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Conserved domains on  [gi|193083180|ref|NP_001122404|]
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cytochrome P450 4F11 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
74-515 0e+00

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: 951.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  74 MKTLTQLVTTYPQGFKLWLGPTFPLLILCHPDIIRPITSASAAVAPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTP 153
Cdd:cd20679    1 LQVVTQLVATYPQGCLWWLGPFYPIIRLFHPDYIRPVLLASAAVAPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 154 AFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYIAAILELSAFVE 233
Cdd:cd20679   81 AFHFNILKPYVKIFNQSTNIMHAKWRRLASEGSARLDMFEHISLMTLDSLQKCVFSFDSNCQEKPSEYIAAILELSALVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 234 KRNQQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGIDDFLKNKAKSKTLDFIDVLLLSKDEDGKEL 313
Cdd:cd20679  161 KRQQQLLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLKAKAKSKTLDFIDVLLLSKDEDGKEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 314 SDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEWDDLAQLPFLTMCIKESLRLHP 393
Cdd:cd20679  241 SDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEIEWDDLAQLPFLTMCIKESLRLHP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 394 PVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAF 473
Cdd:cd20679  321 PVTAISRCCTQDIVLPDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIGQTF 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 193083180 474 AMAEMKVVLALTLLHFRILPTHTEPRRKPELILRAEGGLWLR 515
Cdd:cd20679  401 AMAEMKVVLALTLLRFRVLPDDKEPRRKPELILRAEGGLWLR 442
 
Name Accession Description Interval E-value
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
74-515 0e+00

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: 951.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  74 MKTLTQLVTTYPQGFKLWLGPTFPLLILCHPDIIRPITSASAAVAPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTP 153
Cdd:cd20679    1 LQVVTQLVATYPQGCLWWLGPFYPIIRLFHPDYIRPVLLASAAVAPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 154 AFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYIAAILELSAFVE 233
Cdd:cd20679   81 AFHFNILKPYVKIFNQSTNIMHAKWRRLASEGSARLDMFEHISLMTLDSLQKCVFSFDSNCQEKPSEYIAAILELSALVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 234 KRNQQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGIDDFLKNKAKSKTLDFIDVLLLSKDEDGKEL 313
Cdd:cd20679  161 KRQQQLLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLKAKAKSKTLDFIDVLLLSKDEDGKEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 314 SDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEWDDLAQLPFLTMCIKESLRLHP 393
Cdd:cd20679  241 SDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEIEWDDLAQLPFLTMCIKESLRLHP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 394 PVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAF 473
Cdd:cd20679  321 PVTAISRCCTQDIVLPDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIGQTF 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 193083180 474 AMAEMKVVLALTLLHFRILPTHTEPRRKPELILRAEGGLWLR 515
Cdd:cd20679  401 AMAEMKVVLALTLLRFRVLPDDKEPRRKPELILRAEGGLWLR 442
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
52-514 4.29e-142

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: 417.07  E-value: 4.29e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180   52 PQPPKQNWFWGHQGLVTPTEEGMKTLTQLVTTYPQGFKLWLGPTfPLLILCHPDIIRPI---TSASAAVAPKDMIFYGFL 128
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGPK-PVVVLSGPEAVKEVlikKGEEFSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  129 KPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEgSARLDMFEHISLMTLDSLQKCVF 208
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGE-PGVIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  209 --SFESNCQEKPSEYIAAILELSAFVEKRNQQILLH-TDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLptqgidd 285
Cdd:pfam00067 159 geRFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLfPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETL------- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  286 flkNKAKSKTLDFIDVLLLSKD-EDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKD 364
Cdd:pfam00067 232 ---DSAKKSPRDFLDALLLAKEeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  365 REPIEieWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLPdGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPF 443
Cdd:pfam00067 309 KRSPT--YDDLQNMPYLDAVIKETLRLHPVVPLlLPREVTKDTVIP-GYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPE 385
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193083180  444 RFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRIlptHTEPRRKPELILRAEGGLWL 514
Cdd:pfam00067 386 RFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEV---ELPPGTDPPDIDETPGLLLP 453
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
144-518 1.06e-59

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 202.43  E-value: 1.06e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 144 WSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRlasegSARLDMFEHISLMTLDSLQKCVFSFesncqekPSEYIA 223
Cdd:COG2124   91 HTRLRRLVQPAFTPRRVAALRPRIREIADELLDRLAA-----RGPVDLVEEFARPLPVIVICELLGV-------PEEDRD 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 224 AILELSAfvekrnqqiLLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTqgiddflknkaksktlDFIDVLL 303
Cdd:COG2124  159 RLRRWSD---------ALLDALGPLPPERRRRARRARAELDAYLRELIAERRAEPGD----------------DLLSALL 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 304 LSKDeDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEvqellkdrepieiewddlaqLPFLTM 383
Cdd:COG2124  214 AARD-DGERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE--------------------PELLPA 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 384 CIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPfrfdqenikERSPLAFIPFSA 463
Cdd:COG2124  273 AVEETLRLYPPVPLLPRTATEDVEL-GGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDP---------DRPPNAHLPFGG 342
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 193083180 464 GPRNCIGQAFAMAEMKVVLALTLLHFRI--LPTHTEPRRKPELILRAEGGLWLRVEP 518
Cdd:COG2124  343 GPHRCLGAALARLEARIALATLLRRFPDlrLAPPEELRWRPSLTLRGPKSLPVRLRP 399
PLN02936 PLN02936
epsilon-ring hydroxylase
144-496 8.07e-46

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 167.28  E-value: 8.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 144 WSRHRRMLTPAFHFNILKPYM-KIFNKSVNIMHDKWQRLASEGSArLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYI 222
Cdd:PLN02936 107 WTARRRAVVPSLHRRYLSVMVdRVFCKCAERLVEKLEPVALSGEA-VNMEAKFSQLTLDVIGLSVFNYNFDSLTTDSPVI 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 223 AAILELSAFVEKRNQQILLH--TDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQG----IDDFLkNKAKSKTL 296
Cdd:PLN02936 186 QAVYTALKEAETRSTDLLPYwkVDFLCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGevieGEEYV-NDSDPSVL 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFidvLLLSKDEdgkeLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPieiEWDDLA 376
Cdd:PLN02936 265 RF---LLASREE----VSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPP---TYEDIK 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 377 QLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENI---KER 453
Cdd:PLN02936 335 ELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPvpnETN 414
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 193083180 454 SPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTL--LHFRILPTHT 496
Cdd:PLN02936 415 TDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLqrLDLELVPDQD 459
 
Name Accession Description Interval E-value
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
74-515 0e+00

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: 951.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  74 MKTLTQLVTTYPQGFKLWLGPTFPLLILCHPDIIRPITSASAAVAPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTP 153
Cdd:cd20679    1 LQVVTQLVATYPQGCLWWLGPFYPIIRLFHPDYIRPVLLASAAVAPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 154 AFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYIAAILELSAFVE 233
Cdd:cd20679   81 AFHFNILKPYVKIFNQSTNIMHAKWRRLASEGSARLDMFEHISLMTLDSLQKCVFSFDSNCQEKPSEYIAAILELSALVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 234 KRNQQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGIDDFLKNKAKSKTLDFIDVLLLSKDEDGKEL 313
Cdd:cd20679  161 KRQQQLLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLKAKAKSKTLDFIDVLLLSKDEDGKEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 314 SDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEWDDLAQLPFLTMCIKESLRLHP 393
Cdd:cd20679  241 SDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEIEWDDLAQLPFLTMCIKESLRLHP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 394 PVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAF 473
Cdd:cd20679  321 PVTAISRCCTQDIVLPDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIGQTF 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 193083180 474 AMAEMKVVLALTLLHFRILPTHTEPRRKPELILRAEGGLWLR 515
Cdd:cd20679  401 AMAEMKVVLALTLLRFRVLPDDKEPRRKPELILRAEGGLWLR 442
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
85-515 0e+00

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: 665.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  85 PQGFKLWLGPTFPLLILCHPDIIRPITSASAavaPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYM 164
Cdd:cd20659    1 PRAYVFWLGPFRPILVLNHPDTIKAVLKTSE---PKDRDSYRFLKPWLGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 165 KIFNKSVNIMHDKWQRLASEGSArLDMFEHISLMTLDSLQKCVFSFESNCQE--KPSEYIAAILELSAFVEKRNQQILLH 242
Cdd:cd20659   78 PVYNECTDILLEKWSKLAETGES-VEVFEDISLLTLDIILRCAFSYKSNCQQtgKNHPYVAAVHELSRLVMERFLNPLLH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 243 TDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGiddfLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEA 322
Cdd:cd20659  157 FDWIYYLTPEGRRFKKACDYVHKFAEEIIKKRRKELEDNK----DEALSKRKYLDFLDILLTARDEDGKGLTDEEIRDEV 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 323 DTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREpiEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCC 402
Cdd:cd20659  233 DTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRD--DIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTL 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 403 TQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVL 482
Cdd:cd20659  311 TKPITI-DGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVL 389
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 193083180 483 ALTLLHFRIL--PTHtEPRRKPELILRAEGGLWLR 515
Cdd:cd20659  390 ARILRRFELSvdPNH-PVEPKPGLVLRSKNGIKLK 423
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
74-515 0e+00

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


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 580.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  74 MKTLTQLVTTYPQGFKLWLGPTFPLLILCHPDIIRPITSASAavaPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTP 153
Cdd:cd20678    1 LQKILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSD---PKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTP 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 154 AFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSaRLDMFEHISLMTLDSLQKCVFSFESNCQEKPSE--YIAAILELSAF 231
Cdd:cd20678   78 AFHYDILKPYVKLMADSVRVMLDKWEKLATQDS-SLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSnsYIQAVSDLSNL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 232 VEKRNQQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGIDDFLKNKaksKTLDFIDVLLLSKDEDGK 311
Cdd:cd20678  157 IFQRLRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKKK---RHLDFLDILLFAKDENGK 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 312 ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREpiEIEWDDLAQLPFLTMCIKESLRL 391
Cdd:cd20678  234 SLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGD--SITWEHLDQMPYTTMCIKEALRL 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 392 HPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQ 471
Cdd:cd20678  312 YPPVPGISRELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQ 391
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 193083180 472 AFAMAEMKVVLALTLLHFRILPTHT-EPRRKPELILRAEGGLWLR 515
Cdd:cd20678  392 QFAMNEMKVAVALTLLRFELLPDPTrIPIPIPQLVLKSKNGIHLY 436
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
88-514 1.21e-160

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: 463.15  E-value: 1.21e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  88 FKLWLGPTfPLLILCHPDIIRPITSASAAVapKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIF 167
Cdd:cd20628    4 FRLWIGPK-PYVVVTNPEDIEVILSSSKLI--TKSFLYDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 168 NKSVNIMHDKWQRLASEGSarLDMFEHISLMTLDSLQKCVFSFESNCQEKP-SEYIAAILELSAFVEKRNQQILLHTDFL 246
Cdd:cd20628   81 NENSKILVEKLKKKAGGGE--FDIFPYISLCTLDIICETAMGVKLNAQSNEdSEYVKAVKRILEIILKRIFSPWLRFDFI 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 247 YYLTPDGQRFRRACHLVHDFTDAVIQERR----CTLPTQGIDDFLKNKaksKTLDFIDVLLLSKdEDGKELSDEDIRAEA 322
Cdd:cd20628  159 FRLTSLGKEQRKALKVLHDFTNKVIKERReelkAEKRNSEEDDEFGKK---KRKAFLDLLLEAH-EDGGPLTDEDIREEV 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 323 DTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDrEPIEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCC 402
Cdd:cd20628  235 DTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGD-DDRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 403 TQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVL 482
Cdd:cd20628  314 TEDIKL-DGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMKTLL 392
                        410       420       430
                 ....*....|....*....|....*....|....
gi 193083180 483 ALTLLHFRILPTHT--EPRRKPELILRAEGGLWL 514
Cdd:cd20628  393 AKILRNFRVLPVPPgeDLKLIAEIVLRSKNGIRV 426
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
52-514 4.29e-142

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: 417.07  E-value: 4.29e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180   52 PQPPKQNWFWGHQGLVTPTEEGMKTLTQLVTTYPQGFKLWLGPTfPLLILCHPDIIRPI---TSASAAVAPKDMIFYGFL 128
Cdd:pfam00067   1 PPGPPPLPLFGNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGPK-PVVVLSGPEAVKEVlikKGEEFSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  129 KPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEgSARLDMFEHISLMTLDSLQKCVF 208
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGE-PGVIDITDLLFRAALNVICSILF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  209 --SFESNCQEKPSEYIAAILELSAFVEKRNQQILLH-TDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLptqgidd 285
Cdd:pfam00067 159 geRFGSLEDPKFLELVKAVQELSSLLSSPSPQLLDLfPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETL------- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  286 flkNKAKSKTLDFIDVLLLSKD-EDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKD 364
Cdd:pfam00067 232 ---DSAKKSPRDFLDALLLAKEeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGD 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  365 REPIEieWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLPdGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPF 443
Cdd:pfam00067 309 KRSPT--YDDLQNMPYLDAVIKETLRLHPVVPLlLPREVTKDTVIP-GYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPE 385
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193083180  444 RFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRIlptHTEPRRKPELILRAEGGLWL 514
Cdd:pfam00067 386 RFLDENGKFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEV---ELPPGTDPPDIDETPGLLLP 453
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
88-514 1.79e-135

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: 398.94  E-value: 1.79e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  88 FKLWLGPtFPLLILCHPDIIRPITSASAavapkdMI----FYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPY 163
Cdd:cd20660    4 FRIWLGP-KPIVVLYSAETVEVILSSSK------HIdksfEYDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 164 MKIFNKSVNIMHDKWQRLAseGSARLDMFEHISLMTLDSLQKCVFSFESNCQ-EKPSEYIAAILELSAFVEKRNQQILLH 242
Cdd:cd20660   77 LDVFNEQSEILVKKLKKEV--GKEEFDIFPYITLCALDIICETAMGKSVNAQqNSDSEYVKAVYRMSELVQKRQKNPWLW 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 243 TDFLYYLTPDGQRFRRACHLVHDFTDAVIQERR----CTLPTQGIDDFLKNKAKSKTLDFIDvLLLSKDEDGKELSDEDI 318
Cdd:cd20660  155 PDFIYSLTPDGREHKKCLKILHGFTNKVIQERKaelqKSLEEEEEDDEDADIGKRKRLAFLD-LLLEASEEGTKLSDEDI 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 319 RAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPIEIewDDLAQLPFLTMCIKESLRLHPPVPV 397
Cdd:cd20660  234 REEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFgDSDRPATM--DDLKEMKYLECVIKEALRLFPSVPM 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 398 ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAE 477
Cdd:cd20660  312 FGRTLSEDIEI-GGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHPYAYIPFSAGPRNCIGQKFALME 390
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 193083180 478 MKVVLALTLLHFRI--LPTHTEPRRKPELILRAEGGLWL 514
Cdd:cd20660  391 EKVVLSSILRNFRIesVQKREDLKPAGELILRPVDGIRV 429
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
88-514 2.35e-105

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: 322.48  E-value: 2.35e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  88 FKLWLGPtFPLLILCHPDIIRPITSASAAVAPKDMifYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIF 167
Cdd:cd20680   15 LKLWIGP-VPFVILYHAENVEVILSSSKHIDKSYL--YKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFHFTILSDFLEVM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 168 NKSVNIMHDKWQRLASEGSarLDMFEHISLMTLDSLQKCVFSFESNCQE-KPSEYIAAILELSAFVEKRNQQILLHTDFL 246
Cdd:cd20680   92 NEQSNILVEKLEKHVDGEA--FNCFFDITLCALDIICETAMGKKIGAQSnKDSEYVQAVYRMSDIIQRRQKMPWLWLDLW 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 247 YYLTPDGQRFRRACHLVHDFTDAVIQER---RCTLPTQGIDDFLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEAD 323
Cdd:cd20680  170 YLMFKEGKEHNKNLKILHTFTDNVIAERaeeMKAEEDKTGDSDGESPSKKKRKAFLDMLLSVTDEEGNKLSHEDIREEVD 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 324 TFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPIEIEwdDLAQLPFLTMCIKESLRLHPPVPVISRCC 402
Cdd:cd20680  250 TFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFgKSDRPVTME--DLKKLRYLECVIKESLRLFPSVPLFARSL 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 403 TQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVL 482
Cdd:cd20680  328 CEDCEI-RGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVL 406
                        410       420       430
                 ....*....|....*....|....*....|....
gi 193083180 483 ALTLLHFRILPTHT--EPRRKPELILRAEGGLWL 514
Cdd:cd20680  407 SCILRHFWVEANQKreELGLVGELILRPQNGIWI 440
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
88-491 1.40e-94

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: 294.12  E-value: 1.40e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  88 FKLWLGPTfPLLILCHPDIIRPITSASAAVaPKDMIFYGFlkpWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIF 167
Cdd:cd11057    4 FRAWLGPR-PFVITSDPEIVQVVLNSPHCL-NKSFFYDFF---RLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 168 NKSVNIMHDKWQRLASEGsaRLDMFEHISLMTLDSLQKCVFSFESNCQ-EKPSEYIAAILELSAFVEKRNQQILLHTDFL 246
Cdd:cd11057   79 NEEAQKLVQRLDTYVGGG--EFDILPDLSRCTLEMICQTTLGSDVNDEsDGNEEYLESYERLFELIAKRVLNPWLHPEFI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 247 YYLTPDGQRFRRACHLVHDFTDAVIQERRCTLP---TQGIDDFLKNKAKSKTldFIDvLLLSKDEDGKELSDEDIRAEAD 323
Cdd:cd11057  157 YRLTGDYKEEQKARKILRAFSEKIIEKKLQEVElesNLDSEEDEENGRKPQI--FID-QLLELARNGEEFTDEEIMDEID 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 324 TFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPiEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCT 403
Cdd:cd11057  234 TMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGQ-FITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETT 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 404 QDFVLPDGRVIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVL 482
Cdd:cd11057  313 ADIQLSNGVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIML 392

                 ....*....
gi 193083180 483 ALTLLHFRI 491
Cdd:cd11057  393 AKILRNYRL 401
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
92-514 2.17e-86

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: 272.14  E-value: 2.17e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  92 LGPtFPLLILCHPDIIRPITSASAAVAPKDmIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIFNKSV 171
Cdd:cd20620    8 LGP-RRVYLVTHPDHIQHVLVTNARNYVKG-GVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAMVEAT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 172 NIMHDKWQRLAseGSARLDMFEHISLMTLDSLQKCVFSFESNcqEKPSEYIAAILELSAFVEKRNQQILLHtdFLYYLTP 251
Cdd:cd20620   86 AALLDRWEAGA--RRGPVDVHAEMMRLTLRIVAKTLFGTDVE--GEADEIGDALDVALEYAARRMLSPFLL--PLWLPTP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 252 DGQRFRRACHLVHDFTDAVIQERRctlptqgiddflknKAKSKTLDFIDVLLLSKD-EDGKELSDEDIRAEADTFMFEGH 330
Cdd:cd20620  160 ANRRFRRARRRLDEVIYRLIAERR--------------AAPADGGDLLSMLLAARDeETGEPMSDQQLRDEVMTLFLAGH 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 331 DTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPieiEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPD 410
Cdd:cd20620  226 ETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRPP---TAEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGG 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 411 GRvIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFR 490
Cdd:cd20620  303 YR-IPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFR 381
                        410       420
                 ....*....|....*....|....*.
gi 193083180 491 I--LPTHTePRRKPELILRAEGGLWL 514
Cdd:cd20620  382 LrlVPGQP-VEPEPLITLRPKNGVRM 406
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
143-513 2.61e-85

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: 269.84  E-value: 2.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 143 KWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSArLDMFEHISLMTLDSLQKCVFSFESNCQEKPS--- 219
Cdd:cd11055   59 RWKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAAETGKP-VDMKDLFQGFTLDVILSTAFGIDVDSQNNPDdpf 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 220 -EYIAAILELSAFVEKRNQQILLHTDFLYYLTPDGQRFRRACHLVhDFTDAVIQERRctlptqgiddflKNKAKSKTlDF 298
Cdd:cd11055  138 lKAAKKIFRNSIIRLFLLLLLFPLRLFLFLLFPFVFGFKSFSFLE-DVVKKIIEQRR------------KNKSSRRK-DL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 299 IDVLLLSKDED----GKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREpiEIEWDD 374
Cdd:cd11055  204 LQLMLDAQDSDedvsKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDG--SPTYDT 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 375 LAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERS 454
Cdd:cd11055  282 VSKLKYLDMVINETLRLYPPAFFISRECKEDCTI-NGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRH 360
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193083180 455 PLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILP---THTEPRRKPELILRAEGGLW 513
Cdd:cd11055  361 PYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPckeTEIPLKLVGGATLSPKNGIY 422
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
146-516 3.79e-82

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: 262.21  E-value: 3.79e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 146 RHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSAR---LDMFEHISLMTLDSLQKCVFSFESNC-QEKPSEY 221
Cdd:cd11069   63 RQRKILNPAFSYRHVKELYPIFWSKAEELVDKLEEEIEESGDEsisIDVLEWLSRATLDIIGLAGFGYDFDSlENPDNEL 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 222 IAAILELSAFVEKRNQQILLHT----DFLYYL-TPDGQRFRRACHLVHDFTDAVIQERRctlptqgidDFLKNKAKSKTL 296
Cdd:cd11069  143 AEAYRRLFEPTLLGSLLFILLLflprWLVRILpWKANREIRRAKDVLRRLAREIIREKK---------AALLEGKDDSGK 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLLSKDEDGKE-LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEWDDL 375
Cdd:cd11069  214 DILSILLRANDFADDErLSDEELIDQILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPPDGDLSYDDL 293
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 376 AQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRFD-----QEN 449
Cdd:cd11069  294 DRLPYLNAVCRETLRLYPPVPLTSREATKDTVI-KGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLepdgaASP 372
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193083180 450 IKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPrrkpelILRAEGGLWLRV 516
Cdd:cd11069  373 GGAGSNYALLTFLHGPRSCIGKKFALAEMKVLLAALVSRFEFELDPDAE------VERPIGIITRPP 433
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
88-507 1.71e-80

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: 256.67  E-value: 1.71e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  88 FKLWLGPTfPLLILCHPDIIRPITSASAAVAPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIF 167
Cdd:cd00302    4 FRVRLGGG-PVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 168 NKsvnIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKCVFSfesncqEKPSEYIAAILELSAFVEKRNQQILLHTdfly 247
Cdd:cd00302   83 RE---IARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGG------PDLGEDLEELAELLEALLKLLGPRLLRP---- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 248 YLTPDGQRFRRACHLVHDFTDAVIQERRctlptqgiddflknkakSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMF 327
Cdd:cd00302  150 LPSPRLRRLRRARARLRDYLEELIARRR-----------------AEPADDLDLLLLADADDGGGLSDEEIVAELLTLLL 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 328 EGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPieiewDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFV 407
Cdd:cd00302  213 AGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDGTP-----EDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVE 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 408 LpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQEniKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLL 487
Cdd:cd00302  288 L-GGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPE--REEPRYAHLPFGAGPHRCLGARLARLELKLALATLLR 364
                        410       420
                 ....*....|....*....|.
gi 193083180 488 HFRILP-THTEPRRKPELILR 507
Cdd:cd00302  365 RFDFELvPDEELEWRPSLGTL 385
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
143-513 8.71e-79

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: 253.23  E-value: 8.71e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 143 KWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSaRLDMFEHISLMTLDSLQKCVFSFESNCQEKPS--- 219
Cdd:cd11056   60 KWKELRQKLTPAFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGK-ELEIKDLMARYTTDVIASCAFGLDANSLNDPEnef 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 220 -EYIAAILELSAFVEKRNQQILLHTDFLYYL-----TPDGQRFRRacHLVHDftdaVIQERRctlptqgiddflKNKAKS 293
Cdd:cd11056  139 rEMGRRLFEPSRLRGLKFMLLFFFPKLARLLrlkffPKEVEDFFR--KLVRD----TIEYRE------------KNNIVR 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 294 KtlDFIDVLL-------LSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDRE 366
Cdd:cd11056  201 N--DFIDLLLelkkkgkIEDDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHG 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 367 pIEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGR-VIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF 445
Cdd:cd11056  279 -GELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDvVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERF 357
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193083180 446 DQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPT-HTEPRRKPE---LILRAEGGLW 513
Cdd:cd11056  358 SPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSsKTKIPLKLSpksFVLSPKGGIW 429
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
143-491 1.51e-75

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: 244.74  E-value: 1.51e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 143 KWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLAsEGSARLDMFEHISLMTLDSLQKCVFSFESNCQEKPS--- 219
Cdd:cd20613   73 KWKKRRAILNPAFHRKYLKNLMDEFNESADLLVEKLSKKA-DGKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDPDspf 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 220 -EYIAAILElsAFVEkrnqqilLHTDFLYYLTPDGQRFRR----ACHLVHDFTDAVIQERRctlptqgiddflknKAKSK 294
Cdd:cd20613  152 pKAISLVLE--GIQE-------SFRNPLLKYNPSKRKYRRevreAIKFLRETGRECIEERL--------------EALKR 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 295 TLDFI-DVL--LLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREpiEIE 371
Cdd:cd20613  209 GEEVPnDILthILKASEEEPDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQ--YVE 286
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 372 WDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIK 451
Cdd:cd20613  287 YEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIEL-GGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPE 365
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 193083180 452 ERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI 491
Cdd:cd20613  366 KIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQNFKF 405
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
88-513 3.71e-74

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


Pssm-ID: 410672 [Multi-domain]  Cd Length: 441  Bit Score: 241.50  E-value: 3.71e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  88 FKLWLGP-TFplLILCHPDIIRPITSASAAVAPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKI 166
Cdd:cd11046   14 YKLAFGPkSF--LVISDPAIAKHVLRSNAFSYDKKGLLAEILEPIMGKGLIPADGEIWKKRRRALVPALHKDYLEMMVRV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 167 FNKSVNIMHDKWQRLASEGSArLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYIAAILelSAFVEKRNQQillhTDFL 246
Cdd:cd11046   92 FGRCSERLMEKLDAAAETGES-VDMEEEFSSLTLDIIGLAVFNYDFGSVTEESPVIKAVY--LPLVEAEHRS----VWEP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 247 YY--------LTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGIDDFLKNKAKSKTLDFIDVLLLSKDEDGkelSDEDI 318
Cdd:cd11046  165 PYwdipaalfIVPRQRKFLRDLKLLNDTLDDLIRKRKEMRQEEDIELQQEDYLNEDDPSLLRFLVDMRDEDV---DSKQL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 319 RAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIewDDLAQLPFLTMCIKESLRLHPPVPVI 398
Cdd:cd11046  242 RDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTY--EDLKKLKYTRRVLNESLRLYPQPPVL 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 399 SRCCTQDFVLPDGRV-IPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKER----SPLAFIPFSAGPRNCIGQAF 473
Cdd:cd11046  320 IRRAVEDDKLPGGGVkVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPneviDDFAFLPFGGGPRKCLGDQF 399
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 193083180 474 AMAEMKVVLALTLLHFRILPTHTEPRR--KPELILRAEGGLW 513
Cdd:cd11046  400 ALLEATVALAMLLRRFDFELDVGPRHVgmTTGATIHTKNGLK 441
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
83-491 2.60e-72

Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies based on homology and phylogenetic criteria; family membership is defined as 40% amino acid sequence identity or higher. The plant CYPs have also been classified according to clans; land plants have 11 clans that form two groups: single-family clans (CYP51, CYP74, CYP97, CYP710, CYP711, CYP727, CYP746) and multi-family clans (CYP71, CYP72, CYP85, CYP86). The CYP72 clan is associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. This clan includes: CYP734 enzymes that are involved in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis; CYP714 enzymes that are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels; and CYP72 family enzymes, among others. The CYP72 clan belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 236.47  E-value: 2.60e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  83 TYPQGFKLWLGPTfPLLILCHPDIIRPITSASAAVAPKDMIfYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKP 162
Cdd:cd11052   10 QYGKNFLYWYGTD-PRLYVTEPELIKELLSKKEGYFGKSPL-QPGLKKLLGRGLVMSNGEKWAKHRRIANPAFHGEKLKG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 163 YMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKCVFSfeSNCQEKpseyiAAILELSAfvekrnQQILLH 242
Cdd:cd11052   88 MVPAMVESVSDMLERWKKQMGEEGEEVDVFEEFKALTADIISRTAFG--SSYEEG-----KEVFKLLR------ELQKIC 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 243 TDFLYYLTPDGQRF------RRACHLVHDFTDA---VIQERRCTLPTQGIDDFLKnkaksktlDFIDVLLLS--KDEDGK 311
Cdd:cd11052  155 AQANRDVGIPGSRFlptkgnKKIKKLDKEIEDSlleIIKKREDSLKMGRGDDYGD--------DLLGLLLEAnqSDDQNK 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 312 ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPieiEWDDLAQLPFLTMCIKESLRL 391
Cdd:cd11052  227 NMTVQEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKP---PSDSLSKLKTVSMVINESLRL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 392 HPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRFDQENIK-ERSPLAFIPFSAGPRNCI 469
Cdd:cd11052  304 YPPAVFLTRKAKEDIKL-GGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGVAKaAKHPMAFLPFGLGPRNCI 382
                        410       420
                 ....*....|....*....|..
gi 193083180 470 GQAFAMAEMKVVLALTLLHFRI 491
Cdd:cd11052  383 GQNFATMEAKIVLAMILQRFSF 404
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
75-516 1.51e-70

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: 231.32  E-value: 1.51e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  75 KTLTQLVTTYPQGFKLWLGPTFPLLILCHPDIIRPITSASAAVA---PKDMIFYGFLKPWlgdglllsggdkwS------ 145
Cdd:cd11053    2 GFLERLRARYGDVFTLRVPGLGPVVVLSDPEAIKQIFTADPDVLhpgEGNSLLEPLLGPN-------------Slllldg 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 146 ----RHRRMLTPAFHFNILKPYMK----IFNKSVnimhDKWQRlaseGSaRLDMFEHISLMTLDSLQKCVFSFEsncqeK 217
Cdd:cd11053   69 drhrRRRKLLMPAFHGERLRAYGEliaeITEREI----DRWPP----GQ-PFDLRELMQEITLEVILRVVFGVD-----D 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 218 PSEYIAAILELSAFVEKRNQQILLHTD---FLYYLTPDGqRFRRACHLVHDFTDAVIQERRcTLPTQGIDDFLknkaksk 294
Cdd:cd11053  135 GERLQELRRLLPRLLDLLSSPLASFPAlqrDLGPWSPWG-RFLRARRRIDALIYAEIAERR-AEPDAERDDIL------- 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 295 tldfiDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPieiewDD 374
Cdd:cd11053  206 -----SLLLSARDEDGQPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDP-----ED 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 375 LAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQEnikERS 454
Cdd:cd11053  276 IAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVEL-GGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGR---KPS 351
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193083180 455 PLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEP---RRKPeLILRAEGGLWLRV 516
Cdd:cd11053  352 PYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPRPerpVRRG-VTLAPSRGVRMVV 415
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
144-518 5.92e-70

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


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 230.15  E-value: 5.92e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 144 WSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGsaRLDMFEHISLMTLDSLQKCVFS--FESNCQEKPSEY 221
Cdd:cd11068   72 WGKAHRILMPAFGPLAMRGYFPMMLDIAEQLVLKWERLGPDE--PIDVPDDMTRLTLDTIALCGFGyrFNSFYRDEPHPF 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 222 IAAILELSAFVEKRNQQILLHTDFLYYLTpdgQRFRRACHLVHDFTDAVIQERRcTLPTQGIDDFLknkaksktldfiDV 301
Cdd:cd11068  150 VEAMVRALTEAGRRANRPPILNKLRRRAK---RQFREDIALMRDLVDEIIAERR-ANPDGSPDDLL------------NL 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 302 LLLSKD-EDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPieiEWDDLAQLPF 380
Cdd:cd11068  214 MLNGKDpETGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPP---PYEQVAKLRY 290
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 381 LTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRFDQENIKERSPLAFI 459
Cdd:cd11068  291 IRRVLDETLRLWPTAPAFARKPKEDTVLGGKYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFLPEEFRKLPPNAWK 370
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 460 PFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI-LPTHTEPRRKPELILRAEgGLWLRVEP 518
Cdd:cd11068  371 PFGNGQRACIGRQFALQEATLVLAMLLQRFDFeDDPDYELDIKETLTLKPD-GFRLKARP 429
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
143-495 1.01e-64

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: 216.35  E-value: 1.01e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 143 KWSRHRRMLTPAFHFNILKPYMKIFNksvNIMHDKWQRLASEGSARLDMFEHIslmTLDSLQKCVFSFESN--------C 214
Cdd:cd20621   58 EWKKQRKLLSNSFHFEKLKSRLPMIN---EITKEKIKKLDNQNVNIIQFLQKI---TGEVVIRSFFGEEAKdlkingkeI 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 215 QEKPSEYIAAILEL---SAFVEKRnQQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERrctlptqgIDDFLKNKA 291
Cdd:cd20621  132 QVELVEILIESFLYrfsSPYFQLK-RLIFGRKSWKLFPTKKEKKLQKRVKELRQFIEKIIQNR--------IKQIKKNKD 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 292 KSKTLDFIDVLLLSKDEDGK-ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEI 370
Cdd:cd20621  203 EIKDIIIDLDLYLLQKKKLEqEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITF 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 371 EwdDLAQLPFLTMCIKESLRLHPPVP-VISRCCTQDFVLPDGRvIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQEN 449
Cdd:cd20621  283 E--DLQKLNYLNAFIKEVLRLYNPAPfLFPRVATQDHQIGDLK-IKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQN 359
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 193083180 450 IKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTH 495
Cdd:cd20621  360 NIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFEIEIIP 405
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
144-518 1.06e-59

Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense mechanisms]; Cytochrome P450 is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 202.43  E-value: 1.06e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 144 WSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRlasegSARLDMFEHISLMTLDSLQKCVFSFesncqekPSEYIA 223
Cdd:COG2124   91 HTRLRRLVQPAFTPRRVAALRPRIREIADELLDRLAA-----RGPVDLVEEFARPLPVIVICELLGV-------PEEDRD 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 224 AILELSAfvekrnqqiLLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTqgiddflknkaksktlDFIDVLL 303
Cdd:COG2124  159 RLRRWSD---------ALLDALGPLPPERRRRARRARAELDAYLRELIAERRAEPGD----------------DLLSALL 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 304 LSKDeDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEvqellkdrepieiewddlaqLPFLTM 383
Cdd:COG2124  214 AARD-DGERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAE--------------------PELLPA 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 384 CIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPfrfdqenikERSPLAFIPFSA 463
Cdd:COG2124  273 AVEETLRLYPPVPLLPRTATEDVEL-GGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDP---------DRPPNAHLPFGG 342
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 193083180 464 GPRNCIGQAFAMAEMKVVLALTLLHFRI--LPTHTEPRRKPELILRAEGGLWLRVEP 518
Cdd:COG2124  343 GPHRCLGAALARLEARIALATLLRRFPDlrLAPPEELRWRPSLTLRGPKSLPVRLRP 399
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
144-491 1.83e-59

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: 202.94  E-value: 1.83e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 144 WSRHRRMLTPAFHFNILKpymKIFNKSVNI---MHDKWQRLASEGSARL-DMFEHISLMTLDSLQKCVFSFESNCQEKPS 219
Cdd:cd11070   58 WKRYRKIVAPAFNERNNA---LVWEESIRQaqrLIRYLLEEQPSAKGGGvDVRDLLQRLALNVIGEVGFGFDLPALDEEE 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 220 EYIAAILelSAFvekrnQQILLHTDFLYY------LTPDGQRFRRACHLVHDFTDAVIQERRCTL-PTQGIDDFLKNKAK 292
Cdd:cd11070  135 SSLHDTL--NAI-----KLAIFPPLFLNFpfldrlPWVLFPSRKRAFKDVDEFLSELLDEVEAELsADSKGKQGTESVVA 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 293 SktldfidvlLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEW 372
Cdd:cd11070  208 S---------RLKRARRSGGLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYE 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 373 DDLAQLPFLTMCIKESLRLHPPVPVISRCCTQD----FVLPDGRVIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRFDQ 447
Cdd:cd11070  279 EDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPvvviTGLGQEIVIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGS 358
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 193083180 448 ENIKERSPL-------AFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI 491
Cdd:cd11070  359 TSGEIGAATrftpargAFIPFSAGPRACLGRKFALVEFVAALAELFRQYEW 409
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
88-498 4.66e-59

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: 201.29  E-value: 4.66e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  88 FKLWLGPTfPLLILCHPDII-------------RPITSASaavapkDMIFYGFLkpwlgdgLLLSGGDKWSRHRRMLTPA 154
Cdd:cd20617    4 FTLWLGDV-PTVVLSDPEIIkeafvkngdnfsdRPLLPSF------EIISGGKG-------ILFSNGDYWKELRRFALSS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 155 FHFNILKPYM-KIFNKSVNIMHDKWQRLASEGSArLDMFEHISLMTLDSLQKCVFS--FESNCQEKPSEYIAAILElsaF 231
Cdd:cd20617   70 LTKTKLKKKMeELIEEEVNKLIESLKKHSKSGEP-FDPRPYFKKFVLNIINQFLFGkrFPDEDDGEFLKLVKPIEE---I 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 232 VEKRNQQILLhtDFLYYLTPDG----QRFRRACHLVHDFTDAVIQERRctlptqgiDDFLKNKAKSKTLDFIDVLLLSKD 307
Cdd:cd20617  146 FKELGSGNPS--DFIPILLPFYflylKKLKKSYDKIKDFIEKIIEEHL--------KTIDPNNPRDLIDDELLLLLKEGD 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 308 EDGKElsDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEwdDLAQLPFLTMCIKE 387
Cdd:cd20617  216 SGLFD--DDSIISTCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLS--DRSKLPYLNAVIKE 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 388 SLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENiKERSPLAFIPFSAGPR 466
Cdd:cd20617  292 VLRLRPILPLgLPRVTTEDTEI-GGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLEND-GNKLSEQFIPFGIGKR 369
                        410       420       430
                 ....*....|....*....|....*....|..
gi 193083180 467 NCIGQAFAMAEMKVVLALTLLHFRILPTHTEP 498
Cdd:cd20617  370 NCVGENLARDELFLFFANLLLNFKFKSSDGLP 401
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
146-516 5.25e-59

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: 200.95  E-value: 5.25e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 146 RHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQrlasEGSaRLDMFEHISLMTLDSLQKCVFSfesncQEKPSEYIAAI 225
Cdd:cd11049   72 RQRRLMQPAFHRSRIPAYAEVMREEAEALAGSWR----PGR-VVDVDAEMHRLTLRVVARTLFS-----TDLGPEAAAEL 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 226 LE-LSAFVEKRNQQILLhTDFLYYL-TPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGiddflknkaksktlDFIDVLL 303
Cdd:cd11049  142 RQaLPVVLAGMLRRAVP-PKFLERLpTPGNRRFDRALARLRELVDEIIAEYRASGTDRD--------------DLLSLLL 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 304 LSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIeieWDDLAQLPFLTM 383
Cdd:cd11049  207 AARDEEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLGGRPAT---FEDLPRLTYTRR 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 384 CIKESLRLHPPVPVISRCCTQDFVLPDGRvIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSA 463
Cdd:cd11049  284 VVTEALRLYPPVWLLTRRTTADVELGGHR-LPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGA 362
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193083180 464 GPRNCIGQAFAMAEMKVVLALTLLHFRILPT-HTEPRRKPELILRAEgGLWLRV 516
Cdd:cd11049  363 GARKCIGDTFALTELTLALATIASRWRLRPVpGRPVRPRPLATLRPR-RLRMRV 415
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
143-507 9.20e-59

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: 200.45  E-value: 9.20e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 143 KWSRHRR-----MLTPafhfNILKPYMKIFNKSVNIMHDKWQRLASEGSARLDMFEH-ISLMTLDSLqkCVFSFES---- 212
Cdd:cd11054   65 EWHRLRSavqkpLLRP----KSVASYLPAINEVADDFVERIRRLRDEDGEEVPDLEDeLYKWSLESI--GTVLFGKrlgc 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 213 ---NCQEKPSEYIAAILELSAFVekrNQQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERrctlptqgIDDFLKN 289
Cdd:cd11054  139 lddNPDSDAQKLIEAVKDIFESS---AKLMFGPPLWKYFPTPAWKKFVKAWDTIFDIASKYVDEA--------LEELKKK 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 290 KAKSKT-LDFIDVLLLSKdedgkELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPI 368
Cdd:cd11054  208 DEEDEEeDSLLEYLLSKP-----GLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPI 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 369 EIEwdDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF--D 446
Cdd:cd11054  283 TAE--DLKKMPYLKACIKESLRLYPVAPGNGRILPKDIVL-SGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlrD 359
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193083180 447 QENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPRRKPELILR 507
Cdd:cd11054  360 DSENKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHEELKVKTRLILV 420
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
143-512 6.06e-57

cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana cytochrome P450s (CYP86A1, CYP86A2, CYP86A4, among others), Petunia x hybrida CYP86A22, and Vicia sativa CYP94A1 and CYP94A2. They are P450-dependent fatty acid omega-hydroxylases that catalyze the omega-hydroxylation of various fatty acids. CYP86A2 acts on saturated and unsaturated fatty acids with chain lengths from C12 to C18; CYP86A22 prefers substrates with chain lengths of C16 and C18; and CYP94A1 acts on various fatty acids from 10 to 18 carbons. They play roles in the biosynthesis of extracellular lipids, cutin synthesis, and plant defense. The CYP86A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410687 [Multi-domain]  Cd Length: 432  Bit Score: 195.89  E-value: 6.06e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 143 KWSRHRRMLTPAFHFNILKPYM-KIFNKSVNimhdkwQRL------ASEGSARLDMFEHISLMTLDSLQKCVFSFESNC- 214
Cdd:cd11064   58 LWKFQRKTASHEFSSRALREFMeSVVREKVE------KLLvplldhAAESGKVVDLQDVLQRFTFDVICKIAFGVDPGSl 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 215 -QEKP-SEYIAAILELSAFVEKRNQQIllhtDFLYYLtpdgQRF---------RRACHLVHDFTDAVIQERRCTLptqgi 283
Cdd:cd11064  132 sPSLPeVPFAKAFDDASEAVAKRFIVP----PWLWKL----KRWlnigsekklREAIRVIDDFVYEVISRRREEL----- 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 284 ddFLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLK 363
Cdd:cd11064  199 --NSREEENNVREDLLSRFLASEEEEGEPVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLP 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 364 DREPIEIE---WDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVW-PDPEV 439
Cdd:cd11064  277 KLTTDESRvptYEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWgEDALE 356
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193083180 440 YDPFRF--DQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRIL--PTHtEPRRKPELILRAEGGL 512
Cdd:cd11064  357 FKPERWldEDGGLRPESPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKvvPGH-KVEPKMSLTLHMKGGL 432
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
144-513 1.82e-56

cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases catalyze the first hydroxylation step in the assimilation of alkanes and fatty acids by filamentous fungi. The number of CYP52 proteins depend on the fungal species: for example, Candida tropicalis has seven, Candida maltose has eight, and Yarrowia lipolytica has twelve. The CYP52 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410686 [Multi-domain]  Cd Length: 419  Bit Score: 194.31  E-value: 1.82e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 144 WSRHRRMLTPAF---HFNILKpymkIFNKSVNIMhdkWQRLASEGSArLDMFEHISLMTLDS-----LQKCVFSFESNCQ 215
Cdd:cd11063   60 WKHSRALLRPQFsrdQISDLE----LFERHVQNL---IKLLPRDGST-VDLQDLFFRLTLDSateflFGESVDSLKPGGD 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 216 EKPSEYIA-AILELSAFVEKRnqqILLHTdfLYYLTPDgQRFRRACHLVHDFTDAVIQERRCTLPTQgiddflKNKAKSK 294
Cdd:cd11063  132 SPPAARFAeAFDYAQKYLAKR---LRLGK--LLWLLRD-KKFREACKVVHRFVDPYVDKALARKEES------KDEESSD 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 295 TLDFIDVLLlskdedgKELSD-EDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEwd 373
Cdd:cd11063  200 RYVFLDELA-------KETRDpKELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYE-- 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 374 DLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLP-----DGR---VIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFR 444
Cdd:cd11063  271 DLKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLPrgggpDGKspiFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPER 350
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193083180 445 FdqENIKeRSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTE--PRRKPELILRAEGGLW 513
Cdd:cd11063  351 W--EDLK-RPGWEYLPFNGGPRICLGQQFALTEASYVLVRLLQTFDRIESRDVrpPEERLTLTLSNANGVK 418
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
145-519 5.98e-56

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: 192.82  E-value: 5.98e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 145 SRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSAR-LDMFEHISLMTLDSLQKCVFSFESNCQEKPS-EYI 222
Cdd:cd11061   55 ARRRRVWSHAFSDKALRGYEPRILSHVEQLCEQLDDRAGKPVSWpVDMSDWFNYLSFDVMGDLAFGKSFGMLESGKdRYI 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 223 AAILELSAFVEKrnqqILLHTDFLY------YLTPDGQRFRRAchlVHDFTDAVIQERrctlptqgiddflKNKAKSKTL 296
Cdd:cd11061  135 LDLLEKSMVRLG----VLGHAPWLRpllldlPLFPGATKARKR---FLDFVRAQLKER-------------LKAEEEKRP 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLLSKD-EDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIeWDDL 375
Cdd:cd11061  195 DIFSYLLEAKDpETGEGLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRL-GPKL 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 376 AQLPFLTMCIKESLRLHPPVP-VISRcctqdFVLP-----DGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFR-FDQE 448
Cdd:cd11061  274 KSLPYLRACIDEALRLSPPVPsGLPR-----ETPPggltiDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERwLSRP 348
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193083180 449 N--IKERSplAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRIlptHTEPRRKPELILRAEGGLWLRVEPL 519
Cdd:cd11061  349 EelVRARS--AFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDF---RLAPGEDGEAGEGGFKDAFGRGPGD 416
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
74-489 3.64e-55

cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Characterized members, among others, include: Catharanthus roseus cytochrome P450 72A1 (CYP72A1), also called secologanin synthase (EC 1.3.3.9), that catalyzes the conversion of loganin into secologanin, the precursor of monoterpenoid indole alkaloids and ipecac alkaloids; Medicago truncatula CYP72A67 that catalyzes a key oxidative step in hemolytic sapogenin biosynthesis; and Arabidopsis thaliana CYP72C1, an atypical CYP that acts on brassinolide precursors and functions as a brassinosteroid-inactivating enzyme. This family also includes Panax ginseng CYP716A47 that catalyzes the formation of protopanaxadiol from dammarenediol-II during ginsenoside biosynthesis. CYP72 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 191.34  E-value: 3.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  74 MKTLTQLVTTYPQGFKLWLGPTfPLLILCHPDIIRPITSAsaavapkdmiFYGFLKPWLGDGLLLSGG-------DKWSR 146
Cdd:cd20642    1 MPFIHHTVKTYGKNSFTWFGPI-PRVIIMDPELIKEVLNK----------VYDFQKPKTNPLTKLLATglasyegDKWAK 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 147 HRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASE-GSARLDMFEHISLMTLDSLQKCvfSFESNCQEKpseyiAAI 225
Cdd:cd20642   70 HRKIINPAFHLEKLKNMLPAFYLSCSEMISKWEKLVSSkGSCELDVWPELQNLTSDVISRT--AFGSSYEEG-----KKI 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 226 LELSAfvekrnQQILLHTDFLYYLTPDGQRF------RRACHLVHDFTDAV--IQERRctlptqgiDDFLKNkAKSKTLD 297
Cdd:cd20642  143 FELQK------EQGELIIQALRKVYIPGWRFlptkrnRRMKEIEKEIRSSLrgIINKR--------EKAMKA-GEATNDD 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 298 FIDVLLLSKDEDGKE-------LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPiei 370
Cdd:cd20642  208 LLGILLESNHKEIKEqgnknggMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKP--- 284
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 371 EWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDgRVIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRFdQEN 449
Cdd:cd20642  285 DFEGLNHLKVVTMILYEVLRLYPPVIQLTRAIHKDTKLGD-LTLPAGVQVSLPILLVHRDPELWgDDAKEFNPERF-AEG 362
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 193083180 450 IKE--RSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHF 489
Cdd:cd20642  363 ISKatKGQVSYFPFGWGPRICIGQNFALLEAKMALALILQRF 404
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
145-494 4.59e-55

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: 190.59  E-value: 4.59e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 145 SRHRRMLTPAFH-FNILKPYMK-IFNKSVNIMHDKWQRlASEGSARLDMFEHISLMTLDSLQKCVF--SFESNCQEKPSE 220
Cdd:cd11059   56 SARRRLLSGVYSkSSLLRAAMEpIIRERVLPLIDRIAK-EAGKSGSVDVYPLFTALAMDVVSHLLFgeSFGTLLLGDKDS 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 221 YIAAILELsafvekrnqqilLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGIDDFLKNKAKSKTLDFID 300
Cdd:cd11059  135 RERELLRR------------LLASLAPWLRWLPRYLPLATSRLIIGIYFRAFDEIEEWALDLCARAESSLAESSDSESLT 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 301 VLLLSKDE--DGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQEL-LKDREPieIEWDDLAQ 377
Cdd:cd11059  203 VLLLEKLKglKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGLpGPFRGP--PDLEDLDK 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 378 LPFLTMCIKESLRLHPPVPVisrccTQDFVLPDGRV------IPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF---DQE 448
Cdd:cd11059  281 LPYLNAVIRETLRLYPPIPG-----SLPRVVPEGGAtiggyyIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWldpSGE 355
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 193083180 449 NIKERSpLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPT 494
Cdd:cd11059  356 TAREMK-RAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRTSTT 400
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
83-495 4.67e-54

cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP734As function as multisubstrate and multifunctional enzymes in brassinosteroid (BRs) catabolism and regulation of BRs homeostasis. Arabidopsis thaliana CYP734A1/BAS1 (formerly CYP72B1) inactivates bioactive brassinosteroids such as castasterone (CS) and brassinolide (BL) by C-26 hydroxylation. Rice CYP734As can catalyze C-22 hydroxylation as well as second and third oxidations to produce aldehyde and carboxylate groups at C-26. CYP734 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410732 [Multi-domain]  Cd Length: 428  Bit Score: 188.04  E-value: 4.67e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  83 TYPQGFKLWLGPTfPLLILCHPDIIRPITSASA------AVAP--KDMIFYGFLKpwlgdglllSGGDKWSRHRRMLTPA 154
Cdd:cd20639   10 IYGKTFLYWFGPT-PRLTVADPELIREILLTRAdhfdryEAHPlvRQLEGDGLVS---------LRGEKWAHHRRVITPA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 155 FHFNILKPYMKIFNKSVNIMHDKWQRLASEG-SARLDMFEHISLMTLDSLQKCVF--SFESNcqekpseyiAAILELSAf 231
Cdd:cd20639   80 FHMENLKRLVPHVVKSVADMLDKWEAMAEAGgEGEVDVAEWFQNLTEDVISRTAFgsSYEDG---------KAVFRLQA- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 232 vekrnQQILLHTD-FLYYLTPdGQRF------RRACHLVhdftdaviQERRCTLPT-----QGIDDFLKNKAKSKTL--D 297
Cdd:cd20639  150 -----QQMLLAAEaFRKVYIP-GYRFlptkknRKSWRLD--------KEIRKSLLKlierrQTAADDEKDDEDSKDLlgL 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 298 FIDVlllSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDRE-PIEiewDDLA 376
Cdd:cd20639  216 MISA---KNARNGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDvPTK---DHLP 289
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 377 QLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRF-DQENIKERS 454
Cdd:cd20639  290 KLKTLGMILNETLRLYPPAVATIRRAKKDVKL-GGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFaDGVARAAKH 368
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 193083180 455 PLAFIPFSAGPRNCIGQAFAMAEMKVVLALTL--LHFRILPTH 495
Cdd:cd20639  369 PLAFIPFGLGPRTCVGQNLAILEAKLTLAVILqrFEFRLSPSY 411
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
146-509 1.89e-52

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: 183.64  E-value: 1.89e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 146 RHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWqrlasEGSARLDMFEHISLMTLDslqkcvfsfesncqekpseyIAAI 225
Cdd:cd11044   81 RRRKLLAPAFSREALESYVPTIQAIVQSYLRKW-----LKAGEVALYPELRRLTFD--------------------VAAR 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 226 LELSAFVEKRNQQilLHTDF------LYYLTPD--GQRFRRAC---HLVHDFTDAVIQERRCtlptqgiddflkNKAKSk 294
Cdd:cd11044  136 LLLGLDPEVEAEA--LSQDFetwtdgLFSLPVPlpFTPFGRAIrarNKLLARLEQAIRERQE------------EENAE- 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 295 TLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEvQELLKDREPIEIEwdD 374
Cdd:cd11044  201 AKDALGLLLEAKDEDGEPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQE-QDALGLEEPLTLE--S 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 375 LAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKE-R 453
Cdd:cd11044  278 LKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFEL-GGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDkK 356
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193083180 454 SPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI-------LPTHTEPRRKPELILRAE 509
Cdd:cd11044  357 KPFSLIPFGGGPRECLGKEFAQLEMKILASELLRNYDWellpnqdLEPVVVPTPRPKDGLRVR 419
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
147-488 1.92e-51

plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, cytochrome P450 family 90, subfamily B, polypeptide 1, and cytochrome P450 family 90, subfamily D, polypeptide 2; This family is composed of plant cytochrome P450s including: Arabidopsis thaliana cytochrome P450s 85A1 (CYP85A1 or brassinosteroid-6-oxidase 1), 90A1 (CYP90A1), 88A3 (CYP88A3 or ent-kaurenoic acid oxidase 1), 90B1 (CYP90B1 or Dwarf4 or steroid 22-alpha-hydroxylase), and 90C1 (CYP90C1 or 3-epi-6-deoxocathasterone 23-monooxygenase); Oryza sativa cytochrome P450s 90D2 (CYP90D2 or C6-oxidase), 87A3 (CYP87A3), and 724B1 (CYP724B1 or dwarf protein 11); and Taxus cuspidata cytochrome P450 725A2 (CYP725A2 or taxane 13-alpha-hydroxylase). These enzymes are monooxygenases that catalyze oxidation reactions involved in steroid or hormone biosynthesis. CYP85A1, CYP90D2, and CYP90C1 are involved in brassinosteroids biosynthesis, while CYP88A3 catalyzes three successive oxidations of ent-kaurenoic acid, which is a key step in the synthesis of gibberellins. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410669 [Multi-domain]  Cd Length: 408  Bit Score: 180.45  E-value: 1.92e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 147 HRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEgsarlDMFEHISLMTLDSLQKCVFSFEsncqekPSEYIAAI- 225
Cdd:cd11043   67 RGLLLSFLGPEALKDRLLGDIDELVRQHLDSWWRGKSV-----VVLELAKKMTFELICKLLLGID------PEEVVEELr 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 226 LELSAFVEKRNQqillhtdFLYYLTpdGQRFRRACH---LVHDFTDAVIQERRCTLptqgiddflknKAKSKTLDFIDVL 302
Cdd:cd11043  136 KEFQAFLEGLLS-------FPLNLP--GTTFHRALKarkRIRKELKKIIEERRAEL-----------EKASPKGDLLDVL 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 303 LLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIE-IEWDDLAQLPFL 381
Cdd:cd11043  196 LEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAKRKEEGEgLTWEDYKSMKYT 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 382 TMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENikERSPLAFIPF 461
Cdd:cd11043  276 WQVINETLRLAPIVPGVFRKALQDVEY-KGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKG--KGVPYTFLPF 352
                        330       340
                 ....*....|....*....|....*..
gi 193083180 462 SAGPRNCIGQAFAMAEMkvvlaLTLLH 488
Cdd:cd11043  353 GGGPRLCPGAELAKLEI-----LVFLH 374
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
245-488 1.35e-50

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: 178.56  E-value: 1.35e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 245 FLYYLTPDGQRFRRACHLVHDFTDAVIQERRctlptqgiddflkNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADT 324
Cdd:cd11042  153 FPPLPLPSFRRRDRARAKLKEIFSEIIQKRR-------------KSPDKDEDDMLQTLMDAKYKDGRPLTDDEIAGLLIA 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 325 FMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPiEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQ 404
Cdd:cd11042  220 LLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDD-PLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARK 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 405 DFVLPDGR-VIPKG-IVC---LINiigiHYNPTVWPDPEVYDPFRFDQEN--IKERSPLAFIPFSAGPRNCIGQAFAMAE 477
Cdd:cd11042  299 PFEVEGGGyVIPKGhIVLaspAVS----HRDPEIFKNPDEFDPERFLKGRaeDSKGGKFAYLPFGAGRHRCIGENFAYLQ 374
                        250
                 ....*....|.
gi 193083180 478 MKVVLAlTLLH 488
Cdd:cd11042  375 IKTILS-TLLR 384
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
297-491 2.17e-49

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: 175.20  E-value: 2.17e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDRepieIEWDDLA 376
Cdd:cd11045  191 DLFSALCRAEDEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLALGKGT----LDYEDLG 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 377 QLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQE-NIKERSP 455
Cdd:cd11045  267 QLEVTDWVFKEALRLVPPVPTLPRRAVKDTEV-LGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPErAEDKVHR 345
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 193083180 456 LAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI 491
Cdd:cd11045  346 YAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRRFRW 381
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
145-489 6.67e-49

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: 173.92  E-value: 6.67e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 145 SRHRRMLTPAF-------HFNILKPYMkifnksvnimhDKW-QRLA--SEGSARLDMFEHISLMTLDSLQKCVFSFESNC 214
Cdd:cd11058   59 ARLRRLLAHAFsekalreQEPIIQRYV-----------DLLvSRLRerAGSGTPVDMVKWFNFTTFDIIGDLAFGESFGC 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 215 QE--KPSEYIAAILELSAFVEKRN--QQILLHTDFLYYLTPDGQRFRRACHLvhDFTDAVIQERRCTLPTQGiddflknk 290
Cdd:cd11058  128 LEngEYHPWVALIFDSIKALTIIQalRRYPWLLRLLRLLIPKSLRKKRKEHF--QYTREKVDRRLAKGTDRP-------- 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 291 aksktlDFIDvLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREpiEI 370
Cdd:cd11058  198 ------DFMS-YILRNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSED--DI 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 371 EWDDLAQLPFLTMCIKESLRLHPPVPVI-SRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDP------- 442
Cdd:cd11058  269 TLDSLAQLPYLNAVIQEALRLYPPVPAGlPRVVPAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPerwlgdp 348
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 193083180 443 -FRFDQENiKErsplAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHF 489
Cdd:cd11058  349 rFEFDNDK-KE----AFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNF 391
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
97-497 2.95e-47

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: 169.36  E-value: 2.95e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  97 PLLILCHPDIIRPITSASAAvaPKDMIFYGFLKPWL-GDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMH 175
Cdd:cd11051   11 PLLVVTDPELAEQITQVTNL--PKPPPLRKFLTPLTgGSSLISMEGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVEIFA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 176 DKWQRLASEGSArLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYIAAILELSAFVEKRnqqillhTDFLYYLTPDGQR 255
Cdd:cd11051   89 AILRELAESGEV-FSLEELTTNLTFDVIGRVTLDIDLHAQTGDNSLLTALRLLLALYRSL-------LNPFKRLNPLRPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 256 FRRAchlvhdftdaviQERRctlptqgIDDFLKNKAKSKtldfidvlllskdedgkeLSDEDIRAEADTFMFEGHDTTAS 335
Cdd:cd11051  161 RRWR------------NGRR-------LDRYLKPEVRKR------------------FELERAIDQIKTFLFAGHDTTSS 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 336 GLSWVLYHLAKHPEYQEQCRQEVQELL---KDREPIEIEWDD--LAQLPFLTMCIKESLRLHPPVPVISRCC-TQDFVLP 409
Cdd:cd11051  204 TLCWAFYLLSKHPEVLAKVRAEHDEVFgpdPSAAAELLREGPelLNQLPYTTAVIKETLRLFPPAGTARRGPpGVGLTDR 283
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 410 DGRVIP-KGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPL--AFIPFSAGPRNCIGQAFAMAEMKVVLALTL 486
Cdd:cd11051  284 DGKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHELYPPksAWRPFERGPRNCIGQELAMLELKIILAMTV 363
                        410
                 ....*....|.
gi 193083180 487 LHFRILPTHTE 497
Cdd:cd11051  364 RRFDFEKAYDE 374
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
143-498 1.17e-46

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: 167.88  E-value: 1.17e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 143 KWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSArLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYI 222
Cdd:cd11083   58 AWRRQRRLVMPAFSPKHLRYFFPTLRQITERLRERWERAAAEGEA-VDVHKDLMRYTVDVTTSLAFGYDLNTLERGGDPL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 223 AAILE----------LSAFVEKRnqqillhtdflYYLTPDGQRFRRACHLVHDFTDAVIQERRctlptQGIDDFLKNKAK 292
Cdd:cd11083  137 QEHLErvfpmlnrrvNAPFPYWR-----------YLRLPADRALDRALVEVRALVLDIIAAAR-----ARLAANPALAEA 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 293 SKTLdfiDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEiEW 372
Cdd:cd11083  201 PETL---LAMMLAEDDPDARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPP-LL 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 373 DDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRvIPKG--IVCLINIIGIhyNPTVWPDPEVYDPFRFdQENI 450
Cdd:cd11083  277 EALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVVGDIA-LPAGtpVFLLTRAAGL--DAEHFPDPEEFDPERW-LDGA 352
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193083180 451 KERSPL---AFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI-LPTHTEP 498
Cdd:cd11083  353 RAAEPHdpsSLLPFGAGPRLCPGRSLALMEMKLVFAMLCRNFDIeLPEPAPA 404
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
144-504 4.83e-46

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: 166.62  E-value: 4.83e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 144 WSRHRRMLTPAFHfNILKPYMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLqkCVFSFESNCQEKPSEYiA 223
Cdd:cd11027   62 WKLHRKLAHSALR-LYASGGPRLEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVI--CSITFGKRYKLDDPEF-L 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 224 AILELS-AFVEKRNQQILLhtDFLYYL----TPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGIDDFlknkakskTLDF 298
Cdd:cd11027  138 RLLDLNdKFFELLGAGSLL--DIFPFLkyfpNKALRELKELMKERDEILRKKLEEHKETFDPGNIRDL--------TDAL 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 299 IDVLLLSKDEDGK---ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEV-QELLKDREPieiEWDD 374
Cdd:cd11027  208 IKAKKEAEDEGDEdsgLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELdDVIGRDRLP---TLSD 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 375 LAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKER 453
Cdd:cd11027  285 RKRLPYLEATIAEVLRLSSVVPLaLPHKTTCDTTL-RGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLV 363
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193083180 454 -SPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPrrKPEL 504
Cdd:cd11027  364 pKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEP--PPEL 413
PLN02936 PLN02936
epsilon-ring hydroxylase
144-496 8.07e-46

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 167.28  E-value: 8.07e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 144 WSRHRRMLTPAFHFNILKPYM-KIFNKSVNIMHDKWQRLASEGSArLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYI 222
Cdd:PLN02936 107 WTARRRAVVPSLHRRYLSVMVdRVFCKCAERLVEKLEPVALSGEA-VNMEAKFSQLTLDVIGLSVFNYNFDSLTTDSPVI 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 223 AAILELSAFVEKRNQQILLH--TDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTQG----IDDFLkNKAKSKTL 296
Cdd:PLN02936 186 QAVYTALKEAETRSTDLLPYwkVDFLCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGevieGEEYV-NDSDPSVL 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFidvLLLSKDEdgkeLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPieiEWDDLA 376
Cdd:PLN02936 265 RF---LLASREE----VSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPP---TYEDIK 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 377 QLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENI---KER 453
Cdd:PLN02936 335 ELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGPvpnETN 414
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 193083180 454 SPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTL--LHFRILPTHT 496
Cdd:PLN02936 415 TDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLqrLDLELVPDQD 459
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
143-493 3.56e-45

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: 164.12  E-value: 3.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 143 KWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSArLDMFEHISLMTLDSLQKCVFSFESNCQEKPSeyi 222
Cdd:cd20650   59 EWKRIRSLLSPTFTSGKLKEMFPIIAQYGDVLVKNLRKEAEKGKP-VTLKDVFGAYSMDVITSTSFGVNIDSLNNPQ--- 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 223 aailelSAFVEkrNQQILLHTDFLY----------YLTPDGQRFRrACHLVHDFTDAViqerrctlpTQGIDDFLKNKAK 292
Cdd:cd20650  135 ------DPFVE--NTKKLLKFDFLDplflsitvfpFLTPILEKLN-ISVFPKDVTNFF---------YKSVKKIKESRLD 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 293 SKT---LDFIDVLLLSKDEDGKE----LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDR 365
Cdd:cd20650  197 STQkhrVDFLQLMIDSQNSKETEshkaLSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNK 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 366 EPIEieWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDfVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF 445
Cdd:cd20650  277 APPT--YDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKD-VEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERF 353
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 193083180 446 DQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILP 493
Cdd:cd20650  354 SKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKP 401
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
79-490 6.34e-45

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


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 163.77  E-value: 6.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  79 QLVTTYPQGFKLWLGPTfPLLILCHPDIIRPITSASAAVAPKDMIFYGFLKpWLGDGLLLSGGDKWSRHRRMLTPAFHFN 158
Cdd:cd20641    6 QWKSQYGETFLYWQGTT-PRICISDHELAKQVLSDKFGFFGKSKARPEILK-LSGKGLVFVNGDDWVRHRRVLNPAFSMD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 159 ILKPYMKIFNKSVNIMHDKW--QRLASEG-SARLDMFEHISLMTLDSLqkCVFSFESNCQEKpSEYIAAILELsafvEKR 235
Cdd:cd20641   84 KLKSMTQVMADCTERMFQEWrkQRNNSETeRIEVEVSREFQDLTADII--ATTAFGSSYAEG-IEVFLSQLEL----QKC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 236 NQQILLHTDF--LYYL-TPDGQRFRRACHLVHDFTDAVIQERrctlptqgiddfLKNKAKSKTLDFIDVLLLSKDEDG-- 310
Cdd:cd20641  157 AAASLTNLYIpgTQYLpTPRNLRVWKLEKKVRNSIKRIIDSR------------LTSEGKGYGDDLLGLMLEAASSNEgg 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 311 ----KELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEV-QELLKDREPIEiewDDLAQLPFLTMCI 385
Cdd:cd20641  225 rrteRKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVfRECGKDKIPDA---DTLSKLKLMNMVL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 386 KESLRLHPPVPVISRCCTQDFVLpdGRV-IPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRFdqENIKERS---PLAFIP 460
Cdd:cd20641  302 METLRLYGPVINIARRASEDMKL--GGLeIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRF--ANGVSRAathPNALLS 377
                        410       420       430
                 ....*....|....*....|....*....|
gi 193083180 461 FSAGPRNCIGQAFAMAEMKVVLALTLLHFR 490
Cdd:cd20641  378 FSLGPRACIGQNFAMIEAKTVLAMILQRFS 407
PTZ00404 PTZ00404
cytochrome P450; Provisional
297-491 2.30e-43

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 160.66  E-value: 2.30e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLlskDEDGKElSDEDIRAEADT---FMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREpiEIEWD 373
Cdd:PTZ00404 264 DLLDLLI---KEYGTN-TDDDILSILATildFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRN--KVLLS 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 374 DLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFdqenIKE 452
Cdd:PTZ00404 338 DRQSTPYTVAIIKETLRYKPVSPFgLPRSTSNDIIIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRF----LNP 413
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 193083180 453 RSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI 491
Cdd:PTZ00404 414 DSNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKL 452
PLN02290 PLN02290
cytokinin trans-hydroxylase
83-519 1.86e-42

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 158.82  E-value: 1.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  83 TYPQGFKLWLGPTfPLLILCHPDIIRPITSASAAVAPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKP 162
Cdd:PLN02290  92 QYGKRFIYWNGTE-PRLCLTETELIKELLTKYNTVTGKSWLQQQGTKHFIGRGLLMANGADWYHQRHIAAPAFMGDRLKG 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 163 YMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKCvfSFESNCqEKPSEYIAAILELsafvekrnqQILLH 242
Cdd:PLN02290 171 YAGHMVECTKQMLQSLQKAVESGQTEVEIGEYMTRLTADIISRT--EFDSSY-EKGKQIFHLLTVL---------QRLCA 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 243 TDFLYYLTPDGQ----RFRRACHLVHDFTDAV----IQERRctlptqgiDDFLKNKAKSKTLDFIDVLLL---SKDEDGK 311
Cdd:PLN02290 239 QATRHLCFPGSRffpsKYNREIKSLKGEVERLlmeiIQSRR--------DCVEIGRSSSYGDDLLGMLLNemeKKRSNGF 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 312 ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPieiEWDDLAQLPFLTMCIKESLRL 391
Cdd:PLN02290 311 NLNLQLIMDECKTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETP---SVDHLSKLTLLNMVINESLRL 387
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 392 HPPVPVISRCCTQDFVLPDGRvIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRFDQeniKERSPLA-FIPFSAGPRNCI 469
Cdd:PLN02290 388 YPPATLLPRMAFEDIKLGDLH-IPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAG---RPFAPGRhFIPFAAGPRNCI 463
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193083180 470 GQAFAMAEMKVVLALTLLHFRIlPTHTEPRRKPELIL--RAEGGLWLRVEPL 519
Cdd:PLN02290 464 GQAFAMMEAKIILAMLISKFSF-TISDNYRHAPVVVLtiKPKYGVQVCLKPL 514
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
97-492 9.37e-42

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: 155.38  E-value: 9.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  97 PLLILCHPDIIRPITSASAAVAPKDMIFYGFLKPwLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIFNKSVNIMHD 176
Cdd:cd20649   14 MFVVIAEPDMIKQVLVKDFNNFTNRMKANLITKP-MSDSLLCLRDERWKRVRSILTPAFSAAKMKEMVPLINQACDVLLR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 177 KWQRLASEGSArLDMFEHISLMTLDSLQKCVFSFESNCQEKPSE----YIAAILELSAFvekrNQQILLHTDF------L 246
Cdd:cd20649   93 NLKSYAESGNA-FNIQRCYGCFTMDVVASVAFGTQVDSQKNPDDpfvkNCKRFFEFSFF----RPILILFLAFpfimipL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 247 YYLTPDGQRFRRACHLVHDFTDaVIQERRCTLPTQGIDDFL------KNKAKSKTLDFIDVLLLSKDEDG---------- 310
Cdd:cd20649  168 ARILPNKSRDELNSFFTQCIRN-MIAFRDQQSPEERRRDFLqlmldaRTSAKFLSVEHFDIVNDADESAYdghpnspane 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 311 --------KELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELlkDREPIEIEWDDLAQLPFLT 382
Cdd:cd20649  247 qtkpskqkRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEF--FSKHEMVDYANVQELPYLD 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 383 MCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFS 462
Cdd:cd20649  325 MVIAETLRMYPPAFRFAREAAEDCVV-LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHPFVYLPFG 403
                        410       420       430
                 ....*....|....*....|....*....|
gi 193083180 463 AGPRNCIGQAFAMAEMKVVLALTLLHFRIL 492
Cdd:cd20649  404 AGPRSCIGMRLALLEIKVTLLHILRRFRFQ 433
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
88-489 1.40e-41

cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. CYP714 enzymes are involved in the biosynthesis of gibberellins (GAs) and the mechanism to control their bioactive endogenous levels. They contribute to the production of diverse GA compounds through various oxidations of C and D rings in both monocots and eudicots. CYP714B1 and CYP714B2 encode the enzyme GA 13-oxidase, which is required for GA1 biosynthesis, while CYP714D1 encodes GA 16a,17-epoxidase, which inactivates the non-13-hydroxy GAs in rice. Arabidopsis CYP714A1 is an inactivation enzyme that catalyzes the conversion of GA12 to 16-carboxylated GA12 (16-carboxy-16beta,17-dihydro GA12). CYP714 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 154.49  E-value: 1.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  88 FKLWL---GPTF-------PLLILCHPDIIRPITSASAAVAPKDMIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHF 157
Cdd:cd20640    4 FDKWRkqyGPIFtystgnkQFLYVSRPEMVKEINLCVSLDLGKPSYLKKTLKPLFGGGILTSNGPHWAHQRKIIAPEFFL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 158 NILKPYMKIFNKSVNIMHDKWQ-RLASEGSARLDMF--EHISLMTLDSLQKCVF--SFEsncqeKPSEYIAAILELSAFV 232
Cdd:cd20640   84 DKVKGMVDLMVDSAQPLLSSWEeRIDRAGGMAADIVvdEDLRAFSADVISRACFgsSYS-----KGKEIFSKLRELQKAV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 233 EKRNqqILLHTDFLYYL-TPDGQRFRRACHLVHDFTDAVIQERRCTLPTQGidDFLKNkaksktldfidVLLLSKDEDGK 311
Cdd:cd20640  159 SKQS--VLFSIPGLRHLpTKSNRKIWELEGEIRSLILEIVKEREEECDHEK--DLLQA-----------ILEGARSSCDK 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 312 ELSDED-IRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPieiEWDDLAQLPFLTMCIKESLR 390
Cdd:cd20640  224 KAEAEDfIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPP---DADSLSRMKTVTMVIQETLR 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 391 LHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRF-DQENIKERSPLAFIPFSAGPRNC 468
Cdd:cd20640  301 LYPPAAFVSREALRDMKL-GGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFsNGVAAACKPPHSYMPFGAGARTC 379
                        410       420
                 ....*....|....*....|.
gi 193083180 469 IGQAFAMAEMKVVLALTLLHF 489
Cdd:cd20640  380 LGQNFAMAELKVLVSLILSKF 400
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
265-497 2.48e-41

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: 153.51  E-value: 2.48e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 265 DFTDAVIQERRCtlptqgiddfLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHL 344
Cdd:cd11060  180 RFALEAVAERLA----------EDAESAKGRKDMLDSFLEAGLKDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYL 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 345 AKHPEYQEQCRQEVQELLKDREPIE-IEWDDLAQLPFLTMCIKESLRLHPPVP-----VISRCctqDFVLPdGRVIPKG- 417
Cdd:cd11060  250 LKNPRVYAKLRAEIDAAVAEGKLSSpITFAEAQKLPYLQAVIKEALRLHPPVGlplerVVPPG---GATIC-GRFIPGGt 325
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 418 IVClINIIGIHYNPTVW-PDPEVYDPFRF-----DQENIKERsplAFIPFSAGPRNCIGQAFAMAEM-KVVLALtLLHFR 490
Cdd:cd11060  326 IVG-VNPWVIHRDKEVFgEDADVFRPERWleadeEQRRMMDR---ADLTFGAGSRTCLGKNIALLELyKVIPEL-LRRFD 400

                 ....*..
gi 193083180 491 ILPTHTE 497
Cdd:cd11060  401 FELVDPE 407
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
245-488 1.31e-39

cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant cytochrome P450 family 76 (CYP76 or Cyp76) include: Catharanthus roseus CYP76B6, a multifunctional enzyme catalyzing two sequential oxidation steps leading to the formation of 8-oxogeraniol from geraniol; the Brassicaceae-specific CYP76C subfamily of enzymes that are involved in the metabolism of monoterpenols and phenylurea herbicides; and two P450s from Lamiaceae, CYP76AH and CYP76AK, that are involved in the oxidation of abietane diterpenes. CYP76AH produces ferruginol and 11-hydroxyferruginol, while CYP76AK catalyzes oxidations at the C20 position. Also included in this group is Berberis stolonifera Cyp80, also called berbamunine synthase or (S)-N-methylcoclaurine oxidase [C-O phenol-coupling], that catalyzes the phenol oxidation of N-methylcoclaurine to form the bisbenzylisoquinoline alkaloid berbamunine. The CYP76-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 149.22  E-value: 1.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 245 FLYYLTPDGQRFRRACHL--VHDFTDAVIQERRctlptQGIDdflKNKAKSKTLDFIDVLLLSKDEDGkELSDEDIRAea 322
Cdd:cd11073  166 FLKFLDLQGLRRRMAEHFgkLFDIFDGFIDERL-----AERE---AGGDKKKDDDLLLLLDLELDSES-ELTRNHIKA-- 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 323 dtFMFE----GHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEiEwDDLAQLPFLTMCIKESLRLHPPVPV- 397
Cdd:cd11073  235 --LLLDlfvaGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVE-E-SDISKLPYLQAVVKETLRLHPPAPLl 310
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 398 ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF--DQENIKERSPlAFIPFSAGPRNCIGQAFAM 475
Cdd:cd11073  311 LPRKAEEDVEV-MGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFlgSEIDFKGRDF-ELIPFGSGRRICPGLPLAE 388
                        250
                 ....*....|...
gi 193083180 476 AEMKVVLAlTLLH 488
Cdd:cd11073  389 RMVHLVLA-SLLH 400
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
182-488 2.03e-39

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: 148.47  E-value: 2.03e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 182 ASEGSARLDMFEHISLMTLDSLQKCVFS-----FESNCQEKPSEYIAAILELSAFVEKRNQqillhTDFLYYLTP-DGQR 255
Cdd:cd20618   99 ESESGKPVNLREHLSDLTLNNITRMLFGkryfgESEKESEEAREFKELIDEAFELAGAFNI-----GDYIPWLRWlDLQG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 256 FRRACHLVHD----FTDAVIQERRctlptqgiddfLKNKAKSKTLDFIDVLLLSKDEDGKE-LSDEDIRAEADTFMFEGH 330
Cdd:cd20618  174 YEKRMKKLHAkldrFLQKIIEEHR-----------EKRGESKKGGDDDDDLLLLLDLDGEGkLSDDNIKALLLDMLAAGT 242
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 331 DTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREpieIEWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVL 408
Cdd:cd20618  243 DTSAVTIEWAMAELLRHPEVMRKAQEELDSVVgRERL---VEESDLPKLPYLQAVVKETLRLHPPGPLlLPHESTEDCKV 319
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 409 pDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF---DQENIKERSpLAFIPFSAGPRNCIGQAFAMAEMKVVLAlT 485
Cdd:cd20618  320 -AGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFlesDIDDVKGQD-FELLPFGSGRRMCPGMPLGLRMVQLTLA-N 396

                 ...
gi 193083180 486 LLH 488
Cdd:cd20618  397 LLH 399
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
283-483 2.24e-38

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: 145.47  E-value: 2.24e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 283 IDDFLKNKAKSKTLDFIDV---LLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQ 359
Cdd:cd11062  187 VDEVLRQVSAGDPPSIVTSlfhALLNSDLPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERLREELK 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 360 ELLKDRePIEIEWDDLAQLPFLTMCIKESLRLHPPVPVIS-RCCTQDFVLPDGRVIPKG-IVClINIIGIHYNPTVWPDP 437
Cdd:cd11062  267 TAMPDP-DSPPSLAELEKLPYLTAVIKEGLRLSYGVPTRLpRVVPDEGLYYKGWVIPPGtPVS-MSSYFVHHDEEIFPDP 344
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 193083180 438 EVYDPFRFDQENikERSPLA--FIPFSAGPRNCIGQAFAMAEMKVVLA 483
Cdd:cd11062  345 HEFRPERWLGAA--EKGKLDryLVPFSKGSRSCLGINLAYAELYLALA 390
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
245-518 2.56e-38

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: 145.41  E-value: 2.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 245 FLYYLtPD--GQRFRRACHLVHDFTDAVIQERrctlptqgIDDFLKNKAKSKTLD-FIDVLLLSKDEDGkELSDEDIRAE 321
Cdd:cd11065  158 FLRYL-PSwlGAPWKRKARELRELTRRLYEGP--------FEAAKERMASGTATPsFVKDLLEELDKEG-GLSEEEIKYL 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 322 ADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPieiEWDDLAQLPFLTMCIKESLRLHPPVPV-IS 399
Cdd:cd11065  228 AGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVgPDRLP---TFEDRPNLPYVNAIVKEVLRWRPVAPLgIP 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 400 RCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF--DQENIKERSPLAFIPFSAGPRNCIGQAFAMAE 477
Cdd:cd11065  305 HALTEDDEY-EGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYldDPKGTPDPPDPPHFAFGFGRRICPGRHLAENS 383
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 193083180 478 MKVVLALTLLHFRILPTHTEPRRKPELILRAEGGLWLRVEP 518
Cdd:cd11065  384 LFIAIARLLWAFDIKKPKDEGGKEIPDEPEFTDGLVSHPLP 424
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
283-489 2.95e-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: 145.30  E-value: 2.95e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 283 IDDFLKNKAKSKTLDFIDVLLLSKDEDGK----ELSDEDIRAeadtFMFE----GHDTTASGLSWVLYHLAKHPEYQEQC 354
Cdd:cd11072  190 IDEHLDKKRSKDEDDDDDDLLDLRLQKEGdlefPLTRDNIKA----IILDmflaGTDTSATTLEWAMTELIRNPRVMKKA 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 355 RQEVQELLKDREpiEIEWDDLAQLPFLTMCIKESLRLHPPVP-VISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTV 433
Cdd:cd11072  266 QEEVREVVGGKG--KVTEEDLEKLKYLKAVIKETLRLHPPAPlLLPRECREDCKI-NGYDIPAKTRVIVNAWAIGRDPKY 342
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 193083180 434 WPDPEVYDPFRFDQENIKER-SPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHF 489
Cdd:cd11072  343 WEDPEEFRPERFLDSSIDFKgQDFELIPFGAGRRICPGITFGLANVELALANLLYHF 399
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
243-498 5.79e-37

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: 141.70  E-value: 5.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 243 TDFLYYLTP-DGQRFRRACH----LVHDFTDAVIQERRctlptqgiddfLKNKAKSKTLDFIDVLLLSKDEDGKeLSDED 317
Cdd:cd11076  157 SDHLPWLRWlDLQGIRRRCSalvpRVNTFVGKIIEEHR-----------AKRSNRARDDEDDVDVLLSLQGEEK-LSDSD 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 318 IRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPIEiewDDLAQLPFLTMCIKESLRLHPPVP 396
Cdd:cd11076  225 MIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVgGSRRVAD---SDVAKLPYLQAVVKETLRLHPPGP 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 397 VIS--RCCTQDfVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKER-----SPLAFIPFSAGPRNCI 469
Cdd:cd11076  302 LLSwaRLAIHD-VTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGADvsvlgSDLRLAPFGAGRRVCP 380
                        250       260
                 ....*....|....*....|....*....
gi 193083180 470 GQAFAMAEMKVVLALTLLHFRILPTHTEP 498
Cdd:cd11076  381 GKALGLATVHLWVAQLLHEFEWLPDDAKP 409
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
244-483 1.16e-35

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: 138.14  E-value: 1.16e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 244 DFLYYLTP----------DGQRFRRAchlvhDFTDAVIQERRctlptQGIDDflKNKAKSKTLDFIDVLLLSKDEDGK-E 312
Cdd:cd11075  159 DFFPALTWllnrrrwkkvLELRRRQE-----EVLLPLIRARR-----KRRAS--GEADKDYTDFLLLDLLDLKEEGGErK 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 313 LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREpiEIEWDDLAQLPFLTMCIKESLRLH 392
Cdd:cd11075  227 LTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEA--VVTEEDLPKMPYLKAVVLETLRRH 304
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 393 PPVP-VISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF--------DQENIKErspLAFIPFSA 463
Cdd:cd11075  305 PPGHfLLPHAVTEDTVL-GGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFlaggeaadIDTGSKE---IKMMPFGA 380
                        250       260
                 ....*....|....*....|
gi 193083180 464 GPRNCIGQAFAMAEMKVVLA 483
Cdd:cd11075  381 GRRICPGLGLATLHLELFVA 400
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
264-491 3.17e-35

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


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 136.77  E-value: 3.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 264 HDFTDAVIQERRCTLPTQGIDDflKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIR-AEADTFMfEGHDTTASGLSWVLY 342
Cdd:cd20652  183 HAIYQKIIDEHKRRLKPENPRD--AEDFELCELEKAKKEGEDRDLFDGFYTDEQLHhLLADLFG-AGVDTTITTLRWFLL 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 343 HLAKHPEYQEQCRQEVQELLKDREPIEIEwdDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKG--IV 419
Cdd:cd20652  260 YMALFPKEQRRIQRELDEVVGRPDLVTLE--DLSSLPYLQACISESQRIRSVVPLgIPHGCTEDAVL-AGYRIPKGsmII 336
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193083180 420 CLINiiGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI 491
Cdd:cd20652  337 PLLW--AVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKFRI 406
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
235-491 5.64e-35

cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of predominantly fungal cytochrome P450s (CYPs) with similarity to Fusarium fujikuroi Cytochrome P450 503A1 (CYP503A1, also called ent-kaurene oxidase or cytochrome P450-4), Aspergillus nidulans austinol synthesis protein I (ausI), Alternaria alternata tentoxin synthesis protein 1 (TES1), and Acanthamoeba polyphaga mimivirus cytochrome P450 51 (CYP51, also called P450-LIA1 or sterol 14-alpha demethylase). Ent-kaurene oxidase catalyzes three successive oxidations of the 4-methyl group of ent-kaurene to form kaurenoic acid, an intermediate in gibberellin biosynthesis. AusI and TES1 are cytochrome P450 monooxygenases that mediate the biosynthesis of the meroterpenoids, austinol and dehydroaustinol, and the phytotoxin tentoxin, respectively. P450-LIA1 catalyzes the 14-alpha demethylation of obtusifoliol and functions in steroid biosynthesis. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 136.27  E-value: 5.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 235 RNQQILLHTDFLYYLTPDGQRFRRACH-----LVHDFTDAVIQERRCT---LPT--QGIDDFLKNKAKSKTLDFIDVL-- 302
Cdd:cd11041  133 RNEEWLDLTINYTIDVFAAAAALRLFPpflrpLVAPFLPEPRRLRRLLrraRPLiiPEIERRRKLKKGPKEDKPNDLLqw 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 303 LLSKDEDGKELSDEDIraeADTFM---FEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDrepiEIEWDD--LAQ 377
Cdd:cd11041  213 LIEAAKGEGERTPYDL---ADRQLalsFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAE----HGGWTKaaLNK 285
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 378 LPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF----DQENIKE 452
Cdd:cd11041  286 LKKLDSFMKESQRLNPLSLVsLRRKVLKDVTLSDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFyrlrEQPGQEK 365
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 193083180 453 RSPLA-----FIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI 491
Cdd:cd11041  366 KHQFVstspdFLGFGHGRHACPGRFFASNEIKLILAHLLLNYDF 409
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
239-504 2.04e-34

cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including Diploptera punctata cytochrome P450 15A1 (CYP15A1 or CYP15A1), Panulirus argus CYP2L1, and CYP303A1, CYP304A1, and CYP305A1 from Drosophila melanogaster. CYP15A1, also called methyl farnesoate epoxidase, catalyzes the conversion of methyl farnesoate to juvenile hormone III acid during juvenile hormone biosynthesis. CYP303A1, CYP304A1, and CYP305A1 may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. The CYP15A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410744 [Multi-domain]  Cd Length: 423  Bit Score: 134.27  E-value: 2.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 239 ILLHTDFLYYLTPDGQRFRRACHL---VHDFTDAVIQERRCTLPTQGIDDFlknkaksktldfIDVLL---LSKDEDGKE 312
Cdd:cd20651  153 LLNQFPWLRFIAPEFSGYNLLVELnqkLIEFLKEEIKEHKKTYDEDNPRDL------------IDAYLremKKKEPPSSS 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 313 LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPieiEWDDLAQLPFLTMCIKESLRL 391
Cdd:cd20651  221 FTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVgRDRLP---TLDDRSKLPYTEAVILEVLRI 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 392 HPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIG 470
Cdd:cd20651  298 FTLVPIgIPHRALKDTTL-GGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLG 376
                        250       260       270
                 ....*....|....*....|....*....|....
gi 193083180 471 QAFAMAEMKVVLALTLLHFRILPthtEPRRKPEL 504
Cdd:cd20651  377 ESLARNELFLFFTGLLQNFTFSP---PNGSLPDL 407
PLN02738 PLN02738
carotene beta-ring hydroxylase
14-489 3.49e-34

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 136.58  E-value: 3.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  14 VAASPWLLLLLVGGSWL--LARVLAWTYTFYDNCRRlqcFPQPPKQNwfwGHQGLVTpTEEGMKTLTQLVTTYPQGFKLW 91
Cdd:PLN02738  99 VQKPGFPATLRNGLAKLgpPGELLAFLFTWVEAGEG---YPKIPEAK---GSISAVR-GEAFFIPLYELFLTYGGIFRLT 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180  92 LGPTfPLLILCHPDIIRPITSASAAVAPKDmIFYGFLKPWLGDGLLLSGGDKWSRHRRMLTPAFHFNILKPYMKIFNKSV 171
Cdd:PLN02738 172 FGPK-SFLIVSDPSIAKHILRDNSKAYSKG-ILAEILEFVMGKGLIPADGEIWRVRRRAIVPALHQKYVAAMISLFGQAS 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 172 NIMHDKWQRLASEGSArLDMFEHISLMTLDSLQKCVFSFESNCQEKPSEYIAAILELSAFVEKRNQQILLHTDFLYY--L 249
Cdd:PLN02738 250 DRLCQKLDAAASDGED-VEMESLFSRLTLDIIGKAVFNYDFDSLSNDTGIVEAVYTVLREAEDRSVSPIPVWEIPIWkdI 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 250 TPDGQRFRRACHLVHDFTDAVIqerrctlptqgidDFLKNKAKSKTLDFIDVLLLSKD--------EDGKELSDEDIRAE 321
Cdd:PLN02738 329 SPRQRKVAEALKLINDTLDDLI-------------AICKRMVEEEELQFHEEYMNERDpsilhfllASGDDVSSKQLRDD 395
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 322 ADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIeIEwdDLAQLPFLTMCIKESLRLHPPVPVISRC 401
Cdd:PLN02738 396 LMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPT-IE--DMKKLKYTTRVINESLRLYPQPPVLIRR 472
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 402 CTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF--DQENIKERSP-LAFIPFSAGPRNCIGQAFAMAEM 478
Cdd:PLN02738 473 SLENDML-GGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWplDGPNPNETNQnFSYLPFGGGPRKCVGDMFASFEN 551
                        490
                 ....*....|.
gi 193083180 479 KVVLALTLLHF 489
Cdd:PLN02738 552 VVATAMLVRRF 562
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
245-488 9.81e-32

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


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 127.10  E-value: 9.81e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 245 FLYYLTPDGQ--RFRRACHLVHDFTDAVIQERrctlptqgIDDFlKNKAKSKTLDFIDVLLLSKDEDGKEL-SDEDIRAE 321
Cdd:cd20658  171 FLRGLDLDGHekIVREAMRIIRKYHDPIIDER--------IKQW-REGKKKEEEDWLDVFITLKDENGNPLlTPDEIKAQ 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 322 ADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPIEiewDDLAQLPFLTMCIKESLRLHPPVP-VIS 399
Cdd:cd20658  242 IKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVgKERLVQE---SDIPNLNYVKACAREAFRLHPVAPfNVP 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 400 RCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIK---ERSPLAFIPFSAGPRNCIGQAFAMA 476
Cdd:cd20658  319 HVAMSDTTV-GGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEvtlTEPDLRFISFSTGRRGCPGVKLGTA 397
                        250
                 ....*....|..
gi 193083180 477 eMKVVLALTLLH 488
Cdd:cd20658  398 -MTVMLLARLLQ 408
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
227-519 1.17e-31

cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three functional human members: CYP1A1, CYP1A2 and CYP1B1, which are regulated by the aryl hydrocarbon receptor (AhR), ligand-activated transcriptional factor that dimerizes with AhR nuclear translocator (ARNT). CYP1 enzymes are involved in the metabolism of endogenous hormones, xenobiotics, and drugs. Included in the CYP1 family is CYP1D1 (cytochrome P450 family 1, subfamily D, polypeptide 1), which is not expressed in humans as its gene is pseudogenized due to five nonsense mutations in the putative coding region, but is functional in in other organisms including cynomolgus monkey. Zebrafish CYP1D1 expression is not regulated by AhR. The CYP1 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 126.64  E-value: 1.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 227 ELSAFVEKRNQqillhTDF---LYYLTPDG-QRFRRACHLVHDFTDAVIQERRCTLptqgiddflknkAKSKTLDFIDVL 302
Cdd:cd11028  148 DFGAFVGAGNP-----VDVmpwLRYLTRRKlQKFKELLNRLNSFILKKVKEHLDTY------------DKGHIRDITDAL 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 303 LLSKDE------DGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIewDDLA 376
Cdd:cd11028  211 IKASEEkpeeekPEVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRL--SDRP 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 377 QLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF--DQENIKER 453
Cdd:cd11028  289 NLPYTEAFILETMRHSSFVPFtIPHATTRDTTL-NGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFldDNGLLDKT 367
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193083180 454 SPLAFIPFSAGPRNCIGQAFAMAEMKVVLA--LTLLHFRILPTHteprrkpELILRAEGGLWLRVEPL 519
Cdd:cd11028  368 KVDKFLPFGAGRRRCLGEELARMELFLFFAtlLQQCEFSVKPGE-------KLDLTPIYGLTMKPKPF 428
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
284-488 3.10e-31

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


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 125.61  E-value: 3.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 284 DDFL-----KNKAKS----KTLDFIDVLLLSKDED--GKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQE 352
Cdd:cd20657  184 DALLtkileEHKATAqerkGKPDFLDFVLLENDDNgeGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILK 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 353 QCRQEVQELL-KDREPIEiewDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYN 430
Cdd:cd20657  264 KAQEEMDQVIgRDRRLLE---SDIPNLPYLQAICKETFRLHPSTPLnLPRIASEACEV-DGYYIPKGTRLLVNIWAIGRD 339
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193083180 431 PTVWPDPEVYDPFRF---DQENIKER-SPLAFIPFSAGPRNCIGQAFAMAEMKVVLAlTLLH 488
Cdd:cd20657  340 PDVWENPLEFKPERFlpgRNAKVDVRgNDFELIPFGAGRRICAGTRMGIRMVEYILA-TLVH 400
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
263-498 1.40e-30

cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, most diverse CYP families in vertebrates. It includes many subfamilies across vertebrate species but not all subfamilies are found in multiple vertebrate taxonomic classes. The CYP2U and CYP2R genes are present in the vertebrate ancestor and are shared across all vertebrate classes, whereas some subfamilies are lineage-specific, such as CYP2B and CYP2S in mammals. CYP2 enzymes play important roles in drug metabolism. The CYP2 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 123.44  E-value: 1.40e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 263 VHDFTDAVIQERRCTLptqgidDFlknkakSKTLDFIDVLLLSKDEDGK----ELSDEDIRAEADTFMFEGHDTTASGLS 338
Cdd:cd11026  180 IKSFIRELVEEHRETL------DP------SSPRDFIDCFLLKMEKEKDnpnsEFHEENLVMTVLDLFFAGTETTSTTLR 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 339 WVLYHLAKHPEYQEQCRQEVQELL-KDREPieiEWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPK 416
Cdd:cd11026  248 WALLLLMKYPHIQEKVQEEIDRVIgRNRTP---SLEDRAKMPYTDAVIHEVQRFGDIVPLgVPHAVTRDTKF-RGYTIPK 323
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 417 GIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI-LPTH 495
Cdd:cd11026  324 GTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSLsSPVG 403

                 ...
gi 193083180 496 TEP 498
Cdd:cd11026  404 PKD 406
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
146-499 3.83e-30

cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial CYPs similar to Agrobacterium tumefaciens plant-inducible cytochrome P450-pinF1, which is not essential for virulence but may be involved in the detoxification of plant protective agents at the site of wounding. The P450-pinF1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 120.87  E-value: 3.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 146 RHRRMLTPAFHFNILKPYMK-IFNKsvnIMHDKWQRLASEGSArlDMFEHISLmtldslqkcvfsfesncqEKPSEYIAA 224
Cdd:cd20629   58 RRRRLLQPAFAPRAVARWEEpIVRP---IAEELVDDLADLGRA--DLVEDFAL------------------ELPARVIYA 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 225 ILELSAFVEKRNQQI---LLHTdFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTlPTqgiDDFLKnkaksktldfidv 301
Cdd:cd20629  115 LLGLPEEDLPEFTRLalaMLRG-LSDPPDPDVPAAEAAAAELYDYVLPLIAERRRA-PG---DDLIS------------- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 302 LLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQevqellkDREpieiewddlaqlpFL 381
Cdd:cd20629  177 RLLRAEVEGEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRR-------DRS-------------LI 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 382 TMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFrfdqenikeRSPLAFIPF 461
Cdd:cd20629  237 PAAIEEGLRWEPPVASVPRMALRDVEL-DGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDID---------RKPKPHLVF 306
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 193083180 462 SAGPRNCIGQAFAMAEMKVVLALTLLHF---RILPTHTEPR 499
Cdd:cd20629  307 GGGAHRCLGEHLARVELREALNALLDRLpnlRLDPDAPAPE 347
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
168-487 5.45e-30

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 121.56  E-value: 5.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 168 NKSVNIMHDKWQRL-------ASEGSARLDMFEHISLMTLDSLQKCV-----FSFESNCQEKPS---EYIAAILELSAFV 232
Cdd:cd20653   79 NSFSSIRRDEIRRLlkrlardSKGGFAKVELKPLFSELTFNNIMRMVagkryYGEDVSDAEEAKlfrELVSEIFELSGAG 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 233 EKrnqqillhTDFLYYLT-PDGQRFRRACHLVHDFTDAVIQERrctlptqgIDDFLKNKAKSKTLdFIDVLLLSKDEDGK 311
Cdd:cd20653  159 NP--------ADFLPILRwFDFQGLEKRVKKLAKRRDAFLQGL--------IDEHRKNKESGKNT-MIDHLLSLQESQPE 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 312 ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLK-DREpieIEWDDLAQLPFLTMCIKESLR 390
Cdd:cd20653  222 YYTDEIIKGLILVMLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGqDRL---IEESDLPKLPYLQNIISETLR 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 391 LHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQEnikERSPLAFIPFSAGPRNCI 469
Cdd:cd20653  299 LYPAAPLlVPHESSEDCKI-GGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFEGE---EREGYKLIPFGLGRRACP 374
                        330
                 ....*....|....*....
gi 193083180 470 GQAFAmaeMKVV-LALTLL 487
Cdd:cd20653  375 GAGLA---QRVVgLALGSL 390
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
297-518 5.55e-30

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: 121.75  E-value: 5.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLL-----SKDEDGKELSDEDIR-AEADTFMfEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEi 370
Cdd:cd20674  201 DMTDYMLQglgqpRGEKGMGQLLEGHVHmAVVDLFI-GGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPS- 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 371 eWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLPdGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQEN 449
Cdd:cd20674  279 -YKDRARLPLLNATIAEVLRLRPVVPLaLPHRTTRDSSIA-GYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPG 356
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 193083180 450 IKERsplAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPRrkPELILRAegGLWLRVEP 518
Cdd:cd20674  357 AANR---ALLPFGCGARVCLGEPLARLELFVFLARLLQAFTLLPPSDGAL--PSLQPVA--GINLKVQP 418
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
312-504 7.10e-30

cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome P450 family 7, subfamily B, polypeptide 1, cytochrome P450 family 8, subfamily A, polypeptide 1; This family is composed of cytochrome P450s (CYPs) with similarity to the human P450s CYP7A1, CYP7B1, CYP8B1, CYP39A1 and prostacyclin synthase (CYP8A1). CYP7A1, CYP7B1, CYP8B1, and CYP39A1 are involved in the catabolism of cholesterol to bile acids (BAs) in two major pathways. CYP7A1 (cholesterol 7alpha-hydroxylase) and CYP8B1 (sterol 12-alpha-hydroxylase) function in the classic (or neutral) pathway, which leads to two bile acids: cholic acid (CA) and chenodeoxycholic acid (CDCA). CYP7B1 and CYP39A1 are 7-alpha-hydroxylases involved in the alternative (or acidic) pathway, which leads mainly to the formation of CDCA. Prostacyclin synthase (CYP8A1) catalyzes the isomerization of prostaglandin H2 to prostacyclin (or prostaglandin I2), a potent mediator of vasodilation and anti-platelet aggregation. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 121.70  E-value: 7.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 312 ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEWDD---LAQLPFLTMCIKES 388
Cdd:cd11040  218 GLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTNAILDLtdlLTSCPLLDSTYLET 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 389 LRLHPpVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRF---DQENIKERSPLAFIPFSAG 464
Cdd:cd11040  298 LRLHS-SSTSVRLVTEDTVLGGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkkDGDKKGRGLPGAFRPFGGG 376
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 193083180 465 PRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPRRKPEL 504
Cdd:cd11040  377 ASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWKVPGM 416
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
148-484 1.21e-29

C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 710; C-22 sterol desaturase (EC 1.14.19.41), also called sterol 22-desaturase, is required for the formation of the C-22 double bond in the sterol side chain of delta22-unsaturated sterols, which are present specifically in fungi and plants. This enzyme is also called cytochrome P450 61 (CYP61) in fungi and cytochrome P450 710 (CYP710) in plants. The CYP61/CYP710 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410703 [Multi-domain]  Cd Length: 415  Bit Score: 120.81  E-value: 1.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 148 RRMLTPAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKcVFSfesncqekpSEYIaaile 227
Cdd:cd11082   62 RKSLLPLFTRKALGLYLPIQERVIRKHLAKWLENSKSGDKPIEMRPLIRDLNLETSQT-VFV---------GPYL----- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 228 lsafvekRNQQILLHTDFLYYLT---------PdGQRFRRACH----LVHDFTDAVIQERRCTL----PTQGIDDFLKnk 290
Cdd:cd11082  127 -------DDEARRFRIDYNYFNVgflalpvdfP-GTALWKAIQarkrIVKTLEKCAAKSKKRMAageePTCLLDFWTH-- 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 291 aksKTLDFIDVLLLSKDEDGKELSDEDIraeADT---FMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREP 367
Cdd:cd11082  197 ---EILEEIKEAEEEGEPPPPHSSDEEI---AGTlldFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEP 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 368 iEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPtvWPDPEVYDPFRFDQ 447
Cdd:cd11082  271 -PLTLDLLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLTEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSP 347
                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 193083180 448 ENIKER-SPLAFIPFSAGPRNCIGQAFAMAEMKVVLAL 484
Cdd:cd11082  348 ERQEDRkYKKNFLVFGAGPHQCVGQEYAINHLMLFLAL 385
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
182-516 1.48e-29

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 121.81  E-value: 1.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 182 ASEGSARLDMFEHISLMTLDSLQKCVFSFESNCQekpSEYIAAILELSAFvekRNQQILLHTDFLYYLTPDGQRFR---- 257
Cdd:PLN03195 161 ASFANQVVDMQDLFMRMTLDSICKVGFGVEIGTL---SPSLPENPFAQAF---DTANIIVTLRFIDPLWKLKKFLNigse 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 258 ----RACHLVHDFTDAVIQERRCTLPTQGIDdflKNKAKSKTLD-FIdvlLLSKDEDGKeLSDEDIRAEADTFMFEGHDT 332
Cdd:PLN03195 235 allsKSIKVVDDFTYSVIRRRKAEMDEARKS---GKKVKHDILSrFI---ELGEDPDSN-FTDKSLRDIVLNFVIAGRDT 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 333 TASGLSWVLYHLAKHPEYQEQCRQEVQELLKDR-EPIEIE-----------------WDDLAQLPFLTMCIKESLRLHPP 394
Cdd:PLN03195 308 TATTLSWFVYMIMMNPHVAEKLYSELKALEKERaKEEDPEdsqsfnqrvtqfaglltYDSLGKLQYLHAVITETLRLYPA 387
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 395 VPVISRCCTQDFVLPDGRVIPKGIVcliniigIHYNP-------TVW-PDPEVYDPFRFDQENI-KERSPLAFIPFSAGP 465
Cdd:PLN03195 388 VPQDPKGILEDDVLPDGTKVKAGGM-------VTYVPysmgrmeYNWgPDAASFKPERWIKDGVfQNASPFKFTAFQAGP 460
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193083180 466 RNCIGQAFAMAEMKVVLAL--TLLHFRILPTHtEPRRKPELILRAEGGLWLRV 516
Cdd:PLN03195 461 RICLGKDSAYLQMKMALALlcRFFKFQLVPGH-PVKYRMMTILSMANGLKVTV 512
PLN02655 PLN02655
ent-kaurene oxidase
274-480 1.84e-29

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 121.00  E-value: 1.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 274 RRCTLPTQGIDDFLKNKAKSKTLD-FIDVLLlskdEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQE 352
Cdd:PLN02655 222 RRTAVMKALIKQQKKRIARGEERDcYLDFLL----SEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQE 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 353 QCRQEVQELLKDREPIEiewDDLAQLPFLTMCIKESLRLHPPVPVI-SRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNP 431
Cdd:PLN02655 298 RLYREIREVCGDERVTE---EDLPNLPYLNAVFHETLRKYSPVPLLpPRFVHEDTTL-GGYDIPAGTQIAINIYGCNMDK 373
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 193083180 432 TVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIG--QAFAMAEMKV 480
Cdd:PLN02655 374 KRWENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCAGslQAMLIACMAI 424
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
143-501 4.54e-29

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: 119.38  E-value: 4.54e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 143 KWSRHRRMLTPafhfNILKP-----YMKIFNKSVNIMHDKWQRLaSEGSARLDM------------FEHISLMTLDSLQK 205
Cdd:cd20646   65 KWYRLRSVLNQ----RMLKPkevslYADAINEVVSDLMKRIEYL-RERSGSGVMvsdlanelykfaFEGISSILFETRIG 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 206 CVfsfESNCQEKPSEYIAAI---LELSAFVekrnqqILLhTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERrctlpTQG 282
Cdd:cd20646  140 CL---EKEIPEETQKFIDSIgemFKLSEIV------TLL-PKWTRPYLPFWKRYVDAWDTIFSFGKKLIDKK-----MEE 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 283 IDDFLKN--KAKSKTLDFidvlLLSKDEdgkeLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQE 360
Cdd:cd20646  205 IEERVDRgePVEGEYLTY----LLSSGK----LSPKEVYGSLTELLLAGVDTTSNTLSWALYHLARDPEIQERLYQEVIS 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 361 LLK-DREPIEiewDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEV 439
Cdd:cd20646  277 VCPgDRIPTA---EDIAKMPLLKAVIKETLRLYPVVPGNARVIVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPER 353
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193083180 440 YDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPthtEPRRK 501
Cdd:cd20646  354 FKPERWLRDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALSRLIKRFEVRP---DPSGG 412
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
283-498 1.34e-28

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


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 117.60  E-value: 1.34e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 283 IDDFLKNKAKSKTLDFidvllLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL 362
Cdd:cd20645  197 IDKRLQRYSQGPANDF-----LCDIYHDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVL 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 363 KDREPIEIEwdDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDgRVIPKGIVCLINIIGIHYNPTVWPDPEVYDP 442
Cdd:cd20645  272 PANQTPRAE--DLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGD-YLLPKGTVLMINSQALGSSEEYFEDGRQFKP 348
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193083180 443 FRFDQENiKERSPLAFIPFSAGPRNCIGQafAMAEMKVVLALTLL--HFRILPTHTEP 498
Cdd:cd20645  349 ERWLQEK-HSINPFAHVPFGIGKRMCIGR--RLAELQLQLALCWIiqKYQIVATDNEP 403
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
287-489 2.48e-28

cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in flowering plants and could be classified into ten subfamilies, CYP93A-K. CYP93A appears to be the ancestor that was derived in flowering plants, and the remaining subfamiles show lineage-specific distribution: CYP93B and CYP93C are present in dicots; CYP93F is distributed only in Poaceae; CYP93G and CYP93J are monocot-specific; CYP93E is unique to legumes; CYP93H and CYP93K are only found in Aquilegia coerulea; and CYP93D is Brassicaceae-specific. Members of this family include: Glycyrrhiza echinata CYP93B1, also called licodione synthase (EC 1.14.14.140), that catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively; and Glycine max CYP93A1, also called 3,9-dihydroxypterocarpan 6A-monooxygenase (EC 1.14.14.93), that is involved in the biosynthesis of the phytoalexin glyceollin. CYP93 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 117.31  E-value: 2.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 287 LKNKAKSKTLDFIDVLL-LSKDEDGK-ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-K 363
Cdd:cd20655  196 RKKRKEGGSKDLLDILLdAYEDENAEyKITRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVgK 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 364 DREpieIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPF 443
Cdd:cd20655  276 TRL---VQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKI-NGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPE 351
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193083180 444 RF-------DQENIKERSpLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHF 489
Cdd:cd20655  352 RFlassrsgQELDVRGQH-FKLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCF 403
PLN02687 PLN02687
flavonoid 3'-monooxygenase
244-488 6.74e-28

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 116.83  E-value: 6.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 244 DF---LYYLTPDG--QRFRRACHLVHDFTDAVIQERRCTLPTQGiddflknkakSKTLDFIDVLLLSKDE-----DGKEL 313
Cdd:PLN02687 224 DFvpaLRWLDLQGvvGKMKRLHRRFDAMMNGIIEEHKAAGQTGS----------EEHKDLLSTLLALKREqqadgEGGRI 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 314 SDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPIEIewdDLAQLPFLTMCIKESLRLH 392
Cdd:PLN02687 294 TDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVgRDRLVSES---DLPQLTYLQAVIKETFRLH 370
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 393 PPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF----DQENIKER-SPLAFIPFSAGPR 466
Cdd:PLN02687 371 PSTPLsLPRMAAEECEI-NGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFlpggEHAGVDVKgSDFELIPFGAGRR 449
                        250       260
                 ....*....|....*....|..
gi 193083180 467 NCIGQAFAMaEMKVVLALTLLH 488
Cdd:PLN02687 450 ICAGLSWGL-RMVTLLTATLVH 470
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
237-495 8.42e-28

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


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 115.15  E-value: 8.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 237 QQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPTqgiDDFLKNKaksktLDFIDVLLLSKDEDgkELSDE 316
Cdd:cd20616  154 QALLIKPDIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRIST---AEKLEDH-----MDFATELIFAQKRG--ELTAE 223
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 317 DIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREpieIEWDDLAQLPFLTMCIKESLRLHPPVP 396
Cdd:cd20616  224 NVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGERD---IQNDDLQKLKVLENFINESMRYQPVVD 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 397 VISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPtVWPDPEvydpfRFDQENIKERSPLA-FIPFSAGPRNCIGQAFAM 475
Cdd:cd20616  301 FVMRKALEDDVI-DGYPVKKGTNIILNIGRMHRLE-FFPKPN-----EFTLENFEKNVPSRyFQPFGFGPRSCVGKYIAM 373
                        250       260
                 ....*....|....*....|
gi 193083180 476 AEMKVVLALTLLHFRILPTH 495
Cdd:cd20616  374 VMMKAILVTLLRRFQVCTLQ 393
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
258-487 4.25e-27

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


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 113.39  E-value: 4.25e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 258 RACHLVHDFTDAVIQERrctlptqgiddfLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGL 337
Cdd:cd20636  180 KARDILHEYMEKAIEEK------------LQRQQAAEYCDALDYMIHSARENGKELTMQELKESAVELIFAAFSTTASAS 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 338 SWVLYHLAKHPEYQEQCRQEV--QELLKDRE--PIEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRV 413
Cdd:cd20636  248 TSLVLLLLQHPSAIEKIRQELvsHGLIDQCQccPGALSLEKLSRLRYLDCVVKEVLRLLPPVSGGYRTALQTFEL-DGYQ 326
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193083180 414 IPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSP-LAFIPFSAGPRNCIGQAFAMAEMKvVLALTLL 487
Cdd:cd20636  327 IPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGrFNYIPFGGGVRSCIGKELAQVILK-TLAVELV 400
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
283-498 5.89e-27

cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically reside in dicots and are usually induced by distinct environmental stresses. Characterized members include: Glycine max CYP82A3 that is induced by infection, salinity and drought stresses, and is involved in the jasmonic acid and ethylene signaling pathway, enhancing plant resistance; Arabidopsis thaliana CYP82G1 that catalyzes the breakdown of the C(20)-precursor (E,E)-geranyllinalool to the insect-induced C(16)-homoterpene (E,E)-4,8,12-trimethyltrideca-1,3,7,11-tetraene (TMTT); and Papaver somniferum CYP82N4, also called methyltetrahydroprotoberberine 14-monooxygenase, and CYP82Y1, also called N-methylcanadine 1-hydroxylase. CYP82N4 catalyzes the conversion of N-methylated protoberberine alkaloids N-methylstylopine and N-methylcanadine into protopine and allocryptopine, respectively, in the biosynthesis of isoquinoline alkaloid sanguinarine. CYP82Y1 catalyzes the 1-hydroxylation of N-methylcanadine to 1-hydroxy-N-methylcanadine, the first committed step in the formation of noscapine. CYP82 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 113.48  E-value: 5.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 283 IDDFLKNKAKSKT----LDFIDVLLLSKDEDgKELSDED----IRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQC 354
Cdd:cd20654  200 LEEHRQKRSSSGKskndEDDDDVMMLSILED-SQISGYDadtvIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKA 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 355 RQEVQELL-KDREpieIEWDDLAQLPFLTMCIKESLRLHPPVPVIS-RCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPT 432
Cdd:cd20654  279 QEELDTHVgKDRW---VEESDIKNLVYLQAIVKETLRLYPPGPLLGpREATEDCTV-GGYHVPKGTRLLVNVWKIQRDPN 354
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 433 VWPDPEVYDPFRF--DQENIKERSP-LAFIPFSAGPRNCIGQAFAMAEMKVVLAlTLLH-FRILPTHTEP 498
Cdd:cd20654  355 VWSDPLEFKPERFltTHKDIDVRGQnFELIPFGSGRRSCPGVSFGLQVMHLTLA-RLLHgFDIKTPSNEP 423
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
299-486 5.91e-27

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


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 112.92  E-value: 5.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 299 IDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELlkdrEPIEIEWDDLAQL 378
Cdd:cd20614  190 VAALIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA----GDVPRTPAELRRF 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 379 PFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERsPLAF 458
Cdd:cd20614  266 PLAEALFRETLRLHPPVPFVFRRVLEEIEL-GGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERWLGRDRAPN-PVEL 343
                        170       180       190
                 ....*....|....*....|....*....|.
gi 193083180 459 IPFSAGPRNCIGQAFAMAEM---KVVLALTL 486
Cdd:cd20614  344 LQFGGGPHFCLGYHVACVELvqfIVALAREL 374
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
206-504 1.07e-26

cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific cytochrome P450 that catalyzes omega- and (omega-1)-hydroxylation of fatty acids such as arachidonic acid, docosahexaenoic acid, and other long chain fatty acids. Mutations in CYP2U1 are associated with hereditary spastic paraplegia (HSP), a neurological disorder, and pigmentary degenerative maculopathy associated with progressive spastic paraplegia. CYP2U1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 112.18  E-value: 1.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 206 CVFSFESNCQEKPSEYIAAILELSAFVE-KRNQQILLH--TDFLYYLtPDGQrFRRACHLVHD---FTDAVIQERRCTLP 279
Cdd:cd20666  120 CSMSFGRRFDYQDVEFKTMLGLMSRGLEiSVNSAAILVniCPWLYYL-PFGP-FRELRQIEKDitaFLKKIIADHRETLD 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 280 tqgiddflknkaKSKTLDFIDVLLLSKDEDGKELSDEDIRAE------ADTFmFEGHDTTASGLSWVLYHLAKHPEYQEQ 353
Cdd:cd20666  198 ------------PANPRDFIDMYLLHIEEEQKNNAESSFNEDylfyiiGDLF-IAGTDTTTNTLLWCLLYMSLYPEVQEK 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 354 CRQEVQELL-KDREPieiEWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNP 431
Cdd:cd20666  265 VQAEIDTVIgPDRAP---SLTDKAQMPFTEATIMEVQRMTVVVPLsIPHMASENTVL-QGYTIPKGTVIVPNLWSVHRDP 340
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193083180 432 TVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPrrKPEL 504
Cdd:cd20666  341 AIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPPNAP--KPSM 411
PLN02302 PLN02302
ent-kaurenoic acid oxidase
262-499 1.32e-26

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 112.88  E-value: 1.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 262 LVHDFTDaVIQERRctlptqgidDFLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVL 341
Cdd:PLN02302 242 LVALFQS-IVDERR---------NSRKQNISPRKKDMLDLLLDAEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWAT 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 342 YHLAKHPEYQEQCRQEVQELLKDREPIE--IEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIV 419
Cdd:PLN02302 312 IFLQEHPEVLQKAKAEQEEIAKKRPPGQkgLTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEV-NGYTIPKGWK 390
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 420 CLINIIGIHYNPTVWPDPEVYDPFRFDQENIKersPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPT----- 494
Cdd:PLN02302 391 VLAWFRQVHMDPEVYPNPKEFDPSRWDNYTPK---AGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERLnpgck 467
                        250
                 ....*....|
gi 193083180 495 -----HTEPR 499
Cdd:PLN02302 468 vmylpHPRPK 477
PLN02183 PLN02183
ferulate 5-hydroxylase
209-488 4.01e-26

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 111.48  E-value: 4.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 209 SFESNCQEKPSEYIAAILELSAFVEKRNQqillhTDFLYYL---TPDG--QRFRRACHLVHDFTDAVIQERRCTLPTQGI 283
Cdd:PLN02183 189 AFGSSSNEGQDEFIKILQEFSKLFGAFNV-----ADFIPWLgwiDPQGlnKRLVKARKSLDGFIDDIIDDHIQKRKNQNA 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 284 DDFlknkAKSKTLDFIDVLLLSKDEDGK-----------ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQE 352
Cdd:PLN02183 264 DND----SEEAETDMVDDLLAFYSEEAKvnesddlqnsiKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLK 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 353 QCRQEVQELLK-DREpieIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNP 431
Cdd:PLN02183 340 RVQQELADVVGlNRR---VEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEV-AGYFIPKRSRVMINAWAIGRDK 415
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 193083180 432 TVWPDPEVYDPFRFDQENIKE--RSPLAFIPFSAGPRNCIGQAFAMAEMKVVLAlTLLH 488
Cdd:PLN02183 416 NSWEDPDTFKPSRFLKPGVPDfkGSHFEFIPFGSGRRSCPGMQLGLYALDLAVA-HLLH 473
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
285-504 7.11e-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: 110.10  E-value: 7.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 285 DFLKNKAKSKTLDFID----VLLLSKDEDGKeLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHP--EYQEQCRQEV 358
Cdd:cd11066  193 KKLLAKLKEEIEDGTDkpciVGNILKDKESK-LTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEI 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 359 QELLKDREPIeieWDDLA---QLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVW 434
Cdd:cd11066  272 LEAYGNDEDA---WEDCAaeeKCPYVVALVKETLRYFTVLPLgLPRKTTKDIVY-NGAVIPAGTILFMNAWAANHDPEHF 347
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 435 PDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPrrKPEL 504
Cdd:cd11066  348 GDPDEFIPERWLDASGDLIPGPPHFSFGAGSRMCAGSHLANRELYTAICRLILLFRIGPKDEEE--PMEL 415
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
255-480 1.20e-25

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


Pssm-ID: 410731 [Multi-domain]  Cd Length: 432  Bit Score: 109.13  E-value: 1.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 255 RFRRACHLVHDFTDAVIQERRCTLPTQGiddflknkaksKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTA 334
Cdd:cd20638  179 RGLRARNLIHAKIEENIRAKIQREDTEQ-----------QCKDALQLLIEHSRRNGEPLNLQALKESATELLFGGHETTA 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 335 SGLSWVLYHLAKHPEYQEQCRQEVQE--LL--KDREPIEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpD 410
Cdd:cd20638  248 SAATSLIMFLGLHPEVLQKVRKELQEkgLLstKPNENKELSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFEL-N 326
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 411 GRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKV 480
Cdd:cd20638  327 GYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKI 396
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
303-509 1.40e-25

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: 109.03  E-value: 1.40e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 303 LLSKDEdgkeLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEV----QELLKDREPIeiewddLAQL 378
Cdd:cd20643  224 LLLQDK----LPIEDIKASVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEVlaarQEAQGDMVKM------LKSV 293
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 379 PFLTMCIKESLRLHPPVPVISRCCTQDFVLPDgRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFdqeNIKERSPLAF 458
Cdd:cd20643  294 PLLKAAIKETLRLHPVAVSLQRYITEDLVLQN-YHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERW---LSKDITHFRN 369
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 193083180 459 IPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTH-TEPRRKPELILRAE 509
Cdd:cd20643  370 LGFGFGPRQCLGRRIAETEMQLFLIHMLENFKIETQRlVEVKTTFDLILVPE 421
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
329-502 7.09e-25

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: 107.15  E-value: 7.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 329 GHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEwdDLAQLPFLTMCIKESLRLHPPVPVISRcctqdfVL 408
Cdd:cd20648  246 GVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAA--DVARMPLLKAVVKEVLRLYPVIPGNAR------VI 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 409 PD------GRVIPKGIvcLINIigIHY----NPTVWPDPEVYDPFRFDQENiKERSPLAFIPFSAGPRNCIGQAFAMAEM 478
Cdd:cd20648  318 PDrdiqvgEYIIPKKT--LITL--CHYatsrDENQFPDPNSFRPERWLGKG-DTHHPYASLPFGFGKRSCIGRRIAELEV 392
                        170       180
                 ....*....|....*....|....
gi 193083180 479 KVVLALTLLHFRILPTHTEPRRKP 502
Cdd:cd20648  393 YLALARILTHFEVRPEPGGSPVKP 416
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
302-482 1.24e-24

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 106.56  E-value: 1.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 302 LLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIE-IEWDDLAQLPF 380
Cdd:PLN02196 249 LLGSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGEsLTWEDTKKMPL 328
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 381 LTMCIKESLRLHPPVPVISRCCTQDfVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENikerSPLAFIP 460
Cdd:PLN02196 329 TSRVIQETLRVASILSFTFREAVED-VEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAP----KPNTFMP 403
                        170       180
                 ....*....|....*....|..
gi 193083180 461 FSAGPRNCIGQAFAMAEMKVVL 482
Cdd:PLN02196 404 FGNGTHSCPGNELAKLEISVLI 425
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
273-489 3.24e-24

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: 105.26  E-value: 3.24e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 273 ERRCTLPTQGIDDFLKNKAKSKT-LDFIDVLLLSKDEDgkELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQ 351
Cdd:cd20656  187 ARRDRLTKAIMEEHTLARQKSGGgQQHFVALLTLKEQY--DLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQ 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 352 EQCRQEVQELL-KDREPIEIewdDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYN 430
Cdd:cd20656  265 EKAQEELDRVVgSDRVMTEA---DFPQLPYLQCVVKEALRLHPPTPLMLPHKASENVKIGGYDIPKGANVHVNVWAIARD 341
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 431 PTVWPDPEVYDPFRFDQENIKER-SPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHF 489
Cdd:cd20656  342 PAVWKNPLEFRPERFLEEDVDIKgHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHF 401
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
297-489 4.54e-24

cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or Cyp17a1), also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. It is a dual enzyme that catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reactions. Severe mutations on the enzyme cause combined 17-hydroxylase/17,20-lyase deficiency (17OHD); patients with 17OHD synthesize 11-deoxycorticosterone (DOC) which causes hypertension and hypokalemia. Loss of 17,20-lyase activity precludes sex steroid synthesis and leads to sexual infantilism. Included in this group is a second 17A P450 from teleost fish, CYP17A2, that is more efficient in pregnenolone 17-alpha-hydroxylation than CYP17A1, but does not catalyze the lyase reaction. CYP17A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 104.71  E-value: 4.54e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLLSK----------DEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEV-QELLKDR 365
Cdd:cd20673  202 DLLDALLQAKmnaennnagpDQDSVGLSDDHILMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIdQNIGFSR 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 366 EPieiEWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLPDgRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFR 444
Cdd:cd20673  282 TP---TLSDRNHLPLLEATIREVLRIRPVAPLlIPHVALQDSSIGE-FTIPKGTRVVINLWALHHDEKEWDQPDQFMPER 357
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 193083180 445 F-DQENIKERSP-LAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHF 489
Cdd:cd20673  358 FlDPTGSQLISPsLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRF 404
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
281-515 5.15e-24

cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a retinoic acid-metabolizing cytochrome that plays key roles in retinoic acid (RA) metabolism. It is an all-trans-retinoic acid (atRA) hydroxylase that catalyzes the formation of similar metabolites as CYP26A1. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. In rats, CYP26B1 regulates sex-specific timing of meiotic initiation, independent of RA signaling. CYP26B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 104.55  E-value: 5.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 281 QGIDDFLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEV-- 358
Cdd:cd20637  190 KAIREKLQGTQGKDYADALDILIESAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELrs 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 359 QELLKDREPIE--IEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPD 436
Cdd:cd20637  270 NGILHNGCLCEgtLRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFEL-DGFQIPKGWSVLYSIRDTHDTAPVFKD 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 437 PEVYDPFRFDQENIKERS-PLAFIPFSAGPRNCIGQAFAMAEMKvVLALTLL---HFRiLPTHTEPRRKPELILRAEGGL 512
Cdd:cd20637  349 VDAFDPDRFGQERSEDKDgRFHYLPFGGGVRTCLGKQLAKLFLK-VLAVELAstsRFE-LATRTFPRMTTVPVVHPVDGL 426

                 ...
gi 193083180 513 WLR 515
Cdd:cd20637  427 RVK 429
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
312-509 9.22e-24

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: 103.77  E-value: 9.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 312 ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKD--REPIEIewddLAQLPFLTMCIKESL 389
Cdd:cd20644  227 ELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQisEHPQKA----LTELPLLKAALKETL 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 390 RLHPPVPVISRCCTQDFVLPDGRvIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAfIPFSAGPRNCI 469
Cdd:cd20644  303 RLYPVGITVQRVPSSDLVLQNYH-IPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKH-LAFGFGMRQCL 380
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 193083180 470 GQAFAMAEMKVVLALTLLHFRILPTHTEP-RRKPELILRAE 509
Cdd:cd20644  381 GRRLAEAEMLLLLMHVLKNFLVETLSQEDiKTVYSFILRPE 421
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
311-502 1.14e-23

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: 103.46  E-value: 1.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 311 KELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIEwdDLAQLPFLTMCIKESLR 390
Cdd:cd20647  231 KELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAE--DVPKLPLIRALLKETLR 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 391 LHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKER-SPLAFIPFSAGPRNCI 469
Cdd:cd20647  309 LFPVLPGNGRVTQDDLIV-GGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRvDNFGSIPFGYGIRSCI 387
                        170       180       190
                 ....*....|....*....|....*....|...
gi 193083180 470 GQAFAMAEMKVVLALTLLHFRIlptHTEPRRKP 502
Cdd:cd20647  388 GRRIAELEIHLALIQLLQNFEI---KVSPQTTE 417
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
245-488 2.91e-23

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 102.98  E-value: 2.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 245 FLYYLTPDG--QRFRRACHLVHDFTDAVIQERRctlptqgiDDFLKNKAKSKTLDFIDVLLLSKDEDGKE-LSDEDIRAE 321
Cdd:PLN03112 229 AWRWLDPYGceKKMREVEKRVDEFHDKIIDEHR--------RARSGKLPGGKDMDFVDVLLSLPGENGKEhMDDVEIKAL 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 322 ADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPIEiewDDLAQLPFLTMCIKESLRLHPPVP-VIS 399
Cdd:PLN03112 301 MQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVgRNRMVQE---SDLVHLNYLRCVVRETFRMHPAGPfLIP 377
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 400 RCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF---DQENIKERSPLAF--IPFSAGPRNCIGQAFA 474
Cdd:PLN03112 378 HESLRATTI-NGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHwpaEGSRVEISHGPDFkiLPFSAGKRKCPGAPLG 456
                        250
                 ....*....|....
gi 193083180 475 MAEMKVVLAlTLLH 488
Cdd:PLN03112 457 VTMVLMALA-RLFH 469
PLN03018 PLN03018
homomethionine N-hydroxylase
252-489 3.45e-23

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 102.78  E-value: 3.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 252 DGQ--RFRRACHLVHDFTDAVIQERrctlptqgIDDFLKNKAKSKTLDFIDVLLLSKDEDGKEL-SDEDIRAEADTFMFE 328
Cdd:PLN03018 254 DGQeeRAKVNVNLVRSYNNPIIDER--------VELWREKGGKAAVEDWLDTFITLKDQNGKYLvTPDEIKAQCVEFCIA 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 329 GHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDRepiEIEWDDLAQLPFLTMCIKESLRLHPPVP-VISRCCTQDF 406
Cdd:PLN03018 326 AIDNPANNMEWTLGEMLKNPEILRKALKELDEVVgKDR---LVQESDIPNLNYLKACCRETFRIHPSAHyVPPHVARQDT 402
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 407 VLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQEN--IKE----RSPLAFIPFSAGPRNCIGQAFAMAEMKV 480
Cdd:PLN03018 403 TL-GGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDgiTKEvtlvETEMRFVSFSTGRRGCVGVKVGTIMMVM 481

                 ....*....
gi 193083180 481 VLALTLLHF 489
Cdd:PLN03018 482 MLARFLQGF 490
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
331-494 6.89e-23

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: 100.82  E-value: 6.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 331 DTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPieiEWDD--LAQLPFLTMCIKESLRLHPPVPvisrcctqdFVL 408
Cdd:cd20615  229 DVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGY---PMEDyiLSTDTLLAYCVLESLRLRPLLA---------FSV 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 409 P---------DGRVIPKGIVCLINIIGIHYN-PTVWPDPEVYDPFRFdqENIKERSPL-AFIPFSAGPRNCIGQAFAMAE 477
Cdd:cd20615  297 PessptdkiiGGYRIPANTPVVVDTYALNINnPFWGPDGEAYRPERF--LGISPTDLRyNFWRFGFGPRKCLGQHVADVI 374
                        170
                 ....*....|....*..
gi 193083180 478 MKVVLALTLLHFRILPT 494
Cdd:cd20615  375 LKALLAHLLEQYELKLP 391
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
297-494 2.30e-22

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


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 99.69  E-value: 2.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLLSKDE-----DGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREP-IE 369
Cdd:cd20675  210 DMMDAFILALEKgksgdSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVgRDRLPcIE 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 370 iewdDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDfVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQE 448
Cdd:cd20675  290 ----DQPNLPYVMAFLYEAMRFSSFVPVtIPHATTAD-TSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDE 364
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 193083180 449 NIKERSPLAF--IPFSAGPRNCIGQAFAMAEMKVVLALtLLH---FRILPT 494
Cdd:cd20675  365 NGFLNKDLASsvMIFSVGKRRCIGEELSKMQLFLFTSI-LAHqcnFTANPN 414
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
271-518 6.48e-22

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


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 97.95  E-value: 6.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 271 IQERRCTLPtqgiddflKNKAKSktldFIDVLLLSKDEDGKE---LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKH 347
Cdd:cd20671  186 IEARRPTID--------GNPLHS----YIEALIQKQEEDDPKetlFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKY 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 348 PEYQEQCRQEVQELLKDREPIEIEwdDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGI 427
Cdd:cd20671  254 PHIQKRVQEEIDRVLGPGCLPNYE--DRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQF-KGYLIPKGTPVIPLLSSV 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 428 HYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPThtePRRKP-ELIL 506
Cdd:cd20671  331 LLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLPP---PGVSPaDLDA 407
                        250
                 ....*....|..
gi 193083180 507 RAEGGLWLRVEP 518
Cdd:cd20671  408 TPAAAFTMRPQP 419
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
254-516 7.84e-22

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 98.61  E-value: 7.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 254 QRFRRACHLVHDFTDAVIQERRcTLPTQGIDDFLknkakSKTLDFIDvlllskdeDGKELSDEDIraeadTFMFEGHDTT 333
Cdd:PLN02426 249 RKLKEAIKLVDELAAEVIRQRR-KLGFSASKDLL-----SRFMASIN--------DDKYLRDIVV-----SFLLAGRDTV 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 334 ASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIeIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRV 413
Cdd:PLN02426 310 ASALTSFFWLLSKHPEVASAIREEADRVMGPNQEA-ASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLPDGTF 388
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 414 IPKGIVCLINIIGIHYNPTVW-PDPEVYDPFR------FDQENikersPLAFIPFSAGPRNCIGQAFAMAEMKVVlALTL 486
Cdd:PLN02426 389 VAKGTRVTYHPYAMGRMERIWgPDCLEFKPERwlkngvFVPEN-----PFKYPVFQAGLRVCLGKEMALMEMKSV-AVAV 462
                        250       260       270
                 ....*....|....*....|....*....|....
gi 193083180 487 L---HFRILPTHTE-PRRKPELILRAEGGLWLRV 516
Cdd:PLN02426 463 VrrfDIEVVGRSNRaPRFAPGLTATVRGGLPVRV 496
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
297-488 8.19e-22

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 98.39  E-value: 8.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLLSK-DEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPIEiewDD 374
Cdd:PLN00110 268 DFLDVVMANQeNSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIgRNRRLVE---SD 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 375 LAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKER 453
Cdd:PLN00110 345 LPKLPYLQAICKESFRKHPSTPLnLPRVSTQACEV-NGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKNAKI 423
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 193083180 454 SP----LAFIPFSAGPRNCIGQAFAMAEMKVVLAlTLLH 488
Cdd:PLN00110 424 DPrgndFELIPFGAGRRICAGTRMGIVLVEYILG-TLVH 461
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
245-504 1.32e-21

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


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 97.19  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 245 FLYYLTP--------DGQRFRRACHLVHDFTDAVIQE----RRCTLPTQGIDDFLknkaksktldfiDVLLLSKDEDGKE 312
Cdd:cd20661  166 FLYNAFPwigilpfgKHQQLFRNAAEVYDFLLRLIERfsenRKPQSPRHFIDAYL------------DEMDQNKNDPEST 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 313 LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEieWDDLAQLPFLTMCIKESLRLH 392
Cdd:cd20661  234 FSMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPS--FEDKCKMPYTEAVLHEVLRFC 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 393 PPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQ 471
Cdd:cd20661  312 NIVPLgIFHATSKDAVV-RGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGE 390
                        250       260       270
                 ....*....|....*....|....*....|....
gi 193083180 472 AFAMAEMKVVLALTLLHFRI-LPTHTEPRRKPEL 504
Cdd:cd20661  391 QLARMEMFLFFTALLQRFHLhFPHGLIPDLKPKL 424
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
318-494 1.32e-21

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


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 97.76  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 318 IRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-----KDREPI--EIEwddLAQLPFLTMCIKESLR 390
Cdd:cd20622  263 IHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLRKALYSAHpeavaEGRLPTaqEIA---QARIPYLDAVIEEILR 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 391 LHPPVPVISRCCTQDFVLPdGRVIPKG--IVCLINIigihynPTVW-PDPEVYDPFR-------------FDQENIK--- 451
Cdd:cd20622  340 CANTAPILSREATVDTQVL-GYSIPKGtnVFLLNNG------PSYLsPPIEIDESRRssssaakgkkagvWDSKDIAdfd 412
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 193083180 452 -ER-------------SPLAF--IPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPT 494
Cdd:cd20622  413 pERwlvtdeetgetvfDPSAGptLAFGLGPRGCFGRRLAYLEMRLIITLLVWNFELLPL 471
PLN02966 PLN02966
cytochrome P450 83A1
273-498 1.98e-21

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 97.51  E-value: 1.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 273 ERRCTLPTQGIDDFLKNK-AKSKTLDFIDVLLLSKDED--GKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPE 349
Cdd:PLN02966 242 ERQDTYIQEVVNETLDPKrVKPETESMIDLLMEIYKEQpfASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQ 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 350 YQEQCRQEVQELLKDREPIEIEWDDLAQLPFLTMCIKESLRLHPPVP-VISRCCTQDFVLPdGRVIPKGIVCLINIIGIH 428
Cdd:PLN02966 322 VLKKAQAEVREYMKEKGSTFVTEDDVKNLPYFRALVKETLRIEPVIPlLIPRACIQDTKIA-GYDIPAGTTVNVNAWAVS 400
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193083180 429 YNPTVW-PDPEVYDPFRFDQENIKER-SPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI-LPTHTEP 498
Cdd:PLN02966 401 RDEKEWgPNPDEFRPERFLEKEVDFKgTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFkLPNGMKP 473
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
283-518 2.28e-21

cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in mice and humans. They function as catalysts of arachidonic acid metabolism and are active in the metabolism of fatty acids to generate bioactive compounds. Human CYP2J2, also called arachidonic acid epoxygenase or albendazole monooxygenase (hydroxylating), is a membrane-bound cytochrome P450 primarily expressed in the heart and plays a significant role in cardiovascular diseases. The CYP2J subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 96.41  E-value: 2.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 283 IDDFLKNKAKSKTLDFIDVLL--LSKDED-GKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQ 359
Cdd:cd20662  188 IDKHREDWNPDEPRDFIDAYLkeMAKYPDpTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEID 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 360 ELL-KDREPieiEWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDP 437
Cdd:cd20662  268 RVIgQKRQP---SLADRESMPYTNAVIHEVQRMGNIIPLnVPREVAVDTKL-AGFHLPKGTMILTNLTALHRDPKEWATP 343
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 438 EVYDPFRF-DQENIKERSplAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPThteprrkPELILRAEGGLWLRV 516
Cdd:cd20662  344 DTFNPGHFlENGQFKKRE--AFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKPP-------PNEKLSLKFRMGITL 414

                 ..
gi 193083180 517 EP 518
Cdd:cd20662  415 SP 416
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
309-515 2.55e-21

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


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 95.62  E-value: 2.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 309 DGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEyqeqCRQEVQEllkDREpieiewddlaqlpFLTMCIKES 388
Cdd:cd11080  185 EGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPE----QLAAVRA---DRS-------------LVPRAIAET 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 389 LRLHPPVPVISRCCTQDFVLpDGRVIPKG--IVCLINiiGIHYNPTVWPDPEVYDPFRFDQENIKERSPLA-FIPFSAGP 465
Cdd:cd11080  245 LRYHPPVQLIPRQASQDVVV-SGMEIKKGttVFCLIG--AANRDPAAFEDPDTFNIHREDLGIRSAFSGAAdHLAFGSGR 321
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 193083180 466 RNCIGQAFAMAEMKVVLALtllhfrILPTHTEPRRKPElILRAEGGLWLR 515
Cdd:cd11080  322 HFCVGAALAKREIEIVANQ------VLDALPNIRLEPG-FEYAESGLYTR 364
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
144-493 3.95e-21

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 96.34  E-value: 3.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 144 WSRHRRMLT-PAFHFNILKPYMKIFNKSVNIMHDKWQRLASEGSARLDMFEHISLMTLDSLQKCVFS--FESncQEKPse 220
Cdd:PLN02394 124 WRKMRRIMTvPFFTNKVVQQYRYGWEEEADLVVEDVRANPEAATEGVVIRRRLQLMMYNIMYRMMFDrrFES--EDDP-- 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 221 yiaAILELSAFVEKRNQ--QILLHT--DFLYYLTPDGQRFRRACHLVHD-----FTDAVIQERRCTLPTQGIDdflKNKA 291
Cdd:PLN02394 200 ---LFLKLKALNGERSRlaQSFEYNygDFIPILRPFLRGYLKICQDVKErrlalFKDYFVDERKKLMSAKGMD---KEGL 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 292 KSKtldfIDVLLlsKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEie 371
Cdd:PLN02394 274 KCA----IDHIL--EAQKKGEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVT-- 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 372 WDDLAQLPFLTMCIKESLRLHPPVPVIsrccTQDFVLPDGRV----IPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQ 447
Cdd:PLN02394 346 EPDTHKLPYLQAVVKETLRLHMAIPLL----VPHMNLEDAKLggydIPAESKILVNAWWLANNPELWKNPEEFRPERFLE 421
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 193083180 448 ENIKERS---PLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILP 493
Cdd:PLN02394 422 EEAKVEAngnDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLP 470
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
288-493 1.26e-20

cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The function of CYP2AB1 is unknown. CYP2AB1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 94.14  E-value: 1.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 288 KNKAKSKTLDFIDVLLL----SKDEDGKELSDED-IRAEADTFMfEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL 362
Cdd:cd20667  192 ELRTNEAPQDFIDCYLAqitkTKDDPVSTFSEENmIQVVIDLFL-GGTETTATTLHWALLYMVHHPEIQEKVQQELDEVL 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 363 KDREPIEIEwdDLAQLPFLTMCIKESLRLHPPVPV--ISRCCTQDFVLpdGRVIPKGIVCLINIIGIHYNPTVWPDPEVY 440
Cdd:cd20667  271 GASQLICYE--DRKRLPYTNAVIHEVQRLSNVVSVgaVRQCVTSTTMH--GYYVEKGTIILPNLASVLYDPECWETPHKF 346
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193083180 441 DPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI-LP 493
Cdd:cd20667  347 NPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFqLP 400
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
280-488 1.62e-20

cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is pseudogenized in humans because of five nonsense mutations in the putative coding region. However, in other organisms including cynomolgus monkey, CYP1D1 is a functional drug-metabolizing enzyme that is highly expressed in the liver. CYP1D1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 94.01  E-value: 1.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 280 TQGIDDFLKNKAKSKTLDFIDVLLL---SKDEDGKE--LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQC 354
Cdd:cd20677  194 AKSVQDHYATYDKNHIRDITDALIAlcqERKAEDKSavLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKI 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 355 RQEVQELLKDREPIEieWDDLAQLPFLTMCIKESLRLHPPVP-VISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTV 433
Cdd:cd20677  274 QEEIDEKIGLSRLPR--FEDRKSLHYTEAFINEVFRHSSFVPfTIPHCTTADTTL-NGYFIPKDTCVFINMYQVNHDETL 350
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193083180 434 WPDPEVYDPFRFDQEN---IKERSPLAFIpFSAGPRNCIGQAFAMAEMKVVLAlTLLH 488
Cdd:cd20677  351 WKDPDLFMPERFLDENgqlNKSLVEKVLI-FGMGVRKCLGEDVARNEIFVFLT-TILQ 406
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
283-516 2.15e-20

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


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 93.05  E-value: 2.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 283 IDDFLKNKAKSKTLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRqevqell 362
Cdd:cd11078  175 FADLVAERRREPRDDLISDLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLR------- 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 363 kdrepieiewDDLAQLPfltMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDP 442
Cdd:cd11078  248 ----------ADPSLIP---NAVEETLRYDSPVQGLRRTATRDVEI-GGVTIPAGARVLLLFGSANRDERVFPDPDRFDI 313
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193083180 443 FRfdqENIKERsplafIPFSAGPRNCIGQAFAMAEMKVVL-ALT--LLHFRILPthTEPRRKPELILRAEGGLWLRV 516
Cdd:cd11078  314 DR---PNARKH-----LTFGHGIHFCLGAALARMEARIALeELLrrLPGMRVPG--QEVVYSPSLSFRGPESLPVEW 380
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
307-493 1.30e-19

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


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 91.23  E-value: 1.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 307 DEDGK-ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPieiEWDDLAQLPFLTMC 384
Cdd:cd20676  226 DENANiQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIgRERRP---RLSDRPQLPYLEAF 302
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 385 IKESLRLHPPVP-VISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRF---DQENIKERSPLAFIP 460
Cdd:cd20676  303 ILETFRHSSFVPfTIPHCTTRDTSL-NGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFltaDGTEINKTESEKVML 381
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 193083180 461 FSAGPRNCIGQAFAMAEMKVVLALTL--LHFRILP 493
Cdd:cd20676  382 FGLGKRRCIGESIARWEVFLFLAILLqqLEFSVPP 416
PLN02774 PLN02774
brassinosteroid-6-oxidase
270-518 1.82e-19

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 90.99  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 270 VIQERRCTLPTQgiDDFLKNkaksktldfidvlLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPE 349
Cdd:PLN02774 232 LIQERRASGETH--TDMLGY-------------LMRKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPK 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 350 YQEQCRQEVQELLKDREPIE-IEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIH 428
Cdd:PLN02774 297 ALQELRKEHLAIRERKRPEDpIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMEL-NGYVIPKGWRIYVYTREIN 375
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 429 YNPTVWPDPEVYDPFRFDQENIkERSPLAFIpFSAGPRNCIGQAFAMAEMKvvlalTLLHFRILPTHTEPRRKPELI--- 505
Cdd:PLN02774 376 YDPFLYPDPMTFNPWRWLDKSL-ESHNYFFL-FGGGTRLCPGKELGIVEIS-----TFLHYFVTRYRWEEVGGDKLMkfp 448
                        250
                 ....*....|....
gi 193083180 506 -LRAEGGLWLRVEP 518
Cdd:PLN02774 449 rVEAPNGLHIRVSP 462
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
339-491 1.11e-18

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 88.58  E-value: 1.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 339 WVLYHLAKHPEYQEQCRQEVQELLKD--------REPIEIEWDDLAQLPFLTMCIKESLRLHPpVPVISRCCTQDFVL-- 408
Cdd:cd20633  246 WLLLYLLKHPEAMKAVREEVEQVLKEtgqevkpgGPLINLTRDMLLKTPVLDSAVEETLRLTA-APVLIRAVVQDMTLkm 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 409 PDGR--VIPKG-IVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSplAF-----------IPFSAGPRNCIGQAFA 474
Cdd:cd20633  325 ANGReyALRKGdRLALFPYLAVQMDPEIHPEPHTFKYDRFLNPDGGKKK--DFykngkklkyynMPWGAGVSICPGRFFA 402
                        170
                 ....*....|....*..
gi 193083180 475 MAEMKVVLALTLLHFRI 491
Cdd:cd20633  403 VNEMKQFVFLMLTYFDL 419
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
244-493 1.28e-18

cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called trans-cinnamate 4-monooxygenase (EC 1.14.14.91) or cinnamic acid 4-hydroxylase, catalyzes the regiospecific 4-hydroxylation of cinnamic acid to form precursors of lignin and many other phenolic compounds. It controls the general phenylpropanoid pathway, and controls carbon flux to pigments essential for pollination or UV protection. CYP73 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 88.30  E-value: 1.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 244 DFLYYLTPDGQRFRRACHLVHD-----FTDAVIQERRCTLPTQGIDdflkNKAKSKTLDFIdvllLSKDEDGkELSDEDI 318
Cdd:cd11074  164 DFIPILRPFLRGYLKICKEVKErrlqlFKDYFVDERKKLGSTKSTK----NEGLKCAIDHI----LDAQKKG-EINEDNV 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 319 RAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKdrEPIEIEWDDLAQLPFLTMCIKESLRLHPPVPV- 397
Cdd:cd11074  235 LYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLG--PGVQITEPDLHKLPYLQAVVKETLRLRMAIPLl 312
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 398 ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERS---PLAFIPFSAGPRNCIGQAFA 474
Cdd:cd11074  313 VPHMNLHDAKL-GGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKVEAngnDFRYLPFGVGRRSCPGIILA 391
                        250
                 ....*....|....*....
gi 193083180 475 MAEMKVVLALTLLHFRILP 493
Cdd:cd11074  392 LPILGITIGRLVQNFELLP 410
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
297-505 1.67e-18

cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members are selectively expressed in lung tissues. They are responsible for the bioactivation of several pneumotoxic and carcinogenic chemicals such as benzene, styrene, naphthalene, and 1,1-dichloroethylene. CYP2F1 and CYP2F3 selectively catalyzes the 3-methyl dehydrogenation of 3-methylindole, forming toxic reactive intermediates that can form adducts with proteins and DNA. The CYP2F subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 87.89  E-value: 1.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLLSKDEDGKELS----DEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL-KDREPieiE 371
Cdd:cd20669  202 DFIDCFLTKMAEEKQDPLshfnMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVgRNRLP---T 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 372 WDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENI 450
Cdd:cd20669  279 LEDRARMPYTDAVIHEIQRFADIIPMsLPHAVTRDTNF-RGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNG 357
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 193083180 451 KERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPThteprRKPELI 505
Cdd:cd20669  358 SFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQPL-----GAPEDI 407
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
311-499 1.74e-18

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


Pssm-ID: 410725  Cd Length: 438  Bit Score: 87.74  E-value: 1.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 311 KELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDR-------EPIEIEWDDLAQLPFLTM 383
Cdd:cd20632  209 DVLQDYDKAAHHFAFLWASVGNTIPATFWAMYYLLRHPEALAAVRDEIDHVLQSTgqelgpdFDIHLTREQLDSLVYLES 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 384 CIKESLRLHPPVPVIsRCCTQDFVLP---DGRV-IPKGivcliNIIGI-----HYNPTVWPDPEVYdpfRFDQ--ENIKE 452
Cdd:cd20632  289 AINESLRLSSASMNI-RVVQEDFTLKlesDGSVnLRKG-----DIVALypqslHMDPEIYEDPEVF---KFDRfvEDGKK 359
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193083180 453 RS---------PLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFR--ILPTHTEPR 499
Cdd:cd20632  360 KTtfykrgqklKYYLMPFGSGSSKCPGRFFAVNEIKQFLSLLLLYFDleLLEEQKPPG 417
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
255-511 6.29e-18

cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus P450 monooxygenase AurH which is uniquely capable of forming a homochiral tetrahydrofuran ring, a vital component of the polyketide antibiotic aureothin. AurH catalyzes an unprecedented tandem oxygenation process: first, it catalyzes an asymmetric hydroxylation of deoxyaureothin to yield (7R)-7-hydroxydeoxyaureothin as an intermediate; and second, it mediates another C-O bond formation that leads to O-heterocyclization. The AurH-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410664 [Multi-domain]  Cd Length: 382  Bit Score: 85.49  E-value: 6.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 255 RFRRACHLVHDFTDAVIQERRcTLPTqgiDDFLKNkaksktldfidvlLLSKDEDGKELSDEDIRAEADTFMFEGHDTTA 334
Cdd:cd11038  169 RIEAAVEELYDYADALIEARR-AEPG---DDLIST-------------LVAAEQDGDRLSDEELRNLIVALLFAGVDTTR 231
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 335 SGLSWVLYHLAKHPEyqeqcrqevqellkdrepieiEWDDLAQLPFLTM-CIKESLRLHPPVPVISRCCTQDFVLPDGRv 413
Cdd:cd11038  232 NQLGLAMLTFAEHPD---------------------QWRALREDPELAPaAVEEVLRWCPTTTWATREAVEDVEYNGVT- 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 414 IPKGIVCLINIIGIHYnptvwpDPEVYDPFRFDqenIKERSPLAFiPFSAGPRNCIGQAFAMAEMKVvlALTLLHFRIlp 493
Cdd:cd11038  290 IPAGTVVHLCSHAANR------DPRVFDADRFD---ITAKRAPHL-GFGGGVHHCLGAFLARAELAE--ALTVLARRL-- 355
                        250
                 ....*....|....*...
gi 193083180 494 thTEPRRKPELILRAEGG 511
Cdd:cd11038  356 --PTPAIAGEPTWLPDSG 371
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
311-516 8.25e-18

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 86.21  E-value: 8.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 311 KELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQellkdrepIEIEWDDLAQLPFLTMCIKESLR 390
Cdd:PLN02169 295 KPKKDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEIN--------TKFDNEDLEKLVYLHAALSESMR 366
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 391 LHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVW-PDPEVYDPFRFDQEN--IKERSPLAFIPFSAGPRN 467
Cdd:PLN02169 367 LYPPLPFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNggLRHEPSYKFMAFNSGPRT 446
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193083180 468 CIGQAFAMAEMKVVlALTLLH---FRILPTH-TEPrrKPELILRAEGGLWLRV 516
Cdd:PLN02169 447 CLGKHLALLQMKIV-ALEIIKnydFKVIEGHkIEA--IPSILLRMKHGLKVTV 496
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
143-493 8.72e-18

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 85.80  E-value: 8.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 143 KWSRHRRM--LTPAF-HFNILKPYMKI-FNKSVNIMHDKWqrlasegSARLDMFEHISLMTLDSLQKCVFSFEsncqekP 218
Cdd:PLN02987 121 KGNLHKKMhsLTMSFaNSSIIKDHLLLdIDRLIRFNLDSW-------SSRVLLMEEAKKITFELTVKQLMSFD------P 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 219 SEYIAAIlelsafvekRNQQILLHTDF----LYYLTPDGQRFRRACHLVHDFTDAVIQERRCTlptqgiddflKNKAKSK 294
Cdd:PLN02987 188 GEWTESL---------RKEYVLVIEGFfsvpLPLFSTTYRRAIQARTKVAEALTLVVMKRRKE----------EEEGAEK 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 295 TLDFIDVLLLSKDEdgkeLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQEL-LKDREPIEIEWD 373
Cdd:PLN02987 249 KKDMLAALLASDDG----FSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIrAMKSDSYSLEWS 324
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 374 DLAQLPFLTMCIKESLRLHPPVPVISRCCTQDfVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKER 453
Cdd:PLN02987 325 DYKSMPFTQCVVNETLRVANIIGGIFRRAMTD-IEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTV 403
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 193083180 454 SPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILP 493
Cdd:PLN02987 404 PSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSWVP 443
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
265-499 1.34e-17

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


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 85.13  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 265 DFTDAVIQERRCTL-PTQGIDDFlknkakskTLDFIDVLLLSKDEDGKELSDEDIR-AEADTFMfEGHDTTASGLSWVLY 342
Cdd:cd20663  185 ALLDELLTEHRTTWdPAQPPRDL--------TDAFLAEMEKAKGNPESSFNDENLRlVVADLFS-AGMVTTSTTLSWALL 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 343 HLAKHPEYQEQCRQEVQELL-KDREPieiEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCL 421
Cdd:cd20663  256 LMILHPDVQRRVQQEIDEVIgQVRRP---EMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDIEVQGFLIPKGTTLI 332
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193083180 422 INIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPR 499
Cdd:cd20663  333 TNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVPAGQPR 410
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
339-486 1.72e-17

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


Pssm-ID: 410728  Cd Length: 410  Bit Score: 84.67  E-value: 1.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 339 WVLYHLAKHPEYQEQCRQEVQELLKD--REPIEIEWDDLAQLPFLTMCIKESLRLHPPvPVISRCCTQDFVLPDgRVIPK 416
Cdd:cd20635  232 WTLAFILSHPSVYKKVMEEISSVLGKagKDKIKISEDDLKKMPYIKRCVLEAIRLRSP-GAITRKVVKPIKIKN-YTIPA 309
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193083180 417 GIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPL-AFIPFSAGPRNCIGQAFAMAEMKVVLALTL 486
Cdd:cd20635  310 GDMLMLSPYWAHRNPKYFPDPELFKPERWKKADLEKNVFLeGFVAFGGGRYQCPGRWFALMEIQMFVAMFL 380
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
269-508 3.14e-17

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 83.24  E-value: 3.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 269 AVIQERRCTLptqGIDDFLKnkaksktldfidvLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHP 348
Cdd:cd20630  171 EVIAERRQAP---VEDDLLT-------------TLLRAEEDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHP 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 349 EYQEQCRQEvQELLkdREPIE--IEWDDLAQLPFLtmcikeslrlhppvpvisRCCTQDFVLPdGRVIPKGIVCLINIIG 426
Cdd:cd20630  235 EALRKVKAE-PELL--RNALEevLRWDNFGKMGTA------------------RYATEDVELC-GVTIRKGQMVLLLLPS 292
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 427 IHYNPTVWPDPEVYDPfrfdqenikERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPRRKPELIL 506
Cdd:cd20630  293 ALRDEKVFSDPDRFDV---------RRDPNANIAFGYGPHFCIGAALARLELELAVSTLLRRFPEMELAEPPVFDPHPVL 363

                 ..
gi 193083180 507 RA 508
Cdd:cd20630  364 RA 365
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
252-496 5.33e-17

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


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 82.64  E-value: 5.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 252 DGQRFRRACHLVHDFTDAVIQERRctlpTQGIDDFLKnkaksktldfidvLLLSKDEDGKELSDEDIRAEADTFMFEGHD 331
Cdd:cd11035  142 DAEERAAAAQAVLDYLTPLIAERR----ANPGDDLIS-------------AILNAEIDGRPLTDDELLGLCFLLFLAGLD 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 332 TTASGLSWVLYHLAKHPEYQEQCRQEvqellKDREPIEIEwddlaqlpfltmcikESLRLHPPVPVIsRCCTQDFVLpDG 411
Cdd:cd11035  205 TVASALGFIFRHLARHPEDRRRLRED-----PELIPAAVE---------------ELLRRYPLVNVA-RIVTRDVEF-HG 262
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 412 RVIPKG--IVCLINIIGIhyNPTVWPDPEVYDPfrfdqenikERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLA--LTLL 487
Cdd:cd11035  263 VQLKAGdmVLLPLALANR--DPREFPDPDTVDF---------DRKPNRHLAFGAGPHRCLGSHLARLELRIALEewLKRI 331
                        250
                 ....*....|
gi 193083180 488 -HFRILPTHT 496
Cdd:cd11035  332 pDFRLAPGAQ 341
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
280-491 6.28e-17

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


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 82.92  E-value: 6.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 280 TQGIDDFLKNKAKS--KTLD------FIDVLLLSKDEDGK----ELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKH 347
Cdd:cd20668  177 LQGLEDFIAKKVEHnqRTLDpnsprdFIDSFLIRMQEEKKnpntEFYMKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKH 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 348 PEYQEQCRQEVQELL-KDREPieiEWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQD-----FVLPDG-RVIPkgiv 419
Cdd:cd20668  257 PEVEAKVHEEIDRVIgRNRQP---KFEDRAKMPYTEAVIHEIQRFGDVIPMgLARRVTKDtkfrdFFLPKGtEVFP---- 329
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193083180 420 clinIIG-IHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRI 491
Cdd:cd20668  330 ----MLGsVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRF 398
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
289-498 7.22e-17

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 83.20  E-value: 7.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 289 NKAKSKTLDFIDVLL-LSKDED-GKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDRE 366
Cdd:PLN03234 258 NRPKQETESFIDLLMqIYKDQPfSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKG 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 367 PIEIEwdDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHYNPTVWPD-PEVYDPFRF 445
Cdd:PLN03234 338 YVSEE--DIPNLPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERF 415
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 193083180 446 DQENIK---ERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFR-ILPTHTEP 498
Cdd:PLN03234 416 MKEHKGvdfKGQDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDwSLPKGIKP 472
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
283-493 8.20e-17

cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group includes CYP2C, and similar CYPs including mammalian CYP2E1, also called 4-nitrophenol 2-hydroxylase, as well as chicken CYP2H1 and CYP2H2. The CYP2C subfamily is composed of four human members (CYP2C8, CYP2C9, CYP2C18, CYP2C19) that metabolize approximately 20% of clinically used drugs, and all four exhibit genetic polymorphisms that results in toxicity or altered efficacy of some drugs in affected individuals. CYP2E1 participates in the metabolism of endogenous substrates, including acetone and fatty acids, and exogenous compounds such as anesthetics, ethanol, nicotine, acetaminophen, aspartame, and chlorzoxazone, among others. The CYP2C-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 82.69  E-value: 8.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 283 IDDFLKNKAKS--KTL------DFIDVLLLsKDEDGKELSDEDIRAE------ADTFmFEGHDTTASGLSWVLYHLAKHP 348
Cdd:cd20665  180 IKSYILEKVKEhqESLdvnnprDFIDCFLI-KMEQEKHNQQSEFTLEnlavtvTDLF-GAGTETTSTTLRYGLLLLLKHP 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 349 EYQEQCRQEVQELL-KDREPIeieWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIG 426
Cdd:cd20665  258 EVTAKVQEEIDRVIgRHRSPC---MQDRSHMPYTDAVIHEIQRYIDLVPNnLPHAVTCDTKF-RNYLIPKGTTVITSLTS 333
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193083180 427 IHYNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILP 493
Cdd:cd20665  334 VLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKS 400
PLN02500 PLN02500
cytochrome P450 90B1
313-490 1.61e-16

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 82.22  E-value: 1.61e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 313 LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELL---KDREPIEIEWDDLAQLPFLTMCIKESL 389
Cdd:PLN02500 275 LSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIArakKQSGESELNWEDYKKMEFTQCVINETL 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 390 RLHPPVPVISRCCTQDfVLPDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKERSPLA-------FIPFS 462
Cdd:PLN02500 355 RLGNVVRFLHRKALKD-VRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRGGSSGSssattnnFMPFG 433
                        170       180
                 ....*....|....*....|....*...
gi 193083180 463 AGPRNCIGQAFAMAEMKVVLALTLLHFR 490
Cdd:PLN02500 434 GGPRLCAGSELAKLEMAVFIHHLVLNFN 461
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
252-507 1.63e-16

cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces coelicolor CYP158A1 and CYP158A2, Streptomyces natalensis PimD (also known as CYP107E), Mycobacterium tuberculosis CYP121, and Micromonospora griseorubida MycG (also known as CYP107B). CYP158A1 and CYP158A2 catalyze an unusual oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments; CYP158A2 produces three isomers of biflaviolin and one triflaviolin while CYP158A1 produces only two isomers of biflaviolin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. CYP121 is essential for the viability of M. tuberculosis and is a novel drug target for the inhibition of mycobacterial growth. MycG catalyzes both hydroxylation and epoxidation reactions in the biosynthesis of the 16-membered ring macrolide antibiotic mycinamicin II. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 81.46  E-value: 1.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 252 DGQRFRRACHLVHDFTDAVIQERRctlptQGIDDF-------LKNKAKSKTLDFIDVLLLSKDEDGKeLSDEDIRAEADT 324
Cdd:cd11031  140 DRERFRAWSDALLSTSALTPEEAE-----AARQELrgymaelVAARRAEPGDDLLSALVAARDDDDR-LSEEELVTLAVG 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 325 FMFEGHDTTASGLSWVLYHLAKHPEyqeqcrqEVQELLKDREPIE--IEwddlaqlpfltmcikESLRLHPPVP--VISR 400
Cdd:cd11031  214 LLVAGHETTASQIGNGVLLLLRHPE-------QLARLRADPELVPaaVE---------------ELLRYIPLGAggGFPR 271
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 401 CCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPfrfdqenikERSPLAFIPFSAGPRNCIGQAFAMAEMKV 480
Cdd:cd11031  272 YATEDVEL-GGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDL---------DREPNPHLAFGHGPHHCLGAPLARLELQV 341
                        250       260       270
                 ....*....|....*....|....*....|...
gi 193083180 481 vlALTLLhFRILPT------HTEPRRKPELILR 507
Cdd:cd11031  342 --ALGAL-LRRLPGlrlavpEEELRWREGLLTR 371
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
329-516 2.34e-16

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 80.71  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 329 GHDTTASGLSWVLYHLAKHPEyqeqcrqevqellkdrepieiEWDDLAQLPFL-TMCIKESLRLHPPVPVISRCCTQDFV 407
Cdd:cd11037  214 GLDTTISAIGNALWLLARHPD---------------------QWERLRADPSLaPNAFEEAVRLESPVQTFSRTTTRDTE 272
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 408 LpDGRVIPKG--IVCLI---NiigihYNPTVWPDPEVYDpfrfdqenIkERSPLAFIPFSAGPRNCIGQAFAMAEMKVVL 482
Cdd:cd11037  273 L-AGVTIPAGsrVLVFLgsaN-----RDPRKWDDPDRFD--------I-TRNPSGHVGFGHGVHACVGQHLARLEGEALL 337
                        170       180       190
                 ....*....|....*....|....*....|....
gi 193083180 483 ALTLLHFRILPTHTEPRRKPELILRAEGGLWLRV 516
Cdd:cd11037  338 TALARRVDRIELAGPPVRALNNTLRGLASLPVRI 371
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
281-493 3.73e-16

cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and amphibians. CYP2K6 from zebrafish has been shown to catalyze the conversion of aflatoxin B1 (AFB1) to its cytotoxic derivative AFB1 exo-8,9-epoxide, while its ortholog in rainbow trout CYP2K1 is also capable of oxidizing lauric acid. In birds, CYP2K is one of the largest CYP2 subfamilies. The CYP2K subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 80.62  E-value: 3.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 281 QGIDDFLKNKAKSKTLDFIDVLLLSKDEDgKELSDEDIRAEADTFMF-----EGHDTTASGLSWVLYHLAKHPEYQEQCR 355
Cdd:cd20664  185 ETFMKHLDVLEPNDQRGFIDAFLVKQQEE-EESSDSFFHDDNLTCSVgnlfgAGTDTTGTTLRWGLLLMMKYPEIQKKVQ 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 356 QEVQELLKDREPieiEWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDfVLPDGRVIPKGIVCLINIIGIHYNPTVW 434
Cdd:cd20664  264 EEIDRVIGSRQP---QVEHRKNMPYTDAVIHEIQRFANIVPMnLPHATTRD-VTFRGYFIPKGTYVIPLLTSVLQDKTEW 339
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193083180 435 PDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQafAMAEMKVVLALTLL--HFRILP 493
Cdd:cd20664  340 EKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGE--TLAKMELFLFFTSLlqRFRFQP 398
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
283-487 8.28e-16

cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of rats and rabbits and may have important functions for the olfactory chemosensory system. It is involved in the metabolism of sex steroids and xenobiotic compounds. In cynomolgus monkeys, CYP2G2 is a functional drug-metabolizing enzyme in nasal mucosa. In humans, two different CYP2G genes, CYP2GP1 and CYP2GP2, are pseudogenes because of loss-of-function deletions/mutations. The CYP2G subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 79.58  E-value: 8.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 283 IDDFLKNKAK--------SKTLDFIDVLLLSKDEDGKELSDE----DIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEY 350
Cdd:cd20670  180 LKDFIASRVKineasldpQNPRDFIDCFLIKMHQDKNNPHTEfnlkNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 351 QEQCRQEVQELL-KDREPieiEWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIH 428
Cdd:cd20670  260 EAKIHEEINQVIgPHRLP---SVDDRVKMPYTDAVIHEIQRLTDIVPLgVPHNVIRDTQF-RGYLLPKGTDVFPLLGSVL 335
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 193083180 429 YNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIGQafAMAEMKVVLALTLL 487
Cdd:cd20670  336 KDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGE--AMARMELFLYFTSI 392
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
339-491 1.10e-15

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 79.34  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 339 WVLYHLAKHPEYQEQCRQEVQELLK--------DREPIEIEWDDLAQLPFLTMCIKESLRLHPPVPVIsRCCTQDF--VL 408
Cdd:cd20631  249 WSLFYLLRCPEAMKAATKEVKRTLEktgqkvsdGGNPIVLTREQLDDMPVLGSIIKEALRLSSASLNI-RVAKEDFtlHL 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 409 PDGRV--IPKG-IVCLINIIgIHYNPTVWPDPEVYDPFRFDQENIKERSPLA---------FIPFSAGPRNCIGQAFAMA 476
Cdd:cd20631  328 DSGESyaIRKDdIIALYPQL-LHLDPEIYEDPLTFKYDRYLDENGKEKTTFYkngrklkyyYMPFGSGTSKCPGRFFAIN 406
                        170
                 ....*....|....*
gi 193083180 477 EMKVVLALTLLHFRI 491
Cdd:cd20631  407 EIKQFLSLMLCYFDM 421
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
297-483 1.65e-15

P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome P450cin (P450cin, also called CYP176A1) and similar proteins. P450cin is a bacterial P450 enzyme that catalyzes the enantiospecific hydroxylation of 1,8-cineole to (1R)-6beta-hydroxycineole; its natural reduction-oxidation partner is cindoxin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 78.15  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLLSKdEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEyqeqcrqEVQELLkdrepieiewDDLA 376
Cdd:cd11034  171 DLISRLIEGE-IDGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPE-------DRRRLI----------ADPS 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 377 QLPfltMCIKESLRLHPPVPVISRCCTQDFVLPDGRVIPKGIVCLINIIGIHynptvwpDPEVY-DPFRFDQenikERSP 455
Cdd:cd11034  233 LIP---NAVEEFLRFYSPVAGLARTVTQEVEVGGCRLKPGDRVLLAFASANR-------DEEKFeDPDRIDI----DRTP 298
                        170       180
                 ....*....|....*....|....*...
gi 193083180 456 LAFIPFSAGPRNCIGQAFAMAEMKVVLA 483
Cdd:cd11034  299 NRHLAFGSGVHRCLGSHLARVEARVALT 326
PLN00168 PLN00168
Cytochrome P450; Provisional
271-475 1.70e-15

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 79.22  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 271 IQERRCTLPTQGIDDFLKNKAKSKTLDFIDVLLLSK--DEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHP 348
Cdd:PLN00168 258 IDARREYKNHLGQGGEPPKKETTFEHSYVDTLLDIRlpEDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNP 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 349 EYQEQCRQEVQELLKDREPiEIEWDDLAQLPFLTMCIKESLRLHPPVpvisrcctqDFVLPD---------GRVIPKGIV 419
Cdd:PLN00168 338 SIQSKLHDEIKAKTGDDQE-EVSEEDVHKMPYLKAVVLEGLRKHPPA---------HFVLPHkaaedmevgGYLIPKGAT 407
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193083180 420 CLINIIGIHYNPTVWPDPEVYDPFRF----DQE--NIKERSPLAFIPFSAGPRNCIGQAFAM 475
Cdd:PLN00168 408 VNFMVAEMGRDEREWERPMEFVPERFlaggDGEgvDVTGSREIRMMPFGVGRRICAGLGIAM 469
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
297-514 3.22e-15

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


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 77.21  E-value: 3.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLLSKDEDGKeLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEyqeqcrqevqellkdrepieiEWDDLA 376
Cdd:cd20625  182 DLISALVAAEEDGDR-LSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPE---------------------QLALLR 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 377 QLPFLT-MCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKG--IVCLI---NiigihYNPTVWPDPEVYDPFRFDQENI 450
Cdd:cd20625  240 ADPELIpAAVEELLRYDSPVQLTARVALEDVEI-GGQTIPAGdrVLLLLgaaN-----RDPAVFPDPDRFDITRAPNRHL 313
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193083180 451 kersplafiPFSAGPRNCIGQAFAMAEMKVVLAlTLLH-FRILPTHT-EPRRKPELILRAEGGLWL 514
Cdd:cd20625  314 ---------AFGAGIHFCLGAPLARLEAEIALR-ALLRrFPDLRLLAgEPEWRPSLVLRGLRSLPV 369
PLN02971 PLN02971
tryptophan N-hydroxylase
257-499 5.75e-15

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 77.39  E-value: 5.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 257 RRACHLVHDFTDAVIQERRctlptqgidDFLKNKAKSKTLDFIDVLLLSKDEDGKEL-SDEDIRAEADTFMFEGHDTTAS 335
Cdd:PLN02971 275 RESSAIMDKYHDPIIDERI---------KMWREGKRTQIEDFLDIFISIKDEAGQPLlTADEIKPTIKELVMAAPDNPSN 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 336 GLSWVLYHLAKHPEYQEQCRQEVQELL-KDREpieIEWDDLAQLPFLTMCIKESLRLHPPVPV-ISRCCTQDFVLPdGRV 413
Cdd:PLN02971 346 AVEWAMAEMINKPEILHKAMEEIDRVVgKERF---VQESDIPKLNYVKAIIREAFRLHPVAAFnLPHVALSDTTVA-GYH 421
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 414 IPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIK---ERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFR 490
Cdd:PLN02971 422 IPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFK 501

                 ....*....
gi 193083180 491 ILPTHTEPR 499
Cdd:PLN02971 502 WKLAGSETR 510
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
302-500 8.98e-15

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


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 76.03  E-value: 8.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 302 LLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEyqeqcrqevQ-ELLKdrepieiewDDLAQLPf 380
Cdd:cd11033  194 VLANAEVDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPD---------QwERLR---------ADPSLLP- 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 381 lTMcIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKG-IVCLINIIGIHynptvwpDPEVY-DPFRFDqenIkERSPLAF 458
Cdd:cd11033  255 -TA-VEEILRWASPVIHFRRTATRDTEL-GGQRIRAGdKVVLWYASANR-------DEEVFdDPDRFD---I-TRSPNPH 320
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 193083180 459 IPFSAGPRNCIGQAFAMAEMKVVLALTLLHF-RILPThTEPRR 500
Cdd:cd11033  321 LAFGGGPHFCLGAHLARLELRVLFEELLDRVpDIELA-GEPER 362
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
222-515 1.62e-13

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


Pssm-ID: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 72.18  E-value: 1.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 222 IAAILELSAFVEKRNQQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRctlpTQGIDDFlknkaksktldfIDV 301
Cdd:cd11029  133 ITVICELLGVPEEDRDRFRRWSDALVDTDPPPEEAAAALRELVDYLAELVARKR----AEPGDDL------------LSA 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 302 LLLSKDEDGKeLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPeyqEQCrqevqELLKDRepiEIEWDDLaqlpfl 381
Cdd:cd11029  197 LVAARDEGDR-LSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHP---DQL-----ALLRAD---PELWPAA------ 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 382 tmcIKESLRLHPPVPV-ISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRfdqeniKERSPLAfip 460
Cdd:cd11029  259 ---VEELLRYDGPVALaTLRFATEDVEV-GGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR------DANGHLA--- 325
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193083180 461 FSAGPRNCIGQAFAMAEMKVvlALTLLhFRILP------THTEPRRKPELILRAEGGLWLR 515
Cdd:cd11029  326 FGHGIHYCLGAPLARLEAEI--ALGAL-LTRFPdlrlavPPDELRWRPSFLLRGLRALPVR 383
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
270-516 3.12e-13

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 70.85  E-value: 3.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 270 VIQERRcTLPTQGIDDflknkaksktldfIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPE 349
Cdd:cd11079  150 LLADRR-AAPRDADDD-------------VTARLLRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYLARHPE 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 350 YQEQCRQEVQELlkdrePIEIEwddlaqlpfltmcikESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHY 429
Cdd:cd11079  216 LQARLRANPALL-----PAAID---------------EILRLDDPFVANRRITTRDVEL-GGRTIPAGSRVTLNWASANR 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 430 NPTVWPDPEVYDPfrfdqenikERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHfrILPTHTEPRRKPELILRAE 509
Cdd:cd11079  275 DERVFGDPDEFDP---------DRHAADNLVYGRGIHVCPGAPLARLELRILLEELLAQ--TEAITLAAGGPPERATYPV 343

                 ....*..
gi 193083180 510 GGlWLRV 516
Cdd:cd11079  344 GG-YASV 349
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
270-490 5.66e-13

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 70.92  E-value: 5.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 270 VIQERRCTLPTQGIDDFLKNKaksktlDFIDVLLlskdEDGKE-LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHP 348
Cdd:PLN03141 213 IIEEKRRAMKNKEEDETGIPK------DVVDVLL----RDGSDeLTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCP 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 349 EYQEQCRQEVQEL--LKDREPIEIEWDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDfVLPDGRVIPKGIVCLINIIG 426
Cdd:PLN03141 283 VALQQLTEENMKLkrLKADTGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKD-VEIKGYLIPKGWCVLAYFRS 361
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193083180 427 IHYNPTVWPDPEVYDPFRFDQENIKERSplaFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFR 490
Cdd:PLN03141 362 VHLDEENYDNPYQFNPWRWQEKDMNNSS---FTPFGGGQRLCPGLDLARLEASIFLHHLVTRFR 422
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
298-493 5.68e-12

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


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 67.54  E-value: 5.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 298 FIDVLLLSKdedgkeLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDrEPIEIEwdDLAQ 377
Cdd:cd20627  189 FIDSLLQGN------LSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQVLGK-GPITLE--KIEQ 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 378 LPFLTMCIKESLRLHPPVPVISRccTQDFvlpDGRV----IPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQENIKER 453
Cdd:cd20627  260 LRYCQQVLCETVRTAKLTPVSAR--LQEL---EGKVdqhiIPKETLVLYALGVVLQDNTTWPLPYRFDPDRFDDESVMKS 334
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 193083180 454 spLAFIPFSaGPRNCIGQAFAMAEMKVVLALTLLHFRILP 493
Cdd:cd20627  335 --FSLLGFS-GSQECPELRFAYMVATVLLSVLVRKLRLLP 371
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
303-490 7.56e-12

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 66.85  E-value: 7.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 303 LLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQeqcrqevQELLKDRepieiewDDLAQLpflt 382
Cdd:cd11032  184 LVEAEVDGERLTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVA-------ARLRADP-------SLIPGA---- 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 383 mcIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPfrfdqenikERSPLAFIPFS 462
Cdd:cd11032  246 --IEEVLRYRPPVQRTARVTTEDVEL-GGVTIPAGQLVIAWLASANRDERQFEDPDTFDI---------DRNPNPHLSFG 313
                        170       180
                 ....*....|....*....|....*...
gi 193083180 463 AGPRNCIGQAFAMAEMKVVLALTLLHFR 490
Cdd:cd11032  314 HGIHFCLGAPLARLEARIALEALLDRFP 341
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
145-494 1.03e-11

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 66.39  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 145 SRHRRMLTPAF---HFNILKPYM-KIFNKSVNIMhdkwqrLASEGSArlDMFEHISLMTldslqkcvfsfesncqekPSE 220
Cdd:cd11030   78 TRLRRMLAPEFtvrRVRALRPRIqEIVDELLDAM------EAAGPPA--DLVEAFALPV------------------PSL 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 221 YIAAIL----ELSAFVEKRNQQILLHTDflyyltpDGQRFRRACHLVHDFTDAVIQERRcTLPtqgiDDflknkaksktl 296
Cdd:cd11030  132 VICELLgvpyEDREFFQRRSARLLDLSS-------TAEEAAAAGAELRAYLDELVARKR-REP----GD----------- 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 297 DFIDVLLLSKDEDGkELSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEyqeqcrqevQ-ELLKDrepieiewdDL 375
Cdd:cd11030  189 DLLSRLVAEHGAPG-ELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPE---------QlAALRA---------DP 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 376 AQLPfltMCIKESLRLHPPVP-VISRCCTQDFVLpDGRVIPKG--IVCLINIIgihyN--PTVWPDPEVYDPFRfdqeni 450
Cdd:cd11030  250 SLVP---GAVEELLRYLSIVQdGLPRVATEDVEI-GGVTIRAGegVIVSLPAA----NrdPAVFPDPDRLDITR------ 315
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 193083180 451 KERSPLAFipfSAGPRNCIGQAFAMAEMKVVLAlTLlhFRILPT 494
Cdd:cd11030  316 PARRHLAF---GHGVHQCLGQNLARLELEIALP-TL--FRRFPG 353
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
237-491 3.21e-11

cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) consists of only one functional member CYP2B6, which shows broad substrate specificity and plays a key role in the metabolism of many clinical drugs, environmental toxins, and endogenous compounds. Rodents have multiple functional CYP2B proteins; mouse subfamily members include CYP2B9, 2B10, 2B13, 2B19, and 2B23. CYP2B enzymes are highly inducible by chemicals that interact with the constitutive androstane receptor (CAR) and/or pregnane X receptor (PXR), such as rifampicin and phenobarbital. The CYP2B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 65.18  E-value: 3.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 237 QQILLHTDFLYYLTPDGQRFRRACHLVHDFTDAVIQERRCTLPtqgiddflknkaKSKTLDFIDVLLL----SKDEDGKE 312
Cdd:cd20672  154 QVFELFSGFLKYFPGAHRQIYKNLQEILDYIGHSVEKHRATLD------------PSAPRDFIDTYLLrmekEKSNHHTE 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 313 LSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQEQCRQEVQELLKDREPIEIewDDLAQLPFLTMCIKESLRLH 392
Cdd:cd20672  222 FHHQNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTL--DDRAKMPYTDAVIHEIQRFS 299
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 393 PPVPV-ISRCCTQDFVLpDGRVIPKGI-VCLINIIGIHyNPTVWPDPEVYDPFRFDQENIKERSPLAFIPFSAGPRNCIG 470
Cdd:cd20672  300 DLIPIgVPHRVTKDTLF-RGYLLPKNTeVYPILSSALH-DPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLG 377
                        250       260
                 ....*....|....*....|.
gi 193083180 471 QAFAMAEMKVVLALTLLHFRI 491
Cdd:cd20672  378 EGIARNELFLFFTTILQNFSV 398
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
344-502 4.69e-11

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


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 64.40  E-value: 4.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 344 LAKHPEYQEQCRQEVQELlkdrepieiewDDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLIN 423
Cdd:cd20624  218 LAAHPEQAARAREEAAVP-----------PGPLARPYLRACVLDAVRLWPTTPAVLRESTEDTVW-GGRTVPAGTGFLIF 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 424 IIGIHYNPTVWP-----DPEVYdpfrFDQENIKERsplAFIPFSAGPRNCIGQAFAMAEMKVVLALTLLHFRILPTHtEP 498
Cdd:cd20624  286 APFFHRDDEALPfadrfVPEIW----LDGRAQPDE---GLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLE-SP 357

                 ....
gi 193083180 499 RRKP 502
Cdd:cd20624  358 RSGP 361
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
340-489 1.49e-10

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


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 63.05  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 340 VLYHLAKH-PEYQEQCRQEVQELLKDREPIEIEwdDLAQLPFLTMCIKESLRLHPPVPVISRCCTQDFVLP--DGR-VIP 415
Cdd:cd11071  248 LLARLGLAgEELHARLAEEIRSALGSEGGLTLA--ALEKMPLLKSVVYETLRLHPPVPLQYGRARKDFVIEshDASyKIK 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 416 KGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQEnikERSPLAFIPFSAGP---------RNCIGQAFAMAEMKVVLALTL 486
Cdd:cd11071  326 KGELLVGYQPLATRDPKVFDNPDEFVPDRFMGE---EGKLLKHLIWSNGPeteeptpdnKQCPGKDLVVLLARLFVAELF 402

                 ...
gi 193083180 487 LHF 489
Cdd:cd11071  403 LRY 405
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
337-493 4.08e-10

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


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 61.78  E-value: 4.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 337 LSWVLYHLAKHPEYQEQcrqevqelLKDREPIEIEWddLAQlpfltmcikESLRLHPPVPVISRCCTQDFVLpDGRVIPK 416
Cdd:cd11067  240 VTFAALALHEHPEWRER--------LRSGDEDYAEA--FVQ---------EVRRFYPFFPFVGARARRDFEW-QGYRFPK 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 417 GIVCLINIIGIHYNPTVWPDPEVYDPFRFDQeniKERSPLAFIP-----FSAGPRnCIGQAFAMAEMKVVLA-LTLLHFR 490
Cdd:cd11067  300 GQRVLLDLYGTNHDPRLWEDPDRFRPERFLG---WEGDPFDFIPqgggdHATGHR-CPGEWITIALMKEALRlLARRDYY 375

                 ...
gi 193083180 491 ILP 493
Cdd:cd11067  376 DVP 378
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
339-489 6.26e-10

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 61.31  E-value: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 339 WVLYHLAKHPEYQEQCRQEVQELLKDREP-----IEIEWDDLAQLPFLTMCIKESLRLhPPVPVISRCCTQDFVLP--DG 411
Cdd:cd20634  243 WLLLFLLKHPEAMAAVRGEIQRIKHQRGQpvsqtLTINQELLDNTPVFDSVLSETLRL-TAAPFITREVLQDMKLRlaDG 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 412 RV--IPKG-IVCLINIIGIHYNPTVWPDPEVYDPFRF---DQENIKE------RSPLAFIPFSAGPRNCIGQAFAMAEMK 479
Cdd:cd20634  322 QEynLRRGdRLCLFPFLSPQMDPEIHQEPEVFKYDRFlnaDGTEKKDfykngkRLKYYNMPWGAGDNVCIGRHFAVNSIK 401
                        170
                 ....*....|
gi 193083180 480 VVLALTLLHF 489
Cdd:cd20634  402 QFVFLILTHF 411
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
387-484 2.46e-08

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 55.81  E-value: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 387 ESLRLHPPVPVISRCCTQDFVLPDG----RVIPKGIVCLINIIGIHYNPTVWPDPEVYDPfrfdqenikERSPLAFIPFS 462
Cdd:cd20612  246 EALRLNPIAPGLYRRATTDTTVADGggrtVSIKAGDRVFVSLASAMRDPRAFPDPERFRL---------DRPLESYIHFG 316
                         90       100
                 ....*....|....*....|....*.
gi 193083180 463 AGPRNCIGQAFA---MAEM-KVVLAL 484
Cdd:cd20612  317 HGPHQCLGEEIAraaLTEMlRVVLRL 342
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
353-498 4.20e-08

cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a putative cytochrome P450 of unknown function. 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: 410719  Cd Length: 381  Bit Score: 55.49  E-value: 4.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 353 QCRQEVQELLKDREPIEIEWDDLaqlpfltmcIKESLRLHPPVPVISRCctqdfVLPDGrvIPKGIVCLINIIGIHYNPT 432
Cdd:cd20626  239 EWREANADFAKSATKDGISAKNL---------VKEALRLYPPTRRIYRA-----FQRPG--SSKPEIIAADIEACHRSES 302
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 433 VW-PDPEVYDPFRFDqeNIKERSPLAFIPFSAGPRNCIGQA-FA--MAEMkVVLALtllhFRILPTHTEP 498
Cdd:cd20626  303 IWgPDALEFNPSRWS--KLTPTQKEAFLPFGSGPFRCPAKPvFGprMIAL-LVGAL----LDALGDEWEL 365
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
385-500 3.60e-06

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 49.03  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193083180 385 IKESLRLHPPVPVISRCCTQDFVLpDGRVIPKGIVCLINIIGIHYNPTVWPDPEVYDPFRFDQenikeRSPlafiPFSAG 464
Cdd:cd11036  225 VAETLRYDPPVRLERRFAAEDLEL-AGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGRPTA-----RSA----HFGLG 294
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 193083180 465 PRNCIGQAFAMAEMKVVLALTLLHFRILPTHTEPRR 500
Cdd:cd11036  295 RHACLGAALARAAAAAALRALAARFPGLRAAGPVVR 330
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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