NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720412152|ref|XP_030109981|]
View 

cytochrome P450 3A13 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
67-492 0e+00

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: 818.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGRQPVLAITDPDIIKTVLVKECYSTFTNRRRFGPVGILKKAISISENEEWKRIRALLSPTFTSGRLKEMF 146
Cdd:cd20650     1 KYGKVWGIYDGRQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 147 PIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLKFDIFDPLFLSVTLF 226
Cdd:cd20650    81 PIIAQYGDVLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLKFDFLDPLFLSITVF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 227 PFLTPVFDALNVSLFPRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSQNYKTKESHKALSDVEIVAQSVIFIFAG 306
Cdd:cd20650   161 PFLTPILEKLNISVFPKDVTNFFYKSVKKIKESRLDSTQKHRVDFLQLMIDSQNSKETESHKALSDLEILAQSIIFIFAG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 307 YETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGL 386
Cdd:cd20650   241 YETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEINGV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 387 FIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQ 466
Cdd:cd20650   321 FIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFK 400
                         410       420
                  ....*....|....*....|....*.
gi 1720412152 467 PCKETEIPLKLSKQGLLQPENPLLLK 492
Cdd:cd20650   401 PCKETQIPLKLSLQGLLQPEKPIVLK 426
 
Name Accession Description Interval E-value
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
67-492 0e+00

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: 818.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGRQPVLAITDPDIIKTVLVKECYSTFTNRRRFGPVGILKKAISISENEEWKRIRALLSPTFTSGRLKEMF 146
Cdd:cd20650     1 KYGKVWGIYDGRQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 147 PIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLKFDIFDPLFLSVTLF 226
Cdd:cd20650    81 PIIAQYGDVLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLKFDFLDPLFLSITVF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 227 PFLTPVFDALNVSLFPRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSQNYKTKESHKALSDVEIVAQSVIFIFAG 306
Cdd:cd20650   161 PFLTPILEKLNISVFPKDVTNFFYKSVKKIKESRLDSTQKHRVDFLQLMIDSQNSKETESHKALSDLEILAQSIIFIFAG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 307 YETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGL 386
Cdd:cd20650   241 YETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEINGV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 387 FIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQ 466
Cdd:cd20650   321 FIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFK 400
                         410       420
                  ....*....|....*....|....*.
gi 1720412152 467 PCKETEIPLKLSKQGLLQPENPLLLK 492
Cdd:cd20650   401 PCKETQIPLKLSLQGLLQPEKPIVLK 426
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
39-493 5.83e-149

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: 434.01  E-value: 5.83e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  39 PGPKPLPFLGTIL--AYQKGFWECDIQCHKKYGKMWGLYDGRQPVLAITDPDIIKTVLVKECYSTFTNRRRFG----PVG 112
Cdd:pfam00067   2 PGPPPLPLFGNLLqlGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWfatsRGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 113 ILKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVN 192
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 193 IDSLNNPQDP----FVEKIKKLLKFDIFDPLFLSVTLFPFLTPVFDAL-NVSLFPRDVISFFttsVERMKENRMKEKEKQ 267
Cdd:pfam00067 162 FGSLEDPKFLelvkAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLkRARKKIKDLLDKL---IEERRETLDSAKKSP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 268 RvDFLQLMINSqnyKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATY 347
Cdd:pfam00067 239 R-DFLDALLLA---KEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 348 DTLLQMEYLDMVVNETLRLYPIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDS 426
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKF 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412152 427 INPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEIPLKLSKQGLLQPENPLLLKV 493
Cdd:pfam00067 395 RKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
67-463 9.83e-68

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: 222.85  E-value: 9.83e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGRQPVLAITDPDIIKTVLVKecYSTFTNRRR----FGPVGILKKAISISENEEWKRIRALLSPTFTSGRL 142
Cdd:COG2124    30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRD--PRTFSSDGGlpevLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 143 KEMFPIINQFTDVLVRNMRQGlGEGkptsmkDIFGAYS---MDVITATSFGVNIDSlnnpQDPFVEkikkllkfdifdpl 219
Cdd:COG2124   108 AALRPRIREIADELLDRLAAR-GPV------DLVEEFArplPVIVICELLGVPEED----RDRLRR-------------- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 220 fLSVTLFPFLTPVFDALNVSLFP--RDVISFFTTSVERMKENRmkekekqRVDFLQLMINSQnyktkESHKALSDVEIVA 297
Cdd:COG2124   163 -WSDALLDALGPLPPERRRRARRarAELDAYLRELIAERRAEP-------GDDLLSALLAAR-----DDGERLSDEELRD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 298 QSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIdaalpnkapatydtllqmEYLDMVVNETLRLYPIAGRLERVC 377
Cdd:COG2124   230 ELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTA 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 378 KTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERfskknqdsiNPYMYLPFGSGPRNCIGMRFALINMKVALV 457
Cdd:COG2124   292 TEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCLGAALARLEARIALA 362

                  ....*.
gi 1720412152 458 RVLQNF 463
Cdd:COG2124   363 TLLRRF 368
PLN02290 PLN02290
cytokinin trans-hydroxylase
32-463 1.50e-48

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 175.00  E-value: 1.50e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  32 IFKKLGIPGPKPLPFLGTI-----LAYQKGFWECDIQCH--------------KKYGKMWGLYDGRQPVLAITDPDIIKT 92
Cdd:PLN02290   38 IMERQGVRGPKPRPLTGNIldvsaLVSQSTSKDMDSIHHdivgrllphyvawsKQYGKRFIYWNGTEPRLCLTETELIKE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  93 VLVKecYSTFTNR---RRFGPVGILKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGEGKp 169
Cdd:PLN02290  118 LLTK--YNTVTGKswlQQQGTKHFIGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESGQ- 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 170 TSMKdiFGAY----SMDVITATSFGVNIDslnnpqdpfveKIKKLlkFDIFDPL------------FLSVTLFPfltpvf 233
Cdd:PLN02290  195 TEVE--IGEYmtrlTADIISRTEFDSSYE-----------KGKQI--FHLLTVLqrlcaqatrhlcFPGSRFFP------ 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 234 dalnvSLFPRDVISFfTTSVER-MKENRMKEKEKQRV--------DFLQLMINSQNyKTKESHKALSDVEIVAQSVIFIF 304
Cdd:PLN02290  254 -----SKYNREIKSL-KGEVERlLMEIIQSRRDCVEIgrsssygdDLLGMLLNEME-KKRSNGFNLNLQLIMDECKTFFF 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 305 AGYETTSSALSFALYLLAIHPDVQKKLQDEIdAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEIN 384
Cdd:PLN02290  327 AGHETTALLLTWTLMLLASNPTWQDKVRAEV-AEVCGGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 385 GLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQDSINPYMylPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:PLN02290  406 DLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHFI--PFAAGPRNCIGQAFAMMEAKIILAMLISKF 483
 
Name Accession Description Interval E-value
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
67-492 0e+00

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: 818.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGRQPVLAITDPDIIKTVLVKECYSTFTNRRRFGPVGILKKAISISENEEWKRIRALLSPTFTSGRLKEMF 146
Cdd:cd20650     1 KYGKVWGIYDGRQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 147 PIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLKFDIFDPLFLSVTLF 226
Cdd:cd20650    81 PIIAQYGDVLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLKFDFLDPLFLSITVF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 227 PFLTPVFDALNVSLFPRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSQNYKTKESHKALSDVEIVAQSVIFIFAG 306
Cdd:cd20650   161 PFLTPILEKLNISVFPKDVTNFFYKSVKKIKESRLDSTQKHRVDFLQLMIDSQNSKETESHKALSDLEILAQSIIFIFAG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 307 YETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGL 386
Cdd:cd20650   241 YETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEINGV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 387 FIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQ 466
Cdd:cd20650   321 FIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFK 400
                         410       420
                  ....*....|....*....|....*.
gi 1720412152 467 PCKETEIPLKLSKQGLLQPENPLLLK 492
Cdd:cd20650   401 PCKETQIPLKLSLQGLLQPEKPIVLK 426
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
67-489 0e+00

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: 567.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGRQPVLAITDPDIIKTVLVKEcYSTFTNRRRFGPVGI-LKKAISISENEEWKRIRALLSPTFTSGRLKEM 145
Cdd:cd11055     1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKE-FSNFTNRPLFILLDEpFDSSLLFLKGERWKRLRTTLSPTFSSGKLKLM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 146 FPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLKFDIFDPLFLSVTL 225
Cdd:cd11055    80 VPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKAAKKIFRNSIIRLFLLLLLF 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 226 FPFLTPVFdaLNVSLFPRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSQNYKTKESHKALSDVEIVAQSVIFIFA 305
Cdd:cd11055   160 PLRLFLFL--LFPFVFGFKSFSFLEDVVKKIIEQRRKNKSSRRKDLLQLMLDAQDSDEDVSKKKLTDDEIVAQSFIFLLA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 306 GYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEING 385
Cdd:cd11055   238 GYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFISRECKEDCTING 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 386 LFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTV 465
Cdd:cd11055   318 VFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRF 397
                         410       420
                  ....*....|....*....|....
gi 1720412152 466 QPCKETEIPLKLSKQGLLQPENPL 489
Cdd:cd11055   398 VPCKETEIPLKLVGGATLSPKNGI 421
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
73-489 5.95e-159

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: 458.16  E-value: 5.95e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  73 GLYDGRQPVLAITDPDIIKTVLVKEcYSTFTNRRRFGPVGI--LKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIIN 150
Cdd:cd11056     7 GIYLFRRPALLVRDPELIKQILVKD-FAHFHDRGLYSDEKDdpLSANLFSLDGEKWKELRQKLTPAFTSGKLKNMFPLMV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 151 QFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLKFDIFDPLFLsvTLFPFLT 230
Cdd:cd11056    86 EVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGLDANSLNDPENEFREMGRRLFEPSRLRGLKF--MLLFFFP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 231 PVFDALNVSLFPRDVISFFTTSVERMKENRmKEKEKQRVDFLQLMI---NSQNYKTKESHKALSDVEIVAQSVIFIFAGY 307
Cdd:cd11056   164 KLARLLRLKFFPKEVEDFFRKLVRDTIEYR-EKNNIVRNDFIDLLLelkKKGKIEDDKSEKELTDEELAAQAFVFFLAGF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 308 ETTSSALSFALYLLAIHPDVQKKLQDEIDAALP-NKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEING- 385
Cdd:cd11056   243 ETSSSTLSFALYELAKNPEIQEKLREEIDEVLEkHGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGt 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 386 -LFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFT 464
Cdd:cd11056   323 dVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFR 402
                         410       420
                  ....*....|....*....|....*.
gi 1720412152 465 VQPCKETEIPLKLSKQG-LLQPENPL 489
Cdd:cd11056   403 VEPSSKTKIPLKLSPKSfVLSPKGGI 428
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
39-493 5.83e-149

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: 434.01  E-value: 5.83e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  39 PGPKPLPFLGTIL--AYQKGFWECDIQCHKKYGKMWGLYDGRQPVLAITDPDIIKTVLVKECYSTFTNRRRFG----PVG 112
Cdd:pfam00067   2 PGPPPLPLFGNLLqlGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWfatsRGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 113 ILKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVN 192
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 193 IDSLNNPQDP----FVEKIKKLLKFDIFDPLFLSVTLFPFLTPVFDAL-NVSLFPRDVISFFttsVERMKENRMKEKEKQ 267
Cdd:pfam00067 162 FGSLEDPKFLelvkAVQELSSLLSSPSPQLLDLFPILKYFPGPHGRKLkRARKKIKDLLDKL---IEERRETLDSAKKSP 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 268 RvDFLQLMINSqnyKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATY 347
Cdd:pfam00067 239 R-DFLDALLLA---KEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 348 DTLLQMEYLDMVVNETLRLYPIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDS 426
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKF 394
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412152 427 INPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEIPLKLSKQGLLQPENPLLLKV 493
Cdd:pfam00067 395 RKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLKF 461
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
67-487 5.07e-131

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: 388.04  E-value: 5.07e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGRQPVLAITDPDIIKTVLVKEcYSTFTNRRRFGpvgILKKAISIS----ENEEWKRIRALLSPTFTSGRL 142
Cdd:cd20649     1 KYGPICGYYIGRRMFVVIAEPDMIKQVLVKD-FNNFTNRMKAN---LITKPMSDSllclRDERWKRVRSILTPAFSAAKM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 143 KEMFPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLKFDIFDPLFLS 222
Cdd:cd20649    77 KEMVPLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQVDSQKNPDDPFVKNCKRFFEFSFFRPILIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 223 VTLFPF-LTPVFDAL-NVSlfpRDVI-SFFTTSVERMKENR-MKEKEKQRVDFLQLMINSQN------------------ 280
Cdd:cd20649   157 FLAFPFiMIPLARILpNKS---RDELnSFFTQCIRNMIAFRdQQSPEERRRDFLQLMLDARTsakflsvehfdivndade 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 281 --------------YKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPAT 346
Cdd:cd20649   234 saydghpnspaneqTKPSKQKRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVD 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 347 YDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDS 426
Cdd:cd20649   314 YANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQR 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412152 427 INPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEIPLKLSKQGLLQPEN 487
Cdd:cd20649   394 RHPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIPLQLKSKSTLGPKN 454
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
69-491 1.17e-106

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: 324.48  E-value: 1.17e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  69 GKMWGLYDGRQPVLAITDPDIIKTVL--VKECYSTFTNR--RRFGPVGILkkaisISENEEWKRIRALLSPTFTSGRLKE 144
Cdd:cd20628     1 GGVFRLWIGPKPYVVVTNPEDIEVILssSKLITKSFLYDflKPWLGDGLL-----TSTGEKWRKRRKLLTPAFHFKILES 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 145 MFPIINQFTDVLVRNMRQGLGEGkPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLK---FDIFDPLFL 221
Cdd:cd20628    76 FVEVFNENSKILVEKLKKKAGGG-EFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEiilKRIFSPWLR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 222 SVTLFpFLTPVFDALNVSLfprDVISFFTTSV-----ERMKENRMKEKE------KQRVDFLQLMINSQnyktkESHKAL 290
Cdd:cd20628   155 FDFIF-RLTSLGKEQRKAL---KVLHDFTNKVikerrEELKAEKRNSEEddefgkKKRKAFLDLLLEAH-----EDGGPL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 291 SDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPATYDTLLQMEYLDMVVNETLRLYPI 369
Cdd:cd20628   226 TDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFgDDDRRPTLEDLNKMKYLERVIKETLRLYPS 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 370 AGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFAL 449
Cdd:cd20628   306 VPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIPFSAGPRNCIGQKFAM 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1720412152 450 INMKVALVRVLQNFTVQPCKETEiPLKLSKQGLLQPENPLLL 491
Cdd:cd20628   386 LEMKTLLAKILRNFRVLPVPPGE-DLKLIAEIVLRSKNGIRV 426
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
65-463 3.86e-97

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: 300.20  E-value: 3.86e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  65 HKKYG---KMWGLYdgrQPVLAITDPDIIKTVLVKE-------CYSTFTN--RRRFGPVGILkkaiSISENEEWKRIRAL 132
Cdd:cd20613     8 AKEYGpvfVFWILH---RPIVVVSDPEAVKEVLITLnlpkpprVYSRLAFlfGERFLGNGLV----TEVDHEKWKKRRAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 133 LSPTFTSGRLKEMFPIINQFTDVLVRNMRQgLGEGK-PTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLL 211
Cdd:cd20613    81 LNPAFHRKYLKNLMDEFNESADLLVEKLSK-KADGKtEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDPDSPFPKAISLVL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 212 K---FDIFDPLF-LSVTLFPFLTPVFDALN-VSLFPRDVISffttsvERMKEnrMKEKEKQRVDFLQLMInsqnyKTKES 286
Cdd:cd20613   160 EgiqESFRNPLLkYNPSKRKYRREVREAIKfLRETGRECIE------ERLEA--LKRGEEVPNDILTHIL-----KASEE 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 287 HKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRL 366
Cdd:cd20613   227 EPDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLRL 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 367 YPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMR 446
Cdd:cd20613   307 YPPVPGTSRELTKDIELGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIPSYAYFPFSLGPRSCIGQQ 386
                         410
                  ....*....|....*..
gi 1720412152 447 FALINMKVALVRVLQNF 463
Cdd:cd20613   387 FAQIEAKVILAKLLQNF 403
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
82-478 1.64e-96

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: 298.80  E-value: 1.64e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  82 LAITDPDIIKTVLVKECYS------TFTNRRRFGPVGILkkaisISENEEWKRIRALLSPTFTSGRLKEMFPII----NQ 151
Cdd:cd11069    16 LLVTDPKALKHILVTNSYDfekppaFRRLLRRILGDGLL-----AAEGEEHKRQRKILNPAFSYRHVKELYPIFwskaEE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 152 FTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLKFDIFDPLFLsvTLFPFLTP 231
Cdd:cd11069    91 LVDKLEEEIEESGDESISIDVLEWLSRATLDIIGLAGFGYDFDSLENPDNELAEAYRRLFEPTLLGSLLF--ILLLFLPR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 232 VFDALNVSLFPRDVISFFTTS-------VERMKENRMKEKEKQRVDFLQLMINSQNyktKESHKALSDVEIVAQSVIFIF 304
Cdd:cd11069   169 WLVRILPWKANREIRRAKDVLrrlareiIREKKAALLEGKDDSGKDILSILLRAND---FADDERLSDEELIDQILTFLA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 305 AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNK--APATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVE 382
Cdd:cd11069   246 AGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPpdGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKDTV 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 383 INGLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERF-----SKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVAL 456
Cdd:cd11069   326 IKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWlepdgAASPGGAGSNYALLTFLHGPRSCIGKKFALAEMKVLL 405
                         410       420
                  ....*....|....*....|..
gi 1720412152 457 VRVLQNFTVQPCKETEIPLKLS 478
Cdd:cd11069   406 AALVSRFEFELDPDAEVERPIG 427
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
76-489 1.97e-95

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: 294.42  E-value: 1.97e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  76 DGRQPVLAITDPDIIKTVLVKECYSTFTNRRRFGPVG-ILKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTD 154
Cdd:cd00302     8 LGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGdFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVIREIAR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 155 VLVRNMRQGLGEGKPtsMKDIFGAYSMDVITATSFGvniDSLNNPQDPFVEKIKKLLKfdifdpLFLSVTLFPFLTPVFD 234
Cdd:cd00302    88 ELLDRLAAGGEVGDD--VADLAQPLALDVIARLLGG---PDLGEDLEELAELLEALLK------LLGPRLLRPLPSPRLR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 235 ALNVSLfpRDVISFFTTSVERmkenRMKEKEKQRVDFLQLminsqnykTKESHKALSDVEIVAQSVIFIFAGYETTSSAL 314
Cdd:cd00302   157 RLRRAR--ARLRDYLEELIAR----RRAEPADDLDLLLLA--------DADDGGGLSDEEIVAELLTLLLAGHETTASLL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 315 SFALYLLAIHPDVQKKLQDEIDAALPNkapATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVV 394
Cdd:cd00302   223 AWALYLLARHPEVQERLRAEIDAVLGD---GTPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLV 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 395 MIPTFALHKDPKYWPEPEEFRPERFSkkNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEIP 474
Cdd:cd00302   300 LLSLYAAHRDPEVFPDPDEFDPERFL--PEREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEELE 377
                         410
                  ....*....|....*
gi 1720412152 475 LKLSKqGLLQPENPL 489
Cdd:cd00302   378 WRPSL-GTLGPASLP 391
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
65-489 3.51e-89

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: 279.41  E-value: 3.51e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  65 HKKYGKMWGLYDGRQPVLAITDPDIIKTVLVKEcySTFTNRRRFGPVGILKK------AISISENEEWKRIRALLSPTFT 138
Cdd:cd11054     1 HKKYGPIVREKLGGRDIVHLFDPDDIEKVFRNE--GKYPIRPSLEPLEKYRKkrgkplGLLNSNGEEWHRLRSAVQKPLL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 139 SGR-LKEMFPIINQFTDVLVRNMRQGL---GEGKPTSMKDIFgAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLKfD 214
Cdd:cd11054    79 RPKsVASYLPAINEVADDFVERIRRLRdedGEEVPDLEDELY-KWSLESIGTVLFGKRLGCLDDNPDSDAQKLIEAVK-D 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 215 IFDPLFLSVTLFP----FLTPVFDAL-NVSLFPRDVIS-FFTTSVERMKENRMKEKEKQrvDFLQLMInsqnyktkeSHK 288
Cdd:cd11054   157 IFESSAKLMFGPPlwkyFPTPAWKKFvKAWDTIFDIASkYVDEALEELKKKDEEDEEED--SLLEYLL---------SKP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 289 ALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYP 368
Cdd:cd11054   226 GLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYP 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 369 IAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF--SKKNQDSINPYMYLPFGSGPRNCIGMR 446
Cdd:cd11054   306 VAPGNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlrDDSENKNIHPFASLPFGFGPRMCIGRR 385
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1720412152 447 FALINMKVALVRVLQNFTVQPCKEteiPLKLSKQGLLQPENPL 489
Cdd:cd11054   386 FAELEMYLLLAKLLQNFKVEYHHE---ELKVKTRLILVPDKPL 425
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
79-492 5.33e-89

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: 279.06  E-value: 5.33e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  79 QPVLAITDPDIIKTVLvKECYSTFTNRRRFGPV----GILkkaisISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTD 154
Cdd:cd20659    12 RPILVLNHPDTIKAVL-KTSEPKDRDSYRFLKPwlgdGLL-----LSNGKKWKRNRRLLTPAFHFDILKPYVPVYNECTD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 155 VLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNID-SLNNPQDPFVEKIKKL--LKFD-IFDPLFLSVTLFPfLT 230
Cdd:cd20659    86 ILLEKWSKLAETGESVEVFEDISLLTLDIILRCAFSYKSNcQQTGKNHPYVAAVHELsrLVMErFLNPLLHFDWIYY-LT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 231 PV---FDALNvslfprDVISFFTTSV------ERMKENRMKEKEKQRVDFLQLMINSQnyktKESHKALSDVEIVAQSVI 301
Cdd:cd20659   165 PEgrrFKKAC------DYVHKFAEEIikkrrkELEDNKDEALSKRKYLDFLDILLTAR----DEDGKGLTDEEIRDEVDT 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 302 FIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDV 381
Cdd:cd20659   235 FLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPI 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 382 EINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQ 461
Cdd:cd20659   315 TIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILR 394
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1720412152 462 NFTVQPCKETEIPLKLskQGLLQPENPLLLK 492
Cdd:cd20659   395 RFELSVDPNHPVEPKP--GLVLRSKNGIKLK 423
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
80-463 1.03e-84

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: 267.93  E-value: 1.03e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  80 PVLAITDPDIIKTVLVK-ECYSTFTNRRRFGpvgiLKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVR 158
Cdd:cd11057    12 PFVITSDPEIVQVVLNSpHCLNKSFFYDFFR----LGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIFNEEAQKLVQ 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 159 NMRQGLGEGkPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLlkFDIFDPLFLSVTLFP----FLTPVF- 233
Cdd:cd11057    88 RLDTYVGGG-EFDILPDLSRCTLEMICQTTLGSDVNDESDGNEEYLESYERL--FELIAKRVLNPWLHPefiyRLTGDYk 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 234 -DALNVSLFpRDvisFFTTSVERMKENRMKEKEKQRVDF------LQLMINsQNYKTKESHKALSDVEIVAQSVIFIFAG 306
Cdd:cd11057   165 eEQKARKIL-RA---FSEKIIEKKLQEVELESNLDSEEDeengrkPQIFID-QLLELARNGEEFTDEEIMDEIDTMIFAG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 307 YETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPA-TYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEI-N 384
Cdd:cd11057   240 NDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDGQFiTYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLsN 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 385 GLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd11057   320 GVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNY 399
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
77-467 3.51e-81

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: 258.28  E-value: 3.51e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  77 GRQPVLAITDPDIIKTVLVkecystfTNRRRF---GPVGILKKA----ISISENEEWKRIRALLSPTFTSGRLKEMFPII 149
Cdd:cd20620     9 GPRRVYLVTHPDHIQHVLV-------TNARNYvkgGVYERLKLLlgngLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 150 NQFTDVLVRNMRQGLGEGkPTSMKDIFGAYSMDVITATSFGVNIDSLnnpqdpfVEKIKKLLkfdifdPLFLSVTLFPFL 229
Cdd:cd20620    82 VEATAALLDRWEAGARRG-PVDVHAEMMRLTLRIVAKTLFGTDVEGE-------ADEIGDAL------DVALEYAARRML 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 230 TPVFDALNVSLFP----RDVISFFTTSVERMKENRMKEKEKqRVDFLQLMINSQnykTKESHKALSDVEIVAQSVIFIFA 305
Cdd:cd20620   148 SPFLLPLWLPTPAnrrfRRARRRLDEVIYRLIAERRAAPAD-GGDLLSMLLAAR---DEETGEPMSDQQLRDEVMTLFLA 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 306 GYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPaTYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEING 385
Cdd:cd20620   224 GHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRPP-TAEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGG 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 386 LFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTV 465
Cdd:cd20620   303 YRIPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRL 382

                  ..
gi 1720412152 466 QP 467
Cdd:cd20620   383 RL 384
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
69-468 5.82e-79

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: 252.90  E-value: 5.82e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  69 GKMWGLYDGRQPVLAITDPDIIKTVLVKEcYSTFTNR-RRFGPVGILK-KAISISENEEWKRIRALLSPTFT-SGRLKEM 145
Cdd:cd20617     1 GGIFTLWLGDVPTVVLSDPEIIKEAFVKN-GDNFSDRpLLPSFEIISGgKGILFSNGDYWKELRRFALSSLTkTKLKKKM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 146 FPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQ-DPFVEKIKKLLK----FDIFDPLF 220
Cdd:cd20617    80 EELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDDGEfLKLVKPIEEIFKelgsGNPSDFIP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 221 LSVTLFPFLTPVFDALNVSLFprdviSFFTTSVERMKENRMKEKEKQRVDFLQLMINsqnyktKESHKALSDVEIVAQSV 300
Cdd:cd20617   160 ILLPFYFLYLKKLKKSYDKIK-----DFIEKIIEEHLKTIDPNNPRDLIDDELLLLL------KEGDSGLFDDDSIISTC 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 301 I-FIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIA--GrLERVC 377
Cdd:cd20617   229 LdLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILplG-LPRVT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 378 KTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYmYLPFGSGPRNCIGMRFALINMKVALV 457
Cdd:cd20617   308 TEDTEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGNKLSEQ-FIPFGIGKRNCVGENLARDELFLFFA 386
                         410
                  ....*....|.
gi 1720412152 458 RVLQNFTVQPC 468
Cdd:cd20617   387 NLLLNFKFKSS 397
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
79-492 2.05e-77

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: 249.09  E-value: 2.05e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  79 QPVLAITDPDIIKTVLVKECYstftNRRRFGPVGI---LKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDV 155
Cdd:cd20621    13 KPLISLVDPEYIKEFLQNHHY----YKKKFGPLGIdrlFGKGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINEITKE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 156 LVRNMrqglgEGKPTSMKDIFGAYSMDVITATSFGVNIDSL-NNPQDPFVEKIKKLlkFDIFDPLFLSVTLFPFLTpVFD 234
Cdd:cd20621    89 KIKKL-----DNQNVNIIQFLQKITGEVVIRSFFGEEAKDLkINGKEIQVELVEIL--IESFLYRFSSPYFQLKRL-IFG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 235 ALNVSLFPRDV-------ISFFTTSVERMKENRMK--EKEKQRVDFLQLMINSQNYKTKESHKALSDVEIVAQSVIFIFA 305
Cdd:cd20621   161 RKSWKLFPTKKekklqkrVKELRQFIEKIIQNRIKqiKKNKDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFITFFFA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 306 GYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRL-ERVCKTDVEIN 384
Cdd:cd20621   241 GTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLfPRVATQDHQIG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 385 GLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFT 464
Cdd:cd20621   321 DLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILKNFE 400
                         410       420
                  ....*....|....*....|....*...
gi 1720412152 465 VQPCKETEipLKLSKQGLLQPENPLLLK 492
Cdd:cd20621   401 IEIIPNPK--LKLIFKLLYEPVNDLLLK 426
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
67-467 1.02e-75

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: 244.93  E-value: 1.02e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGRQPVLaITDPDIIKTVlvkecystFTNRRRFGPVGILKKA-------ISISENEEWKRIRALLSPTFTS 139
Cdd:cd11070     1 KLGAVKILFVSRWNIL-VTKPEYLTQI--------FRRRDDFPKPGNQYKIpafygpnVISSEGEDWKRYRKIVAPAFNE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 140 GRLKEMF-PIINQfTDVLVRNM--RQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEkIKKLLKFDIF 216
Cdd:cd11070    72 RNNALVWeESIRQ-AQRLIRYLleEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHD-TLNAIKLAIF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 217 DPLFLSvtlFPFLtpvfDALNVSLFPRDvISFFTTSVERMKE-NRMKEKEKQRVD-FLQLMINSQNYKTKESHK--ALSD 292
Cdd:cd11070   150 PPLFLN---FPFL----DRLPWVLFPSR-KRAFKDVDEFLSElLDEVEAELSADSkGKQGTESVVASRLKRARRsgGLTE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 293 VEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPA--TYDTLLQMEYLDMVVNETLRLYPIA 370
Cdd:cd11070   222 KELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDwdYEEDFPKLPYLLAVIYETLRLYPPV 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 371 GRLERVCKTDVEI-----NGLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQDSINPYM-------YLPFGS 437
Cdd:cd11070   302 QLLNRKTTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSGEIGAATRftpargaFIPFSA 381
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1720412152 438 GPRNCIGMRFALINMKVALVRVLQNF--TVQP 467
Cdd:cd11070   382 GPRACLGRKFALVEFVAALAELFRQYewRVDP 413
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
64-467 1.01e-73

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: 239.02  E-value: 1.01e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  64 CHKKYGKMWGL-YDGRQPVLAITDPDIIKTVLVKECYSTFTN------RRRFGPVGILkkaisISENEEWKRIRALLSPT 136
Cdd:cd11053     7 LRARYGDVFTLrVPGLGPVVVLSDPEAIKQIFTADPDVLHPGegnsllEPLLGPNSLL-----LLDGDRHRRRRKLLMPA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 137 FTSGRLKEMFPIINQFTDVLVRNMRQGlgegKPTSMKDIFGAYSMDVITATSFGVNIDSlnnPQDPFVEKIKKLLKFDIF 216
Cdd:cd11053    82 FHGERLRAYGELIAEITEREIDRWPPG----QPFDLRELMQEITLEVILRVVFGVDDGE---RLQELRRLLPRLLDLLSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 217 dPLFLSVTLFPFLtpvfdaLNVSLFPRdvisfFTTSVERMKE-------NRMKEKEKQRVDFLQLMINSQNyktkESHKA 289
Cdd:cd11053   155 -PLASFPALQRDL------GPWSPWGR-----FLRARRRIDAliyaeiaERRAEPDAERDDILSLLLSARD----EDGQP 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 290 LSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPatyDTLLQMEYLDMVVNETLRLYPI 369
Cdd:cd11053   219 LSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGGDPDP---EDIAKLPYLDAVIKETLRLYPV 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 370 AGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNqdsINPYMYLPFGSGPRNCIGMRFAL 449
Cdd:cd11053   296 APLVPRRVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRK---PSPYEYLPFGGGVRRCIGAAFAL 372
                         410
                  ....*....|....*...
gi 1720412152 450 INMKVALVRVLQNFTVQP 467
Cdd:cd11053   373 LEMKVVLATLLRRFRLEL 390
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
121-489 1.13e-73

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: 239.47  E-value: 1.13e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 121 SENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMrQGLGEGKPTsmkDIF---GAYSMDVITATSFGVNIDSLN 197
Cdd:cd20660    52 STGEKWHSRRKMLTPTFHFKILEDFLDVFNEQSEILVKKL-KKEVGKEEF---DIFpyiTLCALDIICETAMGKSVNAQQ 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 198 NPQDPFVE---KIKKLLKFDIFDPLFLSVTLFpfltpvfdalnvSLFPR--------DVISFFTTSV--ERMKENRMKEK 264
Cdd:cd20660   128 NSDSEYVKavyRMSELVQKRQKNPWLWPDFIY------------SLTPDgrehkkclKILHGFTNKViqERKAELQKSLE 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 265 E------------KQRVDFLQLMINSQnyktkESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQ 332
Cdd:cd20660   196 EeeeddedadigkRKRLAFLDLLLEAS-----EEGTKLSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVH 270
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 333 DEIDAAL-PNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEP 411
Cdd:cd20660   271 EELDRIFgDSDRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDP 350
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412152 412 EEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCkETEIPLKLSKQGLLQPENPL 489
Cdd:cd20660   351 EKFDPDRFLPENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESV-QKREDLKPAGELILRPVDGI 427
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
118-472 8.78e-72

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: 234.01  E-value: 8.78e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 118 ISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSL- 196
Cdd:cd11058    50 ISTADDEDHARLRRLLAHAFSEKALREQEPIIQRYVDLLVSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFGESFGCLe 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 197 NNPQDPFVEKIKKLLKFDifdPLFLSVTLFPFLTPVFDALNVSLFPRDVISFFTTSVERMKEnRMkEKEKQRVDFLQLMI 276
Cdd:cd11058   130 NGEYHPWVALIFDSIKAL---TIIQALRRYPWLLRLLRLLIPKSLRKKRKEHFQYTREKVDR-RL-AKGTDRPDFMSYIL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 277 nsqnyKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYL 356
Cdd:cd11058   205 -----RNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQLPYL 279
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 357 DMVVNETLRLYP-IAGRLERVC-KTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPER--------FSKKNQDS 426
Cdd:cd11058   280 NAVIQEALRLYPpVPAGLPRVVpAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERwlgdprfeFDNDKKEA 359
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1720412152 427 INpymylPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETE 472
Cdd:cd11058   360 FQ-----PFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPESE 400
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
127-463 9.23e-72

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: 234.04  E-value: 9.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 127 KRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGEGKPTS--MKDIFGAYSMDVITATSFGVNIDSLNNPQDPFV 204
Cdd:cd11061    55 ARRRRVWSHAFSDKALRGYEPRILSHVEQLCEQLDDRAGKPVSWPvdMSDWFNYLSFDVMGDLAFGKSFGMLESGKDRYI 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 205 ekIKKLLKF-DIFDPLFLSVTLFPFLtpvfdaLNVSLFP---RDVISFFTTSVERMKEnRMKEKEKQRVDFLQLMINSqn 280
Cdd:cd11061   135 --LDLLEKSmVRLGVLGHAPWLRPLL------LDLPLFPgatKARKRFLDFVRAQLKE-RLKAEEEKRPDIFSYLLEA-- 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 281 yKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKA-PATYDTLLQMEYLDMV 359
Cdd:cd11061   204 -KDPETGEGLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDeIRLGPKLKSLPYLRAC 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 360 VNETLRLYP-IAGRLERVC-KTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPER-FSKKNQDSINPYMYLPFG 436
Cdd:cd11061   283 IDEALRLSPpVPSGLPRETpPGGLTIDGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERwLSRPEELVRARSAFIPFS 362
                         330       340
                  ....*....|....*....|....*..
gi 1720412152 437 SGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd11061   363 IGPRGCIGKNLAYMELRLVLARLLHRY 389
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
67-463 9.83e-68

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: 222.85  E-value: 9.83e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGRQPVLAITDPDIIKTVLVKecYSTFTNRRR----FGPVGILKKAISISENEEWKRIRALLSPTFTSGRL 142
Cdd:COG2124    30 EYGPVFRVRLPGGGAWLVTRYEDVREVLRD--PRTFSSDGGlpevLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 143 KEMFPIINQFTDVLVRNMRQGlGEGkptsmkDIFGAYS---MDVITATSFGVNIDSlnnpQDPFVEkikkllkfdifdpl 219
Cdd:COG2124   108 AALRPRIREIADELLDRLAAR-GPV------DLVEEFArplPVIVICELLGVPEED----RDRLRR-------------- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 220 fLSVTLFPFLTPVFDALNVSLFP--RDVISFFTTSVERMKENRmkekekqRVDFLQLMINSQnyktkESHKALSDVEIVA 297
Cdd:COG2124   163 -WSDALLDALGPLPPERRRRARRarAELDAYLRELIAERRAEP-------GDDLLSALLAAR-----DDGERLSDEELRD 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 298 QSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIdaalpnkapatydtllqmEYLDMVVNETLRLYPIAGRLERVC 377
Cdd:COG2124   230 ELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTA 291
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 378 KTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERfskknqdsiNPYMYLPFGSGPRNCIGMRFALINMKVALV 457
Cdd:COG2124   292 TEDVELGGVTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCLGAALARLEARIALA 362

                  ....*.
gi 1720412152 458 RVLQNF 463
Cdd:COG2124   363 TLLRRF 368
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
68-477 1.06e-67

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: 223.20  E-value: 1.06e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLvkecyST-FTN-----RRR--FGPVgiLKKAISISENEEWKRIRALLSPTFTS 139
Cdd:cd11063     1 YGNTFEVNLLGTRVIFTIEPENIKAVL-----ATqFKDfglgeRRRdaFKPL--LGDGIFTSDGEEWKHSRALLRPQFSR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 140 GRLKEmFPIINQFTDVLVRNMRQGlgeGKPTSMKDIFGAYSMDVITATSFGVNIDSL-----NNPQDPFVEKIKKLLKFD 214
Cdd:cd11063    74 DQISD-LELFERHVQNLIKLLPRD---GSTVDLQDLFFRLTLDSATEFLFGESVDSLkpggdSPPAARFAEAFDYAQKYL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 215 IFDpLFLSVTLFPFLTPVF-DALNVSlfpRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSqnykTKeSHKALSDv 293
Cdd:cd11063   150 AKR-LRLGKLLWLLRDKKFrEACKVV---HRFVDPYVDKALARKEESKDEESSDRYVFLDELAKE----TR-DPKELRD- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 294 EIVAqsvIFIfAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRL 373
Cdd:cd11063   220 QLLN---ILL-AGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLN 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 374 ERVCKTDVEI------NG---LFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQdsiNPYMYLPFGSGPRNCI 443
Cdd:cd11063   296 SRVAVRDTTLprgggpDGkspIFVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWEDLKR---PGWEYLPFNGGPRICL 372
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1720412152 444 GMRFALINMKVALVRVLQNF-TVQPCKETEIPLKL 477
Cdd:cd11063   373 GQQFALTEASYVLVRLLQTFdRIESRDVRPPEERL 407
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
66-467 1.13e-67

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: 223.76  E-value: 1.13e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  66 KKYGKMWGLYDGRQPVLAITDPDIIKTVLVKEcystFTNRRRFGPVGILKK----AISISENEEWKRIRALLSPTFTSGR 141
Cdd:cd11052     9 KQYGKNFLYWYGTDPRLYVTEPELIKELLSKK----EGYFGKSPLQPGLKKllgrGLVMSNGEKWAKHRRIANPAFHGEK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 142 LKEMFPIINQFTDVLVRNMRQGLGEGKPTSmkDI---FGAYSMDVITATSFGVnidSLNNPQDPFvEKIKKLLK--FDIF 216
Cdd:cd11052    85 LKGMVPAMVESVSDMLERWKKQMGEEGEEV--DVfeeFKALTADIISRTAFGS---SYEEGKEVF-KLLRELQKicAQAN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 217 DPLFLSVTLFpFLTP---VFDALNVSLfpRDVISFFTTSveRMKENRMKEKEKQRVDFLQLMINSQNykTKESHKALSDV 293
Cdd:cd11052   159 RDVGIPGSRF-LPTKgnkKIKKLDKEI--EDSLLEIIKK--REDSLKMGRGDDYGDDLLGLLLEANQ--SDDQNKNMTVQ 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 294 EIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPaTYDTLLQMEYLDMVVNETLRLYPIAGRL 373
Cdd:cd11052   232 EIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKP-PSDSLSKLKTVSMVINESLRLYPPAVFL 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 374 ERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPE-PEEFRPERFSKK-NQDSINPYMYLPFGSGPRNCIGMRFALIN 451
Cdd:cd11052   311 TRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGvAKAAKHPMAFLPFGLGPRNCIGQNFATME 390
                         410
                  ....*....|....*...
gi 1720412152 452 MKVALVRVLQ--NFTVQP 467
Cdd:cd11052   391 AKIVLAMILQrfSFTLSP 408
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
62-496 1.07e-66

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: 220.90  E-value: 1.07e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  62 IQCHKKYGKMWGLYDGRQPVLAITDPDIIKTVlvkeCystftNRRRF-----GPVGILKKAI------SISENEEWKRIR 130
Cdd:cd11068     6 LRLADELGPIFKLTLPGRRVVVVSSHDLIAEL----C-----DESRFdkkvsGPLEELRDFAgdglftAYTHEPNWGKAH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 131 ALLSPTFTSGRLKEMFP----IINQFTDVLVRnmrqgLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNP-QDPFVE 205
Cdd:cd11068    77 RILMPAFGPLAMRGYFPmmldIAEQLVLKWER-----LGPDEPIDVPDDMTRLTLDTIALCGFGYRFNSFYRDePHPFVE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 206 KIKKLLKFdifdpLFLSVTLFPFLTPVFDALNvSLFPRDvISFFTTSVERMKENRMKEKEKQRVDFLQLMINSqnyKTKE 285
Cdd:cd11068   152 AMVRALTE-----AGRRANRPPILNKLRRRAK-RQFRED-IALMRDLVDEIIAERRANPDGSPDDLLNLMLNG---KDPE 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 286 SHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPaTYDTLLQMEYLDMVVNETLR 365
Cdd:cd11068   222 TGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPP-PYEQVAKLRYIRRVLDETLR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 366 LYPIAGRLERVCKTDVEINGLF-IPKGTVVMIPTFALHKDPK-YWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCI 443
Cdd:cd11068   301 LWPTAPAFARKPKEDTVLGGKYpLKKGDPVLVLLPALHRDPSvWGEDAEEFRPERFLPEEFRKLPPNAWKPFGNGQRACI 380
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720412152 444 GMRFALINMKVALVRVLQNFTVQPckETEIPLKLsKQGL-LQPENpLLLKVVSR 496
Cdd:cd11068   381 GRQFALQEATLVLAMLLQRFDFED--DPDYELDI-KETLtLKPDG-FRLKARPR 430
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
82-465 6.58e-66

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: 218.71  E-value: 6.58e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  82 LAITDPDIIKTV-LVKECYSTFTNRRRFGPVGIlKKAISISENEEWKRIRALLSPTF--TSGRLKEMFPIINQFTDVLVR 158
Cdd:cd11059    11 VSVNDLDAVREIyGGGFGKTKSYWYFTLRGGGG-PNLFSTLDPKEHSARRRLLSGVYskSSLLRAAMEPIIRERVLPLID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 159 NMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNN-PQDPFVEKIKKLLKFDIFDPLFLSVTLFPFLTPVFDALN 237
Cdd:cd11059    90 RIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLgDKDSRERELLRRLLASLAPWLRWLPRYLPLATSRLIIGI 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 238 VSLFPRDVISFFTTSVERMKENrmKEKEKQRVDFLQLMINSQNyktKESHKALSDVEIVAQSVIFIFAGYETTSSALSFA 317
Cdd:cd11059   170 YFRAFDEIEEWALDLCARAESS--LAESSDSESLTVLLLEKLK---GLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 318 LYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQ-MEYLDMVVNETLRLY-PIAGRLERVCKTDVE-INGLFIPKGTVV 394
Cdd:cd11059   245 IWELSRPPNLQEKLREELAGLPGPFRGPPDLEDLDkLPYLNAVIRETLRLYpPIPGSLPRVVPEGGAtIGGYYIPGGTIV 324
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720412152 395 MIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPY--MYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTV 465
Cdd:cd11059   325 STQAYSLHRDPEVFPDPEEFDPERWLDPSGETAREMkrAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNYRT 397
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
121-487 1.61e-65

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: 218.48  E-value: 1.61e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 121 SENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGEGKPTSMKDIfGAYSMDVITATSFGVNIDSLNNPQ 200
Cdd:cd20680    63 STGEKWRSRRKMLTPTFHFTILSDFLEVMNEQSNILVEKLEKHVDGEAFNCFFDI-TLCALDIICETAMGKKIGAQSNKD 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 201 DPFVEKIKKLLKFdIFDPLFLSVTLFPFLTPVFDALNVSLFPRDVISFFTTSVERMKENRMK-------------EKEKQ 267
Cdd:cd20680   142 SEYVQAVYRMSDI-IQRRQKMPWLWLDLWYLMFKEGKEHNKNLKILHTFTDNVIAERAEEMKaeedktgdsdgesPSKKK 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 268 RVDFLQLMINSqnykTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNK-APAT 346
Cdd:cd20680   221 RKAFLDMLLSV----TDEEGNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSdRPVT 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 347 YDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDS 426
Cdd:cd20680   297 MEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSG 376
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412152 427 INPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEiPLKLSKQGLLQPEN 487
Cdd:cd20680   377 RHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHFWVEANQKRE-ELGLVGELILRPQN 436
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
77-467 3.84e-65

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: 216.80  E-value: 3.84e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  77 GRQPVLAITDPDIIKTVLvKECYSTFtnrRRFGPVGILKKAISI-----SENEEWKRIRALLSPTFTSGRLKEMFPIINQ 151
Cdd:cd11083     9 GRQPVLVISDPELIREVL-RRRPDEF---RRISSLESVFREMGIngvfsAEGDAWRRQRRLVMPAFSPKHLRYFFPTLRQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 152 FTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLkfdifdPLFLSVTLFPFltP 231
Cdd:cd11083    85 ITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYDLNTLERGGDPLQEHLERVF------PMLNRRVNAPF--P 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 232 VFDALNvslFPRD-------------VISFFTTSVERMKEN--RMKEKEkqrvDFLQLMINSQNyktKEShkALSDVEIV 296
Cdd:cd11083   157 YWRYLR---LPADraldralvevralVLDIIAAARARLAANpaLAEAPE----TLLAMMLAEDD---PDA--RLTDDEIY 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 297 AQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPAT-YDTLLQMEYLDMVVNETLRLYPIAGRLER 375
Cdd:cd11083   225 ANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPlLEALDRLPYLEAVARETLRLKPVAPLLFL 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 376 VCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKN--QDSINPYMYLPFGSGPRNCIGMRFALINMK 453
Cdd:cd11083   305 EPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGAraAEPHDPSSLLPFGAGPRLCPGRSLALMEMK 384
                         410
                  ....*....|....
gi 1720412152 454 VALVRVLQNFTVQP 467
Cdd:cd11083   385 LVFAMLCRNFDIEL 398
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
84-463 3.85e-65

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: 216.74  E-value: 3.85e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  84 ITDPDIIKTVlvkecYSTFTNRRR-----FGPVGILKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVR 158
Cdd:cd11062    13 ISDPDFYDEI-----YAGGSRRRKdppyfYGAFGAPGSTFSTVDHDLHRLRRKALSPFFSKRSILRLEPLIQEKVDKLVS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 159 NMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDpfveKIKKLLKFDIFDPLFLSVTLFPFLTPVFDALNV 238
Cdd:cd11062    88 RLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGYLDEPDF----GPEFLDALRALAEMIHLLRHFPWLLKLLRSLPE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 239 SLFPR-----DVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSQNYKTKESHKALSDVEIVAQSVIFIFAGYETTSSA 313
Cdd:cd11062   164 SLLKRlnpglAVFLDFQESIAKQVDEVLRQVSAGDPPSIVTSLFHALLNSDLPPSEKTLERLADEAQTLIGAGTETTART 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 314 LSFALYLLAIHPDVQKKLQDEIDAALPNK-APATYDTLLQMEYLDMVVNETLRL-YPIAGRLERVCKT-DVEINGLFIPK 390
Cdd:cd11062   244 LSVATFHLLSNPEILERLREELKTAMPDPdSPPSLAELEKLPYLTAVIKEGLRLsYGVPTRLPRVVPDeGLYYKGWVIPP 323
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412152 391 GTVVMIPTFALHKDPKYWPEPEEFRPER----FSKKNQDSinpymYL-PFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd11062   324 GTPVSMSSYFVHHDEEIFPDPHEFRPERwlgaAEKGKLDR-----YLvPFSKGSRSCLGINLAYAELYLALAALFRRF 396
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
77-493 7.61e-62

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: 207.88  E-value: 7.61e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  77 GRQPVLAITDPDIIKTVLVKEcySTFTNR----RRFGPVgiLKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQF 152
Cdd:cd11049    21 GPRPAYVVTSPELVRQVLVND--RVFDKGgplfDRARPL--LGNGLATCPGEDHRRQRRLMQPAFHRSRIPAYAEVMREE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 153 TDVLVRNMRqglgEGKPTSMKDIFGAYSMDVITATSFGVNIDslnnpqDPFVEKIKKLLKfDIFDPLFLSVTLFPFLTPV 232
Cdd:cd11049    97 AEALAGSWR----PGRVVDVDAEMHRLTLRVVARTLFSTDLG------PEAAAELRQALP-VVLAGMLRRAVPPKFLERL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 233 FDALNVSLfpRDVISFFTTSVERMKENRmKEKEKQRVDFLQLMINSQNyktkESHKALSDVEIVAQSVIFIFAGYETTSS 312
Cdd:cd11049   166 PTPGNRRF--DRALARLRELVDEIIAEY-RASGTDRDDLLSLLLAARD----EEGRPLSDEELRDQVITLLTAGTETTAS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 313 ALSFALYLLAIHPDVQKKLQDEIDAALPNKaPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGT 392
Cdd:cd11049   239 TLAWAFHLLARHPEVERRLHAELDAVLGGR-PATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGT 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 393 VVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCkeTE 472
Cdd:cd11049   318 EVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPV--PG 395
                         410       420
                  ....*....|....*....|.
gi 1720412152 473 IPLKLSKQGLLQPEnPLLLKV 493
Cdd:cd11049   396 RPVRPRPLATLRPR-RLRMRV 415
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
68-489 1.41e-60

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: 205.29  E-value: 1.41e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVkecystfTNRRRFGPVG--------ILKKAISISENEEWKRIRALLSPTFTS 139
Cdd:cd11046    10 YGPIYKLAFGPKSFLVISDPAIAKHVLR-------SNAFSYDKKGllaeilepIMGKGLIPADGEIWKKRRRALVPALHK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 140 GRLKEMFPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNpQDPFVEKIKKLLkfdiFDPL 219
Cdd:cd11046    83 DYLEMMVRVFGRCSERLMEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVTE-ESPVIKAVYLPL----VEAE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 220 FLSVTLFP--------FLTPVFDALNVSL-FPRDVISFF---------TTSVERMKENRMKEKEKQRVDFLQLMINSqny 281
Cdd:cd11046   158 HRSVWEPPywdipaalFIVPRQRKFLRDLkLLNDTLDDLirkrkemrqEEDIELQQEDYLNEDDPSLLRFLVDMRDE--- 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 282 ktkeshkALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVN 361
Cdd:cd11046   235 -------DVDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLN 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 362 ETLRLYPIAGRLERVCKTDVEI--NGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSIN----PYMYLPF 435
Cdd:cd11046   308 ESLRLYPQPPVLIRRAVEDDKLpgGGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNevidDFAFLPF 387
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720412152 436 GSGPRNCIGMRFALINMKVALVRVLQNFTVQPcKETEIPLKLSKQGLLQPENPL 489
Cdd:cd11046   388 GGGPRKCLGDQFALLEATVALAMLLRRFDFEL-DVGPRHVGMTTGATIHTKNGL 440
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
81-466 1.73e-59

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: 202.04  E-value: 1.73e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  81 VLAITDPDIIKTVlvkecYSTFTNRRR------FGPVGILKKAISISENEEW-KRIRALLSPTFTSGRLKEMFPIINQFT 153
Cdd:cd11060    10 EVSISDPEAIKTI-----YGTRSPYTKsdwykaFRPKDPRKDNLFSERDEKRhAALRRKVASGYSMSSLLSLEPFVDECI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 154 DVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQD--PFVEKIKKLLkfdifdPLFLSVTLFPFLTP 231
Cdd:cd11060    85 DLLVDLLDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFGFLEAGTDvdGYIASIDKLL------PYFAVVGQIPWLDR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 232 VFDaLNVSLFPRDVISFF----TTSVERMKE--NRMKEKEKQRVDFLQLMINSQnyktKESHKALSDVEIVAQSVIFIFA 305
Cdd:cd11060   159 LLL-KNPLGPKRKDKTGFgplmRFALEAVAErlAEDAESAKGRKDMLDSFLEAG----LKDPEKVTDREVVAEALSNILA 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 306 GYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL---PNKAPATYDTLLQMEYLDMVVNETLRLYPIAGR-LERVC-KTD 380
Cdd:cd11060   234 GSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVaegKLSSPITFAEAQKLPYLQAVIKEALRLHPPVGLpLERVVpPGG 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 381 VEINGLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERF--SKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALV 457
Cdd:cd11060   314 ATICGRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWleADEEQRRMMDRADLTFGAGSRTCLGKNIALLELYKVIP 393

                  ....*....
gi 1720412152 458 RVLQNFTVQ 466
Cdd:cd11060   394 ELLRRFDFE 402
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
66-464 1.63e-58

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: 199.60  E-value: 1.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  66 KKYGKMWGLYDGRQPVLAITDPDIIKTVLVKEcySTFTNRRRFGPVGILKKAISIS--ENEEWKRIRALLSPTFTSGRLK 143
Cdd:cd20639     9 KIYGKTFLYWFGPTPRLTVADPELIREILLTR--ADHFDRYEAHPLVRQLEGDGLVslRGEKWAHHRRVITPAFHMENLK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 144 EMFPIINQFTDVLV---RNMRQGLGEGKpTSMKDIFGAYSMDVITATSFGVNIDS---LNNPQDpfvekikKLLKFdiFD 217
Cdd:cd20639    87 RLVPHVVKSVADMLdkwEAMAEAGGEGE-VDVAEWFQNLTEDVISRTAFGSSYEDgkaVFRLQA-------QQMLL--AA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 218 PLFLSVTL--FPFLtPVFDALNVSLFPRDVISFFTTSVERMKENRMKEKEKQRV-DFLQLMINSqnyKTKESHKALSDVE 294
Cdd:cd20639   157 EAFRKVYIpgYRFL-PTKKNRKSWRLDKEIRKSLLKLIERRQTAADDEKDDEDSkDLLGLMISA---KNARNGEKMTVEE 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 295 IVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEI-----DAALPNKapatyDTLLQMEYLDMVVNETLRLYPI 369
Cdd:cd20639   233 IIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVlavcgKGDVPTK-----DHLPKLKTLGMILNETLRLYPP 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 370 AGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSK-KNQDSINPYMYLPFGSGPRNCIGMRF 447
Cdd:cd20639   308 AVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADgVARAAKHPLAFIPFGLGPRTCVGQNL 387
                         410
                  ....*....|....*..
gi 1720412152 448 ALINMKVALVRVLQNFT 464
Cdd:cd20639   388 AILEAKLTLAVILQRFE 404
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
77-467 2.75e-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: 196.27  E-value: 2.75e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  77 GRQPVLAITDPDIIKTVLVKEcYSTF----TNRRRFGPVgiLKKAISISENEEWKRIRALLSPTFTSGRLKE-MFPIINq 151
Cdd:cd11064     9 GGPDGIVTADPANVEHILKTN-FDNYpkgpEFRDLFFDL--LGDGIFNVDGELWKFQRKTASHEFSSRALREfMESVVR- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 152 ftdvlvRNMRQGL--------GEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNN--PQDPFVEKikkllkFDIFdplfL 221
Cdd:cd11064    85 ------EKVEKLLvplldhaaESGKVVDLQDVLQRFTFDVICKIAFGVDPGSLSPslPEVPFAKA------FDDA----S 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 222 SVTLFPFLTPVF-----DALNVSLFPR-----DVISFFTTSV--ERMKE-NRMKEKEKQRVDFLQLMINS-QNYKTKESH 287
Cdd:cd11064   149 EAVAKRFIVPPWlwklkRWLNIGSEKKlreaiRVIDDFVYEVisRRREElNSREEENNVREDLLSRFLASeEEEGEPVSD 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 288 KALSDVEIVaqsviFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKA-----PATYDTLLQMEYLDMVVNE 362
Cdd:cd11064   229 KFLRDIVLN-----FILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTtdesrVPTYEELKKLVYLHAALSE 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 363 TLRLYPIAGRLERVC-KTDVEINGLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQD--SINPYMYLPFGSG 438
Cdd:cd11064   304 SLRLYPPVPFDSKEAvNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWLDEDGGlrPESPYKFPAFNAG 383
                         410       420
                  ....*....|....*....|....*....
gi 1720412152 439 PRNCIGMRFALINMKVALVRVLQNFTVQP 467
Cdd:cd11064   384 PRICLGKDLAYLQMKIVAAAILRRFDFKV 412
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
66-466 1.65e-56

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: 194.42  E-value: 1.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  66 KKYGKMWGLYDGRQPVLAITDPDIIKTVLVKecYSTFTNRRRFGPVGILKKAISISENEEWKRIRALLSPTFTSGRLKEM 145
Cdd:cd20642     9 KTYGKNSFTWFGPIPRVIIMDPELIKEVLNK--VYDFQKPKTNPLTKLLATGLASYEGDKWAKHRKIINPAFHLEKLKNM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 146 FPIINQFTDVLVRNMRQGLGEgKPTSMKDI---FGAYSMDVITATSFGvniDSLNNPQDPFvEKIKKLLKFDIFDPLFLS 222
Cdd:cd20642    87 LPAFYLSCSEMISKWEKLVSS-KGSCELDVwpeLQNLTSDVISRTAFG---SSYEEGKKIF-ELQKEQGELIIQALRKVY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 223 VTLFPFLtPVFDALNVSLFPRDVISFFTTSVERmKENRMKEKEKQRVDFLQLMINSqNYKTKESHK----ALSDVEIVAQ 298
Cdd:cd20642   162 IPGWRFL-PTKRNRRMKEIEKEIRSSLRGIINK-REKAMKAGEATNDDLLGILLES-NHKEIKEQGnkngGMSTEDVIEE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 299 SVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPaTYDTLLQMEYLDMVVNETLRLYPIAGRLERVCK 378
Cdd:cd20642   239 CKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKP-DFEGLNHLKVVTMILYEVLRLYPPVIQLTRAIH 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 379 TDVEINGLFIPKGTVVMIPTFALHKDPKYWPE-PEEFRPERFSK------KNQDSinpymYLPFGSGPRNCIGMRFALIN 451
Cdd:cd20642   318 KDTKLGDLTLPAGVQVSLPILLVHRDPELWGDdAKEFNPERFAEgiskatKGQVS-----YFPFGWGPRICIGQNFALLE 392
                         410
                  ....*....|....*
gi 1720412152 452 MKVALVRVLQNFTVQ 466
Cdd:cd20642   393 AKMALALILQRFSFE 407
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
80-492 2.20e-56

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: 194.14  E-value: 2.20e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  80 PVLAITDPDIIKTVLVKECYSTFTNRRRFGpvgILK----KAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDV 155
Cdd:cd20679    24 PIIRLFHPDYIRPVLLASAAVAPKDELFYG---FLKpwlgDGLLLSSGDKWSRHRRLLTPAFHFNILKPYVKIFNQSTNI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 156 LVRNMRQGLGEGkPTSMkDIFGAYS---MDVITATSFGVNIDSLNNPQDpFVEKIKKLLKFDI--FDPLFLSVTLFPFLT 230
Cdd:cd20679   101 MHAKWRRLASEG-SARL-DMFEHISlmtLDSLQKCVFSFDSNCQEKPSE-YIAAILELSALVVkrQQQLLLHLDFLYYLT 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 231 PvfdalNVSLFPR--DVISFFTTSV--ER--------MKENRMKEKEKQRVDFLQLMINSQNyktkESHKALSDVEIVAQ 298
Cdd:cd20679   178 A-----DGRRFRRacRLVHDFTDAViqERrrtlpsqgVDDFLKAKAKSKTLDFIDVLLLSKD----EDGKELSDEDIRAE 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 299 SVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPAT--YDTLLQMEYLDMVVNETLRLYPIAGRLERV 376
Cdd:cd20679   249 ADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEieWDDLAQLPFLTMCIKESLRLHPPVTAISRC 328
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 377 CKTDVEI-NGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVA 455
Cdd:cd20679   329 CTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIGQTFAMAEMKVV 408
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1720412152 456 LVRVLQNFTVQPckETEIPLKLSkQGLLQPENPLLLK 492
Cdd:cd20679   409 LALTLLRFRVLP--DDKEPRRKP-ELILRAEGGLWLR 442
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
67-463 3.52e-56

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: 193.06  E-value: 3.52e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGRQPVLAITDPDIIKTVLvKECYSTFTNRRRFGPVGILK---KAISISE-NEEWKRIRA-----LLSP-- 135
Cdd:cd11072     1 KYGPLMLLRLGSVPTVVVSSPEAAKEVL-KTHDLVFASRPKLLAARILSyggKDIAFAPyGEYWRQMRKicvleLLSAkr 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 136 --TFTSGRLKEMfpiinqftDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNnpQDPFVEKIKKLLK- 212
Cdd:cd11072    80 vqSFRSIREEEV--------SLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKD--QDKFKELVKEALEl 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 213 ---FDIFDplflsvtLFPFLTPVfdalnvslfprDVISFFTTSVERM---------------KENRMKEKEKQRVDFLQL 274
Cdd:cd11072   150 lggFSVGD-------YFPSLGWI-----------DLLTGLDRKLEKVfkeldaflekiidehLDKKRSKDEDDDDDDLLD 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 275 MINsQNYKTKESHkaLSDVEIVAqsVIF-IF-AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQ 352
Cdd:cd11072   212 LRL-QKEGDLEFP--LTRDNIKA--IILdMFlAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEK 286
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 353 MEYLDMVVNETLRLYPIAGRL-ERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFskknQDSINPYM 431
Cdd:cd11072   287 LKYLKAVIKETLRLHPPAPLLlPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERF----LDSSIDFK 362
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1720412152 432 -----YLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd11072   363 gqdfeLIPFGAGRRICPGITFGLANVELALANLLYHF 399
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
69-470 1.07e-55

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: 191.66  E-value: 1.07e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  69 GKMWGLYDGRQPVLAITDPDIIKTVLVKEcysTFTNR--------RRFGPvgilKKAISISENEEWKRIRALLSPT---F 137
Cdd:cd20651     1 GDVVGLKLGKDKVVVVSGYEAVREVLSRE---EFDGRpdgfffrlRTFGK----RLGITFTDGPFWKEQRRFVLRHlrdF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 138 TSGRlKEMFPIINQFTDVLVRNMRQGlgEGKPTSMKDIFGAYSMDVITATSFGVNIDslnnpqdPFVEKIKKLLK----- 212
Cdd:cd20651    74 GFGR-RSMEEVIQEEAEELIDLLKKG--EKGPIQMPDLFNVSVLNVLWAMVAGERYS-------LEDQKLRKLLElvhll 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 213 ---FDIFDPLFlsvTLFPFLTPVF-DALNVSLF---PRDVISFFTTSVERMKENrmkEKEKQRVDFLQLMINSQNyKTKE 285
Cdd:cd20651   144 frnFDMSGGLL---NQFPWLRFIApEFSGYNLLvelNQKLIEFLKEEIKEHKKT---YDEDNPRDLIDAYLREMK-KKEP 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 286 SHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLR 365
Cdd:cd20651   217 PSSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLR 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 366 LYPIA-GRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIG 444
Cdd:cd20651   297 IFTLVpIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLG 376
                         410       420
                  ....*....|....*....|....*.
gi 1720412152 445 MRFALINMKVALVRVLQNFTVQPCKE 470
Cdd:cd20651   377 ESLARNELFLFFTGLLQNFTFSPPNG 402
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
80-470 1.97e-55

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: 190.54  E-value: 1.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  80 PVLAITDPDIIKTVLVKECYSTFTNRRRF-GPVgILKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVR 158
Cdd:cd11051    11 PLLVVTDPELAEQITQVTNLPKPPPLRKFlTPL-TGGSSLISMEGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVEIFAA 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 159 NMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSlnNPQDPFVEKIKKLLKFDIFDPLFLSVTLFPFltpvfdalnv 238
Cdd:cd11051    90 ILRELAESGEVFSLEELTTNLTFDVIGRVTLDIDLHA--QTGDNSLLTALRLLLALYRSLLNPFKRLNPL---------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 239 SLFPRDVISffttsvermkenrmkekekQRVDflqlminsqNYKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFAL 318
Cdd:cd11051   158 RPLRRWRNG-------------------RRLD---------RYLKPEVRKRFELERAIDQIKTFLFAGHDTTSSTLCWAF 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 319 YLLAIHPDVQKKLQDEIDA-------ALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLeRVCKTDVEI---NGLFI 388
Cdd:cd11051   210 YLLSKHPEVLAKVRAEHDEvfgpdpsAAAELLREGPELLNQLPYTTAVIKETLRLFPPAGTA-RRGPPGVGLtdrDGKEY 288
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 389 P-KGTVVMIPTFALHKDPKYWPEPEEFRPERF--SKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTV 465
Cdd:cd11051   289 PtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWlvDEGHELYPPKSAWRPFERGPRNCIGQELAMLELKIILAMTVRRFDF 368

                  ....*
gi 1720412152 466 QPCKE 470
Cdd:cd11051   369 EKAYD 373
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
77-487 2.15e-55

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: 191.33  E-value: 2.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  77 GRQPVLAITDPDIIKTVLVKECYSTFTNRRRFGP-VGilkKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDV 155
Cdd:cd20678    21 GFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPwIG---KGLLVLNGQKWFQHRRLLTPAFHYDILKPYVKLMADSVRV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 156 LVRNMRQGLGEGKPTsmkDIFGAYS---MDVITATSFGVN----IDSLNNPQDPFVEKIKKLLKFDIFDPLFLSVTLFpF 228
Cdd:cd20678    98 MLDKWEKLATQDSSL---EIFQHVSlmtLDTIMKCAFSHQgscqLDGRSNSYIQAVSDLSNLIFQRLRNFFYHNDFIY-K 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 229 LTPvfdalNVSLFPR--DVISFFTTSVERM-KENRMKEKE------KQRVDFLQLMINSQNyktkESHKALSDVEIVAQS 299
Cdd:cd20678   174 LSP-----HGRRFRRacQLAHQHTDKVIQQrKEQLQDEGElekikkKRHLDFLDILLFAKD----ENGKSLSDEDLRAEV 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 300 VIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKT 379
Cdd:cd20678   245 DTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSK 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 380 DVEI-NGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVR 458
Cdd:cd20678   325 PVTFpDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVAL 404
                         410       420
                  ....*....|....*....|....*....
gi 1720412152 459 VLQNFTVQPcKETEIPLKLSkQGLLQPEN 487
Cdd:cd20678   405 TLLRFELLP-DPTRIPIPIP-QLVLKSKN 431
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
65-483 2.28e-55

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: 190.96  E-value: 2.28e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  65 HKKYGKMWGLYDGRQPVLAITDPDIIKTVLVKECYSTFTN-----RRRFGPvgilkKAISISENEEWKRIRALLSPTFTS 139
Cdd:cd11044    18 YQKYGPVFKTHLLGRPTVFVIGAEAVRFILSGEGKLVRYGwprsvRRLLGE-----NSLSLQDGEEHRRRRKLLAPAFSR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 140 GRLKEMFPIINQftdvLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVnidslnnpqDPFVEKIKKLLKFDIFDPL 219
Cdd:cd11044    93 EALESYVPTIQA----IVQSYLRKWLKAGEVALYPELRRLTFDVAARLLLGL---------DPEVEAEALSQDFETWTDG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 220 FLSVTL-FPFlTPVFDALNVslfpRD-VISFFTTSVERMKENRMKEKEkqrvDFLQLMINSQnyktKESHKALSDVEIVA 297
Cdd:cd11044   160 LFSLPVpLPF-TPFGRAIRA----RNkLLARLEQAIRERQEEENAEAK----DALGLLLEAK----DEDGEPLSMDELKD 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 298 QSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAaLPNKAPATYDTLLQMEYLDMVVNETLRLY-PIAGRLERV 376
Cdd:cd11044   227 QALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDA-LGLEEPLTLESLKKMPYLDQVIKEVLRLVpPVGGGFRKV 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 377 CKtDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSIN-PYMYLPFGSGPRNCIGMRFALINMKVA 455
Cdd:cd11044   306 LE-DFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKkPFSLIPFGGGPRECLGKEFAQLEMKIL 384
                         410       420       430
                  ....*....|....*....|....*....|...
gi 1720412152 456 LVRVLQN--FTVQPCKETEI---PLKLSKQGLL 483
Cdd:cd11044   385 ASELLRNydWELLPNQDLEPvvvPTPRPKDGLR 417
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
66-467 2.08e-54

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: 188.39  E-value: 2.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  66 KKYGKMWGLYDGRQPVLAITDPDIIKTV-------LVKECYSTFTNRRRFGPvGILKkaisiSENEEWKRIRALLSPTFT 138
Cdd:cd20640     9 KQYGPIFTYSTGNKQFLYVSRPEMVKEInlcvsldLGKPSYLKKTLKPLFGG-GILT-----SNGPHWAHQRKIIAPEFF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 139 SGRLKEMFPIINQFTDVLVRN----MRQGLGEGKPTSMKDIFGAYSMDVITATSFGvniDSLNNPQDPFVeKIKKLLKFD 214
Cdd:cd20640    83 LDKVKGMVDLMVDSAQPLLSSweerIDRAGGMAADIVVDEDLRAFSADVISRACFG---SSYSKGKEIFS-KLRELQKAV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 215 IFDPLFLSVTLFpFLTPVFDALNVSLFPRDVISFFTTSVERMKENRMKEKekqrvDFLQLMInsQNYKTKESHKALSDVE 294
Cdd:cd20640   159 SKQSVLFSIPGL-RHLPTKSNRKIWELEGEIRSLILEIVKEREEECDHEK-----DLLQAIL--EGARSSCDKKAEAEDF 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 295 IVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATyDTLLQMEYLDMVVNETLRLYPIAGRLE 374
Cdd:cd20640   231 IVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPPDA-DSLSRMKTVTMVIQETLRLYPPAAFVS 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 375 RVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQDSIN-PYMYLPFGSGPRNCIGMRFALINM 452
Cdd:cd20640   310 REALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACKpPHSYMPFGAGARTCLGQNFAMAEL 389
                         410
                  ....*....|....*
gi 1720412152 453 KVALVRVLQNFTVQP 467
Cdd:cd20640   390 KVLVSLILSKFSFTL 404
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
79-473 1.14e-53

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: 185.85  E-value: 1.14e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  79 QPVLAITDPDIIKTVLVKE-----CYSTFTNRRRFGPVGILKKaisisENEEWKRIRALLSPTFTSGRLKE-MFPIInqf 152
Cdd:cd11043    16 RPTVVSADPEANRFILQNEgklfvSWYPKSVRKLLGKSSLLTV-----SGEEHKRLRGLLLSFLGPEALKDrLLGDI--- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 153 tDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNidslnnpQDPFVEKIKKLlkFDIFDPLFLSVTL-FPFlTP 231
Cdd:cd11043    88 -DELVRQHLDSWWRGKSVVVLELAKKMTFELICKLLLGID-------PEEVVEELRKE--FQAFLEGLLSFPLnLPG-TT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 232 VFDALNVSLFPRDVISffttsvERMKENRM-KEKEKQRVDFLQLMINSQNyktkESHKALSDVEIVAQSVIFIFAGYETT 310
Cdd:cd11043   157 FHRALKARKRIRKELK------KIIEERRAeLEKASPKGDLLDVLLEEKD----EDGDSLTDEEILDNILTLLFAGHETT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 311 SSALSFALYLLAIHPDVQKKL---QDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLF 387
Cdd:cd11043   227 STTLTLAVKFLAENPKVLQELleeHEEIAKRKEEGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEYKGYT 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 388 IPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSinPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQP 467
Cdd:cd11043   307 IPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGV--PYTFLPFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEV 384

                  ....*.
gi 1720412152 468 CKETEI 473
Cdd:cd11043   385 VPDEKI 390
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
68-474 2.02e-52

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: 183.18  E-value: 2.02e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKEcYSTFTNRRRFGPVGILK---KAISISE-NEEWKRIR-----ALLSPTFT 138
Cdd:cd11027     1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKK-SADFAGRPKLFTFDLFSrggKDIAFGDySPTWKLHRklahsALRLYASG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 139 SGRLKEmfpIINQFTDVLVRNMRQGlgEGKPTSMKDIFGAYSMDVITATSFGVNIDslnnPQDPFVEKIKKLLKfDIFDP 218
Cdd:cd11027    80 GPRLEE---KIAEEAEKLLKRLASQ--EGQPFDPKDELFLAVLNVICSITFGKRYK----LDDPEFLRLLDLND-KFFEL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 219 L--FLSVTLFPFLtpvfdalnvSLFPRDVISFFTTSVERM--------KENRMKEKEKQRVDFLQLMINSQNYKTKE--- 285
Cdd:cd11027   150 LgaGSLLDIFPFL---------KYFPNKALRELKELMKERdeilrkklEEHKETFDPGNIRDLTDALIKAKKEAEDEgde 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 286 SHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLR 365
Cdd:cd11027   221 DSGLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 366 LYPIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF-SKKNQDSINPYMYLPFGSGPRNCI 443
Cdd:cd11027   301 LSSVVPlALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFlDENGKLVPKPESFLPFSAGRRVCL 380
                         410       420       430
                  ....*....|....*....|....*....|.
gi 1720412152 444 GMRFALINMKVALVRVLQNFTVQPCKETEIP 474
Cdd:cd11027   381 GESLAKAELFLFLARLLQKFRFSPPEGEPPP 411
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
68-470 2.08e-52

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: 183.16  E-value: 2.08e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKEcySTFTNRRRFGPVG--ILKKAISIS---ENEEWKRIRALLSPTFTSGRL 142
Cdd:cd11065     1 YGPIISLKVGGQTIIVLNSPKAAKDLLEKR--SAIYSSRPRMPMAgeLMGWGMRLLlmpYGPRWRLHRRLFHQLLNPSAV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 143 KEMFPIINQFTDVLVRNMRQglgegKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLkFDIFDPLFLS 222
Cdd:cd11065    79 RKYRPLQELESKQLLRDLLE-----SPDDFLDHIRRYAASIILRLAYGYRVPSYDDPLLRDAEEAMEGF-SEAGSPGAYL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 223 VTLFPFLtpvfdalnvslfpRDVISFFTTSVERmKENRMKEKEKQRV----DFLQLMINSQNYKT---------KESHKA 289
Cdd:cd11065   153 VDFFPFL-------------RYLPSWLGAPWKR-KARELRELTRRLYegpfEAAKERMASGTATPsfvkdlleeLDKEGG 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 290 LSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPI 369
Cdd:cd11065   219 LSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPV 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 370 A-GRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPY--MYLPFGSGPRNCIGMR 446
Cdd:cd11065   299 ApLGIPHALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGTPDPPdpPHFAFGFGRRICPGRH 378
                         410       420
                  ....*....|....*....|....
gi 1720412152 447 FALINMKVALVRVLQNFTVQPCKE 470
Cdd:cd11065   379 LAENSLFIAIARLLWAFDIKKPKD 402
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
77-463 5.41e-52

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: 181.98  E-value: 5.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  77 GRQPVLAITDPDIIKTVLvKECYSTFTNRRRFGPVGIL---KKAISISEN-EEWKRIRA-----LLSP----TFTSGRLK 143
Cdd:cd20618     9 GSVPTVVVSSPEMAKEVL-KTQDAVFASRPRTAAGKIFsynGQDIVFAPYgPHWRHLRKictleLFSAkrleSFQGVRKE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 144 EMfpiinqftDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLkFDIFDPL--FL 221
Cdd:cd20618    88 EL--------SHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEAREFKELI-DEAFELAgaFN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 222 SVTLFPFLTPVFDALNVSLFPR---DVISFFTTSVERMKENRMKEKEKQRVDFLQLMInsqnyKTKESHKALSDVEIVAq 298
Cdd:cd20618   159 IGDYIPWLRWLDLQGYEKRMKKlhaKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLL-----LDLDGEGKLSDDNIKA- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 299 sVI--FIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRL-ER 375
Cdd:cd20618   233 -LLldMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPLLlPH 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 376 VCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINP--YMYLPFGSGPRNCIGMRFALINMK 453
Cdd:cd20618   312 ESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVKGqdFELLPFGSGRRMCPGMPLGLRMVQ 391
                         410
                  ....*....|
gi 1720412152 454 VALVRVLQNF 463
Cdd:cd20618   392 LTLANLLHGF 401
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
67-491 9.46e-50

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: 176.10  E-value: 9.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGrqPVLA--ITDPDIIKTVLVKE-------CYSTFTNRR--RFGPVGILKkaisiSENEEWKRIRALLSP 135
Cdd:cd20648     4 KYGPVWKASFG--PILTvhVADPALIEQVLRQEgkhpvrsDLSSWKDYRqlRGHAYGLLT-----AEGEEWQRLRSLLAK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 136 TFTSGRLKEMFP-IINQFTDVLVRNMRQGLGEGKPTSMKDI---FGAYSMDVITATSFGVNIDSLNnPQDP-----FVEK 206
Cdd:cd20648    77 HMLKPKAVEAYAgVLNAVVTDLIRRLRRQRSRSSPGVVKDIageFYKFGLEGISSVLFESRIGCLE-ANVPeetetFIQS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 207 IKKllkfdIFDPLFLSVTLFPFLTPVFDAlNVSLFPRD---VISFFTTSVE-RMKENRMK--EKEKQRVDFLQLMINSQN 280
Cdd:cd20648   156 INT-----MFVMTLLTMAMPKWLHRLFPK-PWQRFCRSwdqMFAFAKGHIDrRMAEVAAKlpRGEAIEGKYLTYFLAREK 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 281 yktkeshkaLSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVV 360
Cdd:cd20648   230 ---------LPMKSIYGNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVV 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 361 NETLRLYP-IAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNqDSINPYMYLPFGSGP 439
Cdd:cd20648   301 KEVLRLYPvIPGNARVIPDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWLGKG-DTHHPYASLPFGFGK 379
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720412152 440 RNCIGMRFALINMKVALVRVLQNFTVQPCKETEiPLKLSKQGLLQPENPLLL 491
Cdd:cd20648   380 RSCIGRRIAELEVYLALARILTHFEVRPEPGGS-PVKPMTRTLLVPERSINL 430
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
282-465 2.43e-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: 174.43  E-value: 2.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 282 KTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAlpNKAPATYDTLLQMEYLDMVVN 361
Cdd:cd11045   199 AEDEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL--GKGTLDYEDLGQLEVTDWVFK 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 362 ETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFS-KKNQDSINPYMYLPFGSGPR 440
Cdd:cd11045   277 EALRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSpERAEDKVHRYAWAPFGGGAH 356
                         170       180
                  ....*....|....*....|....*
gi 1720412152 441 NCIGMRFALINMKVALVRVLQNFTV 465
Cdd:cd11045   357 KCIGLHFAGMEVKAILHQMLRRFRW 381
PLN02290 PLN02290
cytokinin trans-hydroxylase
32-463 1.50e-48

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 175.00  E-value: 1.50e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  32 IFKKLGIPGPKPLPFLGTI-----LAYQKGFWECDIQCH--------------KKYGKMWGLYDGRQPVLAITDPDIIKT 92
Cdd:PLN02290   38 IMERQGVRGPKPRPLTGNIldvsaLVSQSTSKDMDSIHHdivgrllphyvawsKQYGKRFIYWNGTEPRLCLTETELIKE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  93 VLVKecYSTFTNR---RRFGPVGILKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGEGKp 169
Cdd:PLN02290  118 LLTK--YNTVTGKswlQQQGTKHFIGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESGQ- 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 170 TSMKdiFGAY----SMDVITATSFGVNIDslnnpqdpfveKIKKLlkFDIFDPL------------FLSVTLFPfltpvf 233
Cdd:PLN02290  195 TEVE--IGEYmtrlTADIISRTEFDSSYE-----------KGKQI--FHLLTVLqrlcaqatrhlcFPGSRFFP------ 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 234 dalnvSLFPRDVISFfTTSVER-MKENRMKEKEKQRV--------DFLQLMINSQNyKTKESHKALSDVEIVAQSVIFIF 304
Cdd:PLN02290  254 -----SKYNREIKSL-KGEVERlLMEIIQSRRDCVEIgrsssygdDLLGMLLNEME-KKRSNGFNLNLQLIMDECKTFFF 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 305 AGYETTSSALSFALYLLAIHPDVQKKLQDEIdAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEIN 384
Cdd:PLN02290  327 AGHETTALLLTWTLMLLASNPTWQDKVRAEV-AEVCGGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 385 GLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQDSINPYMylPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:PLN02290  406 DLHIPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHFI--PFAAGPRNCIGQAFAMMEAKIILAMLISKF 483
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
68-470 1.36e-47

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: 170.32  E-value: 1.36e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKECYSTFTNRRRFGPVGILKKAISISENEEWKRIRALLSPTFTSGRLKEMFP 147
Cdd:cd20641    11 YGETFLYWQGTTPRICISDHELAKQVLSDKFGFFGKSKARPEILKLSGKGLVFVNGDDWVRHRRVLNPAFSMDKLKSMTQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 148 IINQFTDVLVRNMRQGL----GEGKPTSMKDIFGAYSMDVITATSFGvniDSLNNPQDPFVEKiKKLLKFDIFDPLFLSV 223
Cdd:cd20641    91 VMADCTERMFQEWRKQRnnseTERIEVEVSREFQDLTADIIATTAFG---SSYAEGIEVFLSQ-LELQKCAAASLTNLYI 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 224 TLFPFLtPVFDALNVSLFPRDVISffttSVERMKENRMKEKEKQR-VDFLQLMIN--SQNYKTKESHKALSDVEIVAQSV 300
Cdd:cd20641   167 PGTQYL-PTPRNLRVWKLEKKVRN----SIKRIIDSRLTSEGKGYgDDLLGLMLEaaSSNEGGRRTERKMSIDEIIDECK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 301 IFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTD 380
Cdd:cd20641   242 TFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVINIARRASED 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 381 VEINGLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKK-NQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVR 458
Cdd:cd20641   322 MKLGGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGvSRAATHPNALLSFSLGPRACIGQNFAMIEAKTVLAM 401
                         410
                  ....*....|..
gi 1720412152 459 VLQNFTVQPCKE 470
Cdd:cd20641   402 ILQRFSFSLSPE 413
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
66-467 1.97e-46

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: 167.14  E-value: 1.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  66 KKYGKMWGLYDGRQPVLAITDPDIIKTVLVKE----CYSTFTNRRR--------FGPVgilkkaisISENEEWKRIRALL 133
Cdd:cd20646     2 KIYGPIWKSKFGPYDIVNVASAELIEQVLRQEgkypMRSDMPHWKEhrdlrghaYGPF--------TEEGEKWYRLRSVL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 134 SPTFTsgRLKEMF---PIINQFTDVLVRNMRQgLGEGKPTS-----MKDIFGAYSMDVITATSFGVNIDSLNN--PQDP- 202
Cdd:cd20646    74 NQRML--KPKEVSlyaDAINEVVSDLMKRIEY-LRERSGSGvmvsdLANELYKFAFEGISSILFETRIGCLEKeiPEETq 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 203 -FVEKIKKLLKFDIFdplflsVTLFP-FLTPVFDALNVSLFPRDVISFFTTSV--ERMKE--NRMKEKEKQRVDFLQLMI 276
Cdd:cd20646   151 kFIDSIGEMFKLSEI------VTLLPkWTRPYLPFWKRYVDAWDTIFSFGKKLidKKMEEieERVDRGEPVEGEYLTYLL 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 277 NSQNYKTKESHKALSDVeivaqsvifIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYL 356
Cdd:cd20646   225 SSGKLSPKEVYGSLTEL---------LLAGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLL 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 357 DMVVNETLRLYPIA---GRLerVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYL 433
Cdd:cd20646   296 KAVIKETLRLYPVVpgnARV--IVEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKHHPFGSI 373
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1720412152 434 PFGSGPRNCIGMRFALINMKVALVRVLQNFTVQP 467
Cdd:cd20646   374 PFGYGVRACVGRRIAELEMYLALSRLIKRFEVRP 407
PTZ00404 PTZ00404
cytochrome P450; Provisional
13-473 3.54e-46

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 167.59  E-value: 3.54e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  13 MLLATSLVLLYLYGTHSHGI-FKKLG---IPGPKPLPFLGTILAYQKGFWECDIQCHKKYGKMWGLYDGRQPVLAITDPD 88
Cdd:PTZ00404    2 MLFNIILFLFIFYIIHNAYKkYKKIHkneLKGPIPIPILGNLHQLGNLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  89 IIKTVLVKEcYSTFTNRRRFGPV--GILKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGE 166
Cdd:PTZ00404   82 LIREMFVDN-FDNFSDRPKIPSIkhGTFYHGIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQVDVLIESMKKIESS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 167 GKPTSMKDIFGAYSMDVITATSFGVNI---DSLNNPQ-----DPFVEKIKKLLKFDIFDPLFLSVTLFPFLTPVFDalnv 238
Cdd:PTZ00404  161 GETFEPRYYLTKFTMSAMFKYIFNEDIsfdEDIHNGKlaelmGPMEQVFKDLGSGSLFDVIEITQPLYYQYLEHTD---- 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 239 SLFPRdVISFFttsVERMKENRMKEK-EKQRvDFLQLMINSqnYKTKESHKALSdveIVAQSVIFIFAGYETTSSALSFA 317
Cdd:PTZ00404  237 KNFKK-IKKFI---KEKYHEHLKTIDpEVPR-DLLDLLIKE--YGTNTDDDILS---ILATILDFFLAGVDTSATSLEWM 306
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 318 LYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAG-RLERVCKTDVEI-NGLFIPKGTVVM 395
Cdd:PTZ00404  307 VLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPfGLPRSTSNDIIIgGGHFIPKDAQIL 386
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412152 396 IPTFALHKDPKYWPEPEEFRPERFSKKNqdsiNPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEI 473
Cdd:PTZ00404  387 INYYSLGRNEKYFENPEQFDPSRFLNPD----SNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGKKI 460
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
127-466 7.15e-46

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: 165.47  E-value: 7.15e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 127 KRIRALLSpTFTSGRLKEMFPIINQFTDVLVRNmrqgLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLnnpqdpFVEK 206
Cdd:cd11042    66 EQLKFGLN-ILRRGKLRGYVPLIVEEVEKYFAK----WGESGEVDLFEEMSELTILTASRCLLGKEVREL------LDDE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 207 IKKLL-KFDI-FDPLFLsvtLFPFL-TPVFDALNVSlfpRDVIS-FFTtsvERMKENRMKEKEKQRvDFLQLMINSQnYK 282
Cdd:cd11042   135 FAQLYhDLDGgFTPIAF---FFPPLpLPSFRRRDRA---RAKLKeIFS---EIIQKRRKSPDKDED-DMLQTLMDAK-YK 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 283 TKEshkALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPATYDTLLQMEYLDMVVN 361
Cdd:cd11042   204 DGR---PLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLgDGDDPLTYDVLKEMPLLHACIK 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 362 ETLRLYPIAGRLERVCKTDVEIN--GLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKN--QDSINPYMYLPFGS 437
Cdd:cd11042   281 ETLRLHPPIHSLMRKARKPFEVEggGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRaeDSKGGKFAYLPFGA 360
                         330       340
                  ....*....|....*....|....*....
gi 1720412152 438 GPRNCIGMRFALINMKVALVRVLQNFTVQ 466
Cdd:cd11042   361 GRHRCIGENFAYLQIKTILSTLLRNFDFE 389
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
66-489 1.47e-43

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: 159.70  E-value: 1.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  66 KKYGKMWGLYDGRQPVLAITDPDIIKTVLVKE----------CYSTFTNRRrfgpvGILKKAISiSENEEWKRIRALLSP 135
Cdd:cd20647     2 REYGKIFKSHFGPQFVVSIADRDMVAQVLRAEgaapqranmeSWQEYRDLR-----GRSTGLIS-AEGEQWLKMRSVLRQ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 136 TFTsgRLKEMFPIINQFTDVL------VRNMRQGLGEGKP-TSMKDIFGAYSMDVITATSFGVNIDSLNN--PQDPfVEK 206
Cdd:cd20647    76 KIL--RPRDVAVYSGGVNEVVadlikrIKTLRSQEDDGETvTNVNDLFFKYSMEGVATILYECRLGCLENeiPKQT-VEY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 207 IKKL-LKFDIFDPLFLSVTLFPFLTPvFDALNVSLFPRDVISFFTTSVERMkENRMKEKEKQ-----RVD--FLQLMINS 278
Cdd:cd20647   153 IEALeLMFSMFKTTMYAGAIPKWLRP-FIPKPWEEFCRSWDGLFKFSQIHV-DNRLREIQKQmdrgeEVKggLLTYLLVS 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 279 qnyktkeshKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDM 358
Cdd:cd20647   231 ---------KELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRA 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 359 VVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKK-NQDSINPYMYLPFGS 437
Cdd:cd20647   302 LLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKdALDRVDNFGSIPFGY 381
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720412152 438 GPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEiPLKLSKQGLLQPENPL 489
Cdd:cd20647   382 GIRSCIGRRIAELEIHLALIQLLQNFEIKVSPQTT-EVHAKTHGLLCPGGSI 432
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
77-463 7.96e-41

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: 152.38  E-value: 7.96e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  77 GRQPVLAITDPDIiktvlVKECYST----FTNRRrfgpvgILKKAISISENEE----------WKRIR-----ALLSP-- 135
Cdd:cd20654     9 GSHPTLVVSSWEM-----AKECFTTndkaFSSRP------KTAAAKLMGYNYAmfgfapygpyWRELRkiatlELLSNrr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 136 --TFTSGRLKEMFPIINQFTDVLVRNmrQGLGEGKPTSMKDIFGAYSMDVITAT-----SFGVNIDSLNNPqdpfVEKIK 208
Cdd:cd20654    78 leKLKHVRVSEVDTSIKELYSLWSNN--KKGGGGVLVEMKQWFADLTFNVILRMvvgkrYFGGTAVEDDEE----AERYK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 209 KLLK--FDIFDpLFLSVTLFPFLTpVFDalnvslfprdvisfFTTSVERMK---------------ENRMKEKEKQRV-- 269
Cdd:cd20654   152 KAIRefMRLAG-TFVVSDAIPFLG-WLD--------------FGGHEKAMKrtakeldsileewleEHRQKRSSSGKSkn 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 270 ---DFLQLMINSQNYKTKESHKAlsDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPAT 346
Cdd:cd20654   216 dedDDDVMMLSILEDSQISGYDA--DTVIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVE 293
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 347 YDTLLQMEYLDMVVNETLRLYPiAGRL--ERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF--SKK 422
Cdd:cd20654   294 ESDIKNLVYLQAIVKETLRLYP-PGPLlgPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFltTHK 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 1720412152 423 NQDSI-NPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd20654   373 DIDVRgQNFELIPFGSGRRSCPGVSFGLQVMHLTLARLLHGF 414
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
67-463 4.94e-40

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: 149.70  E-value: 4.94e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  67 KYGKMWGLYDGRQPVLAITDPDIIKTVLVKEcYSTFTNRRRFGPVGIL----KKAISISE-NEEWKRIRA-LLSPTFTSG 140
Cdd:cd11075     1 KYGPIFTLRMGSRPLIVVASRELAHEALVQK-GSSFASRPPANPLRVLfssnKHMVNSSPyGPLWRTLRRnLVSEVLSPS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 141 RLKEMFPIINQFTDVLVRNMRQGLGEG-KPTSMKDIFgAYSM-DVITATSFGVNIDSlnnpqdpfvEKIKKL-------- 210
Cdd:cd11075    80 RLKQFRPARRRALDNLVERLREEAKENpGPVNVRDHF-RHALfSLLLYMCFGERLDE---------ETVRELervqrell 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 211 ---LKFDIFDplflsvtLFPFLTPVF------DALNVSlfpRDVISFFTTSVERMKEnRMKEKEKQRVDFLQLMINSQNY 281
Cdd:cd11075   150 lsfTDFDVRD-------FFPALTWLLnrrrwkKVLELR---RRQEEVLLPLIRARRK-RRASGEADKDYTDFLLLDLLDL 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 282 KTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVN 361
Cdd:cd11075   219 KEEGGERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 362 ETLRLYPIAGRL--ERVCKtDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF-SKKNQDSINP----YMYLP 434
Cdd:cd11075   299 ETLRRHPPGHFLlpHAVTE-DTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFlAGGEAADIDTgskeIKMMP 377
                         410       420
                  ....*....|....*....|....*....
gi 1720412152 435 FGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd11075   378 FGAGRRICPGLGLATLHLELFVARLVQEF 406
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
126-463 2.21e-39

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: 148.13  E-value: 2.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 126 WKRIRALLSPTFTSGRLKEMF-PIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPqdpfV 204
Cdd:cd20655    61 WKFMKKLCMTELLGPRALERFrPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGE----A 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 205 EKIKKLLK--FDIFDPLFLSVTLFPFltpvfDALNVSLFPR---DVISFFTTSVERM----KENRMKEKEKQRVDFLQLM 275
Cdd:cd20655   137 EEVRKLVKesAELAGKFNASDFIWPL-----KKLDLQGFGKrimDVSNRFDELLERIikehEEKRKKRKEGGSKDLLDIL 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 276 I------NSQNYKTKESHKALsdveIVAqsvIFIfAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDT 349
Cdd:cd20655   212 LdayedeNAEYKITRNHIKAF----ILD---LFI-AGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESD 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 350 LLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF--SKKNQDSI 427
Cdd:cd20655   284 LPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFlaSSRSGQEL 363
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1720412152 428 NP----YMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd20655   364 DVrgqhFKLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCF 403
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
66-463 4.75e-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: 147.29  E-value: 4.75e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  66 KKYGKMWGLYDGRQPVLAITDPDIIKTVLVKECYStFTNRRRFGPVGILKKAISI----SENEEWKRIRALL-SPTFTSG 140
Cdd:cd11073     2 KKYGPIMSLKLGSKTTVVVSSPEAAREVLKTHDRV-LSGRDVPDAVRALGHHKSSivwpPYGPRWRMLRKICtTELFSPK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 141 RLKEMFPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNP-----QDpFVEKIKKLL-KFD 214
Cdd:cd11073    81 RLDATQPLRRRKVRELVRYVREKAGSGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDSEsgsefKE-LVREIMELAgKPN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 215 IFDplflsvtLFPFLTPvFD--------ALNVSLFprdvISFFTTSVERMKENRMKEKEKQRVDFLQLMINsqnyKTKES 286
Cdd:cd11073   160 VAD-------FFPFLKF-LDlqglrrrmAEHFGKL----FDIFDGFIDERLAEREAGGDKKKDDDLLLLLD----LELDS 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 287 HKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPATYDtLLQMEYLDMVVNETLR 365
Cdd:cd11073   224 ESELTRNHIKALLLDLFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIgKDKIVEESD-ISKLPYLQAVVKETLR 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 366 LYPIAGRL-ERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSI-NPYMYLPFGSGPRNCI 443
Cdd:cd11073   303 LHPPAPLLlPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKgRDFELIPFGSGRRICP 382
                         410       420
                  ....*....|....*....|
gi 1720412152 444 GMRFALINMKVALVRVLQNF 463
Cdd:cd11073   383 GLPLAERMVHLVLASLLHSF 402
PLN02936 PLN02936
epsilon-ring hydroxylase
66-466 4.80e-39

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 148.40  E-value: 4.80e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  66 KKYGKMWGLYDGRQPVLAITDPDIIKTVLVKecYSTFTNRRRFGPVG--ILKKAISISENEEWKRIRALLSPTFTSGRLK 143
Cdd:PLN02936   47 NEYGPVYRLAAGPRNFVVVSDPAIAKHVLRN--YGSKYAKGLVAEVSefLFGSGFAIAEGELWTARRRAVVPSLHRRYLS 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 144 EMFP-IINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNpQDPFVEKIKKLLKfdifDPLFLS 222
Cdd:PLN02936  125 VMVDrVFCKCAERLVEKLEPVALSGEAVNMEAKFSQLTLDVIGLSVFNYNFDSLTT-DSPVIQAVYTALK----EAETRS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 223 VTLFPFLTpvFDALNVsLFPRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSQNYKTKE----------SHKALSD 292
Cdd:PLN02936  200 TDLLPYWK--VDFLCK-ISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGEVIEGEEYVNDSdpsvlrfllaSREEVSS 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 293 VEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPaTYDTLLQMEYLDMVVNETLRLYPIAGR 372
Cdd:PLN02936  277 VQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPP-TYEDIKELKYLTRCINESMRLYPHPPV 355
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 373 LERVCKT-DVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKN---QDSINPYMYLPFGSGPRNCIGMRFA 448
Cdd:PLN02936  356 LIRRAQVeDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDLDGpvpNETNTDFRYIPFSGGPRKCVGDQFA 435
                         410
                  ....*....|....*...
gi 1720412152 449 LINMKVALVRVLQNFTVQ 466
Cdd:PLN02936  436 LLEAIVALAVLLQRLDLE 453
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
118-470 6.36e-39

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: 147.83  E-value: 6.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 118 ISISENEEWKR----IRALLSPTF---TSGrlkemfPIINQFTDVLVR--NMRQGLGEGKPTSM-KDIFGAySMDVITAT 187
Cdd:cd20622    54 LVKSTGPAFRKhrslVQDLMTPSFlhnVAA------PAIHSKFLDLIDlwEAKARLAKGRPFSAkEDIHHA-ALDAIWAF 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 188 SFGVNID-SLNNPQDPFVEKIKKL---------LKFDI--FDPLFLSVTlfpFLTPVFDALNVSLFPRdvISFFTTS--- 252
Cdd:cd20622   127 AFGINFDaSQTRPQLELLEAEDSTilpagldepVEFPEapLPDELEAVL---DLADSVEKSIKSPFPK--LSHWFYRnqp 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 253 ----VERMKENRMKEKEKQRVDFLQLMINSQNYKT--------------KESHK-ALSDVEIVAQSVIFIFAGYETTSSA 313
Cdd:cd20622   202 syrrAAKIKDDFLQREIQAIARSLERKGDEGEVRSavdhmvrrelaaaeKEGRKpDYYSQVIHDELFGYLIAGHDTTSTA 281
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 314 LSFALYLLAIHPDVQKKLQDEIDAALP----NKAPATYDTLLQME--YLDMVVNETLRLYPIAGRLERVCKTDVEINGLF 387
Cdd:cd20622   282 LSWGLKYLTANQDVQSKLRKALYSAHPeavaEGRLPTAQEIAQARipYLDAVIEEILRCANTAPILSREATVDTQVLGYS 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 388 IPKGTVVM----IPTF-----------------ALHKDPKYW--PEPEEFRPERFSKKNQDS------INPYMYLPFGSG 438
Cdd:cd20622   362 IPKGTNVFllnnGPSYlsppieidesrrssssaAKGKKAGVWdsKDIADFDPERWLVTDEETgetvfdPSAGPTLAFGLG 441
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1720412152 439 PRNCIGMRFALINMKVALVRVLQNFTVQPCKE 470
Cdd:cd20622   442 PRGCFGRRLAYLEMRLIITLLVWNFELLPLPE 473
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
253-474 1.01e-38

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: 146.28  E-value: 1.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 253 VERMKENRMKEKEKQRVDFLQLMInsQNYKTKESHkalsDVEIVAQSVIFI-FAGYETTSSALSFALYLLAIHPDVQKKL 331
Cdd:cd11041   191 IERRRKLKKGPKEDKPNDLLQWLI--EAAKGEGER----TPYDLADRQLALsFAAIHTTSMTLTHVLLDLAAHPEYIEPL 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 332 QDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGR-LERVCKTDVEI-NGLFIPKGTVVMIPTFALHKDPKYWP 409
Cdd:cd11041   265 REEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVsLRRKVLKDVTLsDGLTLPKGTRIAVPAHAIHRDPDIYP 344
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720412152 410 EPEEFRPERFSKKNQD----------SINPyMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEIP 474
Cdd:cd11041   345 DPETFDGFRFYRLREQpgqekkhqfvSTSP-DFLGFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGERP 418
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
68-474 3.61e-38

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: 144.48  E-value: 3.61e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKEcYSTFTNRrrfgPVGILKKAIS-----IS---ENEEWKRIRALLSPTFTS 139
Cdd:cd20674     1 YGPIYRLRLGLQDVVVLNSKRTIREALVRK-WADFAGR----PHSYTGKLVSqggqdLSlgdYSLLWKAHRKLTRSALQL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 140 GRLKEMFPIINQFTDVLVRNMRQGLGEgkPTsmkDIFGAYSM---DVITATSFGVNIDslnnpQDPFVEKIKKLLKfDIF 216
Cdd:cd20674    76 GIRNSLEPVVEQLTQELCERMRAQAGT--PV---DIQEEFSLltcSIICCLTFGDKED-----KDTLVQAFHDCVQ-ELL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 217 D----PLFLSVTLFPFL----TPVFDALNVSLFPRDviSFFTTSVERMKENRMkekEKQRVDFLQLMINSQNYKTKES-H 287
Cdd:cd20674   145 KtwghWSIQALDSIPFLrffpNPGLRRLKQAVENRD--HIVESQLRQHKESLV---AGQWRDMTDYMLQGLGQPRGEKgM 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 288 KALSDvEIVAQSVIFIF-AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRL 366
Cdd:cd20674   220 GQLLE-GHVHMAVVDLFiGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 367 YPIAGRLERVCKT-DVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF---SKKNQDSinpymyLPFGSGPRNC 442
Cdd:cd20674   299 RPVVPLALPHRTTrDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFlepGAANRAL------LPFGCGARVC 372
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1720412152 443 IGMRFALINMKVALVRVLQNFTVQPCKETEIP 474
Cdd:cd20674   373 LGEPLARLELFVFLARLLQAFTLLPPSDGALP 404
PLN02738 PLN02738
carotene beta-ring hydroxylase
68-496 8.38e-38

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 146.60  E-value: 8.38e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLV--KECYSTftnrrrfgpvGILK--------KAISISENEEWKRIRALLSPTF 137
Cdd:PLN02738  164 YGGIFRLTFGPKSFLIVSDPSIAKHILRdnSKAYSK----------GILAeilefvmgKGLIPADGEIWRVRRRAIVPAL 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 138 TSGRLKEMFPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNpQDPFVEKIKKLLKfdifD 217
Cdd:PLN02738  234 HQKYVAAMISLFGQASDRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNYDFDSLSN-DTGIVEAVYTVLR----E 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 218 PLFLSVTLFPF--------LTPVFDALNVSL-FPRDVISFFTTSVERMKENR--------MKEKEKQRVDFLqlmINSQN 280
Cdd:PLN02738  309 AEDRSVSPIPVweipiwkdISPRQRKVAEALkLINDTLDDLIAICKRMVEEEelqfheeyMNERDPSILHFL---LASGD 385
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 281 yktKESHKALSDveivaQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPaTYDTLLQMEYLDMVV 360
Cdd:PLN02738  386 ---DVSSKQLRD-----DLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFP-TIEDMKKLKYTTRVI 456
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 361 NETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSkknQDSINP------YMYLP 434
Cdd:PLN02738  457 NESLRLYPQPPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWP---LDGPNPnetnqnFSYLP 533
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412152 435 FGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEiPLKLSKQGLLQPENPLLLKVVSR 496
Cdd:PLN02738  534 FGGGPRKCVGDMFASFENVVATAMLVRRFDFQLAPGAP-PVKMTTGATIHTTEGLKMTVTRR 594
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
68-470 1.89e-37

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: 142.84  E-value: 1.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKECySTFTNRRRFGPVGILK---KAISISE-NEEWKRIRALLSPTFT----- 138
Cdd:cd20673     1 YGPIYSLRMGSHTTVIVGHHQLAKEVLLKKG-KEFSGRPRMVTTDLLSrngKDIAFADySATWQLHRKLVHSAFAlfgeg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 139 SGRLKEmfpIINQFTDVLVRNMRQGLGEGKPTSmKDIFGAYSmDVITATSFGVNIDslnnPQDPFVEKIKKLLKfDIFDP 218
Cdd:cd20673    80 SQKLEK---IICQEASSLCDTLATHNGESIDLS-PPLFRAVT-NVICLLCFNSSYK----NGDPELETILNYNE-GIVDT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 219 LFLS--VTLFPFLTpvfdalnvsLFPrdvisffTTSVERMKEN-RMKEK------EKQRVDF------------LQLMIN 277
Cdd:cd20673   150 VAKDslVDIFPWLQ---------IFP-------NKDLEKLKQCvKIRDKllqkklEEHKEKFssdsirdlldalLQAKMN 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 278 SQNYKTKESH--KALSDVEIVAqSVIFIF-AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQME 354
Cdd:cd20673   214 AENNNAGPDQdsVGLSDDHILM-TVGDIFgAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLP 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 355 YLDMVVNETLRLYPIAGRL-ERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF--SKKNQDSINPYM 431
Cdd:cd20673   293 LLEATIREVLRIRPVAPLLiPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFldPTGSQLISPSLS 372
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1720412152 432 YLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQ-------PCKE 470
Cdd:cd20673   373 YLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLEvpdggqlPSLE 418
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
39-463 1.37e-35

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 138.80  E-value: 1.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  39 PGPKPLPFLGTILAYQKGFWECDIQCHKKYGKMWGLYDGRQPVLAITDPDIIKTVLVKEcYSTFTNRRR----------- 107
Cdd:PLN03112   35 PGPPRWPIVGNLLQLGPLPHRDLASLCKKYGPLVYLRLGSVDAITTDDPELIREILLRQ-DDVFASRPRtlaavhlaygc 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 108 ----FGPVGilkkaisisenEEWKRIRAL-LSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMD 182
Cdd:PLN03112  114 gdvaLAPLG-----------PHWKRMRRIcMEHLLTTKRLESFAKHRAEEARHLIQDVWEAAQTGKPVNLREVLGAFSMN 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 183 VIT-----ATSFGVNIDSLNNPQDpFVEKIKKLLKfdifdpLFLSVTLFPFLtPVFDALNVSLFPRD-------VISFFT 250
Cdd:PLN03112  183 NVTrmllgKQYFGAESAGPKEAME-FMHITHELFR------LLGVIYLGDYL-PAWRWLDPYGCEKKmrevekrVDEFHD 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 251 TSVERMKENR-MKEKEKQRVDFLQLMINSQNYKTKEShkaLSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQK 329
Cdd:PLN03112  255 KIIDEHRRARsGKLPGGKDMDFVDVLLSLPGENGKEH---MDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLR 331
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 330 KLQDEIDAAL-PNKAPATYDtLLQMEYLDMVVNETLRLYPiAG--RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPK 406
Cdd:PLN03112  332 KIQEELDSVVgRNRMVQESD-LVHLNYLRCVVRETFRMHP-AGpfLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTK 409
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412152 407 YWPEPEEFRPERF-----SKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:PLN03112  410 IWDDVEEFRPERHwpaegSRVEISHGPDFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCF 471
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
65-489 1.83e-35

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: 136.86  E-value: 1.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  65 HKKYGKMWGLYDGRQPVLAITDPDIIKTVLVKEcySTFTNRRRFGP-----------VGILkkaisISENEEWKRIRA-- 131
Cdd:cd20645     1 HKKFGKIFRMKLGSFESVHIGSPCLLEALYRKE--SAYPQRLEIKPwkayrdyrdeaYGLL-----ILEGQEWQRVRSaf 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 132 ---LLSPtftsgrlKEMFPIINQFTDVLVRNM-RQGLGEGKPTSMKDI---FGAYSMD----VITATSFGVNIDSLNNPQ 200
Cdd:cd20645    74 qkkLMKP-------KEVMKLDGKINEVLADFMgRIDELCDETGRVEDLyseLNKWSFEticlVLYDKRFGLLQQNVEEEA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 201 DPFVEKIKKLLKFdiFDPLFLsvtlfpflTPV--FDALNVSLFPRDVISF---FTTSVERMKENRMKEKEKQRVDFLQLM 275
Cdd:cd20645   147 LNFIKAIKTMMST--FGKMMV--------TPVelHKRLNTKVWQDHTEAWdniFKTAKHCIDKRLQRYSQGPANDFLCDI 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 276 INSQNYKTKESHKALSDVEIvaqsvififAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEY 355
Cdd:cd20645   217 YHDNELSKKELYAAITELQI---------GGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPY 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 356 LDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKnQDSINPYMYLPF 435
Cdd:cd20645   288 LKACLKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQE-KHSINPFAHVPF 366
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720412152 436 GSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETeiPLKLSKQGLLQPENPL 489
Cdd:cd20645   367 GIGKRMCIGRRLAELQLQLALCWIIQKYQIVATDNE--PVEMLHSGILVPSREL 418
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
172-489 3.77e-35

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: 136.30  E-value: 3.77e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 172 MKDIFGAYSMDVITATSFGVNIDSLNNPQDpfVEKIKKLLK--FDIFDPLFLSvTLFPFLTPvFDALNV-----SLFPRd 244
Cdd:cd11076   107 VRKHLQRASLNNIMGSVFGRRYDFEAGNEE--AEELGEMVRegYELLGAFNWS-DHLPWLRW-LDLQGIrrrcsALVPR- 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 245 VISFFTTSVErmkENRMKEKEKQRVDF------LQLminsqnyktkESHKALSDVEIVAQSVIFIFAGYETTSSALSFAL 318
Cdd:cd11076   182 VNTFVGKIIE---EHRAKRSNRARDDEddvdvlLSL----------QGEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIM 248
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 319 YLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPiAGRL---ERVCKTDVEINGLFIPKGTVVM 395
Cdd:cd11076   249 ARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHP-PGPLlswARLAIHDVTVGGHVVPAGTTAM 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 396 IPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYM-----YLPFGSGPRNCIG--MRFALINMKVAlvRVLQNF--TVQ 466
Cdd:cd11076   328 VNMWAITHDPHVWEDPLEFKPERFVAAEGGADVSVLgsdlrLAPFGAGRRVCPGkaLGLATVHLWVA--QLLHEFewLPD 405
                         330       340
                  ....*....|....*....|....*
gi 1720412152 467 PCKETEIP--LKLSkqglLQPENPL 489
Cdd:cd11076   406 DAKPVDLSevLKLS----CEMKNPL 426
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
68-482 5.34e-35

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: 135.67  E-value: 5.34e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKECySTFTNRRRFGPVGILKKAISI---SENEEWKRIRALLSPT---FTSGR 141
Cdd:cd20666     1 YGNIFSLFIGSQLVVVLNDFESVREALVQKA-EVFSDRPSVPLVTILTKGKGIvfaPYGPVWRQQRKFSHSTlrhFGLGK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 142 LKEMFPIINQFTDVLVRNMRQGlgeGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLKFDIFDPLFL 221
Cdd:cd20666    80 LSLEPKIIEEFRYVKAEMLKHG---GDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLMSRGLEISVNSAAIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 222 sVTLFPFL--TPVFDALNVSLFPRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMInsqnyktKESHKALSDVEIVAQS 299
Cdd:cd20666   157 -VNICPWLyyLPFGPFRELRQIEKDITAFLKKIIADHRETLDPANPRDFIDMYLLHI-------EEEQKNNAESSFNEDY 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 300 VIFI-----FAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPATYDTLlQMEYLDMVVNETLRLYPI-AGR 372
Cdd:cd20666   229 LFYIigdlfIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIgPDRAPSLTDKA-QMPFTEATIMEVQRMTVVvPLS 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 373 LERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINM 452
Cdd:cd20666   308 IPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMEL 387
                         410       420       430
                  ....*....|....*....|....*....|
gi 1720412152 453 KVALVRVLQNFTVQPCKETEIPLKLSKQGL 482
Cdd:cd20666   388 FLMFVSLMQSFTFLLPPNAPKPSMEGRFGL 417
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
68-476 2.15e-34

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: 133.84  E-value: 2.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKECYStFTNRRRFGPVGIL--KKAISISENEEWKRIR--ALLS-PTFTSGRl 142
Cdd:cd11026     1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQAEE-FSGRPPVPLFDRVtkGYGVVFSNGERWKQLRrfSLTTlRNFGMGK- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 143 KEMFPIINQFTDVLVRNMRQGlgEGKPTSMKDIFGAYSMDVITATSFGVNIDSlnnpQDPF----VEKIKKLLKF----- 213
Cdd:cd11026    79 RSIEERIQEEAKFLVEAFRKT--KGKPFDPTFLLSNAVSNVICSIVFGSRFDY----EDKEflklLDLINENLRLlsspw 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 214 ----DIFDPLFLSvtLFPFLTPVFDALNVslfprdVISFFTTSVERMKENRMKEKEKQRVD-FLQLMinsqnykTKESHK 288
Cdd:cd11026   153 gqlyNMFPPLLKH--LPGPHQKLFRNVEE------IKSFIRELVEEHRETLDPSSPRDFIDcFLLKM-------EKEKDN 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 289 ALS--DVEIVAQSVIFIF-AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPaTYDTLLQMEYLDMVVNETL 364
Cdd:cd11026   218 PNSefHEENLVMTVLDLFfAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIgRNRTP-SLEDRAKMPYTDAVIHEVQ 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 365 R---LYPIAgrLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRN 441
Cdd:cd11026   297 RfgdIVPLG--VPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRV 374
                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1720412152 442 CIGMRFALINMKVALVRVLQNFTVQ-PCKETEIPLK 476
Cdd:cd11026   375 CLGEGLARMELFLFFTSLLQRFSLSsPVGPKDPDLT 410
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
110-490 4.78e-33

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: 130.22  E-value: 4.78e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 110 PVGILKKaisisENEEWKRIRALLSPTFTSGR-LKEMFPIINQFTDVLVRNM-----RQGLGEGKPTSMKDIFgAYSMDV 183
Cdd:cd20643    55 KYGVLLK-----NGEAWRKDRLILNKEVLAPKvIDNFVPLLNEVSQDFVSRLhkrikKSGSGKWTADLSNDLF-RFALES 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 184 ITATSFGVNIDSLNNPQDP----FVEKIKKLLKfdifdplflsvTLFPFLTpvfdalnvslFPRDVISFFTTSVER---- 255
Cdd:cd20643   129 ICNVLYGERLGLLQDYVNPeaqrFIDAITLMFH-----------TTSPMLY----------IPPDLLRLINTKIWRdhve 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 256 ------MKENRMKEKEKQrvDFLQLMINSQNYKTKESHKALSD---VEIVAQSVIFIFAG-YETTSSALSFALYLLAIHP 325
Cdd:cd20643   188 awdvifNHADKCIQNIYR--DLRQKGKNEHEYPGILANLLLQDklpIEDIKASVTELMAGgVDTTSMTLQWTLYELARNP 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 326 DVQKKLQDEIDAAlPNKAPATYDTLLQM-EYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKD 404
Cdd:cd20643   266 NVQEMLRAEVLAA-RQEAQGDMVKMLKSvPLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRD 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 405 PKYWPEPEEFRPERFSKKNqdsINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEIPLKLSKqgLLQ 484
Cdd:cd20643   345 PTVFPKPEKYDPERWLSKD---ITHFRNLGFGFGPRQCLGRRIAETEMQLFLIHMLENFKIETQRLVEVKTTFDL--ILV 419

                  ....*.
gi 1720412152 485 PENPLL 490
Cdd:cd20643   420 PEKPIN 425
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
124-464 9.22e-33

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: 129.29  E-value: 9.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 124 EEWKRIRALLSPTFTSGRLKEMFPI----INQFTDVLVRNMRQGlgeGKPTSMKDIFgaysMDVITATSFGVNI-DSLNN 198
Cdd:cd11082    56 EEHKELRKSLLPLFTRKALGLYLPIqervIRKHLAKWLENSKSG---DKPIEMRPLI----RDLNLETSQTVFVgPYLDD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 199 PQDpfvekikkllKFDIFDPLFL-SVTLFPFLTPVFdALNVSLFPRDVI-SFFTTSVERMKEnRMKEKEKQR--VDF-LQ 273
Cdd:cd11082   129 EAR----------RFRIDYNYFNvGFLALPVDFPGT-ALWKAIQARKRIvKTLEKCAAKSKK-RMAAGEEPTclLDFwTH 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 274 LMINSQNYKTKES---HKALSDVEIvAQSVI-FIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNK-APATYD 348
Cdd:cd11082   197 EILEEIKEAEEEGeppPPHSSDEEI-AGTLLdFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDePPLTLD 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 349 TLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLF-IPKGTVVMIPTFALHKDPkyWPEPEEFRPERFSKKNQ-DS 426
Cdd:cd11082   276 LLEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLTEDYtVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQeDR 353
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1720412152 427 INPYMYLPFGSGPRNCIGMRFALINMKV--ALVRVLQNFT 464
Cdd:cd11082   354 KYKKNFLVFGAGPHQCVGQEYAINHLMLflALFSTLVDWK 393
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
258-463 1.42e-32

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: 128.88  E-value: 1.42e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 258 ENRMKEKEKQRVDFLQLMINSQNYKTKESHKAL---------------SDVEIVAQSVIFIFAGYETTSSALSFALYLLA 322
Cdd:cd20653   176 EKRVKKLAKRRDAFLQGLIDEHRKNKESGKNTMidhllslqesqpeyyTDEIIKGLILVMLLAGTDTSAVTLEWAMSNLL 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 323 IHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRL-ERVCKTDVEINGLFIPKGTVVMIPTFAL 401
Cdd:cd20653   256 NHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLvPHESSEDCKIGGYDIPRGTMLLVNAWAI 335
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412152 402 HKDPKYWPEPEEFRPERFSKKNQDSinpYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd20653   336 HRDPKLWEDPTKFKPERFEGEEREG---YKLIPFGLGRRACPGAGLAQRVVGLALGSLIQCF 394
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
68-467 1.29e-31

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: 126.07  E-value: 1.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKECySTFTNRRRfgpVGILKKA-----ISISENEEWKRIRALLSPT---FTS 139
Cdd:cd20664     1 YGSIFTVQMGTKKVVVLAGYKTVKEALVNHA-EAFGGRPI---IPIFEDFnkgygILFSNGENWKEMRRFTLTTlrdFGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 140 GRlKEMFPIINQFTDVLVRNMRQGlgEGKPTSMKDIFGAYSMDVITATSFGVNIDSlnnpQDPFVEKIKKLLKFDIF--- 216
Cdd:cd20664    77 GK-KTSEDKILEEIPYLIEVFEKH--KGKPFETTLSMNVAVSNIIASIVLGHRFEY----TDPTLLRMVDRINENMKltg 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 217 DPLFLSVTLFPFLTPvfdalnvslFPRDVISFFTTSVER--------MKENRMKEKEKQRvDFLQLMINSQNyKTKESHK 288
Cdd:cd20664   150 SPSVQLYNMFPWLGP---------FPGDINKLLRNTKELndflmetfMKHLDVLEPNDQR-GFIDAFLVKQQ-EEEESSD 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 289 ALSDVEIVAQSVIFIF-AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLlQMEYLDMVVNETLRLY 367
Cdd:cd20664   219 SFFHDDNLTCSVGNLFgAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQPQVEHRK-NMPYTDAVIHEIQRFA 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 368 PIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMR 446
Cdd:cd20664   298 NIVPmNLPHATTRDVTFRGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGET 377
                         410       420
                  ....*....|....*....|.
gi 1720412152 447 FALINMKVALVRVLQNFTVQP 467
Cdd:cd20664   378 LAKMELFLFFTSLLQRFRFQP 398
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
263-467 2.45e-31

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: 125.16  E-value: 2.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 263 EKEKQRVDFLQLMINSQNyktkesHKALSdVEIVAQSVI-FIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPN 341
Cdd:cd20616   199 EKLEDHMDFATELIFAQK------RGELT-AENVNQCVLeMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGE 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 342 KAPaTYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPkYWPEPEEFRPERFSK 421
Cdd:cd20616   272 RDI-QNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFEK 349
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1720412152 422 KNqdsinPYMYL-PFGSGPRNCIGMRFALINMKVALVRVLQNFTVQP 467
Cdd:cd20616   350 NV-----PSRYFqPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCT 391
PLN02183 PLN02183
ferulate 5-hydroxylase
39-464 3.88e-31

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 126.12  E-value: 3.88e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  39 PGPKPLPFLGTILAYQKGFWECDIQCHKKYGKMWGLYDGRQPVLAITDPDIIKTVL-VKEcySTFTNRrrfgPVGILKKA 117
Cdd:PLN02183   39 PGPKGLPIIGNMLMMDQLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLqVQD--SVFSNR----PANIAISY 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 118 ISISENEE--------WKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGegKPTSMKDIFGAYSMDVITATSF 189
Cdd:PLN02183  113 LTYDRADMafahygpfWRQMRKLCVMKLFSRKRAESWASVRDEVDSMVRSVSSNIG--KPVNIGELIFTLTRNITYRAAF 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 190 GvniDSLNNPQDPFVEKIKKLLK----FDIFDplflsvtLFPFLTPV-FDALNVSLF-PRDVISFFTTSV------ERMK 257
Cdd:PLN02183  191 G---SSSNEGQDEFIKILQEFSKlfgaFNVAD-------FIPWLGWIdPQGLNKRLVkARKSLDGFIDDIiddhiqKRKN 260
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 258 ENRMKEKEKQRVDFLQLMIN--SQNYKTKESHKALSDVEIVAQSVIFI-----FAGYETTSSALSFALYLLAIHPDVQKK 330
Cdd:PLN02183  261 QNADNDSEEAETDMVDDLLAfySEEAKVNESDDLQNSIKLTRDNIKAIimdvmFGGTETVASAIEWAMAELMKSPEDLKR 340
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 331 LQDE-IDAALPNKAPATYDtLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWP 409
Cdd:PLN02183  341 VQQElADVVGLNRRVEESD-LEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWE 419
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412152 410 EPEEFRPERFSKKNQDSI--NPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFT 464
Cdd:PLN02183  420 DPDTFKPSRFLKPGVPDFkgSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFT 476
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
77-472 7.21e-31

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: 123.94  E-value: 7.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  77 GRQPVLAITDPDIIKTVLVKECYSTFTNRRRFG--PVGILKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTD 154
Cdd:cd20615     9 GPTPEIVLTTPEHVKEFYRDSNKHHKAPNNNSGwlFGQLLGQCVGLLSGTDWKRVRKVFDPAFSHSAAVYYIPQFSREAR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 155 VLVRNMRQGLGEGKptsmkdifgaySMDVITATSFgvnidslnnpqdpfvekikKLLKFDIFDPLFLSvTLFPFLTPVFD 234
Cdd:cd20615    89 KWVQNLPTNSGDGR-----------RFVIDPAQAL-------------------KFLPFRVIAEILYG-ELSPEEKEELW 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 235 ALNV---SLFpRDVIS----------FFTTSvermKENRMKEKEKQRVDFLQLMINSQNYKTKES-----HKALSDVEIV 296
Cdd:cd20615   138 DLAPlreELF-KYVIKgglyrfkisrYLPTA----ANRRLREFQTRWRAFNLKIYNRARQRGQSTpivklYEAVEKGDIT 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 297 AQSVI-----FIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQME-YLDMVVNETLRLYPIA 370
Cdd:cd20615   213 FEELLqtldeMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPMEDYILSTDtLLAYCVLESLRLRPLL 292
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 371 G-RLERVCKTDVEINGLFIPKGTVVMIPTFAL-HKDPKYWPEPEEFRPERFSkknqdSINP----YMYLPFGSGPRNCIG 444
Cdd:cd20615   293 AfSVPESSPTDKIIGGYRIPANTPVVVDTYALnINNPFWGPDGEAYRPERFL-----GISPtdlrYNFWRFGFGPRKCLG 367
                         410       420
                  ....*....|....*....|....*...
gi 1720412152 445 MRFALINMKVALVRVLQNFTVQPCKETE 472
Cdd:cd20615   368 QHVADVILKALLAHLLEQYELKLPDQGE 395
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
68-467 2.38e-30

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: 122.79  E-value: 2.38e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKECySTFTNRR-----RFGPVGilkKAISISEN-EEWKRIRALLSP---TFT 138
Cdd:cd11028     1 YGDVFQIRMGSRPVVVLNGLETIKQALVRQG-EDFAGRPdfysfQFISNG---KSMAFSDYgPRWKLHRKLAQNalrTFS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 139 SGR----LKEMfpiINQFTDVLVRNMRQGLGEGKPTSMKD-IFGAYSmDVITATSFGVNIDsLNNPQdpFVEKIKKLLKF 213
Cdd:cd11028    77 NARthnpLEEH---VTEEAEELVTELTENNGKPGPFDPRNeIYLSVG-NVICAICFGKRYS-RDDPE--FLELVKSNDDF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 214 ----------DIFDPLFLsvtLFPFLTPVFDALNVSLfprdvISFFTTSVERMKENRMKEKEKQRVDFLqlmINSQNyKT 283
Cdd:cd11028   150 gafvgagnpvDVMPWLRY---LTRRKLQKFKELLNRL-----NSFILKKVKEHLDTYDKGHIRDITDAL---IKASE-EK 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 284 KESHKA---LSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVV 360
Cdd:cd11028   218 PEEEKPevgLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFI 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 361 NETLR---LYPIAgrLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF--SKKNQDSINPYMYLPF 435
Cdd:cd11028   298 LETMRhssFVPFT--IPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFldDNGLLDKTKVDKFLPF 375
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1720412152 436 GSGPRNCIGMRFALINMKVALVRVLQ--NFTVQP 467
Cdd:cd11028   376 GAGRRRCLGEELARMELFLFFATLLQqcEFSVKP 409
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
69-463 4.92e-30

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: 121.75  E-value: 4.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  69 GKMWGLYDGRQPVLAITDPDIIKTVLVKEcysTFTNRrrfGPV----GILKKAISI-SENEEWKRIRALLSP-------T 136
Cdd:cd20652     1 GSIFSLKMGSVYTVVLSDPKLIRDTFRRD---EFTGR---APLylthGIMGGNGIIcAEGDLWRDQRRFVHDwlrqfgmT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 137 FTSGRLKEMFPIINQFTDVLVRNMRQGlgEGKPTSMKDIFGAYSMDVITATSFGVNIdslnNPQDPFVEKIKKLLK---- 212
Cdd:cd20652    75 KFGNGRAKMEKRIATGVHELIKHLKAE--SGQPVDPSPVLMHSLGNVINDLVFGFRY----KEDDPTWRWLRFLQEegtk 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 213 -FDIFDPlflsVTLFPFLTPVFDALNVSLF----PRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSQNYK--TKE 285
Cdd:cd20652   149 lIGVAGP----VNFLPFLRHLPSYKKAIEFlvqgQAKTHAIYQKIIDEHKRRLKPENPRDAEDFELCELEKAKKEgeDRD 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 286 SHKALSDVEIVAQSVIFIF-AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETL 364
Cdd:cd20652   225 LFDGFYTDEQLHHLLADLFgAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQ 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 365 RL---YPIAgrLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRN 441
Cdd:cd20652   305 RIrsvVPLG--IPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRM 382
                         410       420
                  ....*....|....*....|..
gi 1720412152 442 CIGMRFALINMKVALVRVLQNF 463
Cdd:cd20652   383 CLGDELARMILFLFTARILRKF 404
PLN02655 PLN02655
ent-kaurene oxidase
38-463 6.85e-30

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 121.77  E-value: 6.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  38 IPGpkpLPFLGTILAYQ-----KGF--WEcdiqchKKYGKMWGLYDGRQPVLAITDPDIIKTVLVKEcYSTFTNRRRFGP 110
Cdd:PLN02655    4 VPG---LPVIGNLLQLKekkphRTFtkWS------EIYGPIYTIRTGASSVVVLNSTEVAKEAMVTK-FSSISTRKLSKA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 111 VGIL---KKAISISENEEWKR------IRALLSPT----FTSGRlkemfpiinqftDVLVRNMRQGLGE------GKPTS 171
Cdd:PLN02655   74 LTVLtrdKSMVATSDYGDFHKmvkryvMNNLLGANaqkrFRDTR------------DMLIENMLSGLHAlvkddpHSPVN 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 172 MKDIFGAYSMDVITATSFGVNIDSLnnpqdpFVEKI-KKLLKFDIFDPLFLSvtlfpfltPVFDALNVSLfpRDVISFFT 250
Cdd:PLN02655  142 FRDVFENELFGLSLIQALGEDVESV------YVEELgTEISKEEIFDVLVHD--------MMMCAIEVDW--RDFFPYLS 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 251 TSVERMKENRMKEKEKQRVDFLQLMINSQ-----NYKTKESH--------KALSDVEI---VAQSVIfifAGYETTSSAL 314
Cdd:PLN02655  206 WIPNKSFETRVQTTEFRRTAVMKALIKQQkkriaRGEERDCYldfllseaTHLTDEQLmmlVWEPII---EAADTTLVTT 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 315 SFALYLLAIHPDVQKKLQDEIDAALPNKApATYDTLLQMEYLDMVVNETLRLY-PIAGRLERVCKTDVEINGLFIPKGTV 393
Cdd:PLN02655  283 EWAMYELAKNPDKQERLYREIREVCGDER-VTEEDLPNLPYLNAVFHETLRKYsPVPLLPPRFVHEDTTLGGYDIPAGTQ 361
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 394 VMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:PLN02655  362 IAINIYGCNMDKKRWENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEF 431
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
256-496 7.40e-30

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: 121.37  E-value: 7.40e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 256 MKENRMKEKE-KQRVDFLQLMInSQNYKTKESHKaLSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDE 334
Cdd:cd20657   191 LEEHKATAQErKGKPDFLDFVL-LENDDNGEGER-LTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEE 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 335 IDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEE 413
Cdd:cd20657   269 MDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPSTPlNLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLE 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 414 FRPERFSKKNQDSINP----YMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQ-PCKETEIPLKLSKQ-GL-LQPE 486
Cdd:cd20657   349 FKPERFLPGRNAKVDVrgndFELIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWKlPAGQTPEELNMEEAfGLaLQKA 428
                         250
                  ....*....|
gi 1720412152 487 NPLLLKVVSR 496
Cdd:cd20657   429 VPLVAHPTPR 438
PLN02687 PLN02687
flavonoid 3'-monooxygenase
248-449 1.04e-29

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 121.84  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 248 FFTTSVERMKENRMKEKEKQrVDFLQLMIN-SQNYKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPD 326
Cdd:PLN02687  251 MMNGIIEEHKAAGQTGSEEH-KDLLSTLLAlKREQQADGEGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPD 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 327 VQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDP 405
Cdd:PLN02687  330 ILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPSTPlSLPRMAAEECEINGYHIPKGATLLVNVWAIARDP 409
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1720412152 406 KYWPEPEEFRPERF----SKKNQD-SINPYMYLPFGSGPRNCIGMRFAL 449
Cdd:PLN02687  410 EQWPDPLEFRPDRFlpggEHAGVDvKGSDFELIPFGAGRRICAGLSWGL 458
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
244-486 2.97e-29

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: 119.53  E-value: 2.97e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 244 DVISFFTTSVERMKENRMKEKEKQRVD-FLQLMinSQNYKTKESHKALsdveivaQSVIF-----IFAGYETTSSALSFA 317
Cdd:cd20661   191 EVYDFLLRLIERFSENRKPQSPRHFIDaYLDEM--DQNKNDPESTFSM-------ENLIFsvgelIIAGTETTTNVLRWA 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 318 LYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGR-LERVCKTDVEINGLFIPKGTVVMI 396
Cdd:cd20661   262 ILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLgIFHATSKDAVVRGYSIPKGTTVIT 341
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 397 PTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETeIPLK 476
Cdd:cd20661   342 NLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHGL-IPDL 420
                         250
                  ....*....|.
gi 1720412152 477 LSKQGL-LQPE 486
Cdd:cd20661   421 KPKLGMtLQPQ 431
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
121-496 3.26e-29

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 120.65  E-value: 3.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 121 SENEEWKRIRALLSPTFTSGRLKEmfpiinqFTDVLVRNMRQGLGE--------GKPTSMKDIFGAYSMDVITATSFGVN 192
Cdd:PLN03195  118 VDGELWRKQRKTASFEFASKNLRD-------FSTVVFREYSLKLSSilsqasfaNQVVDMQDLFMRMTLDSICKVGFGVE 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 193 IDSL--NNPQDPFV---EKIKKLLKFDIFDPLFlsvtlfpfltPVFDALNV---SLFPRD--VISFFTTSVERMKENRMK 262
Cdd:PLN03195  191 IGTLspSLPENPFAqafDTANIIVTLRFIDPLW----------KLKKFLNIgseALLSKSikVVDDFTYSVIRRRKAEMD 260
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 263 EKEKQRVD-----FLQLMINSQNYKTKESHKALSDVEIVaqsviFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEI-- 335
Cdd:PLN03195  261 EARKSGKKvkhdiLSRFIELGEDPDSNFTDKSLRDIVLN-----FVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSELka 335
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 336 ---DAAL---PNKAPA------------TYDTLLQMEYLDMVVNETLRLYPIA-----GRLErvckTDVEINGLFIPKGT 392
Cdd:PLN03195  336 lekERAKeedPEDSQSfnqrvtqfagllTYDSLGKLQYLHAVITETLRLYPAVpqdpkGILE----DDVLPDGTKVKAGG 411
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 393 VVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQ-DSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKE 470
Cdd:PLN03195  412 MVTYVPYSMGRMEYNWgPDAASFKPERWIKDGVfQNASPFKFTAFQAGPRICLGKDSAYLQMKMALALLCRFFKFQLVPG 491
                         410       420
                  ....*....|....*....|....*.
gi 1720412152 471 TeiPLKLSKQGLLQPENPLLLKVVSR 496
Cdd:PLN03195  492 H--PVKYRMMTILSMANGLKVTVSRR 515
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
295-491 4.70e-29

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: 118.79  E-value: 4.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 295 IVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLE 374
Cdd:cd20644   233 IKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQ 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 375 RVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKnQDSINPYMYLPFGSGPRNCIGMRFALINMKV 454
Cdd:cd20644   313 RVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDI-RGSGRNFKHLAFGFGMRQCLGRRLAEAEMLL 391
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720412152 455 ALVRVLQNFTVQPCKETEIPLKLSKqgLLQPENPLLL 491
Cdd:cd20644   392 LLMHVLKNFLVETLSQEDIKTVYSF--ILRPEKPPLL 426
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
300-466 1.77e-28

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 118.25  E-value: 1.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 300 VIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCK 378
Cdd:PLN02426  299 VSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMgPNQEAASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAA 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 379 -TDVEINGLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQ-DSINPYMYLPFGSGPRNCIGMRFALINMKVA 455
Cdd:PLN02426  379 eDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGVfVPENPFKYPVFQAGLRVCLGKEMALMEMKSV 458
                         170
                  ....*....|.
gi 1720412152 456 LVRVLQNFTVQ 466
Cdd:PLN02426  459 AVAVVRRFDIE 469
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
294-467 3.36e-28

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 117.53  E-value: 3.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 294 EIVAQSVIFIF-----AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLY- 367
Cdd:PLN02394  288 EINEDNVLYIVeninvAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHm 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 368 PIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF---SKKNQDSINPYMYLPFGSGPRNCIG 444
Cdd:PLN02394  368 AIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFleeEAKVEANGNDFRFLPFGVGRRSCPG 447
                         170       180
                  ....*....|....*....|...
gi 1720412152 445 MRFALINMKVALVRVLQNFTVQP 467
Cdd:PLN02394  448 IILALPILGIVLGRLVQNFELLP 470
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
84-475 4.18e-28

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: 116.31  E-value: 4.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  84 ITDPDIIKTVLVKECYSTF------TNRRRFGPVGILKKAISISEN-----EEWKRIRALLSPTFTSGRLkemfpiINQF 152
Cdd:cd11040    27 ITDPELISAVFRNPKTLSFdpivivVVGRVFGSPESAKKKEGEPGGkglirLLHDLHKKALSGGEGLDRL------NEAM 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 153 TDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSfgvnIDSLNNPQdpFVEKIKKLLK-FDIFDPLFLSVTL-FPFLT 230
Cdd:cd11040   101 LENLSKLLDELSLSGGTSTVEVDLYEWLRDVLTRAT----TEALFGPK--LPELDPDLVEdFWTFDRGLPKLLLgLPRLL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 231 pVFDALNVslfpRD-VISFFTTSVERMKENRmkekeKQRVDFLQLMinsqnykTKESHKA-LSDVEIVAQSVIFIFAG-Y 307
Cdd:cd11040   175 -ARKAYAA----RDrLLKALEKYYQAAREER-----DDGSELIRAR-------AKVLREAgLSEEDIARAELALLWAInA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 308 ETTSSALSFALYLLAiHPDVQKKLQDEIDAAL-----PNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVE 382
Cdd:cd11040   238 NTIPAAFWLLAHILS-DPELLERIREEIEPAVtpdsgTNAILDLTDLLTSCPLLDSTYLETLRLHSSSTSVRLVTEDTVL 316
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 383 INGLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQDSIN---PYMYLPFGSGPRNCIGMRFALINMKVALVR 458
Cdd:cd11040   317 GGGYLLRKGSLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDKKGrglPGAFRPFGGGASLCPGRHFAKNEILAFVAL 396
                         410
                  ....*....|....*..
gi 1720412152 459 VLQNFTVQPCKETEIPL 475
Cdd:cd11040   397 LLSRFDVEPVGGGDWKV 413
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
66-460 4.18e-28

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: 116.09  E-value: 4.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  66 KKYGKMWGLYDGRQPVLAITDPDIIKTVLVKECYSTFTNRRRFGPVGILKKAISISENEEWKRIRALLSPTFTSGRLKEM 145
Cdd:cd20636    20 EKYGNVFKTHLLGRPVIRVTGAENIRKILLGEHTLVSTQWPQSTRILLGSNTLLNSVGELHRQRRKVLARVFSRAALESY 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 146 FPIINqftDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSlnnpqdpfvEKIKKLLKfdIFDPLFLSVTL 225
Cdd:cd20636   100 LPRIQ---DVVRSEVRGWCRGPGPVAVYTAAKSLTFRIAVRILLGLRLEE---------QQFTYLAK--TFEQLVENLFS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 226 FPFLTPvFDALNVSLFPRDVI-SFFTTSV-ERMKENRMKEKEkqrvDFLQLMINSqnykTKESHKALSDVEIVAQSVIFI 303
Cdd:cd20636   166 LPLDVP-FSGLRKGIKARDILhEYMEKAIeEKLQRQQAAEYC----DALDYMIHS----ARENGKELTMQELKESAVELI 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 304 FAGYETTSSALSFALYLLAIHPDVQKKLQDEIDA--------ALPNKapATYDTLLQMEYLDMVVNETLRLY-PIAGRLE 374
Cdd:cd20636   237 FAAFSTTASASTSLVLLLLQHPSAIEKIRQELVShglidqcqCCPGA--LSLEKLSRLRYLDCVVKEVLRLLpPVSGGYR 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 375 RVCKTdVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFS-KKNQDSINPYMYLPFGSGPRNCIGMRFALINMK 453
Cdd:cd20636   315 TALQT-FELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGvEREESKSGRFNYIPFGGGVRSCIGKELAQVILK 393

                  ....*..
gi 1720412152 454 VALVRVL 460
Cdd:cd20636   394 TLAVELV 400
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
295-476 7.13e-28

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: 115.28  E-value: 7.13e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 295 IVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAG-RL 373
Cdd:cd20662   226 LICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPlNV 305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 374 ERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQ----DSinpymYLPFGSGPRNCIGMRFAL 449
Cdd:cd20662   306 PREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLENGQfkkrEA-----FLPFSMGKRACLGEQLAR 380
                         170       180
                  ....*....|....*....|....*..
gi 1720412152 450 INMKVALVRVLQNFTVQPCKETEIPLK 476
Cdd:cd20662   381 SELFIFFTSLLQKFTFKPPPNEKLSLK 407
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
137-467 2.50e-27

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: 114.12  E-value: 2.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 137 FTSGRLKEMFPI----INQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNNPQDPFVEKIKKLLK 212
Cdd:cd20656    74 FTPKRLESLRPIredeVTAMVESIFNDCMSPENEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEQGVEFKAIVS 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 213 FDIFDPLFLSVTLF-PFLTpvfdalnvSLFPRDVISFFTTSVER-------MKENRMKEKE----KQRVDFLQLMinsqn 280
Cdd:cd20656   154 NGLKLGASLTMAEHiPWLR--------WMFPLSEKAFAKHGARRdrltkaiMEEHTLARQKsgggQQHFVALLTL----- 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 281 yktkESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVV 360
Cdd:cd20656   221 ----KEQYDLSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVV 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 361 NETLRLYPIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQD-SINPYMYLPFGSG 438
Cdd:cd20656   297 KEALRLHPPTPlMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDiKGHDFRLLPFGAG 376
                         330       340
                  ....*....|....*....|....*....
gi 1720412152 439 PRNCIGMRFALINMKVALVRVLQNFTVQP 467
Cdd:cd20656   377 RRVCPGAQLGINLVTLMLGHLLHHFSWTP 405
PLN02302 PLN02302
ent-kaurenoic acid oxidase
243-474 2.82e-27

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 114.43  E-value: 2.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 243 RDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSqnykTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLA 322
Cdd:PLN02302  240 KKLVALFQSIVDERRNSRKQNISPRKKDMLDLLLDA----EDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQ 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 323 IHPDVQKKLQDEIDAALPNKAPA----TYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPT 398
Cdd:PLN02302  316 EHPEVLQKAKAEQEEIAKKRPPGqkglTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWF 395
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 399 FALHKDPKYWPEPEEFRPERFSKknqDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQP----CKETEIP 474
Cdd:PLN02302  396 RQVHMDPEVYPNPKEFDPSRWDN---YTPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERlnpgCKVMYLP 472
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
68-485 3.80e-27

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: 113.48  E-value: 3.80e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKECySTFTNRrrfGPVGILKK-----AISISENEEWKRIRALLSPT---FTS 139
Cdd:cd20670     1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQA-DEFSGR---GELATIERnfqghGVALANGERWRILRRFSLTIlrnFGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 140 GRlKEMFPIINQFTDVLVRNMRQGlgEGKPTSMKDIFGAYSMDVITATSFGVNIDS--------LNNPQDPFVEKIKKLL 211
Cdd:cd20670    77 GK-RSIEERIQEEAGYLLEEFRKT--KGAPIDPTFFLSRTVSNVISSVVFGSRFDYedkqflslLRMINESFIEMSTPWA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 212 KfdIFDPLFLSVTLFPFLTPVFDALNVSLfpRDVISffttsvERMKENRMKEKEKQRVDFLQLMINSQNYKTKESHKALS 291
Cdd:cd20670   154 Q--LYDMYSGIMQYLPGRHNRIYYLIEEL--KDFIA------SRVKINEASLDPQNPRDFIDCFLIKMHQDKNNPHTEFN 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 292 DVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPATYDTlLQMEYLDMVVNETLRLYPIA 370
Cdd:cd20670   224 LKNLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIgPHRLPSVDDR-VKMPYTDAVIHEIQRLTDIV 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 371 --GRLERVCKtDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFA 448
Cdd:cd20670   303 plGVPHNVIR-DTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMA 381
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1720412152 449 LINMKVALVRVLQNFTVQ---PCKETEIPLKLSKQGLLQP 485
Cdd:cd20670   382 RMELFLYFTSILQNFSLRslvPPADIDITPKISGFGNIPP 421
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
198-486 8.78e-27

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: 112.24  E-value: 8.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 198 NPQDPFVEKIKKLL-------KFDIFDPLFLSVT-------------------LFPFLTPVFDALNVSLFPRD--VISFF 249
Cdd:cd20667   105 DPQDPIVHATANVIgavvfghRFSSEDPIFLELIrainlglafastiwgrlydAFPWLMRYLPGPHQKIFAYHdaVRSFI 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 250 TTSVERMKENRmKEKEKQRVDFLQlminSQNYKTKESHKALSDVEIVAQSVIFIF-AGYETTSSALSFALYLLAIHPDVQ 328
Cdd:cd20667   185 KKEVIRHELRT-NEAPQDFIDCYL----AQITKTKDDPVSTFSEENMIQVVIDLFlGGTETTATTLHWALLYMVHHPEIQ 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 329 KKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKY 407
Cdd:cd20667   260 EKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSvGAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPEC 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 408 WPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQ-PCKETEIPLKLSKQGLLQPE 486
Cdd:cd20667   340 WETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQlPEGVQELNLEYVFGGTLQPQ 419
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
242-472 1.08e-26

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: 111.97  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 242 PRDVISFFTtsvermkeNRMkEKEKQrvdflqlmiNSQNYKTKESHKA-LSDVeivaqsvifIFAGYETTSSALSFALYL 320
Cdd:cd20665   200 PRDFIDCFL--------IKM-EQEKH---------NQQSEFTLENLAVtVTDL---------FGAGTETTSTTLRYGLLL 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 321 LAIHPDVQKKLQDEIDAAL-PNKAPATYDTlLQMEYLDMVVNETLR---LYPIAgrLERVCKTDVEINGLFIPKGTVVMI 396
Cdd:cd20665   253 LLKHPEVTAKVQEEIDRVIgRHRSPCMQDR-SHMPYTDAVIHEIQRyidLVPNN--LPHAVTCDTKFRNYLIPKGTTVIT 329
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412152 397 P-TFALHkDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETE 472
Cdd:cd20665   330 SlTSVLH-DDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSLVDPK 405
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
68-475 1.69e-26

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: 111.73  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKECYStFTNRRRFGPVGILK--KAISISEN--EEWKRIRALLSP---TFT-- 138
Cdd:cd20677     1 YGDVFQIKLGMLPVVVVSGLETIKQVLLKQGES-FAGRPDFYTFSLIAngKSMTFSEKygESWKLHKKIAKNalrTFSke 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 139 -------SGRLKEMfpIINQFTDvLVRNMRQgLGEGK----PTSMKDIFGAysmDVITATSFGVNIDSLNNPQDPFVEKI 207
Cdd:cd20677    80 eaksstcSCLLEEH--VCAEASE-LVKTLVE-LSKEKgsfdPVSLITCAVA---NVVCALCFGKRYDHSDKEFLTIVEIN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 208 KKLLKfdifdpLFLSVTLFPFLtPVFDALNVSLF--PRDVISFFTTSVERMKENRMKEKEKQRV-DFLQLMIN-SQNYKT 283
Cdd:cd20677   153 NDLLK------ASGAGNLADFI-PILRYLPSPSLkaLRKFISRLNNFIAKSVQDHYATYDKNHIrDITDALIAlCQERKA 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 284 KESHKALSDVEIVAqSVIFIF-AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNE 362
Cdd:cd20677   226 EDKSAVLSDEQIIS-TVNDIFgAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINE 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 363 TLR---LYPIAgrLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDsINPYM---YLPFG 436
Cdd:cd20677   305 VFRhssFVPFT--IPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQ-LNKSLvekVLIFG 381
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1720412152 437 SGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEIPL 475
Cdd:cd20677   382 MGVRKCLGEDVARNEIFVFLTTILQQLKLEKPPGQKLDL 420
PLN02966 PLN02966
cytochrome P450 83A1
9-466 2.30e-26

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 112.15  E-value: 2.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152   9 METWMLLATSLVLLYLYGTHSHGIFKKLGIP-GPKPLPFLGTILAYQK-------GFWEcdiqchKKYGKMWGLYDGRQP 80
Cdd:PLN02966    1 MEDIIIGVVALAAVLLFFLYQKPKTKRYKLPpGPSPLPVIGNLLQLQKlnpqrffAGWA------KKYGPILSYRIGSRT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  81 VLAITDPDIIKTVLvKECYSTFTNR---RRFGPVGILKKAISISENEEWKR-IRAL-LSPTFTSGRLKEMFPIINQFTDV 155
Cdd:PLN02966   75 MVVISSAELAKELL-KTQDVNFADRpphRGHEFISYGRRDMALNHYTPYYReIRKMgMNHLFSPTRVATFKHVREEEARR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 156 LVRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDSLNnpqdpfvEKIKKLLKF-----DIFDPLFLSvTLFPFLT 230
Cdd:PLN02966  154 MMDKINKAADKSEVVDISELMLTFTNSVVCRQAFGKKYNEDG-------EEMKRFIKIlygtqSVLGKIFFS-DFFPYCG 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 231 PVFDALNVSLFPRDVISFFTTSV-----ERMKENRMKEKEKQRVDFLQLMINSQNYKtkeSHKALSDVEIVAQSVIFifA 305
Cdd:PLN02966  226 FLDDLSGLTAYMKECFERQDTYIqevvnETLDPKRVKPETESMIDLLMEIYKEQPFA---SEFTVDNVKAVILDIVV--A 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 306 GYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPA--TYDTLLQMEYLDMVVNETLRLYPIAGRL-ERVCKTDVE 382
Cdd:PLN02966  301 GTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGSTfvTEDDVKNLPYFRALVKETLRIEPVIPLLiPRACIQDTK 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 383 INGLFIPKGTVVMIPTFALHKDPKYW-PEPEEFRPERFSKKNQD-SINPYMYLPFGSGPRNCIGMRFALINMKVALVRVL 460
Cdd:PLN02966  381 IAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDfKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLL 460

                  ....*.
gi 1720412152 461 QNFTVQ 466
Cdd:PLN02966  461 LNFNFK 466
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
285-460 2.78e-26

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: 110.61  E-value: 2.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 285 ESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAlpNKAPATYDTLLQMEYLDMVVNETL 364
Cdd:cd20614   199 DNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA--GDVPRTPAELRRFPLAEALFRETL 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 365 RLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFsKKNQDSINPYMYLPFGSGPRNCIG 444
Cdd:cd20614   277 RLHPPVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERW-LGRDRAPNPVELLQFGGGPHFCLG 355
                         170
                  ....*....|....*....
gi 1720412152 445 MRFA---LINMKVALVRVL 460
Cdd:cd20614   356 YHVAcveLVQFIVALAREL 374
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
123-474 8.09e-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: 109.71  E-value: 8.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 123 NEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGEGK-PTSMKDIFGAYSMDVITATSFGVNIDSLNNpqd 201
Cdd:cd11066    61 DESCKRRRKAAASALNRPAVQSYAPIIDLESKSFIRELLRDSAEGKgDIDPLIYFQRFSLNLSLTLNYGIRLDCVDD--- 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 202 pfvekikkllkfdifDPLFLSVtlfpfltpVFDALNVSLF------PRDVISFFTtSVERMKENRMKEKE--KQRVDFLQ 273
Cdd:cd11066   138 ---------------DSLLLEI--------IEVESAISKFrstssnLQDYIPILR-YFPKMSKFRERADEyrNRRDKYLK 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 274 LMINS----------------QNYKTKEShkALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHP--DVQKKLQDEI 335
Cdd:cd11066   194 KLLAKlkeeiedgtdkpcivgNILKDKES--KLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEI 271
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 336 DAALPNKAPATYDTLLQME--YLDMVVNETLRLY---PIAgrLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPE 410
Cdd:cd11066   272 LEAYGNDEDAWEDCAAEEKcpYVVALVKETLRYFtvlPLG--LPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGD 349
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412152 411 PEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEIP 474
Cdd:cd11066   350 PDEFIPERWLDASGDLIPGPPHFSFGAGSRMCAGSHLANRELYTAICRLILLFRIGPKDEEEPM 413
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
294-467 1.23e-25

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: 109.10  E-value: 1.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 294 EIVAQSVIFIF-----AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLY- 367
Cdd:cd11074   228 EINEDNVLYIVeninvAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLRm 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 368 PIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF---SKKNQDSINPYMYLPFGSGPRNCIG 444
Cdd:cd11074   308 AIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFleeESKVEANGNDFRYLPFGVGRRSCPG 387
                         170       180
                  ....*....|....*....|...
gi 1720412152 445 MRFALINMKVALVRVLQNFTVQP 467
Cdd:cd11074   388 IILALPILGITIGRLVQNFELLP 410
PLN00168 PLN00168
Cytochrome P450; Provisional
11-458 1.36e-25

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 110.04  E-value: 1.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  11 TWMLLATSLVL---LYLYGTHSHGIFKKLGI---PGPKPLPFLGTILAYQKGFWECDI---QCHKKYGKMWGLYDGRQPV 81
Cdd:PLN00168    4 TQLLLLAALLLlplLLLLLGKHGGRGGKKGRrlpPGPPAVPLLGSLVWLTNSSADVEPllrRLIARYGPVVSLRVGSRLS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  82 LAITDPDIIKTVLVkECYSTFTNRRRFGPVGILKKAISI----SENEEWKRIRA-LLSPTFTSGRLKEMFPIINQFTDVL 156
Cdd:PLN00168   84 VFVADRRLAHAALV-ERGAALADRPAVASSRLLGESDNTitrsSYGPVWRLLRRnLVAETLHPSRVRLFAPARAWVRRVL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 157 VRNMRQGLGEGKPTSMKDIFGAYSMDVITATSFGVNIDslnnpqDPFVEKIKKLLKfdifDPLFLSVT---LFPFltpvF 233
Cdd:PLN00168  163 VDKLRREAEDAAAPRVVETFQYAMFCLLVLMCFGERLD------EPAVRAIAAAQR----DWLLYVSKkmsVFAF----F 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 234 DALNVSLFpRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSQNYKTK------------------ESHKALSDVEI 295
Cdd:PLN00168  229 PAVTKHLF-RGRLQKALALRRRQKELFVPLIDARREYKNHLGQGGEPPKKEttfehsyvdtlldirlpeDGDRALTDDEI 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 296 VAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQ-MEYLDMVVNETLRLYPIAGR-L 373
Cdd:PLN00168  308 VNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQEEVSEEDVHkMPYLKAVVLEGLRKHPPAHFvL 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 374 ERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF------SKKNQDSINPYMYLPFGSGPRNCIGMRF 447
Cdd:PLN00168  388 PHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFlaggdgEGVDVTGSREIRMMPFGVGRRICAGLGI 467
                         490
                  ....*....|....
gi 1720412152 448 ALINMK--VA-LVR 458
Cdd:PLN00168  468 AMLHLEyfVAnMVR 481
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
68-482 1.89e-25

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: 108.31  E-value: 1.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKECySTFTNRRRFGPVGILKKA--ISISENEEWKRIRallspTFTSGRLKEm 145
Cdd:cd20669     1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQA-EEFSGRGDYPVFFNFTKGngIAFSNGERWKILR-----RFALQTLRN- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 146 FPI--------INQFTDVLVRNMRQGlgEGKPTSMKDIFGAYSMDVITATSFGVNIDSlnnpQDPFVEKIKKLLK--FDI 215
Cdd:cd20669    74 FGMgkrsieerILEEAQFLLEELRKT--KGAPFDPTFLLSRAVSNIICSVVFGSRFDY----DDKRLLTILNLINdnFQI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 216 FDPLFLSV-TLFPFLTPVFDALNVSLFP-----RDVISfftTSVERMKENRMKEKEKQRVD-FLQLMinSQNYKTKESHk 288
Cdd:cd20669   148 MSSPWGELyNIFPSVMDWLPGPHQRIFQnfeklRDFIA---ESVREHQESLDPNSPRDFIDcFLTKM--AEEKQDPLSH- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 289 aLSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPATYDTLlQMEYLDMVVNETLRLY 367
Cdd:cd20669   222 -FNMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVgRNRLPTLEDRA-RMPYTDAVIHEIQRFA 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 368 PIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMR 446
Cdd:cd20669   300 DIIPmSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGES 379
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1720412152 447 FALINMKVALVRVLQNFTVQPCKETE-IPLKLSKQGL 482
Cdd:cd20669   380 LARMELFLYLTAILQNFSLQPLGAPEdIDLTPLSSGL 416
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
266-496 2.48e-25

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 108.79  E-value: 2.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 266 KQRVDFLQLMINSQNYKTKEShkaLSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPA 345
Cdd:PLN00110  264 KGNPDFLDVVMANQENSTGEK---LTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 346 TYDTLLQMEYLDMVVNETLRLYP-IAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQ 424
Cdd:PLN00110  341 VESDLPKLPYLQAICKESFRKHPsTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKN 420
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720412152 425 DSINP----YMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKETEIPLKLSKQGLLQPENPLLLKVVSR 496
Cdd:PLN00110  421 AKIDPrgndFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVELNMDEAFGLALQKAVPLSAMVTPR 496
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
77-496 2.95e-25

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


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 108.22  E-value: 2.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  77 GRQPVLAITDPDIIKTVLvKECYSTFTNRRRFGPVGILK---KAISISE-NEEWKRIRALLSPTFTS-GRLKEMFPIINQ 151
Cdd:cd20658     9 GNTHVIPVTCPKIAREIL-RKQDAVFASRPLTYATEIISggyKTTVISPyGEQWKKMRKVLTTELMSpKRHQWLHGKRTE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 152 FTDVLVR---NMRQGLGEGKPTSMKDIFGAYSMDVITATSFG------VNIDSLNNPQDpfVEKIKKLlkFDIFDPLF-L 221
Cdd:cd20658    88 EADNLVAyvyNMCKKSNGGGLVNVRDAARHYCGNVIRKLMFGtryfgkGMEDGGPGLEE--VEHMDAI--FTALKCLYaF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 222 SVTLF-PFLT---------PVFDALN-VSLFPRDVISffttsvERMKENRMKEKeKQRVDFLQLMINsqnYKTKESHKAL 290
Cdd:cd20658   164 SISDYlPFLRgldldghekIVREAMRiIRKYHDPIID------ERIKQWREGKK-KEEEDWLDVFIT---LKDENGNPLL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 291 SDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNkapatyDTLLQ------MEYLDMVVNETL 364
Cdd:cd20658   234 TPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGK------ERLVQesdipnLNYVKACAREAF 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 365 RLYPIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSI---NPYMYLPFGSGPR 440
Cdd:cd20658   308 RLHPVAPfNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHLNEDSEVTltePDLRFISFSTGRR 387
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720412152 441 NCIGMRFALINMKVALVRVLQNFT-VQPCKETEIPLKLSKQGLLqPENPLLLKVVSR 496
Cdd:cd20658   388 GCPGVKLGTAMTVMLLARLLQGFTwTLPPNVSSVDLSESKDDLF-MAKPLVLVAKPR 443
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
220-473 6.65e-25

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 107.37  E-value: 6.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 220 FLSVTlFPFLTPVFDAlnvSLFPRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSQNyktkeshkALSDVEIVAQS 299
Cdd:PLN02987  205 FFSVP-LPLFSTTYRR---AIQARTKVAEALTLVVMKRRKEEEEGAEKKKDMLAALLASDD--------GFSDEEIVDFL 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 300 VIFIFAGYETTSSALSFALYLLAIHPDVQKKLQ---DEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRLERV 376
Cdd:PLN02987  273 VALLVAGYETTSTIMTLAVKFLTETPLALAQLKeehEKIRAMKSDSYSLEWSDYKSMPFTQCVVNETLRVANIIGGIFRR 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 377 CKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVAL 456
Cdd:PLN02987  353 AMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPRLCPGYELARVALSVFL 432
                         250
                  ....*....|....*..
gi 1720412152 457 VRVLQNFTVQPCKETEI 473
Cdd:PLN02987  433 HRLVTRFSWVPAEQDKL 449
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
68-467 6.75e-25

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: 106.81  E-value: 6.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVkECYSTFTNRrrfGPVGILKK-----AISISENEEWK-----RIRALLS--- 134
Cdd:cd20671     1 YGPVFTIHLGMQKTVVLTGYEAVKEALV-GTGDEFADR---PPIPIFQAiqhgnGVFFSSGERWRttrrfTVRSMKSlgm 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 135 --PTFTSGRLKEMfpiinQFTDVLVRNMRqglgeGKPTSMKdIFGAYSMDVITATSFGVNIDSlnnpQDPFVEKIKKLLK 212
Cdd:cd20671    77 gkRTIEDKILEEL-----QFLNGQIDSFN-----GKPFPLR-LLGWAPTNITFAMLFGRRFDY----KDPTFVSLLDLID 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 213 fDIF----DPLFLSVTLFPFLTPVFDALNVSLfpRDVISFFTTSVERMKENRMKEKEKQRVDFLQLMINSQNyKTKESHK 288
Cdd:cd20671   142 -EVMvllgSPGLQLFNLYPVLGAFLKLHKPIL--DKVEEVCMILRTLIEARRPTIDGNPLHSYIEALIQKQE-EDDPKET 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 289 ALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYP 368
Cdd:cd20671   218 LFHDANVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFIT 297
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 369 IAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFA 448
Cdd:cd20671   298 LLPHVPRCTAADTQFKGYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLA 377
                         410
                  ....*....|....*....
gi 1720412152 449 LINMKVALVRVLQNFTVQP 467
Cdd:cd20671   378 RTELFIFFTGLLQKFTFLP 396
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
233-462 1.21e-24

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: 106.05  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 233 FDALNVSLFPRDVISffttsvERMKEN-RMK----EKEKQRVDFLQLMINsqnyKTKESHKALSDVEIVAQSVIFIFAGY 307
Cdd:cd20638   174 FSGLYRGLRARNLIH------AKIEENiRAKiqreDTEQQCKDALQLLIE----HSRRNGEPLNLQALKESATELLFGGH 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 308 ETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDM------VVNETLRLYP-IAGRLERVCKTd 380
Cdd:cd20638   244 ETTASAATSLIMFLGLHPEVLQKVRKELQEKGLLSTKPNENKELSMEVLEQlkytgcVIKETLRLSPpVPGGFRVALKT- 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 381 VEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVL 460
Cdd:cd20638   323 FELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELA 402

                  ..
gi 1720412152 461 QN 462
Cdd:cd20638   403 RH 404
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
305-466 1.75e-24

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: 105.55  E-value: 1.75e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 305 AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPATYDTLlQMEYLDMVVNETLRLYPIAG-RLERVCKTDVE 382
Cdd:cd20663   241 AGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIgQVRRPEMADQA-RMPYTNAVIHEVQRFGDIVPlGVPHMTSRDIE 319
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 383 INGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQN 462
Cdd:cd20663   320 VQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQR 399

                  ....
gi 1720412152 463 FTVQ 466
Cdd:cd20663   400 FSFS 403
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
106-463 1.98e-24

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: 104.57  E-value: 1.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 106 RRFGPVGILKKAISISENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMrqgLGEGKPTsmkdifgaysmDVIT 185
Cdd:cd11031    54 PRLTPEPLLPGSLMSMDPPEHTRLRRLVAKAFTARRVERLRPRIEEIADELLDAM---EAQGPPA-----------DLVE 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 186 ATSFgvnidslnnpqdPF-VEKIKKLLKFdifdplflsvtlfpfltPVFDALNVSLFPRDVISFFTTSVERMKENR---- 260
Cdd:cd11031   120 ALAL------------PLpVAVICELLGV-----------------PYEDRERFRAWSDALLSTSALTPEEAEAARqelr 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 261 --MKEK-EKQRV----DFLQLMInsqnyKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQD 333
Cdd:cd11031   171 gyMAELvAARRAepgdDLLSALV-----AARDDDDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRA 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 334 EidaalPNKAPATydtllqmeyldmvVNETLRLYPIAGR--LERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEP 411
Cdd:cd11031   246 D-----PELVPAA-------------VEELLRYIPLGAGggFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDP 307
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720412152 412 EEFRPERFSkknqdsiNPymYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd11031   308 DRLDLDREP-------NP--HLAFGHGPHHCLGAPLARLELQVALGALLRRL 350
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
99-472 3.53e-24

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: 103.57  E-value: 3.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  99 YSTFTNRR-----------RFGPVGilkkaisiSENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQgLGEG 167
Cdd:cd11034    31 TDTFSSKGvtfprpelgefRLMPIE--------TDPPEHKKYRKLLNPFFTPEAVEAFRPRVRQLTNDLIDAFIE-RGEC 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 168 kptsmkdifgaysmDVITATSfgvnidslnnpqDPFVEK-IKKLLKFdifdPLFLSVTLFPFLtpvfDALNVSLFPRDVI 246
Cdd:cd11034   102 --------------DLVTELA------------NPLPARlTLRLLGL----PDEDGERLRDWV----HAILHDEDPEEGA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 247 SFFTTSVERMKEnRMKEKEKQ-RVDFLQLMINSqnyktKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHP 325
Cdd:cd11034   148 AAFAELFGHLRD-LIAERRANpRDDLISRLIEG-----EIDGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHP 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 326 DVQKKLQDEIDAalpnkapatydtllqmeyLDMVVNETLRLY-PIAGrLERVCKTDVEINGLFIPKGTVVMIPTFALHKD 404
Cdd:cd11034   222 EDRRRLIADPSL------------------IPNAVEEFLRFYsPVAG-LARTVTQEVEVGGCRLKPGDRVLLAFASANRD 282
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720412152 405 PKYWPEPEEFRPERFSKKnqdsinpymYLPFGSGPRNCIGMRFALINMKVALVRVLQ---NFTVQPCKETE 472
Cdd:cd11034   283 EEKFEDPDRIDIDRTPNR---------HLAFGSGVHRCLGSHLARVEARVALTEVLKripDFELDPGATCE 344
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
101-463 4.60e-24

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: 103.15  E-value: 4.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 101 TFTNR--RRFGPVGILKKAISISENEEWKRIRALLSPTFtsgrlkeMFPIINQFTDVLVRNMRQGL-GEGKPTSMKDIFG 177
Cdd:cd20629    29 TFSSEtyDATLGGPFLGHSILAMDGEEHRRRRRLLQPAF-------APRAVARWEEPIVRPIAEELvDDLADLGRADLVE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 178 AYSMD---VITATSFGVnidslnnPQDpfvekikkllKFDIFDPLFLSVTLFPFLTPVFDalnvslFPRDVISF--FTTS 252
Cdd:cd20629   102 DFALElpaRVIYALLGL-------PEE----------DLPEFTRLALAMLRGLSDPPDPD------VPAAEAAAaeLYDY 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 253 VERMKENRmkeKEKQRVDFLQLMINSqnykTKESHKaLSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKL- 331
Cdd:cd20629   159 VLPLIAER---RRAPGDDLISRLLRA----EVEGEK-LDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVr 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 332 QDEidaalpnkapatydtllqmEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEP 411
Cdd:cd20629   231 RDR-------------------SLIPAAIEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDP 291
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720412152 412 EEFRPERfskknqdsiNPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd20629   292 DVFDIDR---------KPKPHLVFGGGAHRCLGEHLARVELREALNALLDRL 334
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
274-467 9.57e-24

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: 103.56  E-value: 9.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 274 LMINSQNYKTKESHKA-LSDVEIVaQSVIFIF-AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPATYDTL 350
Cdd:cd20676   216 LIEHCQDKKLDENANIqLSDEKIV-NIVNDLFgAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIgRERRPRLSDRP 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 351 lQMEYLDMVVNETLR---LYPIAgrLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDSI 427
Cdd:cd20676   295 -QLPYLEAFILETFRhssFVPFT--IPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEI 371
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720412152 428 NPYM---YLPFGSGPRNCIGMRFALINMKVALVRVLQN--FTVQP 467
Cdd:cd20676   372 NKTEsekVMLFGLGKRRCIGESIARWEVFLFLAILLQQleFSVPP 416
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
68-465 1.84e-23

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: 102.55  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  68 YGKMWGLYDGRQPVLAITDPDIIKTVLVKECySTFTNRrrfGPVGILKK-----AISISENEEWKRIRALLSPT---FTS 139
Cdd:cd20672     1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQA-EAFSGR---GTIAVVDPifqgyGVIFANGERWKTLRRFSLATmrdFGM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 140 GRlKEMFPIINQFTDVLVRNMRQglGEGKPTSMKDIFGAYSMDVITATSFGVnidslnnpqdpfvekikkllKFDIFDPL 219
Cdd:cd20672    77 GK-RSVEERIQEEAQCLVEELRK--SKGALLDPTFLFQSITANIICSIVFGE--------------------RFDYKDPQ 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 220 FLS-VTLF--------PFLTPVFDALNVSL--FP----------RDVISFFTTSVERMKENRMKEKEKQRVD--FLQLMI 276
Cdd:cd20672   134 FLRlLDLFyqtfslisSFSSQVFELFSGFLkyFPgahrqiyknlQEILDYIGHSVEKHRATLDPSAPRDFIDtyLLRMEK 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 277 NSQNYKTKESHKALSDveivaqSVIFIF-AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEY 355
Cdd:cd20672   214 EKSNHHTEFHHQNLMI------SVLSLFfAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPY 287
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 356 LDMVVNETLR---LYPIaGRLERVCKtDVEINGLFIPKGT-VVMIPTFALHkDPKYWPEPEEFRPERFSKKNQDSINPYM 431
Cdd:cd20672   288 TDAVIHEIQRfsdLIPI-GVPHRVTK-DTLFRGYLLPKNTeVYPILSSALH-DPQYFEQPDTFNPDHFLDANGALKKSEA 364
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1720412152 432 YLPFGSGPRNCIGMRFALINMKVALVRVLQNFTV 465
Cdd:cd20672   365 FMPFSTGKRICLGEGIARNELFLFFTTILQNFSV 398
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
90-472 2.32e-23

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: 101.52  E-value: 2.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  90 IKTVLVKecYSTFTNR--RRFGPVGILKKAISI--SENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMrqglg 165
Cdd:cd11032    23 VKRVLSD--PATFSSDlgRLLPGEDDALTEGSLltMDPPRHRKLRKLVSQAFTPRLIADLEPRIAEITDELLDAV----- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 166 EGKPTsmkdifgaysMDVITATSFgvnidslnnpqdPF-VEKIKKLLKFDIFD-PLFLSVTlfpfltpvfDALnvsLFPR 243
Cdd:cd11032    96 DGRGE----------FDLVEDLAY------------PLpVIVIAELLGVPAEDrELFKKWS---------DAL---VSGL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 244 DVISFFTTSVERMKEnRMKE------------KEKQRVDFLQLMINSQnyktkESHKALSDVEIVAQSVIFIFAGYETTS 311
Cdd:cd11032   142 GDDSFEEEEVEEMAE-ALRElnayllehleerRRNPRDDLISRLVEAE-----VDGERLTDEEIVGFAILLLIAGHETTT 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 312 SALSFALYLLAIHPDVQKKLQDEIDAaLPNkapatydtllqmeyldmVVNETLRLYPIAGRLERVCKTDVEINGLFIPKG 391
Cdd:cd11032   216 NLLGNAVLCLDEDPEVAARLRADPSL-IPG-----------------AIEEVLRYRPPVQRTARVTTEDVELGGVTIPAG 277
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 392 TVVMIPTFALHKDPKYWPEPEEFRPERfskknqdsiNPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF---TVQPC 468
Cdd:cd11032   278 QLVIAWLASANRDERQFEDPDTFDIDR---------NPNPHLSFGHGIHFCLGAPLARLEARIALEALLDRFpriRVDPD 348

                  ....
gi 1720412152 469 KETE 472
Cdd:cd11032   349 VPLE 352
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
242-463 2.45e-23

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: 102.18  E-value: 2.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 242 PRDVISFFTTsvermkenRMKEKEKqrvdflqlminsqNYKTKESHKALsdveiVAQSVIFIFAGYETTSSALSFALYLL 321
Cdd:cd20668   200 PRDFIDSFLI--------RMQEEKK-------------NPNTEFYMKNL-----VMTTLNLFFAGTETVSTTLRYGFLLL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 322 AIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIA--GRLERVCKtDVEINGLFIPKGTVVMIPTF 399
Cdd:cd20668   254 MKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIpmGLARRVTK-DTKFRDFFLPKGTEVFPMLG 332
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720412152 400 ALHKDPKYWPEPEEFRPERFSKKNQDSINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd20668   333 SVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNF 396
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
213-454 5.62e-23

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: 101.08  E-value: 5.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 213 FDIFDPLFLSVTLFPFLTPvFDALNVSLFPRDVISfftTSVER-MKENRMKEKEKQRVDFLQLMINSqnykTKESHKALS 291
Cdd:cd20637   152 FSVFQQFVENVFSLPLDLP-FSGYRRGIRARDSLQ---KSLEKaIREKLQGTQGKDYADALDILIES----AKEHGKELT 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 292 DVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDA------ALPNKAPATYDTLLQMEYLDMVVNETLR 365
Cdd:cd20637   224 MQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELRSngilhnGCLCEGTLRLDTISSLKYLDCVIKEVLR 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 366 LY-PIAGRLERVCKTdVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSK-KNQDSINPYMYLPFGSGPRNCI 443
Cdd:cd20637   304 LFtPVSGGYRTALQT-FELDGFQIPKGWSVLYSIRDTHDTAPVFKDVDAFDPDRFGQeRSEDKDGRFHYLPFGGGVRTCL 382
                         250
                  ....*....|.
gi 1720412152 444 GMRFALINMKV 454
Cdd:cd20637   383 GKQLAKLFLKV 393
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
313-490 7.13e-23

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: 100.46  E-value: 7.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 313 ALSFALYllaiHPDVQKKLQDEIDAALPN----KAPATYDTLLQMEYLDMVVNETLRLYPiAGRLERVCKTDVEINGLFI 388
Cdd:cd20635   233 TLAFILS----HPSVYKKVMEEISSVLGKagkdKIKISEDDLKKMPYIKRCVLEAIRLRS-PGAITRKVVKPIKIKNYTI 307
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 389 PKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQD-SINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQP 467
Cdd:cd20635   308 PAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKADLEkNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFTL 387
                         170       180
                  ....*....|....*....|...
gi 1720412152 468 CKETEIPLKLSKQGLLQPENPLL 490
Cdd:cd20635   388 LDPVPKPSPLHLVGTQQPEGPCR 410
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
39-463 8.71e-23

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 101.31  E-value: 8.71e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  39 PGPKPLPFLGTILAYQK-GFWECDIQCHKKYGKMWGLYDGRQPVLAITDPDIIKTVLvKECYSTFTNRrrfgPVGILKKA 117
Cdd:PLN03234   31 PGPKGLPIIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELL-KTQDLNFTAR----PLLKGQQT 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 118 ISISENE--------EWKRIRAL-LSPTFTSGRLKEMFPIINQFTDVLVRNMRQGLGEGKPTSMKDIFGAYSMDVITATS 188
Cdd:PLN03234  106 MSYQGRElgfgqytaYYREMRKMcMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQA 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 189 FGVNIDSLNNPQDPFVEKIKKLLKfdIFDPLFLSvTLFPFLTPVFDALNVSLFPRDVISFFTTSV-----ERMKENRMKE 263
Cdd:PLN03234  186 FGKRYNEYGTEMKRFIDILYETQA--LLGTLFFS-DLFPYFGFLDNLTGLSARLKKAFKELDTYLqelldETLDPNRPKQ 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 264 KEKQRVDFLQLMINSQNYKTKESHKalsdvEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKA 343
Cdd:PLN03234  263 ETESFIDLLMQIYKDQPFSIKFTHE-----NVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKG 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 344 PATYDTLLQMEYLDMVVNETLRLYP-IAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPE-PEEFRPERFSK 421
Cdd:PLN03234  338 YVSEEDIPNLPYLKAVIKESLRLEPvIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPERFMK 417
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1720412152 422 -------KNQDsinpYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:PLN03234  418 ehkgvdfKGQD----FELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKF 462
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
128-463 4.05e-22

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: 97.62  E-value: 4.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 128 RIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRqglgegkptsmkdifGAYSMDVITATSFgvnidslnnpqdPF-VEK 206
Cdd:cd20625    67 RLRRLVSKAFTPRAVERLRPRIERLVDELLDRLA---------------ARGRVDLVADFAY------------PLpVRV 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 207 IKKLLKFDIFD-PLF--LSVTLFPFLTPV-----FDALNVSLfpRDVISFFTTSVERMKENRmkekekqRVDFLQLMINS 278
Cdd:cd20625   120 ICELLGVPEEDrPRFrgWSAALARALDPGplleeLARANAAA--AELAAYFRDLIARRRADP-------GDDLISALVAA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 279 QNYKTKeshkaLSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEidaalPNKAPAtydtllqmeyldm 358
Cdd:cd20625   191 EEDGDR-----LSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQLALLRAD-----PELIPA------------- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 359 VVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNqdsinpymyLPFGSG 438
Cdd:cd20625   248 AVEELLRYDSPVQLTARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITRAPNRH---------LAFGAG 318
                         330       340
                  ....*....|....*....|....*
gi 1720412152 439 PRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd20625   319 IHFCLGAPLARLEAEIALRALLRRF 343
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
270-456 5.90e-22

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: 97.28  E-value: 5.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 270 DFLQLMINSQnyktkESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEidaalPNKAPAtydt 349
Cdd:cd11035   171 DLISAILNAE-----IDGRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLRED-----PELIPA---- 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 350 llqmeyldmVVNETLRLYPIAgRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERfskknqdsiNP 429
Cdd:cd11035   237 ---------AVEELLRRYPLV-NVARIVTRDVEFHGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR---------KP 297
                         170       180
                  ....*....|....*....|....*..
gi 1720412152 430 YMYLPFGSGPRNCIGMRFALINMKVAL 456
Cdd:cd11035   298 NRHLAFGAGPHRCLGSHLARLELRIAL 324
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
290-456 6.30e-22

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: 97.29  E-value: 6.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 290 LSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDeiDAALPNKApatydtllqmeyldmvVNETLRLYPI 369
Cdd:cd11078   205 LTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRA--DPSLIPNA----------------VEETLRYDSP 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 370 AGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERfskKNQDSinpymYLPFGSGPRNCIGMRFAL 449
Cdd:cd11078   267 VQGLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR---PNARK-----HLTFGHGIHFCLGAALAR 338

                  ....*..
gi 1720412152 450 INMKVAL 456
Cdd:cd11078   339 MEARIAL 345
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
122-460 9.83e-22

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: 96.67  E-value: 9.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 122 ENEEWKRIRALLSPTFTSGRLKEMFPIINQFTDVLVRNMRQGlgegkptsmkdifgaYSMDVITATSfgvnidslnnpqD 201
Cdd:cd11038    75 EGADHARLRGLVNPAFTPKAVEALRPRFRATANDLIDGFAEG---------------GECEFVEAFA------------E 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 202 PF-VEKIKKLLKFDIFD-PLF--LSVTLFPFLTPVFDALnVSLFPRDVISFFTTSVERMKENRMKEKEkqrvDFLQLMIN 277
Cdd:cd11038   128 PYpARVICTLLGLPEEDwPRVhrWSADLGLAFGLEVKDH-LPRIEAAVEELYDYADALIEARRAEPGD----DLISTLVA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 278 SQnyktkESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDeiDAALPNKApatydtllqmeyld 357
Cdd:cd11038   203 AE-----QDGDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDQWRALRE--DPELAPAA-------------- 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 358 mvVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKywpepeEFRPERFSKKNQDSINpymyLPFGS 437
Cdd:cd11038   262 --VEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANRDPR------VFDADRFDITAKRAPH----LGFGG 329
                         330       340
                  ....*....|....*....|...
gi 1720412152 438 GPRNCIGMRFALINMKVALvRVL 460
Cdd:cd11038   330 GVHHCLGAFLARAELAEAL-TVL 351
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
270-444 1.07e-21

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: 97.38  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 270 DFLQLMINSQNYKTKESHKALSDVEIVAQSVIFIF-AGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL-PNKAPATY 347
Cdd:cd20675   210 DMMDAFILALEKGKSGDSGVGLDKEYVPSTVTDIFgASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVgRDRLPCIE 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 348 DTLlQMEYLDMVVNETLR---LYPIAgrLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKK-- 422
Cdd:cd20675   290 DQP-NLPYVMAFLYEAMRfssFVPVT--IPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDEng 366
                         170       180
                  ....*....|....*....|....
gi 1720412152 423 --NQDSINPYMYlpFGSGPRNCIG 444
Cdd:cd20675   367 flNKDLASSVMI--FSVGKRRCIG 388
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
290-469 5.11e-21

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: 94.88  E-value: 5.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 290 LSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALpNKAPATYDTLLQMEYLDMVVNETLR---L 366
Cdd:cd20627   198 LSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQVL-GKGPITLEKIEQLRYCQQVLCETVRtakL 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 367 YPIAGRLErvcktDVE--INGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNqdSINPYMYLPFgSGPRNCIG 444
Cdd:cd20627   277 TPVSARLQ-----ELEgkVDQHIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRFDDES--VMKSFSLLGF-SGSQECPE 348
                         170       180
                  ....*....|....*....|....*
gi 1720412152 445 MRFALINMKVALVRVLQNFTVQPCK 469
Cdd:cd20627   349 LRFAYMVATVLLSVLVRKLRLLPVD 373
PLN02774 PLN02774
brassinosteroid-6-oxidase
251-444 1.53e-20

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 94.07  E-value: 1.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 251 TSVERMKENRMKEKEKQRV---DFL-QLMinsqnyKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPD 326
Cdd:PLN02774  223 KNIVRMLRQLIQERRASGEthtDMLgYLM------RKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPK 296
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 327 VQKKLQDEIDAALPNKAPA---TYDTLLQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHK 403
Cdd:PLN02774  297 ALQELRKEHLAIRERKRPEdpiDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINY 376
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720412152 404 DPKYWPEPEEFRPERFSKKNQDSiNPYMYLpFGSGPRNCIG 444
Cdd:PLN02774  377 DPFLYPDPMTFNPWRWLDKSLES-HNYFFL-FGGGTRLCPG 415
PLN02971 PLN02971
tryptophan N-hydroxylase
254-491 2.60e-18

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 87.79  E-value: 2.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 254 ERMKENRmKEKEKQRVDFLQLMINsqnYKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQD 333
Cdd:PLN02971  291 ERIKMWR-EGKRTQIEDFLDIFIS---IKDEAGQPLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAME 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 334 EIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAG-RLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPE 412
Cdd:PLN02971  367 EIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAfNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPL 446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 413 EFRPERFSKKNQD---SINPYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQ-PCKETEIPLKLSKQGLLQPEnP 488
Cdd:PLN02971  447 SFKPERHLNECSEvtlTENDLRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKlAGSETRVELMESSHDMFLSK-P 525

                  ...
gi 1720412152 489 LLL 491
Cdd:PLN02971  526 LVM 528
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
208-482 4.25e-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: 86.58  E-value: 4.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 208 KKLLKFDifdplflsvTLFPFLT---PVFDALNVSLFPRDVISFFTTsvERMKENR-MKEKEKQRVDFLqlminsqnykt 283
Cdd:cd20632   148 KKFRKFD---------AMFPYLVaniPIELLGATKSIREKLIKYFLP--QKMAKWSnPSEVIQARQELL----------- 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 284 kESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAAL----PNKAPA-----TYDTLLQME 354
Cdd:cd20632   206 -EQYDVLQDYDKAAHHFAFLWASVGNTIPATFWAMYYLLRHPEALAAVRDEIDHVLqstgQELGPDfdihlTREQLDSLV 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 355 YLDMVVNETLRLYPIAGRLeRVCKTDVEIN-----GLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERF----SKKNQD 425
Cdd:cd20632   285 YLESAINESLRLSSASMNI-RVVQEDFTLKlesdgSVNLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFvedgKKKTTF 363
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720412152 426 SIN----PYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNFTVQPCKE-TEIPLKLSKQGL 482
Cdd:cd20632   364 YKRgqklKYYLMPFGSGSSKCPGRFFAVNEIKQFLSLLLLYFDLELLEEqKPPGLDNSRAGL 425
PLN02500 PLN02500
cytochrome P450 90B1
287-463 9.00e-18

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 85.69  E-value: 9.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 287 HKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDE-IDAALPNKAPA----TYDTLLQMEYLDMVVN 361
Cdd:PLN02500  272 HSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEhLEIARAKKQSGeselNWEDYKKMEFTQCVIN 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 362 ETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKN-------QDSINPYMYLP 434
Cdd:PLN02500  352 ETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNnrggssgSSSATTNNFMP 431
                         170       180
                  ....*....|....*....|....*....
gi 1720412152 435 FGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:PLN02500  432 FGGGPRLCAGSELAKLEMAVFIHHLVLNF 460
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
285-456 1.14e-17

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 85.37  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 285 ESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPA---TYDTLLQMEYLDMVVN 361
Cdd:PLN02196  255 GDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGeslTWEDTKKMPLTSRVIQ 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 362 ETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMiPTFA-LHKDPKYWPEPEEFRPERFskknQDSINPYMYLPFGSGPR 440
Cdd:PLN02196  335 ETLRVASILSFTFREAVEDVEYEGYLIPKGWKVL-PLFRnIHHSADIFSDPGKFDPSRF----EVAPKPNTFMPFGNGTH 409
                         170
                  ....*....|....*.
gi 1720412152 441 NCIGMRFALINMKVAL 456
Cdd:PLN02196  410 SCPGNELAKLEISVLI 425
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
292-460 3.67e-17

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: 83.16  E-value: 3.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 292 DVEIVAQSVIFIFAGYETTSSALSFAL-YLLAiHPDvqKKLQDEI--DAALPNKAPATydtllqmeyLDMVVNETLRLYP 368
Cdd:cd20612   185 ADEVRDNVLGTAVGGVPTQSQAFAQILdFYLR-RPG--AAHLAEIqaLARENDEADAT---------LRGYVLEALRLNP 252
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 369 IAGRLERVCKTDVEINGLF-----IPKGTVVMIPTFALHKDPKYWPEPEEFRPERfskknqdSINPYMYlpFGSGPRNCI 443
Cdd:cd20612   253 IAPGLYRRATTDTTVADGGgrtvsIKAGDRVFVSLASAMRDPRAFPDPERFRLDR-------PLESYIH--FGHGPHQCL 323
                         170
                  ....*....|....*..
gi 1720412152 444 GMRFALINMkVALVRVL 460
Cdd:cd20612   324 GEEIARAAL-TEMLRVV 339
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
302-458 4.40e-17

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: 82.63  E-value: 4.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 302 FIFAGYETTSSALSFALYLLAIHPDVQKKLQDEidaalPNKAPAtydtllqmeyldmVVNETLRLYPIAGRLERVCKTDV 381
Cdd:cd11037   210 YLSAGLDTTISAIGNALWLLARHPDQWERLRAD-----PSLAPN-------------AFEEAVRLESPVQTFSRTTTRDT 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 382 EINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERfskknqdsiNPYMYLPFGSGPRNCIGMRFALINMKV---ALVR 458
Cdd:cd11037   272 ELAGVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITR---------NPSGHVGFGHGVHACVGQHLARLEGEAlltALAR 342
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
267-463 4.59e-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: 82.86  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 267 QRVDFLQLMInsqnyKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDaALPNkapat 346
Cdd:cd20630   181 VEDDLLTTLL-----RAEEDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEPE-LLRN----- 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 347 ydtllqmeyldmVVNETLRlYPIAGR--LERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNq 424
Cdd:cd20630   250 ------------ALEEVLR-WDNFGKmgTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRRDPNAN- 315
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720412152 425 dsinpymyLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:cd20630   316 --------IAFGYGPHFCIGAALARLELELAVSTLLRRF 346
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
314-467 2.46e-16

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: 80.65  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 314 LSFALYLLAIHPDVQKKLQDEIDaalpnkapatydtllqmEYLDMVVNETLRLYP----IAGRLervcKTDVEINGLFIP 389
Cdd:cd11067   240 VTFAALALHEHPEWRERLRSGDE-----------------DYAEAFVQEVRRFYPffpfVGARA----RRDFEWQGYRFP 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 390 KGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNqdsINPYMYLPFGSGP-----RnCIGMRFALINMKVAlVRVLQN-- 462
Cdd:cd11067   299 KGQRVLLDLYGTNHDPRLWEDPDRFRPERFLGWE---GDPFDFIPQGGGDhatghR-CPGEWITIALMKEA-LRLLARrd 373

                  ....*.
gi 1720412152 463 -FTVQP 467
Cdd:cd11067   374 yYDVPP 379
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
252-463 2.73e-16

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 81.21  E-value: 2.73e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 252 SVERMKENRMKEKEKQRVDFLQLMINSQNYKTKeSHKALSDVEIvaQSVIF--IFAGYETTSSALSFALYLLAIHPDVQK 329
Cdd:PLN02169  260 SSRRKEEISRAETEPYSKDALTYYMNVDTSKYK-LLKPKKDKFI--RDVIFslVLAGRDTTSSALTWFFWLLSKHPQVMA 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 330 KLQDEIDAALPNkapatyDTLLQMEYLDMVVNETLRLYP-IAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYW 408
Cdd:PLN02169  337 KIRHEINTKFDN------EDLEKLVYLHAALSESMRLYPpLPFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVW 410
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720412152 409 PE-PEEFRPERFSKKNQDSIN--PYMYLPFGSGPRNCIGMRFALINMKVALVRVLQNF 463
Cdd:PLN02169  411 GEdALDFKPERWISDNGGLRHepSYKFMAFNSGPRTCLGKHLALLQMKIVALEIIKNY 468
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
128-463 2.75e-16

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: 80.65  E-value: 2.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 128 RIRALLSPTFTSGRLKEMFPIINQFTDVLVRnmrqGLGEGKPTSMKDIFgAY--SMDVItATSFGVnidslnnpqdPFVE 205
Cdd:cd11029    83 RLRRLVAKAFTPRRVEALRPRIEEITDELLD----ALAARGVVDLVADF-AYplPITVI-CELLGV----------PEED 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 206 KikkllkfDIFDPLFLSVTLFPFLTPVFDALNvslfpRDVISFFTTSVERmkenrmkeKEKQ-RVDFLQLMINSQnyktk 284
Cdd:cd11029   147 R-------DRFRRWSDALVDTDPPPEEAAAAL-----RELVDYLAELVAR--------KRAEpGDDLLSALVAAR----- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 285 ESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEiDAALPNkapatydtllqmeyldmVVNETL 364
Cdd:cd11029   202 DEGDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRAD-PELWPA-----------------AVEELL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 365 RLY-PIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERfsKKNQdsinpymYLPFGSGPRNCI 443
Cdd:cd11029   264 RYDgPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR--DANG-------HLAFGHGIHYCL 334
                         330       340
                  ....*....|....*....|
gi 1720412152 444 GMRFALINMKVALVRVLQNF 463
Cdd:cd11029   335 GAPLARLEAEIALGALLTRF 354
PLN03018 PLN03018
homomethionine N-hydroxylase
294-496 3.74e-16

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 81.21  E-value: 3.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 294 EIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRLYPIAGRL 373
Cdd:PLN03018  314 EIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYV 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 374 -ERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSK-----KNQDSINPYM-YLPFGSGPRNCIGMR 446
Cdd:PLN03018  394 pPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQgdgitKEVTLVETEMrFVSFSTGRRGCVGVK 473
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720412152 447 FALINMKVALVRVLQNFTVQPCKETEiPLKLSK-QGLLQPENPLLLKVVSR 496
Cdd:PLN03018  474 VGTIMMVMMLARFLQGFNWKLHQDFG-PLSLEEdDASLLMAKPLLLSVEPR 523
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
289-463 6.31e-16

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: 79.49  E-value: 6.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 289 ALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDaalpnkapatydtllqmeYLDMVVNETLRLYP 368
Cdd:cd11030   203 ELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPEQLAALRADPS------------------LVPGAVEELLRYLS 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 369 IAGR-LERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKnqdsinpymYLPFGSGPRNCIGMRF 447
Cdd:cd11030   265 IVQDgLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITRPARR---------HLAFGHGVHQCLGQNL 335
                         170
                  ....*....|....*.
gi 1720412152 448 ALINMKVALVRVLQNF 463
Cdd:cd11030   336 ARLELEIALPTLFRRF 351
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
290-467 1.43e-15

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: 78.84  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 290 LSDVEIVAQsVIF--IFAGYETTSSALSFALYLLAIH-PDVQKKLQDEIDAALPNKAPATYDTLLQMEYLDMVVNETLRL 366
Cdd:cd11071   220 LSREEAVHN-LLFmlGFNAFGGFSALLPSLLARLGLAgEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRL 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 367 YP----IAGRlervCKTDVEIN---GLF-IPKGTVVM--IPtFAlHKDPKYWPEPEEFRPERFSKKNQDSINpymYLPFG 436
Cdd:cd11071   299 HPpvplQYGR----ARKDFVIEshdASYkIKKGELLVgyQP-LA-TRDPKVFDNPDEFVPDRFMGEEGKLLK---HLIWS 369
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1720412152 437 SGP---------RNCIGMRFALINMKVALVRVLQN---FTVQP 467
Cdd:cd11071   370 NGPeteeptpdnKQCPGKDLVVLLARLFVAELFLRydtFTIEP 412
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
209-485 2.26e-15

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: 78.18  E-value: 2.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 209 KLLKFDIFDPLFLSVTLFP-------FLTPVF-DALNVS-LFPRDVISFFTTSVER-MKENRMKEKEKQRVDFLQLMINS 278
Cdd:cd20633   158 EFRKFDQLFPRLAYSVLPPkdkleaeRLKRLFwDMLSVSkMSQKENISGWISEQQRqLAEHGMPEYMQDRFMFLLLWASQ 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 279 QNyktkeshkalsdveivaqsvififagyeTTSSALSFALYLLAiHPDVQKKLQDEIDAAL--------PNKAPA--TYD 348
Cdd:cd20633   238 GN----------------------------TGPASFWLLLYLLK-HPEAMKAVREEVEQVLketgqevkPGGPLInlTRD 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 349 TLLQMEYLDMVVNETLRLyPIAGRLERVCKTDVEI---NG--LFIPKG-TVVMIPTFALHKDPKYWPEPEEFRPERFSK- 421
Cdd:cd20633   289 MLLKTPVLDSAVEETLRL-TAAPVLIRAVVQDMTLkmaNGreYALRKGdRLALFPYLAVQMDPEIHPEPHTFKYDRFLNp 367
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720412152 422 ---------KNQDSINPYMyLPFGSGPRNCIGMRFALINMKVALVRVLQNFT---VQPckETEIPLKLSKQ---GLLQP 485
Cdd:cd20633   368 dggkkkdfyKNGKKLKYYN-MPWGAGVSICPGRFFAVNEMKQFVFLMLTYFDlelVNP--DEEIPSIDPSRwgfGTMQP 443
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
290-460 1.69e-14

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


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 74.87  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 290 LSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDeiDAALPNKApatydtllqmeyldmvVNETLRLYP- 368
Cdd:cd11033   205 LTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLRA--DPSLLPTA----------------VEEILRWASp 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 369 -IAGRleRVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERfskknqdSINPymYLPFGSGPRNCIGMRF 447
Cdd:cd11033   267 vIHFR--RTATRDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR-------SPNP--HLAFGGGPHFCLGAHL 335
                         170
                  ....*....|...
gi 1720412152 448 ALINMKVALVRVL 460
Cdd:cd11033   336 ARLELRVLFEELL 348
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
99-460 4.04e-14

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: 73.66  E-value: 4.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152  99 YSTFTNRRRFGPVGILKKAISISENEEWKRiRALLSPTFTSGRLKEMFPIINQftdvLVRNMRQGLGEGKPTSMKDIFGA 178
Cdd:cd11080    30 FTTKSLAERAEPVMRGPVLAQMTGKEHAAK-RAIVVRAFRGDALDHLLPLIKE----NAEELIAPFLERGRVDLVNDFGK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 179 -YSMDVITATsfgVNIDSLNNPQdpFVEKIKKLLKF--------DIFDPLFLSVTLFP-FLTPVFDALNVSlfPR-DVIS 247
Cdd:cd11080   105 pFAVNVTMDM---LGLDKRDHEK--IHEWHSSVAAFitslsqdpEARAHGLRCAEQLSqYLLPVIEERRVN--PGsDLIS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 248 FFTTS-VERMkenrmkekekqrvdflqlminsqnyktkeshkALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPD 326
Cdd:cd11080   178 ILCTAeYEGE--------------------------------ALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPE 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 327 VQKKLQDeiDAALPNKAPAtydtllqmeyldmvvnETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPK 406
Cdd:cd11080   226 QLAAVRA--DRSLVPRAIA----------------ETLRYHPPVQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPA 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720412152 407 YWPEPEEFRPERFSKKNQDSINPYM-YLPFGSGPRNCIGMRFALINMKVALVRVL 460
Cdd:cd11080   288 AFEDPDTFNIHREDLGIRSAFSGAAdHLAFGSGRHFCVGAALAKREIEIVANQVL 342
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
290-461 5.84e-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: 70.08  E-value: 5.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 290 LSDVEIVaqSVIFIFAGYETTSSALSFALYL--LAIHPDVQKKLqdeidAALPNKAPAtydtllqmeyldmVVNETLRLY 367
Cdd:cd11079   179 LTDEEIV--SILRNWTVGELGTIAACVGVLVhyLARHPELQARL-----RANPALLPA-------------AIDEILRLD 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 368 -P-IAGRleRVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERfskknqdsiNPYMYLPFGSGPRNCIGM 445
Cdd:cd11079   239 dPfVANR--RITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR---------HAADNLVYGRGIHVCPGA 307
                         170
                  ....*....|....*.
gi 1720412152 446 RFALINMKVALVRVLQ 461
Cdd:cd11079   308 PLARLELRILLEELLA 323
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
253-448 3.07e-12

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 68.61  E-value: 3.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 253 VERMKENRMKEKEKQRVDFLQLMINSQNYKTKESHKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQ 332
Cdd:PLN03141  210 VKKIIEEKRRAMKNKEEDETGIPKDVVDVLLRDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVALQQLT 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 333 DEiDAALPNKAPATYDTLLQMEYLDM-----VVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKY 407
Cdd:PLN03141  290 EE-NMKLKRLKADTGEPLYWTDYMSLpftqnVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEEN 368
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720412152 408 WPEPEEFRPERFSKKNQDSINpymYLPFGSGPRNCIGMRFA 448
Cdd:PLN03141  369 YDNPYQFNPWRWQEKDMNNSS---FTPFGGGQRLCPGLDLA 406
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
293-471 1.23e-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: 66.33  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 293 VEIVAQSVIFIFAgYETTSSALSFALYLLAIHPDVQKKLQDEidAALPNKAPAtydtllqMEYLDMVVNETLRLYPIAGR 372
Cdd:cd20624   191 VDPEGQVPQWLFA-FDAAGMALLRALALLAAHPEQAARAREE--AAVPPGPLA-------RPYLRACVLDAVRLWPTTPA 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 373 LERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKNQDsinPYMYL-PFGSGPRNCIGMRFALIN 451
Cdd:cd20624   261 VLRESTEDTVWGGRTVPAGTGFLIFAPFFHRDDEALPFADRFVPEIWLDGRAQ---PDEGLvPFSAGPARCPGENLVLLV 337
                         170       180
                  ....*....|....*....|
gi 1720412152 452 MKVALVRVLQNFTVQPCKET 471
Cdd:cd20624   338 ASTALAALLRRAEIDPLESP 357
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
232-487 4.25e-11

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: 64.71  E-value: 4.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 232 VFDALnVSLFPrdvISFFTT---SVERMKENRMKEKEKQRVDFLQLMinSQNYKTKESHKALSDVEIVAQSVIFIFAGYE 308
Cdd:cd20631   168 VFPAL-VAGLP---IHMFKTaksAREALAERLLHENLQKRENISELI--SLRMLLNDTLSTLDEMEKARTHVAMLWASQA 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 309 TTSSALSFALYLLAIHPDVQKKLQDEIDAALP----------NKAPATYDTLLQMEYLDMVVNETLRLYPiAGRLERVCK 378
Cdd:cd20631   242 NTLPATFWSLFYLLRCPEAMKAATKEVKRTLEktgqkvsdggNPIVLTREQLDDMPVLGSIIKEALRLSS-ASLNIRVAK 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 379 TDVEI---NG--LFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFSKKN-QDSIN--------PYMYLPFGSGPRNCIG 444
Cdd:cd20631   321 EDFTLhldSGesYAIRKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENgKEKTTfykngrklKYYYMPFGSGTSKCPG 400
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1720412152 445 MRFALINMKVALVRVLQNFTVQPCKET--EIPLKLSKQGL--LQPEN 487
Cdd:cd20631   401 RFFAINEIKQFLSLMLCYFDMELLDGNakCPPLDQSRAGLgiLPPTH 447
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
318-489 1.64e-09

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: 59.77  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 318 LYLLAiHPDVQKKLQDEIDAALPNKAPATY-------DTLLQMEYLDMVVNETLRLyPIAGRLERVCKTDVEI---NG-- 385
Cdd:cd20634   246 LFLLK-HPEAMAAVRGEIQRIKHQRGQPVSqtltinqELLDNTPVFDSVLSETLRL-TAAPFITREVLQDMKLrlaDGqe 323
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 386 LFIPKG-TVVMIPTFALHKDPKYWPEPEEFRPERFSK----------KNQDSINpYMYLPFGSGPRNCIGMRFALINMKV 454
Cdd:cd20634   324 YNLRRGdRLCLFPFLSPQMDPEIHQEPEVFKYDRFLNadgtekkdfyKNGKRLK-YYNMPWGAGDNVCIGRHFAVNSIKQ 402
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1720412152 455 ALVRVLQNFTVQPC-KETEIPL-KLSKQ--GLLQPENPL 489
Cdd:cd20634   403 FVFLILTHFDVELKdPEAEIPEfDPSRYgfGLLQPEGDI 441
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
342-444 2.73e-08

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 55.90  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 342 KAPATYDTL-LQMEYLDMVVNETLRLYPIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERFS 420
Cdd:cd20619   219 RRPEVFTAFrNDESARAAIINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTRPP 298
                          90       100
                  ....*....|....*....|....
gi 1720412152 421 KKNqdsinpyMYLPFGSGPRNCIG 444
Cdd:cd20619   299 AAS-------RNLSFGLGPHSCAG 315
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
292-456 6.60e-08

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: 54.42  E-value: 6.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 292 DVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDvqkklQDEIDAALPNKAPAtydtllqmeyldmVVNETLRLYPIAg 371
Cdd:cd11036   175 PGDLVANAILLAVQGAEAAAGLVGNAVLALLRRPA-----QWARLRPDPELAAA-------------AVAETLRYDPPV- 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 372 RLE-RVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFRPERfskknqdsiNPYMYLPFGSGPRNCIGMRFALI 450
Cdd:cd11036   236 RLErRFAAEDLELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR---------PTARSAHFGLGRHACLGAALARA 306

                  ....*.
gi 1720412152 451 NMKVAL 456
Cdd:cd11036   307 AAAAAL 312
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
358-482 1.49e-07

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: 53.56  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 358 MVVNETLRLYPIAGRLERVCKtDVEINGLFIPKGTVVmiptfALHKDPKYW-PEPEEFRPERFSK--KNQDSinpyMYLP 434
Cdd:cd20626   260 NLVKEALRLYPPTRRIYRAFQ-RPGSSKPEIIAADIE-----ACHRSESIWgPDALEFNPSRWSKltPTQKE----AFLP 329
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720412152 435 FGSGPRNCIGMR-FA--LINMKV-ALVRVLQNFTVqPCKETEIPLKLSKQGL 482
Cdd:cd20626   330 FGSGPFRCPAKPvFGprMIALLVgALLDALGDEWE-LVSVDGRNVIFGGERL 380
PLN02648 PLN02648
allene oxide synthase
325-419 2.08e-05

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 46.85  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 325 PDVQKKLQDEIDAALPNKAPA-TYDTLLQMEYLDMVVNETLRLYP----IAGRlervCKTDVEIN---GLF-IPKGTvvM 395
Cdd:PLN02648  304 EELQARLAEEVRSAVKAGGGGvTFAALEKMPLVKSVVYEALRIEPpvpfQYGR----AREDFVIEshdAAFeIKKGE--M 377
                          90       100
                  ....*....|....*....|....*...
gi 1720412152 396 I----PtFALhKDPKYWPEPEEFRPERF 419
Cdd:PLN02648  378 LfgyqP-LVT-RDPKVFDRPEEFVPDRF 403
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
290-448 3.22e-05

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 45.96  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 290 LSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVQKKLQDEIDAALpnkapatydtllqmeyldMVVNETLR-LYP 368
Cdd:cd11039   198 MSLEQIRANIKVAIGGGLNEPRDAIAGTCWGLLSNPEQLAEVMAGDVHWL------------------RAFEEGLRwISP 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 369 IaGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPKYWPEPEEFrpERFSKKNQdsinpymYLPFGSGPRNCIGMRFA 448
Cdd:cd11039   260 I-GMSPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRF--DVFRPKSP-------HVSFGAGPHFCAGAWAS 329
CYP_unk cd20623
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
287-461 2.26e-03

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: 410716 [Multi-domain]  Cd Length: 367  Bit Score: 40.33  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 287 HKALSDVEIVAQSVIFIFAGYETTSSALSFALYLLAIHPDVqkklqdeidaalpnkapaTYDTLLQMEYLDMVVNETLRL 366
Cdd:cd20623   189 PAGLTDEEVVHDLVLLLGAGHEPTTNLIGNTLRLMLTDPRF------------------AASLSGGRLSVREALNEVLWR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720412152 367 Y-PIAGRLERVCKTDVEINGLFIPKGTVVMIPTFALHKDPkyWPEPEEFRPErfskknqdSINpYMYLPFGSGPRNCIGM 445
Cdd:cd20623   251 DpPLANLAGRFAARDTELGGQWIRAGDLVVLGLAAANADP--RVRPDPGASM--------SGN-RAHLAFGAGPHRCPAQ 319
                         170
                  ....*....|....*.
gi 1720412152 446 RFALINMKVALVRVLQ 461
Cdd:cd20623   320 ELAETIARTAVEVLLD 335
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH