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Conserved domains on  [gi|584999|sp|Q07217|]
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RecName: Full=Cholesterol side-chain cleavage enzyme, mitochondrial; AltName: Full=CYPXIA1; AltName: Full=Cholesterol desmolase; AltName: Full=Cytochrome P450 11A1; AltName: Full=Cytochrome P450(scc); Flags: Precursor

Protein Classification

cytochrome P450 family protein (domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
80-504 0e+00

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: 850.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    80 FNTFGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRDYRNRKYGVLLKNGEDWRSNRVILNREVISP 159
Cdd:cd20643   1 FQKYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   160 KVLGNFVPLLDEVGQDFVARVHKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMF 239
Cdd:cd20643  81 KVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSNDLFRFALESICNVLYGERLGLLQDYVNPEAQRFIDAITLMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   240 KTTSPMLYIPPAMLRRVGAKIWRDHVEAWDGIFNQADRCIQNIYRTMRQDTNTHGKYPGVLASLLMLDKLSIEDIKASVT 319
Cdd:cd20643 161 HTTSPMLYIPPDLLRLINTKIWRDHVEAWDVIFNHADKCIQNIYRDLRQKGKNEHEYPGILANLLLQDKLPIEDIKASVT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   320 ELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYITEE 399
Cdd:cd20643 241 ELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITED 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   400 IVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQYFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENF 479
Cdd:cd20643 321 LVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRNLGFGFGPRQCLGRRIAETEMQLFLIHMLENF 400
                       410       420
                ....*....|....*....|....*
gi 584999   480 RVDKQRQVEVHSTFELILLPEKPIL 504
Cdd:cd20643 401 KIETQRLVEVKTTFDLILVPEKPIN 425
 
Name Accession Description Interval E-value
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
80-504 0e+00

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: 850.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    80 FNTFGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRDYRNRKYGVLLKNGEDWRSNRVILNREVISP 159
Cdd:cd20643   1 FQKYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   160 KVLGNFVPLLDEVGQDFVARVHKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMF 239
Cdd:cd20643  81 KVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSNDLFRFALESICNVLYGERLGLLQDYVNPEAQRFIDAITLMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   240 KTTSPMLYIPPAMLRRVGAKIWRDHVEAWDGIFNQADRCIQNIYRTMRQDTNTHGKYPGVLASLLMLDKLSIEDIKASVT 319
Cdd:cd20643 161 HTTSPMLYIPPDLLRLINTKIWRDHVEAWDVIFNHADKCIQNIYRDLRQKGKNEHEYPGILANLLLQDKLPIEDIKASVT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   320 ELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYITEE 399
Cdd:cd20643 241 ELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITED 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   400 IVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQYFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENF 479
Cdd:cd20643 321 LVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRNLGFGFGPRQCLGRRIAETEMQLFLIHMLENF 400
                       410       420
                ....*....|....*....|....*
gi 584999   480 RVDKQRQVEVHSTFELILLPEKPIL 504
Cdd:cd20643 401 KIETQRLVEVKTTFDLILVPEKPIN 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
50-507 2.37e-152

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 442.87  E-value: 2.37e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999      50 PGLWRNGLANLYSFWkLDGFRNIHRVMVHNFNTFGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRD 129
Cdd:pfam00067   1 PPGPPPLPLFGNLLQ-LGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     130 YRNRKYGVLLKNGEDWRSNRVILNREVISPKVLgNFVPLLDEVGQDFVARVHKKIERSGqdkwTTDLSQELFKYALESVG 209
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKL-SFEPRVEEEARDLVEKLRKTAGEPG----VIDITDLLFRAALNVIC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     210 SVLYGERLGLMLDYINPEAQHFIDCISLMFKTTSPMLYIPPAMLRRVGAKIWRDHVEAWDGIFNQADRCIQNIYRTMrqD 289
Cdd:pfam00067 155 SILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETL--D 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     290 TNTHGKYPGVLASLLMLD-----KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGD 364
Cdd:pfam00067 233 SAKKSPRDFLDALLLAKEeedgsKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     365 MLQMLKMIPLVKGALKETLRLHPVAV-SLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTEN 443
Cdd:pfam00067 313 TYDDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENG 392
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584999     444 ---QYFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENFRVDKQRQVEVHSTFEL--ILLPEKPILLTL 507
Cdd:pfam00067 393 kfrKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETpgLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
137-480 9.20e-39

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms];


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 146.03  E-value: 9.20e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   137 VLLKNGEDWRSNRVILNReVISPKVLGNFVPLLDEVgqdfVARVHKKIERSGQDkwttDLSQELFKYALESVGSVLyger 216
Cdd:COG2124  91 LLTLDGPEHTRLRKLLAP-AFTPRALRGYRPLIREI----ADRLLDDLWQGGAD----LVLDFAAELTLRVIAELL---- 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   217 lGLmldyinPEAQHFIDCISLMFKTTSPMLYIPPAMLrrvgakiWRDHVEAWDGIFNQADRCIQNIYRTMRQDtnthgky 296
Cdd:COG2124 158 -GV------PLEDRPQLLRWSDALLLRLDPDLGPEEP-------WRRARAARRELDAYLRALIAERRAAPRDD------- 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   297 pgvLASLLML------DKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAvarqstqgdmlqmlk 370
Cdd:COG2124 217 ---LLSLLLSaeddggGRLSDDEIRDELITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPD--------------- 278
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   371 mIPLVKGALKETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLrteNQYfrsLG 450
Cdd:COG2124 279 -RPLLEAVVEETLRLYPPVPLARRVATEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPERFN---NAH---LP 351
                       330       340       350
                ....*....|....*....|....*....|
gi 584999   451 FGFGPRQCLGRRIAETEMQLFLIHMLENFR 480
Cdd:COG2124 352 FGGGPHRCLGAALARLELKVALAELLRRFP 381
PTZ00404 PTZ00404
cytochrome P450; Provisional
57-501 4.25e-31

cytochrome P450; Provisional


Pssm-ID: 173595  Cd Length: 482  Bit Score: 125.61  E-value: 4.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     57 LANLYSFWKLDgfrniHRVMVHNFNTFGPIYREKIGYYDSVNIIKPEMPAILFKAEGHY----PKRLTVEAWTSYRdyrn 132
Cdd:PTZ00404  40 LGNLHQLGNLP-----HRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNfsdrPKIPSIKHGTFYH---- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    133 rkyGVLLKNGEDWRSNRVILNREVISPKVLGNFVPLLDEVgqDFVARVHKKIERSGQdkwTTDLSQELFKYALESVGSVL 212
Cdd:PTZ00404 111 ---GIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQV--DVLIESMKKIESSGE---TFEPRYYLTKFTMSAMFKYI 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    213 YGERLGLMLDYINPEAQHFIDCISLMFKT-TSPMLYIPPAMLRrvgaKIWRDHVEAWDGIFNQADRCIQNIYRTMRQDTN 291
Cdd:PTZ00404 183 FNEDISFDEDIHNGKLAELMGPMEQVFKDlGSGSLFDVIEITQ----PLYYQYLEHTDKNFKKIKKFIKEKYHEHLKTID 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    292 ThgKYPGVLASLLMLDKLSIED-----IKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDML 366
Cdd:PTZ00404 259 P--EVPRDLLDLLIKEYGTNTDddilsILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLL 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    367 QMLKMIPLVKGALKETLRLHPVAV-SLQRYITEEIVIQNYH-IPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTE-N 443
Cdd:PTZ00404 337 SDRQSTPYTVAIIKETLRYKPVSPfGLPRSTSNDIIIGGGHfIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDsN 416
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    444 QYFrsLGFGFGPRQCLGRRIAETEMQLFLIHMLENFRVDK--QRQVEVHSTFELILLPEK 501
Cdd:PTZ00404 417 DAF--MPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSidGKKIDETEEYGLTLKPNK 474
CYP450_TxtE TIGR04458
4-nitrotryptophan synthase; Members of this family are cytochrome P450 enzymes that convert ...
394-479 4.77e-07

4-nitrotryptophan synthase; Members of this family are cytochrome P450 enzymes that convert L-tryptophan into L-4-nitrotryptophan. In thaxtomin gene clusters, this enzyme (TxtE) uses nitric acid (NO) derived from arginine by the nitric oxide synthase TxtD, and O2, to perform the tryptophan nitration. L-4-nitrotryptophan is then used as a non-proteinogenic amino acid by non-ribosomal peptide synthases (NRPS).


Pssm-ID: 275251  Cd Length: 403  Bit Score: 51.80  E-value: 4.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     394 RYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRwlrteNQYFRSLGFGFGPRQCLGRRIAETEMQLFLI 473
Cdd:TIGR04458 295 RVATTDVDMGGVRIKAGQAVALFLGAANRDPEVFERPNDFDLDR-----PNSGRHLSFGQGVHACLGRQIASLQLKWFFV 369

                  ....*.
gi 584999     474 HMLENF 479
Cdd:TIGR04458 370 ALLGRF 375
 
Name Accession Description Interval E-value
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
80-504 0e+00

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: 850.54  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    80 FNTFGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRDYRNRKYGVLLKNGEDWRSNRVILNREVISP 159
Cdd:cd20643   1 FQKYGPIYREKIGYYESVNIINPEDAAILFKSEGMFPERLSVPPWVAYRDYRKRKYGVLLKNGEAWRKDRLILNKEVLAP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   160 KVLGNFVPLLDEVGQDFVARVHKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMF 239
Cdd:cd20643  81 KVIDNFVPLLNEVSQDFVSRLHKRIKKSGSGKWTADLSNDLFRFALESICNVLYGERLGLLQDYVNPEAQRFIDAITLMF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   240 KTTSPMLYIPPAMLRRVGAKIWRDHVEAWDGIFNQADRCIQNIYRTMRQDTNTHGKYPGVLASLLMLDKLSIEDIKASVT 319
Cdd:cd20643 161 HTTSPMLYIPPDLLRLINTKIWRDHVEAWDVIFNHADKCIQNIYRDLRQKGKNEHEYPGILANLLLQDKLPIEDIKASVT 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   320 ELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYITEE 399
Cdd:cd20643 241 ELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVLAARQEAQGDMVKMLKSVPLLKAAIKETLRLHPVAVSLQRYITED 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   400 IVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQYFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENF 479
Cdd:cd20643 321 LVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRNLGFGFGPRQCLGRRIAETEMQLFLIHMLENF 400
                       410       420
                ....*....|....*....|....*
gi 584999   480 RVDKQRQVEVHSTFELILLPEKPIL 504
Cdd:cd20643 401 KIETQRLVEVKTTFDLILVPEKPIN 425
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
80-506 0e+00

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: 537.12  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    80 FNTFGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRDYRNRKYGVLLKNGEDWRSNRVILNREVISP 159
Cdd:cd20644   1 FQELGPIYRENLGGPNMVNVMLPEDVEKLFQSEGLHPRRMTLEPWVAHRQHRGHKCGVFLLNGPEWRFDRLRLNPEVLSP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   160 KVLGNFVPLLDEVGQDFVARVHKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMF 239
Cdd:cd20644  81 AAVQRFLPMLDAVARDFSQALKKRVLQNARGSLTLDVQPDLFRFTLEASNLALYGERLGLVGHSPSSASLRFISAVEVML 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   240 KTTSPMLYIPPAMLRRVGAKIWRDHVEAWDGIFNQADRCIQNIYRTM--RQDTnthgKYPGVLASLLMLDKLSIEDIKAS 317
Cdd:cd20644 161 KTTVPLLFMPRSLSRWISPKLWKEHFEAWDCIFQYADNCIQKIYQELafGRPQ----HYTGIVAELLLQAELSLEAIKAN 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   318 VTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYIT 397
Cdd:cd20644 237 ITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQRVPS 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   398 EEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWL--RTENQYFRSLGFGFGPRQCLGRRIAETEMQLFLIHM 475
Cdd:cd20644 317 SDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLdiRGSGRNFKHLAFGFGMRQCLGRRLAEAEMLLLLMHV 396
                       410       420       430
                ....*....|....*....|....*....|.
gi 584999   476 LENFRVDKQRQVEVHSTFELILLPEKPILLT 506
Cdd:cd20644 397 LKNFLVETLSQEDIKTVYSFILRPEKPPLLT 427
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
80-503 3.04e-156

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: 451.60  E-value: 3.04e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    80 FNTFGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRDYRNRKYGVLLKNGEDWRSNRVILNREVISP 159
Cdd:cd11054   1 HKKYGPIVREKLGGRDIVHLFDPDDIEKVFRNEGKYPIRPSLEPLEKYRKKRGKPLGLLNSNGEEWHRLRSAVQKPLLRP 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   160 KVLGNFVPLLDEVGQDFVARVHKKieRSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMF 239
Cdd:cd11054  81 KSVASYLPAINEVADDFVERIRRL--RDEDGEEVPDLEDELYKWSLESIGTVLFGKRLGCLDDNPDSDAQKLIEAVKDIF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   240 KTTSPMLYIPPaMLRRVGAKIWRDHVEAWDGIFNQADRCIQNIYRTMRQDTNTHGKYPGVLASLLMLDKLSIEDIKASVT 319
Cdd:cd11054 159 ESSAKLMFGPP-LWKYFPTPAWKKFVKAWDTIFDIASKYVDEALEELKKKDEEDEEEDSLLEYLLSKPGLSKKEIVTMAL 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   320 ELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYITEE 399
Cdd:cd11054 238 DLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKD 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   400 IVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQY-----FRSLGFGFGPRQCLGRRIAETEMQLFLIH 474
Cdd:cd11054 318 IVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWLRDDSENknihpFASLPFGFGPRMCIGRRFAELEMYLLLAK 397
                       410       420
                ....*....|....*....|....*....
gi 584999   475 MLENFRVdKQRQVEVHSTFELILLPEKPI 503
Cdd:cd11054 398 LLQNFKV-EYHHEELKVKTRLILVPDKPL 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
50-507 2.37e-152

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 442.87  E-value: 2.37e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999      50 PGLWRNGLANLYSFWkLDGFRNIHRVMVHNFNTFGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRD 129
Cdd:pfam00067   1 PPGPPPLPLFGNLLQ-LGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     130 YRNRKYGVLLKNGEDWRSNRVILNREVISPKVLgNFVPLLDEVGQDFVARVHKKIERSGqdkwTTDLSQELFKYALESVG 209
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKL-SFEPRVEEEARDLVEKLRKTAGEPG----VIDITDLLFRAALNVIC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     210 SVLYGERLGLMLDYINPEAQHFIDCISLMFKTTSPMLYIPPAMLRRVGAKIWRDHVEAWDGIFNQADRCIQNIYRTMrqD 289
Cdd:pfam00067 155 SILFGERFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETL--D 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     290 TNTHGKYPGVLASLLMLD-----KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGD 364
Cdd:pfam00067 233 SAKKSPRDFLDALLLAKEeedgsKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     365 MLQMLKMIPLVKGALKETLRLHPVAV-SLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTEN 443
Cdd:pfam00067 313 TYDDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENG 392
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 584999     444 ---QYFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENFRVDKQRQVEVHSTFEL--ILLPEKPILLTL 507
Cdd:pfam00067 393 kfrKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETpgLLLPPKPYKLKF 461
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
81-505 2.63e-111

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: 337.02  E-value: 2.63e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    81 NTFGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRDYRNRKYGVLLKNGEDWRSNRVILNREVISPK 160
Cdd:cd20646   2 KIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGKYPMRSDMPHWKEHRDLRGHAYGPFTEEGEKWYRLRSVLNQRMLKPK 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   161 VLGNFVPLLDEVGQDFVARVHKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMFK 240
Cdd:cd20646  82 EVSLYADAINEVVSDLMKRIEYLRERSGSGVMVSDLANELYKFAFEGISSILFETRIGCLEKEIPEETQKFIDSIGEMFK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   241 TTSPMLYIPPAMlrRVGAKIWRDHVEAWDGIFNQADRCIQN----IYRTMRQDTNTHGKYpgvLASLLMLDKLSIEDIKA 316
Cdd:cd20646 162 LSEIVTLLPKWT--RPYLPFWKRYVDAWDTIFSFGKKLIDKkmeeIEERVDRGEPVEGEY---LTYLLSSGKLSPKEVYG 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   317 SVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYI 396
Cdd:cd20646 237 SLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVI 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   397 TE-EIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLR---TENQYFRSLGFGFGPRQCLGRRIAETEMQLFL 472
Cdd:cd20646 317 VEkEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRdggLKHHPFGSIPFGYGVRACVGRRIAELEMYLAL 396
                       410       420       430
                ....*....|....*....|....*....|....
gi 584999   473 IHMLENFRVDKQ-RQVEVHSTFELILLPEKPILL 505
Cdd:cd20646 397 SRLIKRFEVRPDpSGGEVKAITRTLLVPNKPINL 430
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
83-501 3.68e-92

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  Cd Length: 419  Bit Score: 287.47  E-value: 3.68e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    83 FGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRDYRNRKYGVLLKNGEDWRSNRVILNREVISPKVL 162
Cdd:cd20645   4 FGKIFRMKLGSFESVHIGSPCLLEALYRKESAYPQRLEIKPWKAYRDYRDEAYGLLILEGQEWQRVRSAFQKKLMKPKEV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   163 GNFVPLLDEVGQDFVARVHKKIERSGQdkwTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMFKTT 242
Cdd:cd20645  84 MKLDGKINEVLADFMGRIDELCDETGR---VEDLYSELNKWSFETICLVLYDKRFGLLQQNVEEEALNFIKAIKTMMSTF 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   243 SPMLYIPPAMLRRVGAKIWRDHVEAWDGIFNQADRCIQNiyRTMRQDTNTHGKYpgvLASLLMLDKLSIEDIKASVTELM 322
Cdd:cd20645 161 GKMMVTPVELHKRLNTKVWQDHTEAWDNIFKTAKHCIDK--RLQRYSQGPANDF---LCDIYHDNELSKKELYAAITELQ 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   323 AGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYITEEIVI 402
Cdd:cd20645 236 IGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVL 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   403 QNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQY--FRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENFR 480
Cdd:cd20645 316 GDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQEKHSInpFAHVPFGIGKRMCIGRRLAELQLQLALCWIIQKYQ 395
                       410       420
                ....*....|....*....|.
gi 584999   481 VDKQRQVEVHSTFELILLPEK 501
Cdd:cd20645 396 IVATDNEPVEMLHSGILVPSR 416
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
83-505 1.09e-87

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: 276.25  E-value: 1.09e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    83 FGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRDYRNRKYGVLLKNGEDWRSNRVILNREVISPKVL 162
Cdd:cd20648   5 YGPVWKASFGPILTVHVADPALIEQVLRQEGKHPVRSDLSSWKDYRQLRGHAYGLLTAEGEEWQRLRSLLAKHMLKPKAV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   163 GNFVPLLDEVGQDFVARVhKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMFKTT 242
Cdd:cd20648  85 EAYAGVLNAVVTDLIRRL-RRQRSRSSPGVVKDIAGEFYKFGLEGISSVLFESRIGCLEANVPEETETFIQSINTMFVMT 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   243 SPMLYIPPAmLRRVGAKIWRDHVEAWDGIFNQA----DRCIQNIYRTMRQDTNTHGKYpgvLASLLMLDKLSIEDIKASV 318
Cdd:cd20648 164 LLTMAMPKW-LHRLFPKPWQRFCRSWDQMFAFAkghiDRRMAEVAAKLPRGEAIEGKY---LTYFLAREKLPMKSIYGNV 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   319 TELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYITE 398
Cdd:cd20648 240 TELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPD 319
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   399 -EIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQY--FRSLGFGFGPRQCLGRRIAETEMQLFLIHM 475
Cdd:cd20648 320 rDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKGDTHhpYASLPFGFGKRSCIGRRIAELEVYLALARI 399
                       410       420       430
                ....*....|....*....|....*....|.
gi 584999   476 LENFRVD-KQRQVEVHSTFELILLPEKPILL 505
Cdd:cd20648 400 LTHFEVRpEPGGSPVKPMTRTLLVPERSINL 430
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
83-503 4.66e-87

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: 274.49  E-value: 4.66e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    83 FGPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEAWTSYRDYRNRKYGVLLKNGEDWRSNRVILNREVISPKVL 162
Cdd:cd20647   4 YGKIFKSHFGPQFVVSIADRDMVAQVLRAEGAAPQRANMESWQEYRDLRGRSTGLISAEGEQWLKMRSVLRQKILRPRDV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   163 GNFVPLLDEVGQDFVARVHKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMFKTT 242
Cdd:cd20647  84 AVYSGGVNEVVADLIKRIKTLRSQEDDGETVTNVNDLFFKYSMEGVATILYECRLGCLENEIPKQTVEYIEALELMFSMF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   243 SPMLYIP--PAMLRRVGAKIWRDHVEAWDGIFN----QADRCIQNIYRTMRQDTNTHGkypGVLASLLMLDKLSIEDIKA 316
Cdd:cd20647 164 KTTMYAGaiPKWLRPFIPKPWEEFCRSWDGLFKfsqiHVDNRLREIQKQMDRGEEVKG---GLLTYLLVSKELTLEEIYA 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   317 SVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYI 396
Cdd:cd20647 241 NMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLPGNGRVT 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   397 TEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTEN----QYFRSLGFGFGPRQCLGRRIAETEMQLFL 472
Cdd:cd20647 321 QDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDAldrvDNFGSIPFGYGIRSCIGRRIAELEIHLAL 400
                       410       420       430
                ....*....|....*....|....*....|..
gi 584999   473 IHMLENFRVDKQRQVE-VHSTFELILLPEKPI 503
Cdd:cd20647 401 IQLLQNFEIKVSPQTTeVHAKTHGLLCPGGSI 432
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
84-498 3.53e-68

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: 223.93  E-value: 3.53e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    84 GPIYREKIGYYDSVNIIKPEM-PAILFKAEGHYPKRLTVEAWTSyrdyRNRKYGVLLKNGEDWRSNRVILNREViSPKVL 162
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELvREVLRDPRDFSSDAGPGLPALG----DFLGDGLLTLDGPEHRRLRRLLAPAF-TPRAL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   163 GNFVPLLDEVGQDFVARvhkkIERSGQDKWttDLSQELFKYALESVGSVLYGERLGLMLDYInpeAQHFIDCISLMFKTT 242
Cdd:cd00302  76 AALRPVIREIARELLDR----LAAGGEVGD--DVADLAQPLALDVIARLLGGPDLGEDLEEL---AELLEALLKLLGPRL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   243 SPMLYIPPAMLRRVGAKIWRDHVEAWdgifnqadrciqniyRTMRQDTNTHGKYPGVLASLLMLDKLSIEDIKASVTELM 322
Cdd:cd00302 147 LRPLPSPRLRRLRRARARLRDYLEEL---------------IARRRAEPADDLDLLLLADADDGGGLSDEEIVAELLTLL 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   323 AGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQMLkmiPLVKGALKETLRLHPVAVSLQRYITEEIVI 402
Cdd:cd00302 212 LAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDGTPEDLSKL---PYLEAVVEETLRLYPPVPLLPRVATEDVEL 288
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   403 QNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWL-RTENQYFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENFRV 481
Cdd:cd00302 289 GGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLpEREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDF 368
                       410
                ....*....|....*..
gi 584999   482 DKQRQVEVHSTFELILL 498
Cdd:cd00302 369 ELVPDEELEWRPSLGTL 385
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
136-503 2.57e-50

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: 177.78  E-value: 2.57e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   136 GVLLKNGEDWRSNRVILNrEVISPKVLGNFVPLLDEVGQDFVARVHKKIERSGqdkwTTDLSQELFKYALESVGSVLYGe 215
Cdd:cd11055  51 SLLFLKGERWKRLRTTLS-PTFSSGKLKLMVPIINDCCDELVEKLEKAAETGK----PVDMKDLFQGFTLDVILSTAFG- 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   216 rlgLMLDYINPEAQHFIDCISLMFK--TTSPMLY--IPPAMLRRVGAKIWRDHVEAwdgifnqADRCIQNIYRTMRQ-DT 290
Cdd:cd11055 125 ---IDVDSQNNPDDPFLKAAKKIFRnsIIRLFLLllLFPLRLFLFLLFPFVFGFKS-------FSFLEDVVKKIIEQrRK 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   291 NTHGKYPGVLasLLMLD-----------KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVA-- 357
Cdd:cd11055 195 NKSSRRKDLL--QLMLDaqdsdedvskkKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVlp 272
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   358 -RQSTQGDMLQMLKMIPLVkgaLKETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPS 436
Cdd:cd11055 273 dDGSPTYDTVSKLKYLDMV---INETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPE 349
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584999   437 RWLRTENQYFRS---LGFGFGPRQCLGRRIAETEMQLFLIHMLENFRVD--KQRQVEVHSTFELILLPEKPI 503
Cdd:cd11055 350 RFSPENKAKRHPyayLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVpcKETEIPLKLVGGATLSPKNGI 421
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
84-505 8.93e-50

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: 176.17  E-value: 8.93e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    84 GPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKrltveawtSYrDYRNRK----YGVLLKNGEDWRSNRVILNREViSP 159
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPEDIEVILSSSKLITK--------SF-LYDFLKpwlgDGLLTSTGEKWRKRRKLLTPAF-HF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   160 KVLGNFVPLLDEVGQDFVARVHKKIersgqDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMF 239
Cdd:cd20628  71 KILESFVEVFNENSKILVEKLKKKA-----GGGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEIIL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   240 K-TTSPMLYIPPA-MLRRVGAKIWRDHVEAWDgiFNQ---ADR---CIQNIYRTMRQDTNTHGKYPGVLASLLMLDK--- 308
Cdd:cd20628 146 KrIFSPWLRFDFIfRLTSLGKEQRKALKVLHD--FTNkviKERreeLKAEKRNSEEDDEFGKKKRKAFLDLLLEAHEdgg 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   309 -LSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAV-----ARQSTQGDMLQM--LKMIplvkgaLK 380
Cdd:cd20628 224 pLTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEifgddDRRPTLEDLNKMkyLERV------IK 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   381 ETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRtENQYFRS----LGFGFGPR 456
Cdd:cd20628 298 ETLRLYPSVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLP-ENSAKRHpyayIPFSAGPR 376
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 584999   457 QCLGRRIAETEMQLFLIHMLENFRV---DKQRQVEVhsTFELILLPEKPILL 505
Cdd:cd20628 377 NCIGQKFAMLEMKTLLAKILRNFRVlpvPPGEDLKL--IAEIVLRSKNGIRV 426
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
83-492 6.45e-49

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: 174.38  E-value: 6.45e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    83 FGPIYREK-IGYYDSVNIIKPE-MPAILFKAEGHYPKrltveaWTSYRDYRNRKYG--VLLKNGEDWRSNRVILNReVIS 158
Cdd:cd11069   1 YGGLIRYRgLFGSERLLVTDPKaLKHILVTNSYDFEK------PPAFRRLLRRILGdgLLAAEGEEHKRQRKILNP-AFS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   159 PKVLGNFVPLLDEVGQDFVARVHKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHF---IDCI 235
Cdd:cd11069  74 YRHVKELYPIFWSKAEELVDKLEEEIEESGDESISIDVLEWLSRATLDIIGLAGFGYDFDSLENPDNELAEAYrrlFEPT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   236 SLMFKTTSPMLYIPPAMLRRVGAKIWRDHVEAWDGIFNQAdrciQNIYRTMRQD-TNTHGKYPGVLASLLM-------LD 307
Cdd:cd11069 154 LLGSLLFILLLFLPRWLVRILPWKANREIRRAKDVLRRLA----REIIREKKAAlLEGKDDSGKDILSILLrandfadDE 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   308 KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQM--LKMIPLVKGALKETLRL 385
Cdd:cd11069 230 RLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDGDLSYddLDRLPYLNAVCRETLRL 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   386 HPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVF-PRPEKYLPSRWL----RTENQYFRS----LGFGFGPR 456
Cdd:cd11069 310 YPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLepdgAASPGGAGSnyalLTFLHGPR 389
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 584999   457 QCLGRRIAETEMQLFLIHMLENFR--VDKQRQVEVHST 492
Cdd:cd11069 390 SCIGKKFALAEMKVLLAALVSRFEfeLDPDAEVERPIG 427
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
84-509 8.98e-49

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: 173.55  E-value: 8.98e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    84 GPIYREKIGYYDSV-----NIIKpEMpailFKAEGHY----PKRLTveawtsyRDYRNRKYGVLLKNGEDWRSNRVILNR 154
Cdd:cd20617   1 GGIFTLWLGDVPTVvlsdpEIIK-EA----FVKNGDNfsdrPLLPS-------FEIISGGKGILFSNGDYWKELRRFALS 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   155 EVISPKVLGNFVPL-LDEVgqDFVARVHKKIERSGQdkwTTDLSQELFKYALESVGSVLYGERLGlmlDYINPEAQHFID 233
Cdd:cd20617  69 SLTKTKLKKKMEELiEEEV--NKLIESLKKHSKSGE---PFDPRPYFKKFVLNIINQFLFGKRFP---DEDDGEFLKLVK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   234 CISLMFKT-TSPMLYIPPAMLRRVGAKIWRDHVEAWDGIFNQADRCIQNIYRTMrqDTNTHGKYPGVLASLLML----DK 308
Cdd:cd20617 141 PIEEIFKElGSGNPSDFIPILLPFYFLYLKKLKKSYDKIKDFIEKIIEEHLKTI--DPNNPRDLIDDELLLLLKegdsGL 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   309 LSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAE----VAVARQSTQGDMLQMlkmiPLVKGALKETLR 384
Cdd:cd20617 219 FDDDSIISTCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEidnvVGNDRRVTLSDRSKL----PYLNAVIKEVLR 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   385 LHPVA-VSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQYF--RSLGFGFGPRQCLGR 461
Cdd:cd20617 295 LRPILpLGLPRVTTEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGNKLseQFIPFGIGKRNCVGE 374
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 584999   462 RIAETEMQLFLIHMLENFrvdkqrqvEVHSTFELILLPEKPILLTLKP 509
Cdd:cd20617 375 NLARDELFLFFANLLLNF--------KFKSSDGLPIDEKEVFGLTLKP 414
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
137-476 6.49e-46

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: 165.83  E-value: 6.49e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   137 VLLKNGEDWRSNRVILNReVISPKVLGNFVPLLDEVGQDFVARVHKKIErsgqdkwttDLSQELFKYALESVGSVLYGER 216
Cdd:cd11065  54 LLMPYGPRWRLHRRLFHQ-LLNPSAVRKYRPLQELESKQLLRDLLESPD---------DFLDHIRRYAASIILRLAYGYR 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   217 LGLMLDYINPEAQHFIDCISLMFKTTSPML-------YIPPAML---RRVGAKIWRDHVEAWDGIFNQAdrciqniyrtm 286
Cdd:cd11065 124 VPSYDDPLLRDAEEAMEGFSEAGSPGAYLVdffpflrYLPSWLGapwKRKARELRELTRRLYEGPFEAA----------- 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   287 RQDTNTHGKYPGVLASLLML----DKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPD----LQEELRAEVAVAR 358
Cdd:cd11065 193 KERMASGTATPSFVKDLLEEldkeGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEvqkkAQEELDRVVGPDR 272
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   359 QSTQGDMLQMlkmiPLVKGALKETLRLHPVA-VSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSR 437
Cdd:cd11065 273 LPTFEDRPNL----PYVNAIVKEVLRWRPVApLGIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPER 348
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 584999   438 WLRTENQYF-----RSLGFGFGPRQCLGRRIAETEMQLFLIHML 476
Cdd:cd11065 349 YLDDPKGTPdppdpPHFAFGFGRRICPGRHLAENSLFIAIARLL 392
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
158-481 2.55e-45

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: 163.93  E-value: 2.55e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   158 SPKVLGNFVPLLDEVGQDFVARVhkkIERSGQDK-WTTDLSQELFKYALESVGSVLYGERLGlMLDyiNPEAQHFIDCIS 236
Cdd:cd11061  66 SDKALRGYEPRILSHVEQLCEQL---DDRAGKPVsWPVDMSDWFNYLSFDVMGDLAFGKSFG-MLE--SGKDRYILDLLE 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   237 LMFKTTSPMLYiPPAMLRRVGA-KIWRDHVEAWDGIFNQADRCiqniyrtMRQDTNTHGKYPGVLASLLMLDK------- 308
Cdd:cd11061 140 KSMVRLGVLGH-APWLRPLLLDlPLFPGATKARKRFLDFVRAQ-------LKERLKAEEEKRPDIFSYLLEAKdpetgeg 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   309 LSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGD-MLQMLKMIPLVKGALKETLRLHP 387
Cdd:cd11061 212 LDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIrLGPKLKSLPYLRACIDEALRLSP 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   388 -VAVSLQRyITEE--IVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQ------YFrsLGFGFGPRQC 458
Cdd:cd11061 292 pVPSGLPR-ETPPggLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEElvrarsAF--IPFSIGPRGC 368
                       330       340
                ....*....|....*....|...
gi 584999   459 LGRRIAETEMQLFLIHMLENFRV 481
Cdd:cd11061 369 IGKNLAYMELRLVLARLLHRYDF 391
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
84-479 2.18e-44

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: 161.95  E-value: 2.18e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    84 GPIYREKIGYYDSVNIIKPEMPAILFKAEGHY----PKRLTVEAwTSYrdyrNRKYGVLLKNGEDWRSNRVILNREVISP 159
Cdd:cd20618   1 GPLMYLRLGSVPTVVVSSPEMAKEVLKTQDAVfasrPRTAAGKI-FSY----NGQDIVFAPYGPHWRHLRKICTLELFSA 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   160 KVLGNFVPLLDEVGQDFVARVHKKIERSGqdkwTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMF 239
Cdd:cd20618  76 KRLESFQGVRKEELSHLVKSLLEESESGK----PVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEAREFKELIDEAF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   240 K-TTSPML--YIPP----------AMLRRVGAKIwrdhveawdgifnqaDRCIQNI---YRTMRQDTNTHGKYPGVLASL 303
Cdd:cd20618 152 ElAGAFNIgdYIPWlrwldlqgyeKRMKKLHAKL---------------DRFLQKIieeHREKRGESKKGGDDDDDLLLL 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   304 LMLD---KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPD----LQEELRAEVAVARQSTQGDMLQM--LKMIpl 374
Cdd:cd20618 217 LDLDgegKLSDDNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEvmrkAQEELDSVVGRERLVEESDLPKLpyLQAV-- 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   375 vkgaLKETLRLHPVA-VSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTE-----NQYFRS 448
Cdd:cd20618 295 ----VKETLRLHPPGpLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDiddvkGQDFEL 370
                       410       420       430
                ....*....|....*....|....*....|.
gi 584999   449 LGFGFGPRQCLGRRIAETEMQLFLIHMLENF 479
Cdd:cd20618 371 LPFGSGRRMCPGMPLGLRMVQLTLANLLHGF 401
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
141-481 3.59e-44

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: 161.17  E-value: 3.59e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   141 NGEDWRSNRVILNrEVISPKVLGNFVPLLDEVGQDFVARVHKKIERSGqdkwTTDLSQELFKYALESVGSVLYGerlglm 220
Cdd:cd11056  57 DGEKWKELRQKLT-PAFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGK----ELEIKDLMARYTTDVIASCAFG------ 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   221 LDYI---NPEAQhFIDCISLMFKTTSP------MLYIPPAMLRRVGAKIWRDHVEawdgifnqaDRCIQNIYRTMRQDTN 291
Cdd:cd11056 126 LDANslnDPENE-FREMGRRLFEPSRLrglkfmLLFFFPKLARLLRLKFFPKEVE---------DFFRKLVRDTIEYREK 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   292 THGKYPGVLASLL------------MLDKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQ 359
Cdd:cd11056 196 NNIVRNDFIDLLLelkkkgkieddkSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLE 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   360 STQG----DMLQ-M--LKMIplvkgaLKETLRLHPVAVSLQRYITEEIVI--QNYHIPCGTLVQLGLYAMGRDPDVFPRP 430
Cdd:cd11056 276 KHGGeltyEALQeMkyLDQV------VNETLRKYPPLPFLDRVCTKDYTLpgTDVVIEKGTPVIIPVYALHHDPKYYPEP 349
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 584999   431 EKYLPSRWLrTENQYFRS----LGFGFGPRQCLGRRIAETEMQLFLIHMLENFRV 481
Cdd:cd11056 350 EKFDPERFS-PENKKKRHpytyLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRV 403
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
84-509 2.00e-43

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: 158.51  E-value: 2.00e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    84 GPIYREKIGYYDSVNIIKPEmpailfkaeghYPKRLTVEAWTSYRdyRNRKY---------GVLLKNGEDWRSNRVILNR 154
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHPD-----------HIQHVLVTNARNYV--KGGVYerlklllgnGLLTSEGDLWRRQRRLAQP 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   155 eVISPKVLGNFVPLLDEVGQDFVARVHkkierSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDc 234
Cdd:cd20620  68 -AFHRRRIAAYADAMVEATAALLDRWE-----AGARRGPVDVHAEMMRLTLRIVAKTLFGTDVEGEADEIGDALDVALE- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   235 iSLMFKTTSPM---LYIPPAMLRRvgakiwrdhveawdgiFNQA----DRCIQNIYRTMRQDTNTHGKypgvLASLLML- 306
Cdd:cd20620 141 -YAARRMLSPFllpLWLPTPANRR----------------FRRArrrlDEVIYRLIAERRAAPADGGD----LLSMLLAa 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   307 ------DKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAE---VAVARQSTQGDMLQMlkmiPLVKG 377
Cdd:cd20620 200 rdeetgEPMSDQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEvdrVLGGRPPTAEDLPQL----PYTEM 275
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   378 ALKETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQ------YFRslgF 451
Cdd:cd20620 276 VLQESLRLYPPAWIIGREAVEDDEIGGYRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAarpryaYFP---F 352
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 584999   452 GFGPRQCLGRRIAETEMQLFLIHMLENFRVDkqrqvevhstfeliLLPEKPI----LLTLKP 509
Cdd:cd20620 353 GGGPRICIGNHFAMMEAVLLLATIAQRFRLR--------------LVPGQPVepepLITLRP 400
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
176-472 4.05e-42

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: 155.54  E-value: 4.05e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   176 FVARVHK---KIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMLDyINPEAQHFIdcisLMFKTTSPMLYIPPAM 252
Cdd:cd11059  80 IRERVLPlidRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLL-GDKDSRERE----LLRRLLASLAPWLRWL 154
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   253 LRRVGAKIWRDHVEAWDGIFNQADR-CIQNIYRTMRQDTNTHGKYPGVLASLLMLDK-----LSIEDIKASVTELMAGGV 326
Cdd:cd11059 155 PRYLPLATSRLIIGIYFRAFDEIEEwALDLCARAESSLAESSDSESLTVLLLEKLKGlkkqgLDDLEIASEALDHIVAGH 234
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   327 DTTSITLLWTLYELARHPDLQEELRAEVAVAR-QSTQGDMLQMLKMIPLVKGALKETLRLH-PVAVSLQRYITE-EIVIQ 403
Cdd:cd11059 235 DTTAVTLTYLIWELSRPPNLQEKLREELAGLPgPFRGPPDLEDLDKLPYLNAVIRETLRLYpPIPGSLPRVVPEgGATIG 314
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584999   404 NYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQYFRSL-----GFGFGPRQCLGRRIAETEMQLFL 472
Cdd:cd11059 315 GYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETAREMkrafwPFGSGSRMCIGMNLALMEMKLAL 388
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
137-480 9.20e-39

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms];


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 146.03  E-value: 9.20e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   137 VLLKNGEDWRSNRVILNReVISPKVLGNFVPLLDEVgqdfVARVHKKIERSGQDkwttDLSQELFKYALESVGSVLyger 216
Cdd:COG2124  91 LLTLDGPEHTRLRKLLAP-AFTPRALRGYRPLIREI----ADRLLDDLWQGGAD----LVLDFAAELTLRVIAELL---- 157
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   217 lGLmldyinPEAQHFIDCISLMFKTTSPMLYIPPAMLrrvgakiWRDHVEAWDGIFNQADRCIQNIYRTMRQDtnthgky 296
Cdd:COG2124 158 -GV------PLEDRPQLLRWSDALLLRLDPDLGPEEP-------WRRARAARRELDAYLRALIAERRAAPRDD------- 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   297 pgvLASLLML------DKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAvarqstqgdmlqmlk 370
Cdd:COG2124 217 ---LLSLLLSaeddggGRLSDDEIRDELITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPD--------------- 278
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   371 mIPLVKGALKETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLrteNQYfrsLG 450
Cdd:COG2124 279 -RPLLEAVVEETLRLYPPVPLARRVATEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPERFN---NAH---LP 351
                       330       340       350
                ....*....|....*....|....*....|
gi 584999   451 FGFGPRQCLGRRIAETEMQLFLIHMLENFR 480
Cdd:COG2124 352 FGGGPHRCLGAALARLELKVALAELLRRFP 381
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
135-480 1.48e-38

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: 145.82  E-value: 1.48e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   135 YGVLLKNGEDWRSNRVILNREvISPKVLGNFVPLLDEVGQDFVARVhkkieRSGQDKWTTDLSQELFKYALESVgsvlYG 214
Cdd:cd11057  45 RGLFSAPYPIWKLQRKALNPS-FNPKILLSFLPIFNEEAQKLVQRL-----DTYVGGGEFDILPDLSRCTLEMI----CQ 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   215 ERLGLMLDYINPEAQHFIDCISLMFKTT-----SPMLYiPPAMLRRVGAkiWRDHVEAW-------DGIFNQADRCIQNI 282
Cdd:cd11057 115 TTLGSDVNDESDGNEEYLESYERLFELIakrvlNPWLH-PEFIYRLTGD--YKEEQKARkilrafsEKIIEKKLQEVELE 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   283 YRTMRQDTNTHGKYPGVLASLLM-----LDKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQE----ELRAE 353
Cdd:cd11057 192 SNLDSEEDEENGRKPQIFIDQLLelarnGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEkvyeEIMEV 271
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   354 VAVARQSTQGDMLQMLKMIPLVkgaLKETLRLHPVAVSLQRYITEEIVIQN-YHIPCGTLVQLGLYAMGRDPDVF-PRPE 431
Cdd:cd11057 272 FPDDGQFITYEDLQQLVYLEMV---LKETMRLFPVGPLVGRETTADIQLSNgVVIPKGTTIVIDIFNMHRRKDIWgPDAD 348
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 584999   432 KYLPSRWLrTENQYFRS----LGFGFGPRQCLGRRIAETEMQLFLIHMLENFR 480
Cdd:cd11057 349 QFDPDNFL-PERSAQRHpyafIPFSAGPRNCIGWRYAMISMKIMLAKILRNYR 400
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
136-481 4.42e-38

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: 144.39  E-value: 4.42e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   136 GVLLKNGEDWRSNRViLNREVISPKVLGNFVPLLDEVGQdfvaRVHKKIERSGQDKWTTDLSQELFKYALESVGSVLYGE 215
Cdd:cd11083  50 GVFSAEGDAWRRQRR-LVMPAFSPKHLRYFFPTLRQITE----RLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGY 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   216 RLglmlDYINPEAQHFIDCISLMFkttsPMLYippamlRRVGAKI--WR----DHVEAWDGIFNQADRCIQNIYRTMRQD 289
Cdd:cd11083 125 DL----NTLERGGDPLQEHLERVF----PMLN------RRVNAPFpyWRylrlPADRALDRALVEVRALVLDIIAAARAR 190
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   290 TNTHGKYP----GVLASLLMLD----KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQST 361
Cdd:cd11083 191 LAANPALAeapeTLLAMMLAEDdpdaRLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGA 270
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   362 QG-DMLQMLKMIPLVKGALKETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWL- 439
Cdd:cd11083 271 RVpPLLEALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLd 350
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 584999   440 ---RTENQYFRS-LGFGFGPRQCLGRRIAETEMQLfLIHML-ENFRV 481
Cdd:cd11083 351 garAAEPHDPSSlLPFGAGPRLCPGRSLALMEMKL-VFAMLcRNFDI 396
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
73-513 5.30e-38

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: 144.20  E-value: 5.30e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    73 HRVMVHNFNTFGPIYREKIGYYDSVNIIKPEM-PAILFKaeGHYPKrltveawtSYRDYRNRK--YGV-LLKNG------ 142
Cdd:cd20613   1 HDLLLEWAKEYGPVFVFWILHRPIVVVSDPEAvKEVLIT--LNLPK--------PPRVYSRLAflFGErFLGNGlvtevd 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   143 -EDWRSNRVILNrEVISPKVLGNFVPLLDEVGQDFVARVHKKIErsgqDKWTTDLSQELFKYALESVGSVLYGERLGLML 221
Cdd:cd20613  71 hEKWKKRRAILN-PAFHRKYLKNLMDEFNESADLLVEKLSKKAD----GKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIE 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   222 DYINPeaqhFIDCISLMFK-----TTSPMLYIPP---AMLRRVgakiwrdhVEAWDGIFNQADRCIQNIYRTMRQDTNTH 293
Cdd:cd20613 146 DPDSP----FPKAISLVLEgiqesFRNPLLKYNPskrKYRREV--------REAIKFLRETGRECIEERLEALKRGEEVP 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   294 gkyPGVLASLL-MLD---KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEV-AV--ARQSTQGDML 366
Cdd:cd20613 214 ---NDILTHILkASEeepDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVdEVlgSKQYVEYEDL 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   367 QMLKMIPLVkgaLKETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQ-- 444
Cdd:cd20613 291 GKLEYLSQV---LKETLRLYPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEki 367
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 584999   445 -YFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENFRvdkqrqvevhstFELIllPEKPI----LLTLKPlKSG 513
Cdd:cd20613 368 pSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFK------------FELV--PGQSFgileEVTLRP-KDG 426
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
142-476 9.29e-38

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: 143.37  E-value: 9.29e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   142 GEDWRSNRVILNREVISPKVLGNFVPLLDEVgqdfVARVHKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLMl 221
Cdd:cd11072  60 GEYWRQMRKICVLELLSAKRVQSFRSIREEE----VSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGK- 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   222 dyinpEAQHFIDcisLMFKTTSpML-------YIPPA----MLRRVGAKIWRdhveawdgIFNQADRCIQNIYRTmRQDT 290
Cdd:cd11072 135 -----DQDKFKE---LVKEALE-LLggfsvgdYFPSLgwidLLTGLDRKLEK--------VFKELDAFLEKIIDE-HLDK 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   291 NTHGKYPGVLASLLMLD---------KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPD----LQEELRAEVAVA 357
Cdd:cd11072 197 KRSKDEDDDDDDLLDLRlqkegdlefPLTRDNIKAIILDMFLAGTDTSATTLEWAMTELIRNPRvmkkAQEEVREVVGGK 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   358 RQSTQGDMLQM--LKMIplvkgaLKETLRLHPVA-VSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYL 434
Cdd:cd11072 277 GKVTEEDLEKLkyLKAV------IKETLRLHPPApLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFR 350
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 584999   435 PSRWLRTE----NQYFRSLGFGFGPRQCLGRRIAETEMQLFLIHML 476
Cdd:cd11072 351 PERFLDSSidfkGQDFELIPFGAGRRICPGITFGLANVELALANLL 396
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
82-479 1.81e-37

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  Cd Length: 435  Bit Score: 143.06  E-value: 1.81e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    82 TFGPIYREKIGYYDSVNIIKPEM----------------PAILFKAEGHYpkrLTVEAWTSYrdyrnrkygvllknGEDW 145
Cdd:cd11073   3 KYGPIMSLKLGSKTTVVVSSPEAarevlkthdrvlsgrdVPDAVRALGHH---KSSIVWPPY--------------GPRW 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   146 RSNRVILNREVISPKVLGNFVPLLDEVGQDFVARVHKKIERSGqdkwTTDLSQELFKYALESVGSVLYGERLGlmlDYIN 225
Cdd:cd11073  66 RMLRKICTTELFSPKRLDATQPLRRRKVRELVRYVREKAGSGE----AVDIGRAAFLTSLNLISNTLFSVDLV---DPDS 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   226 PEAQHFIDCIS-LMFKTTSPML--YIPpaMLRRV---GAKIW-RDHVEAWDGIFnqaDRCIQNIYRTMRQDTNTHGKYPG 298
Cdd:cd11073 139 ESGSEFKELVReIMELAGKPNVadFFP--FLKFLdlqGLRRRmAEHFGKLFDIF---DGFIDERLAEREAGGDKKKDDDL 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   299 VLASLLMLD---KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPD----LQEELRAEVAVARQSTQGDMLQMlkm 371
Cdd:cd11073 214 LLLLDLELDsesELTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEkmakARAELDEVIGKDKIVEESDISKL--- 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   372 iPLVKGALKETLRLHPVAVSL-QRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQY----F 446
Cdd:cd11073 291 -PYLQAVVKETLRLHPPAPLLlPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFkgrdF 369
                       410       420       430
                ....*....|....*....|....*....|...
gi 584999   447 RSLGFGFGPRQCLGRRIAETEMQLFLIHMLENF 479
Cdd:cd11073 370 ELIPFGSGRRICPGLPLAERMVHLVLASLLHSF 402
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
99-508 6.57e-37

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: 141.31  E-value: 6.57e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    99 IIKPEMPAILFKAEGHYPKrltveawtSYRDYR-NRKYG--VLLKNGEDWRsnrviLNREVISPkVLGNFVPLLD----- 170
Cdd:cd11070  17 VTKPEYLTQIFRRRDDFPK--------PGNQYKiPAFYGpnVISSEGEDWK-----RYRKIVAP-AFNERNNALVweesi 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   171 EVGQDFVARVHKKIERSGQDkwTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQHFIDcISLMFKTTSPMLY-IP 249
Cdd:cd11070  83 RQAQRLIRYLLEEQPSAKGG--GVDVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHDTLNA-IKLAIFPPLFLNFpFL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   250 PAMLRRVGAKIWRdhveAWDGIFNQADRCIQNIYRTMRQDTNTHGKYPGVLASLLM----LDKLSIEDIKASVTELMAGG 325
Cdd:cd11070 160 DRLPWVLFPSRKR----AFKDVDEFLSELLDEVEAELSADSKGKQGTESVVASRLKrarrSGGLTEKELLGNLFIFFIAG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   326 VDTTSITLLWTLYELARHPDLQEELRAEV--AVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYITEEIVI- 402
Cdd:cd11070 236 HETTANTLSFALYLLAKHPEVQDWLREEIdsVLGDEPDDWDYEEDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVi 315
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   403 ----QNYHIPCGTLVQLGLYAMGRDPDV-FPRPEKYLPSRWLRT-----ENQYFRS-----LGFGFGPRQCLGRRIAETE 467
Cdd:cd11070 316 tglgQEIVIPKGTYVGYNAYATHRDPTIwGPDADEFDPERWGSTsgeigAATRFTPargafIPFSAGPRACLGRKFALVE 395
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 584999   468 MQLFLIHMLENFRvDKQRQVEVHSTFELILLPEKPILLTLK 508
Cdd:cd11070 396 FVAALAELFRQYE-WRVDPEWEEGETPAGATRDSPAKLRLR 435
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
135-480 1.12e-36

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: 140.50  E-value: 1.12e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   135 YGVLLKNGEDWRSNRVILNReVISPKVLGNFVPLLDEVGQDFVarvhkkieRSGQDKWTTDLSQELFKYALESVGSVLYG 214
Cdd:cd11044  69 NSLSLQDGEEHRRRRKLLAP-AFSREALESYVPTIQAIVQSYL--------RKWLKAGEVALYPELRRLTFDVAARLLLG 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   215 ERLGlmldyinPEAQHFidciSLMFKT-TSPMLYIPPamlrRVGAKIWRDHVEAWDGIFNQADRCIQniyrtmRQDTNTH 293
Cdd:cd11044 140 LDPE-------VEAEAL----SQDFETwTDGLFSLPV----PLPFTPFGRAIRARNKLLARLEQAIR------ERQEEEN 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   294 GKYPGVLASLL-----MLDKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQM 368
Cdd:cd11044 199 AEAKDALGLLLeakdeDGEPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEPLTLESL 278
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   369 LKMiPLVKGALKETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQYFRS 448
Cdd:cd11044 279 KKM-PYLDQVIKEVLRLVPPVGGGFRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKK 357
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 584999   449 ----LGFGFGPRQCLGRRIAETEMQLFLIHMLENFR 480
Cdd:cd11044 358 pfslIPFGGGPRECLGKEFAQLEMKILASELLRNYD 393
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
167-468 1.50e-36

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: 140.02  E-value: 1.50e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   167 PLLDEVGQDFVarvhKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLGLM---LDYinpeaQHFIDCISLMFKTTS 243
Cdd:cd11060  78 PFVDECIDLLV----DLLDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFGFLeagTDV-----DGYIASIDKLLPYFA 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   244 PMLYIPP--AMLRRVGAKIWRDHVEAWDGIFNQADRCIQNIYRTMRQDtntHGKYPGVLASLL-----MLDKLSIEDIKA 316
Cdd:cd11060 149 VVGQIPWldRLLLKNPLGPKRKDKTGFGPLMRFALEAVAERLAEDAES---AKGRKDMLDSFLeaglkDPEKVTDREVVA 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   317 SVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQS-------TQGDMLQMlkmiPLVKGALKETLRLHP-V 388
Cdd:cd11060 226 EALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEgklsspiTFAEAQKL----PYLQAVIKEALRLHPpV 301
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   389 AVSLQRYITEE-IVIQNYHIPCGTLVQLGLYAMGRDPDVF-PRPEKYLPSRWLRTE-------NQYFrsLGFGFGPRQCL 459
Cdd:cd11060 302 GLPLERVVPPGgATICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWLEADeeqrrmmDRAD--LTFGAGSRTCL 379

                ....*....
gi 584999   460 GRRIAETEM 468
Cdd:cd11060 380 GKNIALLEL 388
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
136-507 3.21e-36

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: 139.31  E-value: 3.21e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   136 GVLLKNGEDWRSNRVILNR----EVISpkvlgNFVPLLDEVGQDFVARVHKkiersgQDKWTTDLSQELfkyALESVGSV 211
Cdd:cd20621  50 GLLFSEGEEWKKQRKLLSNsfhfEKLK-----SRLPMINEITKEKIKKLDN------QNVNIIQFLQKI---TGEVVIRS 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   212 LYGERL-GLMLDYINPEAQHFIDCISLMFKTTSPMLYIPPAMLrrVGAKIWRdhveawdgIF-NQADRCIQNIYRTMRQ- 288
Cdd:cd20621 116 FFGEEAkDLKINGKEIQVELVEILIESFLYRFSSPYFQLKRLI--FGRKSWK--------LFpTKKEKKLQKRVKELRQf 185
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   289 -------------DTNTHGKYPGVLASLLML------DKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEE 349
Cdd:cd20621 186 iekiiqnrikqikKNKDEIKDIIIDLDLYLLqkkkleQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEK 265
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   350 LRAEV-AVARQSTQGDMLQMLKMiPLVKGALKETLRLHPVAVSL-QRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVF 427
Cdd:cd20621 266 LRQEIkSVVGNDDDITFEDLQKL-NYLNAFIKEVLRLYNPAPFLfPRVATQDHQIGDLKIKKGWIVNVGYIYNHFNPKYF 344
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   428 PRPEKYLPSRWLRTENQYFRS---LGFGFGPRQCLGRRIAETEMQLFLIHMLENFRVDKQRQVEVHSTFELILLPEKPIL 504
Cdd:cd20621 345 ENPDEFNPERWLNQNNIEDNPfvfIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIEIIPNPKLKLIFKLLYEPVNDLL 424

                ...
gi 584999   505 LTL 507
Cdd:cd20621 425 LKL 427
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
308-503 2.42e-35

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: 137.01  E-value: 2.42e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   308 KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEV-----AVARQSTQGDMLQMlkmiPLVKGALKET 382
Cdd:cd20660 227 KLSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELdrifgDSDRPATMDDLKEM----KYLECVIKEA 302
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   383 LRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLrTENQYFRS----LGFGFGPRQC 458
Cdd:cd20660 303 LRLFPSVPMFGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFL-PENSAGRHpyayIPFSAGPRNC 381
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 584999   459 LGRRIAETEMQLFLIHMLENFRVDK-QRQVEVHSTFELILLPEKPI 503
Cdd:cd20660 382 IGQKFALMEEKVVLSSILRNFRIESvQKREDLKPAGELILRPVDGI 427
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
195-481 2.75e-35

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: 136.56  E-value: 2.75e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   195 DLSQELFKYALESVGSVLYG----ERLGLMLdyinpeaQHFIDCISLmfkTTSPMLYIPPAMLRRVGAKIWRDHVEAWDg 270
Cdd:cd11053 112 DLRELMQEITLEVILRVVFGvddgERLQELR-------RLLPRLLDL---LSSPLASFPALQRDLGPWSPWGRFLRARR- 180
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   271 ifnQADRCIQNIYRTMRQDTNTHGkyPGVLaSLLML------DKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHP 344
Cdd:cd11053 181 ---RIDALIYAEIAERRAEPDAER--DDIL-SLLLSardedgQPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHP 254
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   345 DLQEELRAEVAvarQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDP 424
Cdd:cd11053 255 EVLARLLAELD---ALGGDPDPEDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRP 331
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 584999   425 DVFPRPEKYLPSRWLRTENQYFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENFRV 481
Cdd:cd11053 332 DLYPDPERFRPERFLGRKPSPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRL 388
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
193-481 5.29e-34

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: 132.77  E-value: 5.29e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   193 TTDLSQELFKYALESVGSVLYGERLGLMLdyiNPEAQHfidCISLMFKTTSPMLyIPPAMLRRVGAKIWRDHVEAWDGIF 272
Cdd:cd11049 109 VVDVDAEMHRLTLRVVARTLFSTDLGPEA---AAELRQ---ALPVVLAGMLRRA-VPPKFLERLPTPGNRRFDRALARLR 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   273 NQADRCIqniyRTMRQDTNTHGKypgvLASLLML------DKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDL 346
Cdd:cd11049 182 ELVDEII----AEYRASGTDRDD----LLSLLLAardeegRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEV 253
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   347 QEELRAEV-AVA--RQSTQGDmlqmLKMIPLVKGALKETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRD 423
Cdd:cd11049 254 ERRLHAELdAVLggRPATFED----LPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRD 329
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 584999   424 PDVFPRPEKYLPSRWLRTENQYFRS---LGFGFGPRQCLGRRIAETEMQLFLIHMLENFRV 481
Cdd:cd11049 330 PEVYPDPERFDPDRWLPGRAAAVPRgafIPFGAGARKCIGDTFALTELTLALATIASRWRL 390
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
308-505 7.63e-32

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: 126.90  E-value: 7.63e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   308 KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVA---RQSTQGDMLQMLKMIPLVkgaLKETLR 384
Cdd:cd20659 222 GLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVlgdRDDIEWDDLSKLPYLTMC---IKESLR 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   385 LHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLrTENQYFRS----LGFGFGPRQCLG 460
Cdd:cd20659 299 LYPPVPFIARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFL-PENIKKRDpfafIPFSAGPRNCIG 377
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 584999   461 RRIAETEMQLFLIHMLENFR--VDKQRQVEVHStfELILLPEKPILL 505
Cdd:cd20659 378 QNFAMNEMKVVLARILRRFElsVDPNHPVEPKP--GLVLRSKNGIKL 422
PTZ00404 PTZ00404
cytochrome P450; Provisional
57-501 4.25e-31

cytochrome P450; Provisional


Pssm-ID: 173595  Cd Length: 482  Bit Score: 125.61  E-value: 4.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     57 LANLYSFWKLDgfrniHRVMVHNFNTFGPIYREKIGYYDSVNIIKPEMPAILFKAEGHY----PKRLTVEAWTSYRdyrn 132
Cdd:PTZ00404  40 LGNLHQLGNLP-----HRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDNFDNfsdrPKIPSIKHGTFYH---- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    133 rkyGVLLKNGEDWRSNRVILNREVISPKVLGNFVPLLDEVgqDFVARVHKKIERSGQdkwTTDLSQELFKYALESVGSVL 212
Cdd:PTZ00404 111 ---GIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQV--DVLIESMKKIESSGE---TFEPRYYLTKFTMSAMFKYI 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    213 YGERLGLMLDYINPEAQHFIDCISLMFKT-TSPMLYIPPAMLRrvgaKIWRDHVEAWDGIFNQADRCIQNIYRTMRQDTN 291
Cdd:PTZ00404 183 FNEDISFDEDIHNGKLAELMGPMEQVFKDlGSGSLFDVIEITQ----PLYYQYLEHTDKNFKKIKKFIKEKYHEHLKTID 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    292 ThgKYPGVLASLLMLDKLSIED-----IKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDML 366
Cdd:PTZ00404 259 P--EVPRDLLDLLIKEYGTNTDddilsILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLL 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    367 QMLKMIPLVKGALKETLRLHPVAV-SLQRYITEEIVIQNYH-IPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTE-N 443
Cdd:PTZ00404 337 SDRQSTPYTVAIIKETLRYKPVSPfGLPRSTSNDIIIGGGHfIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDsN 416
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    444 QYFrsLGFGFGPRQCLGRRIAETEMQLFLIHMLENFRVDK--QRQVEVHSTFELILLPEK 501
Cdd:PTZ00404 417 DAF--MPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSidGKKIDETEEYGLTLKPNK 474
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
308-479 4.26e-31

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  Cd Length: 433  Bit Score: 125.02  E-value: 4.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   308 KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEV-AV---ARQSTQGDmLQMLkmiPLVKGALKETL 383
Cdd:cd20655 223 KITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIdSVvgkTRLVQESD-LPNL---PYLQAVVKETL 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   384 RLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTEN---------QYFRSLGFGFG 454
Cdd:cd20655 299 RLHPPGPLLVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLASSRsgqeldvrgQHFKLLPFGSG 378
                       170       180
                ....*....|....*....|....*
gi 584999   455 PRQCLGRRIAETEMQLFLIHMLENF 479
Cdd:cd20655 379 RRGCPGASLAYQVVGTAIAAMVQCF 403
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
142-479 5.21e-31

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: 124.66  E-value: 5.21e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   142 GEDWRSNRVILNREVISPKVLGNFVPLLDEVGQDFVARVHKKIERSGQDKWTTDLsqelFKYALESVGSVL-YGERLG-- 218
Cdd:cd11075  61 GPLWRTLRRNLVSEVLSPSRLKQFRPARRRALDNLVERLREEAKENPGPVNVRDH----FRHALFSLLLYMcFGERLDee 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   219 -----------LMLDYINPEAQHFIdcislmfkttspmlyipPAMLRRVGAKIWRDHVEAwdgIFNQADRCI-----QNI 282
Cdd:cd11075 137 tvrelervqreLLLSFTDFDVRDFF-----------------PALTWLLNRRRWKKVLEL---RRRQEEVLLpliraRRK 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   283 YRTMRQDTNTHGKYPGVLASLLMLD----KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVAR 358
Cdd:cd11075 197 RRASGEADKDYTDFLLLDLLDLKEEggerKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVV 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   359 QSTQGDMLQMLKMIPLVKGALKETLRLH-PVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSR 437
Cdd:cd11075 277 GDEAVVTEEDLPKMPYLKAVVLETLRRHpPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPER 356
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 584999   438 WLRTENQY--------FRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENF 479
Cdd:cd11075 357 FLAGGEAAdidtgskeIKMMPFGAGRRICPGLGLATLHLELFVARLVQEF 406
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
324-505 5.46e-31

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: 124.45  E-value: 5.46e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   324 GGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQS----TQGDMLQM--LKMIplvkgaLKETLRLHPVAVSLQRYIT 397
Cdd:cd20650 239 AGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNkappTYDTVMQMeyLDMV------VNETLRLFPIAGRLERVCK 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   398 EEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRtENQY----FRSLGFGFGPRQCLGRRIAETEMQLFLI 473
Cdd:cd20650 313 KDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSK-KNKDnidpYIYLPFGSGPRNCIGMRFALMNMKLALV 391
                       170       180       190
                ....*....|....*....|....*....|....
gi 584999   474 HMLENF--RVDKQRQVEVHSTFELILLPEKPILL 505
Cdd:cd20650 392 RVLQNFsfKPCKETQIPLKLSLQGLLQPEKPIVL 425
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
195-480 6.34e-31

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: 124.24  E-value: 6.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   195 DLSQELFKYALESVGSVLYGERLglmlDYINPEAQHFIDCISLMFKTTSP--MLYIPPaMLRRVGAKIWRD---HVEAWD 269
Cdd:cd11027 107 DPKDELFLAVLNVICSITFGKRY----KLDDPEFLRLLDLNDKFFELLGAgsLLDIFP-FLKYFPNKALRElkeLMKERD 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   270 GIFnqadrciQNIYRTMRqDTNTHGKYPGVLASLL------------MLDKLSIEDIKASVTELMAGGVDTTSITLLWTL 337
Cdd:cd11027 182 EIL-------RKKLEEHK-ETFDPGNIRDLTDALIkakkeaedegdeDSGLLTDDHLVMTISDIFGAGTETTATTLRWAI 253
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   338 YELARHPDLQEELRAE----VAVARQSTqgdmLQMLKMIPLVKGALKETLRLHPVA-VSLQRYITEEIVIQNYHIPCGTL 412
Cdd:cd11027 254 AYLVNYPEVQAKLHAElddvIGRDRLPT----LSDRKRLPYLEATIAEVLRLSSVVpLALPHKTTCDTTLRGYTIPKGTT 329
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 584999   413 VQLGLYAMGRDPDVFPRPEKYLPSRWLrTENQYFRS-----LGFGFGPRQCLGRRIAETEMQLFLIHMLENFR 480
Cdd:cd11027 330 VLVNLWALHHDPKEWDDPDEFRPERFL-DENGKLVPkpesfLPFSAGRRVCLGESLAKAELFLFLARLLQKFR 401
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
84-481 1.56e-30

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: 122.78  E-value: 1.56e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    84 GPIYREKIGYYDSVNIIKPEMPAILFKAEGHYPKRLTVEA-WTSYRDYRNrkyGVLLKNGEDWRSNRVILNREVISPKVL 162
Cdd:cd20615   1 GPIYRIWSGPTPEIVLTTPEHVKEFYRDSNKHHKAPNNNSgWLFGQLLGQ---CVGLLSGTDWKRVRKVFDPAFSHSAAV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   163 GNFVPLLDEVGQDFvarvhKKIERSGQDKWTTDL--SQELFKYALESVGSVLYGERLGLM---LDYINP---EA-QHFID 233
Cdd:cd20615  78 YYIPQFSREARKWV-----QNLPTNSGDGRRFVIdpAQALKFLPFRVIAEILYGELSPEEkeeLWDLAPlreELfKYVIK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   234 CISLMFKTTSpmlYIPPAMLRRVGA--KIWRDhveawdgiFNQAdrcIQNIYRTMRQDTNTHGKYPGVLASllmldKLSI 311
Cdd:cd20615 153 GGLYRFKISR---YLPTAANRRLREfqTRWRA--------FNLK---IYNRARQRGQSTPIVKLYEAVEKG-----DITF 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   312 EDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQ-MLKMIPLVKGALKETLRLHPVAV 390
Cdd:cd20615 214 EELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPMEDyILSTDTLLAYCVLESLRLRPLLA 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   391 -SLQRYITEEIVIQNYHIPCGTLVQLGLYAM-------GRDPDVFpRPEKYLPSRWLRTENQYFRslgFGFGPRQCLGRR 462
Cdd:cd20615 294 fSVPESSPTDKIIGGYRIPANTPVVVDTYALninnpfwGPDGEAY-RPERFLGISPTDLRYNFWR---FGFGPRKCLGQH 369
                       410
                ....*....|....*....
gi 584999   463 IAETEMQLFLIHMLENFRV 481
Cdd:cd20615 370 VADVILKALLAHLLEQYEL 388
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
154-479 3.07e-30

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: 122.36  E-value: 3.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   154 REVISP-----KVLgNFVPLLDEVGQDFVARVHKkIERSGQdkwTTDLSQELFKYALESVGSVLYGERLGLmLDYINPEA 228
Cdd:cd11062  59 RKALSPffskrSIL-RLEPLIQEKVDKLVSRLRE-AKGTGE---PVNLDDAFRALTADVITEYAFGRSYGY-LDEPDFGP 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   229 Q--HFIDCISLMFKTTSPMLYIPPAM--LRRVGAKIWRDHVEAWDGIfnqADRCIQNIYRTMRQ------DTNTHGKYPG 298
Cdd:cd11062 133 EflDALRALAEMIHLLRHFPWLLKLLrsLPESLLKRLNPGLAVFLDF---QESIAKQVDEVLRQvsagdpPSIVTSLFHA 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   299 VLASLLMLDKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDM-LQMLKMIPLVKG 377
Cdd:cd11062 210 LLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELKTAMPDPDSPPsLAELEKLPYLTA 289
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   378 ALKETLRL-HPVAVSLQRYITEE-IVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTEN-----QYFRSlg 450
Cdd:cd11062 290 VIKEGLRLsYGVPTRLPRVVPDEgLYYKGWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWLGAAEkgkldRYLVP-- 367
                       330       340
                ....*....|....*....|....*....
gi 584999   451 FGFGPRQCLGRRIAETEMQLFLIHMLENF 479
Cdd:cd11062 368 FSKGSRSCLGINLAYAELYLALAALFRRF 396
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
303-500 3.83e-30

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: 122.49  E-value: 3.83e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   303 LLMLDK------LSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVARQSTQGDMLQM--LKMIPL 374
Cdd:cd20679 228 VLLLSKdedgkeLSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEIEWddLAQLPF 307
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   375 VKGALKETLRLHPVAVSLQRYITEEIVIQNYH-IPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWlRTENQYFRS----L 449
Cdd:cd20679 308 LTMCIKESLRLHPPVTAISRCCTQDIVLPDGRvIPKGIICLISIYGTHHNPTVWPDPEVYDPFRF-DPENSQGRSplafI 386
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 584999   450 GFGFGPRQCLGRRIAETEMQLFLIHMLENFRV---DKqrqvEVHSTFELILLPE 500
Cdd:cd20679 387 PFSAGPRNCIGQTFAMAEMKVVLALTLLRFRVlpdDK----EPRRKPELILRAE 436
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
308-482 4.49e-29

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: 118.86  E-value: 4.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   308 KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEV-AVARQSTQGDMLQMLKMIPLVKGALKETLRLH 386
Cdd:cd11042 207 PLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQkEVLGDGDDPLTYDVLKEMPLLHACIKETLRLH 286
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   387 PVAVSLQRYITEEIVIQN--YHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQY-----FRSLGFGFGPRQCL 459
Cdd:cd11042 287 PPIHSLMRKARKPFEVEGggYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDskggkFAYLPFGAGRHRCI 366
                       170       180
                ....*....|....*....|...
gi 584999   460 GRRIAETEMQLFLIHMLENFRVD 482
Cdd:cd11042 367 GENFAYLQIKTILSTLLRNFDFE 389
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
324-505 7.54e-29

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  Cd Length: 441  Bit Score: 118.55  E-value: 7.54e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   324 GGVDTTSITLLWTLYELARHPDLQEELRAEV-AVARQSTQGDMLQMLKMiPLVKGALKETLRLHPVA-VSLQRYITEEIV 401
Cdd:cd11041 238 AAIHTTSMTLTHVLLDLAAHPEYIEPLREEIrSVLAEHGGWTKAALNKL-KKLDSFMKESQRLNPLSlVSLRRKVLKDVT 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   402 IQN-YHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLR------TENQY-FRS-----LGFGFGPRQCLGRRIAETEM 468
Cdd:cd11041 317 LSDgLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRlreqpgQEKKHqFVStspdfLGFGHGRHACPGRFFASNEI 396
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 584999   469 QLFLIHMLENFRV----DKQRQVEVHSTFELILLPEKPILL 505
Cdd:cd11041 397 KLILAHLLLNYDFklpeGGERPKNIWFGEFIMPDPNAKVLV 437
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
141-480 1.37e-28

cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins include: CYP78A5, which is expressed in leaf, flora and embryo, and has been reported to stimulate plant organ growth in Arabidopsis thaliana and to regulate plant architecture, ripening time, and fruit mass in tomato; Glycine max CYP78A10 that functions in regulating seed size/weight and pod number; and Physcomitrella patens CYP78A27 or CYP78A28, which together, are essential in bud formation. The CYP78 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 117.43  E-value: 1.37e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   141 NGEDWRSNRVILNREVISPKVLGNFVPLLDEVGQDFVARVHKKIERSGQdkwtTDLSQELFKYALESV-GSVLygerlGL 219
Cdd:cd11076  56 YGEYWRNLRRIASNHLFSPRRIAASEPQRQAIAAQMVKAIAKEMERSGE----VAVRKHLQRASLNNImGSVF-----GR 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   220 MLDYINPEAQHfiDCISLMFKTTSPMLyippamlrrvGAKIWRDH--VEAWDGIFNQADRC----------IQNIYRTMR 287
Cdd:cd11076 127 RYDFEAGNEEA--EELGEMVREGYELL----------GAFNWSDHlpWLRWLDLQGIRRRCsalvprvntfVGKIIEEHR 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   288 QDTNTHGK----YPGVLASLLMLDKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAVA----RQ 359
Cdd:cd11076 195 AKRSNRARddedDVDVLLSLQGEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAvggsRR 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   360 STQGDMLQMlkmiPLVKGALKETLRLHPVA--VSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSR 437
Cdd:cd11076 275 VADSDVAKL----PYLQAVVKETLRLHPPGplLSWARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPER 350
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|.
gi 584999   438 WLRTE-NQYFRSLG-------FGFGPRQCLGRRIAETEMQLFLIHMLENFR 480
Cdd:cd11076 351 FVAAEgGADVSVLGsdlrlapFGAGRRVCPGKALGLATVHLWVAQLLHEFE 401
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
307-503 1.84e-28

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: 117.55  E-value: 1.84e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   307 DKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEV-AVARQSTQGDMLQMLKMIPLVKGALKETLRL 385
Cdd:cd20680 237 NKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELdEVFGKSDRPVTMEDLKKLRYLECVIKESLRL 316
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   386 HPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLrTENQYFRS----LGFGFGPRQCLGR 461
Cdd:cd20680 317 FPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFF-PENSSGRHpyayIPFSAGPRNCIGQ 395
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 584999   462 RIAETEMQLFLIHMLENFRVD-KQRQVEVHSTFELILLPEKPI 503
Cdd:cd20680 396 RFALMEEKVVLSCILRHFWVEaNQKREELGLVGELILRPQNGI 438
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
141-485 2.31e-28

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: 116.58  E-value: 2.31e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   141 NGEDWRSNRVILNREvISPKVLGNFVPL-LDEVGQdFVARVHKKIeRSGQdkwTTDLSQELFKYALESVGSVLYGERLGL 219
Cdd:cd11051  53 EGEEWKRLRKRFNPG-FSPQHLMTLVPTiLDEVEI-FAAILRELA-ESGE---VFSLEELTTNLTFDVIGRVTLDIDLHA 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   220 MLDYiNPEAQHFIDCISL---MFKTTSPMLYIPPAMLRRVGAKIwrdhveawdgifnqaDRCIQNIYRTmrqdtnthgky 296
Cdd:cd11051 127 QTGD-NSLLTALRLLLALyrsLLNPFKRLNPLRPLRRWRNGRRL---------------DRYLKPEVRK----------- 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   297 pgvlasllmldKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEV---------AVARQSTQGDmlQ 367
Cdd:cd11051 180 -----------RFELERAIDQIKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHdevfgpdpsAAAELLREGP--E 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   368 MLKMIPLVKGALKETLRLHPVAVSL--------------QRYITEEIVIQNYHipcgtlvqlglYAMGRDPDVFPRPEKY 433
Cdd:cd11051 247 LLNQLPYTTAVIKETLRLFPPAGTArrgppgvgltdrdgKEYPTDGCIVYVCH-----------HAIHRDPEYWPRPDEF 315
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 584999   434 LPSRWLRTEN--QYFRSLG---FGFGPRQCLGRRIAETEMQLFLIHMLENFRVDKQR 485
Cdd:cd11051 316 IPERWLVDEGheLYPPKSAwrpFERGPRNCIGQELAMLELKIILAMTVRRFDFEKAY 372
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
167-479 1.89e-27

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: 114.22  E-value: 1.89e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   167 PLLDEVGQDFVARVHKKIERSGQ-D--KW----TTDLsqelfkyalesVGSVLYGERLGlMLDyiNPEAQHFIDCISLMF 239
Cdd:cd11058  79 PIIQRYVDLLVSRLRERAGSGTPvDmvKWfnftTFDI-----------IGDLAFGESFG-CLE--NGEYHPWVALIFDSI 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   240 KTTSPM---LYIPP------AMLRRVGAKIWRDHVEAwdgIFNQADRCIQNiyRTMRQDTNTHgkypgVLASLLMLDKLS 310
Cdd:cd11058 145 KALTIIqalRRYPWllrllrLLIPKSLRKKRKEHFQY---TREKVDRRLAK--GTDRPDFMSY-----ILRNKDEKKGLT 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   311 IEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVavaRQ--STQGDM-LQMLKMIPLVKGALKETLRLHP 387
Cdd:cd11058 215 REELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEI---RSafSSEDDItLDSLAQLPYLNAVIQEALRLYP 291
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   388 -VAVSLQRYITEE-IVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQYFRS--LG----FGFGPRQCL 459
Cdd:cd11058 292 pVPAGLPRVVPAGgATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFEFDNdkKEafqpFSVGPRNCI 371
                       330       340
                ....*....|....*....|
gi 584999   460 GRRIAETEMQLFLIHMLENF 479
Cdd:cd11058 372 GKNLAYAEMRLILAKLLWNF 391
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
142-479 4.22e-27

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  Cd Length: 438  Bit Score: 113.28  E-value: 4.22e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   142 GEDWRSNRVILNREVISPKVLGNFVPlldeVGQDFVARVHKKIERSGQDKWTTDLSQELFKYALESVGSVLYGERLglML 221
Cdd:cd20657  58 GPRWRLLRKLCNLHLFGGKALEDWAH----VRENEVGHMLKSMAEASRKGEPVVLGEMLNVCMANMLGRVMLSKRV--FA 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   222 DYINPEAQHFID-CISLMfkTTSPMLYIP---PAM----LRRVGAKIWRDHvEAWDGIFNQadrciqnIYRTMRQDTNTH 293
Cdd:cd20657 132 AKAGAKANEFKEmVVELM--TVAGVFNIGdfiPSLawmdLQGVEKKMKRLH-KRFDALLTK-------ILEEHKATAQER 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   294 GKYPGVLaSLLML--------DKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDL----QEELRAEVAVARQST 361
Cdd:cd20657 202 KGKPDFL-DFVLLenddngegERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDIlkkaQEEMDQVIGRDRRLL 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   362 QGDMLQMlkmiPLVKGALKETLRLHP-VAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLR 440
Cdd:cd20657 281 ESDIPNL----PYLQAICKETFRLHPsTPLNLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLP 356
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*.
gi 584999   441 TEN-------QYFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENF 479
Cdd:cd20657 357 GRNakvdvrgNDFELIPFGAGRRICAGTRMGIRMVEYILATLVHSF 402
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
82-481 1.15e-26

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: 112.62  E-value: 1.15e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    82 TFGPIYREKIGYYDSVNIIKPEM-PAILFKAEGHYPKRLTVEAWTsyrdyRNRKYGVLLKNGEDWRSNRVILNrEVISPK 160
Cdd:cd20649   1 KYGPICGYYIGRRMFVVIAEPDMiKQVLVKDFNNFTNRMKANLIT-----KPMSDSLLCLRDERWKRVRSILT-PAFSAA 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   161 VLGNFVPLLDEVGQDFVARVhKKIERSGQdkwTTDLSQELFKYALESVGSVLYGERLGLMLDYINPEAQH----FIDCIS 236
Cdd:cd20649  75 KMKEMVPLINQACDVLLRNL-KSYAESGN---AFNIQRCYGCFTMDVVASVAFGTQVDSQKNPDDPFVKNckrfFEFSFF 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   237 ---LMFKTTSPMLYIPpaMLRRVGAKIwRDHVeawDGIFNQadrCIQNIYRTMRQ------------------------- 288
Cdd:cd20649 151 rpiLILFLAFPFIMIP--LARILPNKS-RDEL---NSFFTQ---CIRNMIAFRDQqspeerrrdflqlmldartsakfls 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   289 ----------DTNTHGKYPGVLAS-----LLMLDKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAE 353
Cdd:cd20649 222 vehfdivndaDESAYDGHPNSPANeqtkpSKQKRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLRE 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   354 VAVARQSTQGDMLQMLKMIPLVKGALKETLRLHPVAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKY 433
Cdd:cd20649 302 VDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKF 381
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 584999   434 LPSRWL---RTENQYFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENFRV 481
Cdd:cd20649 382 IPERFTaeaKQRRHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRF 432
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
131-479 1.56e-26

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: 111.81  E-value: 1.56e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   131 RNRKYGVLLKNGED--WRSN-------RVILNREVISPKVLGNFVPLL-DEVGQdFVARVHKKIERSGQDKWTTDLSQEL 200
Cdd:cd20656  39 RTRSAARFSRNGQDliWADYgphyvkvRKLCTLELFTPKRLESLRPIReDEVTA-MVESIFNDCMSPENEGKPVVLRKYL 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   201 FKYALESVGSVLYGERLGLMLDYINPEAQHFIDCISLMFK---TTSPMLYIPpaMLRRVGA---KIWRDHVEAWDGIFnq 274
Cdd:cd20656 118 SAVAFNNITRLAFGKRFVNAEGVMDEQGVEFKAIVSNGLKlgaSLTMAEHIP--WLRWMFPlseKAFAKHGARRDRLT-- 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   275 adRCIQNIYRTMRQDTntHGKYPGVLASLLMLDK--LSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRA 352
Cdd:cd20656 194 --KAIMEEHTLARQKS--GGGQQHFVALLTLKEQydLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQE 269
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   353 E----VAVARQSTQGDMLQMlkmiPLVKGALKETLRLHP-VAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVF 427
Cdd:cd20656 270 EldrvVGSDRVMTEADFPQL----PYLQCVVKEALRLHPpTPLMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVW 345
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 584999   428 PRPEKYLPSRWLRTE----NQYFRSLGFGFGPRQCLGRRIAETEMQLFLIHMLENF 479
Cdd:cd20656 346 KNPLEFRPERFLEEDvdikGHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHF 401
PLN02687 PLN02687
flavonoid 3'-monooxygenase
73-460 1.90e-26

flavonoid 3'-monooxygenase


Pssm-ID: 215371  Cd Length: 517  Bit Score: 112.60  E-value: 1.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999     73 HRVMVHNFNTFGPIYREKIGYYDSVNIIKPEMPAILFKAE----GHYPKRLTVE--AWtSYRDYrnrkygVLLKNGEDWR 146
Cdd:PLN02687  56 HHTMAALAKTYGPLFRLRFGFVDVVVAASASVAAQFLRTHdanfSNRPPNSGAEhmAY-NYQDL------VFAPYGPRWR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    147 SNRVILNREVISPKVLGNFvpllDEVGQDFVARVHKKIERSGQDKwTTDLSQELFKYALESVGSVLYGERL-GLMLDyin 225
Cdd:PLN02687 129 ALRKICAVHLFSAKALDDF----RHVREEEVALLVRELARQHGTA-PVNLGQLVNVCTTNALGRAMVGRRVfAGDGD--- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    226 PEAQHFIDCISLMFKTTSpMLYIP---PAM----LRRVGAKIWRDHvEAWDGIFNQadrcIQNIYRTMRQDTNTHGKypG 298
Cdd:PLN02687 201 EKAREFKEMVVELMQLAG-VFNVGdfvPALrwldLQGVVGKMKRLH-RRFDAMMNG----IIEEHKAAGQTGSEEHK--D 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    299 VLASLLML----------DKLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDL----QEELRAEVAVARQSTQGD 364
Cdd:PLN02687 273 LLSTLLALkreqqadgegGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDIlkkaQEELDAVVGRDRLVSESD 352
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    365 MLQMlkmiPLVKGALKETLRLHP-VAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWL---- 439
Cdd:PLN02687 353 LPQL----TYLQAVIKETFRLHPsTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpgge 428
                        410       420
                 ....*....|....*....|....*
gi 584999    440 ----RTENQYFRSLGFGFGPRQCLG 460
Cdd:PLN02687 429 hagvDVKGSDFELIPFGAGRRICAG 453
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
82-481 2.27e-26

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: 110.87  E-value: 2.27e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999    82 TFGPIYREKIGYYDSVNIIKPEM-PAILFKAEghypKRLTVE-AWTSY-RDYRNRkyGVLLKNGEDWRSNRVILNREVIS 158
Cdd:cd11045   9 RYGPVSWTGMLGLRVVALLGPDAnQLVLRNRD----KAFSSKqGWDPViGPFFHR--GLMLLDFDEHRAHRRIMQQAFTR 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   159 PKVLGnfvplldevgqdFVARVHKKIERSGQDKWTTD--LSQELFKYALESVGS-VLYGERLGLMLDYINpeaQHFIDCI 235
Cdd:cd11045  83 SALAG------------YLDRMTPGIERALARWPTGAgfQFYPAIKELTLDLATrVFLGVDLGPEADKVN---KAFIDTV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   236 SlmfkttSPMLYIPPAMLrrvGAKIWRDHveawdgifnQADRCIQNIYRTM---RQDTNThgkyPGVLASLLML-----D 307
Cdd:cd11045 148 R------ASTAIIRTPIP---GTRWWRGL---------RGRRYLEEYFRRRipeRRAGGG----DDLFSALCRAededgD 205
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   308 KLSIEDIKASVTELMAGGVDTTSITLLWTLYELARHPDLQEELRAEVAvARQSTQGDMlQMLKMIPLVKGALKETLRLHP 387
Cdd:cd11045 206 RFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESL-ALGKGTLDY-EDLGQLEVTDWVFKEALRLVP 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   388 VAVSLQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWL--RTENQYFRS--LGFGFGPRQCLGRRI 463
Cdd:cd11045 284 PVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSpeRAEDKVHRYawAPFGGGAHKCIGLHF 363
                       410
                ....*....|....*...
gi 584999   464 AETEMQLFLIHMLENFRV 481
Cdd:cd11045 364 AGMEVKAILHQMLRRFRW 381
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
317-480 3.39e-26

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: 110.58  E-value: 3.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   317 SVTELMAGGVDTTSITLLWTLYELARHPD----LQEELRAEVAVARQSTQGDMLQMlkmiPLVKGALKETLRLHPVA-VS 391
Cdd:cd20674 230 AVVDLFIGGTETTASTLSWAVAFLLHHPEiqdrLQEELDRVLGPGASPSYKDRARL----PLLNATIAEVLRLRPVVpLA 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   392 LQRYITEEIVIQNYHIPCGTLVQLGLYAMGRDPDVFPRPEKYLPSRWLRTENQYFRSLGFGFGPRQCLGRRIAETEMQLF 471
Cdd:cd20674 306 LPHRTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPGAANRALLPFGCGARVCLGEPLARLELFVF 385

                ....*....
gi 584999   472 LIHMLENFR 480
Cdd:cd20674 386 LARLLQAFT 394
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
158-481 3.46e-26

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: 110.87  E-value: 3.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 584999   158 SPKVLGNFVPLLDEVGQDFVARVHKkieRSGQDKWTTDLSQELFKYALESVGSVLYGERL------GL