....*....|....*....|
gi 7549754  466 ELEfVESQVKCPPLdQSRAGLGILPPLHDI 495
Cdd:cd20652 405 RIA-LPDGQPVDSE-GGNVGITLTPPPFKI 432
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
235-467 3.48e-18

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: 86.90  E-value: 3.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  235 REKLAEGLKHKNlcvrDQVSELIRLRMFLNDTLSTFDDME---KAkTHLAILWASQANTIPATFWSLFQMIRSPEAMKAA 311
Cdd:cd20654 204 RQKRSSSGKSKN----DEDDDDVMMLSILEDSQISGYDADtviKA-TCLELILGGSDTTAVTLTWALSLLLNNPHVLKKA 278
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  312 SEEVSgalqsagqelSSGGSAIYLDQVQLNDLPVLDSIIKEALRLSSAS--LNIRTAKEDFTLhledGSYNIRKDdmIAL 389
Cdd:cd20654 279 QEELD----------THVGKDRWVEESDIKNLVYLQAIVKETLRLYPPGplLGPREATEDCTV----GGYHVPKG--TRL 342
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  390 YPQL--MHLDPEIYPDPLTFKYDRYLdeSGKAKTTFYSNGNKLkcfyMPFGSGATICPGRLFAVQEIKQFLILMLSCFEL 467
Cdd:cd20654 343 LVNVwkIQRDPNVWSDPLEFKPERFL--TTHKDIDVRGQNFEL----IPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDI 416
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
265-471 4.15e-18

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: 86.22  E-value: 4.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  265 DTLSTFDDMEKAKTHLAILWASQ---ANTIPatfWSLFQMIRSPEAMKAASEEVSGALqsagqelssGGSAIYLDQVQLN 341
Cdd:cd11083 213 DPDARLTDDEIYANVLTLLLAGEdttANTLA---WMLYYLASRPDVQARVREEVDAVL---------GGARVPPLLEALD 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  342 DLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAK 420
Cdd:cd11083 281 RLPYLEAVARETLRLkPVAPLLFLEPNEDTVV----GDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAE 356
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 7549754  421 TTFYSNgnklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVE 471
Cdd:cd11083 357 PHDPSS-------LLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIELPE 400
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
223-467 1.84e-17

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: 84.29  E-value: 1.84e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  223 LPIHLFKTAHKAREKLAEGLkHKNLCVR------DQVSELIRLRMFLNDTLSTFDDMEkaktHLAILWASQANTIPATFW 296
Cdd:cd11045 158 IPGTRWWRGLRGRRYLEEYF-RRRIPERragggdDLFSALCRAEDEDGDRFSDDDIVN----HMIFLMMAAHDTTTSTLT 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  297 SLFQMI-RSPEAMKAASEEVsgalqsagQELSSGGsaiyLDQVQLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFtlhl 374
Cdd:cd11045 233 SMAYFLaRHPEWQERLREES--------LALGKGT----LDYEDLGQLEVTDWVFKEALRLvPPVPTLPRRAVKDT---- 296
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 EDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSngnklkcfYMPFGSGATICPGRLFAVQEI 454
Cdd:cd11045 297 EVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRYA--------WAPFGGGAHKCIGLHFAGMEV 368
                       250
                ....*....|...
gi 7549754  455 KQFLILMLSCFEL 467
Cdd:cd11045 369 KAILHQMLRRFRW 381
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
296-490 2.56e-17

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: 84.18  E-value: 2.56e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEvsgalqsagqelssggsaiyLDQV-------QLND---LPVLDSIIKEALRLSS-ASLNI- 363
Cdd:cd11027 251 WAIAYLVNYPEVQAKLHAE--------------------LDDVigrdrlpTLSDrkrLPYLEATIAEVLRLSSvVPLALp 310
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  364 RTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSngnklkcfYMPFGSGATI 443
Cdd:cd11027 311 HKTTCDTTL----RGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVPKPES--------FLPFSAGRRV 378
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 7549754  444 CPGRLFAVQEIkqFLIL--MLSCFELEFVESqvkCPPLD-QSRAGLGILP 490
Cdd:cd11027 379 CLGESLAKAEL--FLFLarLLQKFRFSPPEG---EPPPElEGIPGLVLYP 423
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
296-454 4.59e-17

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: 83.08  E-value: 4.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALQsagqelssGGSAIYLDqvqLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhl 374
Cdd:cd11049 242 WAFHLLARHPEVERRLHAELDAVLG--------GRPATFED---LPRLTYTRRVVTEALRLyPPVWLLTRRTTADVEL-- 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 edGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQEI 454
Cdd:cd11049 309 --GGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGA---------FIPFGAGARKCIGDTFALTEL 377
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
339-458 1.63e-16

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: 81.58  E-value: 1.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  339 QLNDLPVLDSIIKEALRLSSA--SLNIRTAKEDFTLhleDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDES 416
Cdd:cd11059 277 DLDKLPYLNAVIRETLRLYPPipGSLPRVVPEGGAT---IGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPS 353
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 7549754  417 GkakttfySNGNKLKCFYMPFGSGATICPGRLFAVQEIKQFL 458
Cdd:cd11059 354 G-------ETAREMKRAFWPFGSGSRMCIGMNLALMEMKLAL 388
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
296-495 2.68e-16

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: 80.77  E-value: 2.68e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALQSagqelsSGGSAIYLDqvqLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhl 374
Cdd:cd20660 254 WALYLIGSHPEVQEKVHEELDRIFGD------SDRPATMDD---LKEMKYLECVIKEALRLfPSVPMFGRTLSEDIEI-- 322
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 edGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQEI 454
Cdd:cd20660 323 --GGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHPYA---------YIPFSAGPRNCIGQKFALMEE 391
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 7549754  455 KQFLILMLSCFELEFVESQVKCPPLDQSraglgILPPLHDI 495
Cdd:cd20660 392 KVVLSSILRNFRIESVQKREDLKPAGEL-----ILRPVDGI 427
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
290-491 3.80e-16

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: 80.34  E-value: 3.80e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  290 TIPATF-WSLFQMIRSPEAMKAASEEvsgalqsagqelssggsaiyLDQV-------QLND---LPVLDSIIKEALRLSS 358
Cdd:cd20651 240 TTSNTLgFAFLYLLLNPEVQRKVQEE--------------------IDEVvgrdrlpTLDDrskLPYTEAVILEVLRIFT 299
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  359 -ASLNI-RTAKEDFTLhledGSYNIRKDDMI--ALYPqlMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSngnklkcfy 434
Cdd:cd20651 300 lVPIGIpHRALKDTTL----GGYRIPKDTTIlaSLYS--VHMDPEYWGDPEEFRPERFLDEDGKLLKDEWF--------- 364
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 7549754  435 MPFGSGATICPGRLFAVQEIkqFLIL--MLSCFELEFVESQVkcPPLDQSRAGLGILPP 491
Cdd:cd20651 365 LPFGAGKRRCLGESLARNEL--FLFFtgLLQNFTFSPPNGSL--PDLEGIPGGITLSPK 419
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
280-466 5.59e-16

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: 79.91  E-value: 5.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  280 LAILWASQaNTIPATF-WSLFQMIRSPEAMKAASEEVsgalqsagqeLSSGGSAIYLDQVQLNDLPVLDSIIKEALRL-S 357
Cdd:cd11063 222 LNILLAGR-DTTASLLsFLFYELARHPEVWAKLREEV----------LSLFGPEPTPTYEDLKNMKYLRAVINETLRLyP 290
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  358 SASLNIRTAKEDFTLHL---EDGS--YNIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYLDESgkakttfysngnKLK 431
Cdd:cd11063 291 PVPLNSRVAVRDTTLPRgggPDGKspIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWEDLK------------RPG 358
                       170       180       190
                ....*....|....*....|....*....|....*
gi 7549754  432 CFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFE 466
Cdd:cd11063 359 WEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFD 393
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
340-462 5.77e-16

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: 80.00  E-value: 5.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  340 LNDLPVLDSIIKEALRLS-SASLNIRTAKEDFTLHLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGK 418
Cdd:cd11071 282 LEKMPLLKSVVYETLRLHpPVPLQYGRARKDFVIESHDASYKIKKGELLVGYQPLATRDPKVFDNPDEFVPDRFMGEEGK 361
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 7549754  419 A-KTTFYSNGnklkcfymPFGSGAT----ICPGRLFAVQEIKQFLILML 462
Cdd:cd11071 362 LlKHLIWSNG--------PETEEPTpdnkQCPGKDLVVLLARLFVAELF 402
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
60-458 6.90e-16

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: 79.53  E-value: 6.90e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   60 QRKHGHVFTCKLMGKYVHFITNSLSYHKVLCH-GKYFdwkKFHYTTS-AKAFGHRSIDPNDGNTTENINNTFTKTLQGDA 137
Cdd:cd11043   2 IKRYGPVFKTSLFGRPTVVSADPEANRFILQNeGKLF---VSWYPKSvRKLLGKSSLLTVSGEEHKRLRGLLLSFLGPEA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  138 LcslSEAMMQNLQSVMRP--PGLPKSKSNAwVTEGMYAFCYRVMFEAgyltLFGrdISKTDTQKALilnnldnFKQFDQV 215
Cdd:cd11043  79 L---KDRLLGDIDELVRQhlDSWWRGKSVV-VLELAKKMTFELICKL----LLG--IDPEEVVEEL-------RKEFQAF 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  216 FPALVAgLPIHLFKTAH----KAREKLAEGLK----------HKNLCVRDQVSELIRLRmflNDTLSTFDDMEKAKTHLA 281
Cdd:cd11043 142 LEGLLS-FPLNLPGTTFhralKARKRIRKELKkiieerraelEKASPKGDLLDVLLEEK---DEDGDSLTDEEILDNILT 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  282 ILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGqelssGGSAIYLDQVQlnDLPVLDSIIKEALRLSSASL 361
Cdd:cd11043 218 LLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAKRKE-----EGEGLTWEDYK--SMKYTWQVINETLRLAPIVP 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  362 NI-RTAKEDFTLhleDGsYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDES-GKAKTtfysngnklkcfYMPFGS 439
Cdd:cd11043 291 GVfRKALQDVEY---KG-YTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGkGVPYT------------FLPFGG 354
                       410
                ....*....|....*....
gi 7549754  440 GATICPGRLFAVQEIKQFL 458
Cdd:cd11043 355 GPRLCPGAELAKLEILVFL 373
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
288-471 1.83e-15

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: 78.42  E-value: 1.83e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  288 ANTIPATFWSLfqmIRSPEAMKAASEEVSGALQSaGQELSSGGsaiyldqvQLNDLPVLDSIIKEALRLSSA---SLNIR 364
Cdd:cd11061 233 ATALSAIFYYL---ARNPEAYEKLRAELDSTFPS-DDEIRLGP--------KLKSLPYLRACIDEALRLSPPvpsGLPRE 300
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  365 TAKEDFTLhleDGSYnIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKttfysngnKLKCFYMPFGSGATIC 444
Cdd:cd11061 301 TPPGGLTI---DGEY-IPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELV--------RARSAFIPFSIGPRGC 368
                       170       180
                ....*....|....*....|....*..
gi 7549754  445 PGRLFAVQEIKQFLILMLSCFELEFVE 471
Cdd:cd11061 369 IGKNLAYMELRLVLARLLHRYDFRLAP 395
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
322-473 2.08e-15

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: 78.01  E-value: 2.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  322 AGQELSSG--GSAIYL-----DQVQL--NDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLHledGsYNIRKDDMIALYP 391
Cdd:COG2124 237 AGHETTANalAWALYAllrhpEQLARlrAEPELLPAAVEETLRLyPPVPLLPRTATEDVELG---G-VTIPAGDRVLLSL 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  392 QLMHLDPEIYPDPLTFKYDRyldesgkakttfysNGNKlkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFE-LEFV 470
Cdd:COG2124 313 AAANRDPRVFPDPDRFDPDR--------------PPNA----HLPFGGGPHRCLGAALARLEARIALATLLRRFPdLRLA 374

                ...
gi 7549754  471 ESQ 473
Cdd:COG2124 375 PPE 377
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
293-471 7.32e-15

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: 76.48  E-value: 7.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  293 ATFWSLFQMIRSPEAMKAASEEVSgalqsagqelSSGGSAIYLDQVQLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFT 371
Cdd:cd20655 247 TTEWAMAELINNPEVLEKAREEID----------SVVGKTRLVQESDLPNLPYLQAVVKETLRLhPPGPLLVRESTEGCK 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  372 LhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLdESGKAKTTFYSNGNKLKcfYMPFGSGATICPGRLFAV 451
Cdd:cd20655 317 I----NGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFL-ASSRSGQELDVRGQHFK--LLPFGSGRRGCPGASLAY 389
                       170       180
                ....*....|....*....|
gi 7549754  452 QEIKQFLILMLSCFELEFVE 471
Cdd:cd20655 390 QVVGTAIAAMVQCFDWKVGD 409
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
339-501 7.52e-15

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: 76.41  E-value: 7.52e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  339 QLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESg 417
Cdd:cd20628 285 DLNKMKYLERVIKETLRLyPSVPFIGRRLTEDIKL----DGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPEN- 359
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  418 KAKTTFYSngnklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVesqvkcppldqsraglgilPPLHDIEF 497
Cdd:cd20628 360 SAKRHPYA--------YIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFRVLPV-------------------PPGEDLKL 412

                ....
gi 7549754  498 KYKL 501
Cdd:cd20628 413 IAEI 416
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
296-472 1.03e-14

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: 76.25  E-value: 1.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALqsagqelssgGSAIYLDQVQLNDLPVLDSIIKEALRL-SSASLNIRTAKEDftLHL 374
Cdd:cd11046 262 WTLYELSQNPELMAKVQAEVDAVL----------GDRLPPTYEDLKKLKYTRRVLNESLRLyPQPPVLIRRAVED--DKL 329
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 EDGSYNIRK--DDMIALYPqlMHLDPEIYPDPLTFKYDRYLDesgkaktTFYSNGNKLKCFY--MPFGSGATICPGRLFA 450
Cdd:cd11046 330 PGGGVKVPAgtDIFISVYN--LHRSPELWEDPEEFDPERFLD-------PFINPPNEVIDDFafLPFGGGPRKCLGDQFA 400
                       170       180
                ....*....|....*....|..
gi 7549754  451 VQEIKQFLILMLSCFELEFVES 472
Cdd:cd11046 401 LLEATVALAMLLRRFDFELDVG 422
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
297-479 5.98e-14

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: 73.72  E-value: 5.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  297 SLFQMIRSPEAMKAASEEVSGALQSAGQELSSGgsaiyldqvqLNDLPVLDSIIKEALRLSSASLNI-RTAKEDFTLHle 375
Cdd:cd20644 255 TLFELARNPDVQQILRQESLAAAAQISEHPQKA----------LTELPLLKAALKETLRLYPVGITVqRVPSSDLVLQ-- 322
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  376 dgSYNIRKDDM--IALYPqlMHLDPEIYPDPLTFKYDRYLDESGKAkTTFYSngnklkcfyMPFGSGATICPGRLFAVQE 453
Cdd:cd20644 323 --NYHIPAGTLvqVFLYS--LGRSAALFPRPERYDPQRWLDIRGSG-RNFKH---------LAFGFGMRQCLGRRLAEAE 388
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 7549754  454 IKQFLILMLSCFELEFVES-----------QVKCPPL 479
Cdd:cd20644 389 MLLLLMHVLKNFLVETLSQediktvysfilRPEKPPL 425
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
288-473 1.97e-13

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: 72.17  E-value: 1.97e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  288 ANTIPATfwsLFQMIRSPEAMKAASEEVSGALqsagqelssgGSAIYLDQVQLNDLPVLDSIIKEALRL-SSASLNIRTA 366
Cdd:cd20613 251 ANLLSFT---LLELGRHPEILKRLQAEVDEVL----------GSKQYVEYEDLGKLEYLSQVLKETLRLyPPVPGTSREL 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  367 KEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPG 446
Cdd:cd20613 318 TKDIEL----GGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIPSYA---------YFPFSLGPRSCIG 384
                       170       180
                ....*....|....*....|....*..
gi 7549754  447 RLFAVQEIKQFLILMLSCFELEFVESQ 473
Cdd:cd20613 385 QQFAQIEAKVILAKLLQNFKFELVPGQ 411
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
296-475 1.99e-13

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: 72.20  E-value: 1.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALQsagqelssGGSAIYLDQvqLNDLPVLDSIIKEALRLSSASLNI-RTAKEDFTLhl 374
Cdd:cd20659 249 WTLYSLAKHPEHQQKCREEVDEVLG--------DRDDIEWDD--LSKLPYLTMCIKESLRLYPPVPFIaRTLTKPITI-- 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 eDGSYnIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQEI 454
Cdd:cd20659 317 -DGVT-LPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDPFA---------FIPFSAGPRNCIGQNFAMNEM 385
                       170       180
                ....*....|....*....|.
gi 7549754  455 KQFLILMLSCFELEFVESQVK 475
Cdd:cd20659 386 KVVLARILRRFELSVDPNHPV 406
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
296-446 3.93e-13

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: 71.02  E-value: 3.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALQSAGQELSSggsaiyldqvQLNDLPVLDSIIKEALRLSSAS--LNIRTAKEDFTLh 373
Cdd:cd11073 253 WAMAELLRNPEKMAKARAELDEVIGKDKIVEES----------DISKLPYLQAVVKETLRLHPPAplLLPRKAEEDVEV- 321
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 7549754  374 ledGSYNIRKDDMI-----AlypqlMHLDPEIYPDPLTFKYDRYLDESGKAKttfysnGNKLKcfYMPFGSGATICPG 446
Cdd:cd11073 322 ---MGYTIPKGTQVlvnvwA-----IGRDPSVWEDPLEFKPERFLGSEIDFK------GRDFE--LIPFGSGRRICPG 383
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
282-477 7.05e-13

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: 70.52  E-value: 7.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  282 ILWASQANTIPATFWSLFQMIRSPEAMKAASEEVsgalqsagQELSSGGSAiylDQVQLNDLPVLDSIIKEALRL-SSAS 360
Cdd:cd20640 238 IYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEV--------LEVCKGGPP---DADSLSRMKTVTMVIQETLRLyPPAA 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  361 LNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYLDESGKAKTTFYSngnklkcfYMPFGS 439
Cdd:cd20640 307 FVSREALRDMKL----GGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACKPPHS--------YMPFGA 374
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 7549754  440 GATICPGRLFAVQEIKQFLILMLSCFELEFVESQVKCP 477
Cdd:cd20640 375 GARTCLGQNFAMAELKVLVSLILSKFSFTLSPEYQHSP 412
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
296-471 8.45e-13

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: 69.94  E-value: 8.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSgalqsagqelSSGGSAIYLDQVQLNDLPVLDSIIKEALRL-SSASLNI-RTAKEDFTLh 373
Cdd:cd20653 249 WAMSNLLNHPEVLKKAREEID----------TQVGQDRLIEESDLPKLPYLQNIISETLRLyPAAPLLVpHESSEDCKI- 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  374 ledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGkakttfysNGNKLkcfyMPFGSGATICPGRLFAVQE 453
Cdd:cd20653 318 ---GGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEER--------EGYKL----IPFGLGRRACPGAGLAQRV 382
                       170
                ....*....|....*...
gi 7549754  454 IKQFLILMLSCFELEFVE 471
Cdd:cd20653 383 VGLALGSLIQCFEWERVG 400
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
296-469 1.09e-12

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: 69.89  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEvsgaLQSA-GQELssggsaiyldQVQLND---LPVLDSIIKEALRLSSAS-LNI-RTAKED 369
Cdd:cd20618 251 WAMAELLRHPEVMRKAQEE----LDSVvGRER----------LVEESDlpkLPYLQAVVKETLRLHPPGpLLLpHESTED 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  370 FTLhledGSYNIRKDD--MIALYPqlMHLDPEIYPDPLTFKYDRYLDESGKAkttfySNGNKLKcfYMPFGSGATICPGR 447
Cdd:cd20618 317 CKV----AGYDIPAGTrvLVNVWA--IGRDPKVWEDPLEFKPERFLESDIDD-----VKGQDFE--LLPFGSGRRMCPGM 383
                       170       180
                ....*....|....*....|..
gi 7549754  448 LFAVQEIKQFLILMLSCFELEF 469
Cdd:cd20618 384 PLGLRMVQLTLANLLHGFDWSL 405
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
296-465 1.10e-12

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: 69.80  E-value: 1.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALQSAGqelssggsaiYLDQVQLNDLPVLDSIIKEALRLSSAS--LNIRTAKEDFTLh 373
Cdd:cd11072 250 WAMTELIRNPRVMKKAQEEVREVVGGKG----------KVTEEDLEKLKYLKAVIKETLRLHPPAplLLPRECREDCKI- 318
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  374 leDGsYNIRKDDMI-----AlypqlMHLDPEIYPDPLTFKYDRYLDESGKAKttfysnGNKLKcfYMPFGSGATICPGRL 448
Cdd:cd11072 319 --NG-YDIPAKTRVivnawA-----IGRDPKYWEDPEEFRPERFLDSSIDFK------GQDFE--LIPFGAGRRICPGIT 382
                       170
                ....*....|....*..
gi 7549754  449 FAVQEIKQFLILMLSCF 465
Cdd:cd11072 383 FGLANVELALANLLYHF 399
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
253-468 1.12e-12

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: 69.53  E-value: 1.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  253 VSELIRLRmflnDTLSTFDDmEKAKTHLAILWASQANTIPATFWSLFQ-MIRSPEAMKAASEEvsgalqsagqelssggs 331
Cdd:cd11065 206 VKDLLEEL----DKEGGLSE-EEIKYLAGSLYEAGSDTTASTLQTFILaMALHPEVQKKAQEE----------------- 263
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  332 aiyLDQV-------QLND---LPVLDSIIKEALRLSSAS-LNI-RTAKEDFTLhleDGsYNIRKDDMIalYPQL--MHLD 397
Cdd:cd11065 264 ---LDRVvgpdrlpTFEDrpnLPYVNAIVKEVLRWRPVApLGIpHALTEDDEY---EG-YFIPKGTTV--IPNAwaIHHD 334
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7549754  398 PEIYPDPLTFKYDRYLDESGKAKttfysNGNKLkcFYMPFGSGATICPGRLFAVQEIkqFLIL--MLSCFELE 468
Cdd:cd11065 335 PEVYPDPEEFDPERYLDDPKGTP-----DPPDP--PHFAFGFGRRICPGRHLAENSL--FIAIarLLWAFDIK 398
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
231-481 1.26e-12

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: 69.79  E-value: 1.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  231 AHKAREKLAEGLKHKNLcvRDQVSELIRLRMFLNDTLSTFDDMEKAKTHLAI-------LWASQANTIPATFWSLFQMIR 303
Cdd:cd20680 195 AERAEEMKAEEDKTGDS--DGESPSKKKRKAFLDMLLSVTDEEGNKLSHEDIreevdtfMFEGHDTTAAAMNWSLYLLGS 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  304 SPEAMKAASEEVSGALqsagqelssGGSAIYLDQVQLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhledGSYNIR 382
Cdd:cd20680 273 HPEVQRKVHKELDEVF---------GKSDRPVTMEDLKKLRYLECVIKESLRLfPSVPLFARSLCEDCEI----RGFKVP 339
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  383 KDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQEIKQFLILML 462
Cdd:cd20680 340 KGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYA---------YIPFSAGPRNCIGQRFALMEEKVVLSCIL 410
                       250
                ....*....|....*....
gi 7549754  463 SCFELEFVESQVKCPPLDQ 481
Cdd:cd20680 411 RHFWVEANQKREELGLVGE 429
PLN02302 PLN02302
ent-kaurenoic acid oxidase
294-468 4.28e-12

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 68.20  E-value: 4.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   294 TFWSLFQMIRSPEAMKAASEEVSGALQSagqeLSSGGSAIYLDQVQlnDLPVLDSIIKEALRLSSASLNI-RTAKEDFTL 372
Cdd:PLN02302 307 TMWATIFLQEHPEVLQKAKAEQEEIAKK----RPPGQKGLTLKDVR--KMEYLSQVIDETLRLINISLTVfREAKTDVEV 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   373 hledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTtfysngnklkcfYMPFGSGATICPGRLFAVQ 452
Cdd:PLN02302 381 ----NGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTPKAGT------------FLPFGLGSRLCPGNDLAKL 444
                        170
                 ....*....|....*.
gi 7549754   453 EIKQFLILMLSCFELE 468
Cdd:PLN02302 445 EISIFLHHFLLGYRLE 460
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
280-461 4.74e-12

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: 67.85  E-value: 4.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  280 LAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGAlqsagqelssggSAIYLDQVQLNDLPVLDSIIKEALRLSSA 359
Cdd:cd20614 214 RLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA------------GDVPRTPAELRRFPLAEALFRETLRLHPP 281
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  360 -SLNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSNgnklkcfympFG 438
Cdd:cd20614 282 vPFVFRRVLEEIEL----GGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDRAPNPVELLQ----------FG 347
                       170       180
                ....*....|....*....|...
gi 7549754  439 SGATICPGRLFAVQEIKQFLILM 461
Cdd:cd20614 348 GGPHFCLGYHVACVELVQFIVAL 370
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
290-451 6.52e-12

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: 67.27  E-value: 6.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  290 TIPATFWSLFQMIRSPEAMKAASEEVSGALqsagqelssgGSAIYLDQVQLNDLPVLDSIIKEALRLSSAS--LNIRTAK 367
Cdd:cd11075 247 TATALEWAMAELVKNPEIQEKLYEEIKEVV----------GDEAVVTEEDLPKMPYLKAVVLETLRRHPPGhfLLPHAVT 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  368 EDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSNGNKLkcfyMPFGSGATICPGR 447
Cdd:cd11075 317 EDTVL----GGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEAADIDTGSKEIKM----MPFGAGRRICPGL 388

                ....
gi 7549754  448 LFAV 451
Cdd:cd11075 389 GLAT 392
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
209-471 6.52e-12

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: 67.28  E-value: 6.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  209 FKQFDQVFPAL----------VAGLPIHLFKTAHKAREKLAEGLKhknlCVRDQVSELIRLRMFLNDTLSTFDDMEKAKT 278
Cdd:cd11062 148 LRHFPWLLKLLrslpesllkrLNPGLAVFLDFQESIAKQVDEVLR----QVSAGDPPSIVTSLFHALLNSDLPPSEKTLE 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  279 HLA-----ILWA---SQANTIPATFwslFQMIRSPEAMKAASEEVSGALQSAGQELSSggsaiyldqVQLNDLPVLDSII 350
Cdd:cd11062 224 RLAdeaqtLIGAgteTTARTLSVAT---FHLLSNPEILERLREELKTAMPDPDSPPSL---------AELEKLPYLTAVI 291
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  351 KEALRLSSA--SLNIRTAKEDFtlhLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKakttfysngN 428
Cdd:cd11062 292 KEGLRLSYGvpTRLPRVVPDEG---LYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEK---------G 359
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 7549754  429 KLKCFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVE 471
Cdd:cd11062 360 KLDRYLVPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYE 402
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
296-473 9.77e-12

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: 66.85  E-value: 9.77e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALQSagqelSSGGSAIYLDQVQLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTlhL 374
Cdd:cd11064 252 WFFWLLSKNPRVEEKIREELKSKLPK-----LTTDESRVPTYEELKKLVYLHAALSESLRLyPPVPFDSKEAVNDDV--L 324
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 EDGSYnIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYLDESGKAKttfYSNGNKlkcfYMPFGSGATICPGRLFAVQE 453
Cdd:cd11064 325 PDGTF-VKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDGGLR---PESPYK----FPAFNAGPRICLGKDLAYLQ 396
                       170       180
                ....*....|....*....|
gi 7549754  454 IKQFLILMLSCFELEFVESQ 473
Cdd:cd11064 397 MKIVAAAILRRFDFKVVPGH 416
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
296-446 1.10e-11

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: 66.68  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALqsagqelssgGSAIYLDQVQLNDLPVLDSIIKEALRL-SSASLNI-RTAKEdftlH 373
Cdd:cd20657 250 WALAELIRHPDILKKAQEEMDQVI----------GRDRRLLESDIPNLPYLQAICKETFRLhPSTPLNLpRIASE----A 315
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7549754  374 LEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLdESGKAKTTFYSNGNKLkcfyMPFGSGATICPG 446
Cdd:cd20657 316 CEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFL-PGRNAKVDVRGNDFEL----IPFGAGRRICAG 383
PLN02687 PLN02687
flavonoid 3'-monooxygenase
296-446 4.05e-11

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 65.22  E-value: 4.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   296 WSLFQMIRSPEAMKAASEEVSGALqsagqelssgGSAIYLDQVQLNDLPVLDSIIKEALRL-SSASLNI-RTAKEDftlh 373
Cdd:PLN02687 319 WAIAELIRHPDILKKAQEELDAVV----------GRDRLVSESDLPQLTYLQAVIKETFRLhPSTPLSLpRMAAEE---- 384
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7549754   374 LEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLdeSGKAKTTFYSNGNKLKcfYMPFGSGATICPG 446
Cdd:PLN02687 385 CEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFL--PGGEHAGVDVKGSDFE--LIPFGAGRRICAG 453
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
296-474 4.44e-11

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: 64.58  E-value: 4.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEE---VSGALQSAGQELSSGGSAIyldqvqLNDLPVLDSIIKEALRLSSASLNIRTAKEDFTL 372
Cdd:cd11051 207 WAFYLLSKHPEVLAKVRAEhdeVFGPDPSAAAELLREGPEL------LNQLPYTTAVIKETLRLFPPAGTARRGPPGVGL 280
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  373 HLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKtTFYSNGnklkcfYMPFGSGATICPGRLFAVQ 452
Cdd:cd11051 281 TDRDGKEYPTDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHEL-YPPKSA------WRPFERGPRNCIGQELAML 353
                       170       180
                ....*....|....*....|..
gi 7549754  453 EIKQFLILMLSCFELEFVESQV 474
Cdd:cd11051 354 ELKIILAMTVRRFDFEKAYDEW 375
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
289-468 8.83e-11

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: 64.00  E-value: 8.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  289 NTIPATF-WSLFQMIRSPEAMKAASEEVSGALQSagqelssGGSAIYLDqvqLNDLPVLDSIIKEALRLSSA-SLNIRT- 365
Cdd:cd20648 248 DTISSTLsWSLYELSRHPDVQTALHREITAALKD-------NSVPSAAD---VARMPLLKAVVKEVLRLYPViPGNARVi 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  366 AKEDftlhLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDEsGKAKTTFYSngnklkcfyMPFGSGATICP 445
Cdd:cd20648 318 PDRD----IQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGK-GDTHHPYAS---------LPFGFGKRSCI 383
                       170       180
                ....*....|....*....|...
gi 7549754  446 GRLFAVQEIKQFLILMLSCFELE 468
Cdd:cd20648 384 GRRIAELEVYLALARILTHFEVR 406
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
288-468 8.90e-11

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: 63.89  E-value: 8.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  288 ANTIPATFWSLfqmIRSPEAMKAASEEVSGALQSAGQElssggsaiYLDQVQLNDLPVLDSIIKEALRLSS--ASLNIRT 365
Cdd:cd11070 240 ANTLSFALYLL---AKHPEVQDWLREEIDSVLGDEPDD--------WDYEEDFPKLPYLLAVIYETLRLYPpvQLLNRKT 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  366 AKEDFTLHLEDGSYNIRKDdMIALYPQL-MHLDPEIY-PDPLTFKYDRYLDESGKAKTTFYSNGNKlkCFYMPFGSGATI 443
Cdd:cd11070 309 TEPVVVITGLGQEIVIPKG-TYVGYNAYaTHRDPTIWgPDADEFDPERWGSTSGEIGAATRFTPAR--GAFIPFSAGPRA 385
                       170       180
                ....*....|....*....|....*
gi 7549754  444 CPGRLFAVQEIKQFLILMLSCFELE 468
Cdd:cd11070 386 CLGRKFALVEFVAALAELFRQYEWR 410
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
222-467 1.62e-10

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: 63.13  E-value: 1.62e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  222 GLPIHLFKTAHKAREklAEGLKHKnlcVRDQVSELIRLRM--------------FL-----------NDTLSTFDD-MEK 275
Cdd:cd11052 162 GIPGSRFLPTKGNKK--IKKLDKE---IEDSLLEIIKKREdslkmgrgddygddLLgllleanqsddQNKNMTVQEiVDE 236
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  276 AKThlaILWASQANTIPATFWSLFQMIRSPEAMKAASEEVsgaLQSAGQELssggsaiyLDQVQLNDLPVLDSIIKEALR 355
Cdd:cd11052 237 CKT---FFFAGHETTALLLTWTTMLLAIHPEWQEKAREEV---LEVCGKDK--------PPSDSLSKLKTVSMVINESLR 302
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  356 L-SSASLNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYLDesGKAKTTFYSNGnklkcf 433
Cdd:cd11052 303 LyPPAVFLTRKAKEDIKL----GGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFAD--GVAKAAKHPMA------ 370
                       250       260       270
                ....*....|....*....|....*....|....
gi 7549754  434 YMPFGSGATICPGRLFAVQEIKQFLILMLSCFEL 467
Cdd:cd11052 371 FLPFGLGPRNCIGQNFATMEAKIVLAMILQRFSF 404
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
278-466 2.61e-10

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: 62.50  E-value: 2.61e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  278 THLAILW----ASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALqsagqelssgGSAIYLDQVQLNDLPVLDSIIKEA 353
Cdd:cd20656 230 TVIGLLWdmitAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVV----------GSDRVMTEADFPQLPYLQCVVKEA 299
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  354 LRLSSASLNIRTAKEDFTLHLedGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSngnklkcf 433
Cdd:cd20656 300 LRLHPPTPLMLPHKASENVKI--GGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKGHDFR-------- 369
                       170       180       190
                ....*....|....*....|....*....|...
gi 7549754  434 YMPFGSGATICPGRLFAVQEIKQFLILMLSCFE 466
Cdd:cd20656 370 LLPFGAGRRVCPGAQLGINLVTLMLGHLLHHFS 402
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
195-486 2.70e-10

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: 62.43  E-value: 2.70e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  195 TDTQKALILNNLDNFKQFDQVFPAL---VAGLPIHLF---------KTAHKAREK-LAEGLKHK----NLCVRDQVSELI 257
Cdd:cd20650 139 ENTKKLLKFDFLDPLFLSITVFPFLtpiLEKLNISVFpkdvtnffyKSVKKIKESrLDSTQKHRvdflQLMIDSQNSKET 218
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  258 rlrmflnDTLSTFDDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGqelssggSAIYLDQ 337
Cdd:cd20650 219 -------ESHKALSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKA-------PPTYDTV 284
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  338 VQLNdlpVLDSIIKEALRLSSASLNI-RTAKEDFTLhleDGSYnIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYldeS 416
Cdd:cd20650 285 MQME---YLDMVVNETLRLFPIAGRLeRVCKKDVEI---NGVF-IPKGTVVMIPTYALHRDPQYWPEPEEFRPERF---S 354
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7549754  417 GKAKttfysnGNKLKCFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFV-ESQVkcpPLDQSRAGL 486
Cdd:cd20650 355 KKNK------DNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPCkETQI---PLKLSLQGL 416
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
339-479 3.21e-10

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: 62.08  E-value: 3.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  339 QLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYldES 416
Cdd:cd20639 287 HLPKLKTLGMILNETLRLyPPAVATIRRAKKDVKL----GGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARF--AD 360
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7549754  417 GKAKTTFYSNGnklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQVKCPPL 479
Cdd:cd20639 361 GVARAAKHPLA------FIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRLSPSYAHAPTV 417
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
260-468 6.03e-10

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: 61.27  E-value: 6.03e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  260 RMFLNDTLStFDDMEKAKTHLAilwASQANTIPATF-WSLFQMIRSPEAMKAASEEVSGALQSAGQELSSggsaiyldqv 338
Cdd:cd20643 223 NLLLQDKLP-IEDIKASVTELM---AGGVDTTSMTLqWTLYELARNPNVQEMLRAEVLAARQEAQGDMVK---------- 288
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  339 QLNDLPVLDSIIKEALRLSSASLNI-RTAKEDFTLHledgSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLdesg 417
Cdd:cd20643 289 MLKSVPLLKAAIKETLRLHPVAVSLqRYITEDLVLQ----NYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWL---- 360
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 7549754  418 KAKTTFYSNgnklkcfyMPFGSGATICPGRLFAVQEIKQFLILMLSCFELE 468
Cdd:cd20643 361 SKDITHFRN--------LGFGFGPRQCLGRRIAETEMQLFLIHMLENFKIE 403
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
291-483 7.44e-10

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: 60.95  E-value: 7.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  291 IPATFWS----LFQMIRSPEAMKAASEEVSGALqsagqelssgGSAIYLDQVQLNDLPVLDSIIKEALRLSSA------S 360
Cdd:cd11074 246 IETTLWSiewgIAELVNHPEIQKKLRDELDTVL----------GPGVQITEPDLHKLPYLQAVVKETLRLRMAipllvpH 315
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  361 LNIRTAKEdftlhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKttfySNGNKLKcfYMPFGSG 440
Cdd:cd11074 316 MNLHDAKL--------GGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKVE----ANGNDFR--YLPFGVG 381
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 7549754  441 ATICPGRLFAVQEIKQFLILMLSCFELefvesqvkCPPLDQSR 483
Cdd:cd11074 382 RRSCPGIILALPILGITIGRLVQNFEL--------LPPPGQSK 416
PLN02648 PLN02648
allene oxide synthase
313-427 1.26e-09

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 60.33  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   313 EEVSGALQSAGQELSSGGsaiyldqvqLNDLPVLDSIIKEALRLS-SASLNIRTAKEDFTLHLEDGSYNIRKDDMIALYP 391
Cdd:PLN02648 312 EEVRSAVKAGGGGVTFAA---------LEKMPLVKSVVYEALRIEpPVPFQYGRAREDFVIESHDAAFEIKKGEMLFGYQ 382
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 7549754   392 QLMHLDPEIYPDPLTFKYDRYLDESGKA--KTTFYSNG 427
Cdd:PLN02648 383 PLVTRDPKVFDRPEEFVPDRFMGEEGEKllKYVFWSNG 420
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
288-471 1.27e-09

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: 60.29  E-value: 1.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  288 ANTIPATFWSLfqmIRSPEAMKAASEEvsgaLQSAGQELSSGgSAIYLDQVQlnDLPVLDSIIKEALRLSSASLNI--RT 365
Cdd:cd11060 239 AIALRAILYYL---LKNPRVYAKLRAE----IDAAVAEGKLS-SPITFAEAQ--KLPYLQAVIKEALRLHPPVGLPleRV 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  366 A-KEDFTLHledGSYnIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYLDESGKAKTtfysngnKLKCFYMPFGSGATI 443
Cdd:cd11060 309 VpPGGATIC---GRF-IPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWLEADEEQRR-------MMDRADLTFGAGSRT 377
                       170       180
                ....*....|....*....|....*...
gi 7549754  444 CPGRLFAVQEIKQFLILMLSCFELEFVE 471
Cdd:cd11060 378 CLGKNIALLELYKVIPELLRRFDFELVD 405
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
264-477 1.54e-09

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: 59.99  E-value: 1.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  264 NDTLSTFDDMEKAKthlAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVsgaLQSAGQELSsggsaiylDQVQLNDL 343
Cdd:cd20642 227 NGGMSTEDVIEECK---LFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEV---LQVFGNNKP--------DFEGLNHL 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  344 PVLDSIIKEALRLSSASLN-IRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYLDesGKAKT 421
Cdd:cd20642 293 KVVTMILYEVLRLYPPVIQlTRAIHKDTKL----GDLTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERFAE--GISKA 366
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7549754  422 TfysngnKLKCFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQVKCP 477
Cdd:cd20642 367 T------KGQVSYFPFGWGPRICIGQNFALLEAKMALALILQRFSFELSPSYVHAP 416
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
289-495 2.26e-09

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: 59.40  E-value: 2.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  289 NTIpatFWSLFQMIRSPEAMKAASEEVSGALqsAGQELSSggsaiYLDQVQLndlPVLDSIIKEALRLSS-ASLNI-RTA 366
Cdd:cd20666 246 NTL---LWCLLYMSLYPEVQEKVQAEIDTVI--GPDRAPS-----LTDKAQM---PFTEATIMEVQRMTVvVPLSIpHMA 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  367 KEDFTLHledgSYNIRKDDMIalYPQL--MHLDPEIYPDPLTFKYDRYLDESGKAKTtfysngnklKCFYMPFGSGATIC 444
Cdd:cd20666 313 SENTVLQ----GYTIPKGTVI--VPNLwsVHRDPAIWEKPDDFMPSRFLDENGQLIK---------KEAFIPFGIGRRVC 377
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 7549754  445 PGRLFAVQEIKQFLILMLSCFELEFVESQVKcpPLDQSRAGLGILPPLHDI 495
Cdd:cd20666 378 MGEQLAKMELFLMFVSLMQSFTFLLPPNAPK--PSMEGRFGLTLAPCPFNI 426
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
296-492 3.24e-09

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: 58.96  E-value: 3.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSgalqsagQELSSGGSAIYLDQVQLndlPVLDSIIKEALRLSS-ASLNI--RTakedfTL 372
Cdd:cd20674 248 WAVAFLLHHPEIQDRLQEELD-------RVLGPGASPSYKDRARL---PLLNATIAEVLRLRPvVPLALphRT-----TR 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  373 HLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTfysngnklkcfyMPFGSGATICPGRLFAVQ 452
Cdd:cd20674 313 DSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAANRAL------------LPFGCGARVCLGEPLARL 380
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 7549754  453 EIKQFLILMLSCFELEfvesqvkcPPLDqsraglGILPPL 492
Cdd:cd20674 381 ELFVFLARLLQAFTLL--------PPSD------GALPSL 406
PLN02971 PLN02971
tryptophan N-hydroxylase
250-482 3.35e-09

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 59.28  E-value: 3.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   250 RDQVSELIRLRMFLNDT----LSTFDDMEKAKTHLAIlwASQANTIPATFWSLFQMIRSPEAMKAASEEVSgalQSAGQE 325
Cdd:PLN02971 301 RTQIEDFLDIFISIKDEagqpLLTADEIKPTIKELVM--AAPDNPSNAVEWAMAEMINKPEILHKAMEEID---RVVGKE 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   326 lssggsaiylDQVQLNDLPVLD---SIIKEALRLSS-ASLNI-RTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEI 400
Cdd:PLN02971 376 ----------RFVQESDIPKLNyvkAIIREAFRLHPvAAFNLpHVALSDTTV----AGYHIPKGSQVLLSRYGLGRNPKV 441
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   401 YPDPLTFKYDRYLDESGKAKTTfysnGNKLKcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQVKCPPLD 480
Cdd:PLN02971 442 WSDPLSFKPERHLNECSEVTLT----ENDLR--FISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSETRVELME 515

                 ..
gi 7549754   481 QS 482
Cdd:PLN02971 516 SS 517
PLN02655 PLN02655
ent-kaurene oxidase
184-451 4.04e-09

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 58.60  E-value: 4.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   184 YLTLFGRDISKTDTQKALILNNLDNFKQFD--QVFPALvAGLPIHLFK----TAHKAREKLAEGLkhknlcVRDQVSELI 257
Cdd:PLN02655 167 YVEELGTEISKEEIFDVLVHDMMMCAIEVDwrDFFPYL-SWIPNKSFEtrvqTTEFRRTAVMKAL------IKQQKKRIA 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   258 RLRmflnDTLSTFDDMEKAKTHLA------ILW----ASQANTIPATFWSLFQMIRSPEAMKAASEEVSGAlqsagqels 327
Cdd:PLN02655 240 RGE----ERDCYLDFLLSEATHLTdeqlmmLVWepiiEAADTTLVTTEWAMYELAKNPDKQERLYREIREV--------- 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   328 SGGSAIYLDQvqLNDLPVLDSIIKEALRLSSAS--LNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPL 405
Cdd:PLN02655 307 CGDERVTEED--LPNLPYLNAVFHETLRKYSPVplLPPRFVHEDTTL----GGYDIPAGTQIAINIYGCNMDKKRWENPE 380
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 7549754   406 TFKYDRYLDESGKAKTTFysngnKLkcfyMPFGSGATICPGRLFAV 451
Cdd:PLN02655 381 EWDPERFLGEKYESADMY-----KT----MAFGAGKRVCAGSLQAM 417
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
291-467 4.42e-09

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 58.59  E-value: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   291 IPATFWS----LFQMIRSPEAMKAASEEVSGALQSAGQelssggsaiyLDQVQLNDLPVLDSIIKEALRLSSA------S 360
Cdd:PLN02394 306 IETTLWSiewgIAELVNHPEIQKKLRDELDTVLGPGNQ----------VTEPDTHKLPYLQAVVKETLRLHMAipllvpH 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   361 LNIRTAKEdftlhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKttfySNGNKLKcfYMPFGSG 440
Cdd:PLN02394 376 MNLEDAKL--------GGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAKVE----ANGNDFR--FLPFGVG 441
                        170       180
                 ....*....|....*....|....*..
gi 7549754   441 ATICPGRLFAVQEIKQFLILMLSCFEL 467
Cdd:PLN02394 442 RRSCPGIILALPILGIVLGRLVQNFEL 468
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
54-467 7.79e-09

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: 57.55  E-value: 7.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   54 EFLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLC---HGKYFDWKKfhytTSAKAFGHRSIDPNDGNTTENINNTFT 130
Cdd:cd20637  12 GFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILMgehSLVSTEWPR----STRMLLGPNSLVNSIGDIHRHKRKVFS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  131 KTLQGDALCSLSEAMMQNLQSVMRppglpksksnAWVTE----GMYAFCYRVMFEAGYLTLFGRDISKTDtqkaliLNNL 206
Cdd:cd20637  88 KLFSHEALESYLPKIQQVIQDTLR----------VWSSNpepiNVYQEAQKLTFRMAIRVLLGFRVSEEE------LSHL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  207 -DNFKQF-DQVFpALVAGLPIHLFKTAHKAREKLAEGL----KHKNLCVRDQvselirlrmflnDTLSTFDDM-EKAKTH 279
Cdd:cd20637 152 fSVFQQFvENVF-SLPLDLPFSGYRRGIRARDSLQKSLekaiREKLQGTQGK------------DYADALDILiESAKEH 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  280 -------------LAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGalQSAGQELSSGGSAIYLDqvQLNDLPVL 346
Cdd:cd20637 219 gkeltmqelkdstIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELRS--NGILHNGCLCEGTLRLD--TISSLKYL 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  347 DSIIKEALRL-SSASLNIRTAKEDFTLhleDGsYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYS 425
Cdd:cd20637 295 DCVIKEVLRLfTPVSGGYRTALQTFEL---DG-FQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSEDKDGRFH 370
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....
gi 7549754  426 ngnklkcfYMPFGSGATICPGRLFAVQEIKQFLILM--LSCFEL 467
Cdd:cd20637 371 --------YLPFGGGVRTCLGKQLAKLFLKVLAVELasTSRFEL 406
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
296-466 8.20e-09

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 57.94  E-value: 8.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   296 WSLFQMIRSPEAMKAASEEVSGALqsagqelssgGSAIYLDQVQLNDLPVLDSIIKEALRL-SSASLNI-RTAKEdftlH 373
Cdd:PLN00110 311 WSLAEMLKNPSILKRAHEEMDQVI----------GRNRRLVESDLPKLPYLQAICKESFRKhPSTPLNLpRVSTQ----A 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   374 LEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESgKAKTTFYSNGNKLkcfyMPFGSGATICPGRLFAVQE 453
Cdd:PLN00110 377 CEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEK-NAKIDPRGNDFEL----IPFGAGRRICAGTRMGIVL 451
                        170
                 ....*....|...
gi 7549754   454 IKQFLILMLSCFE 466
Cdd:PLN00110 452 VEYILGTLVHSFD 464
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
288-467 9.35e-09

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: 57.61  E-value: 9.35e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  288 ANTIpatFWSLFQMIRSPEAMKAASEEVSgalqsagQELSSGGSAIYLDQvqLNDLPVLDSIIKEALRL-SSASLNIRTA 366
Cdd:cd11057 244 ATTV---AYTLLLLAMHPEVQEKVYEEIM-------EVFPDDGQFITYED--LQQLVYLEMVLKETMRLfPVGPLVGRET 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  367 KEDFTLhleDGSYNIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYLDESgKAKTTFYSngnklkcfYMPFGSGATICP 445
Cdd:cd11057 312 TADIQL---SNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPER-SAQRHPYA--------FIPFSAGPRNCI 379
                       170       180
                ....*....|....*....|..
gi 7549754  446 GRLFAVQEIKQFLILMLSCFEL 467
Cdd:cd11057 380 GWRYAMISMKIMLAKILRNYRL 401
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
296-495 1.61e-08

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: 56.80  E-value: 1.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSgalqsagQELSSGGSAIYLDQVQLndlPVLDSIIKEALRLSS-ASLNI-RTAKEDFTLH 373
Cdd:cd11026 248 WALLLLMKYPHIQEKVQEEID-------RVIGRNRTPSLEDRAKM---PYTDAVIHEVQRFGDiVPLGVpHAVTRDTKFR 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  374 ledgSYNIRKDDMIalYPQL--MHLDPEIYPDPLTFKYDRYLDESGKakttFYSNgnklKCFyMPFGSGATICPGRLFAV 451
Cdd:cd11026 318 ----GYTIPKGTTV--IPNLtsVLRDPKQWETPEEFNPGHFLDEQGK----FKKN----EAF-MPFSAGKRVCLGEGLAR 382
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 7549754  452 QEIKQFLILMLSCFELEFVESQVKcPPLDQSRAGLGILPPLHDI 495
Cdd:cd11026 383 MELFLFFTSLLQRFSLSSPVGPKD-PDLTPRFSGFTNSPRPYQL 425
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
289-467 2.03e-08

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: 56.21  E-value: 2.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  289 NTIPatfWSLFQMIRSPEAMKAASEEVSGALqSAGQELSSGgsaiyldqvQLNDLPVLDSIIKEALRL-SSASLNIRTAK 367
Cdd:cd20646 251 NTLS---WALYHLARDPEIQERLYQEVISVC-PGDRIPTAE---------DIAKMPLLKAVIKETLRLyPVVPGNARVIV 317
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  368 EDftlHLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSngnklkcfyMPFGSGATICPGR 447
Cdd:cd20646 318 EK---EVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKHHPFGS---------IPFGYGVRACVGR 385
                       170       180
                ....*....|....*....|
gi 7549754  448 LFAVQEIKQFLILMLSCFEL 467
Cdd:cd20646 386 RIAELEMYLALSRLIKRFEV 405
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
214-481 3.35e-08

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: 55.79  E-value: 3.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  214 QVFPalvaGLPIHLFKTAHKAREKLAEG--LKHK-NLC---VRDQVSELIRLRMFL--NDTLSTFDDMEKAKTHLA---- 281
Cdd:cd20673 163 QIFP----NKDLEKLKQCVKIRDKLLQKklEEHKeKFSsdsIRDLLDALLQAKMNAenNNAGPDQDSVGLSDDHILmtvg 238
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  282 -ILWASQANTIPATFWSLFQMIRSPEAMKAASEEvsgalqsagqelssggsaiyLDQV-------QLND---LPVLDSII 350
Cdd:cd20673 239 dIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEE--------------------IDQNigfsrtpTLSDrnhLPLLEATI 298
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  351 KEALRLSSAS--LNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSNgn 428
Cdd:cd20673 299 REVLRIRPVAplLIPHVALQDSSI----GEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQLISPSLS-- 372
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 7549754  429 klkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEfvesqvkCPPLDQ 481
Cdd:cd20673 373 -----YLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLE-------VPDGGQ 413
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
264-471 4.00e-08

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: 55.62  E-value: 4.00e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  264 NDTLSTFDDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGqelssggSAIYLDQvqlNDL 343
Cdd:cd20667 215 DDPVSTFSEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQ-------LICYEDR---KRL 284
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  344 PVLDSIIKEALRLSS-ASLNI-RTAKEDFTLHledgSYNIRKDDMIalYPQLMHL--DPEIYPDPLTFKYDRYLDESGka 419
Cdd:cd20667 285 PYTNAVIHEVQRLSNvVSVGAvRQCVTSTTMH----GYYVEKGTII--LPNLASVlyDPECWETPHKFNPGHFLDKDG-- 356
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 7549754  420 ktTFYSNGNklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVE 471
Cdd:cd20667 357 --NFVMNEA-----FLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQLPE 401
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
296-447 4.40e-08

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: 55.41  E-value: 4.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALqsagqelssGGSAIYLDQvQLNDLPVLDSIIKEALR-------LSSASLNIrtakE 368
Cdd:cd11076 246 WIMARMVLHPDIQSKAQAEIDAAV---------GGSRRVADS-DVAKLPYLQAVVKETLRlhppgplLSWARLAI----H 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  369 DFTLhledGSYNIRKD-----DMIALypqlMHlDPEIYPDPLTFKYDRYLDESGKAKttFYSNGNKLKcfYMPFGSGATI 443
Cdd:cd11076 312 DVTV----GGHVVPAGttamvNMWAI----TH-DPHVWEDPLEFKPERFVAAEGGAD--VSVLGSDLR--LAPFGAGRRV 378

                ....
gi 7549754  444 CPGR 447
Cdd:cd11076 379 CPGK 382
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
256-466 4.86e-08

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: 55.07  E-value: 4.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  256 LIRLRMFLNDTLSTFDDMEKAKTHLAIlwASQANTIPATFWSLFQMIRSPEAMKAASEEVSgalQSAGQElssggsaiyl 335
Cdd:cd20658 221 FITLKDENGNPLLTPDEIKAQIKELMI--AAIDNPSNAVEWALAEMLNQPEILRKATEELD---RVVGKE---------- 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  336 DQVQLNDLPVLD---SIIKEALRL-SSASLNI-RTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYD 410
Cdd:cd20658 286 RLVQESDIPNLNyvkACAREAFRLhPVAPFNVpHVAMSDTTV----GGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPE 361
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 7549754  411 RYLDESGKAKTTfysnGNKLKcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFE 466
Cdd:cd20658 362 RHLNEDSEVTLT----EPDLR--FISFSTGRRGCPGVKLGTAMTVMLLARLLQGFT 411
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
270-461 5.41e-08

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: 54.95  E-value: 5.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  270 FDDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVsgalqsagQELSSGGSA-IYLDQvqLNDLPVLDS 348
Cdd:cd11082 216 SSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQ--------ARLRPNDEPpLTLDL--LEEMKYTRQ 285
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  349 IIKEALRLSSASLNI-RTAKEDFTLhleDGSYNIRKDDMIA--LYPQLMhlDPeiYPDPLTFKYDRYlDESGKAKTTFYS 425
Cdd:cd11082 286 VVKEVLRYRPPAPMVpHIAKKDFPL---TEDYTVPKGTIVIpsIYDSCF--QG--FPEPDKFDPDRF-SPERQEDRKYKK 357
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 7549754  426 NgnklkcfYMPFGSGATICPGRLFAVQEIKQFLILM 461
Cdd:cd11082 358 N-------FLVFGAGPHQCVGQEYAINHLMLFLALF 386
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
296-467 6.50e-08

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: 54.70  E-value: 6.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVsgalqsagQELSSGGSAIYLDQVQLNDLPVLDSIIKEALRLSSASLNI-RTAKEDFTLhl 374
Cdd:cd20679 266 WILYNLARHPEYQERCRQEV--------QELLKDREPEEIEWDDLAQLPFLTMCIKESLRLHPPVTAIsRCCTQDIVL-- 335
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 EDGSYnIRKDD--MIALYPqlMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQ 452
Cdd:cd20679 336 PDGRV-IPKGIicLISIYG--THHNPTVWPDPEVYDPFRFDPENSQGRSPLA---------FIPFSAGPRNCIGQTFAMA 403
                       170
                ....*....|....*
gi 7549754  453 EIKQFLILMLSCFEL 467
Cdd:cd20679 404 EMKVVLALTLLRFRV 418
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
290-462 7.68e-08

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: 54.61  E-value: 7.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  290 TIPATF-WSLFQMIRSPEAMKAASEEvsgalqsagqelssggsaiyLDQV-------QLND---LPVLDSIIKEALRLSS 358
Cdd:cd11028 246 TISTTLqWSLLYMIRYPEIQEKVQAE--------------------LDRVigrerlpRLSDrpnLPYTEAFILETMRHSS 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  359 -ASLNI-RTAKEDFTLhledGSYNIRKDDM--IALYpQLMHlDPEIYPDPLTFKYDRYLDESGKAKTTFYSNgnklkcfY 434
Cdd:cd11028 306 fVPFTIpHATTRDTTL----NGYFIPKGTVvfVNLW-SVNH-DEKLWPDPSVFRPERFLDDNGLLDKTKVDK-------F 372
                       170       180
                ....*....|....*....|....*...
gi 7549754  435 MPFGSGATICPGRLFAVQEIKQFLILML 462
Cdd:cd11028 373 LPFGAGRRRCLGEELARMELFLFFATLL 400
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
342-487 9.61e-08

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: 54.46  E-value: 9.61e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  342 DLPVLDSIIKEALRLSSASLNI-RTAKEDFTLHledgSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAK 420
Cdd:cd20649 319 ELPYLDMVIAETLRMYPPAFRFaREAAEDCVVL----GQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRR 394
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7549754  421 TTFysngnklkcFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFV-ESQVkcpPLD-QSRAGLG 487
Cdd:cd20649 395 HPF---------VYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACpETEI---PLQlKSKSTLG 451
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
296-468 1.01e-07

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: 54.15  E-value: 1.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVsgaLQSAGQELSSGGSAIyldqvqlNDLPVLDSIIKEALRLSSA-SLNIRTAKEDFTLhl 374
Cdd:cd20647 259 WATYLLARHPEVQQQVYEEI---VRNLGKRVVPTAEDV-------PKLPLIRALLKETLRLFPVlPGNGRVTQDDLIV-- 326
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 edGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSNgnklkcfyMPFGSGATICPGRLFAVQEI 454
Cdd:cd20647 327 --GGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRVDNFGS--------IPFGYGIRSCIGRRIAELEI 396
                       170
                ....*....|....
gi 7549754  455 KQFLILMLSCFELE 468
Cdd:cd20647 397 HLALIQLLQNFEIK 410
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
336-458 1.69e-07

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: 53.36  E-value: 1.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  336 DQVQLNDLPVL-DSIIKEALRLSSASLNIRTAKEDFTLHledGSyNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRyld 414
Cdd:cd11035 223 DRRRLREDPELiPAAVEELLRRYPLVNVARIVTRDVEFH---GV-QLKAGDMVLLPLALANRDPREFPDPDTVDFDR--- 295
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 7549754  415 esgKAKTtfysngnklkcfYMPFGSGATICPGRLFAVQEIKQFL 458
Cdd:cd11035 296 ---KPNR------------HLAFGAGPHRCLGSHLARLELRIAL 324
PLN02774 PLN02774
brassinosteroid-6-oxidase
336-458 1.89e-07

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 53.24  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   336 DQVQLNDLPVLD---SIIKEALRLSSA--SLNIRTAKEdftlhLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYD 410
Cdd:PLN02774 316 DPIDWNDYKSMRftrAVIFETSRLATIvnGVLRKTTQD-----MELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPW 390
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 7549754   411 RYLDESGKAKTTFysngnklkcfyMPFGSGATICPGRLFAVQEIKQFL 458
Cdd:PLN02774 391 RWLDKSLESHNYF-----------FLFGGGTRLCPGKELGIVEISTFL 427
PLN02936 PLN02936
epsilon-ring hydroxylase
247-473 2.01e-07

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 53.26  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   247 LCVRDQVSElIRLRmflndtlstfDDMekakthLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQsagqel 326
Cdd:PLN02936 268 LASREEVSS-VQLR----------DDL------LSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ------ 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   327 ssGGSAIYLDqvqLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhleDGSYNIRK--DDMIALYPqlMHLDPEIYPD 403
Cdd:PLN02936 325 --GRPPTYED---IKELKYLTRCINESMRLyPHPPVLIRRAQVEDVL---PGGYKVNAgqDIMISVYN--IHRSPEVWER 394
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7549754   404 PLTFKYDRYLDESG---KAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQ 473
Cdd:PLN02936 395 AEEFVPERFDLDGPvpnETNTDFR---------YIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLELVPDQ 458
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
274-463 2.19e-07

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: 53.30  E-value: 2.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  274 EKAKTHLAILWASQANTIPATFWSLFQMIRSPEAM-KAASEEVSGALQSAGQELSSggsAIYLDQvqLNDLPVLDSIIKE 352
Cdd:cd20636 227 ELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIeKIRQELVSHGLIDQCQCCPG---ALSLEK--LSRLRYLDCVVKE 301
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  353 ALR-LSSASLNIRTAKEDFTLhleDGsYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSngnklk 431
Cdd:cd20636 302 VLRlLPPVSGGYRTALQTFEL---DG-YQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGRFN------ 371
                       170       180       190
                ....*....|....*....|....*....|..
gi 7549754  432 cfYMPFGSGATICPGRLFAvQEIKQFLILMLS 463
Cdd:cd20636 372 --YIPFGGGVRSCIGKELA-QVILKTLAVELV 400
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
223-465 3.62e-07

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 52.67  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   223 LPIHLFKTAH----KAREKLAEGLkhkNLCVRDQVSELIRLRMFLNDTLST-------FDDMEKAKTHLAILWASQANTI 291
Cdd:PLN02987 208 VPLPLFSTTYrraiQARTKVAEAL---TLVVMKRRKEEEEGAEKKKDMLAAllasddgFSDEEIVDFLVALLVAGYETTS 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   292 PATFWSLFQMIRSPEAMKAASEEVSGALQSAGQELSsggsaiyLDQVQLNDLPVLDSIIKEALRLSSASLNI-RTAKEDf 370
Cdd:PLN02987 285 TIMTLAVKFLTETPLALAQLKEEHEKIRAMKSDSYS-------LEWSDYKSMPFTQCVVNETLRVANIIGGIfRRAMTD- 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   371 tlhLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGkakTTFYSNgnklkcFYMPFGSGATICPGRLFA 450
Cdd:PLN02987 357 ---IEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSG---TTVPSN------VFTPFGGGPRLCPGYELA 424
                        250
                 ....*....|....*
gi 7549754   451 VQEIKQFLILMLSCF 465
Cdd:PLN02987 425 RVALSVFLHRLVTRF 439
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
296-467 4.18e-07

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: 52.28  E-value: 4.18e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  296 WSLFQMIRSPEAMKAASEEVSGALQsagqelssGGSAIYLDQvqLNDLPVLDSIIKEALRLSSASLNI-RTAKEDFTLHl 374
Cdd:cd20678 261 WILYCLALHPEHQQRCREEIREILG--------DGDSITWEH--LDQMPYTTMCIKEALRLYPPVPGIsRELSKPVTFP- 329
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  375 eDGSyNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKakttfysngNKLKCFYMPFGSGATICPGRLFAVQEI 454
Cdd:cd20678 330 -DGR-SLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSS---------KRHSHAFLPFSAGPRNCIGQQFAMNEM 398
                       170
                ....*....|...
gi 7549754  455 KQFLILMLSCFEL 467
Cdd:cd20678 399 KVAVALTLLRFEL 411
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
296-446 6.70e-07

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 51.62  E-value: 6.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   296 WSLFQMIRSPEAMKAASEEVSGALQSAGqelssggsaiYLDQVQLNDLPVLDSIIKEALRLSSAsLNIRTAKEDFTlHLE 375
Cdd:PLN03234 310 WAMTYLIKYPEAMKKAQDEVRNVIGDKG----------YVSEEDIPNLPYLKAVIKESLRLEPV-IPILLHRETIA-DAK 377
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7549754   376 DGSYNIRKDDMIALYPQLMHLDPEIYPD-PLTFKYDRYLDEsgKAKTTFYSNGNKLkcfyMPFGSGATICPG 446
Cdd:PLN03234 378 IGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERFMKE--HKGVDFKGQDFEL----LPFGSGRRMCPA 443
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
288-468 1.91e-06

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: 50.01  E-value: 1.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  288 ANTIPATF-WSLFQMirSPEAMKAASEEVSGALQSAgqelSSGGSAIYLDQVQLNDLPVLDSIIKEALRLSSAS-LNI-R 364
Cdd:cd11066 241 LDTVPLNLnHLIGHL--SHPPGQEIQEKAYEEILEA----YGNDEDAWEDCAAEEKCPYVVALVKETLRYFTVLpLGLpR 314
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  365 TAKEDFTLhleDGSYnIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGkakttfysnGNKLKCFYMPFGSGATIC 444
Cdd:cd11066 315 KTTKDIVY---NGAV-IPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASG---------DLIPGPPHFSFGAGSRMC 381
                       170       180
                ....*....|....*....|....
gi 7549754  445 PGRLFAVQEIKQFLILMLSCFELE 468
Cdd:cd11066 382 AGSHLANRELYTAICRLILLFRIG 405
PTZ00404 PTZ00404
cytochrome P450; Provisional
296-454 2.00e-06

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 50.11  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   296 WSLFQMIRSPEAMKAASEEVSGALQSAgqelssggsaiylDQVQLND---LPVLDSIIKEALRLSSASLN--IRTAKEDF 370
Cdd:PTZ00404 305 WMVLMLCNYPEIQEKAYNEIKSTVNGR-------------NKVLLSDrqsTPYTVAIIKETLRYKPVSPFglPRSTSNDI 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   371 TLhleDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLdesgkakttfysnGNKLKCFYMPFGSGATICPGRLFA 450
Cdd:PTZ00404 372 II---GGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFL-------------NPDSNDAFMPFSIGPRNCVGQQFA 435

                 ....
gi 7549754   451 VQEI 454
Cdd:PTZ00404 436 QDEL 439
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
352-463 2.07e-06

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 50.03  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  352 EALRLSSAS-LNIRTAKEDFTLHLEDGS-YNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDEsgkakttfysngnk 429
Cdd:cd20612 246 EALRLNPIApGLYRRATTDTTVADGGGRtVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDRPLES-------------- 311
                        90       100       110
                ....*....|....*....|....*....|....
gi 7549754  430 lkcfYMPFGSGATICPGRLFAVQEIKQFLILMLS 463
Cdd:cd20612 312 ----YIHFGHGPHQCLGEEIARAALTEMLRVVLR 341
PLN02290 PLN02290
cytokinin trans-hydroxylase
296-477 2.17e-06

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 50.20  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   296 WSLFQMIRSPEAMKAASEEVSgalQSAGQELSSggsaiyLDQvqLNDLPVLDSIIKEALRL-SSASLNIRTAKEDFTLhl 374
Cdd:PLN02290 338 WTLMLLASNPTWQDKVRAEVA---EVCGGETPS------VDH--LSKLTLLNMVINESLRLyPPATLLPRMAFEDIKL-- 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   375 edGSYNIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYldesgkAKTTFYSNGNklkcfYMPFGSGATICPGRLFAVQE 453
Cdd:PLN02290 405 --GDLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRF------AGRPFAPGRH-----FIPFAAGPRNCIGQAFAMME 471
                        170       180
                 ....*....|....*....|....
gi 7549754   454 IKQFLILMLSCFELEFVESQVKCP 477
Cdd:PLN02290 472 AKIILAMLISKFSFTISDNYRHAP 495
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
288-450 3.13e-06

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: 49.42  E-value: 3.13e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  288 ANTIpatFWSLFQMIRSPEAMKAASEEVSGAL---QSAGQElssggsaiyldqvQLNDLPVLDSIIKEALRLS-SASLNI 363
Cdd:cd20645 243 ANSL---LWILYNLSRNPQAQQKLLQEIQSVLpanQTPRAE-------------DLKNMPYLKACLKESMRLTpSVPFTS 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  364 RTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESgkakttfysngNKLKCF-YMPFGSGAT 442
Cdd:cd20645 307 RTLDKDTVL----GDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQEK-----------HSINPFaHVPFGIGKR 371

                ....*...
gi 7549754  443 ICPGRLFA 450
Cdd:cd20645 372 MCIGRRLA 379
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
337-473 3.79e-06

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: 49.28  E-value: 3.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  337 QVQLNDLP---VLDSIIKEALRLSSA-SLNIRTAKEDFTLhleDGsYNIRKDDMIALYPQLMHLDpEIYPDPLTFKYDRY 412
Cdd:cd20616 273 DIQNDDLQklkVLENFINESMRYQPVvDFVMRKALEDDVI---DG-YPVKKGTNIILNIGRMHRL-EFFPKPNEFTLENF 347
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 7549754  413 ldesgkAKTTFYSngnklkcFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESQ 473
Cdd:cd20616 348 ------EKNVPSR-------YFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGR 395
PLN02966 PLN02966
cytochrome P450 83A1
280-463 4.20e-06

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 49.36  E-value: 4.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   280 LAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQSAGqelssggsAIYLDQVQLNDLPVLDSIIKEALRLSSA 359
Cdd:PLN02966 295 LDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKG--------STFVTEDDVKNLPYFRALVKETLRIEPV 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   360 S--LNIRTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYLDESGKAKTTFYSngnklkcfYMP 436
Cdd:PLN02966 367 IplLIPRACIQDTKI----AGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKGTDYE--------FIP 434
                        170       180
                 ....*....|....*....|....*...
gi 7549754   437 FGSGATICPG-RLFAVQEIKQFLILMLS 463
Cdd:PLN02966 435 FGSGRRMCPGmRLGAAMLEVPYANLLLN 462
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
187-491 1.33e-05

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: 47.45  E-value: 1.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  187 LFGRDISKTDTQKALILNNL-DNFK-------QFDQVFPALVAGLP-IH--LFKTAHKAREKLAEGLK-----HKNLCVR 250
Cdd:cd20669 122 VFGSRFDYDDKRLLTILNLInDNFQimsspwgELYNIFPSVMDWLPgPHqrIFQNFEKLRDFIAESVRehqesLDPNSPR 201
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  251 DQVS-ELIRLRMFLNDTLSTFDDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALqsaGQELSSg 329
Cdd:cd20669 202 DFIDcFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVV---GRNRLP- 277
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  330 gsaiyldqvQLND---LPVLDSIIKEALRLSSA---SLNIR----TAKEDFTLHledgsyniRKDDMIALYPQLmHLDPE 399
Cdd:cd20669 278 ---------TLEDrarMPYTDAVIHEIQRFADIipmSLPHAvtrdTNFRGFLIP--------KGTDVIPLLNSV-HYDPT 339
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  400 IYPDPLTFKYDRYLDESGkaktTFYSNGNklkcfYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVES--QVKCP 477
Cdd:cd20669 340 QFKDPQEFNPEHFLDDNG----SFKKNDA-----FMPFSAGKRICLGESLARMELFLYLTAILQNFSLQPLGApeDIDLT 410
                       330
                ....*....|....
gi 7549754  478 PLDqsrAGLGILPP 491
Cdd:cd20669 411 PLS---SGLGNVPR 421
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
296-466 1.85e-05

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 47.12  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   296 WSLFQMIRSPEAMKAASEEVSGALqsagqelssgGSAIYLDQVQLNDLPVLDSIIKEALRLSSAS--LNIRTAKEDFTLH 373
Cdd:PLN03112 318 WAMAEVIKNPRVLRKIQEELDSVV----------GRNRMVQESDLVHLNYLRCVVRETFRMHPAGpfLIPHESLRATTIN 387
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   374 ledgSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDR-YLDESGKAKTtfySNGNKLKCFymPFGSGATICPGRLFAVQ 452
Cdd:PLN03112 388 ----GYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERhWPAEGSRVEI---SHGPDFKIL--PFSAGKRKCPGAPLGVT 458
                        170
                 ....*....|....
gi 7549754   453 EIKQFLILMLSCFE 466
Cdd:PLN03112 459 MVLMALARLFHCFD 472
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
160-464 1.25e-04

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: 44.42  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  160 KSKSNAWVTEGMYAFCY----RVMFEAGYLTLFGRDISKTD--TQKALIlnnldnfKQFDQVFPALVAgLPIHLFKTAhk 233
Cdd:cd20638 107 RSSVNQWLQSGPCVLVYpevkRLMFRIAMRILLGFEPQQTDreQEQQLV-------EAFEEMIRNLFS-LPIDVPFSG-- 176
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  234 arekLAEGLKHKNLcVRDQVSELIRLRMFLNDTLSTFDD--------------------MEKAKTHLaiLWASQANTIPA 293
Cdd:cd20638 177 ----LYRGLRARNL-IHAKIEENIRAKIQREDTEQQCKDalqlliehsrrngeplnlqaLKESATEL--LFGGHETTASA 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  294 -----TFWSLFqmirsPEAMKAASEEvsgaLQSAGQELSSGGSAIYLDQVQLNDLPVLDSIIKEALRLSS-ASLNIRTAK 367
Cdd:cd20638 250 atsliMFLGLH-----PEVLQKVRKE----LQEKGLLSTKPNENKELSMEVLEQLKYTGCVIKETLRLSPpVPGGFRVAL 320
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  368 EDFTLHledgSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGR 447
Cdd:cd20638 321 KTFELN----GYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFS---------FIPFGGGSRSCVGK 387
                       330
                ....*....|....*...
gi 7549754  448 LFAVQEIKQFLI-LMLSC 464
Cdd:cd20638 388 EFAKVLLKIFTVeLARHC 405
PLN02183 PLN02183
ferulate 5-hydroxylase
296-468 1.38e-04

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 44.46  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   296 WSLFQMIRSPEAMKAASEEVSGALqsagqelssgGSAIYLDQVQLNDLPVLDSIIKEALRLSSA-SLNIRTAKEDFTLhl 374
Cdd:PLN02183 326 WAMAELMKSPEDLKRVQQELADVV----------GLNRRVEESDLEKLTYLKCTLKETLRLHPPiPLLLHETAEDAEV-- 393
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   375 edGSYNI--RKDDMIALYPqlMHLDPEIYPDPLTFKYDRYLDesGKAKTTfysNGNKLKcfYMPFGSGATICPGRLFAVQ 452
Cdd:PLN02183 394 --AGYFIpkRSRVMINAWA--IGRDKNSWEDPDTFKPSRFLK--PGVPDF---KGSHFE--FIPFGSGRRSCPGMQLGLY 462
                        170
                 ....*....|....*.
gi 7549754   453 EIKQFLILMLSCFELE 468
Cdd:PLN02183 463 ALDLAVAHLLHCFTWE 478
PLN03018 PLN03018
homomethionine N-hydroxylase
249-493 3.77e-04

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 43.08  E-value: 3.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   249 VRDQVSELIRLRMFLNDTLSTFDDMEKAKTHLAIlwASQANTIPATFWSLFQMIRSPEAMKAASEEVSgalQSAGQElss 328
Cdd:PLN03018 291 VEDWLDTFITLKDQNGKYLVTPDEIKAQCVEFCI--AAIDNPANNMEWTLGEMLKNPEILRKALKELD---EVVGKD--- 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   329 ggsaiylDQVQLNDLPVLD---SIIKEALRLSSASLNI--RTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPD 403
Cdd:PLN03018 363 -------RLVQESDIPNLNylkACCRETFRIHPSAHYVppHVARQDTTL----GGYFIPKGSHIHVCRPGLGRNPKIWKD 431
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   404 PLTFKYDRYLDESGKAKTTFYSngnKLKCFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVESqvkCPP--LDQ 481
Cdd:PLN03018 432 PLVYEPERHLQGDGITKEVTLV---ETEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHQD---FGPlsLEE 505
                        250
                 ....*....|..
gi 7549754   482 SRAGLGILPPLH 493
Cdd:PLN03018 506 DDASLLMAKPLL 517
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
379-491 5.96e-04

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: 42.25  E-value: 5.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  379 YNIRKD-DMIALYPQLMHlDPEIYPDPLTFKYDRYLDESGKAKTTFYsngnklkcfYMPFGSGATICPGRLFAVQEIKQF 457
Cdd:cd20665 319 YLIPKGtTVITSLTSVLH-DDKEFPNPEKFDPGHFLDENGNFKKSDY---------FMPFSAGKRICAGEGLARMELFLF 388
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 7549754  458 LILMLSCFELefvESQVKCPPLDQS--RAGLGILPP 491
Cdd:cd20665 389 LTTILQNFNL---KSLVDPKDIDTTpvVNGFASVPP 421
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
397-495 9.95e-04

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: 41.45  E-value: 9.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  397 DPEIYPDPLTFKYDRYLDESGKAKttfysngnKLKCFyMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVesqvkC 476
Cdd:cd20670 337 DPKYFRYPEAFYPQHFLDEQGRFK--------KNEAF-VPFSSGKRVCLGEAMARMELFLYFTSILQNFSLRSL-----V 402
                        90       100
                ....*....|....*....|...
gi 7549754  477 PPLD----QSRAGLGILPPLHDI 495
Cdd:cd20670 403 PPADiditPKISGFGNIPPTYEL 425
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
290-465 1.11e-03

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: 41.33  E-value: 1.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  290 TIPATFWSLFQMIRSPEAMKAASEEVSGALQSAgqelssggsaiyldQVQLND---LPVLDSIIKEALRLSS-ASLNI-R 364
Cdd:cd20664 241 TGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSR--------------QPQVEHrknMPYTDAVIHEIQRFANiVPMNLpH 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  365 TAKEDFTL---HLEDGSYnirkddMIALYPQLMHLDPEiYPDPLTFKYDRYLDESGKakttFYSNGNklkcfYMPFGSGA 441
Cdd:cd20664 307 ATTRDVTFrgyFIPKGTY------VIPLLTSVLQDKTE-WEKPEEFNPEHFLDSQGK----FVKRDA-----FMPFSAGR 370
                       170       180
                ....*....|....*....|....
gi 7549754  442 TICPGRLFAVQEIKQFLILMLSCF 465
Cdd:cd20664 371 RVCIGETLAKMELFLFFTSLLQRF 394
PLN00168 PLN00168
Cytochrome P450; Provisional
296-471 1.25e-03

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 41.47  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   296 WSLFQMIRSPEAMKAASEEVSGALQSAGQELSSggsaiylDQVQlnDLPVLDSIIKEALR--------LSSAslnirtAK 367
Cdd:PLN00168 328 WIMAELVKNPSIQSKLHDEIKAKTGDDQEEVSE-------EDVH--KMPYLKAVVLEGLRkhppahfvLPHK------AA 392
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   368 EDftlhLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYL---DESGKAKTTfySNGNKLkcfyMPFGSGATIC 444
Cdd:PLN00168 393 ED----MEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLaggDGEGVDVTG--SREIRM----MPFGVGRRIC 462
                        170       180
                 ....*....|....*....|....*..
gi 7549754   445 PGRLFAVQEIKQFLILMLSCFELEFVE 471
Cdd:PLN00168 463 AGLGIAMLHLEYFVANMVREFEWKEVP 489
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
389-495 1.28e-03

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: 41.30  E-value: 1.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  389 LYPQL---MHlDPEIYPDPLTFKYDRYLDESGKAKttfysngnKLKCFyMPFGSGATICPGRLFAVQEIKQFLILMLSCF 465
Cdd:cd20672 327 VYPILssaLH-DPQYFEQPDTFNPDHFLDANGALK--------KSEAF-MPFSTGKRICLGEGIARNELFLFFTTILQNF 396
                        90       100       110
                ....*....|....*....|....*....|..
gi 7549754  466 ElefVESQVKCPPLDQS--RAGLGILPPLHDI 495
Cdd:cd20672 397 S---VASPVAPEDIDLTpkESGVGKIPPTYQI 425
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
245-477 1.45e-03

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: 40.85  E-value: 1.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  245 KNlCVRDQVSELIRL--RMFLNDTLSTFDDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGalqsa 322
Cdd:cd20677 206 KN-HIRDITDALIALcqERKAEDKSAVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDE----- 279
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  323 gqELSSGGSAIYLDQVqlnDLPVLDSIIKEALRLSS-ASLNI-RTAKEDFTLHledgSYNIRKDD--MIALYpQLMHlDP 398
Cdd:cd20677 280 --KIGLSRLPRFEDRK---SLHYTEAFINEVFRHSSfVPFTIpHCTTADTTLN----GYFIPKDTcvFINMY-QVNH-DE 348
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  399 EIYPDPLTFKYDRYLDESGKAkttfysngNK-LKCFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEfvesqvKCP 477
Cdd:cd20677 349 TLWKDPDLFMPERFLDENGQL--------NKsLVEKVLIFGMGVRKCLGEDVARNEIFVFLTTILQQLKLE------KPP 414
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
343-458 1.90e-03

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 40.49  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   343 LPVLDSIIKEALRLSSASLNI-RTAKEDftlhLEDGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLDESGkakt 421
Cdd:PLN03141 314 LPFTQNVITETLRMGNIINGVmRKAMKD----VEIKGYLIPKGWCVLAYFRSVHLDEENYDNPYQFNPWRWQEKDM---- 385
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 7549754   422 tfySNGNklkcfYMPFGSGATICPGRLFAVQEIKQFL 458
Cdd:PLN03141 386 ---NNSS-----FTPFGGGQRLCPGLDLARLEASIFL 414
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
288-477 2.04e-03

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 40.83  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   288 ANTIPATFWSLFQmirSPEAMKAASEEVSGALqsagqelssGGSAIYLDQVQLNDLPVLDSIIKEALRL-SSASLNIRTA 366
Cdd:PLN02426 310 ASALTSFFWLLSK---HPEVASAIREEADRVM---------GPNQEAASFEEMKEMHYLHAALYESMRLfPPVQFDSKFA 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754   367 KEDFTLhlEDGSYnIRKDDMIALYPQLMHLDPEIY-PDPLTFKYDRYLDESgkaktTFYSNgNKLKcfYMPFGSGATICP 445
Cdd:PLN02426 378 AEDDVL--PDGTF-VAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNG-----VFVPE-NPFK--YPVFQAGLRVCL 446
                        170       180       190
                 ....*....|....*....|....*....|..
gi 7549754   446 GRLFAVQEIKQFLILMLSCFELEFVESQVKCP 477
Cdd:PLN02426 447 GKEMALMEMKSVAVAVVRRFDIEVVGRSNRAP 478
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
265-495 3.75e-03

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: 39.78  E-value: 3.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  265 DTLSTFDDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALqsaGQElssggsaiylDQVQLND-- 342
Cdd:cd20662 216 DPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVI---GQK----------RQPSLADre 282
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  343 -LPVLDSIIKEALRLSS-ASLNI-RTAKEDFTLhledGSYNIRKDDMIALYPQLMHLDPEIYPDPLTFKYDRYLdESGKA 419
Cdd:cd20662 283 sMPYTNAVIHEVQRMGNiIPLNVpREVAVDTKL----AGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFL-ENGQF 357
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  420 KttfysngnKLKCFyMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEfvesqvkcPPLD-----QSRAGLGILPPLHD 494
Cdd:cd20662 358 K--------KREAF-LPFSMGKRACLGEQLARSELFIFFTSLLQKFTFK--------PPPNeklslKFRMGITLSPVPHR 420

                .
gi 7549754  495 I 495
Cdd:cd20662 421 I 421
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
336-411 5.09e-03

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: 39.05  E-value: 5.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7549754  336 DQVQL--NDLPVLDSIIKEALRLSSASLNI-RTAKEDFTLHledGsYNIRKDDMIAL-YPQLMHlDPEIYPDPLTFKYDR 411
Cdd:cd11033 241 DQWERlrADPSLLPTAVEEILRWASPVIHFrRTATRDTELG---G-QRIRAGDKVVLwYASANR-DEEVFDDPDRFDITR 315
PLN02500 PLN02500
cytochrome P450 90B1
394-472 5.77e-03

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 39.08  E-value: 5.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7549754   394 MHLDPEIYPDPLTFKYDRYLDESGKAKTTFYSNGNKlkCFYMPFGSGATICPGRLFAVQEIKQFLILMLSCFELEFVES 472
Cdd:PLN02500 391 VHLDSSLYDQPQLFNPWRWQQNNNRGGSSGSSSATT--NNFMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWELAEA 467
 
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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