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Conserved domains on  [gi|1039011928|gb|ANM61755|]
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cytochrome P450, family 79, subfamily B, polypeptide 3 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02971 PLN02971
tryptophan N-hydroxylase
24-566 0e+00

tryptophan N-hydroxylase


:

Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 1128.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  24 MDTLASNSSDLTTKSSLGMSSFTNMYLLTTLQALAALCFLMILNKIKSSSRNKKLHPLPPGPTGFPIVGMIPAMLKNRPV 103
Cdd:PLN02971    1 MDTLASNSSDLTTKSSPGTSSFTNMYLLTTLQALVAITLLMILKKLKSSSRNKKLHPLPPGPTGFPIVGMIPAMLKNRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 104 FRWLHSLMKELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVI 183
Cdd:PLN02971   81 FRWLHSLMKELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 184 MTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEADGGPTLEDIEHM 263
Cdd:PLN02971  161 MTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEPDGGPTLEDIEHM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 264 DAMFEGLGFTFAFCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQ 343
Cdd:PLN02971  241 DAMFEGLGFTFAFCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 344 PLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLH 423
Cdd:PLN02971  321 PLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLH 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 424 PVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCA 503
Cdd:PLN02971  401 PVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCA 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011928 504 APALGTAITTMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVLVGELRLSEDLYPMVK 566
Cdd:PLN02971  481 APALGTAITTMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVMVGELRLSEDLYPTVK 543
 
Name Accession Description Interval E-value
PLN02971 PLN02971
tryptophan N-hydroxylase
24-566 0e+00

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 1128.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  24 MDTLASNSSDLTTKSSLGMSSFTNMYLLTTLQALAALCFLMILNKIKSSSRNKKLHPLPPGPTGFPIVGMIPAMLKNRPV 103
Cdd:PLN02971    1 MDTLASNSSDLTTKSSPGTSSFTNMYLLTTLQALVAITLLMILKKLKSSSRNKKLHPLPPGPTGFPIVGMIPAMLKNRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 104 FRWLHSLMKELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVI 183
Cdd:PLN02971   81 FRWLHSLMKELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 184 MTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEADGGPTLEDIEHM 263
Cdd:PLN02971  161 MTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEPDGGPTLEDIEHM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 264 DAMFEGLGFTFAFCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQ 343
Cdd:PLN02971  241 DAMFEGLGFTFAFCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 344 PLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLH 423
Cdd:PLN02971  321 PLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLH 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 424 PVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCA 503
Cdd:PLN02971  401 PVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCA 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011928 504 APALGTAITTMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVLVGELRLSEDLYPMVK 566
Cdd:PLN02971  481 APALGTAITTMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVMVGELRLSEDLYPTVK 543
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
116-557 0e+00

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: 864.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 116 TEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRW 195
Cdd:cd20658     1 TDIACIRLGNTHVIPVTCPKIAREILRKQDAVFASRPLTYATEIISGGYKTTVISPYGEQWKKMRKVLTTELMSPKRHQW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 196 LHDNRAEETDHLTAWLYNMVKNS---EPVDLRFVTRHYCGNAIKRLMFGTRTFSeKTEADGGPTLEDIEHMDAMFEGLGF 272
Cdd:cd20658    81 LHGKRTEEADNLVAYVYNMCKKSnggGLVNVRDAARHYCGNVIRKLMFGTRYFG-KGMEDGGPGLEEVEHMDAIFTALKC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 273 TFAFCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQPLLTADEIK 352
Cdd:cd20658   160 LYAFSISDYLPFLRGLDLDGHEKIVREAMRIIRKYHDPIIDERIKQWREGKKKEEEDWLDVFITLKDENGNPLLTPDEIK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 353 PTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPH 432
Cdd:cd20658   240 AQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNVPH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 433 VALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCAAPALGTAIT 512
Cdd:cd20658   320 VAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEVTLTEPDLRFISFSTGRRGCPGVKLGTAMT 399
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1039011928 513 TMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVLVGELRL 557
Cdd:cd20658   400 VMLLARLLQGFTWTLPPNVSSVDLSESKDDLFMAKPLVLVAKPRL 444
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
82-549 6.59e-85

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: 271.46  E-value: 6.59e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  82 PPGPTGFPIVGMIPamlkNRPVFRWLHSLMKELNTE---IACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQK 158
Cdd:pfam00067   1 PPGPPPLPLFGNLL----QLGRKGNLHSVFTKLQKKygpIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 159 ILSNGYKTC-VITPFGEQFKKMRKVIMTEIVCPARHRWLhDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKR 237
Cdd:pfam00067  77 TSRGPFLGKgIVFANGPRWRQLRRFLTPTFTSFGKLSFE-PRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 238 LMFGTRTFSEKTEADggPTLED-IEHMDAMFeglgFTFAFCISDYLPMLTGLdLNGHEKIMRESSAIMDKYHDPIIDERI 316
Cdd:pfam00067 156 ILFGERFGSLEDPKF--LELVKaVQELSSLL----SSPSPQLLDLFPILKYF-PGPHGRKLKRARKKIKDLLDKLIEERR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 317 KMWREGKRTQIeDFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVG 396
Cdd:pfam00067 229 ETLDSAKKSPR-DFLDALLLAKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 397 KERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERH 476
Cdd:pfam00067 308 DKRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERF 387
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011928 477 LNecsEVTLTENDLRFISFSTGKRGCaapaLGTAITTMM----LARLLQGFKWKLAgSETRVELMESSHdMFLSKPL 549
Cdd:pfam00067 388 LD---ENGKFRKSFAFLPFGAGPRNC----LGERLARMEmklfLATLLQNFEVELP-PGTDPPDIDETP-GLLLPPK 455
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
280-531 4.47e-24

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: 104.59  E-value: 4.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 280 DYLPMLTGLDLNGHEKiMRESSAIMDKYHDPIIDERikmwREGKRtqiEDFLDIFISIKDEaGQPLlTADEIKPTIKELV 359
Cdd:COG2124   166 ALLDALGPLPPERRRR-ARRARAELDAYLRELIAER----RAEPG---DDLLSALLAARDD-GERL-SDEELRDELLLLL 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 360 MAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDrvvgkerfvqesdipklnYVKAIIREAFRLHPVAAFnLPHVALSDTT 439
Cdd:COG2124   236 LAGHETTANALAWALYALLRHPEQLARLRAEPE------------------LLPAAVEETLRLYPPVPL-LPRTATEDVE 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 440 VAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNecsevtltendlRFISFSTGKRGCAAPALGTAITTMMLARL 519
Cdd:COG2124   297 LGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDRPPN------------AHLPFGGGPHRCLGAALARLEARIALATL 364
                         250
                  ....*....|...
gi 1039011928 520 LQGF-KWKLAGSE 531
Cdd:COG2124   365 LRRFpDLRLAPPE 377
 
Name Accession Description Interval E-value
PLN02971 PLN02971
tryptophan N-hydroxylase
24-566 0e+00

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 1128.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  24 MDTLASNSSDLTTKSSLGMSSFTNMYLLTTLQALAALCFLMILNKIKSSSRNKKLHPLPPGPTGFPIVGMIPAMLKNRPV 103
Cdd:PLN02971    1 MDTLASNSSDLTTKSSPGTSSFTNMYLLTTLQALVAITLLMILKKLKSSSRNKKLHPLPPGPTGFPIVGMIPAMLKNRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 104 FRWLHSLMKELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVI 183
Cdd:PLN02971   81 FRWLHSLMKELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 184 MTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEADGGPTLEDIEHM 263
Cdd:PLN02971  161 MTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEPDGGPTLEDIEHM 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 264 DAMFEGLGFTFAFCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQ 343
Cdd:PLN02971  241 DAMFEGLGFTFAFCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQ 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 344 PLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLH 423
Cdd:PLN02971  321 PLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLH 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 424 PVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCA 503
Cdd:PLN02971  401 PVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCA 480
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011928 504 APALGTAITTMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVLVGELRLSEDLYPMVK 566
Cdd:PLN02971  481 APALGTAITTMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVMVGELRLSEDLYPTVK 543
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
116-557 0e+00

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: 864.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 116 TEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRW 195
Cdd:cd20658     1 TDIACIRLGNTHVIPVTCPKIAREILRKQDAVFASRPLTYATEIISGGYKTTVISPYGEQWKKMRKVLTTELMSPKRHQW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 196 LHDNRAEETDHLTAWLYNMVKNS---EPVDLRFVTRHYCGNAIKRLMFGTRTFSeKTEADGGPTLEDIEHMDAMFEGLGF 272
Cdd:cd20658    81 LHGKRTEEADNLVAYVYNMCKKSnggGLVNVRDAARHYCGNVIRKLMFGTRYFG-KGMEDGGPGLEEVEHMDAIFTALKC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 273 TFAFCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQPLLTADEIK 352
Cdd:cd20658   160 LYAFSISDYLPFLRGLDLDGHEKIVREAMRIIRKYHDPIIDERIKQWREGKKKEEEDWLDVFITLKDENGNPLLTPDEIK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 353 PTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPH 432
Cdd:cd20658   240 AQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNVPH 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 433 VALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCAAPALGTAIT 512
Cdd:cd20658   320 VAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEVTLTEPDLRFISFSTGRRGCPGVKLGTAMT 399
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1039011928 513 TMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVLVGELRL 557
Cdd:cd20658   400 VMLLARLLQGFTWTLPPNVSSVDLSESKDDLFMAKPLVLVAKPRL 444
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
117-529 3.68e-166

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: 478.97  E-value: 3.68e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 117 EIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWL 196
Cdd:cd20618     2 PLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKIFSYNGQDIVFAPYGPHWRHLRKICTLELFSAKRLESF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 197 HDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEkteaDGGPTLEDIEHMDAMFEGLGFTFAF 276
Cdd:cd20618    82 QGVRKEELSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRYFGE----SEKESEEAREFKELIDEAFELAGAF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 277 CISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFIsiKDEAGQPLLTADEIKPTIK 356
Cdd:cd20618   158 NIGDYIPWLRWLDLQGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLL--LDLDGEGKLSDDNIKALLL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 357 ELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALS 436
Cdd:cd20618   236 DMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLLPHESTE 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 437 DTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMML 516
Cdd:cd20618   316 DCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLES-DIDDVKGQDFELLPFGSGRRMCPGMPLGLRMVQLTL 394
                         410
                  ....*....|...
gi 1039011928 517 ARLLQGFKWKLAG 529
Cdd:cd20618   395 ANLLHGFDWSLPG 407
PLN03018 PLN03018
homomethionine N-hydroxylase
42-563 1.78e-159

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 466.03  E-value: 1.78e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  42 MSSFTNMY--LLTTLQALAALCFL-MILNK-IKSSSRNKKLhplPPGPTGFPIVGMIPAMLKNRPVFRWLHSLMKELNTE 117
Cdd:PLN03018    1 MMSFNTSFqiLLGFIVFIASITLLgRILSRpSKTKDRSRQL---PPGPPGWPILGNLPELIMTRPRSKYFHLAMKELKTD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 118 IACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLH 197
Cdd:PLN03018   78 IACFNFAGTHTITINSDEIAREAFRERDADLADRPQLSIMETIGDNYKSMGTSPYGEQFMKMKKVITTEIMSVKTLNMLE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 198 DNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKT--EADGGPTLEDIEHMDAMFEGLGFTFA 275
Cdd:PLN03018  158 AARTIEADNLIAYIHSMYQRSETVDVRELSRVYGYAVTMRMLFGRRHVTKENvfSDDGRLGKAEKHHLEVIFNTLNCLPG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 276 FCISDYLPM-LTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWRE-GKRTQIEDFLDIFISIKDEAGQPLLTADEIKP 353
Cdd:PLN03018  238 FSPVDYVERwLRGWNIDGQEERAKVNVNLVRSYNNPIIDERVELWREkGGKAAVEDWLDTFITLKDQNGKYLVTPDEIKA 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 354 TIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHV 433
Cdd:PLN03018  318 QCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHV 397
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 434 ALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNE---CSEVTLTENDLRFISFSTGKRGCAAPALGTA 510
Cdd:PLN03018  398 ARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGdgiTKEVTLVETEMRFVSFSTGRRGCVGVKVGTI 477
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039011928 511 ITTMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPLVLVGELRLSEDLYP 563
Cdd:PLN03018  478 MMVMMLARFLQGFNWKLHQDFGPLSLEEDDASLLMAKPLLLSVEPRLAPNLYP 530
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
57-562 1.02e-108

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 334.87  E-value: 1.02e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  57 LAALCFLMILNKIK---SSSRNKKLHPLPPGPTGFPIVGMIpAMLKNRPvfrwlHSLMKELNTE---IACVRLGNTHVIP 130
Cdd:PLN03112    6 LSLLFSVLIFNVLIwrwLNASMRKSLRLPPGPPRWPIVGNL-LQLGPLP-----HRDLASLCKKygpLVYLRLGSVDAIT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 131 VTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDHLTAW 210
Cdd:PLN03112   80 TDDPELIREILLRQDDVFASRPRTLAAVHLAYGCGDVALAPLGPHWKRMRRICMEHLLTTKRLESFAKHRAEEARHLIQD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 211 LYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSeKTEADGGPTLEDIEHMDAMFEGLGFTFafcISDYLPMLTGLDL 290
Cdd:PLN03112  160 VWEAAQTGKPVNLREVLGAFSMNNVTRMLLGKQYFG-AESAGPKEAMEFMHITHELFRLLGVIY---LGDYLPAWRWLDP 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 291 NGHEKIMRESSAIMDKYHDPIIDERIKMwREGKRTQIE--DFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSN 368
Cdd:PLN03112  236 YGCEKKMREVEKRVDEFHDKIIDEHRRA-RSGKLPGGKdmDFVDVLLSLPGENGKEHMDDVEIKALMQDMIAAATDTSAV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 369 AVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKG 448
Cdd:PLN03112  315 TNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPFLIPHESLRATTINGYYIPAK 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 449 SQVLLSRYGLGRNPKVWSDPLSFKPERHL-NECSEVTLTEN-DLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWK 526
Cdd:PLN03112  395 TRVFINTHGLGRNTKIWDDVEEFRPERHWpAEGSRVEISHGpDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWS 474
                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 1039011928 527 LAGSETRVEL-MESSHDMFL--SKPLVLVGELRLSEDLY 562
Cdd:PLN03112  475 PPDGLRPEDIdTQEVYGMTMpkAKPLRAVATPRLAPHLY 513
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
121-543 4.29e-98

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: 304.77  E-value: 4.29e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNR 200
Cdd:cd11072     8 LRLGSVPTVVVSSPEAAKEVLKTHDLVFASRPKLLAARILSYGGKDIAFAPYGEYWRQMRKICVLELLSAKRVQSFRSIR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 201 AEETDHLTAWLYNMVKNSEPVDL--RFVTrhYCGNAIKRLMFGtrtfsEKTEADGGPTLEDIehmdaMFEGLGFTFAFCI 278
Cdd:cd11072    88 EEEVSLLVKKIRESASSSSPVNLseLLFS--LTNDIVCRAAFG-----RKYEGKDQDKFKEL-----VKEALELLGGFSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 279 SDYLPMLTGLD-LNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQPLLTADEIKPTIKE 357
Cdd:cd11072   156 GDYFPSLGWIDlLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEFPLTRDNIKAIILD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 358 LVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSD 437
Cdd:cd11072   236 MFLAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPPAPLLLPRECRED 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 438 TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNecSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLA 517
Cdd:cd11072   316 CKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLD--SSIDFKGQDFELIPFGAGRRICPGITFGLANVELALA 393
                         410       420
                  ....*....|....*....|....*.
gi 1039011928 518 RLLQGFKWKLAGSETRVELmesshDM 543
Cdd:cd11072   394 NLLYHFDWKLPDGMKPEDL-----DM 414
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
121-552 1.16e-92

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: 290.97  E-value: 1.16e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNR 200
Cdd:cd11073    10 LKLGSKTTVVVSSPEAAREVLKTHDRVLSGRDVPDAVRALGHHKSSIVWPPYGPRWRMLRKICTTELFSPKRLDATQPLR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 201 AEETDHLTAWLYNMVKNSEPVDLR---FVTRHycgNAIKRLMFGTRTFSEKTEADGgptlEDIEHMDAMFEGLGftfAFC 277
Cdd:cd11073    90 RRKVRELVRYVREKAGSGEAVDIGraaFLTSL---NLISNTLFSVDLVDPDSESGS----EFKELVREIMELAG---KPN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 278 ISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKE 357
Cdd:cd11073   160 VADFFPFLKFLDLQGLRRRMAEHFGKLFDIFDGFIDERLAEREAGGDKKKDDDLLLLLDLELDSESEL-TRNHIKALLLD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 358 LVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSD 437
Cdd:cd11073   239 LFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLLLPRKAEED 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 438 TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNecSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLA 517
Cdd:cd11073   319 VEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLG--SEIDFKGRDFELIPFGSGRRICPGLPLAERMVHLVLA 396
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 1039011928 518 RLLQGFKWKLAGSETRVEL-MESSHDMFLSK--PLVLV 552
Cdd:cd11073   397 SLLHSFDWKLPDGMKPEDLdMEEKFGLTLQKavPLKAI 434
PLN02687 PLN02687
flavonoid 3'-monooxygenase
50-562 5.16e-91

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 289.40  E-value: 5.16e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  50 LLTTLQALAALCFLMIlnkiKSSSRNKKLHPLPPGPTGFPIVGMIPaMLKNRPvfrwlHSLMKELNTE---IACVRLGNT 126
Cdd:PLN02687    8 LLGTVAVSVLVWCLLL----RRGGSGKHKRPLPPGPRGWPVLGNLP-QLGPKP-----HHTMAALAKTygpLFRLRFGFV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 127 HVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDH 206
Cdd:PLN02687   78 DVVVAASASVAAQFLRTHDANFSNRPPNSGAEHMAYNYQDLVFAPYGPRWRALRKICAVHLFSAKALDDFRHVREEEVAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 207 LTAWLYNMVKNSePVDLRFVTRHYCGNAIKRLMFGTRTFSekteADGGPTLEDIEHMdaMFEGLGFTFAFCISDYLPMLT 286
Cdd:PLN02687  158 LVRELARQHGTA-PVNLGQLVNVCTTNALGRAMVGRRVFA----GDGDEKAREFKEM--VVELMQLAGVFNVGDFVPALR 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 287 GLDLNGHEKIMRESSAIMDKYHDPIIDERiKMWREGKRTQIEDFLDIFISIKDEagQPL------LTADEIKPTIKELVM 360
Cdd:PLN02687  231 WLDLQGVVGKMKRLHRRFDAMMNGIIEEH-KAAGQTGSEEHKDLLSTLLALKRE--QQAdgeggrITDTEIKALLLNLFT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 361 AAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTV 440
Cdd:PLN02687  308 AGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPLSLPRMAAEECEI 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 441 AGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHL--NECSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLAR 518
Cdd:PLN02687  388 NGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpgGEHAGVDVKGSDFELIPFGAGRRICAGLSWGLRMVTLLTAT 467
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1039011928 519 LLQGFKWKLAGSETRVEL-MESSHDMFLSK--PLVLVGELRLSEDLY 562
Cdd:PLN02687  468 LVHAFDWELADGQTPDKLnMEEAYGLTLQRavPLMVHPRPRLLPSAY 514
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
122-550 3.69e-90

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: 284.31  E-value: 3.69e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 122 RLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCP-ARHRWLHdNR 200
Cdd:cd20657     7 KVGSCGVVVASSPPVAKAFLKTHDANFSNRPPNAGATHMAYNAQDMVFAPYGPRWRLLRKLCNLHLFGGkALEDWAH-VR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 201 AEETDHLTAWLYNMVKNSEPVDL-RFVTrhYC-GNAIKRLMFGTRTFsektEADGGPTLEDIEHMdaMFEGLGFTFAFCI 278
Cdd:cd20657    86 ENEVGHMLKSMAEASRKGEPVVLgEMLN--VCmANMLGRVMLSKRVF----AAKAGAKANEFKEM--VVELMTVAGVFNI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 279 SDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTqiEDFLDIFISIKDEAGQ-PLLTADEIKPTIKE 357
Cdd:cd20657   158 GDFIPSLAWMDLQGVEKKMKRLHKRFDALLTKILEEHKATAQERKGK--PDFLDFVLLENDDNGEgERLTDTNIKALLLN 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 358 LVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSD 437
Cdd:cd20657   236 LFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 438 TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNE-CSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMML 516
Cdd:cd20657   316 CEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPGrNAKVDVRGNDFELIPFGAGRRICAGTRMGIRMVEYIL 395
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1039011928 517 ARLLQGFKWKLAGSETRVEL-MESSHDMFLSK--PLV 550
Cdd:cd20657   396 ATLVHSFDWKLPAGQTPEELnMEEAFGLALQKavPLV 432
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
120-552 1.28e-87

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: 277.56  E-value: 1.28e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 120 CVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCP-ARHRWLHd 198
Cdd:cd20655     5 HLRIGSVPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESLLYGSSGFAFAPYGDYWKFMKKLCMTELLGPrALERFRP- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 199 NRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEADggptlediEHMDAMFEGLGFTFAFCI 278
Cdd:cd20655    84 IRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEAE--------EVRKLVKESAELAGKFNA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 279 SDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISI-KDEAGQPLLTADEIKPTIKE 357
Cdd:cd20655   156 SDFIWPLKKLDLQGFGKRIMDVSNRFDELLERIIKEHEEKRKKRKEGGSKDLLDILLDAyEDENAEYKITRNHIKAFILD 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 358 LVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVALSD 437
Cdd:cd20655   236 LFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPL-LVRESTEG 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 438 TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLN---ECSEVTLTENDLRFISFSTGKRGCAAPALGTAITTM 514
Cdd:cd20655   315 CKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLAssrSGQELDVRGQHFKLLPFGSGRRGCPGASLAYQVVGT 394
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1039011928 515 MLARLLQGFKWKLAGSEtRVElMESSHDMFLS--KPLVLV 552
Cdd:cd20655   395 AIAAMVQCFDWKVGDGE-KVN-MEEASGLTLPraHPLKCV 432
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
82-549 6.59e-85

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: 271.46  E-value: 6.59e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  82 PPGPTGFPIVGMIPamlkNRPVFRWLHSLMKELNTE---IACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQK 158
Cdd:pfam00067   1 PPGPPPLPLFGNLL----QLGRKGNLHSVFTKLQKKygpIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 159 ILSNGYKTC-VITPFGEQFKKMRKVIMTEIVCPARHRWLhDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKR 237
Cdd:pfam00067  77 TSRGPFLGKgIVFANGPRWRQLRRFLTPTFTSFGKLSFE-PRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 238 LMFGTRTFSEKTEADggPTLED-IEHMDAMFeglgFTFAFCISDYLPMLTGLdLNGHEKIMRESSAIMDKYHDPIIDERI 316
Cdd:pfam00067 156 ILFGERFGSLEDPKF--LELVKaVQELSSLL----SSPSPQLLDLFPILKYF-PGPHGRKLKRARKKIKDLLDKLIEERR 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 317 KMWREGKRTQIeDFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVG 396
Cdd:pfam00067 229 ETLDSAKKSPR-DFLDALLLAKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 397 KERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERH 476
Cdd:pfam00067 308 DKRSPTYDDLQNMPYLDAVIKETLRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERF 387
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011928 477 LNecsEVTLTENDLRFISFSTGKRGCaapaLGTAITTMM----LARLLQGFKWKLAgSETRVELMESSHdMFLSKPL 549
Cdd:pfam00067 388 LD---ENGKFRKSFAFLPFGAGPRNC----LGERLARMEmklfLATLLQNFEVELP-PGTDPPDIDETP-GLLLPPK 455
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
118-531 2.73e-82

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: 263.31  E-value: 2.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 118 IACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLH 197
Cdd:cd20653     3 IFSLRFGSRLVVVVSSPSAAEECFTKNDIVLANRPRFLTGKHIGYNYTTVGSAPYGDHWRNLRRITTLEIFSSHRLNSFS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 198 DNRAEETDHLTAWLY-NMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEADggptlEDIEHMDAMF-EGLGFTFA 275
Cdd:cd20653    83 SIRRDEIRRLLKRLArDSKGGFAKVELKPLFSELTFNNIMRMVAGKRYYGEDVSDA-----EEAKLFRELVsEIFELSGA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 276 FCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISikdeagQPLLTADEIkptI 355
Cdd:cd20653   158 GNPADFLPILRWFDFQGLEKRVKKLAKRRDAFLQGLIDEHRKNKESGKNTMIDHLLSLQES------QPEYYTDEI---I 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 356 KELVM----AAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLP 431
Cdd:cd20653   229 KGLILvmllAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVP 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 432 HVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTltendlRFISFSTGKRGCAAPALGTAI 511
Cdd:cd20653   309 HESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGEEREGY------KLIPFGLGRRACPGAGLAQRV 382
                         410       420
                  ....*....|....*....|
gi 1039011928 512 TTMMLARLLQGFKWKLAGSE 531
Cdd:cd20653   383 VGLALGSLIQCFEWERVGEE 402
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
121-523 4.29e-82

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: 263.71  E-value: 4.29e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNR 200
Cdd:cd20654     6 LRLGSHPTLVVSSWEMAKECFTTNDKAFSSRPKTAAAKLMGYNYAMFGFAPYGPYWRELRKIATLELLSNRRLEKLKHVR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 201 AEETDHLTAWLY----NMVKNSEPV---------DLRFvtrhycgNAIKRLMFGTRTFSEKTEADGGptlEDIEHMDAMF 267
Cdd:cd20654    86 VSEVDTSIKELYslwsNNKKGGGGVlvemkqwfaDLTF-------NVILRMVVGKRYFGGTAVEDDE---EAERYKKAIR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 268 EGLGFTFAFCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQ--IEDFLDIFISIKDEAGQPL 345
Cdd:cd20654   156 EFMRLAGTFVVSDAIPFLGWLDFGGHEKAMKRTAKELDSILEEWLEEHRQKRSSSGKSKndEDDDDVMMLSILEDSQISG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 346 LTADE-IKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHP 424
Cdd:cd20654   236 YDADTvIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYP 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 425 VAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCAA 504
Cdd:cd20654   316 PGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHKDIDVRGQNFELIPFGSGRRSCPG 395
                         410
                  ....*....|....*....
gi 1039011928 505 PALGTAITTMMLARLLQGF 523
Cdd:cd20654   396 VSFGLQVMHLTLARLLHGF 414
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
121-530 4.76e-77

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: 249.82  E-value: 4.76e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKtcVITPFGEQFKKMRKVIMTEIVcPARHRWLHDNR 200
Cdd:cd20617     6 LWLGDVPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKG--ILFSNGDYWKELRRFALSSLT-KTKLKKKMEEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 201 -AEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRtFSEKTEadgGPTLEDIEHMDAMFEGLGFTFAFcis 279
Cdd:cd20617    83 iEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKR-FPDEDD---GEFLKLVKPIEEIFKELGSGNPS--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 280 DYLPMLTGLDLNGHEKIMRESSAIMDkYHDPIIDERIKMWREGKRTQIEDflDIFISIKDEAGQPLLTADEIKPTIKELV 359
Cdd:cd20617   156 DFIPILLPFYFLYLKKLKKSYDKIKD-FIEKIIEEHLKTIDPNNPRDLID--DELLLLLKEGDSGLFDDDSIISTCLDLF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 360 MAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTT 439
Cdd:cd20617   233 LAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTE 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 440 VAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsevTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARL 519
Cdd:cd20617   313 IGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLEN----DGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANL 388
                         410
                  ....*....|.
gi 1039011928 520 LQGFKWKLAGS 530
Cdd:cd20617   389 LLNFKFKSSDG 399
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
56-527 2.72e-73

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 242.45  E-value: 2.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  56 ALAALCFLMILNKIKSSSRnKKLHPLPPGPTGFPIVGMIPaMLKNRPvfrwlHSLMKELNTEIACV---RLGNTHVIPVT 132
Cdd:PLN00110    8 AAATLLFFITRFFIRSLLP-KPSRKLPPGPRGWPLLGALP-LLGNMP-----HVALAKMAKRYGPVmflKMGTNSMVVAS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 133 CPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIV-CPARHRWLHdNRAEETDHLTAWL 211
Cdd:PLN00110   81 TPEAARAFLKTLDINFSNRPPNAGATHLAYGAQDMVFADYGPRWKLLRKLSNLHMLgGKALEDWSQ-VRTVELGHMLRAM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 212 YNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEadggptlEDIEHMDAMFEGLGFTFAFCISDYLPMLTGLDLN 291
Cdd:PLN00110  160 LELSQRGEPVVVPEMLTFSMANMIGQVILSRRVFETKGS-------ESNEFKDMVVELMTTAGYFNIGDFIPSIAWMDIQ 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 292 GHEKIMRESSAIMDKYHDPIIDERIKMWREgkRTQIEDFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVE 371
Cdd:PLN00110  233 GIERGMKHLHKKFDKLLTRMIEEHTASAHE--RKGNPDFLDVVMANQENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 372 WAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQV 451
Cdd:PLN00110  311 WSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRL 390
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011928 452 LLSRYGLGRNPKVWSDPLSFKPERHLNE-CSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKL 527
Cdd:PLN00110  391 SVNIWAIGRDPDVWENPEEFRPERFLSEkNAKIDPRGNDFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKL 467
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
121-531 4.42e-72

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: 237.14  E-value: 4.42e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYA-QKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDN 199
Cdd:cd11075     8 LRMGSRPLIVVASRELAHEALVQKGSSFASRPPANPlRVLFSSNKHMVNSSPYGPLWRTLRRNLVSEVLSPSRLKQFRPA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 200 RAEETDHLTAWLYNMVK-NSEPVDLRFVTRHycgnaikrLMFG---TRTFSEKTEADggpTLEDIEHMdaMFEGLGFTFA 275
Cdd:cd11075    88 RRRALDNLVERLREEAKeNPGPVNVRDHFRH--------ALFSlllYMCFGERLDEE---TVRELERV--QRELLLSFTD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 276 FCISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQ--IEDFLDIFISIKDEAGQPLLTADEIKP 353
Cdd:cd11075   155 FDVRDFFPALTWLLNRRRWKKVLELRRRQEEVLLPLIRARRKRRASGEADKdyTDFLLLDLLDLKEEGGERKLTDEELVS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 354 TIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHV 433
Cdd:cd11075   235 LCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHFLLPHA 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 434 ALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLN--ECSEVTLTENDLRFISFSTGKRGCAAPALGTAI 511
Cdd:cd11075   315 VTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAggEAADIDTGSKEIKMMPFGAGRRICPGLGLATLH 394
                         410       420
                  ....*....|....*....|
gi 1039011928 512 TTMMLARLLQGFKWKLAGSE 531
Cdd:cd11075   395 LELFVARLVQEFEWKLVEGE 414
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
118-539 4.71e-68

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: 226.60  E-value: 4.71e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 118 IACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLH 197
Cdd:cd20656     4 IISVWIGSTLNVVVSSSELAKEVLKEKDQQLADRHRTRSAARFSRNGQDLIWADYGPHYVKVRKLCTLELFTPKRLESLR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 198 DNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCG----NAIKRLMFGTRTFSEKTEADGgptlEDIEHMDAMFEGLGFT 273
Cdd:cd20656    84 PIREDEVTAMVESIFNDCMSPENEGKPVVLRKYLSavafNNITRLAFGKRFVNAEGVMDE----QGVEFKAIVSNGLKLG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 274 FAFCISDYLPMLTGLdLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQieDFLDIFISIKDEAGqplLTADEIKP 353
Cdd:cd20656   160 ASLTMAEHIPWLRWM-FPLSEKAFAKHGARRDRLTKAIMEEHTLARQKSGGGQ--QHFVALLTLKEQYD---LSEDTVIG 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 354 TIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHV 433
Cdd:cd20656   234 LLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHK 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 434 ALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsEVTLTENDLRFISFSTGKRGCAAPALGTAITT 513
Cdd:cd20656   314 ASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEE--DVDIKGHDFRLLPFGAGRRVCPGAQLGINLVT 391
                         410       420
                  ....*....|....*....|....*...
gi 1039011928 514 MMLARLLQGFKWKLAGSET--RVELMES 539
Cdd:cd20656   392 LMLGHLLHHFSWTPPEGTPpeEIDMTEN 419
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
121-536 7.27e-68

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: 225.94  E-value: 7.27e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIvcpaRHRW----- 195
Cdd:cd11027     7 LYLGSRLVVVLNSGAAIKEALVKKSADFAGRPKLFTFDLFSRGGKDIAFGDYSPTWKLHRKLAHSAL----RLYAsggpr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 196 LHDNRAEETDHLTAWLynMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEadggptLEDIEHM-DAMFEGLGftf 274
Cdd:cd11027    83 LEEKIAEEAEKLLKRL--ASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPE------FLRLLDLnDKFFELLG--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 275 AFCISDYLPMLTGLDlNGHEKIMRESSAIMDKYHDPIIDERIKMWREGkrtQIEDFLDIFISIKDEA------GQPLLTA 348
Cdd:cd11027   152 AGSLLDIFPFLKYFP-NKALRELKELMKERDEILRKKLEEHKETFDPG---NIRDLTDALIKAKKEAedegdeDSGLLTD 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 349 DEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAF 428
Cdd:cd11027   228 DHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 429 NLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsEVTLTENDLRFISFSTGKRGCAAPALG 508
Cdd:cd11027   308 ALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDE--NGKLVPKPESFLPFSAGRRVCLGESLA 385
                         410       420
                  ....*....|....*....|....*...
gi 1039011928 509 TAITTMMLARLLQGFKWKLAGSETRVEL 536
Cdd:cd11027   386 KAELFLFLARLLQKFRFSPPEGEPPPEL 413
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
50-527 3.98e-61

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 209.93  E-value: 3.98e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  50 LLTTLQALAALCFLMILNKIKSSSRnkklhpLPPGPTGFPIVGMIPAMLKNRP---VFRwlhslMKELNTEIACVRLGNT 126
Cdd:PLN03234    4 FLIIAALVAAAAFFFLRSTTKKSLR------LPPGPKGLPIIGNLHQMEKFNPqhfLFR-----LSKLYGPIFTMKIGGR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 127 HVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDH 206
Cdd:PLN03234   73 RLAVISSAELAKELLKTQDLNFTARPLLKGQQTMSYQGRELGFGQYTAYYREMRKMCMVNLFSPNRVASFRPVREEECQR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 207 LTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEADggptlediEHMDAMFEGLGFTFAFCISDYLPMLT 286
Cdd:PLN03234  153 MMDKIYKAADQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMK--------RFIDILYETQALLGTLFFSDLFPYFG 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 287 GLD-LNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTqiEDFLDIFISI-KDEAGQPLLTADEIKPTIKELVMAAPD 364
Cdd:PLN03234  225 FLDnLTGLSARLKKAFKELDTYLQELLDETLDPNRPKQET--ESFIDLLMQIyKDQPFSIKFTHENVKAMILDIVVPGTD 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 365 NPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYH 444
Cdd:PLN03234  303 TAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYD 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 445 IPKGSQVLLSRYGLGRNPKVWSD-PLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGF 523
Cdd:PLN03234  383 IPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERFMKEHKGVDFKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKF 462

                  ....
gi 1039011928 524 KWKL 527
Cdd:PLN03234  463 DWSL 466
PLN02183 PLN02183
ferulate 5-hydroxylase
50-557 4.29e-61

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 210.48  E-value: 4.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  50 LLTTLQALAALCFLMILnkiksSSRNKKLHPLPPGPTGFPIVGMIPAMlkNRPVFRWLHSLMKELNTeIACVRLGNTHVI 129
Cdd:PLN02183   11 SPSFFLILISLFLFLGL-----ISRLRRRLPYPPGPKGLPIIGNMLMM--DQLTHRGLANLAKQYGG-LFHMRMGYLHMV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 130 PVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIvcparhrwLHDNRAEETDHLTA 209
Cdd:PLN02183   83 AVSSPEVARQVLQVQDSVFSNRPANIAISYLTYDRADMAFAHYGPFWRQMRKLCVMKL--------FSRKRAESWASVRD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 210 WLYNMVKN-----SEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEadggpTLEDIEHMDAMFEglgftfAFCISDYLPM 284
Cdd:PLN02183  155 EVDSMVRSvssniGKPVNIGELIFTLTRNITYRAAFGSSSNEGQDE-----FIKILQEFSKLFG------AFNVADFIPW 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 285 LTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWR--------EGKRTQIEDFLDIFIS--IKDEAGQPL-----LTAD 349
Cdd:PLN02183  224 LGWIDPQGLNKRLVKARKSLDGFIDDIIDDHIQKRKnqnadndsEEAETDMVDDLLAFYSeeAKVNESDDLqnsikLTRD 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 350 EIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFn 429
Cdd:PLN02183  304 NIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPL- 382
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 430 LPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLnECSEVTLTENDLRFISFSTGKRGCAAPALGT 509
Cdd:PLN02183  383 LLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFL-KPGVPDFKGSHFEFIPFGSGRRSCPGMQLGL 461
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039011928 510 AITTMMLARLLQGFKWKLAGSETRVELmeSSHDMF-LSKP----LVLVGELRL 557
Cdd:PLN02183  462 YALDLAVAHLLHCFTWELPDGMKPSEL--DMNDVFgLTAPratrLVAVPTYRL 512
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
121-535 1.44e-57

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: 198.57  E-value: 1.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTY-AQKILSNGYKTcVITPFGEQFKKMRKVImteivcparHRWLHDN 199
Cdd:cd11065     7 LKVGGQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPmAGELMGWGMRL-LLMPYGPRWRLHRRLF---------HQLLNPS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 200 RA--------EETDHLtawLYNMVKNsePVDLRFVTRHYCGNAIKRLMFGTRTfsektEADGGPTLEDIEHMDAMFEGLG 271
Cdd:cd11065    77 AVrkyrplqeLESKQL---LRDLLES--PDDFLDHIRRYAASIILRLAYGYRV-----PSYDDPLLRDAEEAMEGFSEAG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 272 FTFAFcISDYLPMLT---GLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQ--IEDFLDifisikDEAGQPLL 346
Cdd:cd11065   147 SPGAY-LVDFFPFLRylpSWLGAPWKRKARELRELTRRLYEGPFEAAKERMASGTATPsfVKDLLE------ELDKEGGL 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 347 TADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVA 426
Cdd:cd11065   220 SEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVA 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 427 AFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcSEVTLTENDLRFISFSTGKRGCAAPA 506
Cdd:cd11065   300 PLGIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDD-PKGTPDPPDPPHFAFGFGRRICPGRH 378
                         410       420
                  ....*....|....*....|....*....
gi 1039011928 507 LGTAITTMMLARLLQGFKWKLAGSETRVE 535
Cdd:cd11065   379 LAENSLFIAIARLLWAFDIKKPKDEGGKE 407
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
123-538 2.60e-57

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: 197.94  E-value: 2.60e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 123 LGNTHVIPVTCPKIAREIFKQqdALFASRPLT-YAQKILSN---GYktcviTPFGEQFKKMRKVIMTEIVCPARHRWLHD 198
Cdd:cd11076    10 LGETRVVITSHPETAREILNS--PAFADRPVKeSAYELMFNraiGF-----APYGEYWRNLRRIASNHLFSPRRIAASEP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 199 NRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEADGgptlEDIEHM-DAMFEGLGftfAFC 277
Cdd:cd11076    83 QRQAIAAQMVKAIAKEMERSGEVAVRKHLQRASLNNIMGSVFGRRYDFEAGNEEA----EELGEMvREGYELLG---AFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 278 ISDYLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERiKMWREGKRTQIEDFLDIFISIKdeaGQPLLTADEIKPTIKE 357
Cdd:cd11076   156 WSDHLPWLRWLDLQGIRRRCSALVPRVNTFVGKIIEEH-RAKRSNRARDDEDDVDVLLSLQ---GEEKLSDSDMIAVLWE 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 358 LVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAA-FNLPHVALS 436
Cdd:cd11076   232 MIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGPlLSWARLAIH 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 437 DTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECS--EVTLTENDLRFISFSTGKRGCAAPALGTAITTM 514
Cdd:cd11076   312 DVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGgaDVSVLGSDLRLAPFGAGRRVCPGKALGLATVHL 391
                         410       420
                  ....*....|....*....|....
gi 1039011928 515 MLARLLQGFKWKLAGSETrVELME 538
Cdd:cd11076   392 WVAQLLHEFEWLPDDAKP-VDLSE 414
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
50-523 7.81e-57

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 198.42  E-value: 7.81e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  50 LLTTLQALAALCFLMILNKIKSSSRNKKLHpLPPGPTGFPIVGmipamlknrpvfRWL-------HSLMKELNT---EIA 119
Cdd:PLN02394    1 LLLLEKTLLGLFVAIVLALLVSKLRGKKLK-LPPGPAAVPIFG------------NWLqvgddlnHRNLAEMAKkygDVF 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 120 CVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKvIMT------EIVCPARH 193
Cdd:PLN02394   68 LLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGDHWRKMRR-IMTvpfftnKVVQQYRY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 194 RWlhdnrAEETDHLtawLYNMVKNSEPVDLRFVTRH------YcgNAIKRLMFGTRTFSEKTeadggPTLEDIEHMDAMF 267
Cdd:PLN02394  147 GW-----EEEADLV---VEDVRANPEAATEGVVIRRrlqlmmY--NIMYRMMFDRRFESEDD-----PLFLKLKALNGER 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 268 EGLGFTFAFCISDYLPMLTGLdLNGHEKIMRE-SSAIMDKYHDPIIDERIK------MWREGKRTQIEDFLDIfiSIKDE 340
Cdd:PLN02394  212 SRLAQSFEYNYGDFIPILRPF-LRGYLKICQDvKERRLALFKDYFVDERKKlmsakgMDKEGLKCAIDHILEA--QKKGE 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 341 agqplLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAF 420
Cdd:PLN02394  289 -----INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETL 363
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 421 RLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKR 500
Cdd:PLN02394  364 RLHMAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAKVEANGNDFRFLPFGVGRR 443
                         490       500
                  ....*....|....*....|...
gi 1039011928 501 GCAAPALGTAITTMMLARLLQGF 523
Cdd:PLN02394  444 SCPGIILALPILGIVLGRLVQNF 466
PLN02966 PLN02966
cytochrome P450 83A1
56-527 4.36e-52

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 185.72  E-value: 4.36e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  56 ALAALCFLMILNKIKSssrnkKLHPLPPGPTGFPIVGMIPAMLKNRPVfRWLHSLMKELNTeIACVRLGNTHVIPVTCPK 135
Cdd:PLN02966   10 ALAAVLLFFLYQKPKT-----KRYKLPPGPSPLPVIGNLLQLQKLNPQ-RFFAGWAKKYGP-ILSYRIGSRTMVVISSAE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 136 IAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDHLTAWLYNMV 215
Cdd:PLN02966   83 LAKELLKTQDVNFADRPPHRGHEFISYGRRDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 216 KNSEPVDLRFVTRHYCGNAIKRLMFGtrtfsEKTEADGGPTLEDIEHMDAMFEGLGFTFafcISDYLPMLTGLD-LNGHE 294
Cdd:PLN02966  163 DKSEVVDISELMLTFTNSVVCRQAFG-----KKYNEDGEEMKRFIKILYGTQSVLGKIF---FSDFFPYCGFLDdLSGLT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 295 KIMRESSAIMDKYHDPIIDERIKMWRegKRTQIEDFLDIFISIKDEagQPL---LTADEIKPTIKELVMAAPDNPSNAVE 371
Cdd:PLN02966  235 AYMKECFERQDTYIQEVVNETLDPKR--VKPETESMIDLLMEIYKE--QPFaseFTVDNVKAVILDIVVAGTDTAAAAVV 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 372 WAIAEMINKPEILHKAMEEIdRVVGKER---FVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKG 448
Cdd:PLN02966  311 WGMTYLMKYPQVLKKAQAEV-REYMKEKgstFVTEDDVKNLPYFRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAG 389
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 449 SQVLLSRYGLGRNPKVWS-DPLSFKPERHLNEcsEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKL 527
Cdd:PLN02966  390 TTVNVNAWAVSRDEKEWGpNPDEFRPERFLEK--EVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFKL 467
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
118-531 7.47e-51

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: 179.63  E-value: 7.47e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 118 IACVRLGNTHVIPVTCPKIAREIFKQQDalFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLH 197
Cdd:cd00302     3 VFRVRLGGGPVVVVSDPELVREVLRDPR--DFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 198 DNRAEETDHLTAWLynmVKNSEPVDLRFVTRHYCGNAIKRLMFGTRtfsekteaDGGPTLEDIEHMDAMFEGLGftfafc 277
Cdd:cd00302    81 VIREIARELLDRLA---AGGEVGDDVADLAQPLALDVIARLLGGPD--------LGEDLEELAELLEALLKLLG------ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 278 isdylPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERikmwregkRTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKE 357
Cdd:cd00302   144 -----PRLLRPLPSPRLRRLRRARARLRDYLEELIARR--------RAEPADDLDLLLLADADDGGGL-SDEEIVAELLT 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 358 LVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKErfvQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVALSD 437
Cdd:cd00302   210 LLLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG---TPEDLSKLPYLEAVVEETLRLYPPVPL-LPRVATED 285
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 438 TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSevtltENDLRFISFSTGKRGCAAPALGTAITTMMLA 517
Cdd:cd00302   286 VELGGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPERE-----EPRYAHLPFGAGPHRCLGARLARLELKLALA 360
                         410
                  ....*....|....
gi 1039011928 518 RLLQGFKWKLAGSE 531
Cdd:cd00302   361 TLLRRFDFELVPDE 374
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
117-524 9.32e-51

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: 180.36  E-value: 9.32e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 117 EIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKvIMT------EIVCP 190
Cdd:cd11074     5 DIFLLRMGQRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFDIFTGKGQDMVFTVYGEHWRKMRR-IMTvpfftnKVVQQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 191 ARHRWlhdnrAEETDHLtawLYNMVKNSEPVDLRFVTRH------YcgNAIKRLMFGTRTFSEKTeadggPTLEDIEHMD 264
Cdd:cd11074    84 YRYGW-----EEEAARV---VEDVKKNPEAATEGIVIRRrlqlmmY--NNMYRIMFDRRFESEDD-----PLFVKLKALN 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 265 AMFEGLGFTFAFCISDYLPMLTGLdLNGHEKIMREssaIMDK----YHDPIIDERIK------MWREGKRTQIEDFLDif 334
Cdd:cd11074   149 GERSRLAQSFEYNYGDFIPILRPF-LRGYLKICKE---VKERrlqlFKDYFVDERKKlgstksTKNEGLKCAIDHILD-- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 335 isiKDEAGQplLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKA 414
Cdd:cd11074   223 ---AQKKGE--INEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQA 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 415 IIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFIS 494
Cdd:cd11074   298 VVKETLRLRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKVEANGNDFRYLP 377
                         410       420       430
                  ....*....|....*....|....*....|
gi 1039011928 495 FSTGKRGCAAPALGTAITTMMLARLLQGFK 524
Cdd:cd11074   378 FGVGRRSCPGIILALPILGITIGRLVQNFE 407
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
116-531 4.92e-47

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: 170.09  E-value: 4.92e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 116 TEIACVRLGNTHVIPVTCPKIAREIFKQQDalFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMteivcpaRHrw 195
Cdd:cd20651     1 GDVVGLKLGKDKVVVVSGYEAVREVLSREE--FDGRPDGFFFRLRTFGKRLGITFTDGPFWKEQRRFVL-------RH-- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 196 LHD---NRA-------EETDHLTAWLYNMVKNSEPVDLRFVTrhYCGNAIKRLMFGTRtFSEkteaDGGPTLEDIEHMDA 265
Cdd:cd20651    70 LRDfgfGRRsmeeviqEEAEELIDLLKKGEKGPIQMPDLFNV--SVLNVLWAMVAGER-YSL----EDQKLRKLLELVHL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 266 MFEGlgFTFAFCISDYLPMLTGL--DLNGHeKIMRESSAIMDKYHDPIIDERIKMWREGkrtQIEDFLDIFIS--IKDEA 341
Cdd:cd20651   143 LFRN--FDMSGGLLNQFPWLRFIapEFSGY-NLLVELNQKLIEFLKEEIKEHKKTYDED---NPRDLIDAYLRemKKKEP 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 342 GQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFR 421
Cdd:cd20651   217 PSSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLR 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 422 LHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsEVTLTENDlRFISFSTGKRG 501
Cdd:cd20651   297 IFTLVPIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDE--DGKLLKDE-WFLPFGAGKRR 373
                         410       420       430
                  ....*....|....*....|....*....|
gi 1039011928 502 CAAPALGTAITTMMLARLLQGFKWKLAGSE 531
Cdd:cd20651   374 CLGESLARNELFLFFTGLLQNFTFSPPNGS 403
PTZ00404 PTZ00404
cytochrome P450; Provisional
48-526 2.15e-44

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 164.13  E-value: 2.15e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  48 MYLLTTLQALaaLCFLMILNKIKsssRNKKLHPLP-PGPTGFPIVGMIpAMLKNRPVFRWlhSLMKELNTEIACVRLGNT 126
Cdd:PTZ00404    1 MMLFNIILFL--FIFYIIHNAYK---KYKKIHKNElKGPIPIPILGNL-HQLGNLPHRDL--TKMSKKYGGIFRIWFADL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 127 HVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTcvITPFGEQFKKMRkvimtEIVCPARHR----WLHDNRAE 202
Cdd:PTZ00404   73 YTVVLSDPILIREMFVDNFDNFSDRPKIPSIKHGTFYHGI--VTSSGEYWKRNR-----EIVGKAMRKtnlkHIYDLLDD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 203 ETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFgTRTFSEKTEADGGPTLEDIEHMDAMFEGLGFTFAFcisDYL 282
Cdd:PTZ00404  146 QVDVLIESMKKIESSGETFEPRYYLTKFTMSAMFKYIF-NEDISFDEDIHNGKLAELMGPMEQVFKDLGSGSLF---DVI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 283 PMLTGLDLNGHEKIMRESSAIMdKYHDPIIDERIKMWR-EGKRtqieDFLDIFIS-IKDEAGQPLLTadeIKPTIKELVM 360
Cdd:PTZ00404  222 EITQPLYYQYLEHTDKNFKKIK-KFIKEKYHEHLKTIDpEVPR----DLLDLLIKeYGTNTDDDILS---ILATILDFFL 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 361 AAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTV 440
Cdd:PTZ00404  294 AGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPFGLPRSTSNDIII 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 441 A-GYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNecsevtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARL 519
Cdd:PTZ00404  374 GgGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLN-------PDSNDAFMPFSIGPRNCVGQQFAQDELYLAFSNI 446

                  ....*..
gi 1039011928 520 LQGFKWK 526
Cdd:PTZ00404  447 ILNFKLK 453
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
120-502 1.61e-43

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: 160.54  E-value: 1.61e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 120 CVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGyKTCVITPFGEQFKKMRKVIMTEI---VCPARHRWL 196
Cdd:cd11028     6 QIRMGSRPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFISNG-KSMAFSDYGPRWKLHRKLAQNALrtfSNARTHNPL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 197 HDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTfsektEADGGPTLEDIEHMDamfEGLGFTFAF 276
Cdd:cd11028    85 EEHVTEEAEELVTELTENNGKPGPFDPRNEIYLSVGNVICAICFGKRY-----SRDDPEFLELVKSND---DFGAFVGAG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 277 CISDYLPMLTGL---DLNGHEKIMRESSAIMDKYhdpiIDERIKMWREGkrtQIEDFLDIFISI-----KDEAGQPLLTA 348
Cdd:cd11028   157 NPVDVMPWLRYLtrrKLQKFKELLNRLNSFILKK----VKEHLDTYDKG---HIRDITDALIKAseekpEEEKPEVGLTD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 349 DEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAF 428
Cdd:cd11028   230 EHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPF 309
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039011928 429 NLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDlRFISFSTGKRGC 502
Cdd:cd11028   310 TIPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLDKTKVD-KFLPFGAGRRRC 382
PLN02655 PLN02655
ent-kaurene oxidase
87-537 6.63e-40

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 151.43  E-value: 6.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  87 GFPIVGMIPAMLKNRP---VFRWlhslmKELNTEIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNG 163
Cdd:PLN02655    6 GLPVIGNLLQLKEKKPhrtFTKW-----SEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSKALTVLTRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 164 YKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDHLTAWLYNMVKNS--EPVDLRFVtrhycgnaIKRLMFG 241
Cdd:PLN02655   81 KSMVATSDYGDFHKMVKRYVMNNLLGANAQKRFRDTRDMLIENMLSGLHALVKDDphSPVNFRDV--------FENELFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 242 ---TRTFSEKTEADGGPTLEDIEHMDAMFEGLGFTFAFCI-----SDYLPMLTGLDLNGHEKIMRES----SAIMDKYhd 309
Cdd:PLN02655  153 lslIQALGEDVESVYVEELGTEISKEEIFDVLVHDMMMCAievdwRDFFPYLSWIPNKSFETRVQTTefrrTAVMKAL-- 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 310 pIIDERIKMWREGKRTQIEDFLdifisiKDEAGQplLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAME 389
Cdd:PLN02655  231 -IKQQKKRIARGEERDCYLDFL------LSEATH--LTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYR 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 390 EIDRVVGKERfVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPL 469
Cdd:PLN02655  302 EIREVCGDER-VTEEDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPE 380
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 470 SFKPERHLNECSEVTltenDL-RFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKL-AGSETRVELM 537
Cdd:PLN02655  381 EWDPERFLGEKYESA----DMyKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWRLrEGDEEKEDTV 446
PLN00168 PLN00168
Cytochrome P450; Provisional
51-549 4.00e-38

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 147.40  E-value: 4.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  51 LTTLQALAALCFLMILNKIKSSSRNKKLHPLPPGPTGFPIVG----MIPAMLKNRPVFRWLHslmkELNTEIACVRLGNT 126
Cdd:PLN00168    6 LLLLAALLLLPLLLLLLGKHGGRGGKKGRRLPPGPPAVPLLGslvwLTNSSADVEPLLRRLI----ARYGPVVSLRVGSR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 127 HVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEETDH 206
Cdd:PLN00168   82 LSVFVADRRLAHAALVERGAALADRPAVASSRLLGESDNTITRSSYGPVWRLLRRNLVAETLHPSRVRLFAPARAWVRRV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 207 LTAWLYnmvKNSEPVDLRFV--TRHYCGNAIKRLM-FGTRTfsekteadGGPTLEDIEhmDAMFEGLGFT------FAFc 277
Cdd:PLN00168  162 LVDKLR---REAEDAAAPRVveTFQYAMFCLLVLMcFGERL--------DEPAVRAIA--AAQRDWLLYVskkmsvFAF- 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 278 isdyLPMLTGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQ-------------IEDFLDIfiSIKDEAGQP 344
Cdd:PLN00168  228 ----FPAVTKHLFRGRLQKALALRRRQKELFVPLIDARREYKNHLGQGGeppkkettfehsyVDTLLDI--RLPEDGDRA 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 345 LlTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVG-KERFVQESDIPKLNYVKAIIREAFRLH 423
Cdd:PLN00168  302 L-TDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGdDQEEVSEEDVHKMPYLKAVVLEGLRKH 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 424 PVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHL----NECSEVTLTEnDLRFISFSTGK 499
Cdd:PLN00168  381 PPAHFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLaggdGEGVDVTGSR-EIRMMPFGVGR 459
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039011928 500 RGCaaPALGTAITTM--MLARLLQGFKWK-LAGSEtrVELMESSH-DMFLSKPL 549
Cdd:PLN00168  460 RIC--AGLGIAMLHLeyFVANMVREFEWKeVPGDE--VDFAEKREfTTVMAKPL 509
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
117-523 1.43e-36

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: 141.30  E-value: 1.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 117 EIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMT----------- 185
Cdd:cd20673     3 PIYSLRMGSHTTVIVGHHQLAKEVLLKKGKEFSGRPRMVTTDLLSRNGKDIAFADYSATWQLHRKLVHSafalfgegsqk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 186 --EIVCparhrwlhdnraEETDHLTAWLYNmvKNSEPVDLRFVTRHYCGNAIKRLMFGTRtFSEkteadGGPTLEDIEHM 263
Cdd:cd20673    83 leKIIC------------QEASSLCDTLAT--HNGESIDLSPPLFRAVTNVICLLCFNSS-YKN-----GDPELETILNY 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 264 DamfEGLGFTFAF-CISDYLPMLTGLDlNGHEKIMRESSAIMDKYHDPIIDERIKMWREGkrtQIEDFLDIFISIKDEA- 341
Cdd:cd20673   143 N---EGIVDTVAKdSLVDIFPWLQIFP-NKDLEKLKQCVKIRDKLLQKKLEEHKEKFSSD---SIRDLLDALLQAKMNAe 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 342 --------GQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVK 413
Cdd:cd20673   216 nnnagpdqDSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLE 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 414 AIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcSEVTLTENDLRFI 493
Cdd:cd20673   296 ATIREVLRIRPVAPLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDP-TGSQLISPSLSYL 374
                         410       420       430
                  ....*....|....*....|....*....|
gi 1039011928 494 SFSTGKRGCAAPALGTAITTMMLARLLQGF 523
Cdd:cd20673   375 PFGAGPRVCLGEALARQELFLFMAWLLQRF 404
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
118-524 9.77e-36

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: 138.70  E-value: 9.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 118 IACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTEIV-CPARHrwL 196
Cdd:cd20674     4 IYRLRLGLQDVVVLNSKRTIREALVRKWADFAGRPHSYTGKLVSQGGQDLSLGDYSLLWKAHRKLTRSALQlGIRNS--L 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 197 HDNRAEETDHLTAWLynMVKNSEPVDL-RFVTRHYCgNAIKRLMFGTrTFSEKTEAdggPTLED-IEHMDAMFEGLGFTf 274
Cdd:cd20674    82 EPVVEQLTQELCERM--RAQAGTPVDIqEEFSLLTC-SIICCLTFGD-KEDKDTLV---QAFHDcVQELLKTWGHWSIQ- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 275 afcISDYLPMLTGLDLNGHEKIMRESsaimdKYHDPIIDERIKMWREGKRT-QIEDFLDIFISI----KDEAGQPLLTAD 349
Cdd:cd20674   154 ---ALDSIPFLRFFPNPGLRRLKQAV-----ENRDHIVESQLRQHKESLVAgQWRDMTDYMLQGlgqpRGEKGMGQLLEG 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 350 EIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFN 429
Cdd:cd20674   226 HVHMAVVDLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLA 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 430 LPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsevtlTENDLRFISFSTGKRGCAAPALGT 509
Cdd:cd20674   306 LPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEP------GAANRALLPFGCGARVCLGEPLAR 379
                         410
                  ....*....|....*
gi 1039011928 510 AITTMMLARLLQGFK 524
Cdd:cd20674   380 LELFVFLARLLQAFT 394
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
118-531 1.54e-35

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: 138.04  E-value: 1.54e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 118 IACVRLGNTHVIPVTCPKIAREIFKQQDAlFASRPLTYAQKI--LSNGYKTCVITPFGEQFKKMRKVIMTEIVCPaRHRW 195
Cdd:cd11054     7 IVREKLGGRDIVHLFDPDDIEKVFRNEGK-YPIRPSLEPLEKyrKKRGKPLGLLNSNGEEWHRLRSAVQKPLLRP-KSVA 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 196 LHDNRAEE-TDHLTAWLYNM--VKNSEPVDLRFVTRHYCGNAIKRLMFGTR--TFSEKTEADggpTLEDIEHMDAMFE-- 268
Cdd:cd11054    85 SYLPAINEvADDFVERIRRLrdEDGEEVPDLEDELYKWSLESIGTVLFGKRlgCLDDNPDSD---AQKLIEAVKDIFEss 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 269 -GLGFTFAFcisdYLPMLTGLdLNGHEKIMRESSAIMDKYhdpiIDERIK--MWREGKRTQIEDFLDIFISIKDeagqpl 345
Cdd:cd11054   162 aKLMFGPPL----WKYFPTPA-WKKFVKAWDTIFDIASKY----VDEALEelKKKDEEDEEEDSLLEYLLSKPG------ 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 346 LTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPV 425
Cdd:cd11054   227 LSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPV 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 426 AAFN---LPHvalsDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcSEVTLTENDLRFISFSTGKRGC 502
Cdd:cd11054   307 APGNgriLPK----DIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRD-DSENKNIHPFASLPFGFGPRMC 381
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1039011928 503 aapaLG--TAITTM--MLARLLQGFKWKLAGSE 531
Cdd:cd11054   382 ----IGrrFAELEMylLLAKLLQNFKVEYHHEE 410
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
276-537 4.96e-35

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: 136.88  E-value: 4.96e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 276 FCISDYLPMLTGLdlnghEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIED----------FLDIFISIKDEAGQpl 345
Cdd:cd20628   152 WLRFDFIFRLTSL-----GKEQRKALKVLHDFTNKVIKERREELKAEKRNSEEDdefgkkkrkaFLDLLLEAHEDGGP-- 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 346 LTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGK-ERFVQESDIPKLNYVKAIIREAFRLHP 424
Cdd:cd20628   225 LTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGDdDRRPTLEDLNKMKYLERVIKETLRLYP 304
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 425 VAAFnLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSevtltenDLR----FISFSTGKR 500
Cdd:cd20628   305 SVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENS-------AKRhpyaYIPFSAGPR 376
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1039011928 501 GCaapaLGT--AITTM--MLARLLQGFKWKLAGSETRVELM 537
Cdd:cd20628   377 NC----IGQkfAMLEMktLLAKILRNFRVLPVPPGEDLKLI 413
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
117-532 1.11e-34

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: 135.40  E-value: 1.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 117 EIACVRLGNTHVIPVTCPKIAREIFKQQDALFA-SRPLTYAQKILSNGyktcVITPFGEQFKKMRKVI------------ 183
Cdd:cd20620     2 DVVRLRLGPRRVYLVTHPDHIQHVLVTNARNYVkGGVYERLKLLLGNG----LLTSEGDLWRRQRRLAqpafhrrriaay 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 184 ---MTEIVCPARHRWLHDNRAEETD------HLTawlynmvknsepvdLRFVTRhycgnaikrLMFGTRTfSEKTEAdGG 254
Cdd:cd20620    78 adaMVEATAALLDRWEAGARRGPVDvhaemmRLT--------------LRIVAK---------TLFGTDV-EGEADE-IG 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 255 PTLEDIEHMdAMFEGLGFtfafcISDYLPMLTGLDLNghekiMRESSAIMDKYHDPIIDERikmwREGKRTQiEDFLD-I 333
Cdd:cd20620   133 DALDVALEY-AARRMLSP-----FLLPLWLPTPANRR-----FRRARRRLDEVIYRLIAER----RAAPADG-GDLLSmL 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 334 FISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKeRFVQESDIPKLNYVK 413
Cdd:cd20620   197 LAARDEETGEPM-SDQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGG-RPPTAEDLPQLPYTE 274
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 414 AIIREAFRLHPvAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsevtLTENDLRF- 492
Cdd:cd20620   275 MVLQESLRLYP-PAWIIGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPE-----REAARPRYa 348
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1039011928 493 -ISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSET 532
Cdd:cd20620   349 yFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPGQP 389
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
121-528 1.52e-32

cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including insect cytochrome P450 306A1 (CYP306A1 or Cyp306a1) and CYP18A1. CYP306A1 functions as a carbon 25-hydroxylase and has an essential role in ecdysteroid biosynthesis during insect development. CYP18A1 is a 26-hydroxylase and plays a key role in steroid hormone inactivation. The CYP306A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 129.84  E-value: 1.52e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQdaLFASRPLTYAQKILSNGYKtcVITPFGEQFKKMRKVI--------MTEIvCPAR 192
Cdd:cd20652     6 LKMGSVYTVVLSDPKLIRDTFRRD--EFTGRAPLYLTHGIMGGNG--IICAEGDLWRDQRRFVhdwlrqfgMTKF-GNGR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 193 HRwLHDNRAEETDHLTAwlyNMVKNSE-PVDLRFVTRHYCGNAIKRLMFGTRtFSEKTeadggPTLEDIEHMDAmfEGLG 271
Cdd:cd20652    81 AK-MEKRIATGVHELIK---HLKAESGqPVDPSPVLMHSLGNVINDLVFGFR-YKEDD-----PTWRWLRFLQE--EGTK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 272 FTFAFCISDYLPMLTGLDLNGHE-KIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFI--------SIKDEAG 342
Cdd:cd20652   149 LIGVAGPVNFLPFLRHLPSYKKAiEFLVQGQAKTHAIYQKIIDEHKRRLKPENPRDAEDFELCELekakkegeDRDLFDG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 343 qpLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRL 422
Cdd:cd20652   229 --FYTDEQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRI 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 423 HPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTEndlRFISFSTGKRGC 502
Cdd:cd20652   307 RSVVPLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPE---AFIPFQTGKRMC 383
                         410       420
                  ....*....|....*....|....*.
gi 1039011928 503 AAPALGTAITTMMLARLLQGFKWKLA 528
Cdd:cd20652   384 LGDELARMILFLFTARILRKFRIALP 409
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
304-524 1.38e-31

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: 126.99  E-value: 1.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 304 MDKYHDPIIDERIK-MWREGKRTQIEDFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPE 382
Cdd:cd20621   182 LRQFIEKIIQNRIKqIKKNKDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPE 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 383 ILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNP 462
Cdd:cd20621   262 IQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNP 341
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039011928 463 KVWSDPLSFKPERHLNecsEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFK 524
Cdd:cd20621   342 KYFENPDEFNPERWLN---QNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFE 400
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
121-526 8.33e-31

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: 124.52  E-value: 8.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNgyKTCVITPFGEQFKKMRKVIMTEIvcpaRH-----RW 195
Cdd:cd20662     7 LQLGSISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFN--KNGLIFSSGQTWKEQRRFALMTL----RNfglgkKS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 196 LHDNRAEETDHLTAWLYNmvKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEADGGPTLEDiEHMDAMFEGLGFTFA 275
Cdd:cd20662    81 LEERIQEECRHLVEAIRE--EKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLD-ETVYLEGSPMSQLYN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 276 F--CISDYLPmltgldlNGHEKIMRESSAIMDKYHDPIIDERiKMWREgkrTQIEDFLDIFIS--IKDEAGQPLLTADEI 351
Cdd:cd20662   158 AfpWIMKYLP-------GSHQTVFSNWKKLKLFVSDMIDKHR-EDWNP---DEPRDFIDAYLKemAKYPDPTTSFNEENL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 352 KPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLP 431
Cdd:cd20662   227 ICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLNVP 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 432 HVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPErHLNECSEVTLTENdlrFISFSTGKRGCAAPALGTAI 511
Cdd:cd20662   307 REVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPG-HFLENGQFKKREA---FLPFSMGKRACLGEQLARSE 382
                         410
                  ....*....|....*
gi 1039011928 512 TTMMLARLLQGFKWK 526
Cdd:cd20662   383 LFIFFTSLLQKFTFK 397
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
213-502 2.27e-30

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: 123.47  E-value: 2.27e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 213 NMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTfseKTEADGGPTLEDIEHMDAMFEGLGFTFAFcisdylPM----LTGL 288
Cdd:cd11064    97 HAAESGKVVDLQDVLQRFTFDVICKIAFGVDP---GSLSPSLPEVPFAKAFDDASEAVAKRFIV------PPwlwkLKRW 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 289 dLN-GHEKIMRESSAIMDKYHDPIIDERI--KMWREGKRTQIEDFLDIFISiKDEAGQPLLTADEIKPTIKELVMAAPDN 365
Cdd:cd11064   168 -LNiGSEKKLREAIRVIDDFVYEVISRRReeLNSREEENNVREDLLSRFLA-SEEEEGEPVSDKFLRDIVLNFILAGRDT 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 366 PSNAVEWAIAEMINKPEILHKAMEEIDRVV-----GKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTV 440
Cdd:cd11064   246 TAAALTWFFWLLSKNPRVEEKIREELKSKLpklttDESRVPTYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLP 325
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011928 441 AGYHIPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNEcSEVTLTENDLRFISFSTGKRGC 502
Cdd:cd11064   326 DGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDE-DGGLRPESPYKFPAFNAGPRIC 387
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
123-528 3.01e-30

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: 122.96  E-value: 3.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 123 LGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGyKTCVITPFGEQFKKMRKVIMTEIvcpaRHRWL--HDNR 200
Cdd:cd20666     9 IGSQLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKG-KGIVFAPYGPVWRQQRKFSHSTL----RHFGLgkLSLE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 201 AEETDHLTAWLYNMVKNSE-PVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEADggpTLediehMDAMFEGL-----GFTF 274
Cdd:cd20666    84 PKIIEEFRYVKAEMLKHGGdPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFK---TM-----LGLMSRGLeisvnSAAI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 275 AFCISDYLPMLTGLDLNGHEKIMRESSAIMDKYhdpIIDERIKMWREGKRtqieDFLDI-FISIKDE---AGQPLLTADE 350
Cdd:cd20666   156 LVNICPWLYYLPFGPFRELRQIEKDITAFLKKI---IADHRETLDPANPR----DFIDMyLLHIEEEqknNAESSFNEDY 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 351 IKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNL 430
Cdd:cd20666   229 LFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSI 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 431 PHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENdlrFISFSTGKRGCAAPALGTA 510
Cdd:cd20666   309 PHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEA---FIPFGIGRRVCMGEQLAKM 385
                         410
                  ....*....|....*...
gi 1039011928 511 ITTMMLARLLQGFKWKLA 528
Cdd:cd20666   386 ELFLMFVSLMQSFTFLLP 403
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
292-527 7.35e-30

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: 121.86  E-value: 7.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 292 GHEKIMRESSAIMDKYHDP--IIDERIKMWREGKRTQIEDFLDIFIS--IkdeAGQplltadeikptikelvmaapDNPS 367
Cdd:cd20613   195 GRECIEERLEALKRGEEVPndILTHILKASEEEPDFDMEELLDDFVTffI---AGQ--------------------ETTA 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 368 NAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVAlSDTTVAGYHIPK 447
Cdd:cd20613   252 NLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELT-KDIELGGYKIPA 330
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 448 GSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsevtltENDLR----FISFSTGKRGCaapaLGTAITTM----MLARL 519
Cdd:cd20613   331 GTTVLVSTYVMGRMEEYFEDPLKFDPERFSPE-------APEKIpsyaYFPFSLGPRSC----IGQQFAQIeakvILAKL 399

                  ....*...
gi 1039011928 520 LQGFKWKL 527
Cdd:cd20613   400 LQNFKFEL 407
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
134-528 1.43e-29

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: 120.77  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 134 PKIAREIFKQQDALFASRPLT-YAQKILsnGyKTCVITPFGEQFKKMRKVIMteivcPArhrwLHDNR--------AEET 204
Cdd:cd11053    31 PEAIKQIFTADPDVLHPGEGNsLLEPLL--G-PNSLLLLDGDRHRRRRKLLM-----PA----FHGERlraygeliAEIT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 205 DHLTA-WLYNmvknsEPVDLRFVTRHYCGNAIKRLMFGtrtfsekteADGGPTLEDIEH-MDAMFEGLGFTFAFCISdYL 282
Cdd:cd11053    99 EREIDrWPPG-----QPFDLRELMQEITLEVILRVVFG---------VDDGERLQELRRlLPRLLDLLSSPLASFPA-LQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 283 PMLTGLDLNGheKIMRESSAIMDKYHDpIIDERikmwREGKRTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAA 362
Cdd:cd11053   164 RDLGPWSPWG--RFLRARRRIDALIYA-EIAER----RAEPDAERDDILSLLLSARDEDGQPL-SDEELRDELMTLLFAG 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 363 PDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKErfvQESDIPKLNYVKAIIREAFRLHPVAaFNLPHVALSDTTVAG 442
Cdd:cd11053   236 HETTATALAWAFYWLHRHPEVLARLLAELDALGGDP---DPEDIAKLPYLDAVIKETLRLYPVA-PLVPRRVKEPVELGG 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 443 YHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsEVTLTEndlrFISFSTGKRGCAAPALGTAITTMMLARLLQG 522
Cdd:cd11053   312 YTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGR--KPSPYE----YLPFGGGVRRCIGAAFALLEMKVVLATLLRR 385

                  ....*.
gi 1039011928 523 FKWKLA 528
Cdd:cd11053   386 FRLELT 391
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
281-521 1.51e-29

cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists of two human members, CYP1A1 and CYP1A2, which overlap in their activities. CYP1A2 is the highly expressed cytochrome enzyme in the human liver, while CYP1A1 is mostly found in extrahepatic tissues. Known common substrates include aromatic compounds such as polycyclic aromatic hydrocarbons, arachidonic acid and eicosapentoic acid, as well as melatonin and 6-hydroxylate melatonin. In addition, CYP1A1 activates procarcinogens into carcinogens via epoxides, and metabolizes heterocyclic aromatic amines of industrial origin. CYP1A2 metabolizes numerous natural products that result in toxic products, such as the transformation of methyleugenol to 1'-hydroxymethyleugenol, estragole to reactive metabolites, and oxidation of nephrotoxins. It also plays an important role in the metabolism of several clinical drugs including analgesics, antipyretics, antipsychotics, antidepressants, anti-inflammatory, and cardiovascular drugs. The CYP1A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 121.27  E-value: 1.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 281 YLP---MLTGLDLNGH-----EKIMRESSAIMDKYH--DpIIDERIKMWREGKRtqiedfldifisikDEAGQPLLTADE 350
Cdd:cd20676   173 YLPnpaMKRFKDINKRfnsflQKIVKEHYQTFDKDNirD-ITDSLIEHCQDKKL--------------DENANIQLSDEK 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 351 IKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNL 430
Cdd:cd20676   238 IVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRHSSFVPFTI 317
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 431 PHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLN-ECSEVTLTENDlRFISFSTGKRGCAAPALGT 509
Cdd:cd20676   318 PHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTaDGTEINKTESE-KVMLFGLGKRRCIGESIAR 396
                         250
                  ....*....|..
gi 1039011928 510 AITTMMLARLLQ 521
Cdd:cd20676   397 WEVFLFLAILLQ 408
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
121-527 2.39e-29

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: 120.06  E-value: 2.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFkQQDALFASRPLTY--AQKILSNGYKTCVitpfGEQFKKMRKVIMteivcPARHR---- 194
Cdd:cd11049    18 IRLGPRPAYVVTSPELVRQVL-VNDRVFDKGGPLFdrARPLLGNGLATCP----GEDHRRQRRLMQ-----PAFHRsrip 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 195 -WLHDNRAEETDHLTAWlynmvKNSEPVDLRFVTRHYCGNAIKRLMFGTRtfsekteaDGGPTLEDIEH-MDAMFEGLgF 272
Cdd:cd11049    88 aYAEVMREEAEALAGSW-----RPGRVVDVDAEMHRLTLRVVARTLFSTD--------LGPEAAAELRQaLPVVLAGM-L 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 273 TFAFcisdYLPMLTGLDLNGHEkimRESSAIMDkYHDpIIDERIKMWREGKRTQiEDFLDIFISIKDEAGQPLlTADEIK 352
Cdd:cd11049   154 RRAV----PPKFLERLPTPGNR---RFDRALAR-LRE-LVDEIIAEYRASGTDR-DDLLSLLLAARDEEGRPL-SDEELR 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 353 PTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKeRFVQESDIPKLNYVKAIIREAFRLHPvAAFNLPH 432
Cdd:cd11049   223 DQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLGG-RPATFEDLPRLTYTRRVVTEALRLYP-PVWLLTR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 433 VALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtltenDLR---FISFSTGKRGCAAPALGT 509
Cdd:cd11049   301 RTTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAA------AVPrgaFIPFGAGARKCIGDTFAL 374
                         410
                  ....*....|....*...
gi 1039011928 510 AITTMMLARLLQgfKWKL 527
Cdd:cd11049   375 TELTLALATIAS--RWRL 390
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
311-536 8.22e-29

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: 118.84  E-value: 8.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 311 IIDERikmwREGKRTQIEDFLDIFISIKD---EAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKA 387
Cdd:cd11055   188 IIEQR----RKNKSSRRKDLLQLMLDAQDsdeDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKL 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 388 MEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLpHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSD 467
Cdd:cd11055   264 IEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFIS-RECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPD 342
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011928 468 PLSFKPERHLNEcsevtltENDLR----FISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKlAGSETRVEL 536
Cdd:cd11055   343 PEKFDPERFSPE-------NKAKRhpyaYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFV-PCKETEIPL 407
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
303-536 1.13e-28

cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). Members of the CYP97 clan include Arabidopsis thaliana cytochrome P450s 97A3 (CYP97A3), CYP97B3, and CYP97C1. CYP97A3 is also called protein LUTEIN DEFICIENT 5 (LUT5) and CYP97C1 is also called carotene epsilon-monooxygenase or protein LUTEIN DEFICIENT 1 (LUT1). These cytochromes function as beta- and epsilon-ring carotenoid hydroxylases and are involved in the biosynthesis of xanthophylls. CYP97 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410672 [Multi-domain]  Cd Length: 441  Bit Score: 118.62  E-value: 1.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 303 IMDKYHDPIIDERikmWREGKRTQIEDFLDIFISIKD--------EAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAI 374
Cdd:cd11046   188 LLNDTLDDLIRKR---KEMRQEEDIELQQEDYLNEDDpsllrflvDMRDEDVDSKQLRDDLMTMLIAGHETTAAVLTWTL 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 375 AEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYH--IPKGSQVL 452
Cdd:cd11046   265 YELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPV-LIRRAVEDDKLPGGGvkVPAGTDIF 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 453 LSRYGLGRNPKVWSDPLSFKPERHL----NECSEVTlteNDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLA 528
Cdd:cd11046   344 ISVYNLHRSPELWEDPEEFDPERFLdpfiNPPNEVI---DDFAFLPFGGGPRKCLGDQFALLEATVALAMLLRRFDFELD 420

                  ....*...
gi 1039011928 529 GSETRVEL 536
Cdd:cd11046   421 VGPRHVGM 428
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
327-502 2.07e-28

cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome P450 1B1 (CYP1B1) is expressed in liver and extrahepatic tissues where it carries out the metabolism of numerous xenobiotics, including metabolic activation of polycyclic aromatic hydrocarbons. It is also important in regulating endogenous metabolic pathways, including the metabolism of steroid hormones, fatty acids, melatonin, and vitamins. CYP1B1 is overexpressed in a wide variety of tumors and is associated with angiogenesis. It is also associated with adipogenesis, obesity, hypertension, and atherosclerosis. It is therefore a target for the treatment of metabolic diseases and cancer. Also included in this subfamily are CYP1C proteins from fish, birds and amphibians. The CYP1B1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 117.80  E-value: 2.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 327 IEDFLDIFISIKDEAGQ----PLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQ 402
Cdd:cd20675   208 PRDMMDAFILALEKGKSgdsgVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPC 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 403 ESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSE 482
Cdd:cd20675   288 IEDQPNLPYVMAFLYEAMRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGF 367
                         170       180
                  ....*....|....*....|..
gi 1039011928 483 VtltENDL--RFISFSTGKRGC 502
Cdd:cd20675   368 L---NKDLasSVMIFSVGKRRC 386
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
306-524 2.44e-28

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: 117.27  E-value: 2.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 306 KYHDPIIDERIKMWREGKRTQIE-----DFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINK 380
Cdd:cd20659   179 KFAEEIIKKRRKELEDNKDEALSkrkylDFLDILLTARDEDGKGL-TDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKH 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 381 PEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPvAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGR 460
Cdd:cd20659   258 PEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYP-PVPFIARTLTKPITIDGVTLPAGTLIAINIYALHH 336
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039011928 461 NPKVWSDPLSFKPERHlnecsevtLTENDLR-----FISFSTGKRGCAAPALGTAITTMMLARLLQGFK 524
Cdd:cd20659   337 NPTVWEDPEEFDPERF--------LPENIKKrdpfaFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFE 397
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
121-536 2.47e-28

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: 117.28  E-value: 2.47e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKtcVITPFGEQFKKMRKVIMTEIvcpaRH-----RW 195
Cdd:cd11026     7 VYLGSKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYG--VVFSNGERWKQLRRFSLTTL----RNfgmgkRS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 196 LHDNRAEETDHLTAWLYNmvKNSEPVDLRFVTRHYCGNAIKRLMFGTRtFSEKTeadggPTLEDIehMDAMFEGLGFTFA 275
Cdd:cd11026    81 IEERIQEEAKFLVEAFRK--TKGKPFDPTFLLSNAVSNVICSIVFGSR-FDYED-----KEFLKL--LDLINENLRLLSS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 276 FCISDY------LPMLTGLdlngHEKIMRESSAIMDkyhdpIIDERIKMWREG-KRTQIEDFLDIF-ISIKDEAGQPLLT 347
Cdd:cd11026   151 PWGQLYnmfpplLKHLPGP----HQKLFRNVEEIKS-----FIRELVEEHRETlDPSSPRDFIDCFlLKMEKEKDNPNSE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 348 ADE--IKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPV 425
Cdd:cd11026   222 FHEenLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDI 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 426 AAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtLTENDlRFISFSTGKRGCaap 505
Cdd:cd11026   302 VPLGVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGK--FKKNE-AFMPFSAGKRVC--- 375
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1039011928 506 aLGTAITTMML----ARLLQGFKWKLAGSETRVEL 536
Cdd:cd11026   376 -LGEGLARMELflffTSLLQRFSLSSPVGPKDPDL 409
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
131-528 3.58e-28

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: 116.99  E-value: 3.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 131 VTCPKIAREIFKQQDALFASRPL--TYAQKILSNGyktcVITPFGEQFKKMRKVIMteivcPA---RH-RWLHD---NRA 201
Cdd:cd11069    18 VTDPKALKHILVTNSYDFEKPPAfrRLLRRILGDG----LLAAEGEEHKRQRKILN-----PAfsyRHvKELYPifwSKA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 202 EEtdhLTAWLYNMVKNSEPVDLRFVTRHYCG----NAIkrlmfGTRTFSEKTEADGGPTLEDIEHMDAMFEG-------- 269
Cdd:cd11069    89 EE---LVDKLEEEIEESGDESISIDVLEWLSratlDII-----GLAGFGYDFDSLENPDNELAEAYRRLFEPtllgsllf 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 270 -LGFTFAFCISDYLPmltgldlNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQPLLTA 348
Cdd:cd11069   161 iLLLFLPRWLVRILP-------WKANREIRRAKDVLRRLAREIIREKKAALLEGKDDSGKDILSILLRANDFADDERLSD 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 349 DEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVV--GKERFVQESDIPKLNYVKAIIREAFRLHPVA 426
Cdd:cd11069   234 EELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALpdPPDGDLSYDDLDRLPYLNAVCRETLRLYPPV 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 427 AFnLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNECSEVTLTENDL--RFISFSTGKRGCa 503
Cdd:cd11069   314 PL-TSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASPGGAGSnyALLTFLHGPRSC- 391
                         410       420
                  ....*....|....*....|....*..
gi 1039011928 504 aPALGTAITTM--MLARLLQGFKWKLA 528
Cdd:cd11069   392 -IGKKFALAEMkvLLAALVSRFEFELD 417
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
117-502 4.82e-28

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: 116.73  E-value: 4.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 117 EIACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKTCVITPFGEQFKKMRKvIMTEIV-------- 188
Cdd:cd20677     3 DVFQIKLGMLPVVVVSGLETIKQVLLKQGESFAGRPDFYTFSLIANGKSMTFSEKYGESWKLHKK-IAKNALrtfskeea 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 189 ----CPARhrwLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRtfsekteadggptledIEHMD 264
Cdd:cd20677    82 ksstCSCL---LEEHVCAEASELVKTLVELSKEKGSFDPVSLITCAVANVVCALCFGKR----------------YDHSD 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 265 AMF--------EGLGFTFAFCISDYLPMLTGLDLNGhEKIMRESSAIMDKYHDPIIDERIKMWREgkrTQIEDFLDIFIS 336
Cdd:cd20677   143 KEFltiveinnDLLKASGAGNLADFIPILRYLPSPS-LKALRKFISRLNNFIAKSVQDHYATYDK---NHIRDITDALIA 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 337 I----KDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYV 412
Cdd:cd20677   219 LcqerKAEDKSAVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYT 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 413 KAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEV--TLTEndl 490
Cdd:cd20677   299 EAFINEVFRHSSFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLnkSLVE--- 375
                         410
                  ....*....|..
gi 1039011928 491 RFISFSTGKRGC 502
Cdd:cd20677   376 KVLIFGMGVRKC 387
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
311-548 1.42e-26

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: 112.32  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 311 IIDERIKMWREGKRtqiedflDIFISI----KDEAGQPL----LTADEIKptikeLVMAAPDNPSNAVEWAIAEMINKPE 382
Cdd:cd11061   181 QLKERLKAEEEKRP-------DIFSYLleakDPETGEGLdleeLVGEARL-----LIVAGSDTTATALSAIFYYLARNPE 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 383 ILHKAMEEIDRVV-GKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSD-TTVAGYHIPKGSQVLLSRYGLGR 460
Cdd:cd11061   249 AYEKLRAELDSTFpSDDEIRLGPKLKSLPYLRACIDEALRLSPPVPSGLPRETPPGgLTIDGEYIPGGTTVSVPIYSIHR 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 461 NPKVWSDPLSFKPERHLNECSEVTLTENdlRFISFSTGKRGCAAPALgtAITTMM--LARLLQGFKWKLAGSETRVELME 538
Cdd:cd11061   329 DERYFPDPFEFIPERWLSRPEELVRARS--AFIPFSIGPRGCIGKNL--AYMELRlvLARLLHRYDFRLAPGEDGEAGEG 404
                         250
                  ....*....|
gi 1039011928 539 SSHDMFLSKP 548
Cdd:cd11061   405 GFKDAFGRGP 414
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
312-528 2.22e-26

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: 111.61  E-value: 2.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 312 IDERIKMWREGKRTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEI 391
Cdd:cd11044   186 LEQAIRERQEEENAEAKDALGLLLEAKDEDGEPL-SMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQ 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 392 DRVVGKERFVQEsDIPKLNYVKAIIREAFRLH-PVAAFNlpHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLS 470
Cdd:cd11044   265 DALGLEEPLTLE-SLKKMPYLDQVIKEVLRLVpPVGGGF--RKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPER 341
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011928 471 FKPERHLNECSEVtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLA 528
Cdd:cd11044   342 FDPERFSPARSED--KKKPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWELL 397
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
118-549 2.29e-26

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: 111.82  E-value: 2.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 118 IACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKtcVITPFGEQFKKMRKVIMTEIvcpaR----- 192
Cdd:cd20664     4 IFTVQMGTKKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYG--ILFSNGENWKEMRRFTLTTL----Rdfgmg 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 193 HRWLHDNRAEETDHLTAWLynMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRtFSekteaDGGPTLEDIehMDAMFEGLGF 272
Cdd:cd20664    78 KKTSEDKILEEIPYLIEVF--EKHKGKPFETTLSMNVAVSNIIASIVLGHR-FE-----YTDPTLLRM--VDRINENMKL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 273 TFAFCISDY--LPMLtGLDLNGHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLdIFISIKDEAGQPLLTADE 350
Cdd:cd20664   148 TGSPSVQLYnmFPWL-GPFPGDINKLLRNTKELNDFLMETFMKHLDVLEPNDQRGFIDAFL-VKQQEEEESSDSFFHDDN 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 351 IKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQEsDIPKLNYVKAIIREAFRLHPVAAFNL 430
Cdd:cd20664   226 LTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVE-HRKNMPYTDAVIHEIQRFANIVPMNL 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 431 PHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNecSEVTLTENDlRFISFSTGKRGCAAPALGTA 510
Cdd:cd20664   305 PHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLD--SQGKFVKRD-AFMPFSAGRRVCIGETLAKM 381
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1039011928 511 ITTMMLARLLQGFKWKLAGSETRVELMESSHDMFLSKPL 549
Cdd:cd20664   382 ELFLFFTSLLQRFRFQPPPGVSEDDLDLTPGLGFTLNPL 420
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
311-531 7.37e-26

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


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 110.00  E-value: 7.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 311 IIDERikmwREGKRTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEE 390
Cdd:cd11042   178 IIQKR----RKSPDKDEDDMLQTLMDAKYKDGRPL-TDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREE 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 391 IDRVVGKERF-VQESDIPKLNYVKAIIREAFRLHPVAaFNLPHVALSDTTV--AGYHIPKGSQVLLSRYGLGRNPKVWSD 467
Cdd:cd11042   253 QKEVLGDGDDpLTYDVLKEMPLLHACIKETLRLHPPI-HSLMRKARKPFEVegGGYVIPKGHIVLASPAVSHRDPEIFKN 331
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039011928 468 PLSFKPERHLNECSEVTLTEnDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSE 531
Cdd:cd11042   332 PDEFDPERFLKGRAEDSKGG-KFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFELVDSP 394
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
118-527 1.35e-25

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: 109.54  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 118 IACVRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNgyKTCVITPFGEQFKKMRKVIMTEIVCPAR-HRWL 196
Cdd:cd20667     4 IYTLWLGSTPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLFG--EKGIICTNGLTWKQQRRFCMTTLRELGLgKQAL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 197 HDNRAEETDHLTAWLYNmvKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKteadggPT-LEDIEHMDamfegLGFTFA 275
Cdd:cd20667    82 ESQIQHEAAELVKVFAQ--ENGRPFDPQDPIVHATANVIGAVVFGHRFSSED------PIfLELIRAIN-----LGLAFA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 276 FCI----SDYLPMLTGLDLNGHEKIMressAIMDKYHDPIIDErIKMWREGKRTQIEDFLDIFIS-IKDEAGQPLLTADE 350
Cdd:cd20667   149 STIwgrlYDAFPWLMRYLPGPHQKIF----AYHDAVRSFIKKE-VIRHELRTNEAPQDFIDCYLAqITKTKDDPVSTFSE 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 351 --IKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAF 428
Cdd:cd20667   224 enMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 429 NLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTEndlRFISFSTGKRGCAAPALG 508
Cdd:cd20667   304 GAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNE---AFLPFSAGHRVCLGEQLA 380
                         410
                  ....*....|....*....
gi 1039011928 509 TAITTMMLARLLQGFKWKL 527
Cdd:cd20667   381 RMELFIFFTTLLRTFNFQL 399
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
121-536 1.84e-25

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: 108.94  E-value: 1.84e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQQDALFASRPLTYA-QKILSN--GYkTCVITPFGEQFKKMRKVIMTEIVCPARHRWLH 197
Cdd:cd11066     7 IRLGNKRIVVVNSFASVRDLWIKNSSALNSRPTFYTfHKVVSStqGF-TIGTSPWDESCKRRRKAAASALNRPAVQSYAP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 198 DNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEkteaDGGPTLEDI---EHMDAMFEGLGFTf 274
Cdd:cd11066    86 IIDLESKSFIRELLRDSAEGKGDIDPLIYFQRFSLNLSLTLNYGIRLDCV----DDDSLLLEIievESAISKFRSTSSN- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 275 afcISDYLPMLTGLDLNG----HEKIMRESsaiMDKYHDPIIDerikmwreGKRTQIEDFLD---IFISIKDEAGQPLLT 347
Cdd:cd11066   161 ---LQDYIPILRYFPKMSkfreRADEYRNR---RDKYLKKLLA--------KLKEEIEDGTDkpcIVGNILKDKESKLTD 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 348 AdEIKPTIKELVMAAPDNPSNAVEWAIAEMINKP--EILHKAMEEIDRVVGK-----ERFVQESdipKLNYVKAIIREAF 420
Cdd:cd11066   227 A-ELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNdedawEDCAAEE---KCPYVVALVKETL 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 421 RLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLnecSEVTLTENDLRFISFSTGKR 500
Cdd:cd11066   303 RYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWL---DASGDLIPGPPHFSFGAGSR 379
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1039011928 501 GCAAPALGTAITTMMLARLLQGFKWKLAGSETRVEL 536
Cdd:cd11066   380 MCAGSHLANRELYTAICRLILLFRIGPKDEEEPMEL 415
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
131-527 2.04e-25

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: 108.96  E-value: 2.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 131 VTCPKIAREIFKQQDAlFASRPLTYaqKILsNGYKTCVITPFGEQFKKMRKVIMTEIvcparhrwLHDNRAEETDHLTA- 209
Cdd:cd11070    17 VTKPEYLTQIFRRRDD-FPKPGNQY--KIP-AFYGPNVISSEGEDWKRYRKIVAPAF--------NERNNALVWEESIRq 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 210 -------WLYNMVKNSEP-VDLRFVTRHYCGNAIKRLMFGTR-TFSEKTEADGGPTLEDIEHMDamFEGLGFTFAFcisd 280
Cdd:cd11070    85 aqrliryLLEEQPSAKGGgVDVRDLLQRLALNVIGEVGFGFDlPALDEEESSLHDTLNAIKLAI--FPPLFLNFPF---- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 281 ylpmltgLDLNGHEKI--MRESSAIMDKYHDPIIDERIKMWREGKRTQIEDFLDIFISIKDEAGQPLLTADEIKPTIKEL 358
Cdd:cd11070   159 -------LDRLPWVLFpsRKRAFKDVDEFLSELLDEVEAELSADSKGKQGTESVVASRLKRARRSGGLTEKELLGNLFIF 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 359 VMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQES--DIPKLNYVKAIIREAFRLHPVAAFnLPHVALS 436
Cdd:cd11070   232 FIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYeeDFPKLPYLLAVIYETLRLYPPVQL-LNRKTTE 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 437 DTTV-----AGYHIPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNECSEVTLTE----NDLRFISFSTGKRGCaapa 506
Cdd:cd11070   311 PVVVitglgQEIVIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSGEIGAATrftpARGAFIPFSAGPRAC---- 386
                         410       420
                  ....*....|....*....|....*
gi 1039011928 507 LGT--AITTMM--LARLLQGFKWKL 527
Cdd:cd11070   387 LGRkfALVEFVaaLAELFRQYEWRV 411
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
297-524 2.30e-25

cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome P450/NADPH--P450 reductase; Cytochrome P450 102A1, also called cytochrome P450(BM-3) or P450BM-3, is a bifunctional cytochrome P450/NADPH--P450 reductase. These proteins fuse an N-terminal cytochrome p450 with a C-terminal cytochrome p450 reductase (CYPOR). It functions as a fatty acid monooxygenase, catalyzing the hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, with activity towards fatty acids with a chain length of 9-18 carbons. Its NADPH-dependent reductase activity (via the C-terminal domain) allows electron transfer from NADPH to the heme iron of the N-terminal cytochrome P450. CYP120A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 108.81  E-value: 2.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 297 MRESSAIMDKYHDPIIDERikmwREGKRTQIEDFLDIFISIKD-EAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAIA 375
Cdd:cd11068   181 FREDIALMRDLVDEIIAER----RANPDGSPDDLLNLMLNGKDpETGEKL-SDENIRYQMITFLIAGHETTSGLLSFALY 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 376 EMINKPEILHKAMEEIDRVVGKERFVQEsDIPKLNYVKAIIREAFRLHPVA-AFNLPhvALSDTTVAG-YHIPKGSQVLL 453
Cdd:cd11068   256 YLLKNPEVLAKARAEVDEVLGDDPPPYE-QVAKLRYIRRVLDETLRLWPTApAFARK--PKEDTVLGGkYPLKKGDPVLV 332
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039011928 454 SRYGLGRNPKVW-SDPLSFKPERHLNEcSEVTLTENdlRFISFSTGKRGCA--APALGTAitTMMLARLLQGFK 524
Cdd:cd11068   333 LLPALHRDPSVWgEDAEEFRPERFLPE-EFRKLPPN--AWKPFGNGQRACIgrQFALQEA--TLVLAMLLQRFD 401
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
258-549 2.93e-25

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: 108.44  E-value: 2.93e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 258 EDIEHMDAMFEGlgFTFAFCISDYLPMLTGL-----------DLNGHEKIMRESSAIMDKYHDPIiderikmwrEGKRTQ 326
Cdd:cd11060   131 TDVDGYIASIDK--LLPYFAVVGQIPWLDRLllknplgpkrkDKTGFGPLMRFALEAVAERLAED---------AESAKG 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 327 IEDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGK---ERFVQE 403
Cdd:cd11060   200 RKDMLDSFLEAGLKDPEKV-TDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEgklSSPITF 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 404 SDIPKLNYVKAIIREAFRLHPVAAFNLP-HVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWS-DPLSFKPERHLNECS 481
Cdd:cd11060   279 AEAQKLPYLQAVIKEALRLHPPVGLPLErVVPPGGATICGRFIPGGTIVGVNPWVIHRDKEVFGeDADVFRPERWLEADE 358
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039011928 482 EvTLTENDLRFISFSTGKRGCaapaLGTAITTMML----ARLLQGFKWKLAGSETrvELMESSHDMFLSKPL 549
Cdd:cd11060   359 E-QRRMMDRADLTFGAGSRTC----LGKNIALLELykviPELLRRFDFELVDPEK--EWKTRNYWFVKQSDF 423
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
121-537 3.67e-25

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: 108.18  E-value: 3.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 121 VRLGNTHVIPVTCPKIAREIFKQqdalfasRPLTY---------AQKILSNGyktcVITPFGEQFKKMRKVIMTEIVcPA 191
Cdd:cd11083     6 FRLGRQPVLVISDPELIREVLRR-------RPDEFrrisslesvFREMGING----VFSAEGDAWRRQRRLVMPAFS-PK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 192 RHRWLHDNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFG--TRTFsektEADGGPTLEDIEHMDAMFEG 269
Cdd:cd11083    74 HLRYFFPTLRQITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGydLNTL----ERGGDPLQEHLERVFPMLNR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 270 LGFTfAFCISDYLPMLTGLDLNGHekiMRESSAIMDKyhdpIIDE-RIKMWREGKRTQIEDFLDIFISIKDEaGQPLLTA 348
Cdd:cd11083   150 RVNA-PFPYWRYLRLPADRALDRA---LVEVRALVLD----IIAAaRARLAANPALAEAPETLLAMMLAEDD-PDARLTD 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 349 DEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERF-VQESDIPKLNYVKAIIREAFRLHPVAA 427
Cdd:cd11083   221 DEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVpPLLEALDRLPYLEAVARETLRLKPVAP 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 428 FnLPHVALSDTTVAGYHIPKGSQV-LLSRYGlGRNPKVWSDPLSFKPERHLNEcSEVTLTENDLRFISFSTGKRGCAAPA 506
Cdd:cd11083   301 L-LFLEPNEDTVVGDIALPAGTPVfLLTRAA-GLDAEHFPDPEEFDPERWLDG-ARAAEPHDPSSLLPFGAGPRLCPGRS 377
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1039011928 507 LGTAITTMMLARLLQGFKWKLAG-SETRVELM 537
Cdd:cd11083   378 LALMEMKLVFAMLCRNFDIELPEpAPAVGEEF 409
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
293-557 1.28e-24

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: 106.58  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 293 HEKIMRessaIMDKYHDPIIDERIKMWREGKRTQIED-------------FLDIFISIKDEAGQplLTADEIKPTIKELV 359
Cdd:cd20660   168 HKKCLK----ILHGFTNKVIQERKAELQKSLEEEEEDdedadigkrkrlaFLDLLLEASEEGTK--LSDEDIREEVDTFM 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 360 MAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGK-ERFVQESDIPKLNYVKAIIREAFRLHP-VAAFNlpHVALSD 437
Cdd:cd20660   242 FEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDsDRPATMDDLKEMKYLECVIKEALRLFPsVPMFG--RTLSED 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 438 TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtlTENDLRFISFSTGKRGCaapaLGTAITTM--- 514
Cdd:cd20660   320 IEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSA---GRHPYAYIPFSAGPRNC----IGQKFALMeek 392
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1039011928 515 -MLARLLQGFkwklagsetRVELMESSHDmflskpLVLVGELRL 557
Cdd:cd20660   393 vVLSSILRNF---------RIESVQKRED------LKPAGELIL 421
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
346-535 1.54e-24

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: 106.28  E-value: 1.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 346 LTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPV 425
Cdd:cd20646   229 LSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPV 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 426 AAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNecsEVTLTENDLRFISFSTGKRGCaap 505
Cdd:cd20646   309 VPGNARVIVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLR---DGGLKHHPFGSIPFGYGVRAC--- 382
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1039011928 506 aLGTAITTM----MLARLLQGFKWKLAGSETRVE 535
Cdd:cd20646   383 -VGRRIAELemylALSRLIKRFEVRPDPSGGEVK 415
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
127-534 2.54e-24

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: 105.34  E-value: 2.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 127 HVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSngyKTCVITPFGEQFKKMRKVIMTEIVCPA-RHRWLHDNRAEETD 205
Cdd:cd11043    17 PTVVSADPEANRFILQNEGKLFVSWYPKSVRKLLG---KSSLLTVSGEEHKRLRGLLLSFLGPEAlKDRLLGDIDELVRQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 206 HLTAWLynmvKNSEPVDLRFVtRHYCGNAIKRLMFGtrtfsekteADGGPTLEDIEHM-DAMFEGL--------GFTFAF 276
Cdd:cd11043    94 HLDSWW----RGKSVVVLELA-KKMTFELICKLLLG---------IDPEEVVEELRKEfQAFLEGLlsfplnlpGTTFHR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 277 CisdylpmltgldLNGHEKIMREssaiMDKyhdpIIDERIKMWREGKRTQieDFLDIFISIKDEAGQPLlTADEIKPTIK 356
Cdd:cd11043   160 A------------LKARKRIRKE----LKK----IIEERRAELEKASPKG--DLLDVLLEEKDEDGDSL-TDEEILDNIL 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 357 ELVMAAPDNPSNAVEWAI---AEMinkPEILHKAMEE---IDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAaFNL 430
Cdd:cd11043   217 TLLFAGHETTSTTLTLAVkflAEN---PKVLQELLEEheeIAKRKEEGEGLTWEDYKSMKYTWQVINETLRLAPIV-PGV 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 431 PHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTendlrFISFSTGKRGCAAPALGTA 510
Cdd:cd11043   293 FRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGVPYT-----FLPFGGGPRLCPGAELAKL 367
                         410       420
                  ....*....|....*....|....
gi 1039011928 511 ITTMMLARLLQGFKWKLAGSETRV 534
Cdd:cd11043   368 EILVFLHHLVTRFRWEVVPDEKIS 391
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
219-527 2.57e-24

cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a microsomal enzyme that is required for the activation of vitamin D; it catalyzes the initial step converting vitamin D into 25-hydroxyvitamin D (25(OH)D), the major circulating metabolite of vitamin D. The 1alpha-hydroxylation of 25(OH)D by CYP27B1 generates the fully active vitamin D metabolite, 1,25-dihydroxyvitamin D (1,25(OH)2D). Mutations in the CYP2R1 gene are associated with an atypical form of vitamin D-deficiency rickets, which has been classified as vitamin D dependent rickets type 1B. CYP2R1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 105.67  E-value: 2.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 219 EPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTeadggptleDIEHMDAMF----EGLGFTFAFcISDYLPMLTGLDLNGHE 294
Cdd:cd20661   114 KPFDPKHLITNAVSNITNLIIFGERFTYEDT---------DFQHMIEIFsenvELAASAWVF-LYNAFPWIGILPFGKHQ 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 295 KIMRESSAIMDKYHDpiideRIKMWREGKRTQI-EDFLDIFISIKDEAGQPLLTA---DEIKPTIKELVMAAPDNPSNAV 370
Cdd:cd20661   184 QLFRNAAEVYDFLLR-----LIERFSENRKPQSpRHFIDAYLDEMDQNKNDPESTfsmENLIFSVGELIIAGTETTTNVL 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 371 EWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQ 450
Cdd:cd20661   259 RWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFHATSKDAVVRGYSIPKGTT 338
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011928 451 VLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTEndlRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKL 527
Cdd:cd20661   339 VITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKE---AFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHF 412
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
237-548 3.62e-24

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: 105.07  E-value: 3.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 237 RLMFGTrtfSEKTEADGGPTLEDIEHMDAMFEGLGFtFAFCISDYLPMLTGLDLNGhekIMRESSAIMDKYHDPIIDERI 316
Cdd:cd11059   117 HLLFGE---SFGTLLLGDKDSRERELLRRLLASLAP-WLRWLPRYLPLATSRLIIG---IYFRAFDEIEEWALDLCARAE 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 317 KmwREGKRTQIEDFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVG 396
Cdd:cd11059   190 S--SLAESSDSESLTVLLLEKLKGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLPG 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 397 KERFVQE-SDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSD-TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPE 474
Cdd:cd11059   268 PFRGPPDlEDLDKLPYLNAVIRETLRLYPPIPGSLPRVVPEGgATIGGYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPE 347
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039011928 475 RHLNECSEvTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLqgfkWKLAGSETRVELMEsSHDMFLSKP 548
Cdd:cd11059   348 RWLDPSGE-TAREMKRAFWPFGSGSRMCIGMNLALMEMKLALAAIY----RNYRTSTTTDDDME-QEDAFLAAP 415
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
280-531 4.47e-24

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: 104.59  E-value: 4.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 280 DYLPMLTGLDLNGHEKiMRESSAIMDKYHDPIIDERikmwREGKRtqiEDFLDIFISIKDEaGQPLlTADEIKPTIKELV 359
Cdd:COG2124   166 ALLDALGPLPPERRRR-ARRARAELDAYLRELIAER----RAEPG---DDLLSALLAARDD-GERL-SDEELRDELLLLL 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 360 MAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDrvvgkerfvqesdipklnYVKAIIREAFRLHPVAAFnLPHVALSDTT 439
Cdd:COG2124   236 LAGHETTANALAWALYALLRHPEQLARLRAEPE------------------LLPAAVEETLRLYPPVPL-LPRTATEDVE 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 440 VAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNecsevtltendlRFISFSTGKRGCAAPALGTAITTMMLARL 519
Cdd:COG2124   297 LGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDRPPN------------AHLPFGGGPHRCLGAALARLEARIALATL 364
                         250
                  ....*....|...
gi 1039011928 520 LQGF-KWKLAGSE 531
Cdd:COG2124   365 LRRFpDLRLAPPE 377
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
294-557 5.66e-24

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: 104.84  E-value: 5.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 294 EKIMRESSAIMDKYHDPIIDERIKMWREGKRtqiEDFLDIFISIKDEAGQPLLTADeIKPTIKELVMAAPDNPSNAVEWA 373
Cdd:cd20680   191 DNVIAERAEEMKAEEDKTGDSDGESPSKKKR---KAFLDMLLSVTDEEGNKLSHED-IREEVDTFMFEGHDTTAAAMNWS 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 374 IAEMINKPEILHKAMEEIDRVVGK-ERFVQESDIPKLNYVKAIIREAFRLHPvaafNLPHVALS---DTTVAGYHIPKGS 449
Cdd:cd20680   267 LYLLGSHPEVQRKVHKELDEVFGKsDRPVTMEDLKKLRYLECVIKESLRLFP----SVPLFARSlceDCEIRGFKVPKGV 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 450 QVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFkWklag 529
Cdd:cd20680   343 NAVIIPYALHRDPRYFPEPEEFRPERFFPENSS---GRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHF-W---- 414
                         250       260
                  ....*....|....*....|....*...
gi 1039011928 530 setrVELMESSHDmflskpLVLVGELRL 557
Cdd:cd20680   415 ----VEANQKREE------LGLVGELIL 432
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
303-526 5.91e-24

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: 104.61  E-value: 5.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 303 IMDKYHDPIIDERIKMWREGKRTQIEDFLD------IFIS--IKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAI 374
Cdd:cd11057   172 ILRAFSEKIIEKKLQEVELESNLDSEEDEEngrkpqIFIDqlLELARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTL 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 375 AEMINKPEILHKAMEEIDRVVG-KERFVQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVALSDTTVA-GYHIPKGSQVL 452
Cdd:cd11057   252 LLLAMHPEVQEKVYEEIMEVFPdDGQFITYEDLQQLVYLEMVLKETMRLFPVGPL-VGRETTADIQLSnGVVIPKGTTIV 330
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039011928 453 LSRYGLGRNPKVW-SDPLSFKPERHLNECSEVtltendlR----FISFSTGKRGCAAPALGTAITTMMLARLLQGFKWK 526
Cdd:cd11057   331 IDIFNMHRRKDIWgPDADQFDPDNFLPERSAQ-------RhpyaFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLK 402
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
298-525 5.63e-23

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: 101.48  E-value: 5.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 298 RESSAIMDKYHDPIIDERIKMWREGKRTQIED---FLDifiSIKDEagqpllTADEIkpTIKELVM----AAPDNPSNAV 370
Cdd:cd11063   168 REACKVVHRFVDPYVDKALARKEESKDEESSDryvFLD---ELAKE------TRDPK--ELRDQLLnillAGRDTTASLL 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 371 EWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLpHVALSDTTV---------A 441
Cdd:cd11063   237 SFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNS-RVAVRDTTLprgggpdgkS 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 442 GYHIPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNecsevtLTENDLRFISFSTGKRGCaapaLGT--AITTM--ML 516
Cdd:cd11063   316 PIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWED------LKRPGWEYLPFNGGPRIC----LGQqfALTEAsyVL 385

                  ....*....
gi 1039011928 517 ARLLQGFKW 525
Cdd:cd11063   386 VRLLQTFDR 394
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
278-526 3.36e-22

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: 99.26  E-value: 3.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 278 ISDYLPmltgldlNGHEKIMReSSAIMDKYhdpiIDERIKMWREG-KRTQIEDFLDIF-ISIKDEAG--QPLLTADEIKP 353
Cdd:cd20665   162 LLDYLP-------GSHNKLLK-NVAYIKSY----ILEKVKEHQESlDVNNPRDFIDCFlIKMEQEKHnqQSEFTLENLAV 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 354 TIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHV 433
Cdd:cd20665   230 TVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLPHA 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 434 ALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSevTLTENDLrFISFSTGKRGCAAPALGTAITT 513
Cdd:cd20665   310 VTCDTKFRNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENG--NFKKSDY-FMPFSAGKRICAGEGLARMELF 386
                         250
                  ....*....|...
gi 1039011928 514 MMLARLLQGFKWK 526
Cdd:cd20665   387 LFLTTILQNFNLK 399
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
329-536 1.31e-21

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: 97.52  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 329 DFLDIFISIKDEAGQPLLT---ADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESD 405
Cdd:cd20669   202 DFIDCFLTKMAEEKQDPLShfnMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLED 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 406 IPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVtl 485
Cdd:cd20669   282 RARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSF-- 359
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039011928 486 tENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSETRVEL 536
Cdd:cd20669   360 -KKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQPLGAPEDIDL 409
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
317-545 1.93e-21

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: 96.94  E-value: 1.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 317 KMWREGKRTQIE-DFLDIFISIKDEAGQPLLTADEIKPT-----IKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEE 390
Cdd:cd11062   185 KQVDEVLRQVSAgDPPSIVTSLFHALLNSDLPPSEKTLErladeAQTLIGAGTETTARTLSVATFHLLSNPEILERLREE 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 391 IDRVVGKER-FVQESDIPKLNYVKAIIREAFRL-HPVAAfNLPHVALSDT-TVAGYHIPKGSQVLLSRYGLGRNPKVWSD 467
Cdd:cd11062   265 LKTAMPDPDsPPSLAELEKLPYLTAVIKEGLRLsYGVPT-RLPRVVPDEGlYYKGWVIPPGTPVSMSSYFVHHDEEIFPD 343
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011928 468 PLSFKPERHLNECSEVTLTENdlrFISFSTGKRGCAAPALGTAITTMMLARLLQgfKWKLAGSETRVELMESSHDMFL 545
Cdd:cd11062   344 PHEFRPERWLGAAEKGKLDRY---LVPFSKGSRSCLGINLAYAELYLALAALFR--RFDLELYETTEEDVEIVHDFFL 416
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
290-502 2.49e-21

cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, X, and Z; This group is composed of family 4 cytochrome P450s from subfamilies A (CYP4A), B (CYP4B), T (CYP4T), X (CYP4X), and Z (CYP4Z). The CYP4A, CYP4X, and CYP4Z subfamilies are specific to mammals, CYP4T is present in fish, while CYP4B is conserved among vertebrates. CYP4As are known for catalyzing arachidonic acid to 20-HETE (20-hydroxy-5Z,8Z,11Z,14Z-eicosatetraenoic acid), and some can also metabolize lauric and palmitic acid. CYP4Bs specialize in omega-hydroxylation of short chain fatty acids and also participates in the metabolism of exogenous compounds that are protoxic including valproic acid (C8), 3-methylindole (C9), 4-ipomeanol, 3-methoxy-4-aminoazobenzene, and several aromatic amines. CYP4X1 is expressed at high levels in the mammalian brain and may play a role in regulating fat metabolism. CYP4Z1 is a fatty acid hydroxylase that is unique among human CYPs in that it is predominantly expressed in the mammary gland. Monophyly was not found with the CYP4T and CYP4B subfamilies, and further consideration should be given to their nomenclature. The CYP4B-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 96.58  E-value: 2.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 290 LNGHEKIMRESSAIMDKYHDPIIDERIK-MWREGKRTQIE-----DFLDIFISIKDEAGQPLLTADeIKPTIKELVMAAP 363
Cdd:cd20678   174 LSPHGRRFRRACQLAHQHTDKVIQQRKEqLQDEGELEKIKkkrhlDFLDILLFAKDENGKSLSDED-LRAEVDTFMFEGH 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 364 DNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPvaafNLPHVA--LSD--TT 439
Cdd:cd20678   253 DTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYP----PVPGISreLSKpvTF 328
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011928 440 VAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSevtltenDLR----FISFSTGKRGC 502
Cdd:cd20678   329 PDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENS-------SKRhshaFLPFSAGPRNC 388
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
126-523 3.31e-21

cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, reptiles, and amphibians. The hominin CYP2D subfamily consists of a functional CYP2D6 and two paralogs, CYP2D7 and CYP2D8, that are often not functional in some species. Human CYP2D6 has a high affinity for alkaloids and can detoxify them. It is also responsible for metabolizing about 25% of commonly used drugs, such as antidepressants, beta-blockers, and antiarrhythmics. The CYP2D subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 96.30  E-value: 3.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 126 THVIPVTCPKIAREIFKQQDALFASRPLTYAQKILSNGYKT--CVITPFGEQFKKMRKVIMTEIvcpaRH-----RWLHD 198
Cdd:cd20663    12 KPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGPKSqgVVLARYGPAWREQRRFSVSTL----RNfglgkKSLEQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 199 NRAEETDHLTAWLYNmvKNSEPVDLRFVTRHYCGNAIKRLMFGTRtFSEkteadGGPTLedIEHMDAMFEGLGFTFAFC- 277
Cdd:cd20663    88 WVTEEAGHLCAAFTD--QAGRPFNPNTLLNKAVCNVIASLIFARR-FEY-----EDPRF--IRLLKLLEESLKEESGFLp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 278 -ISDYLPMLtgLDLNG-HEKIMRESSAIMDkYHDPIIDERIKMWREGKRTQieDFLDIFIS-IKDEAGQP---------- 344
Cdd:cd20663   158 eVLNAFPVL--LRIPGlAGKVFPGQKAFLA-LLDELLTEHRTTWDPAQPPR--DLTDAFLAeMEKAKGNPessfndenlr 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 345 LLTADeikptikeLVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHP 424
Cdd:cd20663   233 LVVAD--------LFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGD 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 425 VAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTEndlRFISFSTGKRGCaa 504
Cdd:cd20663   305 IVPLGVPHMTSRDIEVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPE---AFMPFSAGRRAC-- 379
                         410       420
                  ....*....|....*....|...
gi 1039011928 505 paLGTAITTMML----ARLLQGF 523
Cdd:cd20663   380 --LGEPLARMELflffTCLLQRF 400
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
173-526 3.71e-21

cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes CYP2A1, 2A2, and 2A3 in rats; CYP2A4, 2A5, 2A12, 2A20p, 2A21p, 2A22, and 2A23p in mice; CYP2A6, 2A7, 2A13, 2A18P in humans; CYP2A8, 2A9, 2A14, 2A15, 2A16, and 2A17 in hamsters; CYP2A10 and 2A11 in rabbits; and CYP2A19 in pigs. CYP2A enzymes metabolize numerous xenobiotic compounds, including coumarin, aflatoxin B1, nicotine, cotinine, 1,3-butadiene, and acetaminophen, among others, as well as endogenous compounds, including testosterone, progesterone, and other steroid hormones. Human CYP2A6 is responsible for the systemic clearance of nicotine, while CYP2A13 activates the nicotine-derived procarcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) into DNA-altering compounds that cause lung cancer. The CYP2A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 96.02  E-value: 3.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 173 GEQFKKMRKV-IMTEIVCPARHRWLHDNRAEETDHLTAWLYNMvkNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEa 251
Cdd:cd20668    57 GERAKQLRRFsIATLRDFGVGKRGIEERIQEEAGFLIDALRGT--GGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKE- 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 252 dggpTLEDIEHMDAMFE------GLGFTFAFCISDYLPmltgldlNGHEKIMRESSAIMDkyhdpIIDERIKmwrEGKRT 325
Cdd:cd20668   134 ----FLSLLRMMLGSFQftatstGQLYEMFSSVMKHLP-------GPQQQAFKELQGLED-----FIAKKVE---HNQRT 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 326 ----QIEDFLDIF-ISIKDEAGQPlltadEIKPTIKELVM-------AAPDNPSNAVEWAIAEMINKPEILHKAMEEIDR 393
Cdd:cd20668   195 ldpnSPRDFIDSFlIRMQEEKKNP-----NTEFYMKNLVMttlnlffAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDR 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 394 VVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKP 473
Cdd:cd20668   270 VIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRVTKDTKFRDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNP 349
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039011928 474 ERHLNECSEvtLTENDlRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWK 526
Cdd:cd20668   350 QHFLDDKGQ--FKKSD-AFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFK 399
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
309-533 6.38e-21

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: 95.44  E-value: 6.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 309 DPIIDERIKMWREGKRTQIEDFLDIFIsikDEA-GQPLLTADEIkpTIKELV--MAAPDNPSNAVEWAIAEMINKPEILH 385
Cdd:cd11041   188 IPEIERRRKLKKGPKEDKPNDLLQWLI---EAAkGEGERTPYDL--ADRQLAlsFAAIHTTSMTLTHVLLDLAAHPEYIE 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 386 KAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVA-GYHIPKGSQVLLSRYGLGRNPKV 464
Cdd:cd11041   263 PLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVTLSdGLTLPKGTRIAVPAHAIHRDPDI 342
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011928 465 WSDPLSFKPERHLNE---------CSEVTLTENdlrFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSETR 533
Cdd:cd11041   343 YPDPETFDGFRFYRLreqpgqekkHQFVSTSPD---FLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGER 417
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
123-536 1.14e-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: 94.53  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 123 LGNTHVIPVTCPKIAREIFKQQDALFASRPLTYAQKI--LSNgyktcviTPF---GEQFKKMRKvIMTEIVCPARHRWLH 197
Cdd:cd11056    10 LFRRPALLVRDPELIKQILVKDFAHFHDRGLYSDEKDdpLSA-------NLFsldGEKWKELRQ-KLTPAFTSGKLKNMF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 198 DNRAEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTrtfsektEADggpTLEDIEhmdAMFEGLGF-TFAF 276
Cdd:cd11056    82 PLMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGL-------DAN---SLNDPE---NEFREMGRrLFEP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 277 CISDYLPMLTGLDLNGHEKIMRESsaIMDKYHDP----IIDERIKMwREGKRTQIEDFLDIFISIKDEAGQPLlTADEIK 352
Cdd:cd11056   149 SRLRGLKFMLLFFFPKLARLLRLK--FFPKEVEDffrkLVRDTIEY-REKNNIVRNDFIDLLLELKKKGKIED-DKSEKE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 353 PTIKELV-------MAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKE--RFVQESdIPKLNYVKAIIREAFRLH 423
Cdd:cd11056   225 LTDEELAaqafvffLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHggELTYEA-LQEMKYLDQVVNETLRKY 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 424 PVAAFnLPHVALSDTTVAG--YHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsevtltENDLR----FISFST 497
Cdd:cd11056   304 PPLPF-LDRVCTKDYTLPGtdVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPE-------NKKKRhpytYLPFGD 375
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1039011928 498 GKRGCAAPALGTAITTMMLARLLQGFKWKLAgSETRVEL 536
Cdd:cd11056   376 GPRNCIGMRFGLLQVKLGLVHLLSNFRVEPS-SKTKIPL 413
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
346-534 1.83e-20

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: 94.22  E-value: 1.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 346 LTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPV 425
Cdd:cd20647   233 LTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPV 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 426 AAFNlPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcSEVTLTENdLRFISFSTGKRGCAAP 505
Cdd:cd20647   313 LPGN-GRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRK-DALDRVDN-FGSIPFGYGIRSCIGR 389
                         170       180
                  ....*....|....*....|....*....
gi 1039011928 506 ALGTAITTMMLARLLQGFKWKLAGSETRV 534
Cdd:cd20647   390 RIAELEIHLALIQLLQNFEIKVSPQTTEV 418
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
205-535 1.86e-20

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


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 93.89  E-value: 1.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 205 DHLTAWLYNMVKNSEPVDlRFVTRHYcgNAIKRLMF--------GTRTFSEKTEADG-GPTLEDIEHmDAMFEGLgftFA 275
Cdd:cd20615    85 REARKWVQNLPTNSGDGR-RFVIDPA--QALKFLPFrviaeilyGELSPEEKEELWDlAPLREELFK-YVIKGGL---YR 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 276 FCISDYLPmltgldlnghekimRESSAIMDKYHdpiideriKMWRE------------GKRTQIEDFLDifisiKDEAGQ 343
Cdd:cd20615   158 FKISRYLP--------------TAANRRLREFQ--------TRWRAfnlkiynrarqrGQSTPIVKLYE-----AVEKGD 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 344 plLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEI-----DRVVGKERFVQESDipklNYVKAIIRE 418
Cdd:cd20615   211 --ITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEIsaareQSGYPMEDYILSTD----TLLAYCVLE 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 419 AFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLG-RNPKVWSDPLSFKPERHLNecsevtLTENDLR--FISF 495
Cdd:cd20615   285 SLRLRPLLAFSVPESSPTDKIIGGYRIPANTPVVVDTYALNiNNPFWGPDGEAYRPERFLG------ISPTDLRynFWRF 358
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1039011928 496 STGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSETRVE 535
Cdd:cd20615   359 GFGPRKCLGQHVADVILKALLAHLLEQYELKLPDQGENEE 398
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
329-526 2.93e-20

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: 93.45  E-value: 2.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 329 DFLDIF-ISIKDEAGQPL--LTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESD 405
Cdd:cd20670   202 DFIDCFlIKMHQDKNNPHteFNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDD 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 406 IPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsEVTL 485
Cdd:cd20670   282 RVKMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDE--QGRF 359
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1039011928 486 TENDlRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWK 526
Cdd:cd20670   360 KKNE-AFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSLR 399
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
295-529 7.21e-20

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


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 92.26  E-value: 7.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 295 KIMRESSAIMDKYHDPIIDERIKMwREGKRTQIEDFLDIFISIKDEAGQplLTADEIKPTIKELVMAAPDNPSNAVEWAI 374
Cdd:cd11058   165 LLIPKSLRKKRKEHFQYTREKVDR-RLAKGTDRPDFMSYILRNKDEKKG--LTREELEANASLLIIAGSETTATALSGLT 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 375 AEMINKPEILHKAMEEIdrvvgKERFVQESDI-----PKLNYVKAIIREAFRLHPVAAFNLPHVALSDT-TVAGYHIPKG 448
Cdd:cd11058   242 YYLLKNPEVLRKLVDEI-----RSAFSSEDDItldslAQLPYLNAVIQEALRLYPPVPAGLPRVVPAGGaTIDGQFVPGG 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 449 SQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVtlTENDLR--FISFSTGKRGCAAPALGTAITTMMLARLLQGFKWK 526
Cdd:cd11058   317 TSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFE--FDNDKKeaFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLE 394

                  ...
gi 1039011928 527 LAG 529
Cdd:cd11058   395 LDP 397
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
131-528 1.70e-18

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: 88.17  E-value: 1.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 131 VTCPKIAREIFKQQDALFASRPLT-YAQKILSNGyktcVITPFGEQFKKMRKvimteIVCPARHRwlhDNRAEETDH--- 206
Cdd:cd11052    27 VTEPELIKELLSKKEGYFGKSPLQpGLKKLLGRG----LVMSNGEKWAKHRR-----IANPAFHG---EKLKGMVPAmve 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 207 -----LTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTrtfsekTEADGGPTLEDI-EHMDAMFEGLgFTFAFCISD 280
Cdd:cd11052    95 svsdmLERWKKQMGEEGEEVDVFEEFKALTADIISRTAFGS------SYEEGKEVFKLLrELQKICAQAN-RDVGIPGSR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 281 YLPMLTGLDLNGHEKIMRESsaIMDkyhdpIIDERIKMWREGK-RTQIEDFLDIFI-SIKDEAGQPLLTADEIKPTIKEL 358
Cdd:cd11052   168 FLPTKGNKKIKKLDKEIEDS--LLE-----IIKKREDSLKMGRgDDYGDDLLGLLLeANQSDDQNKNMTVQEIVDECKTF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 359 VMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESdIPKLNYVKAIIREAFRLHPvAAFNLPHVALSDT 438
Cdd:cd11052   241 FFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPSDS-LSKLKTVSMVINESLRLYP-PAVFLTRKAKEDI 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 439 TVAGYHIPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNECSEVtlTENDLRFISFSTGKRGCaapaLGTAITTM--- 514
Cdd:cd11052   319 KLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGVAKA--AKHPMAFLPFGLGPRNC----IGQNFATMeak 392
                         410
                  ....*....|....*
gi 1039011928 515 -MLARLLQGFKWKLA 528
Cdd:cd11052   393 iVLAMILQRFSFTLS 407
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
346-537 2.65e-18

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: 87.50  E-value: 2.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 346 LTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPV 425
Cdd:cd20648   230 LPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPV 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 426 AAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSevtlTENDLRFISFSTGKRGCAAP 505
Cdd:cd20648   310 IPGNARVIPDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGD----THHPYASLPFGFGKRSCIGR 385
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1039011928 506 ALGTAITTMMLARLLQGFKWKLAGSETRVELM 537
Cdd:cd20648   386 RIAELEVYLALARILTHFEVRPEPGGSPVKPM 417
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
339-526 4.58e-18

cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is expressed during development of the gastrointestinal tract, is silenced after birth in the intestine and colon by epigenetic modifications, but is activated following demethylation in colorectal cancer (CRC). Its expression levels in CRC correlate with the degree of malignancy, are higher in metastases and are predictive of survival. Thus, it is an attractive tumor-specific diagnostic and therapeutic target. CYP2W1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 86.78  E-value: 4.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 339 DEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIRE 418
Cdd:cd20671   212 DDPKETLFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHE 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 419 AFRLHPVaafnLPHV---ALSDTTVAGYHIPKGSQV--LLSRYGLGRNPkvWSDPLSFKPERHLNECSEVTLTEndlRFI 493
Cdd:cd20671   292 VQRFITL----LPHVprcTAADTQFKGYLIPKGTPVipLLSSVLLDKTQ--WETPYQFNPNHFLDAEGKFVKKE---AFL 362
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1039011928 494 SFSTGKRGCAAPALGTAITTMMLARLLQGFKWK 526
Cdd:cd20671   363 PFSAGRRVCVGESLARTELFIFFTGLLQKFTFL 395
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
310-524 7.61e-18

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: 86.01  E-value: 7.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 310 PIIDERIKMWREGKRtqiEDFL-DIFisikdeaGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAM 388
Cdd:cd20645   195 HCIDKRLQRYSQGPA---NDFLcDIY-------HDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLL 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 389 EEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVAlSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDP 468
Cdd:cd20645   265 QEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLD-KDTVLGDYLLPKGTVLMINSQALGSSEEYFEDG 343
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011928 469 LSFKPERHLNECSEVtlteNDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFK 524
Cdd:cd20645   344 RQFKPERWLQEKHSI----NPFAHVPFGIGKRMCIGRRLAELQLQLALCWIIQKYQ 395
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
314-551 8.39e-18

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: 85.93  E-value: 8.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 314 ERIKMWRE-GKRTQIEDFLDIFI-SIKDEAGQPL--LTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAME 389
Cdd:cd20650   188 KKIKESRLdSTQKHRVDFLQLMIdSQNSKETESHkaLSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQE 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 390 EIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAfNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPL 469
Cdd:cd20650   268 EIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAG-RLERVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPE 346
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 470 SFKPERHLNECSEvtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAgSETRVELMESSHDMFL-SKP 548
Cdd:cd20650   347 EFRPERFSKKNKD---NIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPC-KETQIPLKLSLQGLLQpEKP 422

                  ...
gi 1039011928 549 LVL 551
Cdd:cd20650   423 IVL 425
PLN02738 PLN02738
carotene beta-ring hydroxylase
358-536 1.31e-17

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 86.12  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 358 LVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGkERFVQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVALSD 437
Cdd:PLN02738  399 MLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLG-DRFPTIEDMKKLKYTTRVINESLRLYPQPPV-LIRRSLEN 476
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 438 TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLA 517
Cdd:PLN02738  477 DMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWPLDGPNPNETNQNFSYLPFGGGPRKCVGDMFASFENVVATA 556
                         170
                  ....*....|....*....
gi 1039011928 518 RLLQGFKWKLAGSETRVEL 536
Cdd:PLN02738  557 MLVRRFDFQLAPGAPPVKM 575
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
295-543 2.65e-17

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 84.33  E-value: 2.65e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 295 KIMRESSAIMDKYHDPIID--ERIKMWREGKRTQI------EDFLD-----IFISIKDEagqplLTADEIKPTIKELVMA 361
Cdd:cd20616   161 DIFFKISWLYKKYEKAVKDlkDAIEILIEQKRRRIstaeklEDHMDfatelIFAQKRGE-----LTAENVNQCVLEMLIA 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 362 APDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGkERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHvALSDTTVA 441
Cdd:cd20616   236 APDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRK-ALEDDVID 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 442 GYHIPKGSQVLLSrygLGRNPKV--WSDPLSFKPErhlNECSEVTLTEndlrFISFSTGKRGCAAPALGTAITTMMLARL 519
Cdd:cd20616   314 GYPVKKGTNIILN---IGRMHRLefFPKPNEFTLE---NFEKNVPSRY----FQPFGFGPRSCVGKYIAMVMMKAILVTL 383
                         250       260
                  ....*....|....*....|....
gi 1039011928 520 LQGFKWKLAGSETrVELMESSHDM 543
Cdd:cd20616   384 LRRFQVCTLQGRC-VENIQKTNDL 406
PLN02936 PLN02936
epsilon-ring hydroxylase
358-527 2.89e-17

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 84.84  E-value: 2.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 358 LVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGkERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSD 437
Cdd:PLN02936  286 MLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ-GRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVED 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 438 TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLA 517
Cdd:PLN02936  365 VLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPVPNETNTDFRYIPFSGGPRKCVGDQFALLEAIVALA 444
                         170
                  ....*....|
gi 1039011928 518 RLLQGFKWKL 527
Cdd:PLN02936  445 VLLQRLDLEL 454
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
50-532 3.13e-17

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 84.60  E-value: 3.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  50 LLTTLQALAALCFLMILNKIKSSSRNKKLhPLPPGPTGFPIVGMIPAMLKNRP-VFrwLHSLMKELNTeiacvrLGNTHV 128
Cdd:PLN02196    6 LFLTLFAGALFLCLLRFLAGFRRSSSTKL-PLPPGTMGWPYVGETFQLYSQDPnVF--FASKQKRYGS------VFKTHV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 129 IPVTC-----PKIAREIFKQQDALFasRPLTYAQKILSNGyKTCVITPFGEQFKKMRKVIMTEIVCPARHRWLHDNRAEE 203
Cdd:PLN02196   77 LGCPCvmissPEAAKFVLVTKSHLF--KPTFPASKERMLG-KQAIFFHQGDYHAKLRKLVLRAFMPDAIRNMVPDIESIA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 204 TDHLTAWLYNMVKNSEPVdlrfvtRHYCGNAIKRLMFGTRTFSEKteadggptlEDIEHMDAMFEGlGFtfafcisDYLP 283
Cdd:PLN02196  154 QESLNSWEGTQINTYQEM------KTYTFNVALLSIFGKDEVLYR---------EDLKRCYYILEK-GY-------NSMP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 284 M-LTGLDLNGHEKIMRESSAIMDKyhdpIIDERikmwREGKRTQiEDFLDIFIsiKDEAGqplLTADEIKPTIKELVMAA 362
Cdd:PLN02196  211 InLPGTLFHKSMKARKELAQILAK----ILSKR----RQNGSSH-NDLLGSFM--GDKEG---LTDEQIADNIIGVIFAA 276
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 363 PDNPSNAVEWAIAEMINKPEILHKAMEE---IDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHvALSDTT 439
Cdd:PLN02196  277 RDTTASVLTWILKYLAENPSVLEAVTEEqmaIRKDKEEGESLTWEDTKKMPLTSRVIQETLRVASILSFTFRE-AVEDVE 355
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 440 VAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHlnecsEVTLTENDlrFISFSTGKRGCAAPALGTAITTMMLARL 519
Cdd:PLN02196  356 YEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRF-----EVAPKPNT--FMPFGNGTHSCPGNELAKLEISVLIHHL 428
                         490
                  ....*....|...
gi 1039011928 520 LQGFKWKLAGSET 532
Cdd:PLN02196  429 TTKYRWSIVGTSN 441
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
298-524 3.59e-17

cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes are known for known for omega-hydroxylation of very long fatty acids (VLFA; C18-C26), leukotrienes, prostaglandins, and vitamins with long alkyl side chains. The CYP4F subfamily show diverse specificities among its members: CYP4F2 and CYP4F3 metabolize pro- and anti-inflammatory leukotrienes; CYP4F8 and CYP4F12 metabolize prostaglandins, endoperoxides and arachidonic acid; CYP4F11 and CYP4F12 metabolize VLFA and are unique in the CYP4F subfamily since they also hydroxylate xenobiotics such as benzphetamine, ethylmorphine, erythromycin, and ebastine. CYP4F belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 83.97  E-value: 3.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 298 RESSAIMDKYHDPIIDER---------IKMWREGKRTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSN 368
Cdd:cd20679   184 RRACRLVHDFTDAVIQERrrtlpsqgvDDFLKAKAKSKTLDFIDVLLLSKDEDGKEL-SDEDIRAEADTFMFEGHDTTAS 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 369 AVEWAIAEMINKPEILHKAMEEIDRVVgKERFVQE---SDIPKLNYVKAIIREAFRLHP----VAAFNLPHVALSDTTVa 441
Cdd:cd20679   263 GLSWILYNLARHPEYQERCRQEVQELL-KDREPEEiewDDLAQLPFLTMCIKESLRLHPpvtaISRCCTQDIVLPDGRV- 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 442 gyhIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQ 521
Cdd:cd20679   341 ---IPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQ---GRSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLL 414

                  ...
gi 1039011928 522 GFK 524
Cdd:cd20679   415 RFR 417
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
342-524 3.95e-17

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


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 84.00  E-value: 3.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 342 GQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEidrvVGKERFVQESDIPKL----NYVKAIIR 417
Cdd:cd20643   226 LQDKLPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAE----VLAARQEAQGDMVKMlksvPLLKAAIK 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 418 EAFRLHPVAAfNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsevtlTENDLRFISFST 497
Cdd:cd20643   302 ETLRLHPVAV-SLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSK------DITHFRNLGFGF 374
                         170       180
                  ....*....|....*....|....*..
gi 1039011928 498 GKRGCAAPALGTAITTMMLARLLQGFK 524
Cdd:cd20643   375 GPRQCLGRRIAETEMQLFLIHMLENFK 401
PLN02302 PLN02302
ent-kaurenoic acid oxidase
311-548 1.92e-16

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 82.07  E-value: 1.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 311 IIDERIKMWREGKRTQIEDFLDIFISIKDEAGQPlLTADEIkptIKELVM---AAPDNPSNAVEWAIAEMINKPEILHKA 387
Cdd:PLN02302  249 IVDERRNSRKQNISPRKKDMLDLLLDAEDENGRK-LDDEEI---IDLLLMylnAGHESSGHLTMWATIFLQEHPEVLQKA 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 388 MEEIDRVVGK----ERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHvALSDTTVAGYHIPKGSQVLLSRYGLGRNPK 463
Cdd:PLN02302  325 KAEQEEIAKKrppgQKGLTLKDVRKMEYLSQVIDETLRLINISLTVFRE-AKTDVEVNGYTIPKGWKVLAWFRQVHMDPE 403
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 464 VWSDPLSFKPERHLNEcsevtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGSETRVelmesshdM 543
Cdd:PLN02302  404 VYPNPKEFDPSRWDNY------TPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERLNPGCKV--------M 469

                  ....*
gi 1039011928 544 FLSKP 548
Cdd:PLN02302  470 YLPHP 474
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
338-541 3.37e-16

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: 81.04  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 338 KDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIR 417
Cdd:cd20649   249 KPSKQKRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIA 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 418 EAFRLHPvAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtlTENDLRFISFST 497
Cdd:cd20649   329 ETLRMYP-PAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQ---RRHPFVYLPFGA 404
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1039011928 498 GKRGCAAPALGTAITTMMLARLLQGFKWKlAGSETRVELMESSH 541
Cdd:cd20649   405 GPRSCIGMRLALLEIKVTLLHILRRFRFQ-ACPETEIPLQLKSK 447
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
367-502 6.05e-16

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: 80.05  E-value: 6.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 367 SNAVE---WAIAEMINKPEILHKAMEEIDRVVGKERF----VQESDIPKLNYVKAIIREAFRLHPVAAfnLPHVALSDTT 439
Cdd:cd20635   224 ANAIPitfWTLAFILSHPSVYKKVMEEISSVLGKAGKdkikISEDDLKKMPYIKRCVLEAIRLRSPGA--ITRKVVKPIK 301
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039011928 440 VAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERhlneCSEVTLTENDL--RFISFSTGKRGC 502
Cdd:cd20635   302 IKNYTIPAGDMLMLSPYWAHRNPKYFPDPELFKPER----WKKADLEKNVFleGFVAFGGGRYQC 362
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
358-523 1.40e-15

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: 79.05  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 358 LVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSD 437
Cdd:cd20672   234 LFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKD 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 438 TTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTENdlrFISFSTGKRGCaapaLGTAITTMML- 516
Cdd:cd20672   314 TLFRGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSEA---FMPFSTGKRIC----LGEGIARNELf 386
                         170
                  ....*....|
gi 1039011928 517 ---ARLLQGF 523
Cdd:cd20672   387 lffTTILQNF 396
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
292-527 1.68e-15

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 79.28  E-value: 1.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 292 GHEKIMRESSAIMDKYHDPIIDERIKmwREGKRTQIE----DFLDIFISIkDEAGQPLLTADE---IKPTIKELVMAAPD 364
Cdd:PLN02169  239 GLERKMRTALATVNRMFAKIISSRRK--EEISRAETEpyskDALTYYMNV-DTSKYKLLKPKKdkfIRDVIFSLVLAGRD 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 365 NPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKErfvqesDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYH 444
Cdd:PLN02169  316 TTSSALTWFFWLLSKHPQVMAKIRHEINTKFDNE------DLEKLVYLHAALSESMRLYPPLPFNHKAPAKPDVLPSGHK 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 445 IPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNECSEVTlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGF 523
Cdd:PLN02169  390 VDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGLR-HEPSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNY 468

                  ....
gi 1039011928 524 KWKL 527
Cdd:PLN02169  469 DFKV 472
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
329-530 3.48e-15

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: 77.88  E-value: 3.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 329 DFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPK 408
Cdd:cd20639   211 DLLGLMISAKNARNGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPK 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 409 LNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNECSEVtlTE 487
Cdd:cd20639   291 LKTLGMILNETLRLYPPAVA-TIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVARA--AK 367
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1039011928 488 NDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGS 530
Cdd:cd20639   368 HPLAFIPFGLGPRTCVGQNLAILEAKLTLAVILQRFEFRLSPS 410
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
372-534 2.41e-14

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: 75.09  E-value: 2.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 372 WAIAEMINKPEILHKAMEEIDRVVGKER-FVQESDIPKLN----YVKAIIREAFRLHpvAAFNLPHVALSDTTVAG-YHI 445
Cdd:cd11040   245 WLLAHILSDPELLERIREEIEPAVTPDSgTNAILDLTDLLtscpLLDSTYLETLRLH--SSSTSVRLVTEDTVLGGgYLL 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 446 PKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNECSEVTLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFK 524
Cdd:cd11040   323 RKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKKGRGLPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFD 402
                         170
                  ....*....|
gi 1039011928 525 WKLAGSETRV 534
Cdd:cd11040   403 VEPVGGGDWK 412
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
328-528 4.45e-14

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: 74.28  E-value: 4.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 328 EDFLDIFISIKDEAGQPLLTADEIKPTIKeLVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVvGKERFVQEsDIP 407
Cdd:cd11045   190 DDLFSALCRAEDEDGDRFSDDDIVNHMIF-LMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL-GKGTLDYE-DLG 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 408 KLNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtlte 487
Cdd:cd11045   267 QLEVTDWVFKEALRLVPPVPT-LPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAE----- 340
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1039011928 488 nDLR----FISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLA 528
Cdd:cd11045   341 -DKVhryaWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRWWSV 384
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
346-524 4.62e-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: 74.49  E-value: 4.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 346 LTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIdrvvgKERFVQESDIPK-----LNYVKAIIREAF 420
Cdd:cd20644   228 LSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQES-----LAAAAQISEHPQkalteLPLLKAALKETL 302
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 421 RLHPVAAFnLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLnecsEVTLTENDLRFISFSTGKR 500
Cdd:cd20644   303 RLYPVGIT-VQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWL----DIRGSGRNFKHLAFGFGMR 377
                         170       180
                  ....*....|....*....|....
gi 1039011928 501 GCAAPALGTAITTMMLARLLQGFK 524
Cdd:cd20644   378 QCLGRRLAEAEMLLLLMHVLKNFL 401
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
312-477 3.73e-13

cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins including Sinorhizobium fredii CYPBJ-4 homolog. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 71.32  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 312 IDERIKMWREGKRTQIED--FLDIFISIKDEAGQPLLTaDEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAME 389
Cdd:cd20614   169 IDARLSQLVATARANGARtgLVAALIRARDDNGAGLSE-QELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCD 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 390 EIDRVVGKERfvQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPL 469
Cdd:cd20614   248 EAAAAGDVPR--TPAELRRFPLAEALFRETLRLHPPVPF-VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPD 324

                  ....*...
gi 1039011928 470 SFKPERHL 477
Cdd:cd20614   325 RFRPERWL 332
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
290-534 5.53e-13

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 71.26  E-value: 5.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 290 LN-GHEKIMRESSAIMDKYHDPIIDERIKMWREGKRtqieDFLDIFI-SIKDEagqplltaDEIKPTIKELVMAAPDNPS 367
Cdd:PLN02426  243 LNiGSERKLKEAIKLVDELAAEVIRQRRKLGFSASK----DLLSRFMaSINDD--------KYLRDIVVSFLLAGRDTVA 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 368 NAVE---WAIAemiNKPEILHKAMEEIDRVVG-KERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGY 443
Cdd:PLN02426  311 SALTsffWLLS---KHPEVASAIREEADRVMGpNQEAASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLPDGT 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 444 HIPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNECSEVtlTENDLRFISFSTGKRGCAAPALgtAITTM--MLARLL 520
Cdd:PLN02426  388 FVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGVFV--PENPFKYPVFQAGLRVCLGKEM--ALMEMksVAVAVV 463
                         250
                  ....*....|....
gi 1039011928 521 QGFKWKLAGSETRV 534
Cdd:PLN02426  464 RRFDIEVVGRSNRA 477
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
281-528 1.52e-12

cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Arabidopsis thaliana CYP709B3 is involved in abscisic acid (ABA) and salt stress response. CYP709 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 69.78  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 281 YLPMLTGLDLNGHEKIMRESsaIMDkyhdpIIDERIKMWREGKRtqiEDFLDIFISI-----KDEAGQPLLTADEIKPTI 355
Cdd:cd20641   171 YLPTPRNLRVWKLEKKVRNS--IKR-----IIDSRLTSEGKGYG---DDLLGLMLEAassneGGRRTERKMSIDEIIDEC 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 356 KELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPvAAFNLPHVAL 435
Cdd:cd20641   241 KTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYG-PVINIARRAS 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 436 SDTTVAGYHIPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNECSEVTLTENDLrfISFSTGKRGCAAPALGTAITTM 514
Cdd:cd20641   320 EDMKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGVSRAATHPNAL--LSFSLGPRACIGQNFAMIEAKT 397
                         250
                  ....*....|....
gi 1039011928 515 MLARLLQGFKWKLA 528
Cdd:cd20641   398 VLAMILQRFSFSLS 411
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
292-537 1.81e-12

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 69.81  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 292 GHEKIMRESSAIMDKYHDPIIDERIKMWREGKRTQIE---DFLDIFISIkDEAGQPLLTADEIKPTIKELVMAAPDNPSN 368
Cdd:PLN03195  232 GSEALLSKSIKVVDDFTYSVIRRRKAEMDEARKSGKKvkhDILSRFIEL-GEDPDSNFTDKSLRDIVLNFVIAGRDTTAT 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 369 AVEWAIAEMINKPEILHKAMEEI--------------------DRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAF 428
Cdd:PLN03195  311 TLSWFVYMIMMNPHVAEKLYSELkalekerakeedpedsqsfnQRVTQFAGLLTYDSLGKLQYLHAVITETLRLYPAVPQ 390
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 429 NLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNEcsEVTLTENDLRFISFSTGKRGCAAPAL 507
Cdd:PLN03195  391 DPKGILEDDVLPDGTKVKAGGMVTYVPYSMGRMEYNWgPDAASFKPERWIKD--GVFQNASPFKFTAFQAGPRICLGKDS 468
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1039011928 508 GTAITTMMLARLLQGFKWKLA-GSETRVELM 537
Cdd:PLN03195  469 AYLQMKMALALLCRFFKFQLVpGHPVKYRMM 499
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
397-521 2.78e-12

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


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 68.71  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 397 KERFVQESDipklNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERH 476
Cdd:cd11067   254 RERLRSGDE----DYAEAFVQEVRRFYPFFPF-VGARARRDFEWQGYRFPKGQRVLLDLYGTNHDPRLWEDPDRFRPERF 328
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039011928 477 LnecsevTLTENDLRFI-----SFSTGKRgCAapalGTAITTMMLARLLQ 521
Cdd:cd11067   329 L------GWEGDPFDFIpqgggDHATGHR-CP----GEWITIALMKEALR 367
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
234-527 3.28e-11

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: 65.61  E-value: 3.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 234 AIKRLMFG--TRTF--SEKTEADGGPTLEDIEHMDAMFEGLgFTfafcisdyLPMltGLDLNGHEKIMRESSAIMDKYHD 309
Cdd:cd20638   125 EVKRLMFRiaMRILlgFEPQQTDREQEQQLVEAFEEMIRNL-FS--------LPI--DVPFSGLYRGLRARNLIHAKIEE 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 310 PIideRIKMWREGKRTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAME 389
Cdd:cd20638   194 NI---RAKIQREDTEQQCKDALQLLIEHSRRNGEPL-NLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRK 269
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 390 EIDRVVGKERFVQESD------IPKLNYVKAIIREAFRLHPVAAFNLpHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPK 463
Cdd:cd20638   270 ELQEKGLLSTKPNENKelsmevLEQLKYTGCVIKETLRLSPPVPGGF-RVALKTFELNGYQIPKGWNVIYSICDTHDVAD 348
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039011928 464 VWSDPLSFKPERHLNECSEvtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKL 527
Cdd:cd20638   349 IFPNKDEFNPDRFMSPLPE---DSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQL 409
PLN02290 PLN02290
cytokinin trans-hydroxylase
372-530 7.67e-11

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 64.45  E-value: 7.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 372 WAIAEMINKPEILHKAMEEIDRVVGKERFVQEsDIPKLNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYHIPKGSQV 451
Cdd:PLN02290  338 WTLMLLASNPTWQDKVRAEVAEVCGGETPSVD-HLSKLTLLNMVINESLRLYPPATL-LPRMAFEDIKLGDLHIPKGLSI 415
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 452 LLSRYGLGRNPKVW-SDPLSFKPERHLNEcsevtLTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGS 530
Cdd:PLN02290  416 WIPVLAIHHSEELWgKDANEFNPDRFAGR-----PFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDN 490
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
131-502 8.91e-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: 63.81  E-value: 8.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 131 VTCPKIAREIFKQQdALFASRPLTYAQKILSNGYKtcVITPFGEQFKKMRKvIMTEIVCPARHRWLHDNRAEETDHLTAW 210
Cdd:cd11051    15 VTDPELAEQITQVT-NLPKPPPLRKFLTPLTGGSS--LISMEGEEWKRLRK-RFNPGFSPQHLMTLVPTILDEVEIFAAI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 211 LYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRtFSEKTEADggPTLEDIEHMDAMFEGLGFTFafciSDYLPMLtgldl 290
Cdd:cd11051    91 LRELAESGEVFSLEELTTNLTFDVIGRVTLDID-LHAQTGDN--SLLTALRLLLALYRSLLNPF----KRLNPLR----- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 291 nghEKIMRESSAIMDKYHDPIIDERIKMwregkrtqiedfldifisikdeagqplltaDEIKPTIKELVMAAPDNPSNAV 370
Cdd:cd11051   159 ---PLRRWRNGRRLDRYLKPEVRKRFEL------------------------------ERAIDQIKTFLFAGHDTTSSTL 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 371 EWAIAEMINKPEILHKAMEEIDRVVGK-----ERFVQESD--IPKLNYVKAIIREAFRLHPVAA---FNLPHVALSDTTV 440
Cdd:cd11051   206 CWAFYLLSKHPEVLAKVRAEHDEVFGPdpsaaAELLREGPelLNQLPYTTAVIKETLRLFPPAGtarRGPPGVGLTDRDG 285
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011928 441 AGYHIPkGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNEcsevtlTENDLRFIS-----FSTGKRGC 502
Cdd:cd11051   286 KEYPTD-GCIVYVCHHAIHRDPEYWPRPDEFIPERWLVD------EGHELYPPKsawrpFERGPRNC 345
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
303-528 1.21e-10

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: 63.70  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 303 IMDKYHDPIIDERIKmwrEGKRTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPE 382
Cdd:cd20636   184 ILHEYMEKAIEEKLQ---RQQAAEYCDALDYMIHSARENGKEL-TMQELKESAVELIFAAFSTTASASTSLVLLLLQHPS 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 383 ILHKAMEEIDRvvgKERFVQESDIP---------KLNYVKAIIREAFRLHPVAAFNLpHVALSDTTVAGYHIPKGSQVLL 453
Cdd:cd20636   260 AIEKIRQELVS---HGLIDQCQCCPgalsleklsRLRYLDCVVKEVLRLLPPVSGGY-RTALQTFELDGYQIPKGWSVMY 335
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039011928 454 SRYGLGRNPKVWSDPLSFKPERHLNECSEVTLTEndLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLA 528
Cdd:cd20636   336 SIRDTHETAAVYQNPEGFDPDRFGVEREESKSGR--FNYIPFGGGVRSCIGKELAQVILKTLAVELVTTARWELA 408
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
193-533 2.43e-10

cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1.14.15.13), also called pulcherriminic acid synthase or cyclo-L-leucyl-L-leucyl dipeptide oxidase or cytochrome P450 CYPX, catalyzes the oxidation of cyclo(L-Leu-L-Leu) (cLL) to yield pulcherriminic acid which forms the red pigment pulcherrimin via a non-enzymatic spontaneous reaction with Fe(3+). It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 62.49  E-value: 2.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 193 HRWLHDNRAEETDHLTAW---------LYNMVKNSEPVDLRFVTRHYCGNAIKRLMfgtRTFSEKTEADGGPTLEDIEhM 263
Cdd:cd11080    21 RRILKDPDGFTTKSLAERaepvmrgpvLAQMTGKEHAAKRAIVVRAFRGDALDHLL---PLIKENAEELIAPFLERGR-V 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 264 DaMFEGLGFTFAFCISdyLPMLtGLDLNGHEKIMRESSAIMD-----------------------KYHDPIIDERikmwR 320
Cdd:cd11080    97 D-LVNDFGKPFAVNVT--MDML-GLDKRDHEKIHEWHSSVAAfitslsqdpearahglrcaeqlsQYLLPVIEER----R 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 321 EGKRTQIEDFLDIfISIKDEAgqplLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEidrvvgkerf 400
Cdd:cd11080   169 VNPGSDLISILCT-AEYEGEA----LSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRAD---------- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 401 vqesdiPKLnyVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPER-HLNE 479
Cdd:cd11080   234 ------RSL--VPRAIAETLRYHPPVQL-IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHReDLGI 304
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011928 480 CSEVTLTEndlRFISFSTGKRGCAAPALGTA----ITTMMLA-----RLLQGFKWKLAGSETR 533
Cdd:cd11080   305 RSAFSGAA---DHLAFGSGRHFCVGAALAKReieiVANQVLDalpniRLEPGFEYAESGLYTR 364
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
338-479 8.02e-10

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: 61.11  E-value: 8.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 338 KDEAGQPLLTA---DEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGkerfvqeSDIPKLN---- 410
Cdd:cd11082   205 AEEEGEPPPPHssdEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRP-------NDEPPLTldll 277
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039011928 411 ----YVKAIIREAFRLHPVAAFnLPHVALSDTTVA-GYHIPKGSQVLLSRYGLGRNPkvWSDPLSFKPERHLNE 479
Cdd:cd11082   278 eemkYTRQVVKEVLRYRPPAPM-VPHIAKKDFPLTeDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPE 348
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
311-530 8.75e-10

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: 61.14  E-value: 8.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 311 IIDERIKMWREGKRTQiEDFLDI-----FISIKDEAGQPL-LTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEIL 384
Cdd:cd20642   190 IINKREKAMKAGEATN-DDLLGIllesnHKEIKEQGNKNGgMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQ 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 385 HKAMEEIDRVVGKerfvQESDIPKLNYVKA---IIREAFRLHPvAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRN 461
Cdd:cd20642   269 ERAREEVLQVFGN----NKPDFEGLNHLKVvtmILYEVLRLYP-PVIQLTRAIHKDTKLGDLTLPAGVQVSLPILLVHRD 343
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 462 PKVW-SDPLSFKPERHLNECSEVtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLAGS 530
Cdd:cd20642   344 PELWgDDAKEFNPERFAEGISKA--TKGQVSYFPFGWGPRICIGQNFALLEAKMALALILQRFSFELSPS 411
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
261-528 1.03e-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: 60.63  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 261 EHMDAMFEglgfTFAFCISDYLPMLTGLDLNGHEKIMReSSAIMDKYHDPIIDERIKmwrEGKRTQIEDFLDIFISIKDE 340
Cdd:cd20637   146 EELSHLFS----VFQQFVENVFSLPLDLPFSGYRRGIR-ARDSLQKSLEKAIREKLQ---GTQGKDYADALDILIESAKE 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 341 AGQPLlTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEI-------DRVVGKERFVQESdIPKLNYVK 413
Cdd:cd20637   218 HGKEL-TMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELrsngilhNGCLCEGTLRLDT-ISSLKYLD 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 414 AIIREAFRLHPVAAFNLpHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtltENDLRF- 492
Cdd:cd20637   296 CVIKEVLRLFTPVSGGY-RTALQTFELDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQERSE----DKDGRFh 370
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1039011928 493 -ISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLA 528
Cdd:cd20637   371 yLPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFELA 407
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
311-525 1.71e-09

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 60.38  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 311 IIDERIKMWREGKRTQiEDFLDIFISIKDEagqplLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEE 390
Cdd:PLN02987  234 VVMKRRKEEEEGAEKK-KDMLAALLASDDG-----FSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEE 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 391 IDRVVGK---ERFVQESDIPKLNYVKAIIREAFRLHPVAAfNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSD 467
Cdd:PLN02987  308 HEKIRAMksdSYSLEWSDYKSMPFTQCVVNETLRVANIIG-GIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKD 386
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039011928 468 PLSFKPERHLNEcSEVTLTENdlRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKW 525
Cdd:PLN02987  387 ARTFNPWRWQSN-SGTTVPSN--VFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSW 441
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
343-502 2.52e-09

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


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 59.62  E-value: 2.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 343 QPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEI-------LHKAMEEI---DRVVGKERFVQeSDIPklnYV 412
Cdd:cd20622   255 KPDYYSQVIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVqsklrkaLYSAHPEAvaeGRLPTAQEIAQ-ARIP---YL 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 413 KAIIREAFRLHPvAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGlgrnPKVWSDPLS---------------------- 470
Cdd:cd20622   331 DAVIEEILRCAN-TAPILSREATVDTQVLGYSIPKGTNVFLLNNG----PSYLSPPIEidesrrssssaakgkkagvwds 405
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1039011928 471 -----FKPERHLNECSEVTLTENDLR---FISFSTGKRGC 502
Cdd:cd20622   406 kdiadFDPERWLVTDEETGETVFDPSagpTLAFGLGPRGC 445
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
356-528 4.04e-09

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: 58.96  E-value: 4.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 356 KELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVgKERFVQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVAL 435
Cdd:cd20640   236 KNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVC-KGGPPDADSLSRMKTVTMVIQETLRLYPPAAF-VSREAL 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 436 SDTTVAGYHIPKGSQVLLSRYGLGRNPKVW-SDPLSFKPERHLNECSEVTLTENdlRFISFSTGKRGCAAPALGTAITTM 514
Cdd:cd20640   314 RDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACKPPH--SYMPFGAGARTCLGQNFAMAELKV 391
                         170
                  ....*....|....
gi 1039011928 515 MLARLLQGFKWKLA 528
Cdd:cd20640   392 LVSLILSKFSFTLS 405
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
367-542 3.68e-08

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


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 55.59  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 367 SNAVEWAIAEMINKPEILHKAMEEIDRVVGKERFVQESdIPKLNYVKAIIREAFR---LHPVAAfNLPHValsDTTVAGY 443
Cdd:cd20627   219 ANLCTWAIYFLTTSEEVQKKLYKEVDQVLGKGPITLEK-IEQLRYCQQVLCETVRtakLTPVSA-RLQEL---EGKVDQH 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 444 HIPKGSQVLlsrYGLG---RNPKVWSDPLSFKPERHLNECSEVTLTendlrFISFStGKRGCAAPALGTAITTMMLARLL 520
Cdd:cd20627   294 IIPKETLVL---YALGvvlQDNTTWPLPYRFDPDRFDDESVMKSFS-----LLGFS-GSQECPELRFAYMVATVLLSVLV 364
                         170       180
                  ....*....|....*....|....*
gi 1039011928 521 QGFKW-KLAGS--ETRVELMESSHD 542
Cdd:cd20627   365 RKLRLlPVDGQvmETKYELVTSPRE 389
PLN02500 PLN02500
cytochrome P450 90B1
299-531 5.75e-08

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 55.25  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 299 ESSAIMDKYHDPIIDERI-KMWREGKRTQIEDFLDIFISikdeagQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEM 377
Cdd:PLN02500  233 KSRATILKFIERKMEERIeKLKEEDESVEEDDLLGWVLK------HSNLSTEQILDLILSLLFAGHETSSVAIALAIFFL 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 378 INKPEILHKAMEEIDRVVGKERFVQES-----DIPKLNYVKAIIREAFRLHPVAAFnLPHVALSDTTVAGYHIPKGSQVL 452
Cdd:PLN02500  307 QGCPKAVQELREEHLEIARAKKQSGESelnweDYKKMEFTQCVINETLRLGNVVRF-LHRKALKDVRYKGYDIPSGWKVL 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 453 LSRYGLGRNPKVWSDPLSFKPERHLNE------CSEVTLTENDlrFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWK 526
Cdd:PLN02500  386 PVIAAVHLDSSLYDQPQLFNPWRWQQNnnrggsSGSSSATTNN--FMPFGGGPRLCAGSELAKLEMAVFIHHLVLNFNWE 463

                  ....*
gi 1039011928 527 LAGSE 531
Cdd:PLN02500  464 LAEAD 468
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
348-521 1.39e-07

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: 53.88  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 348 ADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEIlhKAMEEIDRVVgkeRFVQESDipklNYVKAIIREAFRLHPVAA 427
Cdd:cd20612   185 ADEVRDNVLGTAVGGVPTQSQAFAQILDFYLRRPGA--AHLAEIQALA---RENDEAD----ATLRGYVLEALRLNPIAP 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 428 FnLPHVALSDTTVA-----GYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERhlnecsevtlteNDLRFISFSTGKRGC 502
Cdd:cd20612   256 G-LYRRATTDTTVAdgggrTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR------------PLESYIHFGHGPHQC 322
                         170
                  ....*....|....*....
gi 1039011928 503 AAPALGTAITTMMLARLLQ 521
Cdd:cd20612   323 LGEEIARAALTEMLRVVLR 341
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
294-519 2.11e-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: 52.98  E-value: 2.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 294 EKIMRESSAIMDkYHDPIIDERikmwregKRTQIEDFLDIFISIKDEaGQPLlTADEIKPTIKELVMAAPDNPSNAVEWA 373
Cdd:cd11035   144 EERAAAAQAVLD-YLTPLIAER-------RANPGDDLISAILNAEID-GRPL-TDDELLGLCFLLFLAGLDTVASALGFI 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 374 IAEMINKPEilhkameeiDRvvgkERFVQE-SDIPklnyvkAIIREAFRLHPVaaFNLPHVALSDTTVAGYHIPKGSQVL 452
Cdd:cd11035   214 FRHLARHPE---------DR----RRLREDpELIP------AAVEELLRRYPL--VNVARIVTRDVEFHGVQLKAGDMVL 272
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011928 453 LSRYGLGRNPKVWSDPLSFKPERHLNecsevtltendlRFISFSTGKRGCaapaLGtaittMMLARL 519
Cdd:cd11035   273 LPLALANRDPREFPDPDTVDFDRKPN------------RHLAFGAGPHRC----LG-----SHLARL 318
PLN02774 PLN02774
brassinosteroid-6-oxidase
48-535 4.05e-07

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 52.47  E-value: 4.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928  48 MYLLTTLQALAALCF-LMILNKIKSSSRNkklhpLPPGPTGFPIVGMIPAMLKNRPVFrwlhslMKELNteiacVRLGN- 125
Cdd:PLN02774    3 LVVLGVLVIIVCLCSaLLRWNEVRYSKKG-----LPPGTMGWPLFGETTEFLKQGPDF------MKNQR-----LRYGSf 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 126 --THVI---PVTC--PKIAREIFKQQDALFASrplTYAQKILSNGYKTCVITPFGEQFKKMRKVIMTeIVCPA--RHRWL 196
Cdd:PLN02774   67 fkSHILgcpTIVSmdPELNRYILMNEGKGLVP---GYPQSMLDILGTCNIAAVHGSTHRYMRGSLLS-LISPTmiRDHLL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 197 HDNRAEETDHLTAWlynmvKNSEPVDLRFVTRHycgnaikrlMFGTRTFSEKTEADGGPTLEdiEHMDAMFEGLGFTFAF 276
Cdd:PLN02774  143 PKIDEFMRSHLSGW-----DGLKTIDIQEKTKE---------MALLSALKQIAGTLSKPISE--EFKTEFFKLVLGTLSL 206
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 277 CISdyLPmltglDLNGHEKIMRESSaiMDKYHDPIIDERikmwREGKRTQiEDFLDIFIsiKDEAGQPLLTADEIKPTIK 356
Cdd:PLN02774  207 PID--LP-----GTNYRSGVQARKN--IVRMLRQLIQER----RASGETH-TDMLGYLM--RKEGNRYKLTDEEIIDQII 270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 357 ELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEidRVVGKERFVQE-----SDIPKLNYVKAIIREAFRLHPVAAFNLP 431
Cdd:PLN02774  271 TILYSGYETVSTTSMMAVKYLHDHPKALQELRKE--HLAIRERKRPEdpidwNDYKSMRFTRAVIFETSRLATIVNGVLR 348
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 432 HVAlSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECsevtlTENDLRFISFSTGKRGCAAPALGTAI 511
Cdd:PLN02774  349 KTT-QDMELNGYVIPKGWRIYVYTREINYDPFLYPDPMTFNPWRWLDKS-----LESHNYFFLFGGGTRLCPGKELGIVE 422
                         490       500
                  ....*....|....*....|....*....
gi 1039011928 512 TTMMLARLLQGFKWKLAGSET-----RVE 535
Cdd:PLN02774  423 ISTFLHYFVTRYRWEEVGGDKlmkfpRVE 451
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
335-479 1.09e-06

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 51.22  E-value: 1.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 335 ISIKDEAGQPLLTADEIKPTIKELVM--AAPDNPSNAVEWAIAEMINKPEILHKAMEEIDRVVGK---------ERFV-- 401
Cdd:cd20631   210 ISLRMLLNDTLSTLDEMEKARTHVAMlwASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEKtgqkvsdggNPIVlt 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 402 --QESDIPKLNyvkAIIREAFRLHPvAAFNLpHVALSDTTVA-----GYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPE 474
Cdd:cd20631   290 reQLDDMPVLG---SIIKEALRLSS-ASLNI-RVAKEDFTLHldsgeSYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYD 364

                  ....*
gi 1039011928 475 RHLNE 479
Cdd:cd20631   365 RYLDE 369
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
278-517 4.53e-06

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 48.96  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 278 ISDYLPM-----LTGLDLNGHEKIMRESSAiMDKYHDPIIDER------------IKMWRE--GKRTQI---EDFLDIFI 335
Cdd:cd20630   112 IAEHIPFrvisaMLGVPAEWDEQFRRFGTA-TIRLLPPGLDPEeletaapdvtegLALIEEviAERRQApveDDLLTTLL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 336 SIKDEAGQplLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMINKPEILHKAMEEidrvvgkerfvqesdiPKLnyVKAI 415
Cdd:cd20630   191 RAEEDGER--LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE----------------PEL--LRNA 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 416 IREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECsevtltendlrfISF 495
Cdd:cd20630   251 LEEVLRWDNFGKMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRRDPNAN------------IAF 318
                         250       260
                  ....*....|....*....|..
gi 1039011928 496 STGKRGCAAPALgtAITTMMLA 517
Cdd:cd20630   319 GYGPHFCIGAAL--ARLELELA 338
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
407-519 5.23e-06

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 48.73  E-value: 5.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 407 PKLnyVKAIIREAFRLH-PVAAFNlpHVALSDTTVAGYHIPKGSQVLLSrYG-LGRNPKVWSDPLSF----KPERHLnec 480
Cdd:cd11037   243 PSL--APNAFEEAVRLEsPVQTFS--RTTTRDTELAGVTIPAGSRVLVF-LGsANRDPRKWDDPDRFditrNPSGHV--- 314
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1039011928 481 sevtltendlrfiSFSTGKRGCAApalgtaittMMLARL 519
Cdd:cd11037   315 -------------GFGHGVHACVG---------QHLARL 331
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
384-521 1.41e-05

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: 47.64  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 384 LHKAM-EEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHP-VAAFNlpHVALSDTTV----AGYHIPKGSQVLLSRYG 457
Cdd:cd11071   259 LHARLaEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPpVPLQY--GRARKDFVIeshdASYKIKKGELLVGYQPL 336
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039011928 458 LGRNPKVWSDPLSFKPERHLNEcsEVTLtendLRFISFSTGK---------RGCAAPALGTAITTMMLARLLQ 521
Cdd:cd11071   337 ATRDPKVFDNPDEFVPDRFMGE--EGKL----LKHLIWSNGPeteeptpdnKQCPGKDLVVLLARLFVAELFL 403
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
412-476 2.26e-05

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 46.58  E-value: 2.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011928 412 VKAIIREAFRLH-PVAAFNlpHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERH 476
Cdd:cd11079   227 LPAAIDEILRLDdPFVANR--RITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDRH 290
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
433-519 5.75e-05

cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of bacterial cytochrome P450s from multiple families, including Mycobacterium smegmatis CYP164A2, Streptomyces sp. CYP245A1, Bacillus subtilis CYP107H1, Micromonospora echinospora P450 oxidase Calo2, and putative P450s such as Xylella fastidiosa CYP133 and Mycobacterium tuberculosis CYP140. CYP107H1, also called cytochrome P450(BioI), catalyzes the C-C bond cleavage of fatty acid linked to acyl carrier protein (ACP) to generate pimelic acid for biotin biosynthesis. CYP245A1, also called cytochrome P450 StaP, catalyzes the intramolecular C-C bond formation and oxidative decarboxylation of chromopyrrolic acid (CPA) to form the indolocarbazole core, a key step in staurosporine biosynthesis. CalO2 is involved in calicheamicin biosynthesis. The CYP164-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 45.62  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 433 VALSDTTVAGYHIPKGSQVLLsryGLG---RNPKVWSDPLSFKPERHLNecsevtltendlRFISFSTGKRGCaapaLGT 509
Cdd:cd20625   265 VALEDVEIGGQTIPAGDRVLL---LLGaanRDPAVFPDPDRFDITRAPN------------RHLAFGAGIHFC----LGA 325
                          90
                  ....*....|
gi 1039011928 510 AittmmLARL 519
Cdd:cd20625   326 P-----LARL 330
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
243-519 1.82e-04

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


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 44.13  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 243 RTFSEKTEADGGPTLEDI--EHMDAMFEGLGFTFafcISDY---LPMLTGLDLNG-----HEKIMRESSAIM-------- 304
Cdd:cd11078    81 RAFTPRRIAALEPRIRELaaELLDRLAEDGRADF---VADFaapLPALVIAELLGvpeedMERFRRWADAFAlvtwgrps 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 305 DKYHDPIIDERIKMWR------EGKRTQIEDFLDIFISIKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAIAEMI 378
Cdd:cd11078   158 EEEQVEAAAAVGELWAyfadlvAERRREPRDDLISDLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLL 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 379 NKPEILHKAMEeiDRvvgkerfvqeSDIPKlnyvkaIIREAFRLHPvAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGL 458
Cdd:cd11078   238 EHPDQWRRLRA--DP----------SLIPN------AVEETLRYDS-PVQGLRRTATRDVEIGGVTIPAGARVLLLFGSA 298
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039011928 459 GRNPKVWSDPLSFKPERhlnecsevtltENDLRFISFSTGKRGCaapaLGTAittmmLARL 519
Cdd:cd11078   299 NRDERVFPDPDRFDIDR-----------PNARKHLTFGHGIHFC----LGAA-----LARM 339
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
416-477 4.12e-04

cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 42.90  E-value: 4.12e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039011928 416 IREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSF----KPERHL 477
Cdd:cd11029   259 VEELLRYDGPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLditrDANGHL 324
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
412-478 4.16e-04

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 42.97  E-value: 4.16e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039011928 412 VKAIIREAFRLHPVAaFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLN 478
Cdd:cd11032   242 IPGAIEEVLRYRPPV-QRTARVTTEDVELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDRNPN 307
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
414-523 7.05e-04

AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis proteins including anthracycline biosynthesis proteins DnrQ and AknT, and macrolide antibiotic biosynthesis proteins TylM3 and DesVIII. Streptomyces peucetius DnrQ is involved in the biosynthesis of carminomycin and daunorubicin (daunomycin) while Streptomyces galilaeus AknT functions in the biosynthesis of aclacinomycin A. Streptomyces fradiae TylM3 is involved in the biosynthesis of tylosin derived from the polyketide lactone tylactone, and Streptomyces venezuelae functions in the biosynthesis of methymycin, neomethymycin, narbomycin, and pikromycin. These proteins are required for the glycosylation of specific substrates during the biosynthesis of specific anthracyclines and macrolide antibiotics. Although members of this family belong to the large cytochrome P450 (P450, CYP) superfamily and show significant similarity to cytochrome P450s, they lack heme-binding sites and are not functional cytochromes.


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 42.09  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039011928 414 AIIREAFRLHPVAAfNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERhlnecsevtlteNDLRFI 493
Cdd:cd11036   223 AAVAETLRYDPPVR-LERRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR------------PTARSA 289
                          90       100       110
                  ....*....|....*....|....*....|
gi 1039011928 494 SFSTGKRGCAAPALGTAITTMMLARLLQGF 523
Cdd:cd11036   290 HFGLGRHACLGAALARAAAAAALRALAARF 319
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
421-468 2.81e-03

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 40.20  E-value: 2.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1039011928 421 RLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDP 468
Cdd:cd11030   261 RYLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDP 308
 
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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